CNRS Nantes University UFIP UFIP
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***  prova  ***

elNémo ID: 21072810165020994

Job options:

ID        	=	 21072810165020994
JOBID     	=	 prova
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER prova

HEADER    AMINO-ACID BINDING PROTEIN              25-FEB-93   2LAO              
TITLE     THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-,   
TITLE    2 ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE, ARGININE, ORNITHINE-BINDING PROTEIN;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602                                                  
KEYWDS    AMINO-ACID BINDING PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-H.KIM,B.-H.OH,C.-H.KANG                                            
REVDAT   4   29-NOV-17 2LAO    1       HELIX                                    
REVDAT   3   24-FEB-09 2LAO    1       VERSN                                    
REVDAT   2   01-APR-03 2LAO    1       JRNL                                     
REVDAT   1   22-JUN-94 2LAO    0                                                
JRNL        AUTH   B.H.OH,J.PANDIT,C.H.KANG,K.NIKAIDO,S.GOKCEN,G.F.AMES,S.H.KIM 
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC              
JRNL        TITL 2 LYSINE/ARGININE/ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A 
JRNL        TITL 3 LIGAND.                                                      
JRNL        REF    J.BIOL.CHEM.                  V. 268 11348 1993              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   8496186                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.-H.KANG,W.-C.SHIN,Y.YAMAGATA,S.GOKCEN,G.F.-L.AMES,S.-H.KIM 
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE LYSINE-,ARGININE-,                  
REMARK   1  TITL 2 ORNITHINE-BINDING PROTEIN FROM SALMONELLA TYPHIMURIUM AT 2.7 
REMARK   1  TITL 3 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    J.BIOL.CHEM.                  V. 266 23893 1992              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 22643                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1822                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.760                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2LAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178293.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       18.12500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.09000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.26000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.09000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.26000            
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  44    CG   CD   CE   NZ                                   
REMARK 470     LYS A 225    CG   CD   CE   NZ                                   
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    HIS A 113   NE2   HIS A 113   CD2    -0.073                       
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   7   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TRP A  47   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP A  47   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TRP A 130   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP A 130   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    LYS A 188   CA  -  CB  -  CG  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    TYR A 230   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 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    THR A  12       32.24    -85.04                                   
REMARK 500    SER A  69       51.60   -154.74                                   
REMARK 500    TRP A 130      -51.90   -124.36                                   
REMARK 500    PHE A 169      -49.83   -157.18                                   
REMARK 500    ASP A 193       56.54   -114.35                                   
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    TYR A 178         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: ARGT_SALTY                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        VAL   102             ILE         102                         
REMARK 999                                                                      
REMARK 999 RESIDUE 102 OF THE LAO PROTEIN IS ISOLEUCINE, BUT WAS                
REMARK 999 REPORTED AS VALINE IN SWISS-PROT DATA BANK DUE TO                    
REMARK 999 SEQUENCING ERROR (PERSONAL COMMUNICATION).                           
DBREF  2LAO A    1   238  UNP    P02911   ARGT_SALTY      23    260             
SEQADV 2LAO ILE A  102  UNP  P02911    VAL   124 CONFLICT                       
SEQRES   1 A  238  ALA LEU PRO GLN THR VAL ARG ILE GLY THR ASP THR THR          
SEQRES   2 A  238  TYR ALA PRO PHE SER SER LYS ASP ALA LYS GLY GLU PHE          
SEQRES   3 A  238  ILE GLY PHE ASP ILE ASP LEU GLY ASN GLU MET CYS LYS          
SEQRES   4 A  238  ARG MET GLN VAL LYS CYS THR TRP VAL ALA SER ASP PHE          
SEQRES   5 A  238  ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP          
SEQRES   6 A  238  ALA ILE ILE SER SER LEU SER ILE THR ASP LYS ARG GLN          
SEQRES   7 A  238  GLN GLU ILE ALA PHE SER ASP LYS LEU TYR ALA ALA ASP          
SEQRES   8 A  238  SER ARG LEU ILE ALA ALA LYS GLY SER PRO ILE GLN PRO          
SEQRES   9 A  238  THR LEU GLU SER LEU LYS GLY LYS HIS VAL GLY VAL LEU          
SEQRES  10 A  238  GLN GLY SER THR GLN GLU ALA TYR ALA ASN ASP ASN TRP          
SEQRES  11 A  238  ARG THR LYS GLY VAL ASP VAL VAL ALA TYR ALA ASN GLN          
SEQRES  12 A  238  ASP LEU ILE TYR SER ASP LEU THR ALA GLY ARG LEU ASP          
SEQRES  13 A  238  ALA ALA LEU GLN ASP GLU VAL ALA ALA SER GLU GLY PHE          
SEQRES  14 A  238  LEU LYS GLN PRO ALA GLY LYS GLU TYR ALA PHE ALA GLY          
SEQRES  15 A  238  PRO SER VAL LYS ASP LYS LYS TYR PHE GLY ASP GLY THR          
SEQRES  16 A  238  GLY VAL GLY LEU ARG LYS ASP ASP THR GLU LEU LYS ALA          
SEQRES  17 A  238  ALA PHE ASP LYS ALA LEU THR GLU LEU ARG GLN ASP GLY          
SEQRES  18 A  238  THR TYR ASP LYS MET ALA LYS LYS TYR PHE ASP PHE ASN          
SEQRES  19 A  238  VAL TYR GLY ASP                                              
FORMUL   2  HOH   *89(H2 O)                                                     
HELIX    1   A PHE A   29  MET A   41  1                                  13    
HELIX    2   B LEU A   55  LYS A   60  1                                   6    
HELIX    3   C ASP A   75  GLU A   80  1                                   6    
HELIX    4   D LEU A  106  LEU A  109  1                                   4    
HELIX    5   E THR A  121  ASN A  129  1                                   9    
HELIX    6   F GLN A  143  THR A  151  1                                   9    
HELIX    7   G GLU A  162  GLY A  168  1                                   7    
HELIX    8   H LYS A  188  PHE A  191  1                                   4    
HELIX    9   I THR A  204  GLN A  219  1                                  16    
HELIX   10   J THR A  222  LYS A  228  1                                   7    
SHEET    1   1 5 LYS A  44  ALA A  49  0                                        
SHEET    2   1 5 THR A   5  THR A  10  1                                        
SHEET    3   1 5 ALA A  66  ILE A  67  1                                        
SHEET    4   1 5 VAL A 197  LEU A 199 -1                                        
SHEET    5   1 5 ALA A  82  SER A  84  1                                        
SHEET    1   2 5 ASP A 136  TYR A 140  0                                        
SHEET    2   2 5 HIS A 113  LEU A 117  1                                        
SHEET    3   2 5 ALA A 157  ASP A 161  1                                        
SHEET    4   2 5 SER A  92  ALA A  97 -1                                        
SHEET    5   2 5 TYR A 178  ALA A 181  1                                        
SSBOND   1 CYS A   38    CYS A   45                          1555   1555  2.31  
CISPEP   1 ALA A   15    PRO A   16          0        -1.71                     
CRYST1   36.250   78.520  102.180  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      0.027586  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012736  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009787        0.00000                         
ATOM      1  N   ALA A   1      51.436  44.270  10.041  1.00 53.66           N  
ATOM      2  CA  ALA A   1      50.955  44.766   8.768  1.00 53.06           C  
ATOM      3  C   ALA A   1      49.537  45.148   9.133  1.00 53.22           C  
ATOM      4  O   ALA A   1      48.970  44.538  10.055  1.00 55.56           O  
ATOM      5  CB  ALA A   1      50.876  43.697   7.677  1.00 50.98           C  
ATOM      6  N   LEU A   2      48.955  46.154   8.482  1.00 51.61           N  
ATOM      7  CA  LEU A   2      47.580  46.528   8.769  1.00 49.38           C  
ATOM      8  C   LEU A   2      46.572  45.453   8.330  1.00 49.23           C  
ATOM      9  O   LEU A   2      46.822  44.727   7.358  1.00 51.91           O  
ATOM     10  CB  LEU A   2      47.330  47.867   8.085  1.00 45.80           C  
ATOM     11  CG  LEU A   2      47.009  49.054   8.973  1.00 44.31           C  
ATOM     12  CD1 LEU A   2      47.905  49.032  10.197  1.00 43.56           C  
ATOM     13  CD2 LEU A   2      47.118  50.330   8.147  1.00 41.91           C  
ATOM     14  N   PRO A   3      45.448  45.232   9.024  1.00 46.73           N  
ATOM     15  CA  PRO A   3      44.455  44.250   8.616  1.00 45.78           C  
ATOM     16  C   PRO A   3      43.961  44.634   7.234  1.00 46.63           C  
ATOM     17  O   PRO A   3      43.939  45.825   6.898  1.00 47.34           O  
ATOM     18  CB  PRO A   3      43.403  44.341   9.691  1.00 46.99           C  
ATOM     19  CG  PRO A   3      44.105  44.975  10.878  1.00 44.71           C  
ATOM     20  CD  PRO A   3      45.004  45.979  10.190  1.00 44.42           C  
ATOM     21  N   GLN A   4      43.568  43.676   6.398  1.00 46.47           N  
ATOM     22  CA  GLN A   4      43.029  44.060   5.087  1.00 46.45           C  
ATOM     23  C   GLN A   4      41.693  44.761   5.297  1.00 45.04           C  
ATOM     24  O   GLN A   4      41.393  45.774   4.661  1.00 45.78           O  
ATOM     25  CB  GLN A   4      42.785  42.846   4.192  1.00 46.63           C  
ATOM     26  N   THR A   5      40.909  44.192   6.215  1.00 42.61           N  
ATOM     27  CA  THR A   5      39.653  44.771   6.594  1.00 40.11           C  
ATOM     28  C   THR A   5      39.717  44.816   8.095  1.00 35.37           C  
ATOM     29  O   THR A   5      40.067  43.791   8.671  1.00 35.94           O  
ATOM     30  CB  THR A   5      38.484  43.884   6.138  1.00 43.37           C  
ATOM     31  OG1 THR A   5      38.691  43.602   4.741  1.00 47.16           O  
ATOM     32  CG2 THR A   5      37.113  44.565   6.389  1.00 45.85           C  
ATOM     33  N   VAL A   6      39.468  45.951   8.737  1.00 32.53           N  
ATOM     34  CA  VAL A   6      39.393  46.107  10.193  1.00 29.27           C  
ATOM     35  C   VAL A   6      37.920  45.846  10.630  1.00 28.08           C  
ATOM     36  O   VAL A   6      36.990  46.464  10.072  1.00 24.45           O  
ATOM     37  CB  VAL A   6      39.897  47.581  10.531  1.00 30.89           C  
ATOM     38  CG1 VAL A   6      39.819  47.928  12.011  1.00 28.80           C  
ATOM     39  CG2 VAL A   6      41.390  47.680  10.213  1.00 30.39           C  
ATOM     40  N   ARG A   7      37.656  44.914  11.569  1.00 23.76           N  
ATOM     41  CA  ARG A   7      36.323  44.651  12.059  1.00 22.99           C  
ATOM     42  C   ARG A   7      36.256  45.445  13.334  1.00 20.20           C  
ATOM     43  O   ARG A   7      37.074  45.287  14.226  1.00 21.62           O  
ATOM     44  CB  ARG A   7      36.054  43.177  12.407  1.00 26.36           C  
ATOM     45  CG  ARG A   7      36.116  42.175  11.240  1.00 38.28           C  
ATOM     46  CD  ARG A   7      35.565  40.781  11.633  1.00 47.23           C  
ATOM     47  NE  ARG A   7      34.110  40.616  11.435  1.00 55.32           N  
ATOM     48  CZ  ARG A   7      33.263  40.010  12.321  1.00 60.98           C  
ATOM     49  NH1 ARG A   7      33.642  39.474  13.504  1.00 58.63           N  
ATOM     50  NH2 ARG A   7      31.957  39.910  12.010  1.00 63.43           N  
ATOM     51  N   ILE A   8      35.312  46.338  13.471  1.00 20.96           N  
ATOM     52  CA  ILE A   8      35.204  47.178  14.635  1.00 22.87           C  
ATOM     53  C   ILE A   8      33.926  46.777  15.348  1.00 22.26           C  
ATOM     54  O   ILE A   8      32.866  46.797  14.708  1.00 23.20           O  
ATOM     55  CB  ILE A   8      35.135  48.680  14.204  1.00 22.87           C  
ATOM     56  CG1 ILE A   8      36.277  49.011  13.235  1.00 20.30           C  
ATOM     57  CG2 ILE A   8      35.114  49.516  15.496  1.00 16.27           C  
ATOM     58  CD1 ILE A   8      36.390  50.441  12.691  1.00 26.69           C  
ATOM     59  N   GLY A   9      33.991  46.442  16.631  1.00 19.88           N  
ATOM     60  CA  GLY A   9      32.823  46.073  17.377  1.00 19.68           C  
ATOM     61  C   GLY A   9      32.317  47.315  18.061  1.00 22.33           C  
ATOM     62  O   GLY A   9      33.102  48.150  18.528  1.00 21.18           O  
ATOM     63  N   THR A  10      30.995  47.414  18.136  1.00 22.30           N  
ATOM     64  CA  THR A  10      30.341  48.509  18.821  1.00 24.40           C  
ATOM     65  C   THR A  10      29.031  47.986  19.406  1.00 25.03           C  
ATOM     66  O   THR A  10      28.469  47.013  18.915  1.00 27.09           O  
ATOM     67  CB  THR A  10      30.144  49.663  17.786  1.00 21.31           C  
ATOM     68  OG1 THR A  10      29.779  50.822  18.536  1.00 22.42           O  
ATOM     69  CG2 THR A  10      29.143  49.323  16.709  1.00 20.91           C  
ATOM     70  N   ASP A  11      28.585  48.544  20.515  1.00 25.18           N  
ATOM     71  CA  ASP A  11      27.295  48.270  21.084  1.00 24.50           C  
ATOM     72  C   ASP A  11      26.339  49.337  20.574  1.00 24.99           C  
ATOM     73  O   ASP A  11      26.381  50.481  21.053  1.00 24.16           O  
ATOM     74  CB  ASP A  11      27.398  48.334  22.599  1.00 26.75           C  
ATOM     75  CG  ASP A  11      26.135  47.908  23.337  1.00 32.19           C  
ATOM     76  OD1 ASP A  11      25.054  47.833  22.743  1.00 40.44           O  
ATOM     77  OD2 ASP A  11      26.222  47.644  24.528  1.00 35.65           O  
ATOM     78  N   THR A  12      25.357  48.982  19.747  1.00 27.78           N  
ATOM     79  CA  THR A  12      24.471  49.998  19.169  1.00 27.66           C  
ATOM     80  C   THR A  12      23.257  50.446  19.998  1.00 25.82           C  
ATOM     81  O   THR A  12      22.179  50.779  19.515  1.00 25.56           O  
ATOM     82  CB  THR A  12      24.025  49.491  17.779  1.00 29.46           C  
ATOM     83  OG1 THR A  12      23.332  48.262  17.935  1.00 30.47           O  
ATOM     84  CG2 THR A  12      25.224  49.323  16.868  1.00 28.48           C  
ATOM     85  N   THR A  13      23.372  50.454  21.297  1.00 25.10           N  
ATOM     86  CA  THR A  13      22.276  50.871  22.099  1.00 26.54           C  
ATOM     87  C   THR A  13      22.679  52.159  22.793  1.00 29.29           C  
ATOM     88  O   THR A  13      22.255  52.337  23.940  1.00 30.00           O  
ATOM     89  CB  THR A  13      21.982  49.740  23.091  1.00 27.43           C  
ATOM     90  OG1 THR A  13      23.088  49.548  23.976  1.00 29.45           O  
ATOM     91  CG2 THR A  13      21.676  48.482  22.323  1.00 28.72           C  
ATOM     92  N   TYR A  14      23.525  53.036  22.221  1.00 31.38           N  
ATOM     93  CA  TYR A  14      23.948  54.240  22.921  1.00 32.43           C  
ATOM     94  C   TYR A  14      23.982  55.502  22.064  1.00 30.15           C  
ATOM     95  O   TYR A  14      25.033  56.076  21.740  1.00 27.41           O  
ATOM     96  CB  TYR A  14      25.330  54.040  23.552  1.00 38.74           C  
ATOM     97  CG  TYR A  14      25.618  55.130  24.591  1.00 49.54           C  
ATOM     98  CD1 TYR A  14      24.592  55.621  25.389  1.00 54.90           C  
ATOM     99  CD2 TYR A  14      26.887  55.643  24.757  1.00 51.65           C  
ATOM    100  CE1 TYR A  14      24.815  56.595  26.337  1.00 60.34           C  
ATOM    101  CE2 TYR A  14      27.123  56.620  25.709  1.00 58.41           C  
ATOM    102  CZ  TYR A  14      26.089  57.090  26.494  1.00 62.02           C  
ATOM    103  OH  TYR A  14      26.315  58.058  27.469  1.00 67.66           O  
ATOM    104  N   ALA A  15      22.795  55.971  21.688  1.00 27.28           N  
ATOM    105  CA  ALA A  15      22.695  57.227  20.989  1.00 28.02           C  
ATOM    106  C   ALA A  15      23.226  58.278  21.957  1.00 27.58           C  
ATOM    107  O   ALA A  15      23.183  58.065  23.171  1.00 29.46           O  
ATOM    108  CB  ALA A  15      21.258  57.510  20.667  1.00 29.77           C  
ATOM    109  N   PRO A  16      23.850  59.369  21.533  1.00 28.98           N  
ATOM    110  CA  PRO A  16      24.140  59.693  20.144  1.00 27.18           C  
ATOM    111  C   PRO A  16      25.448  59.112  19.606  1.00 24.48           C  
ATOM    112  O   PRO A  16      25.915  59.544  18.540  1.00 23.71           O  
ATOM    113  CB  PRO A  16      24.090  61.207  20.176  1.00 28.19           C  
ATOM    114  CG  PRO A  16      24.818  61.508  21.465  1.00 25.75           C  
ATOM    115  CD  PRO A  16      24.188  60.497  22.406  1.00 26.61           C  
ATOM    116  N   PHE A  17      26.082  58.193  20.347  1.00 22.73           N  
ATOM    117  CA  PHE A  17      27.356  57.640  19.911  1.00 23.93           C  
ATOM    118  C   PHE A  17      27.218  56.447  18.970  1.00 24.39           C  
ATOM    119  O   PHE A  17      27.823  56.461  17.890  1.00 22.15           O  
ATOM    120  CB  PHE A  17      28.177  57.248  21.124  1.00 23.16           C  
ATOM    121  CG  PHE A  17      28.417  58.454  21.995  1.00 26.16           C  
ATOM    122  CD1 PHE A  17      29.240  59.478  21.539  1.00 27.18           C  
ATOM    123  CD2 PHE A  17      27.821  58.516  23.240  1.00 24.91           C  
ATOM    124  CE1 PHE A  17      29.459  60.574  22.365  1.00 26.46           C  
ATOM    125  CE2 PHE A  17      28.042  59.607  24.059  1.00 27.30           C  
ATOM    126  CZ  PHE A  17      28.865  60.632  23.623  1.00 26.28           C  
ATOM    127  N   SER A  18      26.386  55.454  19.282  1.00 24.94           N  
ATOM    128  CA  SER A  18      26.237  54.299  18.425  1.00 24.18           C  
ATOM    129  C   SER A  18      24.802  53.842  18.523  1.00 22.29           C  
ATOM    130  O   SER A  18      24.347  53.532  19.617  1.00 23.79           O  
ATOM    131  CB  SER A  18      27.149  53.172  18.894  1.00 24.21           C  
ATOM    132  OG  SER A  18      27.106  52.129  17.936  1.00 23.83           O  
ATOM    133  N   SER A  19      24.104  53.765  17.417  1.00 24.29           N  
ATOM    134  CA  SER A  19      22.728  53.318  17.344  1.00 28.24           C  
ATOM    135  C   SER A  19      22.502  52.769  15.942  1.00 28.39           C  
ATOM    136  O   SER A  19      23.403  52.798  15.088  1.00 32.39           O  
ATOM    137  CB  SER A  19      21.768  54.477  17.557  1.00 26.55           C  
ATOM    138  OG  SER A  19      21.200  54.164  18.799  1.00 43.12           O  
ATOM    139  N   LYS A  20      21.282  52.295  15.683  1.00 29.46           N  
ATOM    140  CA  LYS A  20      20.855  51.849  14.383  1.00 30.56           C  
ATOM    141  C   LYS A  20      19.678  52.705  13.993  1.00 29.98           C  
ATOM    142  O   LYS A  20      18.898  53.186  14.824  1.00 28.18           O  
ATOM    143  CB  LYS A  20      20.443  50.427  14.445  1.00 34.46           C  
ATOM    144  CG  LYS A  20      21.491  49.702  13.683  1.00 38.60           C  
ATOM    145  CD  LYS A  20      22.086  48.679  14.595  1.00 44.32           C  
ATOM    146  CE  LYS A  20      23.098  47.934  13.734  1.00 48.46           C  
ATOM    147  NZ  LYS A  20      22.465  47.171  12.674  1.00 53.59           N  
ATOM    148  N   ASP A  21      19.637  53.025  12.720  1.00 30.02           N  
ATOM    149  CA  ASP A  21      18.525  53.813  12.242  1.00 33.49           C  
ATOM    150  C   ASP A  21      17.416  52.904  11.690  1.00 34.06           C  
ATOM    151  O   ASP A  21      17.542  51.676  11.704  1.00 32.45           O  
ATOM    152  CB  ASP A  21      19.043  54.780  11.179  1.00 32.36           C  
ATOM    153  CG  ASP A  21      19.485  54.197   9.844  1.00 34.45           C  
ATOM    154  OD1 ASP A  21      19.440  52.982   9.632  1.00 32.16           O  
ATOM    155  OD2 ASP A  21      19.876  55.000   8.997  1.00 38.00           O  
ATOM    156  N   ALA A  22      16.388  53.484  11.067  1.00 33.73           N  
ATOM    157  CA  ALA A  22      15.284  52.706  10.539  1.00 34.60           C  
ATOM    158  C   ALA A  22      15.720  51.762   9.435  1.00 36.66           C  
ATOM    159  O   ALA A  22      15.121  50.709   9.267  1.00 39.74           O  
ATOM    160  CB  ALA A  22      14.227  53.644  10.014  1.00 33.09           C  
ATOM    161  N   LYS A  23      16.794  52.051   8.698  1.00 37.50           N  
ATOM    162  CA  LYS A  23      17.296  51.111   7.700  1.00 39.55           C  
ATOM    163  C   LYS A  23      18.187  50.050   8.331  1.00 37.92           C  
ATOM    164  O   LYS A  23      18.575  49.156   7.603  1.00 39.91           O  
ATOM    165  CB  LYS A  23      18.173  51.744   6.636  1.00 44.15           C  
ATOM    166  CG  LYS A  23      17.812  53.137   6.230  1.00 54.74           C  
ATOM    167  CD  LYS A  23      16.474  53.201   5.517  1.00 62.79           C  
ATOM    168  CE  LYS A  23      16.203  54.669   5.222  1.00 69.26           C  
ATOM    169  NZ  LYS A  23      17.248  55.284   4.401  1.00 72.68           N  
ATOM    170  N   GLY A  24      18.525  50.010   9.620  1.00 35.86           N  
ATOM    171  CA  GLY A  24      19.528  49.072  10.118  1.00 34.95           C  
ATOM    172  C   GLY A  24      20.985  49.601   9.967  1.00 34.55           C  
ATOM    173  O   GLY A  24      21.930  48.931  10.388  1.00 34.78           O  
ATOM    174  N   GLU A  25      21.256  50.755   9.339  1.00 32.10           N  
ATOM    175  CA  GLU A  25      22.585  51.339   9.308  1.00 31.38           C  
ATOM    176  C   GLU A  25      23.004  51.740  10.713  1.00 29.23           C  
ATOM    177  O   GLU A  25      22.171  52.113  11.549  1.00 29.37           O  
ATOM    178  CB  GLU A  25      22.650  52.605   8.497  1.00 38.44           C  
ATOM    179  CG  GLU A  25      21.879  52.702   7.191  1.00 50.92           C  
ATOM    180  CD  GLU A  25      22.316  51.820   6.032  1.00 59.37           C  
ATOM    181  OE1 GLU A  25      23.371  51.175   6.108  1.00 65.27           O  
ATOM    182  OE2 GLU A  25      21.581  51.802   5.040  1.00 63.56           O  
ATOM    183  N   PHE A  26      24.309  51.695  10.983  1.00 26.77           N  
ATOM    184  CA  PHE A  26      24.902  52.136  12.249  1.00 25.24           C  
ATOM    185  C   PHE A  26      25.002  53.652  12.123  1.00 24.05           C  
ATOM    186  O   PHE A  26      25.452  54.178  11.094  1.00 23.24           O  
ATOM    187  CB  PHE A  26      26.320  51.606  12.431  1.00 25.15           C  
ATOM    188  CG  PHE A  26      26.410  50.119  12.657  1.00 27.52           C  
ATOM    189  CD1 PHE A  26      26.182  49.242  11.616  1.00 31.09           C  
ATOM    190  CD2 PHE A  26      26.699  49.662  13.904  1.00 26.17           C  
ATOM    191  CE1 PHE A  26      26.242  47.900  11.850  1.00 27.74           C  
ATOM    192  CE2 PHE A  26      26.757  48.312  14.121  1.00 27.63           C  
ATOM    193  CZ  PHE A  26      26.523  47.435  13.101  1.00 25.00           C  
ATOM    194  N   ILE A  27      24.656  54.405  13.124  1.00 21.75           N  
ATOM    195  CA  ILE A  27      24.701  55.846  13.010  1.00 22.54           C  
ATOM    196  C   ILE A  27      25.236  56.355  14.333  1.00 24.64           C  
ATOM    197  O   ILE A  27      25.068  55.683  15.374  1.00 24.41           O  
ATOM    198  CB  ILE A  27      23.266  56.428  12.749  1.00 23.21           C  
ATOM    199  CG1 ILE A  27      22.280  55.771  13.703  1.00 29.36           C  
ATOM    200  CG2 ILE A  27      22.846  56.196  11.302  1.00 24.94           C  
ATOM    201  CD1 ILE A  27      21.002  56.564  13.961  1.00 29.88           C  
ATOM    202  N   GLY A  28      25.826  57.556  14.354  1.00 24.72           N  
ATOM    203  CA  GLY A  28      26.222  58.132  15.630  1.00 23.44           C  
ATOM    204  C   GLY A  28      27.620  58.662  15.554  1.00 21.98           C  
ATOM    205  O   GLY A  28      28.385  58.371  14.619  1.00 23.10           O  
ATOM    206  N   PHE A  29      27.987  59.399  16.576  1.00 22.24           N  
ATOM    207  CA  PHE A  29      29.292  60.080  16.595  1.00 23.61           C  
ATOM    208  C   PHE A  29      30.478  59.108  16.561  1.00 21.23           C  
ATOM    209  O   PHE A  29      31.403  59.333  15.790  1.00 21.92           O  
ATOM    210  CB  PHE A  29      29.381  61.006  17.847  1.00 24.27           C  
ATOM    211  CG  PHE A  29      30.568  61.958  17.771  1.00 23.12           C  
ATOM    212  CD1 PHE A  29      30.798  62.667  16.600  1.00 22.78           C  
ATOM    213  CD2 PHE A  29      31.404  62.103  18.869  1.00 27.41           C  
ATOM    214  CE1 PHE A  29      31.869  63.522  16.516  1.00 21.57           C  
ATOM    215  CE2 PHE A  29      32.483  62.978  18.773  1.00 26.99           C  
ATOM    216  CZ  PHE A  29      32.709  63.681  17.604  1.00 23.76           C  
ATOM    217  N   ASP A  30      30.473  58.013  17.312  1.00 18.81           N  
ATOM    218  CA  ASP A  30      31.505  56.992  17.229  1.00 19.33           C  
ATOM    219  C   ASP A  30      31.635  56.414  15.832  1.00 18.92           C  
ATOM    220  O   ASP A  30      32.734  56.130  15.340  1.00 18.08           O  
ATOM    221  CB  ASP A  30      31.184  55.846  18.157  1.00 20.25           C  
ATOM    222  CG  ASP A  30      31.614  56.074  19.577  1.00 24.54           C  
ATOM    223  OD1 ASP A  30      32.154  57.126  19.886  1.00 24.55           O  
ATOM    224  OD2 ASP A  30      31.421  55.172  20.383  1.00 27.40           O  
ATOM    225  N   ILE A  31      30.489  56.265  15.156  1.00 21.22           N  
ATOM    226  CA  ILE A  31      30.444  55.689  13.814  1.00 23.29           C  
ATOM    227  C   ILE A  31      31.051  56.691  12.842  1.00 23.07           C  
ATOM    228  O   ILE A  31      31.811  56.313  11.948  1.00 22.53           O  
ATOM    229  CB  ILE A  31      28.959  55.336  13.373  1.00 22.95           C  
ATOM    230  CG1 ILE A  31      28.252  54.488  14.449  1.00 22.68           C  
ATOM    231  CG2 ILE A  31      28.988  54.664  11.991  1.00 21.73           C  
ATOM    232  CD1 ILE A  31      28.902  53.175  14.922  1.00 23.55           C  
ATOM    233  N   ASP A  32      30.753  57.982  13.024  1.00 22.79           N  
ATOM    234  CA  ASP A  32      31.297  59.003  12.137  1.00 23.95           C  
ATOM    235  C   ASP A  32      32.788  59.102  12.276  1.00 24.22           C  
ATOM    236  O   ASP A  32      33.483  59.006  11.265  1.00 25.49           O  
ATOM    237  CB  ASP A  32      30.690  60.355  12.434  1.00 23.66           C  
ATOM    238  CG  ASP A  32      29.217  60.406  12.043  1.00 25.99           C  
ATOM    239  OD1 ASP A  32      28.765  59.721  11.118  1.00 25.39           O  
ATOM    240  OD2 ASP A  32      28.513  61.146  12.710  1.00 27.51           O  
ATOM    241  N   LEU A  33      33.255  59.228  13.515  1.00 23.55           N  
ATOM    242  CA  LEU A  33      34.674  59.198  13.862  1.00 24.21           C  
ATOM    243  C   LEU A  33      35.360  57.948  13.285  1.00 23.80           C  
ATOM    244  O   LEU A  33      36.374  58.018  12.583  1.00 24.95           O  
ATOM    245  CB  LEU A  33      34.741  59.223  15.365  1.00 21.18           C  
ATOM    246  CG  LEU A  33      35.372  60.353  16.163  1.00 27.23           C  
ATOM    247  CD1 LEU A  33      35.374  61.688  15.445  1.00 25.15           C  
ATOM    248  CD2 LEU A  33      34.600  60.396  17.466  1.00 24.00           C  
ATOM    249  N   GLY A  34      34.772  56.772  13.503  1.00 25.04           N  
ATOM    250  CA  GLY A  34      35.295  55.504  13.010  1.00 22.57           C  
ATOM    251  C   GLY A  34      35.419  55.458  11.513  1.00 22.51           C  
ATOM    252  O   GLY A  34      36.499  55.162  10.999  1.00 23.63           O  
ATOM    253  N   ASN A  35      34.375  55.818  10.785  1.00 21.42           N  
ATOM    254  CA  ASN A  35      34.407  55.793   9.342  1.00 23.24           C  
ATOM    255  C   ASN A  35      35.364  56.769   8.727  1.00 23.83           C  
ATOM    256  O   ASN A  35      36.025  56.435   7.742  1.00 27.57           O  
ATOM    257  CB  ASN A  35      33.059  56.085   8.769  1.00 27.69           C  
ATOM    258  CG  ASN A  35      32.077  54.927   8.852  1.00 31.66           C  
ATOM    259  OD1 ASN A  35      30.886  55.163   9.046  1.00 35.87           O  
ATOM    260  ND2 ASN A  35      32.465  53.655   8.720  1.00 31.42           N  
ATOM    261  N   GLU A  36      35.449  57.960   9.287  1.00 24.43           N  
ATOM    262  CA  GLU A  36      36.400  58.960   8.841  1.00 26.49           C  
ATOM    263  C   GLU A  36      37.847  58.477   9.044  1.00 26.24           C  
ATOM    264  O   GLU A  36      38.651  58.425   8.103  1.00 25.04           O  
ATOM    265  CB  GLU A  36      36.109  60.232   9.622  1.00 27.33           C  
ATOM    266  CG  GLU A  36      36.847  61.475   9.157  1.00 35.47           C  
ATOM    267  CD  GLU A  36      36.561  61.908   7.733  1.00 39.42           C  
ATOM    268  OE1 GLU A  36      35.432  61.729   7.255  1.00 44.95           O  
ATOM    269  OE2 GLU A  36      37.484  62.420   7.104  1.00 41.57           O  
ATOM    270  N   MET A  37      38.196  57.988  10.242  1.00 25.89           N  
ATOM    271  CA  MET A  37      39.523  57.425  10.466  1.00 25.46           C  
ATOM    272  C   MET A  37      39.774  56.306   9.467  1.00 26.94           C  
ATOM    273  O   MET A  37      40.802  56.372   8.794  1.00 28.87           O  
ATOM    274  CB  MET A  37      39.689  56.863  11.861  1.00 22.39           C  
ATOM    275  CG  MET A  37      39.723  57.993  12.859  1.00 21.06           C  
ATOM    276  SD  MET A  37      40.057  57.515  14.554  1.00 25.42           S  
ATOM    277  CE  MET A  37      38.600  56.655  15.053  1.00 24.61           C  
ATOM    278  N   CYS A  38      38.906  55.338   9.198  1.00 27.09           N  
