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

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***  Wad1  ***

elNémo ID: 19012215052351648

Job options:

ID        	=	 19012215052351648
JOBID     	=	 Wad1
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 Wad1

HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   02-MAR-07   2P17              
TITLE     CRYSTAL STRUCTURE OF GK1651 FROM GEOBACILLUS KAUSTOPHILUS             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PIRIN-LIKE PROTEIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS KAUSTOPHILUS;                       
SOURCE   3 ORGANISM_TAXID: 235909;                                              
SOURCE   4 STRAIN: HTA426;                                                      
SOURCE   5 GENE: GK1651;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL-X;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    GK1651, GEOBACILLUS KAUSTOPHILUS, STRUCTURAL GENOMICS, SOUTHEAST      
KEYWDS   2 COLLABORATORY FOR STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, 
KEYWDS   3 SECSG, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PSI,   
KEYWDS   4 UNKNOWN FUNCTION                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHU,J.T.SWINDELL II,L.CHEN,A.EBIHARA,A.SHINKAI,S.KURAMITSU,         
AUTHOR   2 S.YOKOYAMA,Z.-Q.FU,J.P.ROSE,B.C.WANG,SOUTHEAST COLLABORATORY FOR     
AUTHOR   3 STRUCTURAL GENOMICS (SECSG),RIKEN STRUCTURAL GENOMICS/PROTEOMICS     
AUTHOR   4 INITIATIVE (RSGI)                                                    
REVDAT   5   24-JAN-18 2P17    1       AUTHOR JRNL                              
REVDAT   4   13-SEP-17 2P17    1       REMARK                                   
REVDAT   3   13-JUL-11 2P17    1       VERSN                                    
REVDAT   2   24-FEB-09 2P17    1       VERSN                                    
REVDAT   1   01-MAY-07 2P17    0                                                
JRNL        AUTH   J.ZHU,J.T.SWINDELL II,L.CHEN,A.EBIHARA,A.SHINKAI,            
JRNL        AUTH 2 S.KURAMITSU,S.YOKOYAMA,Z.-Q.FU,J.P.ROSE,B.C.WANG             
JRNL        TITL   CRYSTAL STRUCTURE OF GK1651 FROM GEOBACILLUS KAUSTOPHILUS    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33392                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1766                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.52                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2370                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.2210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1951                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.190         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1977 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2680 ; 1.240 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   248 ; 6.483 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;37.205 ;23.708       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   327 ;11.705 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;14.044 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   295 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1516 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   811 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1330 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   180 ; 0.098 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.078 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    38 ; 0.162 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.093 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1266 ; 0.673 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1999 ; 1.103 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   796 ; 1.925 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   681 ; 2.909 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2P17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041838.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : SI CHANNEL 220                     
REMARK 200  OPTICS                         : ROSENBAUM                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.17000                            
REMARK 200   FOR SHELL         : 22.50                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SGXPRO                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MICROBATCH USING 1.0 MICROLITER DROPS    
REMARK 280  CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (5.09 MG/ML) AND    
REMARK 280  SOLUTION CONTAING 30% W/V PEG 4000, 0.1 M SODIUM ACETATE, 0.2 M     
REMARK 280  AMMONIUM ACETATE PH 4.6, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.78550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.84250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.91150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.84250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.78550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.91150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   250                                                      
REMARK 465     ALA A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     PRO A   254                                                      
REMARK 465     PHE A   255                                                      
REMARK 465     VAL A   256                                                      
REMARK 465     MSE A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     PRO A   260                                                      
REMARK 465     GLU A   261                                                      
REMARK 465     GLN A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     ARG A   264                                                      
REMARK 465     GLU A   265                                                      
REMARK 465     ALA A   266                                                      
REMARK 465     ILE A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     ASP A   269                                                      
REMARK 465     TYR A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     GLY A   273                                                      
REMARK 465     ARG A   274                                                      
REMARK 465     PHE A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     ARG A   277                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   58   CZ   NH2                                            
REMARK 480     ARG A   95   NH1                                                 
REMARK 480     LYS A  135   CD   CE                                             
REMARK 480     LYS A  141   NZ                                                  
REMARK 480     GLU A  143   OE2                                                 
REMARK 480     LYS A  158   CE   NZ                                             
REMARK 480     LYS A  209   CE   NZ                                             
REMARK 480     ARG A  232   NH2                                                 
REMARK 480     LYS A  234   CE   NZ                                             
REMARK 480     PRO A  248   CG                                                  
REMARK 480     VAL A  249   CG2                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  58   NE    ARG A  58   CZ      0.127                       
REMARK 500    ARG A  58   CZ    ARG A  58   NH1     0.655                       
REMARK 500    LYS A 135   CE    LYS A 135   NZ      0.679                       
REMARK 500    GLU A 143   CD    GLU A 143   OE2     0.128                       
REMARK 500    LYS A 234   CD    LYS A 234   CE      0.249                       
REMARK 500    VAL A 249   CB    VAL A 249   CG2     0.321                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  58   CD  -  NE  -  CZ  ANGL. DEV. = -23.2 DEGREES          
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =  19.9 DEGREES          
REMARK 500    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. = -21.9 DEGREES          
REMARK 500    ARG A  95   NH1 -  CZ  -  NH2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    LYS A 141   CD  -  CE  -  NZ  ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ARG A 232   NE  -  CZ  -  NH2 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    LYS A 234   CD  -  CE  -  NZ  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    VAL A 249   CG1 -  CB  -  CG2 ANGL. DEV. = -33.9 DEGREES          
REMARK 500    VAL A 249   CA  -  CB  -  CG2 ANGL. DEV. = -20.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  37      122.86    -36.28                                   
REMARK 500    ILE A 164      -74.33    -97.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  58         0.11    SIDE CHAIN                              
REMARK 500    ARG A 232         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 278  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  57   NE2                                                    
REMARK 620 2 HIS A  99   NE2 102.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 278                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: GKA001001651.1   RELATED DB: TARGETDB                    
REMARK 900 RELATED ID: 1J1L   RELATED DB: PDB                                   
REMARK 900 METAL BINDING PROTEIN                                                
DBREF  2P17 A    1   277  UNP    Q5KZF0   Q5KZF0_GEOKA     1    277             
SEQADV 2P17 MSE A    1  UNP  Q5KZF0    MET     1 MODIFIED RESIDUE               
SEQADV 2P17 MSE A   15  UNP  Q5KZF0    MET    15 MODIFIED RESIDUE               
SEQADV 2P17 MSE A   43  UNP  Q5KZF0    MET    43 MODIFIED RESIDUE               
SEQADV 2P17 MSE A   91  UNP  Q5KZF0    MET    91 MODIFIED RESIDUE               
SEQADV 2P17 MSE A  124  UNP  Q5KZF0    MET   124 MODIFIED RESIDUE               
SEQADV 2P17 MSE A  137  UNP  Q5KZF0    MET   137 MODIFIED RESIDUE               
SEQADV 2P17 MSE A  169  UNP  Q5KZF0    MET   169 MODIFIED RESIDUE               
SEQADV 2P17 MSE A  172  UNP  Q5KZF0    MET   172 MODIFIED RESIDUE               
SEQADV 2P17 MSE A  257  UNP  Q5KZF0    MET   257 MODIFIED RESIDUE               
SEQRES   1 A  277  MSE ALA ILE GLN ARG ARG ILE ARG ARG VAL LYS THR VAL          
SEQRES   2 A  277  GLN MSE THR THR ASN SER PRO ILE HIS ARG SER GLY SER          
SEQRES   3 A  277  VAL LEU GLU PRO GLY ASN TRP GLN GLU TYR ASP PRO PHE          
SEQRES   4 A  277  LEU LEU LEU MSE GLU ASP ILE PHE GLU ARG GLY THR PHE          
SEQRES   5 A  277  ASP VAL HIS PRO HIS ARG GLY ILE GLU THR VAL THR TYR          
SEQRES   6 A  277  VAL ILE SER GLY GLU LEU GLU HIS PHE ASP SER LYS ALA          
SEQRES   7 A  277  GLY HIS SER THR LEU GLY PRO GLY ASP VAL GLN TRP MSE          
SEQRES   8 A  277  THR ALA GLY ARG GLY VAL VAL HIS LYS GLU ASP PRO ALA          
SEQRES   9 A  277  SER GLY SER THR VAL HIS SER LEU GLN LEU TRP VAL ASN          
SEQRES  10 A  277  LEU PRO SER ALA TYR LYS MSE THR GLU PRO ARG TYR GLN          
SEQRES  11 A  277  ASN LEU ARG SER LYS ASP MSE PRO VAL ARG LYS GLU GLU          
SEQRES  12 A  277  GLY ALA THR ILE ARG VAL PHE SER GLY SER SER LYS GLY          
SEQRES  13 A  277  VAL LYS ALA PRO THR LYS ASN ILE VAL PRO VAL THR MSE          
SEQRES  14 A  277  VAL GLU MSE ILE VAL GLU PRO GLY THR THR VAL VAL GLN          
SEQRES  15 A  277  ASP LEU PRO GLY HIS TYR ASN GLY PHE LEU TYR ILE LEU          
SEQRES  16 A  277  GLU GLY SER GLY VAL PHE GLY ALA ASP ASN ILE GLU GLY          
SEQRES  17 A  277  LYS ALA GLY GLN ALA LEU PHE PHE SER ARG HIS ASN ARG          
SEQRES  18 A  277  GLY GLU GLU THR GLU LEU ASN VAL THR ALA ARG GLU LYS          
SEQRES  19 A  277  LEU ARG LEU LEU LEU TYR ALA GLY GLU PRO VAL ASN GLU          
SEQRES  20 A  277  PRO VAL VAL ALA TYR GLY PRO PHE VAL MSE ASN THR PRO          
SEQRES  21 A  277  GLU GLN ILE ARG GLU ALA ILE ARG ASP TYR GLN GLU GLY          
SEQRES  22 A  277  ARG PHE GLY ARG                                              
MODRES 2P17 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A   15  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A   43  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A   91  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A  124  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A  137  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A  169  MET  SELENOMETHIONINE                                   
MODRES 2P17 MSE A  172  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  15       8                                                       
HET    MSE  A  43       8                                                       
HET    MSE  A  91       8                                                       
HET    MSE  A 124       8                                                       
HET    MSE  A 137       8                                                       
HET    MSE  A 169       8                                                       
HET    MSE  A 172       8                                                       
HET     FE  A 278       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      FE FE (III) ION                                                     
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   2   FE    FE 3+                                                        
FORMUL   3  HOH   *211(H2 O)                                                    
HELIX    1   1 ASN A   32  ASP A   37  1                                   6    
HELIX    2   2 PRO A  119  LYS A  123  5                                   5    
HELIX    3   3 ARG A  133  MSE A  137  5                                   5    
SHEET    1   A 3 ILE A   3  GLN A   4  0                                        
SHEET    2   A 3 GLU A 224  ALA A 231  1  O  GLU A 226   N  ILE A   3           
SHEET    3   A 3 THR A 179  PRO A 185 -1  N  VAL A 180   O  VAL A 229           
SHEET    1   B 4 ILE A   3  GLN A   4  0                                        
SHEET    2   B 4 GLU A 224  ALA A 231  1  O  GLU A 226   N  ILE A   3           
SHEET    3   B 4 SER A 198  PHE A 201 -1  N  VAL A 200   O  THR A 230           
SHEET    4   B 4 ILE A 206  LYS A 209 -1  O  ILE A 206   N  PHE A 201           
SHEET    1   C 7 ILE A   7  THR A  12  0                                        
SHEET    2   C 7 GLN A 212  PHE A 216 -1  O  ALA A 213   N  LYS A  11           
SHEET    3   C 7 ASN A 189  GLU A 196 -1  N  LEU A 192   O  LEU A 214           
SHEET    4   C 7 LEU A 235  GLY A 242 -1  O  TYR A 240   N  PHE A 191           
SHEET    5   C 7 VAL A 167  VAL A 174 -1  N  THR A 168   O  ALA A 241           
SHEET    6   C 7 ALA A 145  SER A 151 -1  N  ARG A 148   O  GLU A 171           
SHEET    7   C 7 VAL A 139  GLU A 142 -1  N  ARG A 140   O  ILE A 147           
SHEET    1   D 7 MSE A  15  SER A  19  0                                        
SHEET    2   D 7 HIS A  22  LEU A  28 -1  O  SER A  24   N  THR A  16           
SHEET    3   D 7 PHE A  39  PHE A  47 -1  O  GLU A  44   N  GLY A  25           
SHEET    4   D 7 VAL A 109  ASN A 117 -1  O  GLN A 113   N  MSE A  43           
SHEET    5   D 7 ILE A  60  SER A  68 -1  N  VAL A  63   O  LEU A 114           
SHEET    6   D 7 VAL A  88  THR A  92 -1  O  MSE A  91   N  THR A  62           
SHEET    7   D 7 ARG A 128  LEU A 132 -1  O  ARG A 128   N  THR A  92           
SHEET    1   E 4 HIS A  55  HIS A  57  0                                        
SHEET    2   E 4 VAL A  97  PRO A 103 -1  O  VAL A  97   N  HIS A  57           
SHEET    3   E 4 LEU A  71  ASP A  75 -1  N  GLU A  72   O  ASP A 102           
SHEET    4   E 4 GLY A  79  LEU A  83 -1  O  LEU A  83   N  LEU A  71           
SHEET    1   F 2 SER A 153  SER A 154  0                                        
SHEET    2   F 2 VAL A 157  LYS A 158 -1  O  VAL A 157   N  SER A 154           
LINK         NE2 HIS A  57                FE    FE A 278     1555   1555  2.20  
LINK         NE2 HIS A  99                FE    FE A 278     1555   1555  1.92  
LINK         C   MSE A   1                 N   ALA A   2     1555   1555  1.34  
LINK         C   GLN A  14                 N   MSE A  15     1555   1555  1.32  
LINK         C   MSE A  15                 N   THR A  16     1555   1555  1.33  
LINK         C   LEU A  42                 N   MSE A  43     1555   1555  1.33  
LINK         C   MSE A  43                 N   GLU A  44     1555   1555  1.33  
LINK         C   TRP A  90                 N   MSE A  91     1555   1555  1.33  
LINK         C   MSE A  91                 N   THR A  92     1555   1555  1.33  
LINK         C   LYS A 123                 N   MSE A 124     1555   1555  1.33  
LINK         C   MSE A 124                 N   THR A 125     1555   1555  1.33  
LINK         C   ASP A 136                 N   MSE A 137     1555   1555  1.34  
LINK         C   MSE A 137                 N   PRO A 138     1555   1555  1.35  
LINK         C   THR A 168                 N   MSE A 169     1555   1555  1.33  
LINK         C   MSE A 169                 N   VAL A 170     1555   1555  1.33  
LINK         C   GLU A 171                 N   MSE A 172     1555   1555  1.33  
LINK         C   MSE A 172                 N   ILE A 173     1555   1555  1.33  
CISPEP   1 ASP A   37    PRO A   38          0        11.38                     
SITE     1 AC1  2 HIS A  57  HIS A  99                                          
CRYST1   53.571   59.823   69.685  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016716  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014350        0.00000                         
HETATM    1  N   MSE A   1      18.763  18.115  24.626  0.60 21.51           N  
HETATM    2  CA  MSE A   1      19.524  16.907  24.201  1.00 21.12           C  
HETATM    3  C   MSE A   1      20.904  17.293  23.657  1.00 20.05           C  
HETATM    4  O   MSE A   1      21.858  17.345  24.432  1.00 20.05           O  
HETATM    5  CB  MSE A   1      18.720  16.098  23.187  1.00 20.89           C  
HETATM    6  CG  MSE A   1      19.244  14.714  22.881  1.00 22.57           C  
HETATM    7 SE   MSE A   1      18.137  13.985  21.453  0.20 23.18          SE  
HETATM    8  CE  MSE A   1      18.755  15.096  19.971  0.10 22.66           C  
ATOM      9  N   ALA A   2      21.017  17.580  22.355  1.00 19.07           N  
ATOM     10  CA  ALA A   2      22.322  17.913  21.761  1.00 18.23           C  
ATOM     11  C   ALA A   2      22.831  19.232  22.306  1.00 17.43           C  
ATOM     12  O   ALA A   2      22.058  20.062  22.779  1.00 17.38           O  
ATOM     13  CB  ALA A   2      22.251  17.963  20.237  1.00 18.63           C  
ATOM     14  N   ILE A   3      24.143  19.420  22.240  1.00 16.70           N  
ATOM     15  CA  ILE A   3      24.744  20.662  22.668  1.00 16.21           C  
ATOM     16  C   ILE A   3      24.225  21.773  21.753  1.00 15.53           C  
ATOM     17  O   ILE A   3      24.324  21.673  20.533  1.00 15.03           O  
ATOM     18  CB  ILE A   3      26.281  20.558  22.631  1.00 16.53           C  
ATOM     19  CG1 ILE A   3      26.761  19.564  23.701  1.00 16.58           C  
ATOM     20  CG2 ILE A   3      26.928  21.937  22.802  1.00 16.48           C  
ATOM     21  CD1 ILE A   3      28.169  19.033  23.492  1.00 17.73           C  
ATOM     22  N   GLN A   4      23.643  22.808  22.352  1.00 14.95           N  
ATOM     23  CA  GLN A   4      23.057  23.924  21.607  1.00 14.99           C  
ATOM     24  C   GLN A   4      24.077  25.013  21.318  1.00 14.20           C  
ATOM     25  O   GLN A   4      24.668  25.593  22.242  1.00 14.95           O  
ATOM     26  CB  GLN A   4      21.883  24.534  22.385  1.00 15.81           C  
ATOM     27  CG  GLN A   4      20.720  23.582  22.593  1.00 18.94           C  
ATOM     28  CD  GLN A   4      20.157  23.068  21.286  1.00 21.43           C  
ATOM     29  OE1 GLN A   4      19.803  23.851  20.396  1.00 23.72           O  
ATOM     30  NE2 GLN A   4      20.083  21.749  21.150  1.00 21.29           N  
ATOM     31  N   ARG A   5      24.273  25.310  20.037  1.00 12.76           N  
ATOM     32  CA  ARG A   5      25.125  26.427  19.662  1.00 12.47           C  
ATOM     33  C   ARG A   5      24.494  27.775  20.009  1.00 11.84           C  
ATOM     34  O   ARG A   5      23.261  27.913  20.018  1.00 12.38           O  
ATOM     35  CB  ARG A   5      25.467  26.360  18.178  1.00 12.16           C  
ATOM     36  CG  ARG A   5      26.333  25.147  17.834  1.00 11.48           C  
ATOM     37  CD  ARG A   5      27.418  25.508  16.838  1.00  9.98           C  
ATOM     38  NE  ARG A   5      28.102  24.326  16.311  1.00  9.55           N  
ATOM     39  CZ  ARG A   5      29.250  24.377  15.631  1.00  9.26           C  
ATOM     40  NH1 ARG A   5      29.858  25.541  15.399  1.00  9.40           N  
ATOM     41  NH2 ARG A   5      29.800  23.271  15.157  1.00  9.15           N  
ATOM     42  N   ARG A   6      25.366  28.746  20.266  1.00 12.11           N  
ATOM     43  CA  ARG A   6      25.008  30.127  20.554  1.00 13.05           C  
ATOM     44  C   ARG A   6      25.446  30.985  19.374  1.00 12.11           C  
ATOM     45  O   ARG A   6      26.302  30.575  18.576  1.00 11.68           O  
ATOM     46  CB  ARG A   6      25.732  30.605  21.826  1.00 14.44           C  
ATOM     47  CG  ARG A   6      25.186  30.040  23.125  1.00 19.07           C  
ATOM     48  CD  ARG A   6      26.168  30.249  24.265  1.00 23.74           C  
ATOM     49  NE  ARG A   6      27.253  29.271  24.222  1.00 26.84           N  
ATOM     50  CZ  ARG A   6      28.500  29.530  23.835  1.00 27.76           C  
ATOM     51  NH1 ARG A   6      28.849  30.753  23.464  1.00 29.72           N  
ATOM     52  NH2 ARG A   6      29.403  28.557  23.829  1.00 28.55           N  
ATOM     53  N   ILE A   7      24.864  32.174  19.264  1.00 12.47           N  
ATOM     54  CA  ILE A   7      25.335  33.186  18.340  1.00 12.46           C  
ATOM     55  C   ILE A   7      26.371  34.048  19.052  1.00 13.05           C  
ATOM     56  O   ILE A   7      26.052  34.766  20.014  1.00 13.82           O  
ATOM     57  CB  ILE A   7      24.174  34.052  17.781  1.00 12.00           C  
ATOM     58  CG1 ILE A   7      23.128  33.171  17.064  1.00 12.31           C  
ATOM     59  CG2 ILE A   7      24.731  35.164  16.868  1.00 12.21           C  
ATOM     60  CD1 ILE A   7      23.711  32.191  16.026  1.00 11.99           C  
ATOM     61  N   ARG A   8      27.615  33.957  18.597  1.00 12.69           N  
ATOM     62  CA  ARG A   8      28.715  34.646  19.273  1.00 12.90           C  
ATOM     63  C   ARG A   8      28.934  36.070  18.769  1.00 12.60           C  
ATOM     64  O   ARG A   8      29.588  36.875  19.444  1.00 13.26           O  
ATOM     65  CB  ARG A   8      30.006  33.840  19.189  1.00 13.10           C  
ATOM     66  CG  ARG A   8      30.517  33.627  17.781  1.00 13.09           C  
ATOM     67  CD  ARG A   8      31.851  32.881  17.745  1.00 14.31           C  
ATOM     68  NE  ARG A   8      32.285  32.756  16.362  1.00 15.39           N  
ATOM     69  CZ  ARG A   8      32.996  33.673  15.713  1.00 15.91           C  
ATOM     70  NH1 ARG A   8      33.402  34.766  16.349  1.00 16.19           N  
ATOM     71  NH2 ARG A   8      33.314  33.493  14.438  1.00 14.24           N  
ATOM     72  N   ARG A   9      28.385  36.385  17.597  1.00 12.12           N  
ATOM     73  CA  ARG A   9      28.531  37.716  17.022  1.00 12.34           C  
ATOM     74  C   ARG A   9      27.496  37.952  15.939  1.00 11.90           C  
ATOM     75  O   ARG A   9      27.157  37.031  15.192  1.00 11.72           O  
ATOM     76  CB  ARG A   9      29.938  37.887  16.444  1.00 12.79           C  
ATOM     77  CG  ARG A   9      30.209  39.259  15.857  1.00 13.44           C  
ATOM     78  CD  ARG A   9      31.692  39.551  15.739  1.00 14.60           C  
ATOM     79  NE  ARG A   9      32.377  38.638  14.826  1.00 16.02           N  
ATOM     80  CZ  ARG A   9      32.401  38.760  13.501  1.00 16.38           C  
ATOM     81  NH1 ARG A   9      31.753  39.745  12.882  1.00 16.38           N  
ATOM     82  NH2 ARG A   9      33.079  37.880  12.778  1.00 15.38           N  
ATOM     83  N   VAL A  10      26.990  39.182  15.852  1.00 11.76           N  
ATOM     84  CA  VAL A  10      26.021  39.559  14.826  1.00 12.12           C  
ATOM     85  C   VAL A  10      26.584  40.697  13.975  1.00 12.50           C  
ATOM     86  O   VAL A  10      26.755  41.819  14.469  1.00 13.86           O  
ATOM     87  CB  VAL A  10      24.670  40.016  15.436  1.00 12.20           C  
ATOM     88  CG1 VAL A  10      23.684  40.422  14.335  1.00 13.25           C  
ATOM     89  CG2 VAL A  10      24.089  38.940  16.353  1.00 12.56           C  
ATOM     90  N   LYS A  11      26.875  40.412  12.706  1.00 12.19           N  
ATOM     91  CA  LYS A  11      27.425  41.417  11.789  1.00 12.01           C  