ATOM    279  CA  CYS A  38      39.184  54.297   8.195  1.00 27.94           C  
ATOM    280  C   CYS A  38      39.472  54.852   6.827  1.00 29.04           C  
ATOM    281  O   CYS A  38      40.367  54.354   6.139  1.00 28.15           O  
ATOM    282  CB  CYS A  38      38.029  53.355   8.054  1.00 24.84           C  
ATOM    283  SG  CYS A  38      37.723  52.651   9.686  1.00 29.17           S  
ATOM    284  N   LYS A  39      38.780  55.937   6.485  1.00 31.00           N  
ATOM    285  CA  LYS A  39      38.967  56.650   5.229  1.00 32.46           C  
ATOM    286  C   LYS A  39      40.391  57.169   5.142  1.00 30.54           C  
ATOM    287  O   LYS A  39      41.106  56.889   4.193  1.00 32.08           O  
ATOM    288  CB  LYS A  39      38.034  57.821   5.169  1.00 34.80           C  
ATOM    289  CG  LYS A  39      37.652  58.160   3.774  1.00 41.17           C  
ATOM    290  CD  LYS A  39      37.358  59.648   3.746  1.00 51.23           C  
ATOM    291  CE  LYS A  39      37.053  60.051   2.302  1.00 59.45           C  
ATOM    292  NZ  LYS A  39      38.075  59.565   1.367  1.00 65.90           N  
ATOM    293  N   ARG A  40      40.861  57.894   6.144  1.00 30.78           N  
ATOM    294  CA  ARG A  40      42.207  58.442   6.151  1.00 32.21           C  
ATOM    295  C   ARG A  40      43.284  57.342   6.231  1.00 34.71           C  
ATOM    296  O   ARG A  40      44.386  57.458   5.674  1.00 36.23           O  
ATOM    297  CB  ARG A  40      42.373  59.349   7.328  1.00 32.40           C  
ATOM    298  CG  ARG A  40      41.238  60.284   7.596  1.00 36.74           C  
ATOM    299  CD  ARG A  40      41.468  61.560   6.886  1.00 42.88           C  
ATOM    300  NE  ARG A  40      40.402  62.508   7.176  1.00 45.63           N  
ATOM    301  CZ  ARG A  40      40.643  63.773   7.493  1.00 46.14           C  
ATOM    302  NH1 ARG A  40      41.889  64.256   7.585  1.00 47.38           N  
ATOM    303  NH2 ARG A  40      39.599  64.583   7.645  1.00 48.62           N  
ATOM    304  N   MET A  41      42.995  56.241   6.936  1.00 32.89           N  
ATOM    305  CA  MET A  41      43.885  55.106   7.060  1.00 30.91           C  
ATOM    306  C   MET A  41      43.968  54.359   5.772  1.00 32.59           C  
ATOM    307  O   MET A  41      44.935  53.642   5.576  1.00 34.20           O  
ATOM    308  CB  MET A  41      43.404  54.115   8.071  1.00 29.39           C  
ATOM    309  CG  MET A  41      43.586  54.664   9.458  1.00 31.26           C  
ATOM    310  SD  MET A  41      42.516  53.823  10.632  1.00 33.20           S  
ATOM    311  CE  MET A  41      43.076  52.163  10.379  1.00 32.35           C  
ATOM    312  N   GLN A  42      42.942  54.486   4.933  1.00 33.45           N  
ATOM    313  CA  GLN A  42      42.806  53.806   3.670  1.00 34.53           C  
ATOM    314  C   GLN A  42      42.668  52.294   3.828  1.00 35.33           C  
ATOM    315  O   GLN A  42      43.273  51.501   3.111  1.00 37.36           O  
ATOM    316  CB  GLN A  42      43.994  54.180   2.792  1.00 38.86           C  
ATOM    317  CG  GLN A  42      44.012  55.683   2.613  1.00 48.09           C  
ATOM    318  CD  GLN A  42      45.172  56.177   1.784  1.00 55.00           C  
ATOM    319  OE1 GLN A  42      45.265  55.900   0.589  1.00 60.30           O  
ATOM    320  NE2 GLN A  42      46.102  56.938   2.337  1.00 60.62           N  
ATOM    321  N   VAL A  43      41.800  51.855   4.735  1.00 34.35           N  
ATOM    322  CA  VAL A  43      41.490  50.443   4.943  1.00 35.59           C  
ATOM    323  C   VAL A  43      39.980  50.290   4.821  1.00 34.54           C  
ATOM    324  O   VAL A  43      39.236  51.268   4.845  1.00 36.23           O  
ATOM    325  CB  VAL A  43      41.842  49.867   6.362  1.00 35.67           C  
ATOM    326  CG1 VAL A  43      43.338  49.808   6.564  1.00 39.89           C  
ATOM    327  CG2 VAL A  43      41.238  50.735   7.455  1.00 37.58           C  
ATOM    328  N   LYS A  44      39.502  49.053   4.725  1.00 34.98           N  
ATOM    329  CA  LYS A  44      38.089  48.752   4.731  1.00 33.40           C  
ATOM    330  C   LYS A  44      37.802  48.393   6.171  1.00 33.73           C  
ATOM    331  O   LYS A  44      38.544  47.602   6.748  1.00 33.61           O  
ATOM    332  CB  LYS A  44      37.737  47.528   3.904  1.00 35.05           C  
ATOM    333  N   CYS A  45      36.756  48.964   6.765  1.00 33.53           N  
ATOM    334  CA  CYS A  45      36.335  48.687   8.133  1.00 32.20           C  
ATOM    335  C   CYS A  45      34.963  48.076   8.096  1.00 32.24           C  
ATOM    336  O   CYS A  45      34.186  48.370   7.181  1.00 34.66           O  
ATOM    337  CB  CYS A  45      36.264  49.945   8.926  1.00 32.25           C  
ATOM    338  SG  CYS A  45      37.998  50.445   9.074  1.00 31.91           S  
ATOM    339  N   THR A  46      34.624  47.188   8.991  1.00 28.56           N  
ATOM    340  CA  THR A  46      33.305  46.642   8.963  1.00 29.49           C  
ATOM    341  C   THR A  46      32.851  46.777  10.386  1.00 29.26           C  
ATOM    342  O   THR A  46      33.652  46.510  11.264  1.00 30.59           O  
ATOM    343  CB  THR A  46      33.403  45.197   8.503  1.00 28.25           C  
ATOM    344  OG1 THR A  46      33.690  45.267   7.113  1.00 33.86           O  
ATOM    345  CG2 THR A  46      32.128  44.426   8.679  1.00 30.66           C  
ATOM    346  N   TRP A  47      31.617  47.218  10.616  1.00 28.75           N  
ATOM    347  CA  TRP A  47      31.031  47.339  11.931  1.00 26.78           C  
ATOM    348  C   TRP A  47      30.256  46.072  12.300  1.00 27.68           C  
ATOM    349  O   TRP A  47      29.485  45.499  11.511  1.00 25.38           O  
ATOM    350  CB  TRP A  47      30.145  48.540  11.900  1.00 24.94           C  
ATOM    351  CG  TRP A  47      30.946  49.829  11.757  1.00 24.82           C  
ATOM    352  CD1 TRP A  47      31.060  50.435  10.545  1.00 25.50           C  
ATOM    353  CD2 TRP A  47      31.513  50.558  12.760  1.00 23.52           C  
ATOM    354  NE1 TRP A  47      31.691  51.558  10.773  1.00 26.59           N  
ATOM    355  CE2 TRP A  47      31.976  51.658  12.075  1.00 25.29           C  
ATOM    356  CE3 TRP A  47      31.707  50.462  14.098  1.00 26.07           C  
ATOM    357  CZ2 TRP A  47      32.614  52.715  12.674  1.00 23.02           C  
ATOM    358  CZ3 TRP A  47      32.345  51.518  14.709  1.00 28.11           C  
ATOM    359  CH2 TRP A  47      32.793  52.631  14.012  1.00 22.83           C  
ATOM    360  N   VAL A  48      30.549  45.632  13.520  1.00 27.45           N  
ATOM    361  CA  VAL A  48      30.024  44.411  14.078  1.00 25.37           C  
ATOM    362  C   VAL A  48      29.273  44.823  15.335  1.00 25.45           C  
ATOM    363  O   VAL A  48      29.848  45.292  16.319  1.00 25.44           O  
ATOM    364  CB  VAL A  48      31.200  43.441  14.424  1.00 26.35           C  
ATOM    365  CG1 VAL A  48      30.614  42.138  14.905  1.00 28.88           C  
ATOM    366  CG2 VAL A  48      32.089  43.155  13.231  1.00 22.81           C  
ATOM    367  N   ALA A  49      27.949  44.719  15.342  1.00 26.91           N  
ATOM    368  CA  ALA A  49      27.178  44.960  16.554  1.00 27.12           C  
ATOM    369  C   ALA A  49      27.418  43.895  17.598  1.00 27.72           C  
ATOM    370  O   ALA A  49      27.462  42.695  17.318  1.00 31.78           O  
ATOM    371  CB  ALA A  49      25.683  45.000  16.252  1.00 28.27           C  
ATOM    372  N   SER A  50      27.598  44.328  18.812  1.00 27.89           N  
ATOM    373  CA  SER A  50      27.864  43.427  19.887  1.00 31.54           C  
ATOM    374  C   SER A  50      27.416  44.039  21.194  1.00 30.55           C  
ATOM    375  O   SER A  50      27.288  45.248  21.339  1.00 30.91           O  
ATOM    376  CB  SER A  50      29.365  43.117  19.919  1.00 31.30           C  
ATOM    377  OG  SER A  50      29.702  42.434  21.130  1.00 35.38           O  
ATOM    378  N   ASP A  51      27.146  43.184  22.161  1.00 30.27           N  
ATOM    379  CA  ASP A  51      26.914  43.632  23.493  1.00 34.29           C  
ATOM    380  C   ASP A  51      28.228  44.129  24.073  1.00 33.92           C  
ATOM    381  O   ASP A  51      29.293  43.542  23.882  1.00 35.49           O  
ATOM    382  CB  ASP A  51      26.354  42.473  24.316  1.00 44.83           C  
ATOM    383  CG  ASP A  51      24.947  42.030  23.873  1.00 55.36           C  
ATOM    384  OD1 ASP A  51      24.130  42.860  23.415  1.00 60.32           O  
ATOM    385  OD2 ASP A  51      24.668  40.833  23.996  1.00 60.90           O  
ATOM    386  N   PHE A  52      28.158  45.194  24.846  1.00 31.12           N  
ATOM    387  CA  PHE A  52      29.296  45.833  25.434  1.00 30.64           C  
ATOM    388  C   PHE A  52      30.158  44.914  26.233  1.00 31.68           C  
ATOM    389  O   PHE A  52      31.372  45.029  26.157  1.00 33.14           O  
ATOM    390  CB  PHE A  52      28.873  46.951  26.353  1.00 30.75           C  
ATOM    391  CG  PHE A  52      30.013  47.882  26.684  1.00 28.39           C  
ATOM    392  CD1 PHE A  52      30.305  48.913  25.826  1.00 30.94           C  
ATOM    393  CD2 PHE A  52      30.740  47.696  27.832  1.00 31.36           C  
ATOM    394  CE1 PHE A  52      31.337  49.778  26.116  1.00 34.23           C  
ATOM    395  CE2 PHE A  52      31.775  48.563  28.117  1.00 36.40           C  
ATOM    396  CZ  PHE A  52      32.071  49.604  27.261  1.00 33.73           C  
ATOM    397  N   ASP A  53      29.588  44.032  27.035  1.00 35.06           N  
ATOM    398  CA  ASP A  53      30.415  43.124  27.823  1.00 38.09           C  
ATOM    399  C   ASP A  53      31.195  42.050  27.053  1.00 35.30           C  
ATOM    400  O   ASP A  53      32.166  41.494  27.576  1.00 36.86           O  
ATOM    401  CB  ASP A  53      29.522  42.475  28.886  1.00 46.64           C  
ATOM    402  CG  ASP A  53      28.915  43.505  29.848  1.00 56.76           C  
ATOM    403  OD1 ASP A  53      29.571  44.494  30.231  1.00 58.46           O  
ATOM    404  OD2 ASP A  53      27.751  43.304  30.199  1.00 63.95           O  
ATOM    405  N   ALA A  54      30.821  41.816  25.794  1.00 29.90           N  
ATOM    406  CA  ALA A  54      31.481  40.869  24.920  1.00 26.94           C  
ATOM    407  C   ALA A  54      32.584  41.509  24.102  1.00 25.31           C  
ATOM    408  O   ALA A  54      33.372  40.854  23.427  1.00 24.11           O  
ATOM    409  CB  ALA A  54      30.489  40.312  23.962  1.00 26.03           C  
ATOM    410  N   LEU A  55      32.683  42.818  24.116  1.00 25.30           N  
ATOM    411  CA  LEU A  55      33.606  43.508  23.247  1.00 24.52           C  
ATOM    412  C   LEU A  55      35.070  43.237  23.568  1.00 24.35           C  
ATOM    413  O   LEU A  55      35.787  42.802  22.667  1.00 25.65           O  
ATOM    414  CB  LEU A  55      33.315  45.005  23.317  1.00 23.85           C  
ATOM    415  CG  LEU A  55      32.058  45.529  22.646  1.00 23.17           C  
ATOM    416  CD1 LEU A  55      31.862  47.001  23.007  1.00 24.98           C  
ATOM    417  CD2 LEU A  55      32.161  45.316  21.172  1.00 20.18           C  
ATOM    418  N   ILE A  56      35.568  43.439  24.782  1.00 23.52           N  
ATOM    419  CA  ILE A  56      36.967  43.136  25.067  1.00 28.70           C  
ATOM    420  C   ILE A  56      37.262  41.615  24.914  1.00 29.66           C  
ATOM    421  O   ILE A  56      38.305  41.271  24.327  1.00 29.66           O  
ATOM    422  CB  ILE A  56      37.335  43.667  26.506  1.00 26.92           C  
ATOM    423  CG1 ILE A  56      37.268  45.196  26.456  1.00 28.12           C  
ATOM    424  CG2 ILE A  56      38.741  43.195  26.972  1.00 28.91           C  
ATOM    425  CD1 ILE A  56      37.693  45.929  27.749  1.00 29.58           C  
ATOM    426  N   PRO A  57      36.403  40.669  25.339  1.00 30.13           N  
ATOM    427  CA  PRO A  57      36.528  39.242  24.990  1.00 29.99           C  
ATOM    428  C   PRO A  57      36.675  38.980  23.492  1.00 28.52           C  
ATOM    429  O   PRO A  57      37.614  38.302  23.034  1.00 27.94           O  
ATOM    430  CB  PRO A  57      35.293  38.632  25.612  1.00 27.55           C  
ATOM    431  CG  PRO A  57      35.199  39.401  26.908  1.00 26.27           C  
ATOM    432  CD  PRO A  57      35.392  40.823  26.400  1.00 29.59           C  
ATOM    433  N   SER A  58      35.812  39.603  22.694  1.00 27.40           N  
ATOM    434  CA  SER A  58      35.905  39.444  21.267  1.00 26.97           C  
ATOM    435  C   SER A  58      37.189  40.007  20.684  1.00 24.86           C  
ATOM    436  O   SER A  58      37.716  39.469  19.704  1.00 25.44           O  
ATOM    437  CB  SER A  58      34.729  40.106  20.612  1.00 28.82           C  
ATOM    438  OG  SER A  58      33.578  39.424  21.064  1.00 37.68           O  
ATOM    439  N   LEU A  59      37.700  41.090  21.257  1.00 23.94           N  
ATOM    440  CA  LEU A  59      38.946  41.704  20.803  1.00 25.37           C  
ATOM    441  C   LEU A  59      40.131  40.769  21.069  1.00 21.64           C  
ATOM    442  O   LEU A  59      40.943  40.483  20.197  1.00 21.96           O  
ATOM    443  CB  LEU A  59      39.189  43.067  21.542  1.00 22.72           C  
ATOM    444  CG  LEU A  59      40.411  43.898  21.113  1.00 20.13           C  
ATOM    445  CD1 LEU A  59      40.255  44.310  19.654  1.00 15.78           C  
ATOM    446  CD2 LEU A  59      40.565  45.078  22.030  1.00 17.14           C  
ATOM    447  N   LYS A  60      40.179  40.295  22.302  1.00 21.74           N  
ATOM    448  CA  LYS A  60      41.250  39.422  22.739  1.00 25.85           C  
ATOM    449  C   LYS A  60      41.269  38.108  21.965  1.00 27.03           C  
ATOM    450  O   LYS A  60      42.338  37.589  21.634  1.00 27.94           O  
ATOM    451  CB  LYS A  60      41.076  39.198  24.212  1.00 25.47           C  
ATOM    452  CG  LYS A  60      41.257  40.568  24.842  1.00 32.80           C  
ATOM    453  CD  LYS A  60      41.879  40.565  26.204  1.00 37.72           C  
ATOM    454  CE  LYS A  60      40.958  40.221  27.360  1.00 44.08           C  
ATOM    455  NZ  LYS A  60      41.764  40.232  28.576  1.00 48.70           N  
ATOM    456  N   ALA A  61      40.092  37.617  21.577  1.00 24.76           N  
ATOM    457  CA  ALA A  61      39.921  36.383  20.836  1.00 23.52           C  
ATOM    458  C   ALA A  61      40.161  36.522  19.356  1.00 24.61           C  
ATOM    459  O   ALA A  61      40.219  35.537  18.638  1.00 25.71           O  
ATOM    460  CB  ALA A  61      38.514  35.891  21.049  1.00 22.26           C  
ATOM    461  N   LYS A  62      40.292  37.773  18.887  1.00 26.01           N  
ATOM    462  CA  LYS A  62      40.510  38.231  17.507  1.00 24.30           C  
ATOM    463  C   LYS A  62      39.305  38.043  16.619  1.00 22.36           C  
ATOM    464  O   LYS A  62      39.389  37.960  15.386  1.00 23.21           O  
ATOM    465  CB  LYS A  62      41.742  37.542  16.849  1.00 24.82           C  
ATOM    466  CG  LYS A  62      43.001  37.653  17.699  1.00 21.61           C  
ATOM    467  CD  LYS A  62      44.204  37.361  16.864  1.00 24.37           C  
ATOM    468  CE  LYS A  62      45.375  37.589  17.775  1.00 27.28           C  
ATOM    469  NZ  LYS A  62      46.602  37.470  17.007  1.00 28.70           N  
ATOM    470  N   LYS A  63      38.137  38.061  17.265  1.00 23.17           N  
ATOM    471  CA  LYS A  63      36.875  38.091  16.529  1.00 25.14           C  
ATOM    472  C   LYS A  63      36.682  39.475  15.888  1.00 24.80           C  
ATOM    473  O   LYS A  63      36.146  39.589  14.791  1.00 24.72           O  
ATOM    474  CB  LYS A  63      35.727  37.830  17.449  1.00 27.83           C  
ATOM    475  CG  LYS A  63      35.714  36.414  17.964  1.00 34.40           C  
ATOM    476  CD  LYS A  63      34.448  36.316  18.757  1.00 39.81           C  
ATOM    477  CE  LYS A  63      34.412  34.979  19.438  1.00 45.17           C  
ATOM    478  NZ  LYS A  63      33.226  34.927  20.262  1.00 50.73           N  
ATOM    479  N   ILE A  64      37.162  40.537  16.543  1.00 24.42           N  
ATOM    480  CA  ILE A  64      37.142  41.884  15.992  1.00 21.04           C  
ATOM    481  C   ILE A  64      38.573  42.421  16.153  1.00 21.51           C  
ATOM    482  O   ILE A  64      39.375  41.867  16.894  1.00 21.68           O  
ATOM    483  CB  ILE A  64      36.125  42.837  16.752  1.00 19.55           C  
ATOM    484  CG1 ILE A  64      36.438  42.870  18.224  1.00 16.70           C  
ATOM    485  CG2 ILE A  64      34.691  42.406  16.467  1.00 16.99           C  
ATOM    486  CD1 ILE A  64      35.533  43.739  19.065  1.00 18.17           C  
ATOM    487  N   ASP A  65      38.905  43.518  15.474  1.00 21.85           N  
ATOM    488  CA  ASP A  65      40.197  44.181  15.511  1.00 21.61           C  
ATOM    489  C   ASP A  65      40.231  45.478  16.304  1.00 22.87           C  
ATOM    490  O   ASP A  65      41.315  45.953  16.626  1.00 23.73           O  
ATOM    491  CB  ASP A  65      40.656  44.499  14.094  1.00 22.34           C  
ATOM    492  CG  ASP A  65      40.613  43.209  13.310  1.00 23.11           C  
ATOM    493  OD1 ASP A  65      41.228  42.248  13.784  1.00 23.12           O  
ATOM    494  OD2 ASP A  65      39.947  43.158  12.279  1.00 22.27           O  
ATOM    495  N   ALA A  66      39.093  46.101  16.584  1.00 20.86           N  
ATOM    496  CA  ALA A  66      39.054  47.357  17.298  1.00 22.68           C  
ATOM    497  C   ALA A  66      37.675  47.459  17.935  1.00 21.91           C  
ATOM    498  O   ALA A  66      36.696  46.837  17.490  1.00 22.83           O  
ATOM    499  CB  ALA A  66      39.252  48.552  16.333  1.00 19.81           C  
ATOM    500  N   ILE A  67      37.619  48.246  18.999  1.00 22.11           N  
ATOM    501  CA  ILE A  67      36.388  48.529  19.686  1.00 21.07           C  
ATOM    502  C   ILE A  67      36.179  50.040  19.604  1.00 21.39           C  
ATOM    503  O   ILE A  67      37.054  50.781  20.091  1.00 21.82           O  
ATOM    504  CB  ILE A  67      36.447  48.135  21.181  1.00 18.22           C  
ATOM    505  CG1 ILE A  67      36.702  46.631  21.396  1.00 17.83           C  
ATOM    506  CG2 ILE A  67      35.096  48.584  21.800  1.00 18.97           C  
ATOM    507  CD1 ILE A  67      36.997  46.280  22.865  1.00 15.01           C  
ATOM    508  N   ILE A  68      35.087  50.536  19.029  1.00 20.85           N  
ATOM    509  CA  ILE A  68      34.771  51.962  19.172  1.00 21.28           C  
ATOM    510  C   ILE A  68      33.327  51.964  19.674  1.00 20.96           C  
ATOM    511  O   ILE A  68      32.345  51.803  18.934  1.00 24.84           O  
ATOM    512  CB  ILE A  68      34.865  52.740  17.850  1.00 19.96           C  
ATOM    513  CG1 ILE A  68      36.280  52.741  17.254  1.00 18.21           C  
ATOM    514  CG2 ILE A  68      34.489  54.192  18.151  1.00 20.36           C  
ATOM    515  CD1 ILE A  68      36.374  53.351  15.796  1.00 13.57           C  
ATOM    516  N   SER A  69      33.212  52.138  20.980  1.00 20.49           N  
ATOM    517  CA  SER A  69      31.941  52.049  21.629  1.00 22.46           C  
ATOM    518  C   SER A  69      31.952  52.862  22.918  1.00 21.40           C  
ATOM    519  O   SER A  69      31.587  52.315  23.971  1.00 21.63           O  
ATOM    520  CB  SER A  69      31.709  50.578  21.864  1.00 20.88           C  
ATOM    521  OG  SER A  69      30.356  50.318  22.194  1.00 29.43           O  
ATOM    522  N   SER A  70      32.366  54.156  22.873  1.00 20.86           N  
ATOM    523  CA  SER A  70      32.486  55.013  24.051  1.00 21.21           C  
ATOM    524  C   SER A  70      33.275  54.348  25.177  1.00 23.56           C  
ATOM    525  O   SER A  70      32.947  54.414  26.381  1.00 25.04           O  
ATOM    526  CB  SER A  70      31.092  55.398  24.560  1.00 19.72           C  
ATOM    527  OG  SER A  70      30.390  56.106  23.572  1.00 26.34           O  
ATOM    528  N   LEU A  71      34.348  53.652  24.806  1.00 24.94           N  
ATOM    529  CA  LEU A  71      35.037  52.838  25.809  1.00 23.19           C  
ATOM    530  C   LEU A  71      36.004  53.734  26.589  1.00 22.46           C  
ATOM    531  O   LEU A  71      36.937  54.261  25.971  1.00 23.19           O  
ATOM    532  CB  LEU A  71      35.715  51.721  25.033  1.00 21.26           C  
ATOM    533  CG  LEU A  71      36.506  50.727  25.833  1.00 24.99           C  
ATOM    534  CD1 LEU A  71      35.597  49.814  26.604  1.00 22.56           C  
ATOM    535  CD2 LEU A  71      37.372  49.947  24.859  1.00 25.23           C  
ATOM    536  N   SER A  72      35.890  53.985  27.883  1.00 22.19           N  
ATOM    537  CA  SER A  72      36.771  54.953  28.453  1.00 25.12           C  
ATOM    538  C   SER A  72      38.084  54.304  28.825  1.00 25.51           C  
ATOM    539  O   SER A  72      38.203  53.103  29.115  1.00 24.55           O  
ATOM    540  CB  SER A  72      36.053  55.601  29.627  1.00 24.52           C  
ATOM    541  OG  SER A  72      35.669  54.587  30.511  1.00 31.90           O  
ATOM    542  N   ILE A  73      39.101  55.117  28.689  1.00 26.49           N  
ATOM    543  CA  ILE A  73      40.470  54.719  28.933  1.00 26.87           C  
ATOM    544  C   ILE A  73      40.690  54.700  30.440  1.00 29.92           C  
ATOM    545  O   ILE A  73      41.015  55.743  31.065  1.00 29.79           O  
ATOM    546  CB  ILE A  73      41.426  55.663  28.210  1.00 25.84           C  
ATOM    547  CG1 ILE A  73      41.078  55.726  26.726  1.00 21.31           C  
ATOM    548  CG2 ILE A  73      42.876  55.203  28.428  1.00 23.52           C  
ATOM    549  CD1 ILE A  73      41.572  56.902  25.907  1.00 18.20           C  
ATOM    550  N   THR A  74      40.471  53.554  31.048  1.00 30.75           N  
ATOM    551  CA  THR A  74      40.711  53.444  32.466  1.00 32.96           C  
ATOM    552  C   THR A  74      41.991  52.665  32.670  1.00 35.15           C  
ATOM    553  O   THR A  74      42.387  51.857  31.818  1.00 33.89           O  
ATOM    554  CB  THR A  74      39.512  52.748  33.132  1.00 35.05           C  
ATOM    555  OG1 THR A  74      39.451  51.386  32.674  1.00 33.36           O  
ATOM    556  CG2 THR A  74      38.203  53.470  32.799  1.00 35.26           C  
ATOM    557  N   ASP A  75      42.576  52.802  33.847  1.00 37.91           N  
ATOM    558  CA  ASP A  75      43.803  52.109  34.185  1.00 44.06           C  
ATOM    559  C   ASP A  75      43.640  50.587  34.128  1.00 41.17           C  
ATOM    560  O   ASP A  75      44.446  49.853  33.576  1.00 37.60           O  
ATOM    561  CB  ASP A  75      44.229  52.576  35.581  1.00 53.71           C  
ATOM    562  CG  ASP A  75      45.752  52.670  35.706  1.00 65.27           C  
ATOM    563  OD1 ASP A  75      46.399  51.668  36.067  1.00 68.27           O  
ATOM    564  OD2 ASP A  75      46.281  53.759  35.428  1.00 70.64           O  
ATOM    565  N   LYS A  76      42.512  50.108  34.626  1.00 41.84           N  
ATOM    566  CA  LYS A  76      42.187  48.690  34.639  1.00 43.86           C  
ATOM    567  C   LYS A  76      42.080  48.161  33.212  1.00 41.18           C  
ATOM    568  O   LYS A  76      42.548  47.056  32.978  1.00 41.31           O  
ATOM    569  CB  LYS A  76      40.870  48.525  35.441  1.00 48.63           C  
ATOM    570  CG  LYS A  76      40.659  47.192  36.134  1.00 57.21           C  
ATOM    571  CD  LYS A  76      40.265  46.116  35.127  1.00 66.97           C  
ATOM    572  CE  LYS A  76      40.928  44.778  35.451  1.00 73.00           C  
ATOM    573  NZ  LYS A  76      40.877  43.911  34.281  1.00 78.73           N  
ATOM    574  N   ARG A  77      41.540  48.876  32.220  1.00 38.06           N  
ATOM    575  CA  ARG A  77      41.508  48.334  30.875  1.00 36.26           C  
ATOM    576  C   ARG A  77      42.874  48.438  30.222  1.00 35.96           C  
ATOM    577  O   ARG A  77      43.198  47.609  29.375  1.00 37.90           O  
ATOM    578  CB  ARG A  77      40.515  49.068  30.011  1.00 35.35           C  
ATOM    579  CG  ARG A  77      39.089  48.813  30.439  1.00 34.61           C  
ATOM    580  CD  ARG A  77      38.111  49.607  29.602  1.00 34.78           C  
ATOM    581  NE  ARG A  77      36.769  49.308  30.075  1.00 33.49           N  
ATOM    582  CZ  ARG A  77      35.823  50.212  30.249  1.00 31.00           C  
ATOM    583  NH1 ARG A  77      36.006  51.505  30.003  1.00 31.54           N  
ATOM    584  NH2 ARG A  77      34.660  49.780  30.667  1.00 29.81           N  
ATOM    585  N   GLN A  78      43.687  49.437  30.579  1.00 35.53           N  
ATOM    586  CA  GLN A  78      45.037  49.582  30.046  1.00 36.70           C  
ATOM    587  C   GLN A  78      45.924  48.400  30.439  1.00 38.04           C  
ATOM    588  O   GLN A  78      46.872  48.045  29.757  1.00 37.77           O  
ATOM    589  CB  GLN A  78      45.634  50.892  30.544  1.00 35.00           C  
ATOM    590  CG  GLN A  78      44.883  52.058  29.926  1.00 39.46           C  
ATOM    591  CD  GLN A  78      45.595  53.407  29.869  1.00 42.06           C  
ATOM    592  OE1 GLN A  78      46.063  53.867  28.838  1.00 46.20           O  
ATOM    593  NE2 GLN A  78      45.706  54.164  30.928  1.00 41.44           N  
ATOM    594  N   GLN A  79      45.626  47.781  31.569  1.00 41.08           N  
ATOM    595  CA  GLN A  79      46.223  46.534  31.990  1.00 44.98           C  
ATOM    596  C   GLN A  79      45.982  45.448  30.947  1.00 44.86           C  
ATOM    597  O   GLN A  79      46.858  44.607  30.725  1.00 44.97           O  
ATOM    598  CB  GLN A  79      45.610  46.126  33.331  1.00 50.71           C  
ATOM    599  CG  GLN A  79      46.309  46.544  34.634  1.00 60.89           C  
ATOM    600  CD  GLN A  79      46.725  48.011  34.823  1.00 68.88           C  
ATOM    601  OE1 GLN A  79      46.931  48.805  33.894  1.00 72.10           O  
ATOM    602  NE2 GLN A  79      46.903  48.436  36.076  1.00 70.81           N  
ATOM    603  N   GLU A  80      44.823  45.449  30.281  1.00 42.79           N  
ATOM    604  CA  GLU A  80      44.464  44.425  29.308  1.00 41.83           C  
ATOM    605  C   GLU A  80      44.664  44.684  27.816  1.00 37.90           C  
ATOM    606  O   GLU A  80      45.034  43.774  27.048  1.00 34.40           O  
ATOM    607  CB  GLU A  80      43.015  44.058  29.438  1.00 48.44           C  
ATOM    608  CG  GLU A  80      42.522  43.631  30.786  1.00 58.67           C  
ATOM    609  CD  GLU A  80      41.411  42.612  30.612  1.00 65.04           C  
ATOM    610  OE1 GLU A  80      40.376  42.932  30.013  1.00 68.61           O  
ATOM    611  OE2 GLU A  80      41.610  41.481  31.062  1.00 71.43           O  
ATOM    612  N   ILE A  81      44.349  45.924  27.387  1.00 33.82           N  
ATOM    613  CA  ILE A  81      44.290  46.305  25.975  1.00 29.05           C  
ATOM    614  C   ILE A  81      45.005  47.634  25.848  1.00 25.87           C  
ATOM    615  O   ILE A  81      45.335  48.266  26.851  1.00 27.22           O  
ATOM    616  CB  ILE A  81      42.815  46.514  25.425  1.00 27.37           C  
ATOM    617  CG1 ILE A  81      42.013  47.565  26.228  1.00 24.66           C  
ATOM    618  CG2 ILE A  81      42.107  45.176  25.459  1.00 26.45           C  
ATOM    619  CD1 ILE A  81      40.589  47.834  25.674  1.00 19.13           C  
ATOM    620  N   ALA A  82      45.174  48.032  24.598  1.00 23.21           N  
ATOM    621  CA  ALA A  82      45.763  49.291  24.219  1.00 24.57           C  
ATOM    622  C   ALA A  82      44.634  50.221  23.748  1.00 23.88           C  
ATOM    623  O   ALA A  82      43.543  49.755  23.417  1.00 23.49           O  
ATOM    624  CB  ALA A  82      46.746  49.048  23.087  1.00 22.45           C  
ATOM    625  N   PHE A  83      44.848  51.531  23.717  1.00 24.16           N  
ATOM    626  CA  PHE A  83      43.895  52.530  23.290  1.00 24.86           C  
ATOM    627  C   PHE A  83      44.550  53.497  22.327  1.00 25.24           C  
ATOM    628  O   PHE A  83      45.759  53.792  22.411  1.00 27.16           O  
ATOM    629  CB  PHE A  83      43.389  53.378  24.435  1.00 22.66           C  
ATOM    630  CG  PHE A  83      42.443  52.622  25.323  1.00 24.05           C  
ATOM    631  CD1 PHE A  83      41.092  52.559  24.961  1.00 22.90           C  
ATOM    632  CD2 PHE A  83      42.918  52.054  26.490  1.00 22.03           C  
ATOM    633  CE1 PHE A  83      40.215  51.916  25.810  1.00 21.54           C  
ATOM    634  CE2 PHE A  83      42.018  51.415  27.319  1.00 23.09           C  
ATOM    635  CZ  PHE A  83      40.681  51.354  26.985  1.00 20.39           C  
ATOM    636  N   SER A  84      43.757  54.017  21.393  1.00 24.28           N  
ATOM    637  CA  SER A  84      44.224  55.118  20.556  1.00 23.81           C  
ATOM    638  C   SER A  84      44.304  56.331  21.478  1.00 22.23           C  
ATOM    639  O   SER A  84      43.955  56.288  22.662  1.00 20.11           O  
ATOM    640  CB  SER A  84      43.224  55.431  19.431  1.00 23.47           C  
ATOM    641  OG  SER A  84      41.974  55.852  19.991  1.00 20.22           O  
ATOM    642  N   ASP A  85      44.685  57.460  20.890  1.00 23.09           N  
ATOM    643  CA  ASP A  85      44.524  58.725  21.567  1.00 23.67           C  
ATOM    644  C   ASP A  85      43.017  58.941  21.802  1.00 25.37           C  
ATOM    645  O   ASP A  85      42.173  58.346  21.126  1.00 25.13           O  
ATOM    646  CB  ASP A  85      45.094  59.806  20.680  1.00 25.96           C  
ATOM    647  CG  ASP A  85      46.604  59.750  20.647  1.00 27.48           C  
ATOM    648  OD1 ASP A  85      47.232  59.418  21.655  1.00 30.66           O  
ATOM    649  OD2 ASP A  85      47.153  60.028  19.596  1.00 31.07           O  
ATOM    650  N   LYS A  86      42.678  59.783  22.768  1.00 26.85           N  
ATOM    651  CA  LYS A  86      41.312  60.126  23.118  1.00 26.19           C  
ATOM    652  C   LYS A  86      40.479  60.597  21.934  1.00 24.69           C  
ATOM    653  O   LYS A  86      40.923  61.373  21.085  1.00 24.39           O  
ATOM    654  CB  LYS A  86      41.404  61.199  24.177  1.00 31.85           C  
ATOM    655  CG  LYS A  86      40.071  61.670  24.700  1.00 36.13           C  
ATOM    656  CD  LYS A  86      40.222  62.780  25.710  1.00 34.09           C  
ATOM    657  CE  LYS A  86      40.437  64.086  25.023  1.00 37.70           C  
ATOM    658  NZ  LYS A  86      40.306  65.157  25.999  1.00 40.33           N  
ATOM    659  N   LEU A  87      39.259  60.073  21.847  1.00 25.90           N  