ATOM     92  C   LYS A  11      26.349  41.969  10.860  1.00 11.96           C  
ATOM     93  O   LYS A  11      25.613  41.201  10.239  1.00 11.77           O  
ATOM     94  CB  LYS A  11      28.571  40.802  10.960  1.00 12.67           C  
ATOM     95  CG  LYS A  11      28.974  41.582   9.711  1.00 14.24           C  
ATOM     96  CD  LYS A  11      29.816  42.799  10.033  1.00 16.03           C  
ATOM     97  CE  LYS A  11      30.302  43.474   8.752  1.00 16.26           C  
ATOM     98  NZ  LYS A  11      31.013  44.773   9.027  1.00 18.30           N  
ATOM     99  N   THR A  12      26.281  43.297  10.739  1.00 11.79           N  
ATOM    100  CA  THR A  12      25.353  43.936   9.829  1.00 12.30           C  
ATOM    101  C   THR A  12      26.151  44.384   8.614  1.00 12.59           C  
ATOM    102  O   THR A  12      27.067  45.202   8.747  1.00 13.00           O  
ATOM    103  CB  THR A  12      24.657  45.142  10.499  1.00 11.95           C  
ATOM    104  OG1 THR A  12      23.974  44.692  11.676  1.00 12.77           O  
ATOM    105  CG2 THR A  12      23.647  45.765   9.547  1.00 12.22           C  
ATOM    106  N   VAL A  13      25.814  43.849   7.441  1.00 13.08           N  
ATOM    107  CA  VAL A  13      26.557  44.165   6.224  1.00 14.52           C  
ATOM    108  C   VAL A  13      26.341  45.628   5.849  1.00 15.37           C  
ATOM    109  O   VAL A  13      25.205  46.107   5.844  1.00 16.31           O  
ATOM    110  CB  VAL A  13      26.166  43.201   5.064  1.00 14.49           C  
ATOM    111  CG1 VAL A  13      26.837  43.599   3.747  1.00 14.63           C  
ATOM    112  CG2 VAL A  13      26.553  41.780   5.437  1.00 15.75           C  
ATOM    113  N   GLN A  14      27.447  46.329   5.581  1.00 16.81           N  
ATOM    114  CA  GLN A  14      27.426  47.720   5.124  1.00 18.76           C  
ATOM    115  C   GLN A  14      27.878  47.744   3.666  1.00 18.73           C  
ATOM    116  O   GLN A  14      29.060  47.529   3.372  1.00 19.90           O  
ATOM    117  CB  GLN A  14      28.371  48.603   5.961  1.00 18.88           C  
ATOM    118  CG  GLN A  14      28.148  48.563   7.473  0.10 19.99           C  
ATOM    119  CD  GLN A  14      29.100  49.473   8.242  0.80 20.87           C  
ATOM    120  OE1 GLN A  14      29.097  50.698   8.067  1.00 26.04           O  
ATOM    121  NE2 GLN A  14      29.905  48.878   9.114  1.00 22.16           N  
HETATM  122  N   MSE A  15      26.941  47.987   2.764  1.00 18.63           N  
HETATM  123  CA  MSE A  15      27.250  48.001   1.336  1.00 18.59           C  
HETATM  124  C   MSE A  15      27.824  49.332   0.897  1.00 18.23           C  
HETATM  125  O   MSE A  15      27.485  50.381   1.453  1.00 18.87           O  
HETATM  126  CB  MSE A  15      26.016  47.649   0.513  1.00 18.94           C  
HETATM  127  CG  MSE A  15      25.476  46.289   0.873  1.00 19.62           C  
HETATM  128 SE   MSE A  15      24.286  45.605  -0.462  0.40 19.21          SE  
HETATM  129  CE  MSE A  15      25.592  45.150  -1.828  1.00 20.43           C  
ATOM    130  N   THR A  16      28.699  49.270  -0.101  1.00 17.56           N  
ATOM    131  CA  THR A  16      29.317  50.460  -0.670  1.00 17.56           C  
ATOM    132  C   THR A  16      29.176  50.421  -2.181  1.00 17.15           C  
ATOM    133  O   THR A  16      29.092  49.350  -2.776  1.00 16.58           O  
ATOM    134  CB  THR A  16      30.820  50.578  -0.284  1.00 18.28           C  
ATOM    135  OG1 THR A  16      31.337  51.835  -0.740  0.10 17.76           O  
ATOM    136  CG2 THR A  16      31.648  49.448  -0.879  1.00 19.25           C  
ATOM    137  N   THR A  17      29.164  51.593  -2.804  1.00 17.20           N  
ATOM    138  CA  THR A  17      29.104  51.676  -4.252  1.00 17.73           C  
ATOM    139  C   THR A  17      30.512  51.720  -4.844  1.00 17.61           C  
ATOM    140  O   THR A  17      31.282  52.661  -4.592  1.00 18.26           O  
ATOM    141  CB  THR A  17      28.231  52.858  -4.696  1.00 17.81           C  
ATOM    142  OG1 THR A  17      26.901  52.656  -4.191  1.00 19.87           O  
ATOM    143  CG2 THR A  17      28.181  52.958  -6.209  1.00 18.75           C  
ATOM    144  N   ASN A  18      30.856  50.678  -5.597  1.00 17.31           N  
ATOM    145  CA  ASN A  18      32.156  50.591  -6.265  1.00 17.43           C  
ATOM    146  C   ASN A  18      32.164  51.421  -7.532  1.00 17.39           C  
ATOM    147  O   ASN A  18      33.131  52.128  -7.824  1.00 17.41           O  
ATOM    148  CB  ASN A  18      32.501  49.148  -6.641  1.00 17.74           C  
ATOM    149  CG  ASN A  18      32.651  48.246  -5.447  1.00 19.14           C  
ATOM    150  OD1 ASN A  18      33.768  47.971  -4.994  1.00 23.25           O  
ATOM    151  ND2 ASN A  18      31.539  47.758  -4.941  1.00 18.64           N  
ATOM    152  N   SER A  19      31.085  51.311  -8.297  1.00 16.93           N  
ATOM    153  CA  SER A  19      30.973  51.956  -9.601  1.00 16.72           C  
ATOM    154  C   SER A  19      29.497  52.061  -9.958  1.00 16.94           C  
ATOM    155  O   SER A  19      28.641  51.548  -9.241  1.00 16.48           O  
ATOM    156  CB  SER A  19      31.729  51.141 -10.660  1.00 16.95           C  
ATOM    157  OG  SER A  19      30.988  49.999 -11.068  1.00 16.83           O  
ATOM    158  N   PRO A  20      29.181  52.737 -11.074  1.00 17.12           N  
ATOM    159  CA  PRO A  20      27.796  52.844 -11.516  1.00 17.17           C  
ATOM    160  C   PRO A  20      27.143  51.485 -11.809  1.00 16.59           C  
ATOM    161  O   PRO A  20      25.912  51.395 -11.881  1.00 17.65           O  
ATOM    162  CB  PRO A  20      27.909  53.660 -12.807  1.00 17.71           C  
ATOM    163  CG  PRO A  20      29.194  54.399 -12.675  1.00 17.67           C  
ATOM    164  CD  PRO A  20      30.102  53.480 -11.950  1.00 17.64           C  
ATOM    165  N   ILE A  21      27.956  50.446 -11.962  1.00 15.64           N  
ATOM    166  CA  ILE A  21      27.435  49.105 -12.287  1.00 15.28           C  
ATOM    167  C   ILE A  21      27.712  48.059 -11.200  1.00 14.73           C  
ATOM    168  O   ILE A  21      27.438  46.868 -11.396  1.00 14.13           O  
ATOM    169  CB  ILE A  21      27.950  48.609 -13.676  1.00 15.05           C  
ATOM    170  CG1 ILE A  21      29.484  48.525 -13.721  1.00 15.83           C  
ATOM    171  CG2 ILE A  21      27.401  49.503 -14.797  1.00 15.81           C  
ATOM    172  CD1 ILE A  21      30.029  47.829 -14.966  1.00 15.87           C  
ATOM    173  N   HIS A  22      28.228  48.495 -10.050  1.00 13.09           N  
ATOM    174  CA  HIS A  22      28.671  47.547  -9.026  1.00 12.33           C  
ATOM    175  C   HIS A  22      28.608  48.100  -7.611  1.00 12.32           C  
ATOM    176  O   HIS A  22      29.223  49.118  -7.296  1.00 11.97           O  
ATOM    177  CB  HIS A  22      30.099  47.086  -9.351  1.00 12.28           C  
ATOM    178  CG  HIS A  22      30.646  46.036  -8.436  1.00 12.94           C  
ATOM    179  ND1 HIS A  22      31.995  45.902  -8.191  1.00 13.13           N  
ATOM    180  CD2 HIS A  22      30.037  45.053  -7.731  1.00 13.63           C  
ATOM    181  CE1 HIS A  22      32.196  44.886  -7.371  1.00 14.26           C  
ATOM    182  NE2 HIS A  22      31.024  44.363  -7.063  1.00 12.69           N  
ATOM    183  N   ARG A  23      27.825  47.424  -6.774  1.00 11.47           N  
ATOM    184  CA  ARG A  23      27.786  47.679  -5.338  1.00 12.10           C  
ATOM    185  C   ARG A  23      28.229  46.402  -4.635  1.00 11.77           C  
ATOM    186  O   ARG A  23      27.988  45.301  -5.130  1.00 11.82           O  
ATOM    187  CB  ARG A  23      26.374  48.050  -4.881  1.00 13.19           C  
ATOM    188  CG  ARG A  23      25.842  49.334  -5.488  1.00 16.59           C  
ATOM    189  CD  ARG A  23      24.527  49.753  -4.847  1.00 21.88           C  
ATOM    190  NE  ARG A  23      24.734  50.360  -3.532  1.00 26.19           N  
ATOM    191  CZ  ARG A  23      24.320  49.843  -2.374  1.00 27.32           C  
ATOM    192  NH1 ARG A  23      23.644  48.703  -2.343  1.00 28.89           N  
ATOM    193  NH2 ARG A  23      24.567  50.488  -1.241  1.00 28.22           N  
ATOM    194  N   SER A  24      28.873  46.541  -3.485  1.00 12.05           N  
ATOM    195  CA  SER A  24      29.340  45.347  -2.779  1.00 12.91           C  
ATOM    196  C   SER A  24      29.339  45.493  -1.271  1.00 13.40           C  
ATOM    197  O   SER A  24      29.353  46.608  -0.748  1.00 14.89           O  
ATOM    198  CB  SER A  24      30.735  44.919  -3.255  1.00 13.24           C  
ATOM    199  OG  SER A  24      31.689  45.924  -2.966  1.00 15.70           O  
ATOM    200  N   GLY A  25      29.339  44.350  -0.586  1.00 13.68           N  
ATOM    201  CA  GLY A  25      29.401  44.356   0.886  1.00 14.54           C  
ATOM    202  C   GLY A  25      30.219  43.197   1.391  1.00 14.97           C  
ATOM    203  O   GLY A  25      30.137  42.104   0.839  1.00 15.16           O  
ATOM    204  N   SER A  26      31.024  43.444   2.421  1.00 15.13           N  
ATOM    205  CA  SER A  26      31.820  42.388   3.047  1.00 15.66           C  
ATOM    206  C   SER A  26      31.018  41.726   4.157  1.00 14.70           C  
ATOM    207  O   SER A  26      30.559  42.396   5.089  1.00 15.29           O  
ATOM    208  CB  SER A  26      33.155  42.921   3.586  1.00 16.60           C  
ATOM    209  OG  SER A  26      34.153  42.855   2.575  1.00 20.82           O  
ATOM    210  N   VAL A  27      30.808  40.421   4.019  1.00 13.98           N  
ATOM    211  CA  VAL A  27      30.088  39.645   5.027  1.00 13.68           C  
ATOM    212  C   VAL A  27      31.108  39.007   5.973  1.00 13.36           C  
ATOM    213  O   VAL A  27      31.022  39.135   7.199  1.00 13.17           O  
ATOM    214  CB  VAL A  27      29.143  38.600   4.382  1.00 13.48           C  
ATOM    215  CG1 VAL A  27      28.252  37.955   5.439  1.00 14.26           C  
ATOM    216  CG2 VAL A  27      28.279  39.237   3.268  1.00 14.08           C  
ATOM    217  N   LEU A  28      32.076  38.319   5.379  1.00 13.26           N  
ATOM    218  CA  LEU A  28      33.273  37.883   6.071  1.00 12.96           C  
ATOM    219  C   LEU A  28      34.412  38.622   5.400  1.00 13.70           C  
ATOM    220  O   LEU A  28      34.674  38.414   4.201  1.00 13.49           O  
ATOM    221  CB  LEU A  28      33.478  36.363   5.925  1.00 12.84           C  
ATOM    222  CG  LEU A  28      32.823  35.432   6.950  1.00 12.73           C  
ATOM    223  CD1 LEU A  28      31.305  35.512   6.910  1.00 13.97           C  
ATOM    224  CD2 LEU A  28      33.298  33.988   6.729  1.00 13.23           C  
ATOM    225  N   GLU A  29      35.069  39.491   6.161  1.00 14.61           N  
ATOM    226  CA  GLU A  29      36.182  40.275   5.643  1.00 15.46           C  
ATOM    227  C   GLU A  29      37.387  39.373   5.401  1.00 15.91           C  
ATOM    228  O   GLU A  29      37.554  38.373   6.111  1.00 15.77           O  
ATOM    229  CB  GLU A  29      36.539  41.398   6.624  1.00 15.60           C  
ATOM    230  CG  GLU A  29      37.396  40.972   7.829  1.00 17.19           C  
ATOM    231  CD  GLU A  29      36.614  40.286   8.944  1.00 17.06           C  
ATOM    232  OE1 GLU A  29      35.385  40.096   8.810  1.00 17.29           O  
ATOM    233  OE2 GLU A  29      37.245  39.943   9.974  1.00 19.33           O  
ATOM    234  N   PRO A  30      38.220  39.706   4.396  1.00 16.05           N  
ATOM    235  CA  PRO A  30      39.445  38.938   4.167  1.00 16.32           C  
ATOM    236  C   PRO A  30      40.488  39.195   5.256  1.00 16.61           C  
ATOM    237  O   PRO A  30      40.355  40.153   6.020  1.00 16.98           O  
ATOM    238  CB  PRO A  30      39.944  39.463   2.817  1.00 16.98           C  
ATOM    239  CG  PRO A  30      39.403  40.850   2.731  1.00 17.26           C  
ATOM    240  CD  PRO A  30      38.062  40.804   3.419  1.00 16.35           C  
ATOM    241  N   GLY A  31      41.497  38.327   5.325  1.00 16.83           N  
ATOM    242  CA  GLY A  31      42.613  38.495   6.260  1.00 17.05           C  
ATOM    243  C   GLY A  31      42.336  38.079   7.692  1.00 17.50           C  
ATOM    244  O   GLY A  31      43.075  38.458   8.607  1.00 18.59           O  
ATOM    245  N   ASN A  32      41.264  37.317   7.891  1.00 16.65           N  
ATOM    246  CA  ASN A  32      40.886  36.811   9.205  1.00 16.07           C  
ATOM    247  C   ASN A  32      40.646  35.301   9.147  1.00 15.40           C  
ATOM    248  O   ASN A  32      39.682  34.787   9.723  1.00 14.28           O  
ATOM    249  CB  ASN A  32      39.650  37.555   9.721  1.00 15.65           C  
ATOM    250  CG  ASN A  32      39.405  37.331  11.202  1.00 15.37           C  
ATOM    251  OD1 ASN A  32      40.236  36.734  11.897  1.00 16.00           O  
ATOM    252  ND2 ASN A  32      38.259  37.797  11.693  1.00 15.78           N  
ATOM    253  N   TRP A  33      41.559  34.597   8.472  1.00 15.26           N  
ATOM    254  CA  TRP A  33      41.471  33.160   8.289  1.00 15.53           C  
ATOM    255  C   TRP A  33      41.329  32.460   9.632  1.00 13.86           C  
ATOM    256  O   TRP A  33      40.645  31.428   9.736  1.00 14.14           O  
ATOM    257  CB  TRP A  33      42.703  32.616   7.538  1.00 17.15           C  
ATOM    258  CG  TRP A  33      43.922  32.420   8.415  1.00 18.50           C  
ATOM    259  CD1 TRP A  33      44.915  33.326   8.639  1.00 20.72           C  
ATOM    260  CD2 TRP A  33      44.253  31.261   9.206  1.00 20.28           C  
ATOM    261  NE1 TRP A  33      45.842  32.814   9.511  0.80 20.43           N  
ATOM    262  CE2 TRP A  33      45.466  31.546   9.869  0.80 20.39           C  
ATOM    263  CE3 TRP A  33      43.643  30.012   9.414  1.00 21.23           C  
ATOM    264  CZ2 TRP A  33      46.084  30.633  10.730  0.80 19.63           C  
ATOM    265  CZ3 TRP A  33      44.266  29.098  10.272  1.00 20.40           C  
ATOM    266  CH2 TRP A  33      45.477  29.419  10.912  1.00 19.90           C  
ATOM    267  N   GLN A  34      41.976  33.020  10.661  1.00 12.50           N  
ATOM    268  CA  GLN A  34      42.047  32.350  11.951  1.00 11.68           C  
ATOM    269  C   GLN A  34      40.694  32.259  12.625  1.00 11.23           C  
ATOM    270  O   GLN A  34      40.443  31.329  13.377  1.00 11.66           O  
ATOM    271  CB  GLN A  34      43.087  33.008  12.876  1.00 11.20           C  
ATOM    272  CG  GLN A  34      42.774  34.425  13.348  1.00 12.60           C  
ATOM    273  CD  GLN A  34      43.352  35.499  12.445  1.00 14.50           C  
ATOM    274  OE1 GLN A  34      43.540  35.300  11.241  1.00 14.99           O  
ATOM    275  NE2 GLN A  34      43.647  36.652  13.030  1.00 15.25           N  
ATOM    276  N   GLU A  35      39.814  33.222  12.346  1.00 10.09           N  
ATOM    277  CA  GLU A  35      38.469  33.174  12.898  1.00 10.00           C  
ATOM    278  C   GLU A  35      37.513  32.333  12.062  1.00  9.15           C  
ATOM    279  O   GLU A  35      36.605  31.709  12.614  1.00  8.95           O  
ATOM    280  CB  GLU A  35      37.886  34.587  13.076  1.00  9.96           C  
ATOM    281  CG  GLU A  35      36.569  34.614  13.845  1.00 10.77           C  
ATOM    282  CD  GLU A  35      35.964  36.001  13.959  1.00 11.17           C  
ATOM    283  OE1 GLU A  35      36.717  36.997  13.912  1.00 13.50           O  
ATOM    284  OE2 GLU A  35      34.725  36.080  14.110  1.00 12.43           O  
ATOM    285  N   TYR A  36      37.697  32.350  10.740  1.00  9.05           N  
ATOM    286  CA  TYR A  36      36.666  31.827   9.834  1.00  8.87           C  
ATOM    287  C   TYR A  36      36.948  30.470   9.210  1.00  8.36           C  
ATOM    288  O   TYR A  36      36.065  29.906   8.565  1.00  8.95           O  
ATOM    289  CB  TYR A  36      36.400  32.834   8.721  1.00  8.43           C  
ATOM    290  CG  TYR A  36      35.936  34.199   9.186  1.00  9.31           C  
ATOM    291  CD1 TYR A  36      34.973  34.344  10.193  1.00 10.07           C  
ATOM    292  CD2 TYR A  36      36.419  35.339   8.569  1.00 10.24           C  
ATOM    293  CE1 TYR A  36      34.543  35.610  10.593  1.00 10.05           C  
ATOM    294  CE2 TYR A  36      35.978  36.609   8.953  1.00 10.57           C  
ATOM    295  CZ  TYR A  36      35.047  36.728   9.958  1.00  9.71           C  
ATOM    296  OH  TYR A  36      34.603  37.997  10.336  1.00 11.74           O  
ATOM    297  N   ASP A  37      38.157  29.961   9.436  1.00  8.63           N  
ATOM    298  CA  ASP A  37      38.647  28.663   8.943  1.00  8.54           C  
ATOM    299  C   ASP A  37      37.504  27.643   8.956  1.00  8.43           C  
ATOM    300  O   ASP A  37      36.961  27.359  10.023  1.00  8.40           O  
ATOM    301  CB  ASP A  37      39.789  28.231   9.885  1.00  8.99           C  
ATOM    302  CG  ASP A  37      40.556  27.013   9.405  1.00  9.29           C  
ATOM    303  OD1 ASP A  37      40.322  26.542   8.275  1.00  9.83           O  
ATOM    304  OD2 ASP A  37      41.399  26.519  10.200  1.00 10.94           O  
ATOM    305  N   PRO A  38      37.176  27.024   7.801  1.00  8.06           N  
ATOM    306  CA  PRO A  38      37.888  26.997   6.524  1.00  8.01           C  
ATOM    307  C   PRO A  38      37.534  28.095   5.522  1.00  8.43           C  
ATOM    308  O   PRO A  38      38.006  28.054   4.379  1.00  8.77           O  
ATOM    309  CB  PRO A  38      37.460  25.642   5.938  1.00  8.05           C  
ATOM    310  CG  PRO A  38      35.999  25.501   6.406  1.00  8.23           C  
ATOM    311  CD  PRO A  38      35.969  26.167   7.776  1.00  8.32           C  
ATOM    312  N   PHE A  39      36.699  29.053   5.916  1.00  8.19           N  
ATOM    313  CA  PHE A  39      36.279  30.107   4.984  1.00  8.48           C  
ATOM    314  C   PHE A  39      37.271  31.256   4.975  1.00  8.92           C  
ATOM    315  O   PHE A  39      37.875  31.563   6.004  1.00  9.49           O  
ATOM    316  CB  PHE A  39      34.862  30.568   5.323  1.00  8.25           C  
ATOM    317  CG  PHE A  39      33.903  29.430   5.429  1.00  8.32           C  
ATOM    318  CD1 PHE A  39      33.639  28.637   4.322  1.00  8.58           C  
ATOM    319  CD2 PHE A  39      33.316  29.099   6.636  1.00  9.09           C  
ATOM    320  CE1 PHE A  39      32.772  27.543   4.400  1.00  9.54           C  
ATOM    321  CE2 PHE A  39      32.442  28.018   6.715  1.00  8.47           C  
ATOM    322  CZ  PHE A  39      32.172  27.242   5.593  1.00  9.03           C  
ATOM    323  N   LEU A  40      37.464  31.860   3.806  1.00  9.21           N  
ATOM    324  CA  LEU A  40      38.453  32.929   3.668  1.00 10.29           C  
ATOM    325  C   LEU A  40      37.810  34.289   3.504  1.00 11.06           C  
ATOM    326  O   LEU A  40      38.388  35.305   3.894  1.00 12.03           O  
ATOM    327  CB  LEU A  40      39.402  32.634   2.504  1.00 10.93           C  
ATOM    328  CG  LEU A  40      40.288  31.410   2.679  1.00 12.27           C  
ATOM    329  CD1 LEU A  40      40.894  31.025   1.343  1.00 12.20           C  
ATOM    330  CD2 LEU A  40      41.373  31.629   3.746  1.00 15.03           C  
ATOM    331  N   LEU A  41      36.617  34.302   2.920  1.00 11.05           N  
ATOM    332  CA  LEU A  41      35.849  35.529   2.763  1.00 12.07           C  
ATOM    333  C   LEU A  41      34.460  35.205   2.234  1.00 11.10           C  
ATOM    334  O   LEU A  41      34.218  34.119   1.701  1.00 11.04           O  
ATOM    335  CB  LEU A  41      36.562  36.557   1.870  1.00 13.54           C  
ATOM    336  CG  LEU A  41      36.795  36.263   0.394  1.00 15.24           C  
ATOM    337  CD1 LEU A  41      35.553  36.545  -0.450  1.00 17.94           C  
ATOM    338  CD2 LEU A  41      37.967  37.111  -0.127  1.00 14.53           C  
ATOM    339  N   LEU A  42      33.545  36.148   2.420  1.00 11.18           N  
ATOM    340  CA  LEU A  42      32.222  36.055   1.818  1.00 11.17           C  
ATOM    341  C   LEU A  42      31.836  37.466   1.419  1.00 11.83           C  
ATOM    342  O   LEU A  42      31.786  38.354   2.272  1.00 11.66           O  
ATOM    343  CB  LEU A  42      31.193  35.487   2.800  1.00 11.49           C  
ATOM    344  CG  LEU A  42      29.750  35.428   2.273  1.00 11.97           C  
ATOM    345  CD1 LEU A  42      29.601  34.571   1.010  1.00 12.45           C  
ATOM    346  CD2 LEU A  42      28.830  34.906   3.365  1.00 12.03           C  
HETATM  347  N   MSE A  43      31.592  37.650   0.128  1.00 12.78           N  
HETATM  348  CA  MSE A  43      31.301  38.962  -0.438  1.00 14.64           C  
HETATM  349  C   MSE A  43      29.920  38.973  -1.075  1.00 13.34           C  
HETATM  350  O   MSE A  43      29.551  38.028  -1.782  1.00 12.68           O  
HETATM  351  CB  MSE A  43      32.349  39.284  -1.495  1.00 15.22           C  
HETATM  352  CG  MSE A  43      32.206  40.637  -2.127  1.00 17.18           C  
HETATM  353 SE   MSE A  43      33.836  41.073  -3.048  0.30 20.70          SE  
HETATM  354  CE  MSE A  43      35.046  41.016  -1.528  1.00 22.15           C  
ATOM    355  N   GLU A  44      29.172  40.047  -0.823  1.00 12.78           N  
ATOM    356  CA  GLU A  44      27.895  40.291  -1.472  1.00 12.76           C  
ATOM    357  C   GLU A  44      28.123  41.270  -2.606  1.00 12.62           C  
ATOM    358  O   GLU A  44      28.775  42.294  -2.417  1.00 12.72           O  
ATOM    359  CB  GLU A  44      26.883  40.867  -0.481  1.00 13.07           C  
ATOM    360  CG  GLU A  44      25.530  41.202  -1.107  1.00 14.54           C  
ATOM    361  CD  GLU A  44      24.652  42.080  -0.223  0.60 14.02           C  
ATOM    362  OE1 GLU A  44      25.181  42.915   0.550  0.50 14.64           O  
ATOM    363  OE2 GLU A  44      23.418  41.942  -0.320  1.00 17.70           O  
ATOM    364  N   ASP A  45      27.598  40.943  -3.785  1.00 12.20           N  
ATOM    365  CA  ASP A  45      27.755  41.808  -4.957  1.00 12.01           C  
ATOM    366  C   ASP A  45      26.428  42.032  -5.648  1.00 11.73           C  
ATOM    367  O   ASP A  45      25.615  41.114  -5.770  1.00 11.50           O  
ATOM    368  CB  ASP A  45      28.742  41.200  -5.951  1.00 12.18           C  
ATOM    369  CG  ASP A  45      30.156  41.175  -5.417  1.00 14.64           C  
ATOM    370  OD1 ASP A  45      30.818  42.233  -5.441  1.00 15.12           O  
ATOM    371  OD2 ASP A  45      30.604  40.096  -4.983  1.00 17.14           O  
ATOM    372  N   ILE A  46      26.208  43.271  -6.080  1.00 11.04           N  
ATOM    373  CA  ILE A  46      25.116  43.593  -6.979  1.00 11.25           C  
ATOM    374  C   ILE A  46      25.779  44.214  -8.196  1.00 11.21           C  
ATOM    375  O   ILE A  46      26.425  45.263  -8.079  1.00 11.01           O  
ATOM    376  CB  ILE A  46      24.122  44.587  -6.336  1.00 11.23           C  
ATOM    377  CG1 ILE A  46      23.532  43.994  -5.050  1.00 12.28           C  
ATOM    378  CG2 ILE A  46      23.035  44.980  -7.349  1.00 11.34           C  
ATOM    379  CD1 ILE A  46      22.680  44.952  -4.262  1.00 13.67           C  
ATOM    380  N   PHE A  47      25.649  43.580  -9.357  1.00 10.52           N  
ATOM    381  CA  PHE A  47      26.455  43.991 -10.503  1.00 10.95           C  
ATOM    382  C   PHE A  47      25.794  43.778 -11.854  1.00 11.55           C  
ATOM    383  O   PHE A  47      24.896  42.943 -11.993  1.00 11.18           O  
ATOM    384  CB  PHE A  47      27.877  43.396 -10.446  1.00 10.94           C  
ATOM    385  CG  PHE A  47      27.932  41.885 -10.457  1.00 10.74           C  
ATOM    386  CD1 PHE A  47      28.460  41.209 -11.548  1.00 11.25           C  
ATOM    387  CD2 PHE A  47      27.494  41.143  -9.358  1.00 10.19           C  
ATOM    388  CE1 PHE A  47      28.544  39.827 -11.556  1.00 11.85           C  
ATOM    389  CE2 PHE A  47      27.566  39.749  -9.353  1.00  9.92           C  
ATOM    390  CZ  PHE A  47      28.093  39.085 -10.465  1.00 10.62           C  
ATOM    391  N   GLU A  48      26.239  44.562 -12.834  1.00 12.63           N  
ATOM    392  CA  GLU A  48      25.742  44.471 -14.199  1.00 14.26           C  
ATOM    393  C   GLU A  48      26.807  43.910 -15.135  1.00 14.26           C  
ATOM    394  O   GLU A  48      27.972  43.758 -14.751  1.00 14.10           O  
ATOM    395  CB  GLU A  48      25.264  45.851 -14.678  1.00 14.10           C  
ATOM    396  CG  GLU A  48      24.077  46.393 -13.866  1.00 16.42           C  
ATOM    397  CD  GLU A  48      23.724  47.843 -14.166  1.00 17.60           C  
ATOM    398  OE1 GLU A  48      23.667  48.233 -15.359  0.80 21.30           O  
ATOM    399  OE2 GLU A  48      23.480  48.592 -13.196  0.50 18.20           O  