ATOM    660  CA  LEU A  87      38.301  60.486  20.829  1.00 25.00           C  
ATOM    661  C   LEU A  87      37.437  61.650  21.325  1.00 25.78           C  
ATOM    662  O   LEU A  87      37.104  62.551  20.566  1.00 24.26           O  
ATOM    663  CB  LEU A  87      37.443  59.274  20.468  1.00 24.49           C  
ATOM    664  CG  LEU A  87      37.805  58.323  19.299  1.00 28.96           C  
ATOM    665  CD1 LEU A  87      39.266  58.251  19.009  1.00 25.49           C  
ATOM    666  CD2 LEU A  87      37.320  56.958  19.670  1.00 23.23           C  
ATOM    667  N   TYR A  88      37.056  61.645  22.600  1.00 25.48           N  
ATOM    668  CA  TYR A  88      36.277  62.681  23.271  1.00 25.06           C  
ATOM    669  C   TYR A  88      36.307  62.335  24.747  1.00 24.27           C  
ATOM    670  O   TYR A  88      36.715  61.222  25.156  1.00 26.64           O  
ATOM    671  CB  TYR A  88      34.793  62.734  22.805  1.00 22.94           C  
ATOM    672  CG  TYR A  88      33.988  61.434  22.694  1.00 17.81           C  
ATOM    673  CD1 TYR A  88      33.355  60.911  23.795  1.00 16.70           C  
ATOM    674  CD2 TYR A  88      33.996  60.769  21.477  1.00 20.25           C  
ATOM    675  CE1 TYR A  88      32.696  59.713  23.662  1.00 18.31           C  
ATOM    676  CE2 TYR A  88      33.345  59.564  21.341  1.00 21.67           C  
ATOM    677  CZ  TYR A  88      32.709  59.044  22.445  1.00 20.42           C  
ATOM    678  OH  TYR A  88      32.076  57.815  22.326  1.00 21.51           O  
ATOM    679  N   ALA A  89      35.844  63.275  25.557  1.00 24.46           N  
ATOM    680  CA  ALA A  89      35.852  63.130  27.001  1.00 24.18           C  
ATOM    681  C   ALA A  89      34.613  62.406  27.481  1.00 22.89           C  
ATOM    682  O   ALA A  89      33.583  62.443  26.815  1.00 23.12           O  
ATOM    683  CB  ALA A  89      35.873  64.488  27.706  1.00 22.80           C  
ATOM    684  N   ALA A  90      34.675  61.791  28.662  1.00 25.53           N  
ATOM    685  CA  ALA A  90      33.540  61.112  29.280  1.00 25.10           C  
ATOM    686  C   ALA A  90      33.469  61.515  30.751  1.00 24.64           C  
ATOM    687  O   ALA A  90      33.548  60.660  31.647  1.00 23.09           O  
ATOM    688  CB  ALA A  90      33.744  59.614  29.174  1.00 24.32           C  
ATOM    689  N   ASP A  91      33.359  62.834  31.034  1.00 25.08           N  
ATOM    690  CA  ASP A  91      33.363  63.309  32.419  1.00 22.36           C  
ATOM    691  C   ASP A  91      31.942  63.474  32.944  1.00 18.87           C  
ATOM    692  O   ASP A  91      30.966  63.360  32.200  1.00 19.83           O  
ATOM    693  CB  ASP A  91      34.120  64.661  32.518  1.00 26.60           C  
ATOM    694  CG  ASP A  91      35.503  64.672  31.860  1.00 29.42           C  
ATOM    695  OD1 ASP A  91      36.326  63.804  32.140  1.00 31.75           O  
ATOM    696  OD2 ASP A  91      35.761  65.557  31.054  1.00 34.12           O  
ATOM    697  N   SER A  92      31.886  63.697  34.245  1.00 21.33           N  
ATOM    698  CA  SER A  92      30.650  63.924  34.973  1.00 24.17           C  
ATOM    699  C   SER A  92      30.468  65.401  35.268  1.00 23.52           C  
ATOM    700  O   SER A  92      31.427  66.164  35.103  1.00 20.68           O  
ATOM    701  CB  SER A  92      30.654  63.175  36.294  1.00 22.66           C  
ATOM    702  OG  SER A  92      30.726  61.798  35.999  1.00 28.83           O  
ATOM    703  N   ARG A  93      29.305  65.838  35.748  1.00 22.24           N  
ATOM    704  CA  ARG A  93      29.080  67.253  35.965  1.00 20.46           C  
ATOM    705  C   ARG A  93      27.852  67.332  36.832  1.00 23.59           C  
ATOM    706  O   ARG A  93      27.012  66.417  36.790  1.00 22.33           O  
ATOM    707  CB  ARG A  93      28.864  67.892  34.617  1.00 16.00           C  
ATOM    708  CG  ARG A  93      29.066  69.356  34.620  1.00 16.88           C  
ATOM    709  CD  ARG A  93      29.311  69.768  33.190  1.00 19.09           C  
ATOM    710  NE  ARG A  93      29.424  71.213  33.202  1.00 25.22           N  
ATOM    711  CZ  ARG A  93      29.382  71.996  32.121  1.00 28.83           C  
ATOM    712  NH1 ARG A  93      29.240  71.483  30.884  1.00 24.95           N  
ATOM    713  NH2 ARG A  93      29.403  73.337  32.319  1.00 25.27           N  
ATOM    714  N   LEU A  94      27.799  68.365  37.681  1.00 25.18           N  
ATOM    715  CA  LEU A  94      26.640  68.597  38.551  1.00 25.34           C  
ATOM    716  C   LEU A  94      25.501  69.257  37.772  1.00 25.96           C  
ATOM    717  O   LEU A  94      25.721  70.075  36.866  1.00 22.08           O  
ATOM    718  CB  LEU A  94      27.010  69.488  39.767  1.00 18.99           C  
ATOM    719  CG  LEU A  94      27.972  68.894  40.803  1.00 22.20           C  
ATOM    720  CD1 LEU A  94      28.351  69.951  41.818  1.00 21.34           C  
ATOM    721  CD2 LEU A  94      27.299  67.753  41.573  1.00 18.35           C  
ATOM    722  N   ILE A  95      24.263  68.841  38.062  1.00 27.75           N  
ATOM    723  CA  ILE A  95      23.082  69.470  37.493  1.00 27.75           C  
ATOM    724  C   ILE A  95      22.375  70.089  38.690  1.00 25.76           C  
ATOM    725  O   ILE A  95      22.320  69.487  39.765  1.00 21.90           O  
ATOM    726  CB  ILE A  95      22.157  68.429  36.822  1.00 34.05           C  
ATOM    727  CG1 ILE A  95      22.857  67.766  35.666  1.00 38.17           C  
ATOM    728  CG2 ILE A  95      20.869  69.106  36.337  1.00 38.38           C  
ATOM    729  CD1 ILE A  95      23.437  66.455  36.231  1.00 47.36           C  
ATOM    730  N   ALA A  96      21.888  71.318  38.553  1.00 25.56           N  
ATOM    731  CA  ALA A  96      21.119  71.962  39.604  1.00 25.04           C  
ATOM    732  C   ALA A  96      20.100  72.898  38.922  1.00 27.19           C  
ATOM    733  O   ALA A  96      19.977  72.956  37.670  1.00 28.84           O  
ATOM    734  CB  ALA A  96      22.046  72.757  40.522  1.00 18.49           C  
ATOM    735  N   ALA A  97      19.256  73.535  39.737  1.00 27.40           N  
ATOM    736  CA  ALA A  97      18.309  74.533  39.255  1.00 26.76           C  
ATOM    737  C   ALA A  97      19.027  75.675  38.516  1.00 27.91           C  
ATOM    738  O   ALA A  97      20.111  76.105  38.949  1.00 26.56           O  
ATOM    739  CB  ALA A  97      17.551  75.089  40.460  1.00 24.48           C  
ATOM    740  N   LYS A  98      18.474  76.138  37.377  1.00 30.07           N  
ATOM    741  CA  LYS A  98      18.972  77.314  36.671  1.00 31.33           C  
ATOM    742  C   LYS A  98      19.224  78.429  37.648  1.00 31.70           C  
ATOM    743  O   LYS A  98      18.436  78.673  38.569  1.00 31.00           O  
ATOM    744  CB  LYS A  98      17.991  77.845  35.675  1.00 34.69           C  
ATOM    745  CG  LYS A  98      18.407  77.314  34.347  1.00 40.07           C  
ATOM    746  CD  LYS A  98      17.505  77.709  33.207  1.00 45.03           C  
ATOM    747  CE  LYS A  98      17.894  76.716  32.118  1.00 48.62           C  
ATOM    748  NZ  LYS A  98      17.234  77.025  30.861  1.00 56.35           N  
ATOM    749  N   GLY A  99      20.434  78.980  37.521  1.00 32.69           N  
ATOM    750  CA  GLY A  99      20.840  80.091  38.372  1.00 32.59           C  
ATOM    751  C   GLY A  99      21.424  79.705  39.722  1.00 32.75           C  
ATOM    752  O   GLY A  99      21.726  80.610  40.513  1.00 33.80           O  
ATOM    753  N   SER A 100      21.583  78.415  40.030  1.00 32.47           N  
ATOM    754  CA  SER A 100      22.202  77.961  41.263  1.00 32.14           C  
ATOM    755  C   SER A 100      23.647  78.463  41.368  1.00 29.04           C  
ATOM    756  O   SER A 100      24.394  78.347  40.406  1.00 28.24           O  
ATOM    757  CB  SER A 100      22.226  76.423  41.303  1.00 33.68           C  
ATOM    758  OG  SER A 100      22.548  75.994  42.622  1.00 38.84           O  
ATOM    759  N   PRO A 101      24.147  78.951  42.488  1.00 28.58           N  
ATOM    760  CA  PRO A 101      25.537  79.247  42.660  1.00 30.11           C  
ATOM    761  C   PRO A 101      26.407  78.020  42.982  1.00 34.81           C  
ATOM    762  O   PRO A 101      27.605  78.218  43.250  1.00 37.96           O  
ATOM    763  CB  PRO A 101      25.473  80.279  43.727  1.00 30.33           C  
ATOM    764  CG  PRO A 101      24.460  79.665  44.647  1.00 31.12           C  
ATOM    765  CD  PRO A 101      23.380  79.313  43.668  1.00 31.65           C  
ATOM    766  N   ILE A 102      25.855  76.776  42.995  1.00 32.04           N  
ATOM    767  CA  ILE A 102      26.557  75.563  43.373  1.00 29.39           C  
ATOM    768  C   ILE A 102      27.730  75.316  42.439  1.00 27.81           C  
ATOM    769  O   ILE A 102      27.652  75.499  41.225  1.00 24.93           O  
ATOM    770  CB  ILE A 102      25.500  74.410  43.363  1.00 31.79           C  
ATOM    771  CG1 ILE A 102      25.061  74.159  44.770  1.00 33.42           C  
ATOM    772  CG2 ILE A 102      26.043  73.074  42.916  1.00 35.69           C  
ATOM    773  CD1 ILE A 102      23.851  73.203  44.819  1.00 35.80           C  
ATOM    774  N   GLN A 103      28.822  74.833  43.034  1.00 27.21           N  
ATOM    775  CA  GLN A 103      30.043  74.528  42.295  1.00 28.46           C  
ATOM    776  C   GLN A 103      30.497  73.142  42.706  1.00 26.91           C  
ATOM    777  O   GLN A 103      30.218  72.775  43.852  1.00 24.00           O  
ATOM    778  CB  GLN A 103      31.165  75.455  42.659  1.00 29.62           C  
ATOM    779  CG  GLN A 103      31.050  76.734  41.918  1.00 33.09           C  
ATOM    780  CD  GLN A 103      31.303  76.536  40.453  1.00 34.83           C  
ATOM    781  OE1 GLN A 103      30.564  77.008  39.616  1.00 42.12           O  
ATOM    782  NE2 GLN A 103      32.373  75.852  40.075  1.00 38.39           N  
ATOM    783  N   PRO A 104      31.270  72.378  41.931  1.00 25.26           N  
ATOM    784  CA  PRO A 104      31.788  71.070  42.399  1.00 27.04           C  
ATOM    785  C   PRO A 104      32.997  71.137  43.335  1.00 29.17           C  
ATOM    786  O   PRO A 104      33.991  70.444  43.102  1.00 31.27           O  
ATOM    787  CB  PRO A 104      32.050  70.292  41.093  1.00 26.80           C  
ATOM    788  CG  PRO A 104      32.396  71.421  40.135  1.00 24.46           C  
ATOM    789  CD  PRO A 104      31.410  72.536  40.490  1.00 22.97           C  
ATOM    790  N   THR A 105      32.929  71.944  44.409  1.00 28.97           N  
ATOM    791  CA  THR A 105      34.031  72.132  45.337  1.00 29.73           C  
ATOM    792  C   THR A 105      33.485  71.718  46.671  1.00 31.28           C  
ATOM    793  O   THR A 105      32.285  71.833  46.930  1.00 31.77           O  
ATOM    794  CB  THR A 105      34.490  73.592  45.464  1.00 30.12           C  
ATOM    795  OG1 THR A 105      33.390  74.369  45.932  1.00 32.28           O  
ATOM    796  CG2 THR A 105      34.938  74.140  44.129  1.00 30.02           C  
ATOM    797  N   LEU A 106      34.367  71.392  47.579  1.00 32.24           N  
ATOM    798  CA  LEU A 106      33.933  70.919  48.857  1.00 34.61           C  
ATOM    799  C   LEU A 106      33.353  72.096  49.623  1.00 36.74           C  
ATOM    800  O   LEU A 106      32.409  71.957  50.380  1.00 37.36           O  
ATOM    801  CB  LEU A 106      35.145  70.347  49.500  1.00 38.52           C  
ATOM    802  CG  LEU A 106      34.927  69.480  50.685  1.00 44.52           C  
ATOM    803  CD1 LEU A 106      34.147  68.230  50.291  1.00 44.97           C  
ATOM    804  CD2 LEU A 106      36.284  69.137  51.259  1.00 47.76           C  
ATOM    805  N   GLU A 107      33.851  73.289  49.339  1.00 38.81           N  
ATOM    806  CA  GLU A 107      33.475  74.542  49.933  1.00 41.86           C  
ATOM    807  C   GLU A 107      32.032  74.848  49.585  1.00 41.13           C  
ATOM    808  O   GLU A 107      31.189  75.160  50.435  1.00 42.61           O  
ATOM    809  CB  GLU A 107      34.412  75.634  49.401  1.00 49.49           C  
ATOM    810  CG  GLU A 107      35.943  75.327  49.502  1.00 61.04           C  
ATOM    811  CD  GLU A 107      36.600  74.499  48.372  1.00 65.59           C  
ATOM    812  OE1 GLU A 107      36.521  73.260  48.354  1.00 67.68           O  
ATOM    813  OE2 GLU A 107      37.200  75.110  47.485  1.00 69.42           O  
ATOM    814  N   SER A 108      31.722  74.671  48.306  1.00 37.58           N  
ATOM    815  CA  SER A 108      30.388  74.945  47.845  1.00 33.65           C  
ATOM    816  C   SER A 108      29.392  73.874  48.260  1.00 34.58           C  
ATOM    817  O   SER A 108      28.265  74.194  48.586  1.00 35.70           O  
ATOM    818  CB  SER A 108      30.506  75.060  46.392  1.00 30.35           C  
ATOM    819  OG  SER A 108      29.310  75.432  45.770  1.00 35.59           O  
ATOM    820  N   LEU A 109      29.762  72.598  48.306  1.00 34.48           N  
ATOM    821  CA  LEU A 109      28.830  71.526  48.547  1.00 31.28           C  
ATOM    822  C   LEU A 109      28.575  71.223  49.989  1.00 34.83           C  
ATOM    823  O   LEU A 109      27.606  70.523  50.296  1.00 36.04           O  
ATOM    824  CB  LEU A 109      29.343  70.305  47.826  1.00 24.40           C  
ATOM    825  CG  LEU A 109      29.209  70.416  46.321  1.00 22.85           C  
ATOM    826  CD1 LEU A 109      29.876  69.271  45.673  1.00 21.79           C  
ATOM    827  CD2 LEU A 109      27.746  70.436  45.941  1.00 24.31           C  
ATOM    828  N   LYS A 110      29.341  71.715  50.943  1.00 41.05           N  
ATOM    829  CA  LYS A 110      29.034  71.384  52.315  1.00 46.08           C  
ATOM    830  C   LYS A 110      27.741  72.048  52.714  1.00 45.48           C  
ATOM    831  O   LYS A 110      27.539  73.253  52.601  1.00 46.87           O  
ATOM    832  CB  LYS A 110      30.155  71.830  53.192  1.00 51.89           C  
ATOM    833  CG  LYS A 110      31.163  70.693  53.215  1.00 60.82           C  
ATOM    834  CD  LYS A 110      32.483  71.219  53.733  1.00 67.80           C  
ATOM    835  CE  LYS A 110      33.481  70.097  53.808  1.00 70.29           C  
ATOM    836  NZ  LYS A 110      34.804  70.679  53.854  1.00 74.83           N  
ATOM    837  N   GLY A 111      26.820  71.166  53.045  1.00 46.33           N  
ATOM    838  CA  GLY A 111      25.485  71.560  53.452  1.00 47.54           C  
ATOM    839  C   GLY A 111      24.449  71.057  52.457  1.00 48.27           C  
ATOM    840  O   GLY A 111      23.273  70.831  52.786  1.00 52.21           O  
ATOM    841  N   LYS A 112      24.890  70.824  51.227  1.00 43.87           N  
ATOM    842  CA  LYS A 112      23.997  70.449  50.181  1.00 40.46           C  
ATOM    843  C   LYS A 112      23.743  68.952  50.227  1.00 38.77           C  
ATOM    844  O   LYS A 112      24.366  68.230  51.005  1.00 38.23           O  
ATOM    845  CB  LYS A 112      24.622  70.896  48.887  1.00 42.24           C  
ATOM    846  CG  LYS A 112      24.993  72.370  48.831  1.00 46.54           C  
ATOM    847  CD  LYS A 112      23.848  73.340  48.647  1.00 55.48           C  
ATOM    848  CE  LYS A 112      23.245  73.817  49.967  1.00 66.14           C  
ATOM    849  NZ  LYS A 112      22.052  73.091  50.405  1.00 69.69           N  
ATOM    850  N   HIS A 113      22.770  68.498  49.426  1.00 36.57           N  
ATOM    851  CA  HIS A 113      22.337  67.111  49.331  1.00 33.76           C  
ATOM    852  C   HIS A 113      22.532  66.894  47.855  1.00 31.68           C  
ATOM    853  O   HIS A 113      21.968  67.625  47.034  1.00 27.98           O  
ATOM    854  CB  HIS A 113      20.855  66.903  49.650  1.00 38.14           C  
ATOM    855  CG  HIS A 113      20.525  67.523  51.000  1.00 47.24           C  
ATOM    856  ND1 HIS A 113      19.903  68.676  51.271  1.00 52.05           N  
ATOM    857  CD2 HIS A 113      20.978  67.023  52.198  1.00 48.57           C  
ATOM    858  CE1 HIS A 113      19.991  68.886  52.571  1.00 53.20           C  
ATOM    859  NE2 HIS A 113      20.646  67.879  53.119  1.00 52.70           N  
ATOM    860  N   VAL A 114      23.400  65.937  47.548  1.00 30.03           N  
ATOM    861  CA  VAL A 114      23.799  65.626  46.196  1.00 27.17           C  
ATOM    862  C   VAL A 114      23.305  64.229  45.923  1.00 26.46           C  
ATOM    863  O   VAL A 114      23.550  63.331  46.719  1.00 28.87           O  
ATOM    864  CB  VAL A 114      25.352  65.684  46.049  1.00 25.43           C  
ATOM    865  CG1 VAL A 114      25.677  65.539  44.549  1.00 22.72           C  
ATOM    866  CG2 VAL A 114      25.940  66.993  46.639  1.00 26.37           C  
ATOM    867  N   GLY A 115      22.610  63.976  44.841  1.00 25.66           N  
ATOM    868  CA  GLY A 115      22.147  62.638  44.575  1.00 21.40           C  
ATOM    869  C   GLY A 115      23.080  62.034  43.576  1.00 23.75           C  
ATOM    870  O   GLY A 115      23.619  62.696  42.676  1.00 22.39           O  
ATOM    871  N   VAL A 116      23.227  60.734  43.734  1.00 25.70           N  
ATOM    872  CA  VAL A 116      24.115  59.976  42.892  1.00 26.58           C  
ATOM    873  C   VAL A 116      23.408  58.634  42.615  1.00 28.14           C  
ATOM    874  O   VAL A 116      22.565  58.159  43.401  1.00 28.75           O  
ATOM    875  CB  VAL A 116      25.459  59.955  43.735  1.00 26.53           C  
ATOM    876  CG1 VAL A 116      25.602  58.742  44.646  1.00 24.45           C  
ATOM    877  CG2 VAL A 116      26.562  60.139  42.765  1.00 24.04           C  
ATOM    878  N   LEU A 117      23.636  58.026  41.457  1.00 28.86           N  
ATOM    879  CA  LEU A 117      23.089  56.711  41.161  1.00 31.66           C  
ATOM    880  C   LEU A 117      23.867  55.612  41.913  1.00 31.82           C  
ATOM    881  O   LEU A 117      25.091  55.587  41.912  1.00 30.61           O  
ATOM    882  CB  LEU A 117      23.160  56.471  39.699  1.00 28.14           C  
ATOM    883  CG  LEU A 117      22.384  55.288  39.261  1.00 32.32           C  
ATOM    884  CD1 LEU A 117      20.899  55.526  39.410  1.00 34.58           C  
ATOM    885  CD2 LEU A 117      22.730  55.052  37.815  1.00 35.77           C  
ATOM    886  N   GLN A 118      23.184  54.673  42.554  1.00 31.91           N  
ATOM    887  CA  GLN A 118      23.904  53.717  43.336  1.00 32.63           C  
ATOM    888  C   GLN A 118      24.692  52.770  42.414  1.00 30.64           C  
ATOM    889  O   GLN A 118      24.251  52.366  41.343  1.00 29.42           O  
ATOM    890  CB  GLN A 118      22.896  53.015  44.166  1.00 33.51           C  
ATOM    891  CG  GLN A 118      23.541  52.352  45.331  1.00 39.19           C  
ATOM    892  CD  GLN A 118      22.563  51.422  45.993  1.00 43.07           C  
ATOM    893  OE1 GLN A 118      21.787  50.703  45.354  1.00 44.69           O  
ATOM    894  NE2 GLN A 118      22.598  51.469  47.315  1.00 46.54           N  
ATOM    895  N   GLY A 119      25.906  52.496  42.828  1.00 31.05           N  
ATOM    896  CA  GLY A 119      26.825  51.633  42.136  1.00 33.87           C  
ATOM    897  C   GLY A 119      27.509  52.265  40.919  1.00 36.08           C  
ATOM    898  O   GLY A 119      28.194  51.557  40.161  1.00 35.30           O  
ATOM    899  N   SER A 120      27.342  53.559  40.616  1.00 35.22           N  
ATOM    900  CA  SER A 120      28.044  54.049  39.460  1.00 32.03           C  
ATOM    901  C   SER A 120      29.402  54.666  39.835  1.00 30.69           C  
ATOM    902  O   SER A 120      29.777  54.811  40.999  1.00 29.31           O  
ATOM    903  CB  SER A 120      27.044  55.021  38.739  1.00 34.67           C  
ATOM    904  OG  SER A 120      26.809  56.380  39.126  1.00 29.16           O  
ATOM    905  N   THR A 121      30.178  55.049  38.823  1.00 29.77           N  
ATOM    906  CA  THR A 121      31.469  55.705  38.991  1.00 28.77           C  
ATOM    907  C   THR A 121      31.271  57.019  39.692  1.00 24.99           C  
ATOM    908  O   THR A 121      32.068  57.416  40.517  1.00 29.29           O  
ATOM    909  CB  THR A 121      32.121  55.950  37.635  1.00 28.37           C  
ATOM    910  OG1 THR A 121      31.144  56.543  36.795  1.00 32.60           O  
ATOM    911  CG2 THR A 121      32.537  54.668  36.953  1.00 30.32           C  
ATOM    912  N   GLN A 122      30.157  57.705  39.387  1.00 26.57           N  
ATOM    913  CA  GLN A 122      29.813  58.931  40.098  1.00 26.25           C  
ATOM    914  C   GLN A 122      29.701  58.773  41.598  1.00 25.55           C  
ATOM    915  O   GLN A 122      30.231  59.629  42.295  1.00 26.60           O  
ATOM    916  CB  GLN A 122      28.485  59.539  39.577  1.00 22.72           C  
ATOM    917  CG  GLN A 122      28.668  60.156  38.208  1.00 19.38           C  
ATOM    918  CD  GLN A 122      28.647  59.155  37.089  1.00 26.89           C  
ATOM    919  OE1 GLN A 122      29.062  59.395  35.971  1.00 26.86           O  
ATOM    920  NE2 GLN A 122      28.080  57.972  37.222  1.00 25.00           N  
ATOM    921  N   GLU A 123      29.150  57.684  42.152  1.00 28.09           N  
ATOM    922  CA  GLU A 123      28.978  57.453  43.593  1.00 27.20           C  
ATOM    923  C   GLU A 123      30.356  57.177  44.117  1.00 25.65           C  
ATOM    924  O   GLU A 123      30.702  57.722  45.157  1.00 25.60           O  
ATOM    925  CB  GLU A 123      28.139  56.234  43.919  1.00 25.46           C  
ATOM    926  CG  GLU A 123      27.972  55.791  45.312  1.00 30.92           C  
ATOM    927  CD  GLU A 123      27.333  54.423  45.426  1.00 32.69           C  
ATOM    928  OE1 GLU A 123      27.579  53.541  44.619  1.00 35.34           O  
ATOM    929  OE2 GLU A 123      26.530  54.217  46.313  1.00 37.91           O  
ATOM    930  N   ALA A 124      31.190  56.413  43.410  1.00 26.43           N  
ATOM    931  CA  ALA A 124      32.547  56.210  43.872  1.00 25.89           C  
ATOM    932  C   ALA A 124      33.337  57.500  44.061  1.00 25.12           C  
ATOM    933  O   ALA A 124      33.929  57.758  45.117  1.00 27.75           O  
ATOM    934  CB  ALA A 124      33.258  55.318  42.867  1.00 25.04           C  
ATOM    935  N   TYR A 125      33.262  58.382  43.081  1.00 26.91           N  
ATOM    936  CA  TYR A 125      33.906  59.690  43.126  1.00 27.11           C  
ATOM    937  C   TYR A 125      33.344  60.518  44.262  1.00 27.41           C  
ATOM    938  O   TYR A 125      34.076  61.098  45.067  1.00 27.94           O  
ATOM    939  CB  TYR A 125      33.686  60.421  41.788  1.00 25.84           C  
ATOM    940  CG  TYR A 125      34.249  61.828  41.815  1.00 30.51           C  
ATOM    941  CD1 TYR A 125      35.582  62.003  41.523  1.00 30.85           C  
ATOM    942  CD2 TYR A 125      33.463  62.922  42.184  1.00 29.56           C  
ATOM    943  CE1 TYR A 125      36.149  63.263  41.598  1.00 30.92           C  
ATOM    944  CE2 TYR A 125      34.032  64.175  42.265  1.00 31.81           C  
ATOM    945  CZ  TYR A 125      35.373  64.330  41.963  1.00 33.27           C  
ATOM    946  OH  TYR A 125      35.965  65.579  41.985  1.00 39.51           O  
ATOM    947  N   ALA A 126      32.005  60.590  44.329  1.00 30.78           N  
ATOM    948  CA  ALA A 126      31.313  61.411  45.314  1.00 30.61           C  
ATOM    949  C   ALA A 126      31.545  60.884  46.715  1.00 30.48           C  
ATOM    950  O   ALA A 126      31.712  61.662  47.659  1.00 32.86           O  
ATOM    951  CB  ALA A 126      29.822  61.408  45.077  1.00 28.35           C  
ATOM    952  N   ASN A 127      31.621  59.575  46.890  1.00 33.11           N  
ATOM    953  CA  ASN A 127      31.834  58.978  48.201  1.00 35.20           C  
ATOM    954  C   ASN A 127      33.234  59.285  48.708  1.00 32.89           C  
ATOM    955  O   ASN A 127      33.368  59.876  49.779  1.00 31.13           O  
ATOM    956  CB  ASN A 127      31.579  57.460  48.110  1.00 38.43           C  
ATOM    957  CG  ASN A 127      30.102  57.023  48.228  1.00 42.80           C  
ATOM    958  OD1 ASN A 127      29.163  57.763  48.526  1.00 43.05           O  
ATOM    959  ND2 ASN A 127      29.787  55.772  47.968  1.00 45.07           N  
ATOM    960  N   ASP A 128      34.286  59.051  47.910  1.00 36.51           N  
ATOM    961  CA  ASP A 128      35.668  59.331  48.328  1.00 38.76           C  
ATOM    962  C   ASP A 128      35.996  60.797  48.431  1.00 38.36           C  
ATOM    963  O   ASP A 128      36.659  61.206  49.382  1.00 40.15           O  
ATOM    964  CB  ASP A 128      36.723  58.755  47.372  1.00 42.16           C  
ATOM    965  CG  ASP A 128      36.670  57.253  47.146  1.00 47.95           C  
ATOM    966  OD1 ASP A 128      36.008  56.549  47.906  1.00 51.93           O  
ATOM    967  OD2 ASP A 128      37.282  56.772  46.193  1.00 52.59           O  
ATOM    968  N   ASN A 129      35.585  61.612  47.464  1.00 37.40           N  
ATOM    969  CA  ASN A 129      35.921  63.014  47.506  1.00 35.89           C  
ATOM    970  C   ASN A 129      34.988  63.884  48.332  1.00 35.65           C  
ATOM    971  O   ASN A 129      35.417  64.931  48.840  1.00 36.00           O  
ATOM    972  CB  ASN A 129      35.950  63.595  46.118  1.00 39.94           C  
ATOM    973  CG  ASN A 129      36.980  62.997  45.171  1.00 45.15           C  
ATOM    974  OD1 ASN A 129      36.968  61.811  44.840  1.00 45.54           O  
ATOM    975  ND2 ASN A 129      37.898  63.783  44.619  1.00 48.71           N  
ATOM    976  N   TRP A 130      33.716  63.515  48.497  1.00 31.59           N  
ATOM    977  CA  TRP A 130      32.786  64.434  49.110  1.00 29.40           C  
ATOM    978  C   TRP A 130      32.089  63.859  50.315  1.00 26.40           C  
ATOM    979  O   TRP A 130      32.113  64.482  51.379  1.00 26.12           O  
ATOM    980  CB  TRP A 130      31.709  64.912  48.076  1.00 29.76           C  
ATOM    981  CG  TRP A 130      32.150  65.756  46.856  1.00 29.58           C  
ATOM    982  CD1 TRP A 130      33.327  66.474  46.822  1.00 25.67           C  
ATOM    983  CD2 TRP A 130      31.429  65.875  45.667  1.00 27.95           C  
ATOM    984  NE1 TRP A 130      33.349  67.009  45.630  1.00 24.93           N  
ATOM    985  CE2 TRP A 130      32.266  66.677  44.910  1.00 22.81           C  
ATOM    986  CE3 TRP A 130      30.229  65.405  45.136  1.00 22.91           C  
ATOM    987  CZ2 TRP A 130      31.921  67.043  43.630  1.00 20.34           C  
ATOM    988  CZ3 TRP A 130      29.886  65.764  43.854  1.00 19.17           C  
ATOM    989  CH2 TRP A 130      30.728  66.577  43.108  1.00 22.31           C  
ATOM    990  N   ARG A 131      31.473  62.693  50.258  1.00 26.95           N  
ATOM    991  CA  ARG A 131      30.795  62.166  51.427  1.00 28.43           C  
ATOM    992  C   ARG A 131      31.724  61.940  52.639  1.00 29.82           C  
ATOM    993  O   ARG A 131      31.360  62.311  53.768  1.00 30.29           O  
ATOM    994  CB  ARG A 131      30.121  60.894  51.011  1.00 29.78           C  
ATOM    995  CG  ARG A 131      29.245  60.395  52.128  1.00 33.93           C  
ATOM    996  CD  ARG A 131      28.653  59.117  51.630  1.00 39.22           C  
ATOM    997  NE  ARG A 131      28.843  58.208  52.714  1.00 48.93           N  
ATOM    998  CZ  ARG A 131      29.953  57.489  52.834  1.00 52.88           C  
ATOM    999  NH1 ARG A 131      30.987  57.493  51.988  1.00 55.17           N  
ATOM   1000  NH2 ARG A 131      30.066  56.825  53.950  1.00 58.96           N  
ATOM   1001  N   THR A 132      32.963  61.455  52.459  1.00 28.34           N  
ATOM   1002  CA  THR A 132      33.890  61.320  53.572  1.00 28.40           C  
ATOM   1003  C   THR A 132      34.217  62.671  54.225  1.00 30.04           C  
ATOM   1004  O   THR A 132      34.582  62.762  55.404  1.00 29.65           O  
ATOM   1005  CB  THR A 132      35.101  60.612  53.012  1.00 25.39           C  
ATOM   1006  OG1 THR A 132      35.457  61.277  51.828  1.00 27.84           O  
ATOM   1007  CG2 THR A 132      34.796  59.179  52.658  1.00 28.36           C  
ATOM   1008  N   LYS A 133      34.035  63.766  53.475  1.00 31.74           N  
ATOM   1009  CA  LYS A 133      34.337  65.080  53.972  1.00 29.76           C  
ATOM   1010  C   LYS A 133      33.077  65.762  54.444  1.00 33.12           C  
ATOM   1011  O   LYS A 133      33.100  66.964  54.685  1.00 37.46           O  
ATOM   1012  CB  LYS A 133      34.977  65.885  52.893  1.00 28.08           C  
ATOM   1013  CG  LYS A 133      36.173  65.222  52.224  1.00 33.22           C  
ATOM   1014  CD  LYS A 133      37.381  65.005  53.124  1.00 34.44           C  
ATOM   1015  CE  LYS A 133      38.529  64.429  52.282  1.00 35.84           C  
ATOM   1016  NZ  LYS A 133      38.232  63.136  51.676  1.00 39.18           N  
ATOM   1017  N   GLY A 134      31.958  65.070  54.637  1.00 35.59           N  
ATOM   1018  CA  GLY A 134      30.771  65.698  55.185  1.00 36.64           C  
ATOM   1019  C   GLY A 134      29.766  66.282  54.194  1.00 38.80           C  
ATOM   1020  O   GLY A 134      28.843  66.999  54.620  1.00 43.50           O  
ATOM   1021  N   VAL A 135      29.882  66.075  52.881  1.00 35.53           N  
ATOM   1022  CA  VAL A 135      28.817  66.486  51.980  1.00 32.75           C  
ATOM   1023  C   VAL A 135      27.764  65.369  52.130  1.00 32.91           C  
ATOM   1024  O   VAL A 135      28.125  64.195  52.280  1.00 28.90           O  
ATOM   1025  CB  VAL A 135      29.366  66.565  50.552  1.00 30.82           C  
ATOM   1026  CG1 VAL A 135      28.254  66.874  49.550  1.00 26.23           C  
ATOM   1027  CG2 VAL A 135      30.453  67.636  50.526  1.00 29.63           C  
ATOM   1028  N   ASP A 136      26.457  65.650  52.108  1.00 31.50           N  
ATOM   1029  CA  ASP A 136      25.460  64.611  52.261  1.00 29.93           C  
ATOM   1030  C   ASP A 136      25.180  64.047  50.894  1.00 28.19           C  
ATOM   1031  O   ASP A 136      24.452  64.638  50.094  1.00 27.36           O  
ATOM   1032  CB  ASP A 136      24.196  65.192  52.862  1.00 36.85           C  
ATOM   1033  CG  ASP A 136      23.120  64.128  53.000  1.00 47.29           C  
ATOM   1034  OD1 ASP A 136      23.406  63.063  53.567  1.00 56.38           O  
ATOM   1035  OD2 ASP A 136      21.998  64.348  52.533  1.00 50.90           O  
ATOM   1036  N   VAL A 137      25.742  62.889  50.610  1.00 25.72           N  
ATOM   1037  CA  VAL A 137      25.632  62.320  49.284  1.00 27.98           C  
ATOM   1038  C   VAL A 137      24.571  61.257  49.422  1.00 29.98           C  
ATOM   1039  O   VAL A 137      24.693  60.463  50.356  1.00 32.96           O  
ATOM   1040  CB  VAL A 137      26.972  61.692  48.846  1.00 28.60           C  
ATOM   1041  CG1 VAL A 137      26.780  61.007  47.493  1.00 25.51           C  