ATOM    400  N   ARG A  49      26.394  43.591 -16.358  1.00 14.70           N  
ATOM    401  CA  ARG A  49      27.285  43.063 -17.387  1.00 15.37           C  
ATOM    402  C   ARG A  49      28.482  43.989 -17.586  1.00 15.18           C  
ATOM    403  O   ARG A  49      28.331  45.214 -17.684  1.00 15.48           O  
ATOM    404  CB  ARG A  49      26.530  42.886 -18.708  1.00 15.77           C  
ATOM    405  CG  ARG A  49      27.265  42.062 -19.752  1.00 17.12           C  
ATOM    406  CD  ARG A  49      26.311  41.623 -20.850  1.00 17.57           C  
ATOM    407  NE  ARG A  49      26.951  40.805 -21.883  1.00 19.83           N  
ATOM    408  CZ  ARG A  49      27.140  39.489 -21.806  1.00 20.56           C  
ATOM    409  NH1 ARG A  49      26.754  38.796 -20.735  1.00 19.09           N  
ATOM    410  NH2 ARG A  49      27.721  38.856 -22.818  1.00 21.98           N  
ATOM    411  N   GLY A  50      29.667  43.384 -17.615  1.00 15.40           N  
ATOM    412  CA  GLY A  50      30.919  44.107 -17.844  1.00 15.62           C  
ATOM    413  C   GLY A  50      31.685  44.497 -16.593  1.00 15.67           C  
ATOM    414  O   GLY A  50      32.772  45.075 -16.680  1.00 15.77           O  
ATOM    415  N   THR A  51      31.122  44.185 -15.424  1.00 15.11           N  
ATOM    416  CA  THR A  51      31.735  44.559 -14.149  1.00 15.25           C  
ATOM    417  C   THR A  51      33.115  43.925 -13.951  1.00 15.64           C  
ATOM    418  O   THR A  51      34.094  44.626 -13.661  1.00 16.06           O  
ATOM    419  CB  THR A  51      30.827  44.192 -12.952  1.00 14.85           C  
ATOM    420  OG1 THR A  51      29.620  44.962 -13.014  1.00 14.48           O  
ATOM    421  CG2 THR A  51      31.529  44.484 -11.637  1.00 14.61           C  
ATOM    422  N   PHE A  52      33.176  42.605 -14.096  1.00 15.73           N  
ATOM    423  CA  PHE A  52      34.394  41.863 -13.805  1.00 16.40           C  
ATOM    424  C   PHE A  52      35.175  41.477 -15.051  1.00 16.71           C  
ATOM    425  O   PHE A  52      34.617  41.326 -16.136  1.00 17.56           O  
ATOM    426  CB  PHE A  52      34.075  40.619 -12.978  1.00 16.18           C  
ATOM    427  CG  PHE A  52      33.515  40.928 -11.627  1.00 15.60           C  
ATOM    428  CD1 PHE A  52      34.300  41.555 -10.662  1.00 15.48           C  
ATOM    429  CD2 PHE A  52      32.203  40.598 -11.311  1.00 16.47           C  
ATOM    430  CE1 PHE A  52      33.780  41.856  -9.406  1.00 16.74           C  
ATOM    431  CE2 PHE A  52      31.682  40.892 -10.068  1.00 15.74           C  
ATOM    432  CZ  PHE A  52      32.467  41.515  -9.111  1.00 16.00           C  
ATOM    433  N   ASP A  53      36.481  41.334 -14.867  1.00 17.48           N  
ATOM    434  CA  ASP A  53      37.368  40.821 -15.894  1.00 18.12           C  
ATOM    435  C   ASP A  53      37.734  39.384 -15.552  1.00 17.73           C  
ATOM    436  O   ASP A  53      37.445  38.898 -14.457  1.00 18.05           O  
ATOM    437  CB  ASP A  53      38.628  41.682 -15.972  1.00 18.87           C  
ATOM    438  CG  ASP A  53      38.338  43.098 -16.451  1.00 21.47           C  
ATOM    439  OD1 ASP A  53      37.512  43.267 -17.374  1.00 25.94           O  
ATOM    440  OD2 ASP A  53      38.941  44.040 -15.900  1.00 25.79           O  
ATOM    441  N   VAL A  54      38.365  38.705 -16.500  1.00 17.36           N  
ATOM    442  CA  VAL A  54      38.831  37.345 -16.278  1.00 17.15           C  
ATOM    443  C   VAL A  54      40.007  37.392 -15.305  1.00 16.82           C  
ATOM    444  O   VAL A  54      40.918  38.219 -15.454  1.00 17.57           O  
ATOM    445  CB  VAL A  54      39.249  36.698 -17.615  1.00 17.17           C  
ATOM    446  CG1 VAL A  54      39.956  35.375 -17.375  1.00 17.66           C  
ATOM    447  CG2 VAL A  54      38.036  36.505 -18.521  1.00 18.36           C  
ATOM    448  N   HIS A  55      39.979  36.524 -14.297  1.00 15.97           N  
ATOM    449  CA  HIS A  55      41.013  36.519 -13.259  1.00 16.10           C  
ATOM    450  C   HIS A  55      41.370  35.093 -12.864  1.00 14.88           C  
ATOM    451  O   HIS A  55      40.500  34.235 -12.805  1.00 13.65           O  
ATOM    452  CB  HIS A  55      40.552  37.257 -11.992  1.00 17.31           C  
ATOM    453  CG  HIS A  55      40.368  38.732 -12.167  1.00 19.12           C  
ATOM    454  ND1 HIS A  55      41.382  39.566 -12.592  0.60 20.46           N  
ATOM    455  CD2 HIS A  55      39.297  39.529 -11.939  0.80 21.13           C  
ATOM    456  CE1 HIS A  55      40.935  40.810 -12.640  0.90 21.22           C  
ATOM    457  NE2 HIS A  55      39.676  40.816 -12.241  0.80 21.64           N  
ATOM    458  N   PRO A  56      42.656  34.833 -12.594  1.00 14.11           N  
ATOM    459  CA  PRO A  56      43.069  33.545 -12.050  1.00 14.13           C  
ATOM    460  C   PRO A  56      42.763  33.380 -10.556  1.00 13.90           C  
ATOM    461  O   PRO A  56      42.704  34.364  -9.809  1.00 14.97           O  
ATOM    462  CB  PRO A  56      44.582  33.543 -12.289  1.00 14.12           C  
ATOM    463  CG  PRO A  56      44.954  34.985 -12.258  1.00 14.49           C  
ATOM    464  CD  PRO A  56      43.811  35.716 -12.868  1.00 14.83           C  
ATOM    465  N   HIS A  57      42.551  32.132 -10.154  1.00 13.24           N  
ATOM    466  CA  HIS A  57      42.580  31.730  -8.753  1.00 13.11           C  
ATOM    467  C   HIS A  57      43.345  30.415  -8.634  1.00 12.59           C  
ATOM    468  O   HIS A  57      43.384  29.622  -9.567  1.00 11.96           O  
ATOM    469  CB  HIS A  57      41.165  31.528  -8.191  1.00 13.98           C  
ATOM    470  CG  HIS A  57      40.396  32.796  -7.988  1.00 15.46           C  
ATOM    471  ND1 HIS A  57      40.780  33.770  -7.089  1.00 18.75           N  
ATOM    472  CD2 HIS A  57      39.246  33.235  -8.550  1.00 18.74           C  
ATOM    473  CE1 HIS A  57      39.906  34.761  -7.121  1.00 19.28           C  
ATOM    474  NE2 HIS A  57      38.970  34.465  -8.003  1.00 20.14           N  
ATOM    475  N   ARG A  58      43.951  30.196  -7.475  1.00 12.76           N  
ATOM    476  CA  ARG A  58      44.595  28.924  -7.171  1.00 13.29           C  
ATOM    477  C   ARG A  58      44.549  28.637  -5.683  1.00 11.86           C  
ATOM    478  O   ARG A  58      44.519  29.559  -4.872  1.00 12.16           O  
ATOM    479  CB  ARG A  58      46.037  28.865  -7.715  1.00 14.13           C  
ATOM    480  CG  ARG A  58      47.043  29.836  -7.118  1.00 15.71           C  
ATOM    481  CD  ARG A  58      48.373  29.761  -7.885  1.00 16.69           C  
ATOM    482  NE  ARG A  58      49.407  30.593  -7.270  0.60 19.17           N  
ATOM    483  CZ  ARG A  58      50.593  29.819  -7.594  0.00 37.11           C  
ATOM    484  NH1 ARG A  58      51.151  27.940  -7.883  0.90 25.66           N  
ATOM    485  NH2 ARG A  58      51.514  30.733  -7.283  0.00 20.11           N  
ATOM    486  N   GLY A  59      44.495  27.353  -5.342  1.00 11.12           N  
ATOM    487  CA  GLY A  59      44.624  26.935  -3.949  1.00 10.03           C  
ATOM    488  C   GLY A  59      43.397  27.162  -3.080  1.00  9.96           C  
ATOM    489  O   GLY A  59      43.480  27.068  -1.851  1.00 10.54           O  
ATOM    490  N   ILE A  60      42.266  27.468  -3.721  1.00  9.42           N  
ATOM    491  CA  ILE A  60      41.004  27.767  -3.029  1.00  9.25           C  
ATOM    492  C   ILE A  60      39.850  27.169  -3.816  1.00  8.39           C  
ATOM    493  O   ILE A  60      40.040  26.662  -4.927  1.00  8.96           O  
ATOM    494  CB  ILE A  60      40.765  29.300  -2.846  1.00  9.31           C  
ATOM    495  CG1 ILE A  60      40.514  30.004  -4.191  1.00 10.19           C  
ATOM    496  CG2 ILE A  60      41.911  29.939  -2.049  1.00  9.82           C  
ATOM    497  CD1 ILE A  60      40.010  31.458  -4.020  1.00 10.28           C  
ATOM    498  N   GLU A  61      38.668  27.189  -3.208  1.00  8.44           N  
ATOM    499  CA  GLU A  61      37.410  27.000  -3.922  1.00  8.36           C  
ATOM    500  C   GLU A  61      36.567  28.263  -3.789  1.00  8.63           C  
ATOM    501  O   GLU A  61      36.657  28.979  -2.791  1.00  9.26           O  
ATOM    502  CB  GLU A  61      36.613  25.823  -3.366  1.00  8.35           C  
ATOM    503  CG  GLU A  61      37.403  24.528  -3.259  1.00  8.98           C  
ATOM    504  CD  GLU A  61      36.497  23.380  -2.894  1.00 10.24           C  
ATOM    505  OE1 GLU A  61      36.053  23.326  -1.719  1.00 11.97           O  
ATOM    506  OE2 GLU A  61      36.191  22.561  -3.772  1.00 10.62           O  
ATOM    507  N   THR A  62      35.752  28.542  -4.800  1.00  9.01           N  
ATOM    508  CA  THR A  62      34.766  29.612  -4.686  1.00  9.46           C  
ATOM    509  C   THR A  62      33.375  29.030  -4.842  1.00  9.05           C  
ATOM    510  O   THR A  62      33.165  28.097  -5.626  1.00  9.44           O  
ATOM    511  CB  THR A  62      34.963  30.729  -5.709  1.00 10.25           C  
ATOM    512  OG1 THR A  62      34.750  30.215  -7.024  1.00 12.61           O  
ATOM    513  CG2 THR A  62      36.377  31.309  -5.613  1.00 11.92           C  
ATOM    514  N   VAL A  63      32.433  29.567  -4.074  1.00  8.52           N  
ATOM    515  CA  VAL A  63      31.061  29.074  -4.097  1.00  8.69           C  
ATOM    516  C   VAL A  63      30.145  30.261  -4.254  1.00  8.77           C  
ATOM    517  O   VAL A  63      30.139  31.146  -3.390  1.00  8.76           O  
ATOM    518  CB  VAL A  63      30.713  28.322  -2.808  1.00  8.19           C  
ATOM    519  CG1 VAL A  63      29.301  27.756  -2.912  1.00  8.74           C  
ATOM    520  CG2 VAL A  63      31.691  27.161  -2.566  1.00  8.63           C  
ATOM    521  N   THR A  64      29.385  30.283  -5.353  1.00  8.79           N  
ATOM    522  CA  THR A  64      28.495  31.407  -5.651  1.00  9.44           C  
ATOM    523  C   THR A  64      27.055  31.002  -5.433  1.00  9.29           C  
ATOM    524  O   THR A  64      26.647  29.936  -5.883  1.00 10.12           O  
ATOM    525  CB  THR A  64      28.614  31.839  -7.123  1.00  9.79           C  
ATOM    526  OG1 THR A  64      29.993  31.911  -7.504  1.00 12.28           O  
ATOM    527  CG2 THR A  64      27.960  33.200  -7.355  1.00 10.50           C  
ATOM    528  N   TYR A  65      26.304  31.833  -4.709  1.00  9.03           N  
ATOM    529  CA  TYR A  65      24.854  31.702  -4.619  1.00  8.59           C  
ATOM    530  C   TYR A  65      24.234  32.918  -5.297  1.00  8.58           C  
ATOM    531  O   TYR A  65      24.572  34.057  -4.961  1.00  8.33           O  
ATOM    532  CB  TYR A  65      24.385  31.589  -3.155  1.00  9.01           C  
ATOM    533  CG  TYR A  65      22.867  31.612  -3.008  1.00  9.82           C  
ATOM    534  CD1 TYR A  65      22.131  30.428  -2.965  1.00  8.88           C  
ATOM    535  CD2 TYR A  65      22.179  32.817  -2.927  1.00  9.86           C  
ATOM    536  CE1 TYR A  65      20.744  30.443  -2.846  1.00 10.25           C  
ATOM    537  CE2 TYR A  65      20.780  32.852  -2.811  1.00 10.13           C  
ATOM    538  CZ  TYR A  65      20.074  31.665  -2.774  1.00 10.56           C  
ATOM    539  OH  TYR A  65      18.693  31.710  -2.661  1.00 11.89           O  
ATOM    540  N   VAL A  66      23.355  32.681  -6.266  1.00  9.08           N  
ATOM    541  CA  VAL A  66      22.683  33.785  -6.953  1.00  9.91           C  
ATOM    542  C   VAL A  66      21.367  34.093  -6.248  1.00 10.22           C  
ATOM    543  O   VAL A  66      20.466  33.249  -6.196  1.00 10.52           O  
ATOM    544  CB  VAL A  66      22.464  33.474  -8.459  1.00 10.38           C  
ATOM    545  CG1 VAL A  66      21.644  34.561  -9.120  1.00 10.40           C  
ATOM    546  CG2 VAL A  66      23.804  33.326  -9.159  1.00 11.42           C  
ATOM    547  N   ILE A  67      21.269  35.289  -5.675  1.00 10.68           N  
ATOM    548  CA  ILE A  67      20.036  35.707  -5.009  1.00 11.60           C  
ATOM    549  C   ILE A  67      18.999  36.068  -6.060  1.00 11.72           C  
ATOM    550  O   ILE A  67      17.850  35.606  -5.999  1.00 13.39           O  
ATOM    551  CB  ILE A  67      20.278  36.892  -4.042  1.00 11.18           C  
ATOM    552  CG1 ILE A  67      21.361  36.543  -3.012  1.00 11.13           C  
ATOM    553  CG2 ILE A  67      18.962  37.304  -3.349  1.00 12.13           C  
ATOM    554  CD1 ILE A  67      21.859  37.737  -2.186  1.00 11.82           C  
ATOM    555  N   SER A  68      19.409  36.883  -7.034  1.00 12.09           N  
ATOM    556  CA  SER A  68      18.527  37.309  -8.105  1.00 12.12           C  
ATOM    557  C   SER A  68      19.340  37.616  -9.356  1.00 12.24           C  
ATOM    558  O   SER A  68      20.560  37.825  -9.290  1.00 12.03           O  
ATOM    559  CB  SER A  68      17.700  38.526  -7.681  1.00 12.66           C  
ATOM    560  OG  SER A  68      18.531  39.643  -7.412  1.00 12.73           O  
ATOM    561  N   GLY A  69      18.667  37.636 -10.500  1.00 12.12           N  
ATOM    562  CA  GLY A  69      19.323  37.887 -11.776  1.00 12.35           C  
ATOM    563  C   GLY A  69      19.800  36.621 -12.463  1.00 12.75           C  
ATOM    564  O   GLY A  69      19.676  35.518 -11.918  1.00 12.86           O  
ATOM    565  N   GLU A  70      20.324  36.791 -13.673  1.00 13.32           N  
ATOM    566  CA  GLU A  70      20.792  35.677 -14.484  1.00 13.57           C  
ATOM    567  C   GLU A  70      22.286  35.835 -14.698  1.00 13.32           C  
ATOM    568  O   GLU A  70      22.736  36.841 -15.252  1.00 13.51           O  
ATOM    569  CB  GLU A  70      20.052  35.626 -15.824  1.00 14.59           C  
ATOM    570  CG  GLU A  70      18.525  35.508 -15.699  1.00 16.40           C  
ATOM    571  CD  GLU A  70      18.046  34.179 -15.115  0.50 18.19           C  
ATOM    572  OE1 GLU A  70      18.782  33.169 -15.196  0.50 19.37           O  
ATOM    573  OE2 GLU A  70      16.912  34.144 -14.580  0.50 18.78           O  
ATOM    574  N   LEU A  71      23.046  34.848 -14.230  1.00 13.39           N  
ATOM    575  CA  LEU A  71      24.508  34.909 -14.275  1.00 13.42           C  
ATOM    576  C   LEU A  71      25.095  33.989 -15.344  1.00 13.47           C  
ATOM    577  O   LEU A  71      24.677  32.841 -15.471  1.00 13.82           O  
ATOM    578  CB  LEU A  71      25.101  34.554 -12.901  1.00 13.65           C  
ATOM    579  CG  LEU A  71      26.610  34.715 -12.668  1.00 13.84           C  
ATOM    580  CD1 LEU A  71      27.039  36.162 -12.861  1.00 13.09           C  
ATOM    581  CD2 LEU A  71      27.000  34.238 -11.283  1.00 14.17           C  
ATOM    582  N   GLU A  72      26.052  34.517 -16.102  1.00 13.23           N  
ATOM    583  CA  GLU A  72      26.841  33.724 -17.035  1.00 13.62           C  
ATOM    584  C   GLU A  72      28.193  33.433 -16.398  1.00 13.20           C  
ATOM    585  O   GLU A  72      28.936  34.354 -16.015  1.00 14.19           O  
ATOM    586  CB  GLU A  72      27.037  34.469 -18.361  1.00 14.02           C  
ATOM    587  CG  GLU A  72      25.756  34.654 -19.140  1.00 14.68           C  
ATOM    588  CD  GLU A  72      25.920  35.519 -20.379  1.00 15.43           C  
ATOM    589  OE1 GLU A  72      27.066  35.832 -20.773  0.50 15.54           O  
ATOM    590  OE2 GLU A  72      24.883  35.896 -20.956  1.00 19.76           O  
ATOM    591  N   HIS A  73      28.507  32.151 -16.276  1.00 12.34           N  
ATOM    592  CA  HIS A  73      29.793  31.733 -15.714  1.00 12.55           C  
ATOM    593  C   HIS A  73      30.752  31.267 -16.801  1.00 12.10           C  
ATOM    594  O   HIS A  73      30.362  30.567 -17.739  1.00 13.10           O  
ATOM    595  CB  HIS A  73      29.604  30.599 -14.712  1.00 12.74           C  
ATOM    596  CG  HIS A  73      30.882  29.915 -14.346  1.00 12.05           C  
ATOM    597  ND1 HIS A  73      31.745  30.424 -13.403  1.00 12.30           N  
ATOM    598  CD2 HIS A  73      31.459  28.782 -14.815  1.00 12.42           C  
ATOM    599  CE1 HIS A  73      32.802  29.634 -13.303  1.00 12.11           C  
ATOM    600  NE2 HIS A  73      32.651  28.631 -14.151  1.00 11.98           N  
ATOM    601  N   PHE A  74      32.015  31.653 -16.667  1.00 11.61           N  
ATOM    602  CA  PHE A  74      33.078  31.055 -17.452  1.00 11.59           C  
ATOM    603  C   PHE A  74      34.213  30.585 -16.556  1.00 11.43           C  
ATOM    604  O   PHE A  74      34.598  31.286 -15.621  1.00 10.76           O  
ATOM    605  CB  PHE A  74      33.632  32.051 -18.482  1.00 12.08           C  
ATOM    606  CG  PHE A  74      34.907  31.589 -19.110  1.00 12.75           C  
ATOM    607  CD1 PHE A  74      34.880  30.661 -20.143  1.00 14.59           C  
ATOM    608  CD2 PHE A  74      36.136  32.030 -18.623  1.00 12.36           C  
ATOM    609  CE1 PHE A  74      36.072  30.193 -20.709  1.00 14.85           C  
ATOM    610  CE2 PHE A  74      37.326  31.565 -19.181  1.00 14.53           C  
ATOM    611  CZ  PHE A  74      37.290  30.659 -20.224  1.00 13.35           C  
ATOM    612  N   ASP A  75      34.763  29.413 -16.861  1.00 11.08           N  
ATOM    613  CA  ASP A  75      36.089  29.067 -16.363  1.00 10.92           C  
ATOM    614  C   ASP A  75      36.895  28.290 -17.412  1.00 10.88           C  
ATOM    615  O   ASP A  75      36.339  27.695 -18.340  1.00 11.07           O  
ATOM    616  CB  ASP A  75      36.014  28.324 -15.014  1.00 10.84           C  
ATOM    617  CG  ASP A  75      35.476  26.923 -15.147  1.00 11.97           C  
ATOM    618  OD1 ASP A  75      36.232  26.041 -15.610  1.00 13.59           O  
ATOM    619  OD2 ASP A  75      34.297  26.707 -14.789  1.00 13.95           O  
ATOM    620  N   SER A  76      38.215  28.314 -17.254  1.00 10.75           N  
ATOM    621  CA  SER A  76      39.128  27.757 -18.250  1.00 11.77           C  
ATOM    622  C   SER A  76      39.292  26.245 -18.196  1.00 12.54           C  
ATOM    623  O   SER A  76      40.037  25.680 -18.997  1.00 12.92           O  
ATOM    624  CB  SER A  76      40.490  28.439 -18.165  1.00 11.19           C  
ATOM    625  OG  SER A  76      41.072  28.270 -16.877  1.00 11.63           O  
ATOM    626  N   LYS A  77      38.588  25.599 -17.268  1.00 12.92           N  
ATOM    627  CA  LYS A  77      38.525  24.147 -17.242  1.00 14.01           C  
ATOM    628  C   LYS A  77      37.288  23.643 -17.982  1.00 13.98           C  
ATOM    629  O   LYS A  77      37.403  22.853 -18.927  1.00 14.41           O  
ATOM    630  CB  LYS A  77      38.559  23.610 -15.794  1.00 14.34           C  
ATOM    631  CG  LYS A  77      38.506  22.079 -15.667  1.00 16.25           C  
ATOM    632  CD  LYS A  77      39.766  21.443 -16.231  1.00 19.93           C  
ATOM    633  CE  LYS A  77      39.866  19.963 -15.873  1.00 23.00           C  
ATOM    634  NZ  LYS A  77      38.928  19.129 -16.672  1.00 26.78           N  
ATOM    635  N   ALA A  78      36.116  24.119 -17.562  1.00 13.78           N  
ATOM    636  CA  ALA A  78      34.837  23.594 -18.040  1.00 13.88           C  
ATOM    637  C   ALA A  78      34.126  24.472 -19.076  1.00 14.00           C  
ATOM    638  O   ALA A  78      33.182  24.023 -19.737  1.00 15.10           O  
ATOM    639  CB  ALA A  78      33.912  23.307 -16.859  1.00 14.35           C  
ATOM    640  N   GLY A  79      34.565  25.722 -19.218  1.00 13.30           N  
ATOM    641  CA  GLY A  79      33.957  26.628 -20.195  1.00 13.27           C  
ATOM    642  C   GLY A  79      32.754  27.372 -19.643  1.00 13.25           C  
ATOM    643  O   GLY A  79      32.795  27.868 -18.513  1.00 12.99           O  
ATOM    644  N   HIS A  80      31.682  27.443 -20.432  1.00 14.23           N  
ATOM    645  CA  HIS A  80      30.521  28.270 -20.087  1.00 14.93           C  
ATOM    646  C   HIS A  80      29.382  27.532 -19.417  1.00 15.09           C  
ATOM    647  O   HIS A  80      29.040  26.402 -19.791  1.00 15.21           O  
ATOM    648  CB  HIS A  80      29.968  28.964 -21.329  1.00 15.93           C  
ATOM    649  CG  HIS A  80      30.646  30.250 -21.646  1.00 18.35           C  
ATOM    650  ND1 HIS A  80      30.290  31.441 -21.052  1.00 22.57           N  
ATOM    651  CD2 HIS A  80      31.659  30.538 -22.495  1.00 21.04           C  
ATOM    652  CE1 HIS A  80      31.065  32.407 -21.512  1.00 22.45           C  
ATOM    653  NE2 HIS A  80      31.898  31.887 -22.394  1.00 22.13           N  
ATOM    654  N   SER A  81      28.776  28.205 -18.439  1.00 14.55           N  
ATOM    655  CA  SER A  81      27.568  27.723 -17.793  1.00 15.14           C  
ATOM    656  C   SER A  81      26.710  28.924 -17.399  1.00 14.76           C  
ATOM    657  O   SER A  81      27.130  30.066 -17.550  1.00 14.91           O  
ATOM    658  CB  SER A  81      27.916  26.903 -16.564  1.00 15.12           C  
ATOM    659  OG  SER A  81      28.362  27.741 -15.513  1.00 19.74           O  
ATOM    660  N   THR A  82      25.500  28.654 -16.923  1.00 14.94           N  
ATOM    661  CA  THR A  82      24.615  29.712 -16.439  1.00 15.11           C  
ATOM    662  C   THR A  82      24.034  29.356 -15.080  1.00 15.32           C  
ATOM    663  O   THR A  82      23.959  28.180 -14.711  1.00 15.69           O  
ATOM    664  CB  THR A  82      23.453  30.000 -17.415  1.00 15.13           C  
ATOM    665  OG1 THR A  82      22.719  28.798 -17.660  1.00 16.92           O  
ATOM    666  CG2 THR A  82      23.963  30.585 -18.743  1.00 15.64           C  
ATOM    667  N   LEU A  83      23.654  30.393 -14.343  1.00 14.43           N  
ATOM    668  CA  LEU A  83      22.973  30.261 -13.056  1.00 14.27           C  
ATOM    669  C   LEU A  83      21.822  31.233 -13.017  1.00 13.43           C  
ATOM    670  O   LEU A  83      21.942  32.350 -13.513  1.00 14.30           O  
ATOM    671  CB  LEU A  83      23.898  30.593 -11.877  1.00 14.55           C  
ATOM    672  CG  LEU A  83      24.988  29.643 -11.360  1.00 14.70           C  
ATOM    673  CD1 LEU A  83      25.591  30.197 -10.092  1.00 14.79           C  
ATOM    674  CD2 LEU A  83      24.509  28.218 -11.126  1.00 16.62           C  
ATOM    675  N   GLY A  84      20.716  30.803 -12.421  1.00 12.66           N  
ATOM    676  CA  GLY A  84      19.588  31.702 -12.178  1.00 12.14           C  
ATOM    677  C   GLY A  84      19.313  31.873 -10.695  1.00 11.76           C  
ATOM    678  O   GLY A  84      20.071  31.363  -9.852  1.00 11.66           O  
ATOM    679  N   PRO A  85      18.237  32.606 -10.357  1.00 11.79           N  
ATOM    680  CA  PRO A  85      17.892  32.843  -8.963  1.00 11.70           C  
ATOM    681  C   PRO A  85      17.781  31.560  -8.155  1.00 11.66           C  
ATOM    682  O   PRO A  85      17.073  30.637  -8.553  1.00 12.09           O  
ATOM    683  CB  PRO A  85      16.537  33.560  -9.056  1.00 12.04           C  
ATOM    684  CG  PRO A  85      16.628  34.288 -10.331  1.00 12.72           C  
ATOM    685  CD  PRO A  85      17.322  33.323 -11.263  1.00 12.16           C  
ATOM    686  N   GLY A  86      18.506  31.516  -7.038  1.00 11.06           N  
ATOM    687  CA  GLY A  86      18.481  30.360  -6.147  1.00 10.75           C  
ATOM    688  C   GLY A  86      19.490  29.270  -6.456  1.00 10.79           C  
ATOM    689  O   GLY A  86      19.587  28.303  -5.707  1.00 11.32           O  
ATOM    690  N   ASP A  87      20.231  29.422  -7.551  1.00 10.49           N  
ATOM    691  CA  ASP A  87      21.209  28.415  -7.970  1.00 10.24           C  
ATOM    692  C   ASP A  87      22.582  28.681  -7.369  1.00 10.10           C  
ATOM    693  O   ASP A  87      22.900  29.806  -6.976  1.00 10.09           O  
ATOM    694  CB  ASP A  87      21.334  28.391  -9.497  1.00 10.80           C  
ATOM    695  CG  ASP A  87      20.073  27.895 -10.194  1.00 11.75           C  
ATOM    696  OD1 ASP A  87      19.307  27.104  -9.593  1.00 12.20           O  
ATOM    697  OD2 ASP A  87      19.867  28.308 -11.361  1.00 14.33           O  
ATOM    698  N   VAL A  88      23.391  27.624  -7.319  1.00  9.37           N  
ATOM    699  CA  VAL A  88      24.738  27.689  -6.744  1.00  9.22           C  
ATOM    700  C   VAL A  88      25.742  27.082  -7.719  1.00  9.11           C  
ATOM    701  O   VAL A  88      25.397  26.217  -8.522  1.00  9.78           O  
ATOM    702  CB  VAL A  88      24.764  26.962  -5.359  1.00  8.96           C  
ATOM    703  CG1 VAL A  88      26.185  26.714  -4.839  1.00 10.06           C  
ATOM    704  CG2 VAL A  88      23.953  27.760  -4.321  1.00  8.60           C  
ATOM    705  N   GLN A  89      26.968  27.588  -7.700  1.00  9.04           N  
ATOM    706  CA  GLN A  89      28.071  26.898  -8.365  1.00  9.91           C  
ATOM    707  C   GLN A  89      29.244  26.743  -7.407  1.00  9.49           C  