ATOM   1042  CG2 VAL A 137      28.070  62.768  48.763  1.00 26.30           C  
ATOM   1043  N   VAL A 138      23.541  61.207  48.574  1.00 30.11           N  
ATOM   1044  CA  VAL A 138      22.477  60.224  48.700  1.00 28.42           C  
ATOM   1045  C   VAL A 138      22.445  59.349  47.460  1.00 25.79           C  
ATOM   1046  O   VAL A 138      22.356  59.842  46.330  1.00 27.25           O  
ATOM   1047  CB  VAL A 138      21.152  60.980  48.892  1.00 31.36           C  
ATOM   1048  CG1 VAL A 138      20.015  59.985  49.063  1.00 27.05           C  
ATOM   1049  CG2 VAL A 138      21.276  61.922  50.095  1.00 30.37           C  
ATOM   1050  N   ALA A 139      22.477  58.035  47.610  1.00 25.66           N  
ATOM   1051  CA  ALA A 139      22.563  57.161  46.463  1.00 27.22           C  
ATOM   1052  C   ALA A 139      21.194  56.612  46.135  1.00 28.49           C  
ATOM   1053  O   ALA A 139      20.464  56.234  47.057  1.00 27.66           O  
ATOM   1054  CB  ALA A 139      23.507  56.043  46.784  1.00 29.67           C  
ATOM   1055  N   TYR A 140      20.853  56.580  44.851  1.00 28.17           N  
ATOM   1056  CA  TYR A 140      19.517  56.246  44.395  1.00 30.32           C  
ATOM   1057  C   TYR A 140      19.542  54.984  43.588  1.00 32.17           C  
ATOM   1058  O   TYR A 140      20.487  54.786  42.825  1.00 31.46           O  
ATOM   1059  CB  TYR A 140      18.932  57.307  43.495  1.00 26.16           C  
ATOM   1060  CG  TYR A 140      18.501  58.534  44.279  1.00 27.65           C  
ATOM   1061  CD1 TYR A 140      19.437  59.353  44.874  1.00 22.61           C  
ATOM   1062  CD2 TYR A 140      17.145  58.809  44.415  1.00 27.87           C  
ATOM   1063  CE1 TYR A 140      19.031  60.442  45.604  1.00 26.23           C  
ATOM   1064  CE2 TYR A 140      16.736  59.909  45.143  1.00 27.58           C  
ATOM   1065  CZ  TYR A 140      17.691  60.711  45.731  1.00 26.75           C  
ATOM   1066  OH  TYR A 140      17.302  61.801  46.473  1.00 29.74           O  
ATOM   1067  N   ALA A 141      18.518  54.147  43.721  1.00 32.26           N  
ATOM   1068  CA  ALA A 141      18.444  52.917  42.972  1.00 32.78           C  
ATOM   1069  C   ALA A 141      18.136  53.215  41.523  1.00 34.35           C  
ATOM   1070  O   ALA A 141      18.417  52.454  40.593  1.00 37.75           O  
ATOM   1071  CB  ALA A 141      17.336  52.071  43.520  1.00 34.20           C  
ATOM   1072  N   ASN A 142      17.536  54.364  41.279  1.00 37.97           N  
ATOM   1073  CA  ASN A 142      17.039  54.636  39.966  1.00 40.84           C  
ATOM   1074  C   ASN A 142      17.157  56.091  39.569  1.00 42.14           C  
ATOM   1075  O   ASN A 142      16.883  57.002  40.338  1.00 41.10           O  
ATOM   1076  CB  ASN A 142      15.617  54.085  40.016  1.00 45.52           C  
ATOM   1077  CG  ASN A 142      14.604  54.839  39.203  1.00 51.90           C  
ATOM   1078  OD1 ASN A 142      13.804  55.586  39.757  1.00 57.36           O  
ATOM   1079  ND2 ASN A 142      14.618  54.753  37.876  1.00 56.52           N  
ATOM   1080  N   GLN A 143      17.534  56.316  38.320  1.00 43.63           N  
ATOM   1081  CA  GLN A 143      17.721  57.640  37.773  1.00 43.98           C  
ATOM   1082  C   GLN A 143      16.468  58.487  37.781  1.00 42.88           C  
ATOM   1083  O   GLN A 143      16.571  59.688  38.025  1.00 40.16           O  
ATOM   1084  CB  GLN A 143      18.255  57.487  36.374  1.00 46.02           C  
ATOM   1085  CG  GLN A 143      18.925  58.722  35.808  1.00 53.59           C  
ATOM   1086  CD  GLN A 143      20.049  59.294  36.671  1.00 58.29           C  
ATOM   1087  OE1 GLN A 143      21.151  58.747  36.803  1.00 59.14           O  
ATOM   1088  NE2 GLN A 143      19.745  60.434  37.286  1.00 59.44           N  
ATOM   1089  N   ASP A 144      15.288  57.889  37.580  1.00 43.42           N  
ATOM   1090  CA  ASP A 144      14.015  58.614  37.625  1.00 44.71           C  
ATOM   1091  C   ASP A 144      13.765  59.331  38.923  1.00 41.51           C  
ATOM   1092  O   ASP A 144      13.345  60.489  38.943  1.00 41.53           O  
ATOM   1093  CB  ASP A 144      12.824  57.698  37.420  1.00 50.97           C  
ATOM   1094  CG  ASP A 144      12.773  57.209  35.989  1.00 61.28           C  
ATOM   1095  OD1 ASP A 144      12.529  58.050  35.118  1.00 65.49           O  
ATOM   1096  OD2 ASP A 144      12.991  56.012  35.744  1.00 67.00           O  
ATOM   1097  N   LEU A 145      14.039  58.627  40.011  1.00 38.86           N  
ATOM   1098  CA  LEU A 145      13.877  59.173  41.341  1.00 37.24           C  
ATOM   1099  C   LEU A 145      14.858  60.284  41.636  1.00 36.39           C  
ATOM   1100  O   LEU A 145      14.572  61.129  42.482  1.00 35.11           O  
ATOM   1101  CB  LEU A 145      14.072  58.107  42.370  1.00 39.38           C  
ATOM   1102  CG  LEU A 145      12.954  57.880  43.342  1.00 44.38           C  
ATOM   1103  CD1 LEU A 145      13.418  56.793  44.277  1.00 47.58           C  
ATOM   1104  CD2 LEU A 145      12.604  59.128  44.135  1.00 45.93           C  
ATOM   1105  N   ILE A 146      16.034  60.284  40.998  1.00 36.09           N  
ATOM   1106  CA  ILE A 146      16.986  61.382  41.185  1.00 34.85           C  
ATOM   1107  C   ILE A 146      16.363  62.637  40.578  1.00 32.19           C  
ATOM   1108  O   ILE A 146      16.255  63.687  41.220  1.00 31.41           O  
ATOM   1109  CB  ILE A 146      18.369  61.105  40.486  1.00 35.11           C  
ATOM   1110  CG1 ILE A 146      19.077  59.906  41.109  1.00 33.45           C  
ATOM   1111  CG2 ILE A 146      19.272  62.329  40.655  1.00 35.55           C  
ATOM   1112  CD1 ILE A 146      20.397  59.488  40.428  1.00 33.93           C  
ATOM   1113  N   TYR A 147      15.916  62.509  39.339  1.00 30.89           N  
ATOM   1114  CA  TYR A 147      15.355  63.630  38.632  1.00 32.92           C  
ATOM   1115  C   TYR A 147      14.110  64.175  39.310  1.00 34.65           C  
ATOM   1116  O   TYR A 147      13.990  65.408  39.458  1.00 33.55           O  
ATOM   1117  CB  TYR A 147      15.105  63.172  37.194  1.00 33.87           C  
ATOM   1118  CG  TYR A 147      16.413  63.044  36.396  1.00 38.00           C  
ATOM   1119  CD1 TYR A 147      17.543  63.770  36.777  1.00 38.26           C  
ATOM   1120  CD2 TYR A 147      16.470  62.212  35.285  1.00 36.64           C  
ATOM   1121  CE1 TYR A 147      18.708  63.669  36.061  1.00 40.53           C  
ATOM   1122  CE2 TYR A 147      17.638  62.110  34.556  1.00 40.29           C  
ATOM   1123  CZ  TYR A 147      18.753  62.836  34.949  1.00 43.87           C  
ATOM   1124  OH  TYR A 147      19.940  62.739  34.220  1.00 46.04           O  
ATOM   1125  N   SER A 148      13.249  63.309  39.864  1.00 36.65           N  
ATOM   1126  CA  SER A 148      12.058  63.792  40.531  1.00 38.60           C  
ATOM   1127  C   SER A 148      12.418  64.445  41.847  1.00 35.84           C  
ATOM   1128  O   SER A 148      11.841  65.484  42.191  1.00 37.18           O  
ATOM   1129  CB  SER A 148      11.101  62.635  40.729  1.00 40.43           C  
ATOM   1130  OG  SER A 148      11.735  61.543  41.365  1.00 53.00           O  
ATOM   1131  N   ASP A 149      13.392  63.927  42.584  1.00 33.83           N  
ATOM   1132  CA  ASP A 149      13.809  64.602  43.803  1.00 34.74           C  
ATOM   1133  C   ASP A 149      14.453  65.964  43.602  1.00 32.48           C  
ATOM   1134  O   ASP A 149      14.282  66.872  44.426  1.00 31.41           O  
ATOM   1135  CB  ASP A 149      14.767  63.711  44.586  1.00 36.55           C  
ATOM   1136  CG  ASP A 149      14.050  62.649  45.390  1.00 40.35           C  
ATOM   1137  OD1 ASP A 149      12.943  62.269  45.026  1.00 46.80           O  
ATOM   1138  OD2 ASP A 149      14.591  62.184  46.379  1.00 39.93           O  
ATOM   1139  N   LEU A 150      15.207  66.114  42.522  1.00 34.15           N  
ATOM   1140  CA  LEU A 150      15.832  67.383  42.139  1.00 35.69           C  
ATOM   1141  C   LEU A 150      14.692  68.331  41.816  1.00 35.93           C  
ATOM   1142  O   LEU A 150      14.601  69.391  42.402  1.00 35.58           O  
ATOM   1143  CB  LEU A 150      16.679  67.221  40.888  1.00 34.65           C  
ATOM   1144  CG  LEU A 150      18.025  67.873  40.700  1.00 32.38           C  
ATOM   1145  CD1 LEU A 150      18.203  67.883  39.210  1.00 30.24           C  
ATOM   1146  CD2 LEU A 150      18.147  69.266  41.236  1.00 28.90           C  
ATOM   1147  N   THR A 151      13.797  67.902  40.935  1.00 37.51           N  
ATOM   1148  CA  THR A 151      12.608  68.640  40.549  1.00 40.47           C  
ATOM   1149  C   THR A 151      11.735  69.066  41.723  1.00 40.86           C  
ATOM   1150  O   THR A 151      11.226  70.176  41.768  1.00 43.00           O  
ATOM   1151  CB  THR A 151      11.923  67.703  39.573  1.00 42.92           C  
ATOM   1152  OG1 THR A 151      12.679  67.879  38.364  1.00 43.87           O  
ATOM   1153  CG2 THR A 151      10.425  67.880  39.479  1.00 47.99           C  
ATOM   1154  N   ALA A 152      11.600  68.182  42.697  1.00 41.44           N  
ATOM   1155  CA  ALA A 152      10.864  68.407  43.925  1.00 40.44           C  
ATOM   1156  C   ALA A 152      11.619  69.236  44.966  1.00 40.19           C  
ATOM   1157  O   ALA A 152      11.105  69.527  46.057  1.00 40.65           O  
ATOM   1158  CB  ALA A 152      10.516  67.042  44.530  1.00 42.07           C  
ATOM   1159  N   GLY A 153      12.887  69.565  44.715  1.00 37.70           N  
ATOM   1160  CA  GLY A 153      13.627  70.355  45.675  1.00 35.16           C  
ATOM   1161  C   GLY A 153      14.148  69.548  46.835  1.00 37.36           C  
ATOM   1162  O   GLY A 153      14.659  70.135  47.801  1.00 37.11           O  
ATOM   1163  N   ARG A 154      14.070  68.210  46.731  1.00 37.56           N  
ATOM   1164  CA  ARG A 154      14.649  67.326  47.742  1.00 39.45           C  
ATOM   1165  C   ARG A 154      16.173  67.221  47.688  1.00 37.67           C  
ATOM   1166  O   ARG A 154      16.863  66.946  48.682  1.00 38.81           O  
ATOM   1167  CB  ARG A 154      14.111  65.931  47.622  1.00 42.13           C  
ATOM   1168  CG  ARG A 154      12.709  65.762  48.187  1.00 51.79           C  
ATOM   1169  CD  ARG A 154      12.629  64.264  48.411  1.00 61.16           C  
ATOM   1170  NE  ARG A 154      11.376  63.765  48.952  1.00 68.08           N  
ATOM   1171  CZ  ARG A 154      11.082  63.817  50.256  1.00 70.71           C  
ATOM   1172  NH1 ARG A 154      11.930  64.361  51.148  1.00 71.23           N  
ATOM   1173  NH2 ARG A 154       9.927  63.279  50.662  1.00 69.69           N  
ATOM   1174  N   LEU A 155      16.725  67.451  46.510  1.00 34.60           N  
ATOM   1175  CA  LEU A 155      18.157  67.401  46.294  1.00 29.78           C  
ATOM   1176  C   LEU A 155      18.587  68.776  45.867  1.00 29.79           C  
ATOM   1177  O   LEU A 155      17.843  69.442  45.147  1.00 29.65           O  
ATOM   1178  CB  LEU A 155      18.543  66.471  45.160  1.00 28.06           C  
ATOM   1179  CG  LEU A 155      18.403  64.983  45.302  1.00 23.62           C  
ATOM   1180  CD1 LEU A 155      18.676  64.374  43.950  1.00 23.44           C  
ATOM   1181  CD2 LEU A 155      19.302  64.482  46.397  1.00 21.76           C  
ATOM   1182  N   ASP A 156      19.808  69.162  46.218  1.00 28.30           N  
ATOM   1183  CA  ASP A 156      20.369  70.399  45.704  1.00 29.30           C  
ATOM   1184  C   ASP A 156      21.053  70.233  44.349  1.00 28.38           C  
ATOM   1185  O   ASP A 156      21.110  71.173  43.559  1.00 28.84           O  
ATOM   1186  CB  ASP A 156      21.370  70.949  46.684  1.00 31.82           C  
ATOM   1187  CG  ASP A 156      20.680  71.334  47.969  1.00 34.00           C  
ATOM   1188  OD1 ASP A 156      19.879  72.255  47.917  1.00 43.10           O  
ATOM   1189  OD2 ASP A 156      20.919  70.730  49.007  1.00 37.05           O  
ATOM   1190  N   ALA A 157      21.598  69.071  44.038  1.00 25.52           N  
ATOM   1191  CA  ALA A 157      22.319  68.830  42.806  1.00 25.68           C  
ATOM   1192  C   ALA A 157      22.393  67.321  42.633  1.00 25.99           C  
ATOM   1193  O   ALA A 157      22.175  66.528  43.579  1.00 26.52           O  
ATOM   1194  CB  ALA A 157      23.739  69.362  42.887  1.00 21.79           C  
ATOM   1195  N   ALA A 158      22.698  66.940  41.403  1.00 23.79           N  
ATOM   1196  CA  ALA A 158      22.900  65.555  41.074  1.00 24.18           C  
ATOM   1197  C   ALA A 158      24.223  65.464  40.321  1.00 24.34           C  
ATOM   1198  O   ALA A 158      24.493  66.312  39.466  1.00 24.24           O  
ATOM   1199  CB  ALA A 158      21.772  65.081  40.185  1.00 24.98           C  
ATOM   1200  N   LEU A 159      25.098  64.508  40.637  1.00 22.98           N  
ATOM   1201  CA  LEU A 159      26.298  64.325  39.836  1.00 23.30           C  
ATOM   1202  C   LEU A 159      25.955  63.272  38.814  1.00 24.71           C  
ATOM   1203  O   LEU A 159      25.627  62.144  39.193  1.00 25.18           O  
ATOM   1204  CB  LEU A 159      27.495  63.812  40.639  1.00 23.61           C  
ATOM   1205  CG  LEU A 159      28.855  63.629  39.958  1.00 20.40           C  
ATOM   1206  CD1 LEU A 159      29.343  64.950  39.387  1.00 21.77           C  
ATOM   1207  CD2 LEU A 159      29.858  63.128  40.990  1.00 21.43           C  
ATOM   1208  N   GLN A 160      26.067  63.600  37.535  1.00 24.83           N  
ATOM   1209  CA  GLN A 160      25.766  62.665  36.482  1.00 27.98           C  
ATOM   1210  C   GLN A 160      26.826  62.717  35.408  1.00 25.67           C  
ATOM   1211  O   GLN A 160      27.653  63.631  35.394  1.00 26.85           O  
ATOM   1212  CB  GLN A 160      24.448  62.996  35.818  1.00 34.39           C  
ATOM   1213  CG  GLN A 160      23.367  61.932  35.935  1.00 43.04           C  
ATOM   1214  CD  GLN A 160      22.552  62.119  37.186  1.00 45.97           C  
ATOM   1215  OE1 GLN A 160      21.763  63.059  37.242  1.00 51.56           O  
ATOM   1216  NE2 GLN A 160      22.635  61.260  38.194  1.00 49.40           N  
ATOM   1217  N   ASP A 161      26.809  61.724  34.527  1.00 22.09           N  
ATOM   1218  CA  ASP A 161      27.594  61.743  33.321  1.00 22.81           C  
ATOM   1219  C   ASP A 161      27.153  62.970  32.512  1.00 23.28           C  
ATOM   1220  O   ASP A 161      25.953  63.159  32.287  1.00 23.07           O  
ATOM   1221  CB  ASP A 161      27.346  60.492  32.481  1.00 22.27           C  
ATOM   1222  CG  ASP A 161      28.121  60.556  31.174  1.00 24.14           C  
ATOM   1223  OD1 ASP A 161      29.340  60.476  31.228  1.00 29.16           O  
ATOM   1224  OD2 ASP A 161      27.546  60.745  30.102  1.00 25.18           O  
ATOM   1225  N   GLU A 162      28.066  63.765  31.954  1.00 23.48           N  
ATOM   1226  CA  GLU A 162      27.693  65.023  31.302  1.00 25.07           C  
ATOM   1227  C   GLU A 162      26.865  64.836  30.049  1.00 24.42           C  
ATOM   1228  O   GLU A 162      25.794  65.415  29.872  1.00 25.46           O  
ATOM   1229  CB  GLU A 162      28.975  65.797  30.998  1.00 26.53           C  
ATOM   1230  CG  GLU A 162      28.851  67.139  30.275  1.00 27.46           C  
ATOM   1231  CD  GLU A 162      30.203  67.838  30.057  1.00 32.20           C  
ATOM   1232  OE1 GLU A 162      31.264  67.206  30.093  1.00 26.30           O  
ATOM   1233  OE2 GLU A 162      30.209  69.046  29.823  1.00 32.72           O  
ATOM   1234  N   VAL A 163      27.290  63.959  29.146  1.00 26.72           N  
ATOM   1235  CA  VAL A 163      26.566  63.784  27.910  1.00 26.27           C  
ATOM   1236  C   VAL A 163      25.229  63.123  28.202  1.00 27.68           C  
ATOM   1237  O   VAL A 163      24.226  63.483  27.596  1.00 27.58           O  
ATOM   1238  CB  VAL A 163      27.395  62.951  26.914  1.00 23.32           C  
ATOM   1239  CG1 VAL A 163      26.550  62.619  25.697  1.00 27.65           C  
ATOM   1240  CG2 VAL A 163      28.546  63.784  26.360  1.00 22.99           C  
ATOM   1241  N   ALA A 164      25.171  62.232  29.181  1.00 29.01           N  
ATOM   1242  CA  ALA A 164      23.920  61.571  29.495  1.00 30.47           C  
ATOM   1243  C   ALA A 164      22.904  62.558  30.059  1.00 31.24           C  
ATOM   1244  O   ALA A 164      21.743  62.550  29.652  1.00 34.02           O  
ATOM   1245  CB  ALA A 164      24.171  60.468  30.512  1.00 31.12           C  
ATOM   1246  N   ALA A 165      23.339  63.423  30.966  1.00 29.45           N  
ATOM   1247  CA  ALA A 165      22.520  64.473  31.516  1.00 28.38           C  
ATOM   1248  C   ALA A 165      22.087  65.426  30.424  1.00 29.30           C  
ATOM   1249  O   ALA A 165      20.943  65.882  30.447  1.00 30.70           O  
ATOM   1250  CB  ALA A 165      23.307  65.245  32.523  1.00 27.93           C  
ATOM   1251  N   SER A 166      22.938  65.755  29.452  1.00 30.63           N  
ATOM   1252  CA  SER A 166      22.553  66.654  28.370  1.00 36.41           C  
ATOM   1253  C   SER A 166      21.416  66.101  27.538  1.00 37.00           C  
ATOM   1254  O   SER A 166      20.299  66.629  27.519  1.00 36.47           O  
ATOM   1255  CB  SER A 166      23.704  66.937  27.396  1.00 38.04           C  
ATOM   1256  OG  SER A 166      24.771  67.624  28.026  1.00 48.50           O  
ATOM   1257  N   GLU A 167      21.704  64.937  26.982  1.00 37.70           N  
ATOM   1258  CA  GLU A 167      20.799  64.293  26.066  1.00 41.21           C  
ATOM   1259  C   GLU A 167      19.544  63.875  26.770  1.00 41.75           C  
ATOM   1260  O   GLU A 167      18.433  64.161  26.342  1.00 45.12           O  
ATOM   1261  CB  GLU A 167      21.465  63.076  25.462  1.00 40.64           C  
ATOM   1262  CG  GLU A 167      22.634  63.423  24.581  1.00 40.29           C  
ATOM   1263  CD  GLU A 167      22.221  64.076  23.284  1.00 43.39           C  
ATOM   1264  OE1 GLU A 167      21.408  63.523  22.561  1.00 46.01           O  
ATOM   1265  OE2 GLU A 167      22.731  65.132  22.949  1.00 45.39           O  
ATOM   1266  N   GLY A 168      19.689  63.317  27.949  1.00 42.38           N  
ATOM   1267  CA  GLY A 168      18.559  62.705  28.586  1.00 42.68           C  
ATOM   1268  C   GLY A 168      17.832  63.514  29.622  1.00 42.57           C  
ATOM   1269  O   GLY A 168      16.961  62.912  30.254  1.00 49.34           O  
ATOM   1270  N   PHE A 169      18.053  64.779  29.895  1.00 36.50           N  
ATOM   1271  CA  PHE A 169      17.248  65.400  30.923  1.00 33.75           C  
ATOM   1272  C   PHE A 169      17.297  66.849  30.632  1.00 35.55           C  
ATOM   1273  O   PHE A 169      16.216  67.403  30.553  1.00 37.98           O  
ATOM   1274  CB  PHE A 169      17.759  65.202  32.362  1.00 29.05           C  
ATOM   1275  CG  PHE A 169      17.044  66.022  33.444  1.00 29.66           C  
ATOM   1276  CD1 PHE A 169      15.733  65.766  33.804  1.00 32.55           C  
ATOM   1277  CD2 PHE A 169      17.698  67.053  34.090  1.00 30.70           C  
ATOM   1278  CE1 PHE A 169      15.096  66.514  34.791  1.00 31.28           C  
ATOM   1279  CE2 PHE A 169      17.068  67.797  35.072  1.00 30.25           C  
ATOM   1280  CZ  PHE A 169      15.762  67.529  35.437  1.00 32.27           C  
ATOM   1281  N   LEU A 170      18.429  67.489  30.419  1.00 33.36           N  
ATOM   1282  CA  LEU A 170      18.404  68.918  30.220  1.00 35.06           C  
ATOM   1283  C   LEU A 170      17.789  69.238  28.862  1.00 38.99           C  
ATOM   1284  O   LEU A 170      17.399  70.381  28.618  1.00 40.32           O  
ATOM   1285  CB  LEU A 170      19.829  69.453  30.333  1.00 32.91           C  
ATOM   1286  CG  LEU A 170      20.581  69.234  31.634  1.00 29.70           C  
ATOM   1287  CD1 LEU A 170      22.011  69.694  31.450  1.00 30.95           C  
ATOM   1288  CD2 LEU A 170      19.879  69.966  32.762  1.00 32.44           C  
ATOM   1289  N   LYS A 171      17.740  68.249  27.947  1.00 42.16           N  
ATOM   1290  CA  LYS A 171      17.045  68.446  26.691  1.00 45.86           C  
ATOM   1291  C   LYS A 171      15.581  68.028  26.792  1.00 48.66           C  
ATOM   1292  O   LYS A 171      14.744  68.394  25.965  1.00 52.35           O  
ATOM   1293  CB  LYS A 171      17.770  67.665  25.600  1.00 48.18           C  
ATOM   1294  CG  LYS A 171      19.029  68.380  25.088  1.00 50.54           C  
ATOM   1295  CD  LYS A 171      19.712  67.682  23.901  1.00 54.77           C  
ATOM   1296  CE  LYS A 171      20.883  68.580  23.430  1.00 61.28           C  
ATOM   1297  NZ  LYS A 171      21.666  68.067  22.304  1.00 63.50           N  
ATOM   1298  N   GLN A 172      15.187  67.282  27.817  1.00 50.65           N  
ATOM   1299  CA  GLN A 172      13.795  66.889  27.964  1.00 52.39           C  
ATOM   1300  C   GLN A 172      12.988  68.052  28.540  1.00 52.64           C  
ATOM   1301  O   GLN A 172      13.545  68.978  29.149  1.00 50.99           O  
ATOM   1302  CB  GLN A 172      13.646  65.658  28.900  1.00 55.75           C  
ATOM   1303  CG  GLN A 172      14.159  64.289  28.401  1.00 62.41           C  
ATOM   1304  CD  GLN A 172      14.603  64.211  26.936  1.00 67.52           C  
ATOM   1305  OE1 GLN A 172      13.814  64.217  25.988  1.00 71.65           O  
ATOM   1306  NE2 GLN A 172      15.890  64.155  26.661  1.00 69.65           N  
ATOM   1307  N   PRO A 173      11.641  68.037  28.440  1.00 54.36           N  
ATOM   1308  CA  PRO A 173      10.769  69.068  28.987  1.00 51.71           C  
ATOM   1309  C   PRO A 173      11.042  69.271  30.458  1.00 48.99           C  
ATOM   1310  O   PRO A 173      11.133  70.386  30.961  1.00 47.14           O  
ATOM   1311  CB  PRO A 173       9.380  68.550  28.695  1.00 54.90           C  
ATOM   1312  CG  PRO A 173       9.544  67.789  27.403  1.00 54.52           C  
ATOM   1313  CD  PRO A 173      10.827  67.046  27.708  1.00 56.54           C  
ATOM   1314  N   ALA A 174      11.220  68.149  31.152  1.00 49.31           N  
ATOM   1315  CA  ALA A 174      11.488  68.185  32.577  1.00 49.18           C  
ATOM   1316  C   ALA A 174      12.764  68.923  32.943  1.00 47.89           C  
ATOM   1317  O   ALA A 174      12.805  69.428  34.062  1.00 50.63           O  
ATOM   1318  CB  ALA A 174      11.601  66.777  33.144  1.00 49.65           C  
ATOM   1319  N   GLY A 175      13.770  69.046  32.073  1.00 43.00           N  
ATOM   1320  CA  GLY A 175      14.986  69.713  32.466  1.00 42.99           C  
ATOM   1321  C   GLY A 175      15.052  71.196  32.126  1.00 42.66           C  
ATOM   1322  O   GLY A 175      16.032  71.843  32.508  1.00 40.22           O  
ATOM   1323  N   LYS A 176      14.044  71.774  31.474  1.00 41.76           N  
ATOM   1324  CA  LYS A 176      14.106  73.151  31.025  1.00 41.82           C  
ATOM   1325  C   LYS A 176      14.480  74.163  32.083  1.00 39.53           C  
ATOM   1326  O   LYS A 176      15.155  75.115  31.721  1.00 39.55           O  
ATOM   1327  CB  LYS A 176      12.778  73.572  30.399  1.00 47.08           C  
ATOM   1328  CG  LYS A 176      11.624  73.398  31.374  1.00 59.61           C  
ATOM   1329  CD  LYS A 176      10.288  73.965  30.905  1.00 67.65           C  
ATOM   1330  CE  LYS A 176       9.170  73.514  31.861  1.00 70.75           C  
ATOM   1331  NZ  LYS A 176       9.429  73.858  33.254  1.00 71.22           N  
ATOM   1332  N   GLU A 177      14.145  73.965  33.353  1.00 36.46           N  
ATOM   1333  CA  GLU A 177      14.540  74.898  34.382  1.00 36.65           C  
ATOM   1334  C   GLU A 177      15.840  74.519  35.080  1.00 33.59           C  
ATOM   1335  O   GLU A 177      16.134  74.997  36.185  1.00 31.58           O  
ATOM   1336  CB  GLU A 177      13.455  74.989  35.424  1.00 43.63           C  
ATOM   1337  CG  GLU A 177      12.030  75.266  34.943  1.00 56.68           C  
ATOM   1338  CD  GLU A 177      11.906  76.500  34.061  1.00 65.19           C  
ATOM   1339  OE1 GLU A 177      12.230  77.595  34.541  1.00 69.42           O  
ATOM   1340  OE2 GLU A 177      11.502  76.349  32.899  1.00 68.65           O  
ATOM   1341  N   TYR A 178      16.665  73.656  34.495  1.00 31.38           N  
ATOM   1342  CA  TYR A 178      17.826  73.103  35.164  1.00 30.48           C  
ATOM   1343  C   TYR A 178      19.002  73.290  34.240  1.00 29.53           C  
ATOM   1344  O   TYR A 178      18.823  73.541  33.048  1.00 29.65           O  
ATOM   1345  CB  TYR A 178      17.620  71.593  35.479  1.00 30.58           C  
ATOM   1346  CG  TYR A 178      16.655  71.436  36.638  1.00 30.73           C  
ATOM   1347  CD1 TYR A 178      17.172  71.491  37.903  1.00 28.73           C  
ATOM   1348  CD2 TYR A 178      15.275  71.397  36.411  1.00 32.07           C  
ATOM   1349  CE1 TYR A 178      16.308  71.531  38.960  1.00 31.14           C  
ATOM   1350  CE2 TYR A 178      14.404  71.435  37.468  1.00 29.30           C  
ATOM   1351  CZ  TYR A 178      14.957  71.521  38.717  1.00 32.25           C  
ATOM   1352  OH  TYR A 178      14.144  71.661  39.804  1.00 41.50           O  
ATOM   1353  N   ALA A 179      20.202  73.203  34.807  1.00 28.09           N  
ATOM   1354  CA  ALA A 179      21.405  73.461  34.063  1.00 23.47           C  
ATOM   1355  C   ALA A 179      22.586  72.867  34.809  1.00 23.07           C  
ATOM   1356  O   ALA A 179      22.558  72.635  36.037  1.00 23.81           O  
ATOM   1357  CB  ALA A 179      21.638  74.960  33.965  1.00 21.72           C  
ATOM   1358  N   PHE A 180      23.656  72.696  34.040  1.00 22.35           N  
ATOM   1359  CA  PHE A 180      24.938  72.287  34.582  1.00 22.60           C  
ATOM   1360  C   PHE A 180      25.425  73.301  35.570  1.00 22.28           C  
ATOM   1361  O   PHE A 180      25.403  74.491  35.262  1.00 23.46           O  
ATOM   1362  CB  PHE A 180      25.907  72.152  33.444  1.00 20.56           C  
ATOM   1363  CG  PHE A 180      25.717  70.858  32.643  1.00 22.45           C  
ATOM   1364  CD1 PHE A 180      25.479  69.638  33.274  1.00 21.91           C  
ATOM   1365  CD2 PHE A 180      25.835  70.903  31.273  1.00 24.15           C  
ATOM   1366  CE1 PHE A 180      25.375  68.501  32.502  1.00 20.55           C  
ATOM   1367  CE2 PHE A 180      25.726  69.750  30.521  1.00 24.54           C  
ATOM   1368  CZ  PHE A 180      25.498  68.542  31.135  1.00 22.28           C  
ATOM   1369  N   ALA A 181      25.778  72.902  36.773  1.00 21.73           N  
ATOM   1370  CA  ALA A 181      26.304  73.847  37.719  1.00 21.55           C  
ATOM   1371  C   ALA A 181      27.818  73.678  37.793  1.00 23.68           C  
ATOM   1372  O   ALA A 181      28.348  72.715  38.364  1.00 25.81           O  
ATOM   1373  CB  ALA A 181      25.689  73.623  39.100  1.00 20.04           C  
ATOM   1374  N   GLY A 182      28.534  74.661  37.235  1.00 23.85           N  
ATOM   1375  CA  GLY A 182      29.982  74.689  37.241  1.00 21.36           C  
ATOM   1376  C   GLY A 182      30.549  73.870  36.099  1.00 20.47           C  
ATOM   1377  O   GLY A 182      29.806  73.410  35.218  1.00 22.23           O  
ATOM   1378  N   PRO A 183      31.872  73.671  36.051  1.00 17.52           N  
ATOM   1379  CA  PRO A 183      32.506  72.925  34.965  1.00 20.99           C  
ATOM   1380  C   PRO A 183      32.458  71.403  35.215  1.00 22.90           C  
ATOM   1381  O   PRO A 183      32.155  70.939  36.331  1.00 22.89           O  
ATOM   1382  CB  PRO A 183      33.885  73.529  34.942  1.00 21.14           C  
ATOM   1383  CG  PRO A 183      34.138  73.698  36.431  1.00 20.19           C  
ATOM   1384  CD  PRO A 183      32.810  74.204  36.998  1.00 15.38           C  
ATOM   1385  N   SER A 184      32.770  70.571  34.240  1.00 24.95           N  
ATOM   1386  CA  SER A 184      32.754  69.151  34.470  1.00 26.86           C  
ATOM   1387  C   SER A 184      33.867  68.711  35.422  1.00 28.46           C  
ATOM   1388  O   SER A 184      34.854  69.420  35.692  1.00 27.33           O  
ATOM   1389  CB  SER A 184      32.853  68.505  33.131  1.00 25.97           C  
ATOM   1390  OG  SER A 184      34.035  68.996  32.575  1.00 29.65           O  
ATOM   1391  N   VAL A 185      33.636  67.564  36.055  1.00 29.95           N  
ATOM   1392  CA  VAL A 185      34.606  67.026  36.970  1.00 32.49           C  
ATOM   1393  C   VAL A 185      35.400  65.951  36.249  1.00 33.07           C  
ATOM   1394  O   VAL A 185      34.890  64.988  35.681  1.00 31.06           O  
ATOM   1395  CB  VAL A 185      33.834  66.531  38.220  1.00 32.30           C  
ATOM   1396  CG1 VAL A 185      32.887  65.379  38.001  1.00 38.77           C  
ATOM   1397  CG2 VAL A 185      34.903  66.083  39.167  1.00 36.53           C  
ATOM   1398  N   LYS A 186      36.679  66.188  36.138  1.00 33.48           N  
ATOM   1399  CA  LYS A 186      37.528  65.252  35.456  1.00 36.63           C  
ATOM   1400  C   LYS A 186      38.279  64.542  36.544  1.00 37.91           C  
ATOM   1401  O   LYS A 186      38.721  65.205  37.482  1.00 42.31           O  
ATOM   1402  CB  LYS A 186      38.501  65.978  34.568  1.00 35.66           C  
ATOM   1403  CG  LYS A 186      37.813  66.853  33.563  1.00 40.27           C  
ATOM   1404  CD  LYS A 186      38.814  67.818  32.942  1.00 47.49           C  
ATOM   1405  CE  LYS A 186      38.255  68.487  31.685  1.00 51.22           C  
ATOM   1406  NZ  LYS A 186      38.311  67.570  30.547  1.00 58.23           N  
ATOM   1407  N   ASP A 187      38.351  63.222  36.475  1.00 38.49           N  
ATOM   1408  CA  ASP A 187      39.171  62.425  37.355  1.00 39.69           C  
ATOM   1409  C   ASP A 187      39.454  61.098  36.669  1.00 39.41           C  
ATOM   1410  O   ASP A 187      38.579  60.231  36.608  1.00 40.44           O  
ATOM   1411  CB  ASP A 187      38.462  62.142  38.658  1.00 43.48           C  
ATOM   1412  CG  ASP A 187      39.494  61.898  39.742  1.00 48.49           C  
ATOM   1413  OD1 ASP A 187      40.062  60.809  39.814  1.00 49.17           O  
ATOM   1414  OD2 ASP A 187      39.728  62.829  40.511  1.00 55.78           O  
ATOM   1415  N   LYS A 188      40.661  60.849  36.176  1.00 39.61           N  
ATOM   1416  CA  LYS A 188      41.042  59.621  35.464  1.00 38.22           C  
ATOM   1417  C   LYS A 188      40.791  58.373  36.297  1.00 33.37           C  
ATOM   1418  O   LYS A 188      40.332  57.358  35.793  1.00 33.08           O  
ATOM   1419  CB  LYS A 188      42.514  59.868  35.059  1.00 43.72           C  
ATOM   1420  CG  LYS A 188      43.555  58.808  34.728  1.00 52.15           C  
ATOM   1421  CD  LYS A 188      43.194  57.926  33.548  1.00 60.05           C  
ATOM   1422  CE  LYS A 188      44.354  56.999  33.190  1.00 63.87           C  
ATOM   1423  NZ  LYS A 188      44.124  56.437  31.868  1.00 68.17           N  
ATOM   1424  N   LYS A 189      40.954  58.463  37.602  1.00 32.63           N  
ATOM   1425  CA  LYS A 189      40.719  57.328  38.440  1.00 34.44           C  
ATOM   1426  C   LYS A 189      39.297  56.881  38.397  1.00 36.32           C  
ATOM   1427  O   LYS A 189      39.129  55.676  38.460  1.00 37.87           O  
ATOM   1428  CB  LYS A 189      41.066  57.599  39.895  1.00 37.70           C  
ATOM   1429  CG  LYS A 189      40.566  56.510  40.829  1.00 43.67           C  
ATOM   1430  CD  LYS A 189      41.232  56.406  42.182  1.00 53.87           C  
ATOM   1431  CE  LYS A 189      41.441  57.709  42.946  1.00 55.23           C  
ATOM   1432  NZ  LYS A 189      41.798  57.357  44.312  1.00 58.49           N  
ATOM   1433  N   TYR A 190      38.273  57.736  38.277  1.00 35.91           N  
ATOM   1434  CA  TYR A 190      36.906  57.223  38.345  1.00 32.90           C  
ATOM   1435  C   TYR A 190      36.238  57.254  37.007  1.00 30.44           C  
ATOM   1436  O   TYR A 190      35.425  56.387  36.687  1.00 32.84           O  
ATOM   1437  CB  TYR A 190      36.068  58.027  39.332  1.00 34.31           C  
ATOM   1438  CG  TYR A 190      36.679  58.150  40.727  1.00 34.87           C  
ATOM   1439  CD1 TYR A 190      37.535  59.200  40.995  1.00 34.45           C  
ATOM   1440  CD2 TYR A 190      36.410  57.222  41.714  1.00 35.64           C  
ATOM   1441  CE1 TYR A 190      38.121  59.341  42.230  1.00 33.57           C  
ATOM   1442  CE2 TYR A 190      36.994  57.359  42.957  1.00 35.41           C  
ATOM   1443  CZ  TYR A 190      37.851  58.413  43.199  1.00 36.41           C  
ATOM   1444  OH  TYR A 190      38.473  58.542  44.433  1.00 41.66           O  
ATOM   1445  N   PHE A 191      36.637  58.225  36.181  1.00 28.03           N  
ATOM   1446  CA  PHE A 191      35.974  58.441  34.901  1.00 27.58           C  
ATOM   1447  C   PHE A 191      36.811  58.041  33.717  1.00 28.09           C  
ATOM   1448  O   PHE A 191      36.280  58.015  32.612  1.00 30.10           O  
ATOM   1449  CB  PHE A 191      35.527  59.959  34.754  1.00 25.48           C  
ATOM   1450  CG  PHE A 191      34.702  60.384  35.980  1.00 28.87           C  
ATOM   1451  CD1 PHE A 191      33.642  59.605  36.447  1.00 29.58           C  
ATOM   1452  CD2 PHE A 191      35.067  61.497  36.714  1.00 31.50           C  
ATOM   1453  CE1 PHE A 191      32.970  59.924  37.616  1.00 29.88           C  
ATOM   1454  CE2 PHE A 191      34.383  61.813  37.877  1.00 29.97           C  
ATOM   1455  CZ  PHE A 191      33.343  61.030  38.331  1.00 28.86           C  
ATOM   1456  N   GLY A 192      38.095  57.706  33.936  1.00 29.68           N  
ATOM   1457  CA  GLY A 192      39.017  57.394  32.869  1.00 28.78           C  
ATOM   1458  C   GLY A 192      39.520  58.646  32.189  1.00 30.65           C  
ATOM   1459  O   GLY A 192      39.201  59.765  32.601  1.00 34.04           O  
ATOM   1460  N   ASP A 193      40.239  58.488  31.094  1.00 31.76           N  
ATOM   1461  CA  ASP A 193      40.838  59.610  30.409  1.00 32.50           C  
ATOM   1462  C   ASP A 193      40.253  59.838  29.027  1.00 29.25           C  
ATOM   1463  O   ASP A 193      40.959  59.877  28.020  1.00 30.42           O  
ATOM   1464  CB  ASP A 193      42.316  59.339  30.336  1.00 38.58           C  
ATOM   1465  CG  ASP A 193      43.049  60.614  30.645  1.00 46.19           C  
ATOM   1466  OD1 ASP A 193      43.238  61.400  29.720  1.00 53.39           O  
ATOM   1467  OD2 ASP A 193      43.397  60.830  31.808  1.00 53.46           O  
ATOM   1468  N   GLY A 194      38.942  60.018  28.969  1.00 26.80           N  
ATOM   1469  CA  GLY A 194      38.248  60.123  27.712  1.00 24.42           C  
ATOM   1470  C   GLY A 194      37.961  58.710  27.240  1.00 22.49           C  
ATOM   1471  O   GLY A 194      38.124  57.746  27.993  1.00 24.37           O  
ATOM   1472  N   THR A 195      37.497  58.570  26.017  1.00 22.30           N  
ATOM   1473  CA  THR A 195      37.226  57.277  25.438  1.00 21.33           C  
ATOM   1474  C   THR A 195      38.231  57.098  24.316  1.00 21.07           C  
ATOM   1475  O   THR A 195      38.734  58.117  23.806  1.00 22.45           O  
ATOM   1476  CB  THR A 195      35.805  57.209  24.857  1.00 22.80           C  
ATOM   1477  OG1 THR A 195      35.644  58.161  23.809  1.00 23.41           O  
ATOM   1478  CG2 THR A 195      34.816  57.499  25.935  1.00 21.58           C  
ATOM   1479  N   GLY A 196      38.486  55.890  23.824  1.00 18.48           N  
ATOM   1480  CA  GLY A 196      39.458  55.712  22.769  1.00 17.92           C  
ATOM   1481  C   GLY A 196      39.106  54.471  22.013  1.00 20.22           C  
ATOM   1482  O   GLY A 196      38.196  53.747  22.430  1.00 21.64           O  
ATOM   1483  N   VAL A 197      39.754  54.230  20.874  1.00 19.42           N  
ATOM   1484  CA  VAL A 197      39.555  53.019  20.086  1.00 18.01           C  
ATOM   1485  C   VAL A 197      40.286  51.909  20.897  1.00 20.46           C  
ATOM   1486  O   VAL A 197      41.480  52.058  21.202  1.00 23.59           O  
ATOM   1487  CB  VAL A 197      40.187  53.210  18.679  1.00 18.07           C  
ATOM   1488  CG1 VAL A 197      39.959  51.979  17.834  1.00 17.87           C  
ATOM   1489  CG2 VAL A 197      39.570  54.367  17.932  1.00 15.62           C  
ATOM   1490  N   GLY A 198      39.627  50.844  21.351  1.00 17.56           N  
ATOM   1491  CA  GLY A 198      40.253  49.738  22.044  1.00 19.78           C  
ATOM   1492  C   GLY A 198      40.915  48.816  21.018  1.00 21.20           C  
ATOM   1493  O   GLY A 198      40.301  48.397  20.023  1.00 22.04           O  
ATOM   1494  N   LEU A 199      42.159  48.433  21.254  1.00 21.78           N  
ATOM   1495  CA  LEU A 199      42.969  47.687  20.314  1.00 22.17           C  
ATOM   1496  C   LEU A 199      43.762  46.628  21.073  1.00 23.98           C  
ATOM   1497  O   LEU A 199      43.988  46.751  22.277  1.00 24.71           O  
ATOM   1498  CB  LEU A 199      43.941  48.623  19.637  1.00 22.61           C  
ATOM   1499  CG  LEU A 199      43.406  49.707  18.714  1.00 22.72           C  
ATOM   1500  CD1 LEU A 199      44.409  50.810  18.576  1.00 27.19           C  
ATOM   1501  CD2 LEU A 199      43.118  49.130  17.348  1.00 22.30           C  
ATOM   1502  N   ARG A 200      44.225  45.551  20.452  1.00 25.67           N  
ATOM   1503  CA  ARG A 200      45.104  44.537  21.071  1.00 25.89           C  
ATOM   1504  C   ARG A 200      46.414  45.197  21.422  1.00 25.55           C  
ATOM   1505  O   ARG A 200      46.944  45.947  20.631  1.00 24.76           O  
ATOM   1506  CB  ARG A 200      45.357  43.384  20.099  1.00 23.94           C  
ATOM   1507  CG  ARG A 200      44.166  42.461  20.266  1.00 24.95           C  
ATOM   1508  CD  ARG A 200      44.157  41.194  19.456  1.00 19.34           C  
ATOM   1509  NE  ARG A 200      44.263  41.512  18.054  1.00 19.21           N  
ATOM   1510  CZ  ARG A 200      43.236  41.564  17.219  1.00 17.70           C  
ATOM   1511  NH1 ARG A 200      41.978  41.326  17.623  1.00 20.51           N  
ATOM   1512  NH2 ARG A 200      43.505  41.817  15.943  1.00 17.78           N  
ATOM   1513  N   LYS A 201      47.008  44.916  22.573  1.00 26.35           N  
ATOM   1514  CA  LYS A 201      48.257  45.532  22.976  1.00 29.67           C  
ATOM   1515  C   LYS A 201      49.389  45.363  21.982  1.00 31.19           C  
ATOM   1516  O   LYS A 201      50.249  46.229  21.814  1.00 35.37           O  
ATOM   1517  CB  LYS A 201      48.766  44.935  24.261  1.00 31.47           C  
ATOM   1518  CG  LYS A 201      48.050  45.522  25.450  1.00 37.06           C  
ATOM   1519  CD  LYS A 201      49.179  45.675  26.459  1.00 41.00           C  
ATOM   1520  CE  LYS A 201      48.797  46.461  27.682  1.00 42.96           C  
ATOM   1521  NZ  LYS A 201      47.818  45.707  28.434  1.00 46.14           N  
ATOM   1522  N   ASP A 202      49.324  44.303  21.227  1.00 33.46           N  
ATOM   1523  CA  ASP A 202      50.323  43.894  20.236  1.00 34.40           C  
ATOM   1524  C   ASP A 202      50.182  44.562  18.901  1.00 31.20           C  
ATOM   1525  O   ASP A 202      51.083  44.552  18.089  1.00 28.14           O  
ATOM   1526  CB  ASP A 202      50.245  42.399  20.076  1.00 43.33           C  
ATOM   1527  CG  ASP A 202      48.784  41.874  20.126  1.00 50.29           C  
ATOM   1528  OD1 ASP A 202      48.205  41.667  21.221  1.00 50.73           O  
ATOM   1529  OD2 ASP A 202      48.204  41.762  19.057  1.00 54.02           O  
ATOM   1530  N   ASP A 203      49.058  45.201  18.647  1.00 31.82           N  
ATOM   1531  CA  ASP A 203      48.818  45.752  17.334  1.00 32.56           C  
ATOM   1532  C   ASP A 203      49.235  47.195  17.224  1.00 32.96           C  
ATOM   1533  O   ASP A 203      48.433  48.108  16.957  1.00 35.60           O  
ATOM   1534  CB  ASP A 203      47.307  45.559  16.955  1.00 31.03           C  
ATOM   1535  CG  ASP A 203      46.980  44.129  16.565  1.00 33.73           C  
ATOM   1536  OD1 ASP A 203      47.813  43.234  16.621  1.00 35.90           O  
ATOM   1537  OD2 ASP A 203      45.870  43.881  16.145  1.00 37.35           O  
ATOM   1538  N   THR A 204      50.554  47.371  17.329  1.00 31.91           N  
ATOM   1539  CA  THR A 204      51.051  48.729  17.302  1.00 30.61           C  
ATOM   1540  C   THR A 204      50.950  49.388  15.942  1.00 28.73           C  
ATOM   1541  O   THR A 204      50.725  50.585  15.959  1.00 32.12           O  
ATOM   1542  CB  THR A 204      52.494  48.717  17.823  1.00 34.36           C  
ATOM   1543  OG1 THR A 204      53.272  47.817  17.077  1.00 38.51           O  
ATOM   1544  CG2 THR A 204      52.546  48.213  19.254  1.00 33.65           C  
ATOM   1545  N   GLU A 205      51.050  48.795  14.753  1.00 28.58           N  
ATOM   1546  CA  GLU A 205      50.872  49.538  13.519  1.00 31.15           C  
ATOM   1547  C   GLU A 205      49.431  50.012  13.380  1.00 31.39           C  
ATOM   1548  O   GLU A 205      49.199  51.136  12.917  1.00 28.22           O  
ATOM   1549  CB  GLU A 205      51.187  48.705  12.309  1.00 38.12           C  
ATOM   1550  CG  GLU A 205      52.609  48.196  12.330  1.00 50.85           C  
ATOM   1551  CD  GLU A 205      52.612  46.710  12.023  1.00 58.15           C  
ATOM   1552  OE1 GLU A 205      52.423  45.913  12.952  1.00 63.64           O  
ATOM   1553  OE2 GLU A 205      52.753  46.355  10.849  1.00 58.43           O  
ATOM   1554  N   LEU A 206      48.456  49.201  13.824  1.00 28.22           N  
ATOM   1555  CA  LEU A 206      47.058  49.594  13.790  1.00 28.25           C  
ATOM   1556  C   LEU A 206      46.832  50.750  14.755  1.00 26.39           C  
ATOM   1557  O   LEU A 206      46.170  51.707  14.356  1.00 27.53           O  
ATOM   1558  CB  LEU A 206      46.171  48.414  14.156  1.00 27.45           C  
ATOM   1559  CG  LEU A 206      44.659  48.578  13.890  1.00 26.08           C  
ATOM   1560  CD1 LEU A 206      44.410  48.961  12.433  1.00 22.33           C  
ATOM   1561  CD2 LEU A 206      43.945  47.288  14.260  1.00 26.81           C  
ATOM   1562  N   LYS A 207      47.376  50.777  15.965  1.00 25.84           N  
ATOM   1563  CA  LYS A 207      47.286  51.974  16.807  1.00 28.59           C  
ATOM   1564  C   LYS A 207      47.874  53.245  16.182  1.00 30.25           C  
ATOM   1565  O   LYS A 207      47.289  54.337  16.297  1.00 30.52           O  
ATOM   1566  CB  LYS A 207      47.979  51.729  18.163  1.00 28.35           C  
ATOM   1567  CG  LYS A 207      47.818  52.937  19.055  1.00 28.53           C  
ATOM   1568  CD  LYS A 207      48.384  52.725  20.430  1.00 30.44           C  
ATOM   1569  CE  LYS A 207      48.926  54.072  20.931  1.00 29.83           C  
ATOM   1570  NZ  LYS A 207      47.913  55.083  21.163  1.00 32.10           N  
ATOM   1571  N   ALA A 208      49.031  53.102  15.521  1.00 28.72           N  
ATOM   1572  CA  ALA A 208      49.702  54.194  14.861  1.00 25.77           C  
ATOM   1573  C   ALA A 208      48.833  54.743  13.754  1.00 24.96           C  
ATOM   1574  O   ALA A 208      48.698  55.946  13.557  1.00 26.74           O  
ATOM   1575  CB  ALA A 208      50.983  53.660  14.293  1.00 26.14           C  
ATOM   1576  N   ALA A 209      48.233  53.839  12.998  1.00 22.79           N  
ATOM   1577  CA  ALA A 209      47.358  54.194  11.911  1.00 23.16           C  
ATOM   1578  C   ALA A 209      46.116  54.922  12.427  1.00 23.12           C  
ATOM   1579  O   ALA A 209      45.804  55.977  11.865  1.00 26.30           O  
ATOM   1580  CB  ALA A 209      46.987  52.917  11.165  1.00 21.83           C  
ATOM   1581  N   PHE A 210      45.415  54.460  13.471  1.00 23.36           N  
ATOM   1582  CA  PHE A 210      44.320  55.207  14.103  1.00 25.09           C  
ATOM   1583  C   PHE A 210      44.797  56.531  14.696  1.00 26.57           C  
ATOM   1584  O   PHE A 210      44.151  57.573  14.496  1.00 29.74           O  
ATOM   1585  CB  PHE A 210      43.644  54.438  15.252  1.00 22.77           C  
ATOM   1586  CG  PHE A 210      42.585  53.479  14.734  1.00 26.37           C  
ATOM   1587  CD1 PHE A 210      41.393  53.960  14.216  1.00 26.82           C  
ATOM   1588  CD2 PHE A 210      42.789  52.106  14.784  1.00 26.89           C  
ATOM   1589  CE1 PHE A 210      40.407  53.089  13.747  1.00 24.90           C  
ATOM   1590  CE2 PHE A 210      41.796  51.248  14.309  1.00 27.36           C  
ATOM   1591  CZ  PHE A 210      40.601  51.727  13.792  1.00 25.44           C  
ATOM   1592  N   ASP A 211      45.916  56.591  15.410  1.00 26.60           N  
ATOM   1593  CA  ASP A 211      46.385  57.852  15.954  1.00 27.15           C  
ATOM   1594  C   ASP A 211      46.700  58.901  14.895  1.00 27.83           C  
ATOM   1595  O   ASP A 211      46.269  60.060  15.033  1.00 25.90           O  
ATOM   1596  CB  ASP A 211      47.604  57.563  16.833  1.00 26.29           C  
ATOM   1597  CG  ASP A 211      47.248  56.899  18.156  1.00 27.08           C  
ATOM   1598  OD1 ASP A 211      46.078  56.815  18.527  1.00 27.92           O  
ATOM   1599  OD2 ASP A 211      48.157  56.468  18.845  1.00 30.51           O  
ATOM   1600  N   LYS A 212      47.368  58.497  13.804  1.00 27.94           N  
ATOM   1601  CA  LYS A 212      47.686  59.410  12.717  1.00 30.60           C  
ATOM   1602  C   LYS A 212      46.407  59.999  12.130  1.00 29.26           C  
ATOM   1603  O   LYS A 212      46.215  61.217  12.118  1.00 29.45           O  
ATOM   1604  CB  LYS A 212      48.485  58.664  11.634  1.00 33.32           C  
ATOM   1605  CG  LYS A 212      48.986  59.537  10.468  1.00 37.77           C  
ATOM   1606  CD  LYS A 212      49.742  58.714   9.444  1.00 39.13           C  
ATOM   1607  CE  LYS A 212      50.388  59.617   8.410  1.00 43.13           C  
ATOM   1608  NZ  LYS A 212      49.574  59.818   7.216  1.00 47.22           N  
ATOM   1609  N   ALA A 213      45.470  59.126  11.786  1.00 28.13           N  
ATOM   1610  CA  ALA A 213      44.211  59.547  11.205  1.00 27.40           C  
ATOM   1611  C   ALA A 213      43.406  60.445  12.136  1.00 26.26           C  
ATOM   1612  O   ALA A 213      42.849  61.447  11.670  1.00 28.53           O  
ATOM   1613  CB  ALA A 213      43.388  58.322  10.855  1.00 28.32           C  
ATOM   1614  N   LEU A 214      43.375  60.189  13.440  1.00 25.81           N  
ATOM   1615  CA  LEU A 214      42.655  61.045  14.338  1.00 25.91           C  
ATOM   1616  C   LEU A 214      43.323  62.430  14.394  1.00 28.72           C  
ATOM   1617  O   LEU A 214      42.605  63.428  14.319  1.00 26.77           O  
ATOM   1618  CB  LEU A 214      42.600  60.399  15.721  1.00 26.10           C  
ATOM   1619  CG  LEU A 214      41.934  61.274  16.818  1.00 28.76           C  
ATOM   1620  CD1 LEU A 214      40.471  61.526  16.458  1.00 27.22           C  
ATOM   1621  CD2 LEU A 214      42.075  60.612  18.175  1.00 29.81           C  
ATOM   1622  N   THR A 215      44.650  62.599  14.464  1.00 32.22           N  
ATOM   1623  CA  THR A 215      45.282  63.915  14.485  1.00 33.15           C  
ATOM   1624  C   THR A 215      44.990  64.725  13.241  1.00 32.88           C  
ATOM   1625  O   THR A 215      44.659  65.914  13.334  1.00 33.64           O  
ATOM   1626  CB  THR A 215      46.777  63.768  14.637  1.00 35.14           C  
ATOM   1627  OG1 THR A 215      46.977  63.006  15.830  1.00 36.30           O  
ATOM   1628  CG2 THR A 215      47.481  65.136  14.733  1.00 39.33           C  
ATOM   1629  N   GLU A 216      45.062  64.061  12.092  1.00 33.97           N  
ATOM   1630  CA  GLU A 216      44.709  64.652  10.817  1.00 36.33           C  
ATOM   1631  C   GLU A 216      43.304  65.213  10.742  1.00 37.55           C  
ATOM   1632  O   GLU A 216      43.114  66.378  10.357  1.00 36.18           O  
ATOM   1633  CB  GLU A 216      44.838  63.640   9.715  1.00 38.81           C  
ATOM   1634  CG  GLU A 216      46.323  63.407   9.467  1.00 45.03           C  
ATOM   1635  CD  GLU A 216      46.654  62.381   8.399  1.00 48.40           C  
ATOM   1636  OE1 GLU A 216      45.785  62.005   7.599  1.00 50.92           O  
ATOM   1637  OE2 GLU A 216      47.813  61.968   8.400  1.00 49.81           O  
ATOM   1638  N   LEU A 217      42.294  64.412  11.110  1.00 35.83           N  
ATOM   1639  CA  LEU A 217      40.945  64.912  11.007  1.00 30.91           C  
ATOM   1640  C   LEU A 217      40.705  65.925  12.089  1.00 30.18           C  
ATOM   1641  O   LEU A 217      39.813  66.752  11.918  1.00 31.92           O  
ATOM   1642  CB  LEU A 217      39.923  63.754  11.065  1.00 30.58           C  
ATOM   1643  CG  LEU A 217      39.727  62.842  12.244  1.00 28.48           C  
ATOM   1644  CD1 LEU A 217      38.727  63.426  13.192  1.00 29.39           C  
ATOM   1645  CD2 LEU A 217      39.201  61.494  11.757  1.00 29.04           C  
ATOM   1646  N   ARG A 218      41.427  65.947  13.197  1.00 29.70           N  
ATOM   1647  CA  ARG A 218      41.262  67.026  14.133  1.00 33.81           C  
ATOM   1648  C   ARG A 218      41.871  68.306  13.578  1.00 40.62           C  
ATOM   1649  O   ARG A 218      41.209  69.357  13.590  1.00 42.35           O  
ATOM   1650  CB  ARG A 218      41.929  66.725  15.424  1.00 32.90           C  
ATOM   1651  CG  ARG A 218      40.994  65.910  16.266  1.00 35.75           C  
ATOM   1652  CD  ARG A 218      41.599  65.617  17.624  1.00 38.18           C  
ATOM   1653  NE  ARG A 218      41.860  66.801  18.437  1.00 44.48           N  
ATOM   1654  CZ  ARG A 218      40.880  67.611  18.862  1.00 46.47           C  
ATOM   1655  NH1 ARG A 218      39.597  67.401  18.560  1.00 45.97           N  
ATOM   1656  NH2 ARG A 218      41.188  68.612  19.682  1.00 48.56           N  
ATOM   1657  N   GLN A 219      43.091  68.231  13.014  1.00 42.31           N  
ATOM   1658  CA  GLN A 219      43.769  69.400  12.471  1.00 43.39           C  
ATOM   1659  C   GLN A 219      43.092  70.062  11.296  1.00 41.69           C  
ATOM   1660  O   GLN A 219      43.072  71.280  11.257  1.00 45.27           O  
ATOM   1661  CB  GLN A 219      45.181  69.066  12.052  1.00 46.33           C  
ATOM   1662  CG  GLN A 219      46.003  68.925  13.325  1.00 56.61           C  
ATOM   1663  CD  GLN A 219      47.517  68.917  13.106  1.00 63.33           C  
ATOM   1664  OE1 GLN A 219      48.067  68.178  12.290  1.00 66.58           O  
ATOM   1665  NE2 GLN A 219      48.285  69.724  13.831  1.00 67.29           N  
ATOM   1666  N   ASP A 220      42.502  69.366  10.344  1.00 39.53           N  
ATOM   1667  CA  ASP A 220      41.816  70.003   9.245  1.00 37.10           C  
ATOM   1668  C   ASP A 220      40.372  70.412   9.564  1.00 38.84           C  
ATOM   1669  O   ASP A 220      39.604  70.748   8.655  1.00 39.32           O  
ATOM   1670  CB  ASP A 220      41.838  69.046   8.062  1.00 39.43           C  
ATOM   1671  CG  ASP A 220      41.018  67.756   8.176  1.00 39.55           C  
ATOM   1672  OD1 ASP A 220      40.410  67.489   9.203  1.00 41.08           O  
ATOM   1673  OD2 ASP A 220      40.965  67.017   7.204  1.00 40.34           O  
ATOM   1674  N   GLY A 221      39.901  70.243  10.802  1.00 38.05           N  
ATOM   1675  CA  GLY A 221      38.577  70.714  11.195  1.00 36.83           C  
ATOM   1676  C   GLY A 221      37.430  69.738  11.008  1.00 37.71           C  
ATOM   1677  O   GLY A 221      36.308  70.010  11.440  1.00 36.98           O  
ATOM   1678  N   THR A 222      37.659  68.562  10.420  1.00 36.76           N  
ATOM   1679  CA  THR A 222      36.604  67.568  10.226  1.00 33.27           C  
ATOM   1680  C   THR A 222      36.022  67.180  11.583  1.00 32.25           C  
ATOM   1681  O   THR A 222      34.804  67.056  11.690  1.00 32.95           O  
ATOM   1682  CB  THR A 222      37.185  66.336   9.550  1.00 32.08           C  
ATOM   1683  OG1 THR A 222      37.892  66.801   8.418  1.00 34.46           O  
ATOM   1684  CG2 THR A 222      36.151  65.366   9.079  1.00 35.27           C  
ATOM   1685  N   TYR A 223      36.819  67.067  12.654  1.00 29.13           N  
ATOM   1686  CA  TYR A 223      36.321  66.674  13.950  1.00 29.54           C  
ATOM   1687  C   TYR A 223      35.211  67.617  14.397  1.00 33.21           C  
ATOM   1688  O   TYR A 223      34.155  67.150  14.855  1.00 32.57           O  
ATOM   1689  CB  TYR A 223      37.466  66.678  14.974  1.00 26.47           C  
ATOM   1690  CG  TYR A 223      37.078  66.176  16.365  1.00 25.72           C  
ATOM   1691  CD1 TYR A 223      36.334  66.968  17.222  1.00 21.91           C  
ATOM   1692  CD2 TYR A 223      37.433  64.904  16.756  1.00 24.71           C  
ATOM   1693  CE1 TYR A 223      35.940  66.512  18.445  1.00 19.14           C  
ATOM   1694  CE2 TYR A 223      37.036  64.437  17.987  1.00 19.22           C  
ATOM   1695  CZ  TYR A 223      36.298  65.238  18.798  1.00 19.57           C  
ATOM   1696  OH  TYR A 223      35.900  64.774  20.008  1.00 21.71           O  
ATOM   1697  N   ASP A 224      35.440  68.934  14.241  1.00 34.34           N  
ATOM   1698  CA  ASP A 224      34.455  69.915  14.688  1.00 34.77           C  
ATOM   1699  C   ASP A 224      33.183  69.931  13.894  1.00 31.76           C  
ATOM   1700  O   ASP A 224      32.126  70.049  14.496  1.00 34.43           O  
ATOM   1701  CB  ASP A 224      35.000  71.322  14.664  1.00 38.94           C  
ATOM   1702  CG  ASP A 224      36.136  71.493  15.658  1.00 42.83           C  
ATOM   1703  OD1 ASP A 224      36.046  71.027  16.803  1.00 42.38           O  
ATOM   1704  OD2 ASP A 224      37.131  72.099  15.261  1.00 50.46           O  
ATOM   1705  N   LYS A 225      33.277  69.753  12.579  1.00 33.00           N  
ATOM   1706  CA  LYS A 225      32.129  69.658  11.692  1.00 33.66           C  
ATOM   1707  C   LYS A 225      31.342  68.435  12.113  1.00 36.46           C  
ATOM   1708  O   LYS A 225      30.126  68.533  12.293  1.00 40.92           O  
ATOM   1709  CB  LYS A 225      32.525  69.466  10.219  1.00 28.36           C  
ATOM   1710  N   MET A 226      32.014  67.308  12.379  1.00 35.37           N  
ATOM   1711  CA  MET A 226      31.304  66.115  12.768  1.00 33.44           C  
ATOM   1712  C   MET A 226      30.673  66.290  14.121  1.00 30.65           C  
ATOM   1713  O   MET A 226      29.519  65.934  14.278  1.00 29.62           O  
ATOM   1714  CB  MET A 226      32.229  64.897  12.796  1.00 35.25           C  
ATOM   1715  CG  MET A 226      32.679  64.611  11.383  1.00 36.92           C  
ATOM   1716  SD  MET A 226      33.308  62.951  11.068  1.00 42.08           S  
ATOM   1717  CE  MET A 226      34.866  63.120  11.892  1.00 39.96           C  
ATOM   1718  N   ALA A 227      31.368  66.862  15.121  1.00 30.91           N  
ATOM   1719  CA  ALA A 227      30.771  67.002  16.443  1.00 32.81           C  
ATOM   1720  C   ALA A 227      29.532  67.909  16.416  1.00 35.09           C  
ATOM   1721  O   ALA A 227      28.519  67.594  17.072  1.00 34.07           O  
ATOM   1722  CB  ALA A 227      31.813  67.594  17.403  1.00 27.62           C  
ATOM   1723  N   LYS A 228      29.577  68.949  15.589  1.00 37.99           N  
ATOM   1724  CA  LYS A 228      28.497  69.912  15.423  1.00 40.99           C  
ATOM   1725  C   LYS A 228      27.132  69.272  15.191  1.00 39.78           C  
ATOM   1726  O   LYS A 228      26.127  69.807  15.667  1.00 41.62           O  
ATOM   1727  CB  LYS A 228      28.788  70.845  14.267  1.00 44.64           C  
ATOM   1728  CG  LYS A 228      29.347  72.117  14.812  1.00 51.86           C  
ATOM   1729  CD  LYS A 228      28.167  73.035  15.117  1.00 61.78           C  
ATOM   1730  CE  LYS A 228      28.148  74.216  14.126  1.00 68.79           C  
ATOM   1731  NZ  LYS A 228      28.098  73.792  12.727  1.00 71.89           N  
ATOM   1732  N   LYS A 229      27.046  68.083  14.579  1.00 38.61           N  
ATOM   1733  CA  LYS A 229      25.763  67.437  14.356  1.00 37.64           C  
ATOM   1734  C   LYS A 229      25.083  67.009  15.632  1.00 36.27           C  
ATOM   1735  O   LYS A 229      23.860  66.831  15.684  1.00 39.53           O  
ATOM   1736  CB  LYS A 229      25.889  66.187  13.556  1.00 39.70           C  
ATOM   1737  CG  LYS A 229      26.211  66.394  12.109  1.00 46.12           C  
ATOM   1738  CD  LYS A 229      26.362  65.010  11.471  1.00 53.01           C  
ATOM   1739  CE  LYS A 229      25.164  64.082  11.652  1.00 53.53           C  
ATOM   1740  NZ  LYS A 229      25.450  62.859  10.934  1.00 55.47           N  
ATOM   1741  N   TYR A 230      25.854  66.779  16.686  1.00 35.40           N  
ATOM   1742  CA  TYR A 230      25.287  66.159  17.872  1.00 31.38           C  
ATOM   1743  C   TYR A 230      25.414  67.003  19.076  1.00 31.44           C  
ATOM   1744  O   TYR A 230      24.548  66.949  19.943  1.00 30.83           O  
ATOM   1745  CB  TYR A 230      25.961  64.831  18.252  1.00 29.01           C  
ATOM   1746  CG  TYR A 230      26.120  63.881  17.094  1.00 26.63           C  
ATOM   1747  CD1 TYR A 230      27.139  64.017  16.180  1.00 22.99           C  
ATOM   1748  CD2 TYR A 230      25.174  62.926  16.944  1.00 28.69           C  
ATOM   1749  CE1 TYR A 230      27.206  63.179  15.097  1.00 25.81           C  
ATOM   1750  CE2 TYR A 230      25.233  62.087  15.864  1.00 30.57           C  
ATOM   1751  CZ  TYR A 230      26.238  62.214  14.937  1.00 29.82           C  
ATOM   1752  OH  TYR A 230      26.234  61.355  13.851  1.00 25.77           O  
ATOM   1753  N   PHE A 231      26.496  67.776  19.146  1.00 33.94           N  
ATOM   1754  CA  PHE A 231      26.844  68.424  20.401  1.00 34.98           C  
ATOM   1755  C   PHE A 231      27.007  69.881  20.118  1.00 36.68           C  
ATOM   1756  O   PHE A 231      27.629  70.263  19.133  1.00 37.51           O  
ATOM   1757  CB  PHE A 231      28.171  67.882  20.972  1.00 33.09           C  
ATOM   1758  CG  PHE A 231      28.114  66.370  21.186  1.00 32.29           C  
ATOM   1759  CD1 PHE A 231      27.253  65.847  22.155  1.00 33.06           C  
ATOM   1760  CD2 PHE A 231      28.868  65.531  20.374  1.00 29.74           C  
ATOM   1761  CE1 PHE A 231      27.121  64.479  22.309  1.00 31.05           C  
ATOM   1762  CE2 PHE A 231      28.732  64.159  20.534  1.00 31.30           C  
ATOM   1763  CZ  PHE A 231      27.864  63.644  21.494  1.00 32.70           C  
ATOM   1764  N   ASP A 232      26.434  70.658  21.013  1.00 40.80           N  
ATOM   1765  CA  ASP A 232      26.546  72.104  20.940  1.00 44.43           C  
ATOM   1766  C   ASP A 232      27.661  72.513  21.882  1.00 43.60           C  
ATOM   1767  O   ASP A 232      27.855  73.707  22.082  1.00 47.96           O  
ATOM   1768  CB  ASP A 232      25.247  72.759  21.370  1.00 51.75           C  
ATOM   1769  CG  ASP A 232      24.743  72.155  22.687  1.00 64.70           C  
ATOM   1770  OD1 ASP A 232      25.303  72.460  23.753  1.00 69.07           O  
ATOM   1771  OD2 ASP A 232      23.811  71.333  22.633  1.00 72.80           O  
ATOM   1772  N   PHE A 233      28.351  71.579  22.543  1.00 39.81           N  
ATOM   1773  CA  PHE A 233      29.469  71.937  23.393  1.00 37.52           C  
ATOM   1774  C   PHE A 233      30.768  71.251  22.960  1.00 36.69           C  
ATOM   1775  O   PHE A 233      30.798  70.430  22.031  1.00 37.24           O  
ATOM   1776  CB  PHE A 233      29.155  71.580  24.831  1.00 36.29           C  
ATOM   1777  CG  PHE A 233      29.101  70.098  25.139  1.00 40.98           C  
ATOM   1778  CD1 PHE A 233      28.035  69.338  24.710  1.00 41.52           C  
ATOM   1779  CD2 PHE A 233      30.132  69.531  25.872  1.00 40.57           C  
ATOM   1780  CE1 PHE A 233      28.025  67.999  25.028  1.00 43.27           C  
ATOM   1781  CE2 PHE A 233      30.100  68.199  26.183  1.00 38.66           C  
ATOM   1782  CZ  PHE A 233      29.047  67.440  25.760  1.00 40.49           C  
ATOM   1783  N   ASN A 234      31.897  71.532  23.597  1.00 34.87           N  
ATOM   1784  CA  ASN A 234      33.141  70.908  23.199  1.00 32.53           C  
ATOM   1785  C   ASN A 234      33.263  69.528  23.815  1.00 29.08           C  
ATOM   1786  O   ASN A 234      33.702  69.362  24.944  1.00 27.19           O  
ATOM   1787  CB  ASN A 234      34.231  71.822  23.624  1.00 33.89           C  
ATOM   1788  CG  ASN A 234      35.607  71.229  23.481  1.00 35.20           C  
ATOM   1789  OD1 ASN A 234      36.424  71.443  24.357  1.00 37.49           O  
ATOM   1790  ND2 ASN A 234      36.004  70.467  22.486  1.00 35.73           N  
ATOM   1791  N   VAL A 235      32.736  68.529  23.102  1.00 28.28           N  
ATOM   1792  CA  VAL A 235      32.803  67.135  23.546  1.00 28.29           C  
ATOM   1793  C   VAL A 235      34.224  66.644  23.755  1.00 26.34           C  
ATOM   1794  O   VAL A 235      34.466  65.690  24.488  1.00 26.41           O  
ATOM   1795  CB  VAL A 235      32.252  66.027  22.583  1.00 30.68           C  
ATOM   1796  CG1 VAL A 235      31.055  65.417  23.285  1.00 29.16           C  
ATOM   1797  CG2 VAL A 235      32.067  66.526  21.171  1.00 27.96           C  
ATOM   1798  N   TYR A 236      35.167  67.204  23.016  1.00 24.89           N  
ATOM   1799  CA  TYR A 236      36.536  66.773  23.147  1.00 24.60           C  
ATOM   1800  C   TYR A 236      37.096  66.992  24.537  1.00 27.25           C  
ATOM   1801  O   TYR A 236      37.800  66.109  25.026  1.00 24.16           O  
ATOM   1802  CB  TYR A 236      37.346  67.494  22.096  1.00 25.78           C  
ATOM   1803  CG  TYR A 236      38.747  66.920  22.051  1.00 30.12           C  
ATOM   1804  CD1 TYR A 236      38.992  65.702  21.439  1.00 30.39           C  