ATOM    708  O   GLN A  89      29.472  27.595  -6.535  1.00  9.65           O  
ATOM    709  CB  GLN A  89      28.501  27.608  -9.655  1.00  9.93           C  
ATOM    710  CG  GLN A  89      29.043  29.009  -9.411  1.00 11.49           C  
ATOM    711  CD  GLN A  89      29.183  29.857 -10.680  1.00 11.03           C  
ATOM    712  OE1 GLN A  89      28.948  29.395 -11.796  1.00 12.42           O  
ATOM    713  NE2 GLN A  89      29.576  31.115 -10.495  1.00 12.74           N  
ATOM    714  N   TRP A  90      29.987  25.662  -7.592  1.00  9.35           N  
ATOM    715  CA  TRP A  90      31.100  25.308  -6.726  1.00  9.53           C  
ATOM    716  C   TRP A  90      32.316  25.142  -7.627  1.00  9.99           C  
ATOM    717  O   TRP A  90      32.376  24.205  -8.428  1.00  9.89           O  
ATOM    718  CB  TRP A  90      30.780  23.994  -6.016  1.00  9.78           C  
ATOM    719  CG  TRP A  90      31.506  23.774  -4.728  1.00  9.83           C  
ATOM    720  CD1 TRP A  90      32.834  23.440  -4.560  1.00  9.98           C  
ATOM    721  CD2 TRP A  90      30.941  23.861  -3.420  1.00  9.33           C  
ATOM    722  NE1 TRP A  90      33.115  23.309  -3.214  1.00  9.44           N  
ATOM    723  CE2 TRP A  90      31.973  23.573  -2.495  1.00  9.49           C  
ATOM    724  CE3 TRP A  90      29.654  24.165  -2.932  1.00  9.04           C  
ATOM    725  CZ2 TRP A  90      31.759  23.586  -1.110  1.00  9.09           C  
ATOM    726  CZ3 TRP A  90      29.440  24.180  -1.561  1.00 10.33           C  
ATOM    727  CH2 TRP A  90      30.490  23.892  -0.663  1.00 10.13           C  
HETATM  728  N   MSE A  91      33.275  26.054  -7.513  1.00 10.25           N  
HETATM  729  CA  MSE A  91      34.432  25.998  -8.388  1.00 11.78           C  
HETATM  730  C   MSE A  91      35.674  25.714  -7.568  1.00 10.73           C  
HETATM  731  O   MSE A  91      36.044  26.497  -6.700  1.00 10.81           O  
HETATM  732  CB  MSE A  91      34.593  27.296  -9.170  1.00 12.99           C  
HETATM  733  CG  MSE A  91      35.680  27.184 -10.224  1.00 15.90           C  
HETATM  734 SE   MSE A  91      36.147  28.857 -11.095  0.50 14.96          SE  
HETATM  735  CE  MSE A  91      34.529  29.879 -10.760  1.00 21.72           C  
ATOM    736  N   THR A  92      36.299  24.577  -7.838  1.00 10.02           N  
ATOM    737  CA  THR A  92      37.569  24.228  -7.210  1.00  9.76           C  
ATOM    738  C   THR A  92      38.684  24.758  -8.099  1.00  9.60           C  
ATOM    739  O   THR A  92      38.851  24.289  -9.226  1.00 10.26           O  
ATOM    740  CB  THR A  92      37.701  22.705  -7.046  1.00  9.66           C  
ATOM    741  OG1 THR A  92      36.540  22.216  -6.361  1.00  9.89           O  
ATOM    742  CG2 THR A  92      38.963  22.334  -6.267  1.00 11.07           C  
ATOM    743  N   ALA A  93      39.446  25.728  -7.602  1.00  9.63           N  
ATOM    744  CA  ALA A  93      40.526  26.299  -8.421  1.00  9.96           C  
ATOM    745  C   ALA A  93      41.763  25.403  -8.433  1.00 10.45           C  
ATOM    746  O   ALA A  93      42.399  25.265  -9.474  1.00 10.29           O  
ATOM    747  CB  ALA A  93      40.885  27.693  -7.953  1.00  9.91           C  
ATOM    748  N   GLY A  94      42.092  24.814  -7.285  1.00 10.29           N  
ATOM    749  CA  GLY A  94      43.243  23.920  -7.151  1.00 10.83           C  
ATOM    750  C   GLY A  94      44.511  24.497  -7.761  1.00 10.42           C  
ATOM    751  O   GLY A  94      44.883  25.636  -7.485  1.00 11.07           O  
ATOM    752  N   ARG A  95      45.175  23.691  -8.585  1.00 11.71           N  
ATOM    753  CA  ARG A  95      46.442  24.123  -9.193  1.00 12.85           C  
ATOM    754  C   ARG A  95      46.324  25.427  -9.997  1.00 12.58           C  
ATOM    755  O   ARG A  95      47.311  26.150 -10.155  1.00 13.29           O  
ATOM    756  CB  ARG A  95      47.049  23.010 -10.050  1.00 13.48           C  
ATOM    757  CG  ARG A  95      46.228  22.604 -11.254  1.00 15.46           C  
ATOM    758  CD  ARG A  95      46.874  21.420 -11.985  1.00 15.86           C  
ATOM    759  NE  ARG A  95      46.904  20.222 -11.150  1.00 21.49           N  
ATOM    760  CZ  ARG A  95      47.066  18.990 -11.616  0.40 21.52           C  
ATOM    761  NH1 ARG A  95      47.433  18.964 -12.860  0.00 22.38           N  
ATOM    762  NH2 ARG A  95      47.066  17.965 -10.777  1.00 25.39           N  
ATOM    763  N   GLY A  96      45.125  25.721 -10.490  1.00 12.29           N  
ATOM    764  CA  GLY A  96      44.874  27.012 -11.103  1.00 12.34           C  
ATOM    765  C   GLY A  96      43.815  26.992 -12.177  1.00 12.33           C  
ATOM    766  O   GLY A  96      43.706  26.032 -12.945  1.00 12.41           O  
ATOM    767  N   VAL A  97      43.026  28.068 -12.220  1.00 12.05           N  
ATOM    768  CA  VAL A  97      41.996  28.236 -13.237  1.00 12.32           C  
ATOM    769  C   VAL A  97      41.743  29.730 -13.377  1.00 11.45           C  
ATOM    770  O   VAL A  97      42.024  30.488 -12.444  1.00 12.29           O  
ATOM    771  CB  VAL A  97      40.688  27.482 -12.820  1.00 12.78           C  
ATOM    772  CG1 VAL A  97      39.930  28.213 -11.694  1.00 13.26           C  
ATOM    773  CG2 VAL A  97      39.787  27.216 -14.007  1.00 14.01           C  
ATOM    774  N   VAL A  98      41.259  30.168 -14.542  1.00 11.37           N  
ATOM    775  CA  VAL A  98      40.710  31.524 -14.629  1.00 11.45           C  
ATOM    776  C   VAL A  98      39.203  31.446 -14.720  1.00 11.33           C  
ATOM    777  O   VAL A  98      38.648  30.454 -15.198  1.00 11.77           O  
ATOM    778  CB  VAL A  98      41.271  32.395 -15.805  1.00 12.08           C  
ATOM    779  CG1 VAL A  98      42.776  32.644 -15.636  1.00 12.78           C  
ATOM    780  CG2 VAL A  98      40.967  31.784 -17.152  1.00 12.65           C  
ATOM    781  N   HIS A  99      38.544  32.498 -14.254  1.00 10.79           N  
ATOM    782  CA  HIS A  99      37.094  32.554 -14.330  1.00 11.66           C  
ATOM    783  C   HIS A  99      36.597  33.974 -14.553  1.00 11.30           C  
ATOM    784  O   HIS A  99      37.333  34.945 -14.358  1.00 11.57           O  
ATOM    785  CB  HIS A  99      36.484  31.975 -13.043  1.00 11.71           C  
ATOM    786  CG  HIS A  99      36.393  32.960 -11.922  1.00 14.53           C  
ATOM    787  ND1 HIS A  99      35.190  33.378 -11.392  0.90 16.47           N  
ATOM    788  CD2 HIS A  99      37.356  33.628 -11.247  1.00 15.07           C  
ATOM    789  CE1 HIS A  99      35.418  34.250 -10.426  0.90 16.16           C  
ATOM    790  NE2 HIS A  99      36.725  34.422 -10.319  0.80 17.30           N  
ATOM    791  N   LYS A 100      35.331  34.088 -14.941  1.00 11.55           N  
ATOM    792  CA  LYS A 100      34.641  35.379 -14.978  1.00 12.57           C  
ATOM    793  C   LYS A 100      33.160  35.131 -14.753  1.00 12.53           C  
ATOM    794  O   LYS A 100      32.586  34.213 -15.339  1.00 12.86           O  
ATOM    795  CB  LYS A 100      34.843  36.084 -16.320  1.00 13.08           C  
ATOM    796  CG  LYS A 100      34.092  37.399 -16.442  1.00 14.43           C  
ATOM    797  CD  LYS A 100      34.457  38.128 -17.726  1.00 17.71           C  
ATOM    798  CE  LYS A 100      33.370  39.137 -18.079  1.00 19.38           C  
ATOM    799  NZ  LYS A 100      33.893  40.306 -18.837  1.00 22.26           N  
ATOM    800  N   GLU A 101      32.556  35.949 -13.896  1.00 12.54           N  
ATOM    801  CA  GLU A 101      31.118  35.891 -13.640  1.00 13.13           C  
ATOM    802  C   GLU A 101      30.526  37.157 -14.231  1.00 13.29           C  
ATOM    803  O   GLU A 101      30.919  38.261 -13.842  1.00 13.74           O  
ATOM    804  CB  GLU A 101      30.822  35.794 -12.132  1.00 13.78           C  
ATOM    805  CG  GLU A 101      31.682  34.761 -11.385  1.00 14.38           C  
ATOM    806  CD  GLU A 101      31.545  33.345 -11.930  1.00 15.27           C  
ATOM    807  OE1 GLU A 101      30.475  33.003 -12.467  1.00 16.77           O  
ATOM    808  OE2 GLU A 101      32.511  32.568 -11.790  1.00 18.13           O  
ATOM    809  N   ASP A 102      29.620  36.998 -15.193  1.00 13.40           N  
ATOM    810  CA  ASP A 102      29.094  38.141 -15.934  1.00 13.40           C  
ATOM    811  C   ASP A 102      27.569  38.036 -16.054  1.00 13.54           C  
ATOM    812  O   ASP A 102      27.063  37.028 -16.531  1.00 13.41           O  
ATOM    813  CB  ASP A 102      29.733  38.186 -17.328  1.00 14.08           C  
ATOM    814  CG  ASP A 102      29.783  39.595 -17.911  1.00 15.67           C  
ATOM    815  OD1 ASP A 102      29.703  40.576 -17.144  1.00 15.89           O  
ATOM    816  OD2 ASP A 102      29.933  39.721 -19.149  1.00 18.00           O  
ATOM    817  N   PRO A 103      26.826  39.063 -15.597  1.00 13.15           N  
ATOM    818  CA  PRO A 103      25.378  38.995 -15.818  1.00 13.83           C  
ATOM    819  C   PRO A 103      24.995  38.917 -17.293  1.00 14.61           C  
ATOM    820  O   PRO A 103      25.687  39.468 -18.161  1.00 14.88           O  
ATOM    821  CB  PRO A 103      24.865  40.304 -15.203  1.00 13.73           C  
ATOM    822  CG  PRO A 103      25.923  40.648 -14.173  1.00 13.33           C  
ATOM    823  CD  PRO A 103      27.205  40.273 -14.849  1.00 13.61           C  
ATOM    824  N   ALA A 104      23.881  38.243 -17.558  1.00 15.50           N  
ATOM    825  CA  ALA A 104      23.273  38.260 -18.890  1.00 16.38           C  
ATOM    826  C   ALA A 104      22.907  39.701 -19.268  1.00 16.91           C  
ATOM    827  O   ALA A 104      22.655  40.530 -18.394  1.00 16.92           O  
ATOM    828  CB  ALA A 104      22.035  37.381 -18.914  1.00 16.19           C  
ATOM    829  N   SER A 105      22.896  39.999 -20.570  1.00 18.10           N  
ATOM    830  CA  SER A 105      22.516  41.330 -21.055  1.00 18.85           C  
ATOM    831  C   SER A 105      21.195  41.787 -20.434  1.00 18.99           C  
ATOM    832  O   SER A 105      20.220  41.039 -20.416  1.00 19.92           O  
ATOM    833  CB  SER A 105      22.416  41.337 -22.583  1.00 19.40           C  
ATOM    834  OG  SER A 105      22.235  42.652 -23.080  1.00 21.96           O  
ATOM    835  N   GLY A 106      21.190  43.001 -19.887  1.00 19.03           N  
ATOM    836  CA  GLY A 106      20.000  43.568 -19.251  1.00 19.11           C  
ATOM    837  C   GLY A 106      19.668  43.046 -17.861  1.00 18.44           C  
ATOM    838  O   GLY A 106      18.702  43.497 -17.244  1.00 19.48           O  
ATOM    839  N   SER A 107      20.461  42.101 -17.355  1.00 17.69           N  
ATOM    840  CA  SER A 107      20.213  41.549 -16.025  1.00 16.66           C  
ATOM    841  C   SER A 107      21.151  42.142 -14.981  1.00 16.03           C  
ATOM    842  O   SER A 107      22.325  42.391 -15.258  1.00 16.17           O  
ATOM    843  CB  SER A 107      20.361  40.027 -16.055  1.00 16.68           C  
ATOM    844  OG  SER A 107      20.004  39.449 -14.808  1.00 16.63           O  
ATOM    845  N   THR A 108      20.612  42.387 -13.794  1.00 14.67           N  
ATOM    846  CA  THR A 108      21.421  42.739 -12.632  1.00 14.09           C  
ATOM    847  C   THR A 108      21.500  41.511 -11.732  1.00 13.61           C  
ATOM    848  O   THR A 108      20.474  40.967 -11.333  1.00 13.87           O  
ATOM    849  CB  THR A 108      20.807  43.906 -11.849  1.00 14.41           C  
ATOM    850  OG1 THR A 108      20.773  45.073 -12.683  1.00 16.38           O  
ATOM    851  CG2 THR A 108      21.630  44.220 -10.602  1.00 14.65           C  
ATOM    852  N   VAL A 109      22.717  41.063 -11.437  1.00 12.01           N  
ATOM    853  CA  VAL A 109      22.918  39.913 -10.557  1.00 11.23           C  
ATOM    854  C   VAL A 109      23.184  40.365  -9.135  1.00 11.16           C  
ATOM    855  O   VAL A 109      24.014  41.236  -8.904  1.00 11.25           O  
ATOM    856  CB  VAL A 109      24.065  39.008 -11.067  1.00 10.57           C  
ATOM    857  CG1 VAL A 109      24.447  37.932 -10.039  1.00 10.92           C  
ATOM    858  CG2 VAL A 109      23.656  38.334 -12.359  1.00 11.60           C  
ATOM    859  N   HIS A 110      22.452  39.778  -8.187  1.00 10.66           N  
ATOM    860  CA  HIS A 110      22.740  39.921  -6.769  1.00 10.36           C  
ATOM    861  C   HIS A 110      23.233  38.558  -6.308  1.00 10.08           C  
ATOM    862  O   HIS A 110      22.493  37.582  -6.415  1.00 10.28           O  
ATOM    863  CB  HIS A 110      21.449  40.320  -6.039  1.00 10.20           C  
ATOM    864  CG  HIS A 110      21.625  40.658  -4.592  1.00 11.36           C  
ATOM    865  ND1 HIS A 110      20.553  40.883  -3.757  1.00 12.95           N  
ATOM    866  CD2 HIS A 110      22.732  40.804  -3.827  1.00 11.56           C  
ATOM    867  CE1 HIS A 110      20.992  41.166  -2.542  1.00 13.53           C  
ATOM    868  NE2 HIS A 110      22.313  41.123  -2.557  1.00 12.64           N  
ATOM    869  N   SER A 111      24.478  38.490  -5.826  1.00 10.05           N  
ATOM    870  CA  SER A 111      25.088  37.199  -5.474  1.00  9.88           C  
ATOM    871  C   SER A 111      25.876  37.241  -4.175  1.00  9.95           C  
ATOM    872  O   SER A 111      26.232  38.310  -3.670  1.00  9.96           O  
ATOM    873  CB  SER A 111      26.008  36.715  -6.603  1.00 10.57           C  
ATOM    874  OG  SER A 111      27.062  37.633  -6.835  1.00 12.08           O  
ATOM    875  N   LEU A 112      26.127  36.052  -3.639  1.00  9.54           N  
ATOM    876  CA  LEU A 112      27.025  35.879  -2.498  1.00 10.10           C  
ATOM    877  C   LEU A 112      28.159  34.977  -2.937  1.00  9.71           C  
ATOM    878  O   LEU A 112      27.900  33.873  -3.414  1.00  9.85           O  
ATOM    879  CB  LEU A 112      26.289  35.245  -1.324  1.00 10.52           C  
ATOM    880  CG  LEU A 112      25.301  36.185  -0.645  1.00 11.19           C  
ATOM    881  CD1 LEU A 112      24.286  35.402   0.151  1.00 12.11           C  
ATOM    882  CD2 LEU A 112      26.053  37.187   0.247  1.00 13.14           C  
ATOM    883  N   GLN A 113      29.401  35.445  -2.792  1.00  9.77           N  
ATOM    884  CA  GLN A 113      30.584  34.714  -3.234  1.00 10.32           C  
ATOM    885  C   GLN A 113      31.445  34.321  -2.039  1.00  9.61           C  
ATOM    886  O   GLN A 113      32.028  35.187  -1.392  1.00  9.93           O  
ATOM    887  CB  GLN A 113      31.400  35.579  -4.198  1.00 11.11           C  
ATOM    888  CG  GLN A 113      32.622  34.897  -4.771  1.00 14.40           C  
ATOM    889  CD  GLN A 113      32.289  34.043  -5.972  1.00 17.79           C  
ATOM    890  OE1 GLN A 113      31.177  33.532  -6.101  1.00 20.52           O  
ATOM    891  NE2 GLN A 113      33.250  33.884  -6.863  1.00 20.56           N  
ATOM    892  N   LEU A 114      31.520  33.019  -1.774  1.00  9.09           N  
ATOM    893  CA  LEU A 114      32.282  32.468  -0.654  1.00  9.14           C  
ATOM    894  C   LEU A 114      33.601  31.890  -1.149  1.00  9.28           C  
ATOM    895  O   LEU A 114      33.639  31.266  -2.209  1.00  9.59           O  
ATOM    896  CB  LEU A 114      31.451  31.353  -0.010  1.00  9.30           C  
ATOM    897  CG  LEU A 114      32.062  30.589   1.151  1.00  8.95           C  
ATOM    898  CD1 LEU A 114      31.906  31.397   2.441  1.00 10.71           C  
ATOM    899  CD2 LEU A 114      31.401  29.219   1.286  1.00 10.11           C  
ATOM    900  N   TRP A 115      34.679  32.125  -0.403  1.00  9.12           N  
ATOM    901  CA  TRP A 115      35.942  31.426  -0.661  1.00  9.40           C  
ATOM    902  C   TRP A 115      36.188  30.418   0.425  1.00  9.21           C  
ATOM    903  O   TRP A 115      36.044  30.712   1.619  1.00  8.61           O  
ATOM    904  CB  TRP A 115      37.117  32.396  -0.676  1.00 10.64           C  
ATOM    905  CG  TRP A 115      37.190  33.308  -1.860  1.00 12.20           C  
ATOM    906  CD1 TRP A 115      36.222  33.527  -2.802  1.00 14.03           C  
ATOM    907  CD2 TRP A 115      38.290  34.156  -2.202  1.00 15.06           C  
ATOM    908  NE1 TRP A 115      36.665  34.451  -3.727  1.00 14.45           N  
ATOM    909  CE2 TRP A 115      37.930  34.853  -3.378  1.00 14.99           C  
ATOM    910  CE3 TRP A 115      39.555  34.381  -1.635  1.00 15.95           C  
ATOM    911  CZ2 TRP A 115      38.794  35.774  -3.999  1.00 14.95           C  
ATOM    912  CZ3 TRP A 115      40.411  35.304  -2.251  1.00 15.23           C  
ATOM    913  CH2 TRP A 115      40.021  35.981  -3.421  1.00 14.90           C  
ATOM    914  N   VAL A 116      36.570  29.218  -0.002  1.00  8.68           N  
ATOM    915  CA  VAL A 116      36.897  28.137   0.928  1.00  9.07           C  
ATOM    916  C   VAL A 116      38.362  27.784   0.730  1.00  9.35           C  
ATOM    917  O   VAL A 116      38.817  27.618  -0.403  1.00  9.22           O  
ATOM    918  CB  VAL A 116      36.039  26.892   0.662  1.00  8.65           C  
ATOM    919  CG1 VAL A 116      36.257  25.844   1.758  1.00  9.38           C  
ATOM    920  CG2 VAL A 116      34.556  27.239   0.556  1.00 10.14           C  
ATOM    921  N   ASN A 117      39.117  27.681   1.815  1.00  9.19           N  
ATOM    922  CA  ASN A 117      40.523  27.309   1.691  1.00  9.44           C  
ATOM    923  C   ASN A 117      40.660  25.845   1.300  1.00  9.76           C  
ATOM    924  O   ASN A 117      39.822  25.018   1.659  1.00 10.90           O  
ATOM    925  CB  ASN A 117      41.241  27.555   3.014  1.00  9.77           C  
ATOM    926  CG  ASN A 117      42.739  27.672   2.852  1.00 10.80           C  
ATOM    927  OD1 ASN A 117      43.250  27.823   1.742  1.00 10.91           O  
ATOM    928  ND2 ASN A 117      43.456  27.627   3.980  1.00 13.74           N  
ATOM    929  N   LEU A 118      41.712  25.538   0.545  1.00  9.62           N  
ATOM    930  CA  LEU A 118      42.123  24.152   0.330  1.00  9.90           C  
ATOM    931  C   LEU A 118      43.297  23.845   1.251  1.00  9.98           C  
ATOM    932  O   LEU A 118      44.229  24.656   1.357  1.00 10.54           O  
ATOM    933  CB  LEU A 118      42.538  23.900  -1.122  1.00  9.62           C  
ATOM    934  CG  LEU A 118      41.437  23.899  -2.199  1.00  9.80           C  
ATOM    935  CD1 LEU A 118      42.022  23.874  -3.597  1.00 12.00           C  
ATOM    936  CD2 LEU A 118      40.528  22.707  -2.021  1.00 12.07           C  
ATOM    937  N   PRO A 119      43.270  22.666   1.904  1.00 10.16           N  
ATOM    938  CA  PRO A 119      44.434  22.241   2.693  1.00 10.01           C  
ATOM    939  C   PRO A 119      45.628  22.021   1.769  1.00 10.24           C  
ATOM    940  O   PRO A 119      45.455  21.791   0.566  1.00  9.50           O  
ATOM    941  CB  PRO A 119      44.002  20.899   3.284  1.00 10.49           C  
ATOM    942  CG  PRO A 119      42.511  20.862   3.154  1.00 11.02           C  
ATOM    943  CD  PRO A 119      42.178  21.679   1.958  1.00 10.08           C  
ATOM    944  N   SER A 120      46.825  22.102   2.341  1.00 11.05           N  
ATOM    945  CA  SER A 120      48.058  21.923   1.573  1.00 11.51           C  
ATOM    946  C   SER A 120      48.005  20.670   0.693  1.00 10.81           C  
ATOM    947  O   SER A 120      48.442  20.700  -0.463  1.00 11.09           O  
ATOM    948  CB  SER A 120      49.250  21.847   2.530  1.00 12.52           C  
ATOM    949  OG  SER A 120      50.457  21.672   1.822  0.85 16.52           O  
ATOM    950  N   ALA A 121      47.462  19.580   1.241  1.00 10.94           N  
ATOM    951  CA  ALA A 121      47.376  18.320   0.494  1.00 10.34           C  
ATOM    952  C   ALA A 121      46.606  18.433  -0.819  1.00 10.79           C  
ATOM    953  O   ALA A 121      46.807  17.628  -1.724  1.00 10.93           O  
ATOM    954  CB  ALA A 121      46.776  17.216   1.341  1.00 10.51           C  
ATOM    955  N   TYR A 122      45.717  19.417  -0.925  1.00 10.54           N  
ATOM    956  CA  TYR A 122      44.828  19.512  -2.078  1.00 11.02           C  
ATOM    957  C   TYR A 122      44.994  20.801  -2.865  1.00 11.61           C  
ATOM    958  O   TYR A 122      44.250  21.037  -3.829  1.00 11.94           O  
ATOM    959  CB  TYR A 122      43.367  19.404  -1.634  1.00 10.74           C  
ATOM    960  CG  TYR A 122      43.015  18.123  -0.904  1.00 10.19           C  
ATOM    961  CD1 TYR A 122      42.555  17.004  -1.605  1.00 10.24           C  
ATOM    962  CD2 TYR A 122      43.111  18.031   0.486  1.00 10.22           C  
ATOM    963  CE1 TYR A 122      42.231  15.830  -0.939  1.00 10.67           C  
ATOM    964  CE2 TYR A 122      42.780  16.851   1.160  1.00  9.95           C  
ATOM    965  CZ  TYR A 122      42.336  15.759   0.434  1.00 10.51           C  
ATOM    966  OH  TYR A 122      42.001  14.596   1.096  1.00 11.73           O  
ATOM    967  N   LYS A 123      45.940  21.646  -2.463  1.00 12.16           N  
ATOM    968  CA  LYS A 123      46.103  22.943  -3.126  1.00 13.39           C  
ATOM    969  C   LYS A 123      46.395  22.803  -4.615  1.00 14.19           C  
ATOM    970  O   LYS A 123      46.058  23.686  -5.410  1.00 13.82           O  
ATOM    971  CB  LYS A 123      47.168  23.796  -2.431  1.00 14.16           C  
ATOM    972  CG  LYS A 123      46.618  24.518  -1.220  1.00 15.80           C  
ATOM    973  CD  LYS A 123      47.489  25.677  -0.809  1.00 18.97           C  
ATOM    974  CE  LYS A 123      47.023  26.256   0.516  1.00 19.70           C  
ATOM    975  NZ  LYS A 123      45.724  26.954   0.348  1.00 19.38           N  
HETATM  976  N   MSE A 124      46.994  21.675  -4.989  1.00 14.28           N  
HETATM  977  CA  MSE A 124      47.395  21.435  -6.378  1.00 16.24           C  
HETATM  978  C   MSE A 124      46.475  20.476  -7.112  1.00 15.04           C  
HETATM  979  O   MSE A 124      46.835  19.967  -8.178  1.00 14.69           O  
HETATM  980  CB  MSE A 124      48.841  20.931  -6.440  1.00 17.97           C  
HETATM  981  CG  MSE A 124      49.845  21.948  -5.928  1.00 25.39           C  
HETATM  982 SE   MSE A 124      50.121  23.423  -7.181  1.00 48.94          SE  
HETATM  983  CE  MSE A 124      51.262  22.513  -8.487  1.00 41.91           C  
ATOM    984  N   THR A 125      45.287  20.240  -6.558  1.00 14.50           N  
ATOM    985  CA  THR A 125      44.300  19.352  -7.170  1.00 14.48           C  
ATOM    986  C   THR A 125      43.838  19.922  -8.514  1.00 14.48           C  
ATOM    987  O   THR A 125      43.995  21.118  -8.782  1.00 14.00           O  
ATOM    988  CB  THR A 125      43.100  19.077  -6.202  1.00 14.99           C  
ATOM    989  OG1 THR A 125      42.332  17.955  -6.656  1.00 16.16           O  
ATOM    990  CG2 THR A 125      42.196  20.287  -6.084  1.00 14.08           C  
ATOM    991  N   GLU A 126      43.328  19.051  -9.382  1.00 14.93           N  
ATOM    992  CA  GLU A 126      42.815  19.493 -10.678  1.00 15.48           C  
ATOM    993  C   GLU A 126      41.641  20.443 -10.467  1.00 15.02           C  
ATOM    994  O   GLU A 126      40.831  20.216  -9.572  1.00 15.03           O  
ATOM    995  CB  GLU A 126      42.348  18.303 -11.518  1.00 16.29           C  
ATOM    996  CG  GLU A 126      43.461  17.388 -12.033  1.00 18.79           C  
ATOM    997  CD  GLU A 126      44.279  17.998 -13.156  0.90 20.82           C  
ATOM    998  OE1 GLU A 126      43.752  18.856 -13.902  1.00 24.18           O  
ATOM    999  OE2 GLU A 126      45.457  17.609 -13.304  0.20 20.82           O  
ATOM   1000  N   PRO A 127      41.555  21.512 -11.286  1.00 14.00           N  
ATOM   1001  CA  PRO A 127      40.351  22.348 -11.197  1.00 13.55           C  
ATOM   1002  C   PRO A 127      39.098  21.565 -11.578  1.00 12.99           C  
ATOM   1003  O   PRO A 127      39.156  20.636 -12.399  1.00 13.28           O  
ATOM   1004  CB  PRO A 127      40.607  23.487 -12.195  1.00 13.94           C  
ATOM   1005  CG  PRO A 127      41.749  23.037 -13.044  1.00 15.44           C  
ATOM   1006  CD  PRO A 127      42.517  22.000 -12.293  1.00 14.55           C  
ATOM   1007  N   ARG A 128      37.972  21.943 -10.979  1.00 12.48           N  
ATOM   1008  CA  ARG A 128      36.705  21.242 -11.182  1.00 13.24           C  
ATOM   1009  C   ARG A 128      35.586  22.257 -10.994  1.00 12.44           C  
ATOM   1010  O   ARG A 128      35.699  23.171 -10.172  1.00 12.79           O  
ATOM   1011  CB  ARG A 128      36.603  20.073 -10.184  1.00 13.80           C  
ATOM   1012  CG  ARG A 128      35.243  19.420  -9.965  1.00 16.28           C  
ATOM   1013  CD  ARG A 128      35.381  18.264  -8.966  0.70 15.91           C  
ATOM   1014  NE  ARG A 128      35.609  18.644  -7.559  0.80 19.26           N  
ATOM   1015  CZ  ARG A 128      35.999  17.776  -6.620  1.00 19.64           C  
ATOM   1016  NH1 ARG A 128      36.226  16.514  -6.955  1.00 20.73           N  
ATOM   1017  NH2 ARG A 128      36.180  18.151  -5.361  1.00 19.56           N  
ATOM   1018  N   TYR A 129      34.514  22.088 -11.754  1.00 10.81           N  
ATOM   1019  CA  TYR A 129      33.353  22.958 -11.681  1.00 10.12           C  
ATOM   1020  C   TYR A 129      32.109  22.111 -11.477  1.00 10.04           C  
ATOM   1021  O   TYR A 129      31.917  21.094 -12.146  1.00 10.86           O  
ATOM   1022  CB  TYR A 129      33.227  23.784 -12.969  1.00 10.24           C  
ATOM   1023  CG  TYR A 129      32.004  24.673 -12.985  1.00 10.83           C  
ATOM   1024  CD1 TYR A 129      31.973  25.862 -12.250  1.00 10.99           C  
ATOM   1025  CD2 TYR A 129      30.877  24.324 -13.727  1.00 10.90           C  
ATOM   1026  CE1 TYR A 129      30.858  26.669 -12.255  1.00 10.43           C  
ATOM   1027  CE2 TYR A 129      29.735  25.130 -13.736  1.00  9.59           C  
ATOM   1028  CZ  TYR A 129      29.742  26.304 -13.002  1.00  8.89           C  
ATOM   1029  OH  TYR A 129      28.634  27.120 -13.013  1.00  9.98           O  
ATOM   1030  N   GLN A 130      31.285  22.527 -10.522  1.00  9.20           N  
ATOM   1031  CA  GLN A 130      29.987  21.900 -10.278  1.00  9.12           C  
ATOM   1032  C   GLN A 130      28.890  22.947 -10.357  1.00 10.03           C  
ATOM   1033  O   GLN A 130      28.933  23.957  -9.652  1.00 10.14           O  
ATOM   1034  CB  GLN A 130      29.955  21.232  -8.907  1.00  9.77           C  
ATOM   1035  CG  GLN A 130      31.072  20.266  -8.653  1.00  8.60           C  
ATOM   1036  CD  GLN A 130      31.019  19.718  -7.255  1.00  9.03           C  
ATOM   1037  OE1 GLN A 130      30.147  18.899  -6.931  1.00  9.91           O  
ATOM   1038  NE2 GLN A 130      31.944  20.157  -6.408  1.00  8.50           N  
ATOM   1039  N   ASN A 131      27.925  22.704 -11.233  1.00 10.65           N  
ATOM   1040  CA  ASN A 131      26.743  23.553 -11.349  1.00 11.07           C  
ATOM   1041  C   ASN A 131      25.619  22.926 -10.524  1.00 11.40           C  
ATOM   1042  O   ASN A 131      25.176  21.806 -10.799  1.00 11.81           O  
ATOM   1043  CB  ASN A 131      26.351  23.694 -12.825  1.00 12.37           C  
ATOM   1044  CG  ASN A 131      25.325  24.774 -13.057  1.00 14.05           C  
ATOM   1045  OD1 ASN A 131      24.134  24.552 -12.877  1.00 17.96           O  
ATOM   1046  ND2 ASN A 131      25.784  25.957 -13.458  1.00 15.95           N  
ATOM   1047  N   LEU A 132      25.170  23.645  -9.501  1.00 11.61           N  
ATOM   1048  CA  LEU A 132      24.242  23.097  -8.517  1.00 12.14           C  
ATOM   1049  C   LEU A 132      22.891  23.789  -8.605  1.00 11.94           C  
ATOM   1050  O   LEU A 132      22.630  24.756  -7.905  1.00 11.57           O  
ATOM   1051  CB  LEU A 132      24.829  23.222  -7.101  1.00 11.95           C  
ATOM   1052  CG  LEU A 132      26.222  22.624  -6.897  1.00 12.60           C  
ATOM   1053  CD1 LEU A 132      26.753  22.942  -5.499  1.00 13.74           C  
ATOM   1054  CD2 LEU A 132      26.240  21.115  -7.175  1.00 12.73           C  
ATOM   1055  N   ARG A 133      22.041  23.296  -9.491  1.00 12.85           N  
ATOM   1056  CA  ARG A 133      20.725  23.878  -9.667  1.00 13.35           C  
ATOM   1057  C   ARG A 133      19.872  23.611  -8.441  1.00 13.30           C  
ATOM   1058  O   ARG A 133      19.833  22.499  -7.916  1.00 13.58           O  
ATOM   1059  CB  ARG A 133      20.049  23.307 -10.912  1.00 13.66           C  
ATOM   1060  CG  ARG A 133      20.814  23.569 -12.181  1.00 16.25           C  
ATOM   1061  CD  ARG A 133      20.858  25.045 -12.526  1.00 20.85           C  
ATOM   1062  NE  ARG A 133      21.434  25.239 -13.853  1.00 23.28           N  
ATOM   1063  CZ  ARG A 133      21.368  26.361 -14.556  1.00 23.90           C  
ATOM   1064  NH1 ARG A 133      20.762  27.435 -14.067  1.00 25.16           N  
ATOM   1065  NH2 ARG A 133      21.927  26.407 -15.760  1.00 25.17           N  
ATOM   1066  N   SER A 134      19.184  24.648  -7.984  1.00 13.39           N  
ATOM   1067  CA  SER A 134      18.328  24.547  -6.812  1.00 13.58           C  
ATOM   1068  C   SER A 134      17.408  23.325  -6.909  1.00 13.33           C  
ATOM   1069  O   SER A 134      17.297  22.543  -5.964  1.00 13.37           O  
ATOM   1070  CB  SER A 134      17.507  25.829  -6.679  1.00 13.95           C  
ATOM   1071  OG  SER A 134      16.617  25.759  -5.580  1.00 15.28           O  
ATOM   1072  N   LYS A 135      16.788  23.152  -8.072  1.00 14.21           N  
ATOM   1073  CA  LYS A 135      15.805  22.090  -8.273  1.00 14.97           C  
ATOM   1074  C   LYS A 135      16.389  20.677  -8.146  1.00 14.74           C  
ATOM   1075  O   LYS A 135      15.652  19.721  -7.900  1.00 16.07           O  
ATOM   1076  CB  LYS A 135      15.111  22.258  -9.632  1.00 15.27           C  
ATOM   1077  CG  LYS A 135      16.041  22.031 -10.821  1.00 16.68           C  
ATOM   1078  CD  LYS A 135      15.241  21.883 -12.170  0.00 29.31           C  
ATOM   1079  CE  LYS A 135      13.927  20.961 -12.253  0.00 40.03           C  
ATOM   1080  NZ  LYS A 135      13.450  21.035 -14.363  0.30 11.70           N  
ATOM   1081  N   ASP A 136      17.706  20.553  -8.300  1.00 14.55           N  
ATOM   1082  CA  ASP A 136      18.369  19.248  -8.265  1.00 14.28           C  
ATOM   1083  C   ASP A 136      18.871  18.858  -6.877  1.00 13.70           C  
ATOM   1084  O   ASP A 136      19.343  17.739  -6.687  1.00 14.58           O  
ATOM   1085  CB  ASP A 136      19.539  19.185  -9.264  1.00 14.51           C  
ATOM   1086  CG  ASP A 136      19.086  19.261 -10.720  1.00 15.44           C  
ATOM   1087  OD1 ASP A 136      17.968  18.786 -11.032  1.00 19.16           O  
ATOM   1088  OD2 ASP A 136      19.852  19.788 -11.555  1.00 17.64           O  
HETATM 1089  N   MSE A 137      18.787  19.783  -5.917  1.00 12.89           N  
HETATM 1090  CA  MSE A 137      19.289  19.526  -4.579  1.00 12.48           C  
HETATM 1091  C   MSE A 137      18.266  18.809  -3.718  1.00 11.65           C  
HETATM 1092  O   MSE A 137      17.059  19.045  -3.859  1.00 12.35           O  
HETATM 1093  CB  MSE A 137      19.698  20.832  -3.889  1.00 12.21           C  
HETATM 1094  CG  MSE A 137      20.842  21.580  -4.553  1.00 13.85           C  
HETATM 1095 SE   MSE A 137      22.490  20.542  -4.771  0.75 13.36          SE  
HETATM 1096  CE  MSE A 137      22.355  20.217  -6.693  1.00 14.95           C  
ATOM   1097  N   PRO A 138      18.740  17.939  -2.805  1.00 11.15           N  
ATOM   1098  CA  PRO A 138      17.773  17.304  -1.911  1.00 11.04           C  
ATOM   1099  C   PRO A 138      17.257  18.304  -0.876  1.00 11.75           C  
ATOM   1100  O   PRO A 138      17.889  19.329  -0.637  1.00 11.36           O  
ATOM   1101  CB  PRO A 138      18.570  16.167  -1.273  1.00 10.94           C  
ATOM   1102  CG  PRO A 138      20.005  16.648  -1.289  1.00  9.97           C  
ATOM   1103  CD  PRO A 138      20.129  17.508  -2.529  1.00 10.52           C  
ATOM   1104  N   VAL A 139      16.093  18.021  -0.308  1.00 12.76           N  
ATOM   1105  CA  VAL A 139      15.437  18.955   0.584  1.00 14.37           C  
ATOM   1106  C   VAL A 139      14.855  18.212   1.770  1.00 14.35           C  
ATOM   1107  O   VAL A 139      14.234  17.154   1.598  1.00 14.88           O  
ATOM   1108  CB  VAL A 139      14.324  19.732  -0.165  1.00 14.80           C  
ATOM   1109  CG1 VAL A 139      13.306  18.781  -0.787  1.00 17.58           C  
ATOM   1110  CG2 VAL A 139      13.643  20.744   0.740  1.00 16.36           C  
ATOM   1111  N   ARG A 140      15.095  18.743   2.966  1.00 14.52           N  
ATOM   1112  CA  ARG A 140      14.327  18.391   4.151  1.00 15.06           C  
ATOM   1113  C   ARG A 140      13.034  19.174   4.118  1.00 15.79           C  
ATOM   1114  O   ARG A 140      13.046  20.395   4.226  1.00 14.95           O  
ATOM   1115  CB  ARG A 140      15.057  18.809   5.428  1.00 15.86           C  
ATOM   1116  CG  ARG A 140      15.989  17.814   6.016  1.00 16.67           C  
ATOM   1117  CD  ARG A 140      16.726  18.454   7.203  1.00 16.74           C  
ATOM   1118  NE  ARG A 140      15.894  18.654   8.388  1.00 16.80           N  
ATOM   1119  CZ  ARG A 140      16.218  19.452   9.402  1.00 16.14           C  
ATOM   1120  NH1 ARG A 140      17.357  20.131   9.374  1.00 13.60           N  
ATOM   1121  NH2 ARG A 140      15.406  19.592  10.445  1.00 16.84           N  
ATOM   1122  N   LYS A 141      11.913  18.479   3.981  1.00 16.35           N  
ATOM   1123  CA  LYS A 141      10.615  19.122   4.010  1.00 17.87           C  
ATOM   1124  C   LYS A 141      10.013  18.929   5.389  1.00 18.42           C  
ATOM   1125  O   LYS A 141       9.843  17.789   5.864  1.00 19.74           O  
ATOM   1126  CB  LYS A 141       9.698  18.536   2.930  1.00 17.60           C  
ATOM   1127  CG  LYS A 141      10.275  18.608   1.509  1.00 18.82           C  
ATOM   1128  CD  LYS A 141       9.344  18.000   0.453  1.00 18.50           C  
ATOM   1129  CE  LYS A 141       8.421  19.045  -0.153  0.10 18.54           C  
ATOM   1130  NZ  LYS A 141       7.462  18.007  -0.696  0.00 39.72           N  
ATOM   1131  N   GLU A 142       9.717  20.041   6.048  1.00 18.14           N  
ATOM   1132  CA  GLU A 142       9.057  20.002   7.346  1.00 18.54           C  
ATOM   1133  C   GLU A 142       7.806  20.870   7.287  1.00 18.03           C  
ATOM   1134  O   GLU A 142       7.615  21.637   6.337  1.00 18.51           O  
ATOM   1135  CB  GLU A 142      10.008  20.460   8.457  1.00 18.42           C  
ATOM   1136  CG  GLU A 142      11.325  19.674   8.491  1.00 20.07           C  
ATOM   1137  CD  GLU A 142      12.099  19.852   9.772  1.00 22.14           C  
ATOM   1138  OE1 GLU A 142      12.021  20.941  10.376  0.80 21.89           O  
ATOM   1139  OE2 GLU A 142      12.793  18.894  10.178  1.00 23.74           O  
ATOM   1140  N   GLU A 143       6.926  20.709   8.273  1.00 18.30           N  
ATOM   1141  CA  GLU A 143       5.774  21.582   8.402  1.00 18.98           C  
ATOM   1142  C   GLU A 143       6.296  22.993   8.618  1.00 17.89           C  
ATOM   1143  O   GLU A 143       6.976  23.255   9.607  1.00 19.45           O  
ATOM   1144  CB  GLU A 143       4.902  21.141   9.582  1.00 18.85           C  
ATOM   1145  CG  GLU A 143       3.774  22.112   9.983  1.00 21.13           C  
ATOM   1146  CD  GLU A 143       3.055  21.684  11.257  0.20 19.95           C  
ATOM   1147  OE1 GLU A 143       3.631  21.824  12.363  1.00 22.25           O  
ATOM   1148  OE2 GLU A 143       1.816  21.082  11.167  0.00 38.54           O  
ATOM   1149  N   GLY A 144       6.000  23.872   7.669  1.00 17.20           N  
ATOM   1150  CA  GLY A 144       6.364  25.277   7.766  1.00 15.78           C  
ATOM   1151  C   GLY A 144       7.808  25.596   7.410  1.00 14.53           C  
ATOM   1152  O   GLY A 144       8.260  26.720   7.622  1.00 14.14           O  
ATOM   1153  N   ALA A 145       8.554  24.619   6.898  1.00 14.24           N  
ATOM   1154  CA  ALA A 145       9.938  24.911   6.496  1.00 13.71           C  
ATOM   1155  C   ALA A 145      10.491  23.972   5.440  1.00 13.35           C  
ATOM   1156  O   ALA A 145      10.144  22.791   5.385  1.00 14.27           O  
ATOM   1157  CB  ALA A 145      10.868  24.917   7.712  1.00 13.96           C  
ATOM   1158  N   THR A 146      11.386  24.505   4.622  1.00 12.60           N  
ATOM   1159  CA  THR A 146      12.178  23.672   3.731  1.00 12.40           C  
ATOM   1160  C   THR A 146      13.635  23.996   3.973  1.00 11.82           C  
ATOM   1161  O   THR A 146      14.002  25.155   4.180  1.00 11.47           O  
ATOM   1162  CB  THR A 146      11.842  23.860   2.250  1.00 13.10           C  
ATOM   1163  OG1 THR A 146      11.946  25.234   1.899  1.00 15.20           O  
ATOM   1164  CG2 THR A 146      10.433  23.385   1.937  1.00 14.93           C  
ATOM   1165  N   ILE A 147      14.447  22.950   4.013  1.00 11.42           N  
ATOM   1166  CA  ILE A 147      15.888  23.088   4.165  1.00 10.90           C  
ATOM   1167  C   ILE A 147      16.502  22.402   2.954  1.00 10.56           C  
ATOM   1168  O   ILE A 147      16.464  21.170   2.847  1.00 11.21           O  
ATOM   1169  CB  ILE A 147      16.402  22.454   5.476  1.00 10.85           C  
ATOM   1170  CG1 ILE A 147      15.687  23.078   6.685  1.00 11.45           C  
ATOM   1171  CG2 ILE A 147      17.920  22.624   5.590  1.00 10.74           C  
ATOM   1172  CD1 ILE A 147      14.516  22.242   7.180  1.00 14.26           C  
ATOM   1173  N   ARG A 148      17.034  23.208   2.035  1.00 10.09           N  
ATOM   1174  CA  ARG A 148      17.614  22.719   0.786  1.00  9.71           C  
ATOM   1175  C   ARG A 148      19.110  22.577   0.992  1.00  9.70           C  
ATOM   1176  O   ARG A 148      19.775  23.501   1.436  1.00 10.05           O  
ATOM   1177  CB  ARG A 148      17.319  23.701  -0.346  1.00  9.91           C  
ATOM   1178  CG  ARG A 148      17.730  23.222  -1.717  1.00 11.21           C  
ATOM   1179  CD  ARG A 148      17.205  24.170  -2.776  1.00 12.83           C  
ATOM   1180  NE  ARG A 148      15.746  24.096  -2.899  1.00 14.35           N  
ATOM   1181  CZ  ARG A 148      14.872  24.995  -2.436  0.90 19.03           C  
ATOM   1182  NH1 ARG A 148      15.250  26.102  -1.770  1.00 20.93           N  
ATOM   1183  NH2 ARG A 148      13.581  24.764  -2.637  1.00 22.63           N  
ATOM   1184  N   VAL A 149      19.633  21.396   0.694  1.00  8.79           N  
ATOM   1185  CA  VAL A 149      21.018  21.085   1.003  1.00  8.49           C  
ATOM   1186  C   VAL A 149      21.864  21.223  -0.263  1.00  8.28           C  
ATOM   1187  O   VAL A 149      21.739  20.426  -1.188  1.00  8.58           O  
ATOM   1188  CB  VAL A 149      21.171  19.666   1.607  1.00  8.36           C  
ATOM   1189  CG1 VAL A 149      22.597  19.447   2.100  1.00  9.65           C  
ATOM   1190  CG2 VAL A 149      20.166  19.460   2.744  1.00  9.31           C  
ATOM   1191  N   PHE A 150      22.740  22.227  -0.287  1.00  7.36           N  
ATOM   1192  CA  PHE A 150      23.648  22.448  -1.413  1.00  7.88           C  
ATOM   1193  C   PHE A 150      24.977  21.735  -1.248  1.00  7.81           C  
ATOM   1194  O   PHE A 150      25.643  21.418  -2.235  1.00  8.60           O  
ATOM   1195  CB  PHE A 150      23.874  23.941  -1.645  1.00  7.90           C  
ATOM   1196  CG  PHE A 150      22.723  24.611  -2.332  1.00  7.56           C  
ATOM   1197  CD1 PHE A 150      22.614  24.550  -3.711  1.00  8.55           C  
ATOM   1198  CD2 PHE A 150      21.738  25.281  -1.603  1.00  8.49           C  
ATOM   1199  CE1 PHE A 150      21.562  25.159  -4.374  1.00  8.81           C  
ATOM   1200  CE2 PHE A 150      20.665  25.901  -2.266  1.00  7.36           C  
ATOM   1201  CZ  PHE A 150      20.578  25.827  -3.649  1.00  7.73           C  
ATOM   1202  N   SER A 151      25.353  21.485   0.002  1.00  7.48           N  
ATOM   1203  CA  SER A 151      26.577  20.746   0.316  1.00  7.25           C  
ATOM   1204  C   SER A 151      26.466  20.177   1.710  1.00  7.26           C  
ATOM   1205  O   SER A 151      25.824  20.770   2.582  1.00  7.30           O  
ATOM   1206  CB  SER A 151      27.798  21.663   0.222  1.00  7.64           C  
ATOM   1207  OG  SER A 151      29.002  20.913   0.333  1.00  8.13           O  
ATOM   1208  N   GLY A 152      27.086  19.017   1.931  1.00  7.58           N  
ATOM   1209  CA  GLY A 152      27.071  18.407   3.252  1.00  8.35           C  
ATOM   1210  C   GLY A 152      25.713  17.833   3.566  1.00  8.72           C  
ATOM   1211  O   GLY A 152      25.062  17.245   2.698  1.00  8.89           O  
ATOM   1212  N   SER A 153      25.288  17.981   4.816  1.00  9.62           N  
ATOM   1213  CA  SER A 153      24.055  17.315   5.225  1.00 10.76           C  
ATOM   1214  C   SER A 153      23.245  18.081   6.242  1.00 10.51           C  
ATOM   1215  O   SER A 153      23.758  18.950   6.948  1.00 10.59           O  
ATOM   1216  CB  SER A 153      24.370  15.942   5.805  1.00 11.64           C  
ATOM   1217  OG  SER A 153      25.093  16.096   7.007  1.00 12.62           O  
ATOM   1218  N   SER A 154      21.970  17.730   6.306  1.00 10.51           N  
ATOM   1219  CA  SER A 154      21.077  18.303   7.291  1.00 10.67           C  
ATOM   1220  C   SER A 154      20.179  17.170   7.761  1.00 10.99           C  
ATOM   1221  O   SER A 154      19.383  16.648   6.984  1.00 10.78           O  
ATOM   1222  CB  SER A 154      20.275  19.436   6.662  1.00 10.79           C  
ATOM   1223  OG  SER A 154      19.549  20.178   7.636  1.00 10.87           O  
ATOM   1224  N   LYS A 155      20.333  16.806   9.032  1.00 11.51           N  
ATOM   1225  CA  LYS A 155      19.641  15.649   9.639  1.00 12.25           C  
ATOM   1226  C   LYS A 155      19.698  14.424   8.712  1.00 11.69           C  
ATOM   1227  O   LYS A 155      18.697  13.734   8.487  1.00 11.87           O  
ATOM   1228  CB  LYS A 155      18.198  15.996  10.028  1.00 12.62           C  
ATOM   1229  CG  LYS A 155      18.065  17.120  11.045  1.00 15.72           C  
ATOM   1230  CD  LYS A 155      18.308  16.627  12.439  1.00 18.95           C  
ATOM   1231  CE  LYS A 155      18.074  17.722  13.467  1.00 20.95           C  
ATOM   1232  NZ  LYS A 155      18.041  17.109  14.815  1.00 23.25           N  
ATOM   1233  N   GLY A 156      20.884  14.167   8.168  1.00 11.35           N  
ATOM   1234  CA  GLY A 156      21.117  12.970   7.358  1.00 12.02           C  
ATOM   1235  C   GLY A 156      20.763  13.119   5.887  1.00 12.05           C  
ATOM   1236  O   GLY A 156      21.077  12.231   5.094  1.00 13.54           O  
ATOM   1237  N   VAL A 157      20.101  14.213   5.513  1.00 11.37           N  
ATOM   1238  CA  VAL A 157      19.842  14.511   4.088  1.00 11.37           C  
ATOM   1239  C   VAL A 157      21.122  15.095   3.494  1.00 11.43           C  
ATOM   1240  O   VAL A 157      21.591  16.157   3.926  1.00 12.44           O  
ATOM   1241  CB  VAL A 157      18.634  15.459   3.887  1.00 11.32           C  
ATOM   1242  CG1 VAL A 157      18.412  15.802   2.405  1.00 12.19           C  
ATOM   1243  CG2 VAL A 157      17.360  14.814   4.455  1.00 11.64           C  
ATOM   1244  N   LYS A 158      21.680  14.390   2.510  1.00 11.13           N  
ATOM   1245  CA  LYS A 158      23.044  14.648   2.032  1.00 11.48           C  
ATOM   1246  C   LYS A 158      23.047  15.092   0.582  1.00 10.86           C  
ATOM   1247  O   LYS A 158      22.476  14.422  -0.273  1.00 11.50           O  
ATOM   1248  CB  LYS A 158      23.883  13.375   2.180  1.00 11.95           C  
ATOM   1249  CG  LYS A 158      25.267  13.441   1.567  1.00 13.85           C  
ATOM   1250  CD  LYS A 158      26.069  12.199   1.906  0.80 15.38           C  
ATOM   1251  CE  LYS A 158      27.485  12.418   1.268  0.00 34.78           C  
ATOM   1252  NZ  LYS A 158      28.365  11.172   1.694  0.00 38.50           N  
ATOM   1253  N   ALA A 159      23.688  16.220   0.292  1.00 10.43           N  
ATOM   1254  CA  ALA A 159      23.845  16.652  -1.096  1.00 10.64           C  
ATOM   1255  C   ALA A 159      24.950  15.809  -1.744  1.00 10.68           C  
ATOM   1256  O   ALA A 159      25.894  15.404  -1.079  1.00 10.83           O  
ATOM   1257  CB  ALA A 159      24.215  18.120  -1.171  1.00 10.67           C  
ATOM   1258  N   PRO A 160      24.832  15.539  -3.053  1.00 11.84           N  
ATOM   1259  CA  PRO A 160      25.895  14.768  -3.697  1.00 11.86           C  
ATOM   1260  C   PRO A 160      27.119  15.608  -4.075  1.00 11.37           C  
ATOM   1261  O   PRO A 160      28.113  15.073  -4.567  1.00 11.60           O  
ATOM   1262  CB  PRO A 160      25.204  14.235  -4.954  1.00 12.68           C  
ATOM   1263  CG  PRO A 160      24.259  15.258  -5.301  1.00 12.04           C  
ATOM   1264  CD  PRO A 160      23.749  15.865  -3.994  1.00 12.62           C  
ATOM   1265  N   THR A 161      27.037  16.910  -3.823  1.00 10.53           N  
ATOM   1266  CA  THR A 161      28.107  17.844  -4.119  1.00  9.93           C  
ATOM   1267  C   THR A 161      29.450  17.318  -3.632  1.00 10.18           C  
ATOM   1268  O   THR A 161      29.580  16.881  -2.496  1.00 10.45           O  
ATOM   1269  CB  THR A 161      27.789  19.170  -3.426  1.00  9.45           C  
ATOM   1270  OG1 THR A 161      26.483  19.587  -3.827  1.00  9.33           O  
ATOM   1271  CG2 THR A 161      28.817  20.257  -3.781  1.00  9.52           C  
ATOM   1272  N   LYS A 162      30.442  17.335  -4.517  1.00  9.79           N  
ATOM   1273  CA  LYS A 162      31.786  16.884  -4.159  1.00 10.41           C  
ATOM   1274  C   LYS A 162      32.483  17.938  -3.303  1.00  9.83           C  
ATOM   1275  O   LYS A 162      32.446  19.142  -3.610  1.00  8.92           O  
ATOM   1276  CB  LYS A 162      32.608  16.591  -5.411  1.00 10.90           C  
ATOM   1277  CG  LYS A 162      31.982  15.565  -6.350  1.00 13.93           C  
ATOM   1278  CD  LYS A 162      32.764  15.492  -7.650  0.30 16.71           C  
ATOM   1279  CE  LYS A 162      32.346  14.300  -8.489  0.60 19.19           C  
ATOM   1280  NZ  LYS A 162      33.194  14.206  -9.706  0.60 22.33           N  
ATOM   1281  N   ASN A 163      33.078  17.487  -2.206  1.00  9.90           N  
ATOM   1282  CA  ASN A 163      33.794  18.364  -1.296  1.00 10.46           C  
ATOM   1283  C   ASN A 163      35.231  17.878  -1.155  1.00 11.17           C  
ATOM   1284  O   ASN A 163      35.500  16.672  -1.205  1.00 11.69           O  
ATOM   1285  CB  ASN A 163      33.170  18.357   0.110  1.00 10.21           C  
ATOM   1286  CG  ASN A 163      31.917  19.255   0.261  1.00 10.23           C  
ATOM   1287  OD1 ASN A 163      31.344  19.304   1.349  1.00 10.61           O  
ATOM   1288  ND2 ASN A 163      31.505  19.950  -0.791  1.00  9.29           N  
ATOM   1289  N   ILE A 164      36.128  18.834  -0.944  1.00 11.38           N  
ATOM   1290  CA  ILE A 164      37.454  18.545  -0.429  1.00 11.79           C  
ATOM   1291  C   ILE A 164      37.392  18.818   1.083  1.00 11.34           C  
ATOM   1292  O   ILE A 164      37.338  17.877   1.875  1.00 13.32           O  
ATOM   1293  CB  ILE A 164      38.529  19.345  -1.202  1.00 12.24           C  
ATOM   1294  CG1 ILE A 164      38.627  18.797  -2.638  1.00 14.24           C  
ATOM   1295  CG2 ILE A 164      39.879  19.244  -0.519  1.00 12.37           C  
ATOM   1296  CD1 ILE A 164      39.312  19.695  -3.615  1.00 16.37           C  
ATOM   1297  N   VAL A 165      37.366  20.087   1.492  1.00 11.19           N  
ATOM   1298  CA  VAL A 165      37.027  20.406   2.872  1.00 10.99           C  
ATOM   1299  C   VAL A 165      35.531  20.131   3.031  1.00 10.27           C  
ATOM   1300  O   VAL A 165      34.723  20.670   2.269  1.00  9.79           O  
ATOM   1301  CB  VAL A 165      37.316  21.897   3.219  1.00 11.13           C  
ATOM   1302  CG1 VAL A 165      36.653  22.298   4.540  1.00 12.21           C  
ATOM   1303  CG2 VAL A 165      38.809  22.155   3.293  1.00 13.20           C  
ATOM   1304  N   PRO A 166      35.146  19.293   4.015  1.00  9.38           N  
ATOM   1305  CA  PRO A 166      33.715  19.121   4.272  1.00  9.46           C  
ATOM   1306  C   PRO A 166      33.038  20.438   4.614  1.00  9.15           C  
ATOM   1307  O   PRO A 166      33.448  21.121   5.555  1.00  9.97           O  
ATOM   1308  CB  PRO A 166      33.677  18.167   5.481  1.00 10.10           C  
ATOM   1309  CG  PRO A 166      34.973  17.409   5.397  1.00 10.68           C  
ATOM   1310  CD  PRO A 166      35.962  18.452   4.915  1.00  9.38           C  
ATOM   1311  N   VAL A 167      32.024  20.788   3.831  1.00  8.29           N  
ATOM   1312  CA  VAL A 167      31.251  22.009   4.040  1.00  8.67           C  
ATOM   1313  C   VAL A 167      29.768  21.670   4.006  1.00  8.48           C  
ATOM   1314  O   VAL A 167      29.281  21.011   3.077  1.00  8.62           O  
ATOM   1315  CB  VAL A 167      31.562  23.080   2.960  1.00  8.62           C  
ATOM   1316  CG1 VAL A 167      30.638  24.309   3.079  1.00  9.89           C  
ATOM   1317  CG2 VAL A 167      33.017  23.515   3.044  1.00  9.39           C  
ATOM   1318  N   THR A 168      29.047  22.117   5.019  1.00  8.72           N  
ATOM   1319  CA  THR A 168      27.595  22.061   5.009  1.00  8.58           C  
ATOM   1320  C   THR A 168      27.061  23.425   4.609  1.00  8.37           C  
ATOM   1321  O   THR A 168      27.400  24.434   5.229  1.00  8.73           O  
ATOM   1322  CB  THR A 168      27.063  21.613   6.366  1.00  9.05           C  
ATOM   1323  OG1 THR A 168      27.327  20.208   6.512  1.00 10.03           O  
ATOM   1324  CG2 THR A 168      25.558  21.887   6.505  1.00 10.56           C  