ATOM   1805  CD2 TYR A 236      39.755  67.588  22.702  1.00 32.03           C  
ATOM   1806  CE1 TYR A 236      40.250  65.145  21.481  1.00 30.54           C  
ATOM   1807  CE2 TYR A 236      41.006  67.034  22.753  1.00 33.89           C  
ATOM   1808  CZ  TYR A 236      41.245  65.830  22.139  1.00 33.01           C  
ATOM   1809  OH  TYR A 236      42.515  65.310  22.213  1.00 31.57           O  
ATOM   1810  N   GLY A 237      36.744  68.093  25.220  1.00 31.30           N  
ATOM   1811  CA  GLY A 237      37.302  68.436  26.516  1.00 35.43           C  
ATOM   1812  C   GLY A 237      38.654  69.103  26.270  1.00 41.74           C  
ATOM   1813  O   GLY A 237      38.843  69.804  25.266  1.00 42.67           O  
ATOM   1814  N   ASP A 238      39.632  68.814  27.124  1.00 47.86           N  
ATOM   1815  CA  ASP A 238      40.936  69.454  27.040  1.00 53.26           C  
ATOM   1816  C   ASP A 238      41.963  68.498  26.444  1.00 54.11           C  
ATOM   1817  O   ASP A 238      42.103  67.376  26.936  1.00 54.48           O  
ATOM   1818  CB  ASP A 238      41.363  69.897  28.450  1.00 57.29           C  
ATOM   1819  CG  ASP A 238      40.377  70.804  29.190  1.00 61.17           C  
ATOM   1820  OD1 ASP A 238      39.660  71.580  28.548  1.00 63.34           O  
ATOM   1821  OD2 ASP A 238      40.333  70.734  30.420  1.00 63.51           O  
ATOM   1822  OXT ASP A 238      42.606  68.875  25.470  1.00 55.41           O  
TER    1823      ASP A 238                                                      
HETATM 1824  O   HOH A 401      35.465  53.833  22.185  1.00 17.40           O  
HETATM 1825  O   HOH A 402      29.833  70.386  37.786  1.00 17.14           O  
HETATM 1826  O   HOH A 403      43.753  45.097  17.757  1.00 22.49           O  
HETATM 1827  O   HOH A 404      24.857  59.467  39.438  1.00 26.25           O  
HETATM 1828  O   HOH A 405      30.130  62.511  29.393  1.00 26.09           O  
HETATM 1829  O   HOH A 406      32.008  64.455  29.050  1.00 27.43           O  
HETATM 1830  O   HOH A 407      22.720  75.246  37.739  1.00 30.15           O  
HETATM 1831  O   HOH A 408      45.727  42.952  24.365  1.00 41.65           O  
HETATM 1832  O   HOH A 409      38.011  62.094  33.829  1.00 30.81           O  
HETATM 1833  O   HOH A 410      33.942  44.685  27.038  1.00 35.76           O  
HETATM 1834  O   HOH A 411      30.964  61.368  26.619  1.00 34.24           O  
HETATM 1835  O   HOH A 412      48.617  46.257  13.995  1.00 40.71           O  
HETATM 1836  O   HOH A 413      38.451  69.665  14.181  1.00 42.41           O  
HETATM 1837  O   HOH A 414      29.069  54.296  21.592  1.00 32.80           O  
HETATM 1838  O   HOH A 415      31.392  60.205  33.382  1.00 26.86           O  
HETATM 1839  O   HOH A 416      41.323  54.851  35.386  1.00 41.30           O  
HETATM 1840  O   HOH A 417      47.615  48.564  19.641  1.00 37.18           O  
HETATM 1841  O   HOH A 418      26.295  58.430  11.683  1.00 28.55           O  
HETATM 1842  O   HOH A 419      43.316  62.914  20.769  1.00 37.49           O  
HETATM 1843  O   HOH A 420      47.487  52.523  24.517  1.00 49.40           O  
HETATM 1844  O   HOH A 421      45.375  57.150  24.655  1.00 34.87           O  
HETATM 1845  O   HOH A 422      28.371  77.698  37.121  1.00 30.46           O  
HETATM 1846  O   HOH A 423      26.976  77.322  39.566  1.00 33.68           O  
HETATM 1847  O   HOH A 424      46.464  56.777   9.347  1.00 38.81           O  
HETATM 1848  O   HOH A 425      24.274  66.742  24.219  1.00 60.46           O  
HETATM 1849  O   HOH A 426      41.517  39.337  13.840  1.00 31.33           O  
HETATM 1850  O   HOH A 427      32.092  73.522  25.975  1.00 39.26           O  
HETATM 1851  O   HOH A 428      32.174  71.055  29.411  1.00 36.89           O  
HETATM 1852  O   HOH A 429      28.265  51.858  22.797  1.00 37.34           O  
HETATM 1853  O   HOH A 430      19.135  72.831  42.485  1.00 32.19           O  
HETATM 1854  O   HOH A 431      40.088  60.905  51.071  1.00 58.03           O  
HETATM 1855  O   HOH A 432      36.600  60.864  30.865  1.00 54.93           O  
HETATM 1856  O   HOH A 433      33.249  52.654  28.984  1.00 52.77           O  
HETATM 1857  O   HOH A 434      25.174  58.031  37.025  1.00 53.10           O  
HETATM 1858  O   HOH A 435      50.756  56.142  17.706  1.00 49.00           O  
HETATM 1859  O   HOH A 436      34.155  69.241  20.631  1.00 43.95           O  
HETATM 1860  O   HOH A 437      38.068  35.985  25.013  1.00 36.44           O  
HETATM 1861  O   HOH A 438      28.659  62.891  54.888  1.00 42.17           O  
HETATM 1862  O   HOH A 439      16.173  71.962  43.010  1.00 58.30           O  
HETATM 1863  O   HOH A 440      20.537  61.013  22.161  1.00 54.84           O  
HETATM 1864  O   HOH A 441      23.386  73.334  31.137  1.00 48.08           O  
HETATM 1865  O   HOH A 442      26.714  56.786   9.479  1.00 37.84           O  
HETATM 1866  O   HOH A 443      34.618  56.366  21.671  1.00 20.82           O  
HETATM 1867  O   HOH A 444      23.376  57.265  17.525  1.00 30.89           O  
HETATM 1868  O   HOH A 445      39.537  32.774  18.658  1.00 33.83           O  
HETATM 1869  O   HOH A 446      43.832  35.533  20.599  1.00 31.85           O  
HETATM 1870  O   HOH A 447      44.860  63.470  18.386  1.00 41.61           O  
HETATM 1871  O   HOH A 448      24.831  59.624  34.475  1.00 46.43           O  
HETATM 1872  O   HOH A 449      14.729  75.822  38.554  1.00 52.02           O  
HETATM 1873  O   HOH A 450      32.697  65.399  26.603  1.00 44.50           O  
HETATM 1874  O   HOH A 451      29.067  59.741  27.892  1.00 80.96           O  
HETATM 1875  O   HOH A 452      49.769  49.147  21.355  1.00 56.15           O  
HETATM 1876  O   HOH A 453      29.928  53.057  42.979  1.00 41.64           O  
HETATM 1877  O   HOH A 454      35.555  67.893  29.949  1.00 60.63           O  
HETATM 1878  O   HOH A 455      29.335  57.762   9.107  1.00 43.67           O  
HETATM 1879  O   HOH A 456      33.451  57.708  32.035  1.00 56.83           O  
HETATM 1880  O   HOH A 457      35.749  67.962  44.659  1.00 56.71           O  
HETATM 1881  O   HOH A 458      26.529  43.202  13.484  1.00 57.44           O  
HETATM 1882  O   HOH A 459      23.037  64.632  20.098  1.00 54.55           O  
HETATM 1883  O   HOH A 460      45.876  61.044  17.590  1.00 36.10           O  
HETATM 1884  O   HOH A 461      24.523  46.012  19.933  1.00 54.36           O  
HETATM 1885  O   HOH A 462      25.740  61.340  53.197  1.00 52.28           O  
HETATM 1886  O   HOH A 463      36.762  70.764  33.847  1.00 58.22           O  
HETATM 1887  O   HOH A 464      51.390  47.806   8.632  1.00 45.48           O  
HETATM 1888  O   HOH A 465      38.419  39.020  12.771  1.00 44.13           O  
HETATM 1889  O   HOH A 466      41.978  33.841  22.360  1.00 42.46           O  
HETATM 1890  O   HOH A 468      27.874  69.775  28.194  1.00 47.01           O  
HETATM 1891  O   HOH A 469      34.097  70.483  27.337  1.00 50.35           O  
HETATM 1892  O   HOH A 470      38.043  67.992  37.950  1.00 54.55           O  
HETATM 1893  O   HOH A 471      27.285  56.399  41.293  1.00 61.41           O  
HETATM 1894  O   HOH A 472      26.088  68.532  53.205  1.00 52.81           O  
HETATM 1895  O   HOH A 473      48.001  56.862  23.019  1.00 46.16           O  
HETATM 1896  O   HOH A 474      50.644  57.453  14.461  1.00 44.32           O  
HETATM 1897  O   HOH A 475      33.393  68.088  28.498  1.00 49.10           O  
HETATM 1898  O   HOH A 476      32.409  60.005   8.702  1.00 53.15           O  
HETATM 1899  O   HOH A 477      37.455  50.266  33.771  1.00 45.82           O  
HETATM 1900  O   HOH A 478      18.104  54.322  36.435  1.00 51.97           O  
HETATM 1901  O   HOH A 479      46.626  40.918  17.224  1.00 54.78           O  
HETATM 1902  O   HOH A 480      18.767  51.454  17.195  1.00 57.45           O  
HETATM 1903  O   HOH A 481      19.698  51.524  19.636  1.00 69.46           O  
HETATM 1904  O   HOH A 482      15.673  55.190  43.166  1.00 54.05           O  
HETATM 1905  O   HOH A 483      46.087  55.034  26.256  1.00 58.68           O  
HETATM 1906  O   HOH A 484      33.070  56.747  50.358  1.00 49.56           O  
HETATM 1907  O   HOH A 485      50.703  42.230  15.789  1.00 53.38           O  
HETATM 1908  O   HOH A 486      23.187  70.734  16.488  1.00 68.53           O  
HETATM 1909  O   HOH A 487      23.338  70.407  19.208  1.00 70.34           O  
HETATM 1910  O   HOH A 488      12.213  72.029  34.341  1.00 58.45           O  
HETATM 1911  O   HOH A 489      41.869  65.388  38.789  1.00 63.29           O  
HETATM 1912  O   HOH A 490      47.266  56.519   4.783  1.00 60.77           O  
CONECT  283  338                                                                
CONECT  338  283                                                                
MASTER      315    0    0   10   10    0    0    6 1911    1    2   19          
END                                                                             


A second structure was input as follows:


HEADER    AMINO-ACID BINDING PROTEIN              25-FEB-93   1LST              
TITLE     THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC LYSINE-, ARGININE-,   
TITLE    2 ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A LIGAND                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE, ARGININE, ORNITHINE-BINDING PROTEIN;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602                                                  
KEYWDS    AMINO-ACID BINDING PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-H.KIM,B.-H.OH                                                      
REVDAT   4   29-NOV-17 1LST    1       HELIX                                    
REVDAT   3   24-FEB-09 1LST    1       VERSN                                    
REVDAT   2   01-APR-03 1LST    1       JRNL                                     
REVDAT   1   22-JUN-94 1LST    0                                                
JRNL        AUTH   B.H.OH,J.PANDIT,C.H.KANG,K.NIKAIDO,S.GOKCEN,G.F.AMES,S.H.KIM 
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF THE PERIPLASMIC              
JRNL        TITL 2 LYSINE/ARGININE/ORNITHINE-BINDING PROTEIN WITH AND WITHOUT A 
JRNL        TITL 3 LIGAND.                                                      
JRNL        REF    J.BIOL.CHEM.                  V. 268 11348 1993              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   8496186                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.-H.KANG,W.-C.SHIN,Y.YAMAGATA,S.GOKCEN,G.F.-L.AMES,S.-H.KIM 
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE LYSINE-, ARGININE-,                 
REMARK   1  TITL 2 ORNITHINE-BINDING PROTEIN FROM SALMONELLA TYPHIMURIUM AT 2.7 
REMARK   1  TITL 3 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    J.BIOL.CHEM.                  V. 266 23893 1992              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 23359                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1805                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.540                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174820.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       18.89500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.96500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.96500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.89500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.81500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS A   239                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 110    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     GLU A 177    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     LYS A 189    CG   CD   CE   NZ                                   
REMARK 470     LYS A 228    CG   CD   CE   NZ                                   
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    HIS A 113   NE2   HIS A 113   CD2    -0.075                       
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    TRP A  47   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A  47   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    TRP A 130   CD1 -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    TRP A 130   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TYR A 147   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    GLY A 237   N   -  CA  -  C   ANGL. DEV. = -15.8 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    THR A  12       34.33    -82.50                                   
REMARK 500    SER A  69       47.50   -161.90                                   
REMARK 500    PHE A 169      -58.42   -141.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS A 240                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: ARGT_SALTY                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        VAL   102             ILE         102                         
REMARK 999                                                                      
REMARK 999 RESIDUE 102 OF THE LAO PROTEIN IS ISOLEUCINE, BUT WAS                
REMARK 999 REPORTED AS VALINE IN SWISS-PROT DATA BANK DUE TO                    
REMARK 999 SEQUENCING ERROR (PERSONAL COMMUNICATION).                           
DBREF  1LST A    1   238  UNP    P02911   ARGT_SALTY      23    260             
SEQADV 1LST ILE A  102  UNP  P02911    VAL   124 CONFLICT                       
SEQRES   1 A  239  ALA LEU PRO GLN THR VAL ARG ILE GLY THR ASP THR THR          
SEQRES   2 A  239  TYR ALA PRO PHE SER SER LYS ASP ALA LYS GLY GLU PHE          
SEQRES   3 A  239  ILE GLY PHE ASP ILE ASP LEU GLY ASN GLU MET CYS LYS          
SEQRES   4 A  239  ARG MET GLN VAL LYS CYS THR TRP VAL ALA SER ASP PHE          
SEQRES   5 A  239  ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP          
SEQRES   6 A  239  ALA ILE ILE SER SER LEU SER ILE THR ASP LYS ARG GLN          
SEQRES   7 A  239  GLN GLU ILE ALA PHE SER ASP LYS LEU TYR ALA ALA ASP          
SEQRES   8 A  239  SER ARG LEU ILE ALA ALA LYS GLY SER PRO ILE GLN PRO          
SEQRES   9 A  239  THR LEU GLU SER LEU LYS GLY LYS HIS VAL GLY VAL LEU          
SEQRES  10 A  239  GLN GLY SER THR GLN GLU ALA TYR ALA ASN ASP ASN TRP          
SEQRES  11 A  239  ARG THR LYS GLY VAL ASP VAL VAL ALA TYR ALA ASN GLN          
SEQRES  12 A  239  ASP LEU ILE TYR SER ASP LEU THR ALA GLY ARG LEU ASP          
SEQRES  13 A  239  ALA ALA LEU GLN ASP GLU VAL ALA ALA SER GLU GLY PHE          
SEQRES  14 A  239  LEU LYS GLN PRO ALA GLY LYS GLU TYR ALA PHE ALA GLY          
SEQRES  15 A  239  PRO SER VAL LYS ASP LYS LYS TYR PHE GLY ASP GLY THR          
SEQRES  16 A  239  GLY VAL GLY LEU ARG LYS ASP ASP THR GLU LEU LYS ALA          
SEQRES  17 A  239  ALA PHE ASP LYS ALA LEU THR GLU LEU ARG GLN ASP GLY          
SEQRES  18 A  239  THR TYR ASP LYS MET ALA LYS LYS TYR PHE ASP PHE ASN          
SEQRES  19 A  239  VAL TYR GLY ASP LYS                                          
HET    LYS  A 240      10                                                       
HETNAM     LYS LYSINE                                                           
FORMUL   2  LYS    C6 H15 N2 O2 1+                                              
FORMUL   3  HOH   *199(H2 O)                                                    
HELIX    1   A PHE A   29  MET A   41  1                                  13    
HELIX    2   B LEU A   55  LYS A   60  1                                   6    
HELIX    3   C ASP A   75  GLU A   80  1                                   6    
HELIX    4   D LEU A  106  LEU A  109  1                                   4    
HELIX    5   E THR A  121  ASN A  129  1                                   9    
HELIX    6   F GLN A  143  THR A  151  1                                   9    
HELIX    7   G GLU A  162  GLY A  168  1                                   7    
HELIX    8   H LYS A  188  PHE A  191  1                                   4    
HELIX    9   I THR A  204  GLN A  219  1                                  16    
HELIX   10   J THR A  222  LYS A  228  1                                   7    
SHEET    1   1 5 LYS A  44  ALA A  49  0                                        
SHEET    2   1 5 THR A   5  THR A  10  1                                        
SHEET    3   1 5 ALA A  66  ILE A  67  1                                        
SHEET    4   1 5 VAL A 197  LEU A 199 -1                                        
SHEET    5   1 5 ALA A  82  SER A  84  1                                        
SHEET    1   2 5 ASP A 136  TYR A 140  0                                        
SHEET    2   2 5 HIS A 113  LEU A 117  1                                        
SHEET    3   2 5 ALA A 157  ASP A 161  1                                        
SHEET    4   2 5 SER A  92  ALA A  97 -1                                        
SHEET    5   2 5 TYR A 178  ALA A 181  1                                        
SSBOND   1 CYS A   38    CYS A   45                          1555   1555  2.01  
CISPEP   1 ALA A   15    PRO A   16          0         4.08                     
SITE     1 AC1 13 ASP A  11  TYR A  14  PHE A  52  SER A  69                    
SITE     2 AC1 13 SER A  70  SER A  72  ARG A  77  LEU A 117                    
SITE     3 AC1 13 SER A 120  THR A 121  GLN A 122  ASP A 161                    
SITE     4 AC1 13 HOH A 426                                                     
CRYST1   37.790   59.630  115.930  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026462  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008626        0.00000                         
ATOM      1  N   ALA A   1      19.369  88.165  50.553  1.00 70.42           N  
ATOM      2  CA  ALA A   1      20.320  87.836  51.572  1.00 70.30           C  
ATOM      3  C   ALA A   1      20.770  86.371  51.506  1.00 69.35           C  
ATOM      4  O   ALA A   1      20.528  85.561  52.410  1.00 71.17           O  
ATOM      5  CB  ALA A   1      19.690  88.125  52.940  1.00 71.87           C  
ATOM      6  N   LEU A   2      21.436  85.981  50.422  1.00 66.16           N  
ATOM      7  CA  LEU A   2      22.031  84.651  50.374  1.00 62.78           C  
ATOM      8  C   LEU A   2      23.360  84.688  51.130  1.00 60.84           C  
ATOM      9  O   LEU A   2      23.968  85.772  51.171  1.00 61.42           O  
ATOM     10  CB  LEU A   2      22.261  84.256  48.936  1.00 61.89           C  
ATOM     11  CG  LEU A   2      20.995  84.214  48.119  1.00 61.54           C  
ATOM     12  CD1 LEU A   2      21.370  83.775  46.731  1.00 63.11           C  
ATOM     13  CD2 LEU A   2      19.973  83.291  48.744  1.00 60.35           C  
ATOM     14  N   PRO A   3      23.839  83.601  51.774  1.00 58.10           N  
ATOM     15  CA  PRO A   3      25.134  83.568  52.431  1.00 55.80           C  
ATOM     16  C   PRO A   3      26.280  83.849  51.469  1.00 54.93           C  
ATOM     17  O   PRO A   3      26.187  83.660  50.257  1.00 55.14           O  
ATOM     18  CB  PRO A   3      25.185  82.187  53.070  1.00 55.72           C  
ATOM     19  CG  PRO A   3      24.273  81.328  52.232  1.00 55.93           C  
ATOM     20  CD  PRO A   3      23.154  82.313  51.918  1.00 56.85           C  
ATOM     21  N   GLN A   4      27.388  84.340  52.019  1.00 54.15           N  
ATOM     22  CA  GLN A   4      28.575  84.609  51.210  1.00 52.13           C  
ATOM     23  C   GLN A   4      29.162  83.296  50.686  1.00 48.91           C  
ATOM     24  O   GLN A   4      29.678  83.204  49.562  1.00 49.37           O  
ATOM     25  CB  GLN A   4      29.640  85.327  52.049  1.00 53.76           C  
ATOM     26  N   THR A   5      29.058  82.290  51.560  1.00 44.14           N  
ATOM     27  CA  THR A   5      29.485  80.947  51.273  1.00 39.74           C  
ATOM     28  C   THR A   5      28.308  80.043  51.545  1.00 35.08           C  
ATOM     29  O   THR A   5      27.744  80.087  52.645  1.00 35.11           O  
ATOM     30  CB  THR A   5      30.655  80.569  52.168  1.00 41.62           C  
ATOM     31  OG1 THR A   5      31.605  81.608  51.937  1.00 45.01           O  
ATOM     32  CG2 THR A   5      31.221  79.204  51.899  1.00 41.46           C  
ATOM     33  N   VAL A   6      27.932  79.264  50.545  1.00 27.99           N  
ATOM     34  CA  VAL A   6      26.917  78.248  50.699  1.00 22.61           C  
ATOM     35  C   VAL A   6      27.684  76.946  50.951  1.00 19.55           C  
ATOM     36  O   VAL A   6      28.575  76.581  50.167  1.00 17.86           O  
ATOM     37  CB  VAL A   6      26.111  78.149  49.433  1.00 21.13           C  
ATOM     38  CG1 VAL A   6      25.082  77.002  49.533  1.00 21.03           C  
ATOM     39  CG2 VAL A   6      25.418  79.492  49.239  1.00 21.21           C  
ATOM     40  N   ARG A   7      27.377  76.260  52.068  1.00 16.77           N  
ATOM     41  CA  ARG A   7      28.034  75.021  52.461  1.00 13.67           C  
ATOM     42  C   ARG A   7      27.191  73.859  51.930  1.00 12.49           C  
ATOM     43  O   ARG A   7      26.013  73.746  52.260  1.00 12.27           O  
ATOM     44  CB  ARG A   7      28.145  75.014  53.978  1.00 13.68           C  
ATOM     45  CG  ARG A   7      29.102  76.129  54.449  1.00 16.83           C  
ATOM     46  CD  ARG A   7      29.208  76.266  55.973  1.00 16.89           C  
ATOM     47  NE  ARG A   7      29.383  74.994  56.671  1.00 19.15           N  
ATOM     48  CZ  ARG A   7      30.525  74.271  56.714  1.00 17.36           C  
ATOM     49  NH1 ARG A   7      31.641  74.657  56.110  1.00 18.26           N  
ATOM     50  NH2 ARG A   7      30.531  73.132  57.392  1.00 18.18           N  
ATOM     51  N   ILE A   8      27.723  73.037  51.037  1.00 12.80           N  
ATOM     52  CA  ILE A   8      26.972  71.972  50.385  1.00 13.14           C  
ATOM     53  C   ILE A   8      27.532  70.640  50.850  1.00 12.18           C  
ATOM     54  O   ILE A   8      28.731  70.367  50.697  1.00 13.88           O  
ATOM     55  CB  ILE A   8      27.107  72.044  48.857  1.00 13.58           C  
ATOM     56  CG1 ILE A   8      26.758  73.469  48.354  1.00 12.96           C  
ATOM     57  CG2 ILE A   8      26.182  70.960  48.237  1.00 10.36           C  
ATOM     58  CD1 ILE A   8      26.953  73.664  46.831  1.00 16.76           C  
ATOM     59  N   GLY A   9      26.660  69.830  51.448  1.00 13.01           N  
ATOM     60  CA  GLY A   9      27.034  68.506  51.902  1.00 12.06           C  
ATOM     61  C   GLY A   9      26.781  67.463  50.813  1.00 12.23           C  
ATOM     62  O   GLY A   9      25.761  67.514  50.109  1.00 12.05           O  
ATOM     63  N   THR A  10      27.685  66.492  50.731  1.00 11.98           N  
ATOM     64  CA  THR A  10      27.561  65.397  49.785  1.00 12.30           C  
ATOM     65  C   THR A  10      28.251  64.170  50.398  1.00 14.49           C  
ATOM     66  O   THR A  10      29.154  64.256  51.256  1.00 15.40           O  
ATOM     67  CB  THR A  10      28.218  65.812  48.419  1.00 12.87           C  
ATOM     68  OG1 THR A  10      27.768  64.846  47.467  1.00 13.11           O  
ATOM     69  CG2 THR A  10      29.762  65.873  48.438  1.00 10.92           C  
ATOM     70  N   ASP A  11      27.820  62.992  49.954  1.00 14.06           N  
ATOM     71  CA  ASP A  11      28.395  61.725  50.357  1.00 14.03           C  
ATOM     72  C   ASP A  11      29.184  61.268  49.135  1.00 14.23           C  
ATOM     73  O   ASP A  11      28.656  60.836  48.089  1.00 14.08           O  
ATOM     74  CB  ASP A  11      27.255  60.771  50.704  1.00 15.71           C  
ATOM     75  CG  ASP A  11      27.613  59.292  50.661  1.00 19.66           C  
ATOM     76  OD1 ASP A  11      28.762  58.923  50.885  1.00 20.02           O  
ATOM     77  OD2 ASP A  11      26.721  58.508  50.384  1.00 22.49           O  
ATOM     78  N   THR A  12      30.499  61.287  49.334  1.00 13.59           N  
ATOM     79  CA  THR A  12      31.423  61.014  48.244  1.00 13.99           C  
ATOM     80  C   THR A  12      31.681  59.543  47.941  1.00 12.87           C  
ATOM     81  O   THR A  12      32.812  59.189  47.593  1.00 13.41           O  
ATOM     82  CB  THR A  12      32.740  61.783  48.558  1.00 15.70           C  
ATOM     83  OG1 THR A  12      33.189  61.475  49.874  1.00 20.08           O  
ATOM     84  CG2 THR A  12      32.496  63.282  48.430  1.00 16.14           C  
ATOM     85  N   THR A  13      30.700  58.648  48.090  1.00 13.58           N  
ATOM     86  CA  THR A  13      30.877  57.241  47.756  1.00 14.59           C  
ATOM     87  C   THR A  13      29.784  56.802  46.783  1.00 13.73           C  
ATOM     88  O   THR A  13      29.242  55.701  46.894  1.00 16.15           O  
ATOM     89  CB  THR A  13      30.857  56.374  49.077  1.00 13.81           C  
ATOM     90  OG1 THR A  13      29.618  56.565  49.725  1.00 17.43           O  
ATOM     91  CG2 THR A  13      31.964  56.734  50.023  1.00 15.94           C  
ATOM     92  N   TYR A  14      29.420  57.627  45.812  1.00 12.18           N  
ATOM     93  CA  TYR A  14      28.366  57.268  44.876  1.00 12.77           C  
ATOM     94  C   TYR A  14      28.737  57.721  43.455  1.00 13.11           C  
ATOM     95  O   TYR A  14      28.135  58.617  42.848  1.00 12.17           O  
ATOM     96  CB  TYR A  14      27.111  57.924  45.381  1.00 11.24           C  
ATOM     97  CG  TYR A  14      25.862  57.069  45.335  1.00 12.50           C  
ATOM     98  CD1 TYR A  14      25.733  55.916  46.102  1.00 10.39           C  
ATOM     99  CD2 TYR A  14      24.823  57.487  44.534  1.00 12.84           C  
ATOM    100  CE1 TYR A  14      24.543  55.200  46.079  1.00  9.67           C  
ATOM    101  CE2 TYR A  14      23.635  56.772  44.500  1.00 12.74           C  
ATOM    102  CZ  TYR A  14      23.500  55.640  45.290  1.00 11.35           C  
ATOM    103  OH  TYR A  14      22.280  54.972  45.275  1.00  9.80           O  
ATOM    104  N   ALA A  15      29.795  57.132  42.904  1.00 13.58           N  
ATOM    105  CA  ALA A  15      30.274  57.509  41.596  1.00 14.97           C  
ATOM    106  C   ALA A  15      29.208  57.078  40.596  1.00 16.67           C  
ATOM    107  O   ALA A  15      28.518  56.092  40.865  1.00 16.91           O  
ATOM    108  CB  ALA A  15      31.582  56.792  41.321  1.00 15.89           C  
ATOM    109  N   PRO A  16      28.957  57.741  39.467  1.00 15.66           N  
ATOM    110  CA  PRO A  16      29.694  58.893  38.985  1.00 14.94           C  
ATOM    111  C   PRO A  16      29.122  60.230  39.485  1.00 14.80           C  
ATOM    112  O   PRO A  16      29.434  61.290  38.915  1.00 15.41           O  
ATOM    113  CB  PRO A  16      29.621  58.689  37.477  1.00 15.39           C  
ATOM    114  CG  PRO A  16      28.186  58.249  37.279  1.00 13.36           C  
ATOM    115  CD  PRO A  16      27.917  57.365  38.509  1.00 15.76           C  
ATOM    116  N   PHE A  17      28.258  60.228  40.511  1.00 12.27           N  
ATOM    117  CA  PHE A  17      27.594  61.443  40.939  1.00 12.81           C  
ATOM    118  C   PHE A  17      28.445  62.177  41.939  1.00 13.41           C  
ATOM    119  O   PHE A  17      28.590  63.397  41.828  1.00 12.53           O  
ATOM    120  CB  PHE A  17      26.195  61.127  41.558  1.00 12.19           C  
ATOM    121  CG  PHE A  17      25.245  60.571  40.485  1.00 12.34           C  
ATOM    122  CD1 PHE A  17      24.700  61.408  39.503  1.00 13.40           C  
ATOM    123  CD2 PHE A  17      24.951  59.211  40.455  1.00 14.18           C  
ATOM    124  CE1 PHE A  17      23.890  60.904  38.498  1.00 14.02           C  
ATOM    125  CE2 PHE A  17      24.134  58.707  39.442  1.00 15.95           C  
ATOM    126  CZ  PHE A  17      23.615  59.547  38.463  1.00 15.17           C  
ATOM    127  N   SER A  18      29.049  61.467  42.875  1.00 12.58           N  
ATOM    128  CA  SER A  18      29.853  62.117  43.880  1.00 13.67           C  
ATOM    129  C   SER A  18      30.913  61.139  44.354  1.00 15.29           C  
ATOM    130  O   SER A  18      30.573  60.086  44.917  1.00 13.73           O  
ATOM    131  CB  SER A  18      28.945  62.545  45.042  1.00 12.58           C  
ATOM    132  OG  SER A  18      29.709  63.258  46.024  1.00 16.53           O  
ATOM    133  N   SER A  19      32.190  61.443  44.166  1.00 15.16           N  
ATOM    134  CA  SER A  19      33.251  60.616  44.713  1.00 17.72           C  
ATOM    135  C   SER A  19      34.499  61.473  44.852  1.00 17.34           C  
ATOM    136  O   SER A  19      34.429  62.691  44.706  1.00 16.20           O  
ATOM    137  CB  SER A  19      33.539  59.378  43.804  1.00 18.71           C  
ATOM    138  OG  SER A  19      33.959  59.846  42.554  1.00 24.25           O  
ATOM    139  N   LYS A  20      35.631  60.894  45.178  1.00 19.55           N  
ATOM    140  CA  LYS A  20      36.843  61.652  45.331  1.00 23.41           C  
ATOM    141  C   LYS A  20      37.872  61.089  44.386  1.00 23.29           C  
ATOM    142  O   LYS A  20      37.842  59.889  44.092  1.00 23.34           O  
ATOM    143  CB  LYS A  20      37.318  61.563  46.772  1.00 27.28           C  
ATOM    144  CG  LYS A  20      36.533  62.568  47.572  1.00 34.71           C  
ATOM    145  CD  LYS A  20      37.101  62.687  48.960  1.00 43.23           C  
ATOM    146  CE  LYS A  20      36.553  64.005  49.519  1.00 48.76           C  
ATOM    147  NZ  LYS A  20      36.844  64.109  50.946  1.00 54.29           N  
ATOM    148  N   ASP A  21      38.741  61.942  43.832  1.00 22.42           N  
ATOM    149  CA  ASP A  21      39.807  61.438  42.984  1.00 22.71           C  
ATOM    150  C   ASP A  21      41.041  61.051  43.811  1.00 22.97           C  
ATOM    151  O   ASP A  21      41.022  61.128  45.052  1.00 22.19           O  
ATOM    152  CB  ASP A  21      40.151  62.499  41.962  1.00 23.13           C  
ATOM    153  CG  ASP A  21      40.839  63.772  42.441  1.00 25.62           C  
ATOM    154  OD1 ASP A  21      41.274  63.896  43.586  1.00 22.53           O  
ATOM    155  OD2 ASP A  21      40.924  64.677  41.624  1.00 29.80           O  
ATOM    156  N   ALA A  22      42.177  60.798  43.158  1.00 24.61           N  
ATOM    157  CA  ALA A  22      43.387  60.368  43.872  1.00 27.45           C  
ATOM    158  C   ALA A  22      43.999  61.375  44.818  1.00 27.64           C  
ATOM    159  O   ALA A  22      44.688  61.008  45.769  1.00 29.14           O  
ATOM    160  CB  ALA A  22      44.492  59.972  42.900  1.00 28.02           C  
ATOM    161  N   LYS A  23      43.782  62.655  44.532  1.00 28.15           N  
ATOM    162  CA  LYS A  23      44.264  63.722  45.407  1.00 29.06           C  
ATOM    163  C   LYS A  23      43.249  64.040  46.499  1.00 28.23           C  
ATOM    164  O   LYS A  23      43.495  64.917  47.326  1.00 28.94           O  
ATOM    165  CB  LYS A  23      44.466  65.030  44.691  1.00 29.98           C  
ATOM    166  CG  LYS A  23      45.208  65.052  43.416  1.00 35.10           C  
ATOM    167  CD  LYS A  23      45.159  66.535  43.073  1.00 39.20           C  
ATOM    168  CE  LYS A  23      45.068  66.758  41.561  1.00 43.11           C  
ATOM    169  NZ  LYS A  23      43.776  66.369  41.013  1.00 44.51           N  
ATOM    170  N   GLY A  24      42.053  63.426  46.488  1.00 28.47           N  
ATOM    171  CA  GLY A  24      41.008  63.732  47.455  1.00 25.86           C  
ATOM    172  C   GLY A  24      40.120  64.902  47.053  1.00 25.48           C  
ATOM    173  O   GLY A  24      39.365  65.410  47.878  1.00 27.67           O  
ATOM    174  N   GLU A  25      40.207  65.415  45.838  1.00 24.71           N  
ATOM    175  CA  GLU A  25      39.284  66.438  45.339  1.00 26.05           C  
ATOM    176  C   GLU A  25      37.935  65.784  45.046  1.00 23.18           C  
ATOM    177  O   GLU A  25      37.872  64.624  44.632  1.00 20.38           O  
ATOM    178  CB  GLU A  25      39.780  67.054  44.036  1.00 31.59           C  
ATOM    179  CG  GLU A  25      41.008  67.936  44.158  1.00 44.09           C  
ATOM    180  CD  GLU A  25      40.614  69.281  44.759  1.00 52.91           C  
ATOM    181  OE1 GLU A  25      40.081  70.105  44.005  1.00 58.27           O  
ATOM    182  OE2 GLU A  25      40.810  69.492  45.964  1.00 56.96           O  
ATOM    183  N   PHE A  26      36.854  66.528  45.200  1.00 21.75           N  
ATOM    184  CA  PHE A  26      35.485  66.062  44.986  1.00 20.92           C  
ATOM    185  C   PHE A  26      35.234  66.022  43.480  1.00 19.48           C  
ATOM    186  O   PHE A  26      35.561  66.984  42.770  1.00 18.25           O  
ATOM    187  CB  PHE A  26      34.477  67.036  45.649  1.00 24.79           C  
ATOM    188  CG  PHE A  26      34.385  67.084  47.190  1.00 29.07           C  
ATOM    189  CD1 PHE A  26      35.380  67.642  47.973  1.00 33.69           C  
ATOM    190  CD2 PHE A  26      33.259  66.609  47.837  1.00 29.26           C  
ATOM    191  CE1 PHE A  26      35.249  67.718  49.352  1.00 33.20           C  
ATOM    192  CE2 PHE A  26      33.133  66.688  49.213  1.00 28.90           C  
ATOM    193  CZ  PHE A  26      34.126  67.240  49.975  1.00 28.69           C  
ATOM    194  N   ILE A  27      34.688  64.940  42.932  1.00 16.45           N  
ATOM    195  CA  ILE A  27      34.430  64.831  41.499  1.00 16.96           C  
ATOM    196  C   ILE A  27      33.089  64.160  41.237  1.00 14.51           C  
ATOM    197  O   ILE A  27      32.580  63.386  42.055  1.00 15.60           O  
ATOM    198  CB  ILE A  27      35.506  63.989  40.747  1.00 16.86           C  
ATOM    199  CG1 ILE A  27      35.637  62.613  41.374  1.00 17.53           C  
ATOM    200  CG2 ILE A  27      36.828  64.761  40.737  1.00 19.66           C  
ATOM    201  CD1 ILE A  27      36.414  61.642  40.490  1.00 18.40           C  
ATOM    202  N   GLY A  28      32.479  64.465  40.102  1.00 13.83           N  
ATOM    203  CA  GLY A  28      31.269  63.777  39.703  1.00 11.75           C  
ATOM    204  C   GLY A  28      30.213  64.728  39.210  1.00 11.35           C  
ATOM    205  O   GLY A  28      30.333  65.946  39.349  1.00 13.79           O  
ATOM    206  N   PHE A  29      29.137  64.194  38.655  1.00 11.84           N  
ATOM    207  CA  PHE A  29      28.093  65.001  38.060  1.00 13.54           C  
ATOM    208  C   PHE A  29      27.417  65.914  39.084  1.00 14.44           C  
ATOM    209  O   PHE A  29      27.101  67.064  38.748  1.00 13.05           O  
ATOM    210  CB  PHE A  29      27.063  64.083  37.414  1.00 13.14           C  
ATOM    211  CG  PHE A  29      26.039  64.822  36.550  1.00 14.71           C  
ATOM    212  CD1 PHE A  29      26.460  65.723  35.573  1.00 14.38           C  
ATOM    213  CD2 PHE A  29      24.683  64.565  36.719  1.00 14.14           C  
ATOM    214  CE1 PHE A  29      25.517  66.345  34.772  1.00 16.25           C  
ATOM    215  CE2 PHE A  29      23.757  65.195  35.911  1.00 13.34           C  
ATOM    216  CZ  PHE A  29      24.172  66.086  34.942  1.00 13.29           C  
ATOM    217  N   ASP A  30      27.221  65.466  40.340  1.00 13.38           N  
ATOM    218  CA  ASP A  30      26.635  66.320  41.379  1.00 12.86           C  
ATOM    219  C   ASP A  30      27.511  67.511  41.697  1.00 13.37           C  
ATOM    220  O   ASP A  30      26.999  68.623  41.908  1.00 13.05           O  
ATOM    221  CB  ASP A  30      26.411  65.557  42.690  1.00 11.57           C  
ATOM    222  CG  ASP A  30      25.127  64.729  42.730  1.00 13.94           C  
ATOM    223  OD1 ASP A  30      24.314  64.812  41.819  1.00 13.97           O  
ATOM    224  OD2 ASP A  30      24.929  64.016  43.707  1.00 16.49           O  
ATOM    225  N   ILE A  31      28.823  67.280  41.663  1.00 11.99           N  
ATOM    226  CA  ILE A  31      29.805  68.335  41.952  1.00 14.45           C  
ATOM    227  C   ILE A  31      29.784  69.322  40.779  1.00 13.87           C  
ATOM    228  O   ILE A  31      29.719  70.542  40.977  1.00 12.98           O  
ATOM    229  CB  ILE A  31      31.268  67.702  42.163  1.00 14.01           C  
ATOM    230  CG1 ILE A  31      31.210  66.528  43.194  1.00 15.06           C  
ATOM    231  CG2 ILE A  31      32.265  68.795  42.596  1.00 15.18           C  
ATOM    232  CD1 ILE A  31      30.700  66.787  44.611  1.00 14.01           C  
ATOM    233  N   ASP A  32      29.751  68.825  39.539  1.00 13.63           N  
ATOM    234  CA  ASP A  32      29.694  69.704  38.375  1.00 15.28           C  
ATOM    235  C   ASP A  32      28.444  70.569  38.353  1.00 16.09           C  
ATOM    236  O   ASP A  32      28.535  71.783  38.079  1.00 14.80           O  
ATOM    237  CB  ASP A  32      29.738  68.903  37.073  1.00 14.01           C  
ATOM    238  CG  ASP A  32      31.059  68.189  36.852  1.00 16.22           C  
ATOM    239  OD1 ASP A  32      32.064  68.522  37.483  1.00 17.57           O  
ATOM    240  OD2 ASP A  32      31.091  67.257  36.046  1.00 18.74           O  
ATOM    241  N   LEU A  33      27.276  69.981  38.641  1.00 13.88           N  
ATOM    242  CA  LEU A  33      26.048  70.740  38.701  1.00 14.18           C  
ATOM    243  C   LEU A  33      26.084  71.759  39.839  1.00 15.67           C  
ATOM    244  O   LEU A  33      25.724  72.922  39.600  1.00 15.28           O  
ATOM    245  CB  LEU A  33      24.848  69.822  38.904  1.00 15.52           C  
ATOM    246  CG  LEU A  33      24.379  68.974  37.743  1.00 17.33           C  
ATOM    247  CD1 LEU A  33      23.395  67.933  38.233  1.00 18.87           C  
ATOM    248  CD2 LEU A  33      23.715  69.864  36.715  1.00 18.89           C  
ATOM    249  N   GLY A  34      26.518  71.386  41.059  1.00 14.80           N  
ATOM    250  CA  GLY A  34      26.571  72.316  42.187  1.00 14.16           C  
ATOM    251  C   GLY A  34      27.488  73.500  41.864  1.00 15.34           C  
ATOM    252  O   GLY A  34      27.155  74.678  42.078  1.00 14.79           O  
ATOM    253  N   ASN A  35      28.675  73.223  41.342  1.00 15.42           N  
ATOM    254  CA  ASN A  35      29.611  74.294  41.020  1.00 16.13           C  
ATOM    255  C   ASN A  35      29.121  75.217  39.904  1.00 16.43           C  
ATOM    256  O   ASN A  35      29.310  76.432  39.993  1.00 16.00           O  
ATOM    257  CB  ASN A  35      30.944  73.724  40.613  1.00 14.83           C  
ATOM    258  CG  ASN A  35      31.766  73.186  41.771  1.00 16.08           C  
ATOM    259  OD1 ASN A  35      32.641  72.341  41.565  1.00 20.09           O  
ATOM    260  ND2 ASN A  35      31.565  73.582  43.014  1.00 15.94           N  
ATOM    261  N   GLU A  36      28.451  74.706  38.886  1.00 16.33           N  
ATOM    262  CA  GLU A  36      27.926  75.554  37.825  1.00 17.55           C  
ATOM    263  C   GLU A  36      26.810  76.438  38.379  1.00 17.27           C  
ATOM    264  O   GLU A  36      26.776  77.651  38.130  1.00 17.87           O  
ATOM    265  CB  GLU A  36      27.391  74.686  36.685  1.00 15.86           C  
ATOM    266  CG  GLU A  36      26.879  75.521  35.526  1.00 16.34           C  
ATOM    267  CD  GLU A  36      27.941  76.370  34.829  1.00 21.93           C  
ATOM    268  OE1 GLU A  36      29.128  76.029  34.831  1.00 23.71           O  
ATOM    269  OE2 GLU A  36      27.590  77.399  34.254  1.00 26.13           O  
ATOM    270  N   MET A  37      25.875  75.865  39.175  1.00 16.46           N  
ATOM    271  CA  MET A  37      24.821  76.640  39.826  1.00 16.10           C  
ATOM    272  C   MET A  37      25.429  77.711  40.755  1.00 17.05           C  
ATOM    273  O   MET A  37      25.003  78.873  40.671  1.00 16.31           O  
ATOM    274  CB  MET A  37      23.886  75.737  40.651  1.00 15.80           C  
ATOM    275  CG  MET A  37      22.955  74.926  39.747  1.00 14.66           C  
ATOM    276  SD  MET A  37      21.660  73.972  40.576  1.00 17.97           S  
ATOM    277  CE  MET A  37      22.702  72.738  41.284  1.00 17.59           C  
ATOM    278  N   CYS A  38      26.453  77.414  41.580  1.00 15.99           N  
ATOM    279  CA  CYS A  38      27.073  78.408  42.446  1.00 17.35           C  
ATOM    280  C   CYS A  38      27.647  79.567  41.647  1.00 19.80           C  
ATOM    281  O   CYS A  38      27.463  80.723  42.055  1.00 19.95           O  
ATOM    282  CB  CYS A  38      28.183  77.791  43.266  1.00 17.58           C  
ATOM    283  SG  CYS A  38      27.498  76.595  44.466  1.00 20.66           S  
ATOM    284  N   LYS A  39      28.266  79.256  40.499  1.00 20.84           N  
ATOM    285  CA  LYS A  39      28.826  80.224  39.558  1.00 23.61           C  
ATOM    286  C   LYS A  39      27.707  81.113  39.032  1.00 23.46           C  
ATOM    287  O   LYS A  39      27.840  82.335  39.083  1.00 26.41           O  
ATOM    288  CB  LYS A  39      29.487  79.485  38.409  1.00 26.96           C  
ATOM    289  CG  LYS A  39      30.105  80.357  37.361  1.00 33.91           C  
ATOM    290  CD  LYS A  39      30.240  79.572  36.065  1.00 39.14           C  
ATOM    291  CE  LYS A  39      30.924  80.426  34.986  1.00 46.36           C  
ATOM    292  NZ  LYS A  39      30.187  81.642  34.643  1.00 50.47           N  
ATOM    293  N   ARG A  40      26.583  80.577  38.564  1.00 21.46           N  
ATOM    294  CA  ARG A  40      25.460  81.404  38.148  1.00 22.44           C  
ATOM    295  C   ARG A  40      24.763  82.176  39.264  1.00 26.03           C  
ATOM    296  O   ARG A  40      24.224  83.267  39.026  1.00 24.48           O  
ATOM    297  CB  ARG A  40      24.433  80.557  37.441  1.00 21.95           C  
ATOM    298  CG  ARG A  40      25.156  80.101  36.202  1.00 25.33           C  
ATOM    299  CD  ARG A  40      24.285  79.290  35.319  1.00 27.13           C  
ATOM    300  NE  ARG A  40      25.104  78.716  34.269  1.00 27.40           N  
ATOM    301  CZ  ARG A  40      24.803  78.791  32.975  1.00 25.78           C  
ATOM    302  NH1 ARG A  40      23.715  79.430  32.563  1.00 24.62           N  
ATOM    303  NH2 ARG A  40      25.543  78.118  32.100  1.00 23.53           N  
ATOM    304  N   MET A  41      24.775  81.679  40.510  1.00 25.31           N  
ATOM    305  CA  MET A  41      24.197  82.388  41.649  1.00 24.79           C  
ATOM    306  C   MET A  41      25.094  83.495  42.160  1.00 25.18           C  
ATOM    307  O   MET A  41      24.689  84.331  42.957  1.00 25.42           O  
ATOM    308  CB  MET A  41      23.941  81.423  42.794  1.00 23.25           C  
ATOM    309  CG  MET A  41      22.802  80.475  42.470  1.00 26.37           C  
ATOM    310  SD  MET A  41      22.904  78.973  43.501  1.00 30.87           S  
ATOM    311  CE  MET A  41      22.467  79.756  45.013  1.00 26.91           C  
ATOM    312  N   GLN A  42      26.343  83.451  41.737  1.00 26.53           N  
ATOM    313  CA  GLN A  42      27.366  84.382  42.145  1.00 31.02           C  
ATOM    314  C   GLN A  42      27.618  84.334  43.637  1.00 32.09           C  
ATOM    315  O   GLN A  42      27.889  85.346  44.291  1.00 32.25           O  
ATOM    316  CB  GLN A  42      26.996  85.793  41.757  1.00 33.82           C  
ATOM    317  CG  GLN A  42      26.812  85.904  40.277  1.00 39.78           C  
ATOM    318  CD  GLN A  42      26.060  87.187  40.064  1.00 46.97           C  
ATOM    319  OE1 GLN A  42      24.826  87.239  40.027  1.00 50.83           O  
ATOM    320  NE2 GLN A  42      26.852  88.264  40.060  1.00 48.94           N  
ATOM    321  N   VAL A  43      27.593  83.099  44.166  1.00 30.80           N  
ATOM    322  CA  VAL A  43      27.932  82.839  45.573  1.00 27.55           C  
ATOM    323  C   VAL A  43      29.195  81.989  45.600  1.00 26.63           C  
ATOM    324  O   VAL A  43      29.573  81.372  44.599  1.00 25.88           O  
ATOM    325  CB  VAL A  43      26.844  82.049  46.340  1.00 26.16           C  
ATOM    326  CG1 VAL A  43      25.619  82.921  46.482  1.00 27.57           C  
ATOM    327  CG2 VAL A  43      26.480  80.752  45.611  1.00 25.00           C  
ATOM    328  N   LYS A  44      29.895  81.937  46.714  1.00 26.62           N  
ATOM    329  CA  LYS A  44      31.004  81.025  46.871  1.00 27.88           C  
ATOM    330  C   LYS A  44      30.438  79.747  47.513  1.00 24.71           C  
ATOM    331  O   LYS A  44      29.543  79.849  48.339  1.00 22.37           O  
ATOM    332  CB  LYS A  44      32.040  81.669  47.765  1.00 33.21           C  
ATOM    333  CG  LYS A  44      32.740  82.834  47.097  1.00 41.49           C  
ATOM    334  CD  LYS A  44      33.570  82.271  45.947  1.00 51.18           C  
ATOM    335  CE  LYS A  44      34.670  83.252  45.502  1.00 59.29           C  
ATOM    336  NZ  LYS A  44      34.265  84.063  44.359  1.00 65.84           N  
ATOM    337  N   CYS A  45      30.894  78.540  47.209  1.00 24.02           N  
ATOM    338  CA  CYS A  45      30.320  77.335  47.783  1.00 22.79           C  
ATOM    339  C   CYS A  45      31.423  76.481  48.335  1.00 22.72           C  
ATOM    340  O   CYS A  45      32.483  76.423  47.711  1.00 24.28           O  
ATOM    341  CB  CYS A  45      29.569  76.537  46.723  1.00 19.92           C  
ATOM    342  SG  CYS A  45      28.059  77.354  46.244  1.00 18.17           S  
ATOM    343  N   THR A  46      31.233  75.869  49.489  1.00 19.83           N  
ATOM    344  CA  THR A  46      32.219  74.971  50.048  1.00 21.40           C  
ATOM    345  C   THR A  46      31.590  73.585  50.026  1.00 18.18           C  
ATOM    346  O   THR A  46      30.419  73.484  50.386  1.00 17.31           O  
ATOM    347  CB  THR A  46      32.529  75.375  51.498  1.00 23.78           C  
ATOM    348  OG1 THR A  46      33.132  76.652  51.367  1.00 32.02           O  
ATOM    349  CG2 THR A  46      33.411  74.395  52.264  1.00 23.29           C  
ATOM    350  N   TRP A  47      32.293  72.536  49.629  1.00 17.40           N  
ATOM    351  CA  TRP A  47      31.754  71.184  49.673  1.00 17.03           C  
ATOM    352  C   TRP A  47      32.198  70.539  50.983  1.00 15.97           C  
ATOM    353  O   TRP A  47      33.348  70.691  51.382  1.00 14.61           O  
ATOM    354  CB  TRP A  47      32.265  70.358  48.478  1.00 14.83           C  
ATOM    355  CG  TRP A  47      31.567  70.782  47.192  1.00 17.19           C  
ATOM    356  CD1 TRP A  47      32.109  71.760  46.406  1.00 17.78           C  
ATOM    357  CD2 TRP A  47      30.363  70.304  46.696  1.00 16.73           C  
ATOM    358  NE1 TRP A  47      31.242  71.905  45.424  1.00 19.21           N  
ATOM    359  CE2 TRP A  47      30.201  71.067  45.546  1.00 17.26           C  
ATOM    360  CE3 TRP A  47      29.404  69.356  47.026  1.00 16.33           C  
ATOM    361  CZ2 TRP A  47      29.105  70.906  44.721  1.00 16.75           C  
ATOM    362  CZ3 TRP A  47      28.307  69.184  46.194  1.00 15.15           C  
ATOM    363  CH2 TRP A  47      28.151  69.955  45.053  1.00 14.86           C  
ATOM    364  N   VAL A  48      31.301  69.807  51.637  1.00 14.31           N  
ATOM    365  CA  VAL A  48      31.547  69.172  52.918  1.00 14.88           C  
ATOM    366  C   VAL A  48      31.165  67.707  52.762  1.00 15.08           C  
ATOM    367  O   VAL A  48      30.000  67.424  52.478  1.00 15.26           O  
ATOM    368  CB  VAL A  48      30.674  69.839  54.024  1.00 15.88           C  
ATOM    369  CG1 VAL A  48      30.903  69.134  55.351  1.00 16.37           C  
ATOM    370  CG2 VAL A  48      31.031  71.326  54.172  1.00 16.08           C  
ATOM    371  N   ALA A  49      32.076  66.754  52.960  1.00 15.33           N  
ATOM    372  CA  ALA A  49      31.780  65.334  52.805  1.00 15.13           C  
ATOM    373  C   ALA A  49      31.131  64.845  54.083  1.00 16.05           C  
ATOM    374  O   ALA A  49      31.460  65.309  55.177  1.00 18.52           O  
ATOM    375  CB  ALA A  49      33.060  64.570  52.557  1.00 12.90           C  
ATOM    376  N   SER A  50      30.159  63.965  53.988  1.00 15.69           N  
ATOM    377  CA  SER A  50      29.440  63.431  55.122  1.00 16.86           C  
ATOM    378  C   SER A  50      28.949  62.035  54.757  1.00 17.31           C  
ATOM    379  O   SER A  50      28.798  61.690  53.576  1.00 16.17           O  
ATOM    380  CB  SER A  50      28.287  64.372  55.370  1.00 17.53           C  
ATOM    381  OG  SER A  50      27.241  63.883  56.180  1.00 22.56           O  
ATOM    382  N   ASP A  51      28.760  61.156  55.734  1.00 16.78           N  
ATOM    383  CA  ASP A  51      27.989  59.943  55.490  1.00 16.59           C  
ATOM    384  C   ASP A  51      26.586  60.328  55.053  1.00 14.40           C  
ATOM    385  O   ASP A  51      26.063  61.326  55.564  1.00 12.36           O  
ATOM    386  CB  ASP A  51      27.878  59.113  56.754  1.00 21.14           C  
ATOM    387  CG  ASP A  51      29.142  58.347  57.092  1.00 25.80           C  
ATOM    388  OD1 ASP A  51      30.075  58.292  56.292  1.00 29.48           O  
ATOM    389  OD2 ASP A  51      29.171  57.769  58.167  1.00 33.02           O  
ATOM    390  N   PHE A  52      25.972  59.586  54.129  1.00 11.75           N  
ATOM    391  CA  PHE A  52      24.643  59.891  53.654  1.00 11.91           C  
ATOM    392  C   PHE A  52      23.585  60.092  54.745  1.00 13.27           C  
ATOM    393  O   PHE A  52      22.807  61.040  54.670  1.00 13.67           O  
ATOM    394  CB  PHE A  52      24.175  58.787  52.717  1.00 10.43           C  
ATOM    395  CG  PHE A  52      22.891  59.185  51.981  1.00 12.51           C  
ATOM    396  CD1 PHE A  52      22.945  60.147  50.971  1.00 12.50           C  
ATOM    397  CD2 PHE A  52      21.675  58.617  52.323  1.00 13.44           C  
ATOM    398  CE1 PHE A  52      21.795  60.517  50.312  1.00 10.54           C  
ATOM    399  CE2 PHE A  52      20.526  59.002  51.650  1.00 11.93           C  
ATOM    400  CZ  PHE A  52      20.588  59.935  50.637  1.00 11.81           C  
ATOM    401  N   ASP A  53      23.528  59.261  55.800  1.00 13.50           N  
ATOM    402  CA  ASP A  53      22.498  59.405  56.809  1.00 15.60           C  
ATOM    403  C   ASP A  53      22.722  60.587  57.742  1.00 13.46           C  
ATOM    404  O   ASP A  53      21.829  60.910  58.519  1.00 15.74           O  
ATOM    405  CB  ASP A  53      22.368  58.113  57.657  1.00 18.02           C  
ATOM    406  CG  ASP A  53      23.500  57.786  58.623  1.00 26.91           C  
ATOM    407  OD1 ASP A  53      24.639  58.281  58.472  1.00 27.66           O  
ATOM    408  OD2 ASP A  53      23.211  57.007  59.542  1.00 31.85           O  
ATOM    409  N   ALA A  54      23.875  61.237  57.694  1.00 12.65           N  
ATOM    410  CA  ALA A  54      24.105  62.422  58.501  1.00 11.97           C  
ATOM    411  C   ALA A  54      23.709  63.687  57.736  1.00 14.10           C  
ATOM    412  O   ALA A  54      23.638  64.774  58.339  1.00 14.80           O  
ATOM    413  CB  ALA A  54      25.556  62.510  58.828  1.00 12.54           C  
ATOM    414  N   LEU A  55      23.370  63.611  56.439  1.00 11.96           N  
ATOM    415  CA  LEU A  55      23.158  64.823  55.659  1.00 13.03           C  
ATOM    416  C   LEU A  55      21.933  65.638  56.029  1.00 13.06           C  
ATOM    417  O   LEU A  55      22.025  66.849  56.308  1.00 13.09           O  
ATOM    418  CB  LEU A  55      23.121  64.438  54.184  1.00 12.35           C  
ATOM    419  CG  LEU A  55      24.459  64.006  53.531  1.00 13.62           C  
ATOM    420  CD1 LEU A  55      24.128  63.477  52.167  1.00 14.16           C  
ATOM    421  CD2 LEU A  55      25.457  65.148  53.364  1.00 14.50           C  
ATOM    422  N   ILE A  56      20.757  65.033  56.105  1.00 13.62           N  
ATOM    423  CA  ILE A  56      19.595  65.811  56.494  1.00 14.39           C  
ATOM    424  C   ILE A  56      19.693  66.289  57.959  1.00 15.09           C  
ATOM    425  O   ILE A  56      19.333  67.447  58.159  1.00 13.54           O  
ATOM    426  CB  ILE A  56      18.338  64.935  56.207  1.00 14.71           C  
ATOM    427  CG1 ILE A  56      18.150  64.827  54.685  1.00 12.35           C  
ATOM    428  CG2 ILE A  56      17.095  65.524  56.883  1.00 15.43           C  
ATOM    429  CD1 ILE A  56      16.983  63.926  54.312  1.00 15.81           C  
ATOM    430  N   PRO A  57      20.164  65.542  59.001  1.00 15.70           N  
ATOM    431  CA  PRO A  57      20.490  66.081  60.317  1.00 15.52           C  
ATOM    432  C   PRO A  57      21.407  67.304  60.274  1.00 14.94           C  
ATOM    433  O   PRO A  57      21.138  68.329  60.913  1.00 15.42           O  
ATOM    434  CB  PRO A  57      21.106  64.893  61.062  1.00 16.18           C  
ATOM    435  CG  PRO A  57      20.410  63.689  60.470  1.00 16.97           C  
ATOM    436  CD  PRO A  57      20.376  64.077  58.999  1.00 16.45           C  
ATOM    437  N   SER A  58      22.511  67.227  59.532  1.00 13.91           N  
ATOM    438  CA  SER A  58      23.414  68.361  59.416  1.00 15.77           C  
ATOM    439  C   SER A  58      22.770  69.597  58.819  1.00 15.91           C  
ATOM    440  O   SER A  58      23.083  70.731  59.250  1.00 17.45           O  
ATOM    441  CB  SER A  58      24.613  68.022  58.558  1.00 15.80           C  
ATOM    442  OG  SER A  58      25.269  67.076  59.351  1.00 21.33           O  
ATOM    443  N   LEU A  59      21.925  69.387  57.811  1.00 13.16           N  
ATOM    444  CA  LEU A  59      21.181  70.483  57.201  1.00 15.01           C  
ATOM    445  C   LEU A  59      20.243  71.160  58.222  1.00 16.11           C  
ATOM    446  O   LEU A  59      20.183  72.394  58.364  1.00 14.31           O  
ATOM    447  CB  LEU A  59      20.331  69.972  55.981  1.00 13.82           C  
ATOM    448  CG  LEU A  59      19.487  71.009  55.208  1.00 12.85           C  
ATOM    449  CD1 LEU A  59      20.420  71.977  54.535  1.00 13.12           C  
ATOM    450  CD2 LEU A  59      18.657  70.370  54.147  1.00 14.39           C  
ATOM    451  N   LYS A  60      19.481  70.317  58.936  1.00 15.56           N  
ATOM    452  CA  LYS A  60      18.550  70.823  59.897  1.00 17.39           C  
ATOM    453  C   LYS A  60      19.284  71.552  61.026  1.00 18.98           C  
ATOM    454  O   LYS A  60      18.773  72.547  61.542  1.00 21.08           O  
ATOM    455  CB  LYS A  60      17.716  69.643  60.411  1.00 19.24           C  
ATOM    456  CG  LYS A  60      16.648  69.333  59.390  1.00 22.28           C  
ATOM    457  CD  LYS A  60      15.553  68.507  60.008  1.00 27.40           C  
ATOM    458  CE  LYS A  60      16.008  67.108  60.068  1.00 32.24           C  
ATOM    459  NZ  LYS A  60      15.196  66.376  61.019  1.00 38.72           N  
ATOM    460  N   ALA A  61      20.478  71.113  61.401  1.00 16.99           N  
ATOM    461  CA  ALA A  61      21.269  71.769  62.409  1.00 17.96           C  
ATOM    462  C   ALA A  61      22.079  72.959  61.877  1.00 19.24           C  
ATOM    463  O   ALA A  61      22.820  73.568  62.645  1.00 20.79           O  
ATOM    464  CB  ALA A  61      22.206  70.721  63.028  1.00 17.91           C  
ATOM    465  N   LYS A  62      21.984  73.336  60.597  1.00 17.16           N  
ATOM    466  CA  LYS A  62      22.711  74.422  59.944  1.00 18.01           C  
ATOM    467  C   LYS A  62      24.212  74.229  59.890  1.00 18.23           C  
ATOM    468  O   LYS A  62      24.982  75.182  59.760  1.00 18.78           O  
ATOM    469  CB  LYS A  62      22.414  75.809  60.599  1.00 18.97           C  
ATOM    470  CG  LYS A  62      20.913  76.097  60.573  1.00 25.11           C  
ATOM    471  CD  LYS A  62      20.409  77.452  61.052  1.00 30.04           C  
ATOM    472  CE  LYS A  62      20.613  78.455  59.916  1.00 39.70           C  
ATOM    473  NZ  LYS A  62      19.623  79.536  59.905  1.00 43.23           N  
ATOM    474  N   LYS A  63      24.693  72.978  59.911  1.00 16.97           N  
ATOM    475  CA  LYS A  63      26.120  72.720  59.713  1.00 16.78           C  
ATOM    476  C   LYS A  63      26.488  72.809  58.225  1.00 15.68           C  
ATOM    477  O   LYS A  63      27.666  72.964  57.867  1.00 14.77           O  
ATOM    478  CB  LYS A  63      26.504  71.338  60.209  1.00 18.36           C  
ATOM    479  CG  LYS A  63      26.247  71.151  61.696  1.00 22.51           C  
ATOM    480  CD  LYS A  63      26.838  69.793  61.969  1.00 30.66           C  
ATOM    481  CE  LYS A  63      26.525  69.243  63.353  1.00 36.40           C  
ATOM    482  NZ  LYS A  63      27.089  67.894  63.462  1.00 41.53           N  
ATOM    483  N   ILE A  64      25.467  72.647  57.356  1.00 14.72           N  
ATOM    484  CA  ILE A  64      25.567  72.837  55.900  1.00 14.73           C  
ATOM    485  C   ILE A  64      24.283  73.561  55.508  1.00 12.01           C  
ATOM    486  O   ILE A  64      23.317  73.571  56.276  1.00 13.21           O  
ATOM    487  CB  ILE A  64      25.645  71.496  55.068  1.00 14.76           C  
ATOM    488  CG1 ILE A  64      24.435  70.561  55.372  1.00 14.94           C  
ATOM    489  CG2 ILE A  64      27.065  70.936  55.286  1.00 12.39           C  
ATOM    490  CD1 ILE A  64      24.455  69.211  54.607  1.00 14.75           C  
ATOM    491  N   ASP A  65      24.284  74.149  54.322  1.00 12.00           N  
ATOM    492  CA  ASP A  65      23.167  74.917  53.827  1.00 12.56           C  
ATOM    493  C   ASP A  65      22.400  74.219  52.738  1.00 13.45           C  
ATOM    494  O   ASP A  65      21.265  74.609  52.463  1.00 14.51           O  
ATOM    495  CB  ASP A  65      23.642  76.262  53.275  1.00 13.07           C  
ATOM    496  CG  ASP A  65      24.409  77.002  54.358  1.00 15.79           C  
ATOM    497  OD1 ASP A  65      23.862  77.210  55.444  1.00 17.13           O  
ATOM    498  OD2 ASP A  65      25.581  77.287  54.152  1.00 15.13           O  
ATOM    499  N   ALA A  66      22.989  73.235  52.068  1.00 11.59           N  
ATOM    500  CA  ALA A  66      22.286  72.545  50.996  1.00 12.81           C  
ATOM    501  C   ALA A  66      22.850  71.120  50.866  1.00 13.10           C  
ATOM    502  O   ALA A  66      23.980  70.848  51.330  1.00 14.16           O  
ATOM    503  CB  ALA A  66      22.487  73.313  49.691  1.00 13.49           C  
ATOM    504  N   ILE A  67      22.070  70.210  50.291  1.00 10.64           N  
ATOM    505  CA  ILE A  67      22.524  68.847  50.071  1.00 10.12           C  
ATOM    506  C   ILE A  67      22.454  68.587  48.578  1.00 10.30           C  
ATOM    507  O   ILE A  67      21.354  68.727  47.995  1.00 10.12           O  
ATOM    508  CB  ILE A  67      21.604  67.792  50.785  1.00  9.37           C  
ATOM    509  CG1 ILE A  67      21.586  68.012  52.311  1.00 10.67           C  
ATOM    510  CG2 ILE A  67      22.084  66.360  50.400  1.00  9.02           C  
ATOM    511  CD1 ILE A  67      20.432  67.252  53.015  1.00  9.32           C  
ATOM    512  N   ILE A  68      23.576  68.161  47.971  1.00 10.81           N  
ATOM    513  CA  ILE A  68      23.506  67.659  46.593  1.00 11.87           C  
ATOM    514  C   ILE A  68      24.241  66.326  46.672  1.00 10.47           C  
ATOM    515  O   ILE A  68      25.461  66.259  46.763  1.00 10.15           O  
ATOM    516  CB  ILE A  68      24.184  68.638  45.563  1.00 11.92           C  
ATOM    517  CG1 ILE A  68      23.506  70.028  45.653  1.00 11.08           C  
ATOM    518  CG2 ILE A  68      24.072  68.064  44.138  1.00 10.78           C  
ATOM    519  CD1 ILE A  68      24.188  71.140  44.837  1.00 14.98           C  
ATOM    520  N   SER A  69      23.460  65.253  46.639  1.00 11.42           N  
ATOM    521  CA  SER A  69      24.009  63.932  46.895  1.00 11.66           C  
ATOM    522  C   SER A  69      23.054  62.867  46.370  1.00 12.07           C  
ATOM    523  O   SER A  69      22.723  61.908  47.071  1.00 10.65           O  
ATOM    524  CB  SER A  69      24.222  63.846  48.444  1.00 12.65           C  
ATOM    525  OG  SER A  69      25.137  62.853  48.894  1.00 13.89           O  
ATOM    526  N   SER A  70      22.558  63.008  45.133  1.00 10.07           N  
ATOM    527  CA  SER A  70      21.556  62.113  44.558  1.00 12.14           C  
ATOM    528  C   SER A  70      20.362  61.928  45.508  1.00 12.36           C  
ATOM    529  O   SER A  70      19.782  60.836  45.626  1.00 11.84           O  
ATOM    530  CB  SER A  70      22.183  60.726  44.214  1.00 12.46           C  
ATOM    531  OG  SER A  70      23.299  60.840  43.325  1.00 16.60           O  
ATOM    532  N   LEU A  71      19.951  63.048  46.148  1.00 10.78           N  
ATOM    533  CA  LEU A  71      18.890  63.012  47.149  1.00 11.72           C  
ATOM    534  C   LEU A  71      17.515  63.002  46.516  1.00  9.81           C  
ATOM    535  O   LEU A  71      17.080  64.015  45.986  1.00 10.65           O  
ATOM    536  CB  LEU A  71      19.023  64.219  48.105  1.00 10.85           C  
ATOM    537  CG  LEU A  71      18.148  64.209  49.365  1.00 11.56           C  
ATOM    538  CD1 LEU A  71      18.684  63.122  50.333  1.00 11.36           C  
ATOM    539  CD2 LEU A  71      18.162  65.612  50.032  1.00 12.46           C  
ATOM    540  N   SER A  72      16.839  61.851  46.514  1.00 10.28           N  
ATOM    541  CA  SER A  72      15.519  61.730  45.923  1.00 12.45           C  
ATOM    542  C   SER A  72      14.474  62.576  46.635  1.00 11.94           C  
ATOM    543  O   SER A  72      14.468  62.651  47.860  1.00 10.16           O  
ATOM    544  CB  SER A  72      15.082  60.277  45.947  1.00 12.88           C  