HETATM 1325  N   MSE A 169      26.268  23.446   3.546  1.00  8.06           N  
HETATM 1326  CA  MSE A 169      25.661  24.669   3.048  1.00  7.79           C  
HETATM 1327  C   MSE A 169      24.202  24.376   2.789  1.00  8.06           C  
HETATM 1328  O   MSE A 169      23.872  23.507   1.979  1.00  7.83           O  
HETATM 1329  CB  MSE A 169      26.333  25.151   1.763  1.00  8.31           C  
HETATM 1330  CG  MSE A 169      25.692  26.416   1.205  1.00  8.78           C  
HETATM 1331 SE   MSE A 169      26.563  26.895  -0.470  0.70  9.04          SE  
HETATM 1332  CE  MSE A 169      25.500  28.467  -0.913  1.00 10.64           C  
ATOM   1333  N   VAL A 170      23.341  25.063   3.535  1.00  7.82           N  
ATOM   1334  CA  VAL A 170      21.916  24.839   3.433  1.00  8.62           C  
ATOM   1335  C   VAL A 170      21.157  26.143   3.290  1.00  8.72           C  
ATOM   1336  O   VAL A 170      21.546  27.173   3.853  1.00  8.70           O  
ATOM   1337  CB  VAL A 170      21.342  24.048   4.644  1.00  9.39           C  
ATOM   1338  CG1 VAL A 170      21.984  22.649   4.776  1.00  8.96           C  
ATOM   1339  CG2 VAL A 170      21.460  24.825   5.945  1.00  9.74           C  
ATOM   1340  N   GLU A 171      20.090  26.098   2.511  1.00  8.55           N  
ATOM   1341  CA  GLU A 171      19.174  27.219   2.401  1.00  8.96           C  
ATOM   1342  C   GLU A 171      17.888  26.897   3.154  1.00  9.24           C  
ATOM   1343  O   GLU A 171      17.243  25.882   2.879  1.00  9.74           O  
ATOM   1344  CB  GLU A 171      18.883  27.502   0.936  1.00  9.26           C  
ATOM   1345  CG  GLU A 171      17.945  28.679   0.708  1.00 10.83           C  
ATOM   1346  CD  GLU A 171      17.622  28.846  -0.745  1.00 13.63           C  
ATOM   1347  OE1 GLU A 171      17.597  27.817  -1.447  1.00 14.13           O  
ATOM   1348  OE2 GLU A 171      17.376  29.991  -1.170  1.00 15.69           O  
HETATM 1349  N   MSE A 172      17.524  27.762   4.095  1.00  9.59           N  
HETATM 1350  CA  MSE A 172      16.300  27.575   4.867  1.00 10.71           C  
HETATM 1351  C   MSE A 172      15.271  28.606   4.487  1.00 11.25           C  
HETATM 1352  O   MSE A 172      15.583  29.796   4.408  1.00 11.47           O  
HETATM 1353  CB  MSE A 172      16.568  27.697   6.359  1.00 10.59           C  
HETATM 1354  CG  MSE A 172      17.589  26.748   6.876  1.00 11.23           C  
HETATM 1355 SE   MSE A 172      17.568  26.860   8.798  0.50 12.21          SE  
HETATM 1356  CE  MSE A 172      19.229  26.153   9.062  1.00 12.84           C  
ATOM   1357  N   ILE A 173      14.055  28.134   4.241  1.00 10.86           N  
ATOM   1358  CA  ILE A 173      12.893  28.995   4.068  1.00 11.98           C  
ATOM   1359  C   ILE A 173      11.913  28.565   5.153  1.00 11.23           C  
ATOM   1360  O   ILE A 173      11.454  27.416   5.170  1.00 12.22           O  
ATOM   1361  CB  ILE A 173      12.258  28.858   2.683  1.00 12.32           C  
ATOM   1362  CG1 ILE A 173      13.279  29.195   1.578  1.00 12.72           C  
ATOM   1363  CG2 ILE A 173      11.047  29.785   2.587  1.00 13.58           C  
ATOM   1364  CD1 ILE A 173      12.776  28.942   0.141  1.00 14.63           C  
ATOM   1365  N   VAL A 174      11.623  29.486   6.066  1.00 10.73           N  
ATOM   1366  CA  VAL A 174      10.918  29.138   7.296  1.00 11.28           C  
ATOM   1367  C   VAL A 174       9.722  30.061   7.476  1.00 11.42           C  
ATOM   1368  O   VAL A 174       9.863  31.278   7.412  1.00 11.85           O  
ATOM   1369  CB  VAL A 174      11.860  29.252   8.518  1.00 11.30           C  
ATOM   1370  CG1 VAL A 174      11.192  28.685   9.760  1.00 11.80           C  
ATOM   1371  CG2 VAL A 174      13.186  28.500   8.271  1.00 11.97           C  
ATOM   1372  N   GLU A 175       8.553  29.472   7.712  1.00 12.10           N  
ATOM   1373  CA  GLU A 175       7.331  30.247   7.933  1.00 13.51           C  
ATOM   1374  C   GLU A 175       7.323  30.832   9.343  1.00 13.73           C  
ATOM   1375  O   GLU A 175       7.877  30.233  10.272  1.00 13.70           O  
ATOM   1376  CB  GLU A 175       6.083  29.383   7.679  1.00 14.14           C  
ATOM   1377  CG  GLU A 175       6.024  28.693   6.298  1.00 17.52           C  
ATOM   1378  CD  GLU A 175       6.081  29.657   5.120  1.00 23.42           C  
ATOM   1379  OE1 GLU A 175       5.265  30.601   5.083  1.00 25.55           O  
ATOM   1380  OE2 GLU A 175       6.936  29.464   4.220  1.00 25.15           O  
ATOM   1381  N   PRO A 176       6.693  32.015   9.519  1.00 14.10           N  
ATOM   1382  CA  PRO A 176       6.660  32.645  10.837  1.00 14.43           C  
ATOM   1383  C   PRO A 176       6.112  31.691  11.890  1.00 14.35           C  
ATOM   1384  O   PRO A 176       5.093  31.022  11.645  1.00 15.09           O  
ATOM   1385  CB  PRO A 176       5.698  33.825  10.653  1.00 14.93           C  
ATOM   1386  CG  PRO A 176       5.706  34.112   9.209  1.00 15.06           C  
ATOM   1387  CD  PRO A 176       5.998  32.814   8.496  1.00 14.28           C  
ATOM   1388  N   GLY A 177       6.788  31.627  13.032  1.00 14.58           N  
ATOM   1389  CA  GLY A 177       6.383  30.761  14.136  1.00 14.17           C  
ATOM   1390  C   GLY A 177       6.979  29.365  14.131  1.00 14.42           C  
ATOM   1391  O   GLY A 177       6.928  28.660  15.134  1.00 15.21           O  
ATOM   1392  N   THR A 178       7.532  28.951  12.990  1.00 13.80           N  
ATOM   1393  CA  THR A 178       8.158  27.632  12.886  1.00 13.67           C  
ATOM   1394  C   THR A 178       9.611  27.638  13.380  1.00 13.54           C  
ATOM   1395  O   THR A 178      10.371  28.564  13.111  1.00 12.89           O  
ATOM   1396  CB  THR A 178       8.081  27.105  11.433  1.00 13.46           C  
ATOM   1397  OG1 THR A 178       6.709  26.869  11.096  1.00 15.63           O  
ATOM   1398  CG2 THR A 178       8.855  25.782  11.259  1.00 13.50           C  
ATOM   1399  N   THR A 179       9.954  26.583  14.111  1.00 13.26           N  
ATOM   1400  CA  THR A 179      11.309  26.337  14.591  1.00 13.96           C  
ATOM   1401  C   THR A 179      11.921  25.198  13.783  1.00 14.08           C  
ATOM   1402  O   THR A 179      11.275  24.168  13.555  1.00 15.43           O  
ATOM   1403  CB  THR A 179      11.324  26.006  16.106  1.00 14.59           C  
ATOM   1404  OG1 THR A 179      10.794  27.122  16.834  1.00 15.23           O  
ATOM   1405  CG2 THR A 179      12.747  25.737  16.593  1.00 15.82           C  
ATOM   1406  N   VAL A 180      13.166  25.410  13.353  1.00 13.47           N  
ATOM   1407  CA  VAL A 180      13.946  24.450  12.564  1.00 13.93           C  
ATOM   1408  C   VAL A 180      15.254  24.214  13.295  1.00 12.80           C  
ATOM   1409  O   VAL A 180      15.794  25.131  13.916  1.00 12.49           O  
ATOM   1410  CB  VAL A 180      14.279  25.017  11.147  1.00 14.35           C  
ATOM   1411  CG1 VAL A 180      15.153  24.058  10.348  1.00 17.09           C  
ATOM   1412  CG2 VAL A 180      13.020  25.307  10.368  1.00 17.10           C  
ATOM   1413  N   VAL A 181      15.768  22.991  13.205  1.00 11.90           N  
ATOM   1414  CA  VAL A 181      17.048  22.650  13.813  1.00 11.97           C  
ATOM   1415  C   VAL A 181      18.031  22.186  12.743  1.00 11.47           C  
ATOM   1416  O   VAL A 181      17.692  21.328  11.907  1.00 11.74           O  
ATOM   1417  CB  VAL A 181      16.881  21.505  14.843  1.00 12.22           C  
ATOM   1418  CG1 VAL A 181      18.211  21.110  15.429  1.00 13.59           C  
ATOM   1419  CG2 VAL A 181      15.929  21.920  15.957  1.00 13.42           C  
ATOM   1420  N   GLN A 182      19.236  22.752  12.766  1.00 10.41           N  
ATOM   1421  CA  GLN A 182      20.350  22.248  11.959  1.00 10.24           C  
ATOM   1422  C   GLN A 182      21.405  21.582  12.854  1.00 10.49           C  
ATOM   1423  O   GLN A 182      21.900  22.205  13.800  1.00 11.13           O  
ATOM   1424  CB  GLN A 182      20.982  23.387  11.165  1.00 10.23           C  
ATOM   1425  CG  GLN A 182      22.235  22.971  10.403  1.00  9.92           C  
ATOM   1426  CD  GLN A 182      21.961  22.022   9.253  1.00  9.24           C  
ATOM   1427  OE1 GLN A 182      20.967  22.167   8.545  1.00  9.90           O  
ATOM   1428  NE2 GLN A 182      22.845  21.053   9.055  1.00  8.45           N  
ATOM   1429  N   ASP A 183      21.753  20.335  12.535  1.00  9.72           N  
ATOM   1430  CA  ASP A 183      22.836  19.607  13.221  1.00  9.69           C  
ATOM   1431  C   ASP A 183      24.193  19.971  12.639  1.00  9.52           C  
ATOM   1432  O   ASP A 183      24.327  20.145  11.426  1.00 10.04           O  
ATOM   1433  CB  ASP A 183      22.634  18.092  13.112  1.00  9.83           C  
ATOM   1434  CG  ASP A 183      22.482  17.626  11.673  1.00 10.28           C  
ATOM   1435  OD1 ASP A 183      21.690  18.238  10.924  1.00 10.51           O  
ATOM   1436  OD2 ASP A 183      23.163  16.649  11.292  1.00 14.14           O  
ATOM   1437  N   LEU A 184      25.198  20.090  13.506  1.00  9.13           N  
ATOM   1438  CA  LEU A 184      26.568  20.327  13.062  1.00  9.79           C  
ATOM   1439  C   LEU A 184      27.533  19.552  13.924  1.00  9.76           C  
ATOM   1440  O   LEU A 184      27.377  19.527  15.137  1.00 10.06           O  
ATOM   1441  CB  LEU A 184      26.934  21.809  13.190  1.00 10.33           C  
ATOM   1442  CG  LEU A 184      26.201  22.784  12.276  1.00 10.95           C  
ATOM   1443  CD1 LEU A 184      26.550  24.192  12.709  1.00 11.42           C  
ATOM   1444  CD2 LEU A 184      26.564  22.545  10.797  1.00 12.30           C  
ATOM   1445  N   PRO A 185      28.549  18.924  13.309  1.00  9.50           N  
ATOM   1446  CA  PRO A 185      29.625  18.320  14.111  1.00 10.19           C  
ATOM   1447  C   PRO A 185      30.290  19.401  14.960  1.00  9.82           C  
ATOM   1448  O   PRO A 185      30.411  20.548  14.517  1.00  9.59           O  
ATOM   1449  CB  PRO A 185      30.588  17.787  13.060  1.00  9.93           C  
ATOM   1450  CG  PRO A 185      29.713  17.565  11.832  1.00 10.78           C  
ATOM   1451  CD  PRO A 185      28.722  18.683  11.864  1.00  9.85           C  
ATOM   1452  N   GLY A 186      30.713  19.045  16.167  1.00 10.11           N  
ATOM   1453  CA  GLY A 186      31.214  20.045  17.114  1.00 10.19           C  
ATOM   1454  C   GLY A 186      32.415  20.854  16.643  1.00 10.14           C  
ATOM   1455  O   GLY A 186      32.594  22.017  17.045  1.00 10.83           O  
ATOM   1456  N   HIS A 187      33.234  20.263  15.777  1.00  9.72           N  
ATOM   1457  CA  HIS A 187      34.441  20.943  15.328  1.00  9.58           C  
ATOM   1458  C   HIS A 187      34.186  21.857  14.124  1.00  9.27           C  
ATOM   1459  O   HIS A 187      35.074  22.625  13.729  1.00  9.03           O  
ATOM   1460  CB  HIS A 187      35.555  19.937  15.021  1.00  9.91           C  
ATOM   1461  CG  HIS A 187      35.292  19.084  13.821  1.00 10.30           C  
ATOM   1462  ND1 HIS A 187      34.222  18.217  13.740  1.00 11.44           N  
ATOM   1463  CD2 HIS A 187      35.959  18.969  12.647  1.00 12.07           C  
ATOM   1464  CE1 HIS A 187      34.245  17.602  12.570  1.00 12.57           C  
ATOM   1465  NE2 HIS A 187      35.285  18.044  11.885  1.00 14.20           N  
ATOM   1466  N   TYR A 188      32.988  21.796  13.539  1.00  8.38           N  
ATOM   1467  CA  TYR A 188      32.696  22.682  12.407  1.00  7.92           C  
ATOM   1468  C   TYR A 188      32.631  24.134  12.886  1.00  7.67           C  
ATOM   1469  O   TYR A 188      32.194  24.428  14.005  1.00  8.37           O  
ATOM   1470  CB  TYR A 188      31.371  22.323  11.737  1.00  8.36           C  
ATOM   1471  CG  TYR A 188      31.408  21.261  10.656  1.00  7.70           C  
ATOM   1472  CD1 TYR A 188      32.294  20.192  10.701  1.00  9.37           C  
ATOM   1473  CD2 TYR A 188      30.502  21.321   9.592  1.00  9.29           C  
ATOM   1474  CE1 TYR A 188      32.282  19.216   9.708  1.00  8.07           C  
ATOM   1475  CE2 TYR A 188      30.486  20.353   8.589  1.00  8.18           C  
ATOM   1476  CZ  TYR A 188      31.380  19.307   8.656  1.00  8.97           C  
ATOM   1477  OH  TYR A 188      31.359  18.319   7.683  1.00 10.00           O  
ATOM   1478  N   ASN A 189      33.036  25.031  11.994  1.00  7.76           N  
ATOM   1479  CA  ASN A 189      33.035  26.457  12.229  1.00  8.43           C  
ATOM   1480  C   ASN A 189      32.085  27.056  11.210  1.00  8.41           C  
ATOM   1481  O   ASN A 189      32.172  26.741  10.026  1.00  8.58           O  
ATOM   1482  CB  ASN A 189      34.466  26.989  12.056  1.00  7.96           C  
ATOM   1483  CG  ASN A 189      34.605  28.470  12.402  1.00  8.43           C  
ATOM   1484  OD1 ASN A 189      33.814  29.028  13.162  1.00  8.64           O  
ATOM   1485  ND2 ASN A 189      35.641  29.094  11.870  1.00  9.21           N  
ATOM   1486  N   GLY A 190      31.172  27.920  11.647  1.00  9.14           N  
ATOM   1487  CA  GLY A 190      30.210  28.448  10.697  1.00  9.62           C  
ATOM   1488  C   GLY A 190      29.437  29.670  11.115  1.00  8.74           C  
ATOM   1489  O   GLY A 190      29.698  30.291  12.154  1.00  8.21           O  
ATOM   1490  N   PHE A 191      28.468  30.002  10.278  1.00  8.51           N  
ATOM   1491  CA  PHE A 191      27.690  31.206  10.432  1.00  8.15           C  
ATOM   1492  C   PHE A 191      26.492  31.077   9.506  1.00  7.80           C  
ATOM   1493  O   PHE A 191      26.429  30.166   8.670  1.00  7.58           O  
ATOM   1494  CB  PHE A 191      28.535  32.442  10.045  1.00  8.89           C  
ATOM   1495  CG  PHE A 191      28.948  32.459   8.600  1.00  7.80           C  
ATOM   1496  CD1 PHE A 191      28.133  33.074   7.659  1.00  8.54           C  
ATOM   1497  CD2 PHE A 191      30.091  31.799   8.172  1.00  8.77           C  
ATOM   1498  CE1 PHE A 191      28.466  33.057   6.311  1.00  9.54           C  
ATOM   1499  CE2 PHE A 191      30.439  31.768   6.826  1.00  8.43           C  
ATOM   1500  CZ  PHE A 191      29.635  32.402   5.893  1.00  9.30           C  
ATOM   1501  N   LEU A 192      25.557  31.999   9.625  1.00  7.62           N  
ATOM   1502  CA  LEU A 192      24.481  32.087   8.636  1.00  8.03           C  
ATOM   1503  C   LEU A 192      24.309  33.522   8.176  1.00  8.44           C  
ATOM   1504  O   LEU A 192      24.712  34.448   8.877  1.00  8.44           O  
ATOM   1505  CB  LEU A 192      23.156  31.470   9.155  1.00  8.47           C  
ATOM   1506  CG  LEU A 192      22.547  32.053  10.432  1.00  7.95           C  
ATOM   1507  CD1 LEU A 192      21.781  33.354  10.172  1.00  9.27           C  
ATOM   1508  CD2 LEU A 192      21.637  31.026  11.100  1.00  9.18           C  
ATOM   1509  N   TYR A 193      23.738  33.697   6.993  1.00  8.47           N  
ATOM   1510  CA  TYR A 193      23.460  35.024   6.475  1.00  8.73           C  
ATOM   1511  C   TYR A 193      21.996  35.086   6.087  1.00  8.58           C  
ATOM   1512  O   TYR A 193      21.497  34.196   5.393  1.00  8.27           O  
ATOM   1513  CB  TYR A 193      24.362  35.343   5.268  1.00  9.97           C  
ATOM   1514  CG  TYR A 193      24.048  36.685   4.669  1.00 10.64           C  
ATOM   1515  CD1 TYR A 193      24.441  37.851   5.306  1.00 11.75           C  
ATOM   1516  CD2 TYR A 193      23.312  36.784   3.481  1.00 12.23           C  
ATOM   1517  CE1 TYR A 193      24.137  39.091   4.765  1.00 12.46           C  
ATOM   1518  CE2 TYR A 193      22.985  38.027   2.937  1.00 14.33           C  
ATOM   1519  CZ  TYR A 193      23.418  39.170   3.590  1.00 13.21           C  
ATOM   1520  OH  TYR A 193      23.114  40.418   3.075  1.00 15.87           O  
ATOM   1521  N   ILE A 194      21.296  36.132   6.537  1.00  7.62           N  
ATOM   1522  CA  ILE A 194      19.863  36.210   6.348  1.00  8.38           C  
ATOM   1523  C   ILE A 194      19.531  37.019   5.098  1.00  8.95           C  
ATOM   1524  O   ILE A 194      19.911  38.183   4.983  1.00  9.71           O  
ATOM   1525  CB  ILE A 194      19.152  36.804   7.593  1.00  8.51           C  
ATOM   1526  CG1 ILE A 194      19.479  35.953   8.819  1.00  8.47           C  
ATOM   1527  CG2 ILE A 194      17.648  36.826   7.370  1.00  8.80           C  
ATOM   1528  CD1 ILE A 194      19.035  36.563  10.140  1.00 10.69           C  
ATOM   1529  N   LEU A 195      18.812  36.380   4.176  1.00  9.31           N  
ATOM   1530  CA  LEU A 195      18.410  37.014   2.924  1.00  9.91           C  
ATOM   1531  C   LEU A 195      17.121  37.823   3.059  1.00 11.06           C  
ATOM   1532  O   LEU A 195      16.971  38.879   2.423  1.00 11.28           O  
ATOM   1533  CB  LEU A 195      18.217  35.948   1.834  1.00  9.96           C  
ATOM   1534  CG  LEU A 195      19.467  35.141   1.476  1.00 11.03           C  
ATOM   1535  CD1 LEU A 195      19.091  33.901   0.670  1.00 11.89           C  
ATOM   1536  CD2 LEU A 195      20.448  36.015   0.732  1.00 12.99           C  
ATOM   1537  N   GLU A 196      16.190  37.314   3.859  1.00 11.16           N  
ATOM   1538  CA  GLU A 196      14.821  37.860   3.926  1.00 12.68           C  
ATOM   1539  C   GLU A 196      14.268  37.585   5.312  1.00 11.76           C  
ATOM   1540  O   GLU A 196      14.476  36.504   5.867  1.00 11.27           O  
ATOM   1541  CB  GLU A 196      13.933  37.181   2.873  1.00 13.03           C  
ATOM   1542  CG  GLU A 196      12.570  37.828   2.622  1.00 16.76           C  
ATOM   1543  CD  GLU A 196      11.643  36.913   1.807  1.00 17.53           C  
ATOM   1544  OE1 GLU A 196      12.135  35.928   1.199  1.00 22.92           O  
ATOM   1545  OE2 GLU A 196      10.421  37.174   1.783  1.00 21.84           O  
ATOM   1546  N   GLY A 197      13.554  38.554   5.868  1.00 11.29           N  
ATOM   1547  CA  GLY A 197      12.844  38.345   7.121  1.00 11.41           C  
ATOM   1548  C   GLY A 197      13.696  38.453   8.369  1.00 11.48           C  
ATOM   1549  O   GLY A 197      14.726  39.131   8.399  1.00 11.66           O  
ATOM   1550  N   SER A 198      13.232  37.787   9.418  1.00 11.67           N  
ATOM   1551  CA  SER A 198      13.851  37.873  10.732  1.00 11.74           C  
ATOM   1552  C   SER A 198      13.430  36.692  11.580  1.00 11.55           C  
ATOM   1553  O   SER A 198      12.465  35.988  11.265  1.00 11.82           O  
ATOM   1554  CB  SER A 198      13.449  39.167  11.447  1.00 12.35           C  
ATOM   1555  OG  SER A 198      12.045  39.241  11.605  1.00 15.15           O  
ATOM   1556  N   GLY A 199      14.181  36.478  12.650  1.00 11.35           N  
ATOM   1557  CA  GLY A 199      13.906  35.384  13.551  1.00 10.93           C  
ATOM   1558  C   GLY A 199      14.764  35.494  14.785  1.00 11.40           C  
ATOM   1559  O   GLY A 199      15.417  36.515  15.012  1.00 11.64           O  
ATOM   1560  N   VAL A 200      14.739  34.442  15.599  1.00 10.65           N  
ATOM   1561  CA  VAL A 200      15.637  34.318  16.753  1.00 11.12           C  
ATOM   1562  C   VAL A 200      16.440  33.016  16.602  1.00 10.89           C  
ATOM   1563  O   VAL A 200      15.956  32.037  16.009  1.00 11.13           O  
ATOM   1564  CB  VAL A 200      14.894  34.385  18.117  1.00 11.72           C  
ATOM   1565  CG1 VAL A 200      14.308  35.762  18.321  1.00 12.49           C  
ATOM   1566  CG2 VAL A 200      13.813  33.333  18.207  1.00 12.04           C  
ATOM   1567  N   PHE A 201      17.655  33.016  17.153  1.00 10.82           N  
ATOM   1568  CA  PHE A 201      18.658  32.024  16.773  1.00 11.36           C  
ATOM   1569  C   PHE A 201      19.463  31.547  17.954  1.00 11.84           C  
ATOM   1570  O   PHE A 201      19.864  32.341  18.797  1.00 11.62           O  
ATOM   1571  CB  PHE A 201      19.622  32.631  15.744  1.00 11.68           C  
ATOM   1572  CG  PHE A 201      18.964  33.028  14.465  1.00 10.57           C  
ATOM   1573  CD1 PHE A 201      18.882  32.124  13.407  1.00 10.85           C  
ATOM   1574  CD2 PHE A 201      18.404  34.292  14.313  1.00  9.37           C  
ATOM   1575  CE1 PHE A 201      18.273  32.491  12.222  1.00 11.84           C  
ATOM   1576  CE2 PHE A 201      17.777  34.652  13.136  1.00 10.57           C  
ATOM   1577  CZ  PHE A 201      17.714  33.756  12.087  1.00 10.92           C  
ATOM   1578  N   GLY A 202      19.728  30.246  17.985  1.00 12.16           N  
ATOM   1579  CA  GLY A 202      20.655  29.673  18.955  1.00 13.34           C  
ATOM   1580  C   GLY A 202      20.079  29.515  20.338  1.00 14.08           C  
ATOM   1581  O   GLY A 202      18.897  29.768  20.571  1.00 14.42           O  
ATOM   1582  N   ALA A 203      20.943  29.103  21.265  1.00 14.99           N  
ATOM   1583  CA  ALA A 203      20.532  28.809  22.633  1.00 16.06           C  
ATOM   1584  C   ALA A 203      19.892  29.986  23.365  1.00 17.05           C  
ATOM   1585  O   ALA A 203      19.001  29.789  24.204  1.00 17.46           O  
ATOM   1586  CB  ALA A 203      21.707  28.284  23.424  1.00 16.14           C  
ATOM   1587  N   ASP A 204      20.332  31.197  23.036  1.00 17.09           N  
ATOM   1588  CA  ASP A 204      19.894  32.404  23.733  1.00 18.00           C  
ATOM   1589  C   ASP A 204      18.866  33.218  22.943  1.00 17.42           C  
ATOM   1590  O   ASP A 204      18.539  34.346  23.330  1.00 17.98           O  
ATOM   1591  CB  ASP A 204      21.100  33.286  24.070  1.00 18.46           C  
ATOM   1592  CG  ASP A 204      22.112  32.587  24.954  0.80 19.87           C  
ATOM   1593  OD1 ASP A 204      21.712  32.051  26.010  0.60 20.95           O  
ATOM   1594  OD2 ASP A 204      23.310  32.575  24.592  0.60 21.22           O  
ATOM   1595  N   ASN A 205      18.372  32.663  21.836  1.00 16.50           N  
ATOM   1596  CA  ASN A 205      17.346  33.329  21.026  1.00 16.04           C  
ATOM   1597  C   ASN A 205      17.749  34.746  20.606  1.00 15.36           C  
ATOM   1598  O   ASN A 205      16.994  35.715  20.771  1.00 15.45           O  
ATOM   1599  CB  ASN A 205      15.984  33.317  21.741  1.00 16.35           C  
ATOM   1600  CG  ASN A 205      15.469  31.914  21.988  1.00 18.48           C  
ATOM   1601  OD1 ASN A 205      15.394  31.106  21.075  1.00 21.69           O  
ATOM   1602  ND2 ASN A 205      15.093  31.630  23.225  1.00 22.38           N  
ATOM   1603  N   ILE A 206      18.955  34.850  20.056  1.00 14.36           N  
ATOM   1604  CA  ILE A 206      19.492  36.114  19.570  1.00 14.01           C  
ATOM   1605  C   ILE A 206      18.771  36.519  18.286  1.00 13.59           C  
ATOM   1606  O   ILE A 206      18.553  35.693  17.394  1.00 13.21           O  
ATOM   1607  CB  ILE A 206      21.021  35.989  19.322  1.00 14.05           C  
ATOM   1608  CG1 ILE A 206      21.770  35.723  20.633  1.00 13.96           C  
ATOM   1609  CG2 ILE A 206      21.597  37.202  18.591  1.00 15.16           C  
ATOM   1610  CD1 ILE A 206      21.573  36.776  21.747  1.00 15.82           C  
ATOM   1611  N   GLU A 207      18.381  37.788  18.202  1.00 13.25           N  
ATOM   1612  CA  GLU A 207      17.644  38.277  17.049  1.00 13.30           C  
ATOM   1613  C   GLU A 207      18.556  38.415  15.855  1.00 12.96           C  
ATOM   1614  O   GLU A 207      19.719  38.801  15.984  1.00 13.07           O  
ATOM   1615  CB  GLU A 207      17.007  39.639  17.346  1.00 13.79           C  
ATOM   1616  CG  GLU A 207      15.844  39.593  18.331  1.00 15.99           C  
ATOM   1617  CD  GLU A 207      15.496  40.960  18.881  1.00 18.45           C  
ATOM   1618  OE1 GLU A 207      15.992  41.978  18.341  1.00 20.94           O  
ATOM   1619  OE2 GLU A 207      14.716  41.019  19.852  0.40 17.69           O  
ATOM   1620  N   GLY A 208      18.011  38.089  14.690  1.00 12.10           N  
ATOM   1621  CA  GLY A 208      18.687  38.345  13.431  1.00 11.33           C  
ATOM   1622  C   GLY A 208      17.689  38.757  12.369  1.00 11.12           C  
ATOM   1623  O   GLY A 208      16.557  38.261  12.342  1.00 10.72           O  
ATOM   1624  N   LYS A 209      18.120  39.647  11.482  1.00 10.99           N  
ATOM   1625  CA  LYS A 209      17.263  40.087  10.369  1.00 10.88           C  
ATOM   1626  C   LYS A 209      18.039  40.155   9.060  1.00 10.05           C  
ATOM   1627  O   LYS A 209      19.267  40.048   9.053  1.00  9.92           O  
ATOM   1628  CB  LYS A 209      16.585  41.433  10.654  1.00 11.10           C  
ATOM   1629  CG  LYS A 209      17.559  42.516  10.997  1.00 12.61           C  
ATOM   1630  CD  LYS A 209      16.839  43.799  11.405  0.20 11.49           C  
ATOM   1631  CE  LYS A 209      17.968  44.754  11.307  0.00 33.96           C  
ATOM   1632  NZ  LYS A 209      18.816  44.800  12.525  0.00 35.88           N  
ATOM   1633  N   ALA A 210      17.309  40.331   7.957  1.00 10.71           N  
ATOM   1634  CA  ALA A 210      17.908  40.400   6.637  1.00 10.80           C  
ATOM   1635  C   ALA A 210      19.082  41.369   6.588  1.00 10.32           C  
ATOM   1636  O   ALA A 210      19.015  42.499   7.107  1.00 10.96           O  
ATOM   1637  CB  ALA A 210      16.864  40.772   5.582  1.00 11.46           C  
ATOM   1638  N   GLY A 211      20.161  40.904   5.971  1.00  9.95           N  
ATOM   1639  CA  GLY A 211      21.375  41.698   5.817  1.00 10.07           C  
ATOM   1640  C   GLY A 211      22.371  41.496   6.938  1.00  9.77           C  
ATOM   1641  O   GLY A 211      23.395  42.177   6.987  1.00 10.24           O  
ATOM   1642  N   GLN A 212      22.081  40.551   7.828  1.00  9.31           N  
ATOM   1643  CA  GLN A 212      22.993  40.229   8.929  1.00  9.65           C  
ATOM   1644  C   GLN A 212      23.580  38.841   8.799  1.00  9.44           C  
ATOM   1645  O   GLN A 212      22.904  37.905   8.340  1.00  9.81           O  
ATOM   1646  CB  GLN A 212      22.290  40.357  10.281  1.00  9.95           C  
ATOM   1647  CG  GLN A 212      21.720  41.754  10.518  1.00 10.46           C  
ATOM   1648  CD  GLN A 212      21.256  41.933  11.934  1.00 10.44           C  
ATOM   1649  OE1 GLN A 212      20.452  41.144  12.438  1.00 11.36           O  
ATOM   1650  NE2 GLN A 212      21.759  42.975  12.596  1.00 10.12           N  
ATOM   1651  N   ALA A 213      24.842  38.733   9.212  1.00  9.39           N  
ATOM   1652  CA  ALA A 213      25.511  37.443   9.391  1.00  9.33           C  
ATOM   1653  C   ALA A 213      25.621  37.137  10.872  1.00  9.31           C  
ATOM   1654  O   ALA A 213      26.049  37.993  11.658  1.00  9.43           O  
ATOM   1655  CB  ALA A 213      26.884  37.457   8.748  1.00  9.58           C  
ATOM   1656  N   LEU A 214      25.231  35.920  11.251  1.00  8.92           N  
ATOM   1657  CA  LEU A 214      25.240  35.481  12.654  1.00  9.06           C  
ATOM   1658  C   LEU A 214      26.228  34.347  12.777  1.00  8.95           C  
ATOM   1659  O   LEU A 214      26.080  33.339  12.098  1.00  9.07           O  
ATOM   1660  CB  LEU A 214      23.839  35.046  13.098  1.00  9.81           C  
ATOM   1661  CG  LEU A 214      22.864  36.164  13.489  1.00 10.56           C  
ATOM   1662  CD1 LEU A 214      22.443  37.006  12.288  1.00 11.09           C  
ATOM   1663  CD2 LEU A 214      21.632  35.551  14.126  1.00 11.16           C  
ATOM   1664  N   PHE A 215      27.251  34.539  13.612  1.00  7.82           N  
ATOM   1665  CA  PHE A 215      28.351  33.580  13.724  1.00  7.89           C  
ATOM   1666  C   PHE A 215      28.129  32.655  14.896  1.00  8.19           C  
ATOM   1667  O   PHE A 215      27.632  33.087  15.939  1.00  8.67           O  
ATOM   1668  CB  PHE A 215      29.677  34.321  13.876  1.00  8.29           C  
ATOM   1669  CG  PHE A 215      30.035  35.121  12.670  1.00  7.30           C  
ATOM   1670  CD1 PHE A 215      30.834  34.574  11.665  1.00  8.59           C  
ATOM   1671  CD2 PHE A 215      29.521  36.406  12.494  1.00  8.13           C  
ATOM   1672  CE1 PHE A 215      31.137  35.308  10.522  1.00  9.29           C  
ATOM   1673  CE2 PHE A 215      29.813  37.141  11.360  1.00  9.49           C  
ATOM   1674  CZ  PHE A 215      30.626  36.601  10.377  1.00  8.62           C  
ATOM   1675  N   PHE A 216      28.533  31.392  14.744  1.00  8.29           N  
ATOM   1676  CA  PHE A 216      28.233  30.363  15.733  1.00  8.48           C  
ATOM   1677  C   PHE A 216      29.384  30.167  16.723  1.00  8.81           C  
ATOM   1678  O   PHE A 216      30.547  30.266  16.360  1.00  9.06           O  
ATOM   1679  CB  PHE A 216      27.927  28.996  15.077  1.00  8.54           C  
ATOM   1680  CG  PHE A 216      26.925  29.046  13.948  1.00  8.81           C  
ATOM   1681  CD1 PHE A 216      25.899  29.997  13.927  1.00  8.89           C  
ATOM   1682  CD2 PHE A 216      26.983  28.097  12.918  1.00  9.99           C  
ATOM   1683  CE1 PHE A 216      24.988  30.030  12.876  1.00  8.83           C  
ATOM   1684  CE2 PHE A 216      26.063  28.120  11.867  1.00 10.18           C  
ATOM   1685  CZ  PHE A 216      25.057  29.085  11.850  1.00  9.42           C  
ATOM   1686  N   SER A 217      29.019  29.842  17.963  1.00  9.25           N  
ATOM   1687  CA  SER A 217      29.976  29.370  18.953  1.00  9.30           C  
ATOM   1688  C   SER A 217      30.734  28.156  18.448  1.00  9.46           C  
ATOM   1689  O   SER A 217      30.227  27.389  17.643  1.00  9.69           O  
ATOM   1690  CB  SER A 217      29.251  29.002  20.257  1.00  9.42           C  
ATOM   1691  OG  SER A 217      28.153  28.142  19.994  1.00 10.09           O  
ATOM   1692  N   ARG A 218      31.944  27.994  18.964  1.00 10.15           N  
ATOM   1693  CA  ARG A 218      32.781  26.847  18.656  1.00 10.67           C  
ATOM   1694  C   ARG A 218      32.646  25.775  19.718  1.00 10.55           C  
ATOM   1695  O   ARG A 218      32.423  26.079  20.893  1.00 11.79           O  
ATOM   1696  CB  ARG A 218      34.241  27.285  18.580  1.00 10.53           C  
ATOM   1697  CG  ARG A 218      34.533  28.330  17.496  1.00 12.66           C  
ATOM   1698  CD  ARG A 218      34.432  27.768  16.084  1.00 12.87           C  
ATOM   1699  NE  ARG A 218      35.509  26.834  15.752  1.00 12.12           N  
ATOM   1700  CZ  ARG A 218      36.711  27.165  15.255  1.00  9.68           C  
ATOM   1701  NH1 ARG A 218      37.050  28.429  15.029  1.00 11.50           N  
ATOM   1702  NH2 ARG A 218      37.601  26.212  15.006  1.00 10.42           N  
ATOM   1703  N   HIS A 219      32.770  24.520  19.289  1.00 10.68           N  
ATOM   1704  CA  HIS A 219      32.651  23.387  20.188  1.00 10.77           C  
ATOM   1705  C   HIS A 219      33.785  22.397  19.924  1.00 11.48           C  
ATOM   1706  O   HIS A 219      34.723  22.713  19.203  1.00 11.83           O  
ATOM   1707  CB  HIS A 219      31.239  22.797  20.066  1.00 11.18           C  
ATOM   1708  CG  HIS A 219      30.184  23.803  20.387  1.00 10.88           C  
ATOM   1709  ND1 HIS A 219      29.715  23.995  21.667  1.00 11.44           N  
ATOM   1710  CD2 HIS A 219      29.591  24.750  19.622  1.00 11.28           C  
ATOM   1711  CE1 HIS A 219      28.846  24.991  21.670  1.00 12.27           C  
ATOM   1712  NE2 HIS A 219      28.750  25.463  20.441  1.00 11.56           N  
ATOM   1713  N   ASN A 220      33.712  21.222  20.540  1.00 12.24           N  
ATOM   1714  CA  ASN A 220      34.780  20.232  20.459  1.00 12.77           C  
ATOM   1715  C   ASN A 220      34.524  19.184  19.401  1.00 12.70           C  
ATOM   1716  O   ASN A 220      33.382  18.794  19.171  1.00 12.68           O  
ATOM   1717  CB  ASN A 220      34.941  19.519  21.803  1.00 12.98           C  
ATOM   1718  CG  ASN A 220      35.290  20.465  22.925  1.00 14.75           C  
ATOM   1719  OD1 ASN A 220      36.343  21.094  22.905  1.00 16.68           O  
ATOM   1720  ND2 ASN A 220      34.410  20.572  23.914  1.00 17.52           N  
ATOM   1721  N   ARG A 221      35.597  18.705  18.777  1.00 13.02           N  
ATOM   1722  CA  ARG A 221      35.491  17.577  17.856  1.00 14.67           C  
ATOM   1723  C   ARG A 221      34.833  16.399  18.582  1.00 14.52           C  
ATOM   1724  O   ARG A 221      35.107  16.138  19.764  1.00 14.79           O  
ATOM   1725  CB  ARG A 221      36.876  17.176  17.345  1.00 14.80           C  
ATOM   1726  CG  ARG A 221      36.867  16.137  16.232  1.00 16.47           C  
ATOM   1727  CD  ARG A 221      38.264  15.588  15.967  1.00 17.36           C  
ATOM   1728  NE  ARG A 221      38.217  14.476  15.022  1.00 23.00           N  
ATOM   1729  CZ  ARG A 221      38.218  14.603  13.695  1.00 24.37           C  
ATOM   1730  NH1 ARG A 221      38.278  15.806  13.128  1.00 25.92           N  
ATOM   1731  NH2 ARG A 221      38.165  13.517  12.931  1.00 26.34           N  
ATOM   1732  N   GLY A 222      33.944  15.714  17.871  1.00 14.59           N  
ATOM   1733  CA  GLY A 222      33.248  14.558  18.424  1.00 14.67           C  
ATOM   1734  C   GLY A 222      31.936  14.871  19.114  1.00 14.95           C  
ATOM   1735  O   GLY A 222      31.192  13.956  19.469  1.00 15.42           O  
ATOM   1736  N   GLU A 223      31.646  16.152  19.326  1.00 14.60           N  
ATOM   1737  CA  GLU A 223      30.383  16.551  19.936  1.00 15.08           C  
ATOM   1738  C   GLU A 223      29.298  16.737  18.889  1.00 15.22           C  
ATOM   1739  O   GLU A 223      29.557  17.240  17.791  1.00 16.70           O  
ATOM   1740  CB  GLU A 223      30.547  17.820  20.760  1.00 15.15           C  
ATOM   1741  CG  GLU A 223      31.502  17.624  21.925  1.00 15.55           C  
ATOM   1742  CD  GLU A 223      31.726  18.883  22.730  1.00 17.44           C  
ATOM   1743  OE1 GLU A 223      31.479  19.988  22.200  1.00 16.35           O  
ATOM   1744  OE2 GLU A 223      32.162  18.764  23.897  1.00 18.87           O  
ATOM   1745  N   GLU A 224      28.083  16.325  19.230  1.00 14.17           N  
ATOM   1746  CA  GLU A 224      26.946  16.522  18.346  1.00 13.83           C  
ATOM   1747  C   GLU A 224      26.301  17.821  18.786  1.00 13.55           C  
ATOM   1748  O   GLU A 224      25.862  17.943  19.931  1.00 14.24           O  
ATOM   1749  CB  GLU A 224      25.978  15.317  18.403  1.00 13.92           C  
ATOM   1750  CG  GLU A 224      26.533  14.051  17.715  1.00 15.62           C  
ATOM   1751  CD  GLU A 224      25.615  12.806  17.780  0.60 14.58           C  
ATOM   1752  OE1 GLU A 224      24.512  12.881  18.374  0.80 17.05           O  
ATOM   1753  OE2 GLU A 224      26.014  11.734  17.232  1.00 17.82           O  
ATOM   1754  N   THR A 225      26.309  18.822  17.900  1.00 11.91           N  
ATOM   1755  CA  THR A 225      25.746  20.130  18.225  1.00 11.91           C  
ATOM   1756  C   THR A 225      24.569  20.460  17.318  1.00 11.97           C  
ATOM   1757  O   THR A 225      24.398  19.856  16.261  1.00 11.43           O  
ATOM   1758  CB  THR A 225      26.779  21.293  18.125  1.00 11.89           C  
ATOM   1759  OG1 THR A 225      27.055  21.604  16.750  1.00 11.21           O  
ATOM   1760  CG2 THR A 225      28.089  20.974  18.883  1.00 11.26           C  
ATOM   1761  N   GLU A 226      23.753  21.411  17.761  1.00 11.51           N  
ATOM   1762  CA  GLU A 226      22.585  21.847  17.004  1.00 12.54           C  
ATOM   1763  C   GLU A 226      22.454  23.358  17.051  1.00 11.99           C  
ATOM   1764  O   GLU A 226      22.850  23.997  18.034  1.00 12.42           O  
ATOM   1765  CB  GLU A 226      21.315  21.192  17.561  1.00 12.39           C  
ATOM   1766  CG  GLU A 226      21.160  19.732  17.127  1.00 14.41           C  
ATOM   1767  CD  GLU A 226      19.989  19.007  17.775  1.00 14.90           C  
ATOM   1768  OE1 GLU A 226      19.341  19.581  18.667  1.00 18.90           O  
ATOM   1769  OE2 GLU A 226      19.755  17.839  17.398  1.00 19.73           O  
ATOM   1770  N   LEU A 227      21.929  23.923  15.966  1.00 12.18           N  
ATOM   1771  CA  LEU A 227      21.521  25.318  15.956  1.00 12.18           C  
ATOM   1772  C   LEU A 227      20.027  25.445  15.721  1.00 12.37           C  
ATOM   1773  O   LEU A 227      19.501  24.985  14.696  1.00 12.43           O  
ATOM   1774  CB  LEU A 227      22.263  26.111  14.893  1.00 12.43           C  
ATOM   1775  CG  LEU A 227      21.832  27.580  14.968  1.00 14.53           C  
ATOM   1776  CD1 LEU A 227      22.745  28.339  15.909  1.00 13.32           C  
ATOM   1777  CD2 LEU A 227      21.819  28.222  13.609  1.00 15.35           C  
ATOM   1778  N   ASN A 228      19.360  26.079  16.679  1.00 12.43           N  
ATOM   1779  CA  ASN A 228      17.930  26.338  16.611  1.00 13.24           C  
ATOM   1780  C   ASN A 228      17.633  27.645  15.882  1.00 12.49           C  
ATOM   1781  O   ASN A 228      18.313  28.648  16.088  1.00 12.20           O  
ATOM   1782  CB  ASN A 228      17.326  26.384  18.025  1.00 13.84           C  
ATOM   1783  CG  ASN A 228      17.400  25.051  18.746  0.90 16.49           C  
ATOM   1784  OD1 ASN A 228      17.553  23.998  18.127  1.00 19.81           O  
ATOM   1785  ND2 ASN A 228      17.289  25.093  20.068  0.20 15.50           N  
ATOM   1786  N   VAL A 229      16.625  27.607  15.017  1.00 12.11           N  
ATOM   1787  CA  VAL A 229      16.190  28.760  14.242  1.00 12.03           C  
ATOM   1788  C   VAL A 229      14.676  28.880  14.369  1.00 11.78           C  
ATOM   1789  O   VAL A 229      13.962  27.926  14.063  1.00 12.14           O  
ATOM   1790  CB  VAL A 229      16.513  28.568  12.730  1.00 11.90           C  
ATOM   1791  CG1 VAL A 229      15.892  29.676  11.887  1.00 13.18           C  
ATOM   1792  CG2 VAL A 229      18.025  28.518  12.504  1.00 12.86           C  
ATOM   1793  N   THR A 230      14.188  30.036  14.823  1.00 11.87           N  
ATOM   1794  CA  THR A 230      12.735  30.286  14.867  1.00 11.84           C  
ATOM   1795  C   THR A 230      12.404  31.529  14.052  1.00 11.59           C  
ATOM   1796  O   THR A 230      12.912  32.603  14.347  1.00 11.82           O  
ATOM   1797  CB  THR A 230      12.219  30.464  16.317  1.00 12.25           C  
ATOM   1798  OG1 THR A 230      12.573  29.311  17.093  1.00 13.80           O  
ATOM   1799  CG2 THR A 230      10.707  30.635  16.327  1.00 13.13           C  
ATOM   1800  N   ALA A 231      11.553  31.383  13.032  1.00 11.43           N  
ATOM   1801  CA  ALA A 231      11.168  32.546  12.208  1.00 11.56           C  
ATOM   1802  C   ALA A 231      10.191  33.434  12.959  1.00 12.45           C  
ATOM   1803  O   ALA A 231       9.271  32.938  13.607  1.00 12.43           O  
ATOM   1804  CB  ALA A 231      10.551  32.109  10.886  1.00 11.37           C  
ATOM   1805  N   ARG A 232      10.401  34.741  12.866  1.00 12.68           N  
ATOM   1806  CA  ARG A 232       9.387  35.694  13.310  1.00 14.59           C  
ATOM   1807  C   ARG A 232       8.640  36.288  12.118  1.00 15.28           C  
ATOM   1808  O   ARG A 232       7.411  36.276  12.100  1.00 17.19           O  
ATOM   1809  CB  ARG A 232       9.995  36.736  14.243  1.00 14.96           C  
ATOM   1810  CG  ARG A 232      10.435  36.128  15.591  1.00 17.59           C  
ATOM   1811  CD  ARG A 232       9.273  35.427  16.325  1.00 20.34           C  
ATOM   1812  NE  ARG A 232       9.736  34.508  17.365  1.00 23.67           N  
ATOM   1813  CZ  ARG A 232       8.944  33.684  18.045  0.90 23.84           C  
ATOM   1814  NH1 ARG A 232       9.459  32.886  18.972  1.00 24.98           N  
ATOM   1815  NH2 ARG A 232       8.077  33.063  17.169  0.00 35.02           N  
ATOM   1816  N   GLU A 233       9.374  36.796  11.133  1.00 15.57           N  
ATOM   1817  CA  GLU A 233       8.810  37.055   9.812  1.00 15.72           C  
ATOM   1818  C   GLU A 233       9.155  35.879   8.882  1.00 15.69           C  
ATOM   1819  O   GLU A 233       9.956  35.006   9.254  1.00 16.91           O  
ATOM   1820  CB  GLU A 233       9.352  38.352   9.225  1.00 16.40           C  
ATOM   1821  CG  GLU A 233       9.112  39.604  10.038  1.00 17.04           C  
ATOM   1822  CD  GLU A 233       9.870  40.777   9.452  1.00 20.94           C  
ATOM   1823  OE1 GLU A 233      11.109  40.838   9.615  1.00 19.77           O  
ATOM   1824  OE2 GLU A 233       9.224  41.622   8.798  1.00 21.82           O  
ATOM   1825  N   LYS A 234       8.539  35.828   7.701  1.00 14.93           N  
ATOM   1826  CA  LYS A 234       8.908  34.825   6.690  1.00 14.44           C  
ATOM   1827  C   LYS A 234      10.413  34.929   6.461  1.00 13.51           C  
ATOM   1828  O   LYS A 234      10.910  35.972   6.050  1.00 13.73           O  
ATOM   1829  CB  LYS A 234       8.132  35.063   5.383  1.00 14.91           C  
ATOM   1830  CG  LYS A 234       8.315  33.999   4.306  1.00 16.85           C  
ATOM   1831  CD  LYS A 234       7.818  32.642   4.764  0.20 16.02           C  
ATOM   1832  CE  LYS A 234       8.032  31.749   3.266  0.00 31.27           C  
ATOM   1833  NZ  LYS A 234       7.753  32.193   1.828  0.00 39.94           N  
ATOM   1834  N   LEU A 235      11.125  33.837   6.737  1.00 12.33           N  
ATOM   1835  CA  LEU A 235      12.580  33.864   6.844  1.00 11.47           C  
ATOM   1836  C   LEU A 235      13.248  33.057   5.737  1.00 10.71           C  
ATOM   1837  O   LEU A 235      12.871  31.915   5.485  1.00 11.39           O  
ATOM   1838  CB  LEU A 235      12.991  33.310   8.216  1.00 11.58           C  
ATOM   1839  CG  LEU A 235      14.450  33.173   8.640  1.00 10.50           C  
ATOM   1840  CD1 LEU A 235      15.111  34.532   8.770  1.00 10.05           C  
ATOM   1841  CD2 LEU A 235      14.514  32.460   9.973  1.00 10.96           C  
ATOM   1842  N   ARG A 236      14.240  33.660   5.090  1.00 10.07           N  
ATOM   1843  CA  ARG A 236      15.072  32.945   4.136  1.00  9.57           C  
ATOM   1844  C   ARG A 236      16.531  33.210   4.488  1.00  8.95           C  
ATOM   1845  O   ARG A 236      16.915  34.355   4.677  1.00  9.16           O  
ATOM   1846  CB  ARG A 236      14.774  33.380   2.700  1.00 10.01           C  
ATOM   1847  CG  ARG A 236      15.444  32.510   1.647  1.00 12.79           C  
ATOM   1848  CD  ARG A 236      14.867  32.800   0.263  1.00 17.56           C  
ATOM   1849  NE  ARG A 236      15.332  31.833  -0.728  1.00 20.61           N  
ATOM   1850  CZ  ARG A 236      14.694  31.549  -1.862  1.00 21.48           C  
ATOM   1851  NH1 ARG A 236      13.538  32.144  -2.166  1.00 23.99           N  
ATOM   1852  NH2 ARG A 236      15.208  30.657  -2.695  1.00 22.13           N  
ATOM   1853  N   LEU A 237      17.335  32.153   4.594  1.00  8.13           N  
ATOM   1854  CA  LEU A 237      18.730  32.321   5.001  1.00  7.67           C  
ATOM   1855  C   LEU A 237      19.614  31.232   4.408  1.00  7.57           C  
ATOM   1856  O   LEU A 237      19.132  30.179   4.002  1.00  7.48           O  
ATOM   1857  CB  LEU A 237      18.849  32.346   6.532  1.00  8.06           C  
ATOM   1858  CG  LEU A 237      18.478  31.068   7.299  1.00  8.60           C  
ATOM   1859  CD1 LEU A 237      19.590  30.017   7.298  1.00  9.16           C  
ATOM   1860  CD2 LEU A 237      18.108  31.432   8.727  1.00  8.56           C  
ATOM   1861  N   LEU A 238      20.909  31.515   4.366  1.00  7.08           N  
ATOM   1862  CA  LEU A 238      21.928  30.531   4.012  1.00  7.95           C  
ATOM   1863  C   LEU A 238      22.801  30.258   5.221  1.00  8.15           C  
ATOM   1864  O   LEU A 238      23.282  31.181   5.857  1.00  8.39           O  
ATOM   1865  CB  LEU A 238      22.783  31.041   2.848  1.00  7.91           C  
ATOM   1866  CG  LEU A 238      22.071  31.182   1.502  1.00  9.21           C  
ATOM   1867  CD1 LEU A 238      22.917  32.041   0.584  1.00 10.69           C  
ATOM   1868  CD2 LEU A 238      21.783  29.829   0.888  1.00 11.31           C  
ATOM   1869  N   LEU A 239      22.999  28.982   5.532  1.00  8.07           N  
ATOM   1870  CA  LEU A 239      23.892  28.570   6.612  1.00  7.73           C  
ATOM   1871  C   LEU A 239      25.106  27.887   6.001  1.00  7.33           C  
ATOM   1872  O   LEU A 239      24.967  26.983   5.163  1.00  7.67           O  
ATOM   1873  CB  LEU A 239      23.173  27.616   7.578  1.00  8.04           C  
ATOM   1874  CG  LEU A 239      23.901  27.106   8.827  1.00  8.09           C  
ATOM   1875  CD1 LEU A 239      22.919  26.820   9.951  1.00  9.87           C  
ATOM   1876  CD2 LEU A 239      24.721  25.846   8.514  1.00  8.67           C  
ATOM   1877  N   TYR A 240      26.292  28.311   6.440  1.00  7.14           N  
ATOM   1878  CA  TYR A 240      27.555  27.765   5.956  1.00  7.03           C  
ATOM   1879  C   TYR A 240      28.347  27.289   7.156  1.00  7.54           C  
ATOM   1880  O   TYR A 240      28.540  28.051   8.097  1.00  7.20           O  
ATOM   1881  CB  TYR A 240      28.394  28.847   5.299  1.00  7.28           C  
ATOM   1882  CG  TYR A 240      27.819  29.570   4.105  1.00  7.53           C  
ATOM   1883  CD1 TYR A 240      28.129  29.158   2.809  1.00  7.65           C  
ATOM   1884  CD2 TYR A 240      27.028  30.712   4.262  1.00  8.46           C  
ATOM   1885  CE1 TYR A 240      27.656  29.876   1.689  1.00  8.12           C  
ATOM   1886  CE2 TYR A 240      26.556  31.426   3.153  1.00  8.59           C  
ATOM   1887  CZ  TYR A 240      26.873  30.994   1.874  1.00  8.54           C  
ATOM   1888  OH  TYR A 240      26.414  31.710   0.787  1.00  8.77           O  
ATOM   1889  N   ALA A 241      28.830  26.045   7.133  1.00  7.83           N  
ATOM   1890  CA  ALA A 241      29.683  25.566   8.212  1.00  7.89           C  
ATOM   1891  C   ALA A 241      30.631  24.547   7.645  1.00  8.44           C  
ATOM   1892  O   ALA A 241      30.248  23.769   6.780  1.00  9.15           O  
ATOM   1893  CB  ALA A 241      28.845  24.960   9.322  1.00  7.90           C  
ATOM   1894  N   GLY A 242      31.875  24.548   8.102  1.00  8.25           N  
ATOM   1895  CA  GLY A 242      32.840  23.637   7.526  1.00  8.45           C  
ATOM   1896  C   GLY A 242      33.874  23.158   8.515  1.00  8.30           C  
ATOM   1897  O   GLY A 242      34.021  23.713   9.605  1.00  8.53           O  
ATOM   1898  N   GLU A 243      34.615  22.145   8.104  1.00  8.70           N  
ATOM   1899  CA  GLU A 243      35.672  21.597   8.932  1.00  9.39           C  
ATOM   1900  C   GLU A 243      36.922  22.464   8.800  1.00  9.13           C  
ATOM   1901  O   GLU A 243      37.454  22.598   7.701  1.00  9.14           O  
ATOM   1902  CB  GLU A 243      35.982  20.193   8.454  1.00 10.35           C  
ATOM   1903  CG  GLU A 243      37.120  19.529   9.180  1.00 12.42           C  
ATOM   1904  CD  GLU A 243      37.223  18.080   8.792  1.00 14.49           C  
ATOM   1905  OE1 GLU A 243      37.860  17.798   7.763  1.00 16.51           O  
ATOM   1906  OE2 GLU A 243      36.661  17.228   9.524  1.00 18.41           O  
ATOM   1907  N   PRO A 244      37.395  23.068   9.910  1.00  9.30           N  
ATOM   1908  CA  PRO A 244      38.631  23.858   9.812  1.00  9.81           C  
ATOM   1909  C   PRO A 244      39.828  23.095   9.257  1.00 10.21           C  
ATOM   1910  O   PRO A 244      39.987  21.903   9.533  1.00 10.85           O  
ATOM   1911  CB  PRO A 244      38.894  24.285  11.265  1.00  9.88           C  
ATOM   1912  CG  PRO A 244      37.529  24.332  11.875  1.00  9.26           C  
ATOM   1913  CD  PRO A 244      36.829  23.121  11.271  1.00  9.80           C  
ATOM   1914  N   VAL A 245      40.644  23.804   8.477  1.00 10.42           N  
ATOM   1915  CA  VAL A 245      41.847  23.243   7.856  1.00 11.56           C  
ATOM   1916  C   VAL A 245      42.975  23.200   8.880  1.00 12.36           C  
ATOM   1917  O   VAL A 245      43.763  22.251   8.896  1.00 12.61           O  
ATOM   1918  CB  VAL A 245      42.249  24.042   6.593  1.00 11.34           C  
ATOM   1919  CG1 VAL A 245      43.550  23.527   6.024  1.00 12.12           C  
ATOM   1920  CG2 VAL A 245      41.153  23.968   5.545  1.00 13.09           C  
ATOM   1921  N   ASN A 246      43.030  24.209   9.751  1.00 12.83           N  
ATOM   1922  CA  ASN A 246      44.041  24.267  10.805  1.00 14.43           C  
ATOM   1923  C   ASN A 246      45.469  24.271  10.256  1.00 15.81           C  
ATOM   1924  O   ASN A 246      46.361  23.586  10.779  1.00 16.57           O  
ATOM   1925  CB  ASN A 246      43.817  23.126  11.815  1.00 14.04           C  
ATOM   1926  CG  ASN A 246      42.538  23.308  12.624  1.00 14.39           C  
ATOM   1927  OD1 ASN A 246      42.257  24.394  13.120  1.00 15.91           O  
ATOM   1928  ND2 ASN A 246      41.765  22.241  12.759  1.00 14.62           N  
ATOM   1929  N   GLU A 247      45.672  25.046   9.198  1.00 16.79           N  
ATOM   1930  CA  GLU A 247      47.008  25.211   8.624  1.00 18.45           C  
ATOM   1931  C   GLU A 247      47.361  26.676   8.534  1.00 20.26           C  
ATOM   1932  O   GLU A 247      46.493  27.491   8.226  1.00 20.72           O  
ATOM   1933  CB  GLU A 247      47.081  24.583   7.232  1.00 18.03           C  
ATOM   1934  CG  GLU A 247      47.041  23.082   7.265  1.00 17.18           C  
ATOM   1935  CD  GLU A 247      46.920  22.459   5.889  1.00 16.07           C  
ATOM   1936  OE1 GLU A 247      46.899  23.192   4.870  1.00 15.52           O  
ATOM   1937  OE2 GLU A 247      46.838  21.224   5.854  1.00 16.25           O  
ATOM   1938  N   PRO A 248      48.649  27.014   8.787  1.00 22.08           N  
ATOM   1939  CA  PRO A 248      49.093  28.399   8.615  1.00 23.52           C  
ATOM   1940  C   PRO A 248      48.701  28.895   7.229  1.00 24.47           C  
ATOM   1941  O   PRO A 248      48.917  28.194   6.235  0.60 24.72           O  
ATOM   1942  CB  PRO A 248      50.620  28.317   8.739  0.40 23.34           C  
ATOM   1943  CG  PRO A 248      50.859  27.016   9.152  0.00 20.00           C  
ATOM   1944  CD  PRO A 248      49.731  26.114   9.236  0.60 22.01           C  
ATOM   1945  N   VAL A 249      48.099  30.078   7.175  1.00 25.23           N  
ATOM   1946  CA  VAL A 249      47.668  30.672   5.916  1.00 25.99           C  
ATOM   1947  C   VAL A 249      48.707  31.652   5.370  1.00 26.14           C  
ATOM   1948  O   VAL A 249      48.767  31.899   4.161  1.00 27.08           O  
ATOM   1949  CB  VAL A 249      46.330  31.401   6.081  1.00 25.95           C  
ATOM   1950  CG1 VAL A 249      45.501  31.308   4.820  1.00 26.67           C  
ATOM   1951  CG2 VAL A 249      45.452  29.791   6.281  0.00 20.00           C  
TER    1952      VAL A 249                                                      
HETATM 1953 FE    FE A 278      37.271  35.565  -8.874  0.50 13.19          FE  
HETATM 1954  O   HOH A 279      34.837  21.308  -0.464  1.00 11.94           O  
HETATM 1955  O   HOH A 280      27.918  31.605  -1.561  1.00  9.12           O  
HETATM 1956  O   HOH A 281      17.371  27.839  -4.119  1.00 12.79           O  
HETATM 1957  O   HOH A 282      31.553  28.299  14.565  1.00  8.67           O  
HETATM 1958  O   HOH A 283      46.850  19.215   4.068  1.00 13.00           O  
HETATM 1959  O   HOH A 284      35.774  31.000  15.308  1.00 13.02           O  
HETATM 1960  O   HOH A 285      27.935  17.091  -0.122  1.00 12.64           O  
HETATM 1961  O   HOH A 286      39.059  36.209   6.447  1.00 12.73           O  
HETATM 1962  O   HOH A 287      32.305  31.337  12.872  1.00 14.06           O  
HETATM 1963  O   HOH A 288      37.117  23.415  15.294  1.00 12.28           O  
HETATM 1964  O   HOH A 289      21.606  10.282   3.348  1.00 11.97           O  
HETATM 1965  O   HOH A 290      33.796  24.450  16.462  1.00 13.38           O  
HETATM 1966  O   HOH A 291      23.395  15.333   9.012  1.00 13.82           O  
HETATM 1967  O   HOH A 292      29.556  18.560   5.751  1.00 11.83           O  
HETATM 1968  O   HOH A 293      38.069  22.873   0.184  1.00 13.62           O  
HETATM 1969  O   HOH A 294      38.947  20.525  11.866  1.00 13.61           O  
HETATM 1970  O   HOH A 295      39.277  21.882  14.179  1.00 12.93           O  
HETATM 1971  O   HOH A 296      20.843  26.436  19.179  1.00 15.67           O  
HETATM 1972  O   HOH A 297      28.331  45.044  12.325  1.00 15.57           O  
HETATM 1973  O   HOH A 298      44.428  20.207   7.271  1.00 23.77           O  
HETATM 1974  O   HOH A 299      22.315  20.724 -10.869  1.00 15.85           O  
HETATM 1975  O   HOH A 300      23.637  43.847 -17.097  1.00 16.24           O  
HETATM 1976  O   HOH A 301      23.533  12.607  -2.142  1.00 14.68           O  
HETATM 1977  O   HOH A 302       7.650  24.662  14.850  1.00 19.85           O  
HETATM 1978  O   HOH A 303      32.090  26.118 -16.473  1.00 16.21           O  
HETATM 1979  O   HOH A 304      28.413  12.006  15.874  1.00 20.14           O  
HETATM 1980  O   HOH A 305      39.511  28.841  13.718  1.00 15.65           O  
HETATM 1981  O   HOH A 306      15.849  37.693 -10.687  1.00 19.11           O  
HETATM 1982  O   HOH A 307      30.931  22.272  23.613  1.00 17.38           O  
HETATM 1983  O   HOH A 308      13.893  20.993  12.328  1.00 22.12           O  
HETATM 1984  O   HOH A 309      30.978  40.935 -14.754  1.00 13.83           O  
HETATM 1985  O   HOH A 310      33.044  30.325  20.681  1.00 18.56           O  
HETATM 1986  O   HOH A 311      16.085  13.785   8.507  1.00 18.12           O  
HETATM 1987  O   HOH A 312      19.169  41.819  14.703  1.00 17.71           O  
HETATM 1988  O   HOH A 313      23.415  21.688 -13.288  1.00 22.73           O  
HETATM 1989  O   HOH A 314      40.366  30.551   6.929  1.00 19.22           O  
HETATM 1990  O   HOH A 315      31.940  30.025  -7.745  1.00 15.85           O  
HETATM 1991  O   HOH A 316      39.615  18.374  -7.965  1.00 22.90           O  
HETATM 1992  O   HOH A 317      24.484  17.112  15.905  1.00 17.88           O  
HETATM 1993  O   HOH A 318      23.554  12.045  20.886  1.00 18.41           O  
HETATM 1994  O   HOH A 319      30.519  17.639   3.309  1.00 13.66           O  
HETATM 1995  O   HOH A 320      36.897  22.287  17.748  1.00 18.60           O  
HETATM 1996  O   HOH A 321      19.000  39.620  20.390  1.00 21.98           O  
HETATM 1997  O   HOH A 322      27.454  14.592  21.301  1.00 18.50           O  
HETATM 1998  O   HOH A 323      33.052  16.237  15.303  1.00 17.49           O  
HETATM 1999  O   HOH A 324      47.729  25.922  -5.747  1.00 20.30           O  
HETATM 2000  O   HOH A 325      20.572  44.468   8.434  1.00 19.94           O  
HETATM 2001  O   HOH A 326      43.662  27.504 -17.336  1.00 20.32           O  
HETATM 2002  O   HOH A 327      34.041  37.333 -11.790  1.00 17.95           O  
HETATM 2003  O   HOH A 328      28.188  17.897  -8.431  1.00 20.58           O  
HETATM 2004  O   HOH A 329      34.849  20.377 -14.127  1.00 17.83           O  
HETATM 2005  O   HOH A 330      32.656  48.348 -11.932  1.00 25.54           O  
HETATM 2006  O   HOH A 331      32.066  39.828  10.003  1.00 18.96           O  
HETATM 2007  O   HOH A 332      29.090  38.011  -4.866  1.00 18.74           O  
HETATM 2008  O   HOH A 333      27.900  16.223   6.343  1.00 19.82           O  
HETATM 2009  O   HOH A 334      22.100  32.162  20.694  1.00 13.42           O  
HETATM 2010  O   HOH A 335      18.084  40.665  -4.960  1.00 19.34           O  
HETATM 2011  O   HOH A 336      31.363  34.981 -17.960  1.00 26.67           O  
HETATM 2012  O   HOH A 337      26.085  19.055   8.703  1.00 20.48           O  
HETATM 2013  O   HOH A 338      41.808  28.123   6.423  1.00 16.63           O  
HETATM 2014  O   HOH A 339      31.700  41.543 -20.117  1.00 31.66           O  
HETATM 2015  O   HOH A 340       6.862  42.332   9.655  1.00 21.39           O  
HETATM 2016  O   HOH A 341      13.415  41.124   4.654  1.00 21.87           O  
HETATM 2017  O   HOH A 342      40.536  15.570  -4.876  1.00 24.61           O  
HETATM 2018  O   HOH A 343      16.659  44.085   7.345  1.00 24.61           O  
HETATM 2019  O   HOH A 344       9.490  38.263   5.442  1.00 23.63           O  
HETATM 2020  O   HOH A 345      32.327  15.944   8.137  1.00 20.69           O  
HETATM 2021  O   HOH A 346      38.219  15.794   6.168  1.00 21.64           O  
HETATM 2022  O   HOH A 347      22.748  45.008   6.159  1.00 22.66           O  
HETATM 2023  O   HOH A 348      29.021  46.380  10.170  1.00 22.06           O  
HETATM 2024  O   HOH A 349      20.495  40.903  17.335  1.00 20.15           O  
HETATM 2025  O   HOH A 350      35.008  15.998   2.157  1.00 20.89           O  
HETATM 2026  O   HOH A 351      28.957  55.406  -9.140  1.00 32.25           O  
HETATM 2027  O   HOH A 352      27.662  31.453 -19.823  1.00 22.37           O  
HETATM 2028  O   HOH A 353      14.904  29.321  -7.602  1.00 25.91           O  
HETATM 2029  O   HOH A 354      41.855  14.786   3.735  1.00 24.38           O  
HETATM 2030  O   HOH A 355      28.092  20.497 -12.973  1.00 23.21           O  
HETATM 2031  O   HOH A 356      17.297  39.286 -14.615  1.00 23.64           O  
HETATM 2032  O   HOH A 357      17.692  42.075 -13.385  1.00 27.48           O  
HETATM 2033  O   HOH A 358      35.976  15.377  -3.764  1.00 21.35           O  
HETATM 2034  O   HOH A 359      37.603  42.413 -12.353  1.00 27.37           O  
HETATM 2035  O   HOH A 360      40.766  40.212 -18.774  1.00 19.28           O  
HETATM 2036  O   HOH A 361      30.036  45.052   5.717  1.00 18.43           O  
HETATM 2037  O   HOH A 362      22.709  14.576  21.518  1.00 18.34           O  
HETATM 2038  O   HOH A 363      23.239  26.983 -19.680  1.00 24.10           O  
HETATM 2039  O   HOH A 364      40.559  37.596  14.483  1.00 22.59           O  
HETATM 2040  O   HOH A 365      15.055  28.698  17.948  1.00 23.18           O  
HETATM 2041  O   HOH A 366      17.138  25.404 -10.093  1.00 19.28           O  
HETATM 2042  O   HOH A 367      43.094  37.048  -9.535  1.00 30.35           O  
HETATM 2043  O   HOH A 368      14.745  25.863   1.224  1.00 20.60           O  
HETATM 2044  O   HOH A 369      15.251  40.997   2.145  1.00 27.37           O  
HETATM 2045  O   HOH A 370      21.948  16.072  16.677  1.00 19.74           O  
HETATM 2046  O   HOH A 371      28.508  14.879  -7.460  1.00 26.19           O  
HETATM 2047  O   HOH A 372      30.832  12.324  17.332  1.00 22.74           O  
HETATM 2048  O   HOH A 373      15.504  21.586  -4.119  1.00 25.31           O  
HETATM 2049  O   HOH A 374      41.279  35.861   3.679  1.00 20.57           O  
HETATM 2050  O   HOH A 375      44.403  25.911  13.562  1.00 20.73           O  
HETATM 2051  O   HOH A 376      30.373  23.965 -17.110  1.00 19.88           O  
HETATM 2052  O   HOH A 377      12.408  30.207  19.861  1.00 28.66           O  
HETATM 2053  O   HOH A 378      11.979  22.956 -12.956  1.00 22.49           O  
HETATM 2054  O   HOH A 379      11.847  15.618   3.548  1.00 21.88           O  
HETATM 2055  O   HOH A 380      49.164  26.139  -8.204  1.00 28.10           O  
HETATM 2056  O   HOH A 381      30.508  37.771 -21.024  1.00 21.20           O  
HETATM 2057  O   HOH A 382      43.373  32.762  -5.725  1.00 30.48           O  
HETATM 2058  O   HOH A 383      31.779  26.273 -23.101  1.00 24.06           O  
HETATM 2059  O   HOH A 384      32.513  14.779  -1.267  1.00 23.28           O  
HETATM 2060  O   HOH A 385      25.893  16.822  11.813  1.00 23.86           O  
HETATM 2061  O   HOH A 386       4.517  28.484  11.084  1.00 19.98           O  
HETATM 2062  O   HOH A 387      30.209  52.800   9.703  1.00 30.87           O  
HETATM 2063  O   HOH A 388      41.682  27.383  12.606  1.00 23.18           O  
HETATM 2064  O   HOH A 389      32.462  18.335 -11.376  1.00 25.48           O  
HETATM 2065  O   HOH A 390      13.572  17.019   8.552  1.00 29.34           O  
HETATM 2066  O   HOH A 391      33.280  30.502   9.647  1.00 27.10           O  
HETATM 2067  O   HOH A 392      18.685  42.308  18.795  1.00 30.53           O  
HETATM 2068  O   HOH A 393       9.400  26.482   1.597  1.00 26.62           O  
HETATM 2069  O   HOH A 394      41.464  19.567   9.157  1.00 24.14           O  
HETATM 2070  O   HOH A 395      21.612  16.750  -6.075  1.00 25.13           O  
HETATM 2071  O   HOH A 396      24.239  11.978   5.480  1.00 36.21           O  
HETATM 2072  O   HOH A 397       8.558  27.394   4.116  1.00 22.44           O  
HETATM 2073  O   HOH A 398      15.785  29.922 -10.896  1.00 22.33           O  
HETATM 2074  O   HOH A 399      28.585  54.054  -1.253  1.00 31.19           O  
HETATM 2075  O   HOH A 400      16.877  27.889  21.397  1.00 26.03           O  
HETATM 2076  O   HOH A 401      23.993  33.550  22.096  1.00 25.16           O  
HETATM 2077  O   HOH A 402      26.335  15.876  14.335  1.00 25.31           O  
HETATM 2078  O   HOH A 403      22.205  12.217  -4.516  1.00 18.36           O  
HETATM 2079  O   HOH A 404      44.657  17.696   4.384  1.00 22.20           O  
HETATM 2080  O   HOH A 405      28.568  14.508  14.527  1.00 24.80           O  
HETATM 2081  O   HOH A 406      16.616  30.552  19.059  1.00 22.59           O  
HETATM 2082  O   HOH A 407      39.626  16.789   3.734  1.00 28.18           O  
HETATM 2083  O   HOH A 408      25.452  19.997 -13.947  1.00 25.62           O  
HETATM 2084  O   HOH A 409      48.615  27.457  -3.941  1.00 29.28           O  
HETATM 2085  O   HOH A 410      30.536  24.058 -19.982  1.00 25.41           O  
HETATM 2086  O   HOH A 411       5.947  34.208  15.625  1.00 29.63           O  
HETATM 2087  O   HOH A 412      26.479  47.118 -18.170  1.00 28.36           O  
HETATM 2088  O   HOH A 413      32.534  15.799   3.099  1.00 22.61           O  
HETATM 2089  O   HOH A 414      14.502  15.015  10.261  1.00 22.28           O  
HETATM 2090  O   HOH A 415       7.611  18.634  10.265  1.00 30.00           O  
HETATM 2091  O   HOH A 416      28.995  15.418   1.906  1.00 22.71           O  
HETATM 2092  O   HOH A 417      20.504  14.822  -4.820  1.00 27.88           O  
HETATM 2093  O   HOH A 418      39.100  20.263   6.651  1.00 26.20           O  
HETATM 2094  O   HOH A 419      49.191  20.601 -14.850  1.00 26.19           O  
HETATM 2095  O   HOH A 420      27.884  14.509   4.375  1.00 32.78           O  
HETATM 2096  O   HOH A 421      25.024  47.963  -8.887  1.00 27.23           O  
HETATM 2097  O   HOH A 422      15.115  29.188  -4.974  1.00 21.15           O  
HETATM 2098  O   HOH A 423      18.067  21.595  19.187  1.00 27.30           O  
HETATM 2099  O   HOH A 424      34.223  13.925  14.108  1.00 23.94           O  
HETATM 2100  O   HOH A 425       7.428  22.213   3.707  1.00 26.39           O  
HETATM 2101  O   HOH A 426      30.525  15.501  15.982  1.00 26.21           O  
HETATM 2102  O   HOH A 427      15.140  36.024  -6.382  1.00 26.30           O  
HETATM 2103  O   HOH A 428      19.896  29.179 -17.217  1.00 26.38           O  
HETATM 2104  O   HOH A 429      12.122  38.471  17.926  1.00 27.22           O  
HETATM 2105  O   HOH A 430      25.927  50.780  -8.584  1.00 29.50           O  
HETATM 2106  O   HOH A 431      24.965  48.658   7.728  1.00 30.09           O  
HETATM 2107  O   HOH A 432      21.722  40.116  21.138  1.00 28.28           O  
HETATM 2108  O   HOH A 433       9.595  40.781   6.203  1.00 27.19           O  
HETATM 2109  O   HOH A 434      31.323  46.172   3.333  1.00 29.41           O  
HETATM 2110  O   HOH A 435      17.554  28.679 -12.625  1.00 26.20           O  
HETATM 2111  O   HOH A 436      42.976  19.682  11.875  1.00 26.99           O  
HETATM 2112  O   HOH A 437      25.904  30.739 -21.546  1.00 30.15           O  
HETATM 2113  O   HOH A 438      39.597  41.204  10.717  1.00 27.74           O  
HETATM 2114  O   HOH A 439      18.560  41.349  -9.494  1.00 21.80           O  
HETATM 2115  O   HOH A 440      42.626  18.689   6.085  1.00 30.43           O  
HETATM 2116  O   HOH A 441      21.932  32.949 -16.712  1.00 31.67           O  
HETATM 2117  O   HOH A 442      32.773  12.741  -3.551  1.00 30.82           O  
HETATM 2118  O   HOH A 443      14.634  27.019  19.931  1.00 29.21           O  
HETATM 2119  O   HOH A 444      18.456  18.366  20.908  1.00 23.82           O  
HETATM 2120  O   HOH A 445      31.271  19.689  26.367  1.00 24.41           O  
HETATM 2121  O   HOH A 446      16.282  19.912 -13.284  1.00 39.76           O  
HETATM 2122  O   HOH A 447      14.222  36.635  -8.899  1.00 26.43           O  
HETATM 2123  O   HOH A 448      50.549  21.894  -1.680  1.00 26.75           O  
HETATM 2124  O   HOH A 449      14.041  38.889  15.220  1.00 28.81           O  
HETATM 2125  O   HOH A 450      27.649  23.370 -16.038  1.00 27.22           O  
HETATM 2126  O   HOH A 451      43.507  39.076  11.328  1.00 29.08           O  
HETATM 2127  O   HOH A 452      22.424  14.359  12.674  1.00 25.92           O  
HETATM 2128  O   HOH A 453       3.295  27.527   8.772  1.00 32.57           O  
HETATM 2129  O   HOH A 454      14.149  25.168  -6.484  1.00 26.48           O  
HETATM 2130  O   HOH A 455      31.885  26.559  23.469  1.00 30.36           O  
HETATM 2131  O   HOH A 456      17.877  14.821  -4.880  1.00 30.27           O  
HETATM 2132  O   HOH A 457      32.095  15.276  11.108  1.00 29.95           O  
HETATM 2133  O   HOH A 458      46.525  27.776   3.636  1.00 25.00           O  
HETATM 2134  O   HOH A 459      23.806  18.447  -9.914  1.00 30.20           O  
HETATM 2135  O   HOH A 460      11.867  15.820   6.585  1.00 34.44           O  
HETATM 2136  O   HOH A 461      23.369  44.716 -19.882  1.00 31.36           O  
HETATM 2137  O   HOH A 462      36.977  14.608   4.100  1.00 29.03           O  
HETATM 2138  O   HOH A 463      24.519  25.820 -17.262  1.00 32.12           O  
HETATM 2139  O   HOH A 464      24.230  39.559  20.321  1.00 28.80           O  
HETATM 2140  O   HOH A 465      32.837  14.530   6.000  1.00 29.87           O  
HETATM 2141  O   HOH A 466      19.741  46.477  10.462  1.00 31.64           O  
HETATM 2142  O   HOH A 467      42.255  39.921 -16.401  1.00 26.58           O  
HETATM 2143  O   HOH A 468      16.225  38.543  -1.385  1.00 37.56           O  
HETATM 2144  O   HOH A 469      23.696  32.239 -21.705  1.00 29.43           O  
HETATM 2145  O   HOH A 470      15.776  39.425  -3.925  1.00 27.86           O  
HETATM 2146  O   HOH A 471      17.254  33.886  -3.464  1.00 27.10           O  
HETATM 2147  O   HOH A 472      22.833  12.098  -7.082  1.00 26.58           O  
HETATM 2148  O   HOH A 473      16.206  47.197  10.806  1.00 46.04           O  
HETATM 2149  O   HOH A 474      24.767  13.299  13.961  1.00 28.09           O  
HETATM 2150  O   HOH A 475      51.320  24.363  -2.158  1.00 41.84           O  
HETATM 2151  O   HOH A 476      30.730  28.157 -25.052  1.00 29.72           O  
HETATM 2152  O   HOH A 477      34.755  13.969  11.473  1.00 32.84           O  
HETATM 2153  O   HOH A 478      29.608  13.989  12.259  1.00 32.33           O  
HETATM 2154  O   HOH A 479      27.214  24.247 -19.033  1.00 38.10           O  
HETATM 2155  O   HOH A 480      33.522  35.062 -20.087  1.00 30.43           O  
HETATM 2156  O   HOH A 481      29.626  21.980  26.012  1.00 29.17           O  
HETATM 2157  O   HOH A 482      25.962  37.657  19.805  1.00 30.67           O  
HETATM 2158  O   HOH A 483      10.767  40.318  13.934  1.00 35.42           O  
HETATM 2159  O   HOH A 484       5.537  19.261   1.368  1.00 34.58           O  
HETATM 2160  O   HOH A 485       5.558  26.285  15.671  1.00 30.82           O  
HETATM 2161  O   HOH A 486      30.764  21.325 -16.501  1.00 24.71           O  
HETATM 2162  O   HOH A 487      21.278  43.544   0.156  1.00 33.15           O  
HETATM 2163  O   HOH A 488      33.923  21.923  -7.594  1.00 15.22           O  
HETATM 2164  O   HOH A 489      34.981  20.250  -4.133  1.00 16.81           O  
CONECT    1    2                                                                
CONECT    2    1    3    5                                                      
CONECT    3    2    4    9                                                      
CONECT    4    3                                                                
CONECT    5    2    6                                                           
CONECT    6    5    7                                                           
CONECT    7    6    8                                                           
CONECT    8    7                                                                
CONECT    9    3                                                                
CONECT  115  122                                                                
CONECT  122  115  123                                                           
CONECT  123  122  124  126                                                      
CONECT  124  123  125  130                                                      
CONECT  125  124                                                                
CONECT  126  123  127                                                           
CONECT  127  126  128                                                           
CONECT  128  127  129                                                           
CONECT  129  128                                                                
CONECT  130  124                                                                
CONECT  341  347                                                                
CONECT  347  341  348                                                           
CONECT  348  347  349  351                                                      
CONECT  349  348  350  355                                                      
CONECT  350  349                                                                
CONECT  351  348  352                                                           
CONECT  352  351  353                                                           
CONECT  353  352  354                                                           
CONECT  354  353                                                                
CONECT  355  349                                                                
CONECT  474 1953                                                                
CONECT  716  728                                                                
CONECT  728  716  729                                                           
CONECT  729  728  730  732                                                      
CONECT  730  729  731  736                                                      
CONECT  731  730                                                                
CONECT  732  729  733                                                           
CONECT  733  732  734                                                           
CONECT  734  733  735                                                           
CONECT  735  734                                                                
CONECT  736  730                                                                
CONECT  790 1953                                                                
CONECT  969  976                                                                
CONECT  976  969  977                                                           
CONECT  977  976  978  980                                                      
CONECT  978  977  979  984                                                      
CONECT  979  978                                                                
CONECT  980  977  981                                                           
CONECT  981  980  982                                                           
CONECT  982  981  983                                                           
CONECT  983  982                                                                
CONECT  984  978                                                                
CONECT 1083 1089                                                                
CONECT 1089 1083 1090                                                           
CONECT 1090 1089 1091 1093                                                      
CONECT 1091 1090 1092 1097                                                      
CONECT 1092 1091                                                                
CONECT 1093 1090 1094                                                           
CONECT 1094 1093 1095                                                           
CONECT 1095 1094 1096                                                           
CONECT 1096 1095                                                                
CONECT 1097 1091                                                                
CONECT 1320 1325                                                                
CONECT 1325 1320 1326                                                           
CONECT 1326 1325 1327 1329                                                      
CONECT 1327 1326 1328 1333                                                      
CONECT 1328 1327                                                                
CONECT 1329 1326 1330                                                           
CONECT 1330 1329 1331                                                           
CONECT 1331 1330 1332                                                           
CONECT 1332 1331                                                                
CONECT 1333 1327                                                                
CONECT 1342 1349                                                                
CONECT 1349 1342 1350                                                           
CONECT 1350 1349 1351 1353                                                      
CONECT 1351 1350 1352 1357                                                      
CONECT 1352 1351                                                                
CONECT 1353 1350 1354                                                           
CONECT 1354 1353 1355                                                           
CONECT 1355 1354 1356                                                           
CONECT 1356 1355                                                                
CONECT 1357 1351                                                                
CONECT 1953  474  790                                                           
MASTER      397    0    9    3   27    0    1    6 2163    1   82   22          
END                                                                             



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

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