ATOM    545  OG  SER A  72      15.887  59.533  45.035  1.00 11.68           O  
ATOM    546  N   ILE A  73      13.597  63.190  45.837  1.00 11.01           N  
ATOM    547  CA  ILE A  73      12.506  64.043  46.276  1.00 12.13           C  
ATOM    548  C   ILE A  73      11.355  63.111  46.595  1.00 12.81           C  
ATOM    549  O   ILE A  73      10.724  62.535  45.694  1.00 13.61           O  
ATOM    550  CB  ILE A  73      12.086  65.045  45.140  1.00 13.77           C  
ATOM    551  CG1 ILE A  73      13.307  65.812  44.655  1.00 13.02           C  
ATOM    552  CG2 ILE A  73      10.977  65.994  45.666  1.00 14.07           C  
ATOM    553  CD1 ILE A  73      12.991  66.632  43.386  1.00 16.78           C  
ATOM    554  N   THR A  74      11.093  62.887  47.881  1.00 13.53           N  
ATOM    555  CA  THR A  74      10.014  61.970  48.266  1.00 15.54           C  
ATOM    556  C   THR A  74       9.028  62.734  49.126  1.00 15.11           C  
ATOM    557  O   THR A  74       9.398  63.711  49.798  1.00 15.36           O  
ATOM    558  CB  THR A  74      10.543  60.762  49.091  1.00 13.59           C  
ATOM    559  OG1 THR A  74      11.051  61.291  50.317  1.00 13.52           O  
ATOM    560  CG2 THR A  74      11.612  59.984  48.367  1.00 11.79           C  
ATOM    561  N   ASP A  75       7.842  62.162  49.224  1.00 16.67           N  
ATOM    562  CA  ASP A  75       6.796  62.703  50.066  1.00 18.44           C  
ATOM    563  C   ASP A  75       7.280  62.782  51.514  1.00 19.54           C  
ATOM    564  O   ASP A  75       7.120  63.818  52.164  1.00 17.68           O  
ATOM    565  CB  ASP A  75       5.598  61.794  49.912  1.00 21.06           C  
ATOM    566  CG  ASP A  75       4.334  62.216  50.649  1.00 28.60           C  
ATOM    567  OD1 ASP A  75       4.289  63.288  51.267  1.00 30.78           O  
ATOM    568  OD2 ASP A  75       3.358  61.459  50.578  1.00 35.52           O  
ATOM    569  N   LYS A  76       7.900  61.736  52.064  1.00 19.47           N  
ATOM    570  CA  LYS A  76       8.415  61.780  53.425  1.00 22.01           C  
ATOM    571  C   LYS A  76       9.437  62.873  53.714  1.00 21.79           C  
ATOM    572  O   LYS A  76       9.328  63.635  54.695  1.00 22.62           O  
ATOM    573  CB  LYS A  76       9.049  60.465  53.762  1.00 27.58           C  
ATOM    574  CG  LYS A  76       8.143  59.616  54.576  1.00 37.96           C  
ATOM    575  CD  LYS A  76       9.047  58.558  55.189  1.00 48.05           C  
ATOM    576  CE  LYS A  76       9.989  59.184  56.239  1.00 53.49           C  
ATOM    577  NZ  LYS A  76      10.971  58.203  56.679  1.00 58.64           N  
ATOM    578  N   ARG A  77      10.450  62.971  52.851  1.00 17.49           N  
ATOM    579  CA  ARG A  77      11.429  64.031  53.007  1.00 17.00           C  
ATOM    580  C   ARG A  77      10.864  65.452  52.888  1.00 17.05           C  
ATOM    581  O   ARG A  77      11.345  66.352  53.582  1.00 15.65           O  
ATOM    582  CB  ARG A  77      12.552  63.817  51.981  1.00 14.21           C  
ATOM    583  CG  ARG A  77      13.464  62.697  52.432  1.00 11.45           C  
ATOM    584  CD  ARG A  77      14.380  62.319  51.307  1.00 11.85           C  
ATOM    585  NE  ARG A  77      15.257  61.247  51.724  1.00 11.69           N  
ATOM    586  CZ  ARG A  77      15.997  60.551  50.867  1.00 12.42           C  
ATOM    587  NH1 ARG A  77      15.956  60.832  49.554  1.00  9.27           N  
ATOM    588  NH2 ARG A  77      16.797  59.583  51.343  1.00 11.16           N  
ATOM    589  N   GLN A  78       9.827  65.691  52.067  1.00 18.27           N  
ATOM    590  CA  GLN A  78       9.199  67.012  51.945  1.00 21.55           C  
ATOM    591  C   GLN A  78       8.475  67.422  53.213  1.00 22.52           C  
ATOM    592  O   GLN A  78       8.162  68.588  53.394  1.00 23.69           O  
ATOM    593  CB  GLN A  78       8.187  67.051  50.836  1.00 24.03           C  
ATOM    594  CG  GLN A  78       8.922  66.809  49.553  1.00 32.00           C  
ATOM    595  CD  GLN A  78       8.559  67.787  48.467  1.00 36.19           C  
ATOM    596  OE1 GLN A  78       8.151  67.427  47.374  1.00 37.11           O  
ATOM    597  NE2 GLN A  78       8.759  69.075  48.662  1.00 39.70           N  
ATOM    598  N   GLN A  79       8.185  66.506  54.129  1.00 22.41           N  
ATOM    599  CA  GLN A  79       7.604  66.888  55.392  1.00 23.83           C  
ATOM    600  C   GLN A  79       8.681  67.558  56.215  1.00 23.58           C  
ATOM    601  O   GLN A  79       8.361  68.346  57.102  1.00 23.97           O  
ATOM    602  CB  GLN A  79       7.079  65.670  56.156  1.00 26.90           C  
ATOM    603  CG  GLN A  79       6.010  64.882  55.387  1.00 36.88           C  
ATOM    604  CD  GLN A  79       5.088  65.761  54.521  1.00 43.88           C  
ATOM    605  OE1 GLN A  79       4.358  66.638  55.013  1.00 49.04           O  
ATOM    606  NE2 GLN A  79       5.099  65.621  53.189  1.00 44.00           N  
ATOM    607  N   GLU A  80       9.950  67.259  55.963  1.00 21.03           N  
ATOM    608  CA  GLU A  80      11.026  67.779  56.756  1.00 21.77           C  
ATOM    609  C   GLU A  80      11.855  68.876  56.121  1.00 19.91           C  
ATOM    610  O   GLU A  80      12.323  69.769  56.837  1.00 18.77           O  
ATOM    611  CB  GLU A  80      12.025  66.744  57.095  1.00 27.88           C  
ATOM    612  CG  GLU A  80      11.593  65.406  57.595  1.00 38.59           C  
ATOM    613  CD  GLU A  80      12.837  64.602  57.771  1.00 45.72           C  
ATOM    614  OE1 GLU A  80      13.284  63.953  56.833  1.00 49.20           O  
ATOM    615  OE2 GLU A  80      13.394  64.675  58.847  1.00 47.06           O  
ATOM    616  N   ILE A  81      12.135  68.769  54.823  1.00 17.02           N  
ATOM    617  CA  ILE A  81      13.007  69.720  54.149  1.00 15.91           C  
ATOM    618  C   ILE A  81      12.296  70.162  52.874  1.00 15.51           C  
ATOM    619  O   ILE A  81      11.202  69.691  52.568  1.00 16.35           O  
ATOM    620  CB  ILE A  81      14.442  69.099  53.785  1.00 16.52           C  
ATOM    621  CG1 ILE A  81      14.357  67.883  52.847  1.00 14.80           C  
ATOM    622  CG2 ILE A  81      15.138  68.710  55.109  1.00 16.41           C  
ATOM    623  CD1 ILE A  81      15.747  67.483  52.336  1.00 15.73           C  
ATOM    624  N   ALA A  82      12.920  71.093  52.152  1.00 15.01           N  
ATOM    625  CA  ALA A  82      12.446  71.615  50.895  1.00 13.88           C  
ATOM    626  C   ALA A  82      13.429  71.139  49.814  1.00 14.63           C  
ATOM    627  O   ALA A  82      14.595  70.807  50.115  1.00 14.84           O  
ATOM    628  CB  ALA A  82      12.455  73.134  50.921  1.00 14.82           C  
ATOM    629  N   PHE A  83      12.995  71.129  48.548  1.00 13.33           N  
ATOM    630  CA  PHE A  83      13.856  70.719  47.451  1.00 12.95           C  
ATOM    631  C   PHE A  83      13.861  71.720  46.328  1.00 13.68           C  
ATOM    632  O   PHE A  83      12.854  72.375  46.092  1.00 14.28           O  
ATOM    633  CB  PHE A  83      13.416  69.407  46.834  1.00 13.69           C  
ATOM    634  CG  PHE A  83      13.663  68.176  47.703  1.00 15.18           C  
ATOM    635  CD1 PHE A  83      12.691  67.753  48.620  1.00 17.22           C  
ATOM    636  CD2 PHE A  83      14.854  67.472  47.567  1.00 14.91           C  
ATOM    637  CE1 PHE A  83      12.908  66.622  49.401  1.00 14.34           C  
ATOM    638  CE2 PHE A  83      15.045  66.335  48.359  1.00 13.86           C  
ATOM    639  CZ  PHE A  83      14.084  65.919  49.256  1.00 13.55           C  
ATOM    640  N   SER A  84      14.981  71.893  45.644  1.00 13.64           N  
ATOM    641  CA  SER A  84      14.960  72.575  44.350  1.00 15.86           C  
ATOM    642  C   SER A  84      14.105  71.735  43.370  1.00 16.48           C  
ATOM    643  O   SER A  84      13.671  70.614  43.672  1.00 16.01           O  
ATOM    644  CB  SER A  84      16.385  72.675  43.748  1.00 14.81           C  
ATOM    645  OG  SER A  84      16.880  71.380  43.371  1.00 13.32           O  
ATOM    646  N   ASP A  85      13.914  72.220  42.149  1.00 16.87           N  
ATOM    647  CA  ASP A  85      13.408  71.425  41.042  1.00 15.05           C  
ATOM    648  C   ASP A  85      14.371  70.282  40.754  1.00 13.22           C  
ATOM    649  O   ASP A  85      15.532  70.300  41.177  1.00 15.22           O  
ATOM    650  CB  ASP A  85      13.294  72.284  39.781  1.00 18.93           C  
ATOM    651  CG  ASP A  85      12.210  73.331  39.873  1.00 22.03           C  
ATOM    652  OD1 ASP A  85      11.168  73.109  40.483  1.00 23.33           O  
ATOM    653  OD2 ASP A  85      12.414  74.389  39.313  1.00 25.87           O  
ATOM    654  N   LYS A  86      13.906  69.317  39.978  1.00 13.41           N  
ATOM    655  CA  LYS A  86      14.638  68.105  39.675  1.00 12.09           C  
ATOM    656  C   LYS A  86      15.969  68.332  38.993  1.00 11.81           C  
ATOM    657  O   LYS A  86      16.026  69.022  37.983  1.00 14.01           O  
ATOM    658  CB  LYS A  86      13.736  67.226  38.791  1.00 16.15           C  
ATOM    659  CG  LYS A  86      14.355  65.900  38.432  1.00 18.69           C  
ATOM    660  CD  LYS A  86      13.369  64.955  37.769  1.00 21.83           C  
ATOM    661  CE  LYS A  86      13.414  65.061  36.275  1.00 27.12           C  
ATOM    662  NZ  LYS A  86      12.579  64.047  35.639  1.00 31.73           N  
ATOM    663  N   LEU A  87      17.032  67.726  39.486  1.00 10.98           N  
ATOM    664  CA  LEU A  87      18.333  67.722  38.862  1.00 13.40           C  
ATOM    665  C   LEU A  87      18.454  66.560  37.878  1.00 14.45           C  
ATOM    666  O   LEU A  87      19.054  66.754  36.825  1.00 14.60           O  
ATOM    667  CB  LEU A  87      19.431  67.603  39.922  1.00 13.59           C  
ATOM    668  CG  LEU A  87      19.534  68.737  40.990  1.00 18.54           C  
ATOM    669  CD1 LEU A  87      20.711  68.557  41.963  1.00 15.61           C  
ATOM    670  CD2 LEU A  87      19.791  70.022  40.264  1.00 17.80           C  
ATOM    671  N   TYR A  88      17.998  65.335  38.163  1.00 13.98           N  
ATOM    672  CA  TYR A  88      18.009  64.216  37.217  1.00 12.75           C  
ATOM    673  C   TYR A  88      17.128  63.102  37.798  1.00 14.78           C  
ATOM    674  O   TYR A  88      16.745  63.160  38.978  1.00 12.59           O  
ATOM    675  CB  TYR A  88      19.450  63.667  36.963  1.00 11.07           C  
ATOM    676  CG  TYR A  88      20.339  63.422  38.173  1.00 13.10           C  
ATOM    677  CD1 TYR A  88      20.176  62.261  38.919  1.00 11.79           C  
ATOM    678  CD2 TYR A  88      21.233  64.404  38.573  1.00 11.91           C  
ATOM    679  CE1 TYR A  88      20.936  62.072  40.038  1.00 12.29           C  
ATOM    680  CE2 TYR A  88      21.996  64.213  39.696  1.00 11.32           C  
ATOM    681  CZ  TYR A  88      21.853  63.035  40.406  1.00 13.59           C  
ATOM    682  OH  TYR A  88      22.622  62.836  41.529  1.00 13.27           O  
ATOM    683  N   ALA A  89      16.798  62.099  36.997  1.00 12.73           N  
ATOM    684  CA  ALA A  89      15.915  61.020  37.414  1.00 12.74           C  
ATOM    685  C   ALA A  89      16.739  59.973  38.152  1.00 13.92           C  
ATOM    686  O   ALA A  89      17.981  59.921  37.983  1.00 14.89           O  
ATOM    687  CB  ALA A  89      15.286  60.368  36.193  1.00 13.82           C  
ATOM    688  N   ALA A  90      16.113  59.153  38.994  1.00 12.98           N  
ATOM    689  CA  ALA A  90      16.857  58.127  39.672  1.00 14.38           C  
ATOM    690  C   ALA A  90      15.927  56.963  39.971  1.00 17.27           C  
ATOM    691  O   ALA A  90      14.994  57.114  40.785  1.00 21.19           O  
ATOM    692  CB  ALA A  90      17.417  58.676  40.971  1.00 16.51           C  
ATOM    693  N   ASP A  91      16.104  55.829  39.288  1.00 16.38           N  
ATOM    694  CA  ASP A  91      15.370  54.601  39.599  1.00 17.34           C  
ATOM    695  C   ASP A  91      16.224  53.657  40.402  1.00 14.04           C  
ATOM    696  O   ASP A  91      17.445  53.817  40.387  1.00 14.62           O  
ATOM    697  CB  ASP A  91      14.928  53.851  38.348  1.00 20.02           C  
ATOM    698  CG  ASP A  91      13.778  54.594  37.696  1.00 27.36           C  
ATOM    699  OD1 ASP A  91      12.791  54.913  38.355  1.00 29.05           O  
ATOM    700  OD2 ASP A  91      13.885  54.889  36.516  1.00 32.83           O  
ATOM    701  N   SER A  92      15.607  52.704  41.102  1.00 13.73           N  
ATOM    702  CA  SER A  92      16.333  51.721  41.900  1.00 15.74           C  
ATOM    703  C   SER A  92      16.404  50.375  41.183  1.00 15.48           C  
ATOM    704  O   SER A  92      15.423  49.988  40.525  1.00 15.22           O  
ATOM    705  CB  SER A  92      15.644  51.510  43.249  1.00 16.39           C  
ATOM    706  OG  SER A  92      15.965  52.590  44.089  1.00 19.55           O  
ATOM    707  N   ARG A  93      17.480  49.615  41.346  1.00 15.48           N  
ATOM    708  CA  ARG A  93      17.554  48.312  40.687  1.00 16.06           C  
ATOM    709  C   ARG A  93      18.504  47.415  41.472  1.00 14.26           C  
ATOM    710  O   ARG A  93      19.489  47.915  42.062  1.00 15.45           O  
ATOM    711  CB  ARG A  93      18.050  48.521  39.243  1.00 13.70           C  
ATOM    712  CG  ARG A  93      17.781  47.300  38.341  1.00 14.80           C  
ATOM    713  CD  ARG A  93      17.838  47.747  36.890  1.00 14.77           C  
ATOM    714  NE  ARG A  93      17.674  46.598  36.019  1.00 17.33           N  
ATOM    715  CZ  ARG A  93      17.890  46.647  34.697  1.00 19.60           C  
ATOM    716  NH1 ARG A  93      18.279  47.764  34.068  1.00 15.01           N  
ATOM    717  NH2 ARG A  93      17.716  45.515  34.006  1.00 19.41           N  
ATOM    718  N   LEU A  94      18.222  46.107  41.528  1.00 13.91           N  
ATOM    719  CA  LEU A  94      19.081  45.139  42.217  1.00 13.79           C  
ATOM    720  C   LEU A  94      20.257  44.704  41.360  1.00 14.22           C  
ATOM    721  O   LEU A  94      20.124  44.608  40.120  1.00 15.36           O  
ATOM    722  CB  LEU A  94      18.359  43.857  42.556  1.00 15.68           C  
ATOM    723  CG  LEU A  94      17.668  43.561  43.856  1.00 21.73           C  
ATOM    724  CD1 LEU A  94      17.294  42.099  43.788  1.00 19.84           C  
ATOM    725  CD2 LEU A  94      18.545  43.794  45.068  1.00 17.52           C  
ATOM    726  N   ILE A  95      21.408  44.449  41.973  1.00 13.94           N  
ATOM    727  CA  ILE A  95      22.542  43.875  41.271  1.00 16.67           C  
ATOM    728  C   ILE A  95      22.928  42.598  42.017  1.00 20.15           C  
ATOM    729  O   ILE A  95      22.734  42.519  43.238  1.00 19.44           O  
ATOM    730  CB  ILE A  95      23.827  44.742  41.222  1.00 15.58           C  
ATOM    731  CG1 ILE A  95      24.347  45.136  42.567  1.00 13.02           C  
ATOM    732  CG2 ILE A  95      23.486  45.902  40.312  1.00 15.37           C  
ATOM    733  CD1 ILE A  95      25.611  45.998  42.492  1.00 16.40           C  
ATOM    734  N   ALA A  96      23.447  41.594  41.297  1.00 19.82           N  
ATOM    735  CA  ALA A  96      23.864  40.327  41.871  1.00 20.49           C  
ATOM    736  C   ALA A  96      24.893  39.742  40.925  1.00 22.47           C  
ATOM    737  O   ALA A  96      25.236  40.371  39.924  1.00 22.94           O  
ATOM    738  CB  ALA A  96      22.682  39.367  41.968  1.00 20.54           C  
ATOM    739  N   ALA A  97      25.471  38.589  41.246  1.00 23.09           N  
ATOM    740  CA  ALA A  97      26.401  37.881  40.363  1.00 23.45           C  
ATOM    741  C   ALA A  97      25.740  37.511  39.045  1.00 21.88           C  
ATOM    742  O   ALA A  97      24.537  37.230  38.992  1.00 21.95           O  
ATOM    743  CB  ALA A  97      26.890  36.591  41.011  1.00 23.62           C  
ATOM    744  N   LYS A  98      26.520  37.578  37.971  1.00 25.07           N  
ATOM    745  CA  LYS A  98      26.056  37.241  36.636  1.00 29.18           C  
ATOM    746  C   LYS A  98      25.480  35.848  36.650  1.00 30.32           C  
ATOM    747  O   LYS A  98      26.045  34.948  37.271  1.00 30.25           O  
ATOM    748  CB  LYS A  98      27.199  37.261  35.660  1.00 34.17           C  
ATOM    749  CG  LYS A  98      27.249  38.539  34.898  1.00 42.91           C  
ATOM    750  CD  LYS A  98      28.506  38.555  34.065  1.00 48.45           C  
ATOM    751  CE  LYS A  98      28.482  39.762  33.122  1.00 53.89           C  
ATOM    752  NZ  LYS A  98      28.460  41.036  33.825  1.00 56.00           N  
ATOM    753  N   GLY A  99      24.344  35.623  36.029  1.00 31.36           N  
ATOM    754  CA  GLY A  99      23.804  34.280  36.062  1.00 35.05           C  
ATOM    755  C   GLY A  99      22.978  33.982  37.291  1.00 37.36           C  
ATOM    756  O   GLY A  99      22.328  32.930  37.357  1.00 39.51           O  
ATOM    757  N   SER A 100      22.970  34.873  38.281  1.00 36.92           N  
ATOM    758  CA  SER A 100      22.102  34.727  39.436  1.00 37.12           C  
ATOM    759  C   SER A 100      20.631  34.578  39.031  1.00 35.00           C  
ATOM    760  O   SER A 100      20.090  35.342  38.225  1.00 35.00           O  
ATOM    761  CB  SER A 100      22.211  35.945  40.347  1.00 36.99           C  
ATOM    762  OG  SER A 100      21.424  35.743  41.506  1.00 39.62           O  
ATOM    763  N   PRO A 101      19.920  33.628  39.613  1.00 34.20           N  
ATOM    764  CA  PRO A 101      18.474  33.552  39.529  1.00 35.26           C  
ATOM    765  C   PRO A 101      17.745  34.657  40.288  1.00 36.30           C  
ATOM    766  O   PRO A 101      16.527  34.780  40.105  1.00 38.00           O  
ATOM    767  CB  PRO A 101      18.172  32.202  40.061  1.00 36.06           C  
ATOM    768  CG  PRO A 101      19.232  32.098  41.140  1.00 36.24           C  
ATOM    769  CD  PRO A 101      20.473  32.548  40.408  1.00 33.67           C  
ATOM    770  N   ILE A 102      18.434  35.457  41.127  1.00 34.37           N  
ATOM    771  CA  ILE A 102      17.791  36.473  41.946  1.00 31.46           C  
ATOM    772  C   ILE A 102      16.972  37.477  41.131  1.00 30.10           C  
ATOM    773  O   ILE A 102      17.324  37.973  40.062  1.00 28.16           O  
ATOM    774  CB  ILE A 102      18.923  37.133  42.796  1.00 33.20           C  
ATOM    775  CG1 ILE A 102      19.302  36.165  43.918  1.00 32.21           C  
ATOM    776  CG2 ILE A 102      18.499  38.493  43.350  1.00 34.21           C  
ATOM    777  CD1 ILE A 102      20.494  36.636  44.772  1.00 31.44           C  
ATOM    778  N   GLN A 103      15.786  37.693  41.653  1.00 29.15           N  
ATOM    779  CA  GLN A 103      14.824  38.619  41.119  1.00 28.44           C  
ATOM    780  C   GLN A 103      14.467  39.518  42.281  1.00 28.16           C  
ATOM    781  O   GLN A 103      14.573  39.079  43.440  1.00 26.84           O  
ATOM    782  CB  GLN A 103      13.584  37.876  40.646  1.00 30.01           C  
ATOM    783  CG  GLN A 103      13.803  37.153  39.331  1.00 34.02           C  
ATOM    784  CD  GLN A 103      14.153  38.117  38.209  1.00 37.55           C  
ATOM    785  OE1 GLN A 103      13.428  39.075  37.912  1.00 38.59           O  
ATOM    786  NE2 GLN A 103      15.303  37.902  37.588  1.00 39.19           N  
ATOM    787  N   PRO A 104      13.999  40.751  42.082  1.00 27.32           N  
ATOM    788  CA  PRO A 104      13.597  41.616  43.190  1.00 28.33           C  
ATOM    789  C   PRO A 104      12.294  41.106  43.823  1.00 29.66           C  
ATOM    790  O   PRO A 104      11.322  41.870  43.867  1.00 31.99           O  
ATOM    791  CB  PRO A 104      13.517  42.999  42.527  1.00 27.69           C  
ATOM    792  CG  PRO A 104      13.048  42.681  41.127  1.00 28.00           C  
ATOM    793  CD  PRO A 104      13.863  41.424  40.791  1.00 25.98           C  
ATOM    794  N   THR A 105      12.152  39.856  44.292  1.00 28.92           N  
ATOM    795  CA  THR A 105      10.885  39.404  44.850  1.00 30.17           C  
ATOM    796  C   THR A 105      11.194  38.724  46.162  1.00 29.27           C  
ATOM    797  O   THR A 105      12.302  38.219  46.370  1.00 28.33           O  
ATOM    798  CB  THR A 105      10.149  38.397  43.926  1.00 31.04           C  
ATOM    799  OG1 THR A 105      10.956  37.231  43.765  1.00 31.97           O  
ATOM    800  CG2 THR A 105       9.829  39.036  42.569  1.00 32.94           C  
ATOM    801  N   LEU A 106      10.180  38.613  46.998  1.00 29.84           N  
ATOM    802  CA  LEU A 106      10.348  38.085  48.329  1.00 31.10           C  
ATOM    803  C   LEU A 106      10.741  36.633  48.258  1.00 32.05           C  
ATOM    804  O   LEU A 106      11.660  36.174  48.941  1.00 34.35           O  
ATOM    805  CB  LEU A 106       9.036  38.254  49.092  1.00 33.26           C  
ATOM    806  CG  LEU A 106       8.972  37.908  50.567  1.00 34.33           C  
ATOM    807  CD1 LEU A 106       9.961  38.788  51.322  1.00 33.53           C  
ATOM    808  CD2 LEU A 106       7.549  38.098  51.062  1.00 32.40           C  
ATOM    809  N   GLU A 107      10.100  35.953  47.336  1.00 33.53           N  
ATOM    810  CA  GLU A 107      10.282  34.533  47.107  1.00 36.49           C  
ATOM    811  C   GLU A 107      11.704  34.225  46.662  1.00 35.77           C  
ATOM    812  O   GLU A 107      12.313  33.233  47.061  1.00 37.36           O  
ATOM    813  CB  GLU A 107       9.294  34.003  46.044  1.00 41.40           C  
ATOM    814  CG  GLU A 107       8.467  34.955  45.142  1.00 52.22           C  
ATOM    815  CD  GLU A 107       7.584  35.951  45.902  1.00 56.78           C  
ATOM    816  OE1 GLU A 107       6.724  35.529  46.669  1.00 60.24           O  
ATOM    817  OE2 GLU A 107       7.832  37.158  45.801  1.00 60.57           O  
ATOM    818  N   SER A 108      12.298  35.103  45.859  1.00 34.44           N  
ATOM    819  CA  SER A 108      13.659  34.952  45.391  1.00 30.99           C  
ATOM    820  C   SER A 108      14.684  35.299  46.468  1.00 28.95           C  
ATOM    821  O   SER A 108      15.764  34.715  46.568  1.00 29.17           O  
ATOM    822  CB  SER A 108      13.749  35.865  44.195  1.00 33.26           C  
ATOM    823  OG  SER A 108      14.908  35.652  43.422  1.00 39.01           O  
ATOM    824  N   LEU A 109      14.362  36.313  47.258  1.00 25.94           N  
ATOM    825  CA  LEU A 109      15.299  36.875  48.196  1.00 23.82           C  
ATOM    826  C   LEU A 109      15.203  36.335  49.598  1.00 24.87           C  
ATOM    827  O   LEU A 109      16.103  36.634  50.397  1.00 23.18           O  
ATOM    828  CB  LEU A 109      15.114  38.401  48.235  1.00 22.80           C  
ATOM    829  CG  LEU A 109      15.460  39.206  46.987  1.00 21.63           C  
ATOM    830  CD1 LEU A 109      14.928  40.618  47.111  1.00 21.70           C  
ATOM    831  CD2 LEU A 109      16.969  39.176  46.795  1.00 21.85           C  
ATOM    832  N   LYS A 110      14.130  35.627  49.983  1.00 26.76           N  
ATOM    833  CA  LYS A 110      14.022  35.166  51.367  1.00 27.86           C  
ATOM    834  C   LYS A 110      15.251  34.313  51.688  1.00 29.00           C  
ATOM    835  O   LYS A 110      15.711  33.507  50.861  1.00 30.06           O  
ATOM    836  CB  LYS A 110      12.738  34.359  51.537  1.00 29.94           C  
ATOM    837  N   GLY A 111      15.870  34.628  52.837  1.00 28.34           N  
ATOM    838  CA  GLY A 111      17.119  33.979  53.208  1.00 30.18           C  
ATOM    839  C   GLY A 111      18.386  34.506  52.513  1.00 31.14           C  
ATOM    840  O   GLY A 111      19.492  34.004  52.768  1.00 34.05           O  
ATOM    841  N   LYS A 112      18.331  35.493  51.622  1.00 30.36           N  
ATOM    842  CA  LYS A 112      19.525  36.035  50.987  1.00 28.08           C  
ATOM    843  C   LYS A 112      20.007  37.230  51.815  1.00 24.88           C  
ATOM    844  O   LYS A 112      19.281  37.749  52.669  1.00 24.82           O  
ATOM    845  CB  LYS A 112      19.214  36.507  49.584  1.00 31.78           C  
ATOM    846  CG  LYS A 112      18.724  35.440  48.630  1.00 38.72           C  
ATOM    847  CD  LYS A 112      19.795  34.393  48.480  1.00 44.14           C  
ATOM    848  CE  LYS A 112      19.375  33.381  47.428  1.00 48.51           C  
ATOM    849  NZ  LYS A 112      20.417  32.374  47.283  1.00 51.23           N  
ATOM    850  N   HIS A 113      21.217  37.727  51.577  1.00 21.53           N  
ATOM    851  CA  HIS A 113      21.757  38.839  52.333  1.00 20.75           C  
ATOM    852  C   HIS A 113      21.778  39.920  51.276  1.00 19.77           C  
ATOM    853  O   HIS A 113      22.429  39.719  50.238  1.00 18.46           O  
ATOM    854  CB  HIS A 113      23.171  38.587  52.792  1.00 22.94           C  
ATOM    855  CG  HIS A 113      23.303  37.252  53.470  1.00 27.97           C  
ATOM    856  ND1 HIS A 113      22.749  36.841  54.598  1.00 28.32           N  
ATOM    857  CD2 HIS A 113      23.993  36.209  52.910  1.00 31.04           C  
ATOM    858  CE1 HIS A 113      23.066  35.580  54.729  1.00 31.51           C  
ATOM    859  NE2 HIS A 113      23.823  35.208  53.718  1.00 32.43           N  
ATOM    860  N   VAL A 114      21.049  41.008  51.519  1.00 19.31           N  
ATOM    861  CA  VAL A 114      20.891  42.133  50.592  1.00 18.24           C  
ATOM    862  C   VAL A 114      21.419  43.404  51.273  1.00 17.31           C  
ATOM    863  O   VAL A 114      20.998  43.744  52.391  1.00 16.61           O  
ATOM    864  CB  VAL A 114      19.403  42.318  50.245  1.00 17.25           C  
ATOM    865  CG1 VAL A 114      19.244  43.523  49.311  1.00 16.03           C  
ATOM    866  CG2 VAL A 114      18.857  41.027  49.639  1.00 16.69           C  
ATOM    867  N   GLY A 115      22.350  44.079  50.610  1.00 15.63           N  
ATOM    868  CA  GLY A 115      22.928  45.299  51.164  1.00 15.70           C  
ATOM    869  C   GLY A 115      22.184  46.541  50.675  1.00 16.13           C  
ATOM    870  O   GLY A 115      21.767  46.603  49.499  1.00 14.82           O  
ATOM    871  N   VAL A 116      22.022  47.528  51.577  1.00 14.94           N  
ATOM    872  CA  VAL A 116      21.383  48.805  51.253  1.00 13.71           C  
ATOM    873  C   VAL A 116      22.136  49.860  52.054  1.00 14.75           C  
ATOM    874  O   VAL A 116      22.702  49.628  53.142  1.00 13.48           O  
ATOM    875  CB  VAL A 116      19.844  48.890  51.652  1.00 14.30           C  
ATOM    876  CG1 VAL A 116      18.995  48.019  50.718  1.00 13.67           C  
ATOM    877  CG2 VAL A 116      19.663  48.481  53.133  1.00 11.62           C  
ATOM    878  N   LEU A 117      22.160  51.070  51.499  1.00 13.89           N  
ATOM    879  CA  LEU A 117      22.799  52.208  52.165  1.00 12.80           C  
ATOM    880  C   LEU A 117      21.913  52.719  53.297  1.00 11.73           C  
ATOM    881  O   LEU A 117      20.735  53.001  53.090  1.00 12.46           O  
ATOM    882  CB  LEU A 117      23.049  53.324  51.117  1.00 12.14           C  
ATOM    883  CG  LEU A 117      23.605  54.679  51.558  1.00 12.24           C  
ATOM    884  CD1 LEU A 117      24.995  54.528  52.152  1.00 10.04           C  
ATOM    885  CD2 LEU A 117      23.657  55.598  50.319  1.00 11.32           C  
ATOM    886  N   GLN A 118      22.488  52.874  54.474  1.00 12.23           N  
ATOM    887  CA  GLN A 118      21.783  53.432  55.619  1.00 15.68           C  
ATOM    888  C   GLN A 118      21.344  54.887  55.306  1.00 14.78           C  
ATOM    889  O   GLN A 118      22.109  55.779  54.879  1.00 15.49           O  
ATOM    890  CB  GLN A 118      22.762  53.329  56.792  1.00 17.88           C  
ATOM    891  CG  GLN A 118      22.419  53.608  58.250  1.00 29.24           C  
ATOM    892  CD  GLN A 118      23.535  53.055  59.156  1.00 33.48           C  
ATOM    893  OE1 GLN A 118      24.746  53.335  59.050  1.00 37.01           O  
ATOM    894  NE2 GLN A 118      23.092  52.196  60.054  1.00 36.34           N  
ATOM    895  N   GLY A 119      20.065  55.122  55.493  1.00 14.60           N  
ATOM    896  CA  GLY A 119      19.479  56.436  55.347  1.00 14.17           C  
ATOM    897  C   GLY A 119      18.836  56.598  53.986  1.00 15.08           C  
ATOM    898  O   GLY A 119      18.167  57.616  53.783  1.00 13.84           O  
ATOM    899  N   SER A 120      18.964  55.627  53.054  1.00 14.81           N  
ATOM    900  CA  SER A 120      18.424  55.755  51.710  1.00 13.25           C  
ATOM    901  C   SER A 120      16.974  55.346  51.582  1.00 12.24           C  
ATOM    902  O   SER A 120      16.401  54.647  52.433  1.00 10.20           O  
ATOM    903  CB  SER A 120      19.279  54.928  50.749  1.00 12.04           C  
ATOM    904  OG  SER A 120      19.157  53.536  51.051  1.00 11.99           O  
ATOM    905  N   THR A 121      16.371  55.725  50.464  1.00 10.97           N  
ATOM    906  CA  THR A 121      15.021  55.284  50.134  1.00 11.94           C  
ATOM    907  C   THR A 121      15.048  53.746  49.931  1.00 12.74           C  
ATOM    908  O   THR A 121      14.078  53.065  50.256  1.00 11.85           O  
ATOM    909  CB  THR A 121      14.547  55.953  48.858  1.00 13.02           C  
ATOM    910  OG1 THR A 121      15.542  55.654  47.892  1.00 13.93           O  
ATOM    911  CG2 THR A 121      14.376  57.464  48.984  1.00 12.92           C  
ATOM    912  N   GLN A 122      16.164  53.172  49.439  1.00 12.16           N  
ATOM    913  CA  GLN A 122      16.316  51.721  49.293  1.00 11.55           C  
ATOM    914  C   GLN A 122      16.274  51.007  50.641  1.00 12.31           C  
ATOM    915  O   GLN A 122      15.636  49.960  50.725  1.00 12.56           O  
ATOM    916  CB  GLN A 122      17.641  51.381  48.615  1.00 12.22           C  
ATOM    917  CG  GLN A 122      17.719  51.761  47.134  1.00 13.61           C  
ATOM    918  CD  GLN A 122      18.195  53.186  46.864  1.00 17.16           C  
ATOM    919  OE1 GLN A 122      18.767  53.882  47.714  1.00 14.01           O  
ATOM    920  NE2 GLN A 122      17.980  53.639  45.647  1.00 15.39           N  
ATOM    921  N   GLU A 123      16.867  51.587  51.699  1.00 11.94           N  
ATOM    922  CA  GLU A 123      16.851  51.009  53.029  1.00 13.92           C  
ATOM    923  C   GLU A 123      15.405  51.015  53.491  1.00 15.82           C  
ATOM    924  O   GLU A 123      14.930  49.973  53.947  1.00 15.54           O  
ATOM    925  CB  GLU A 123      17.659  51.825  54.004  1.00 14.05           C  
ATOM    926  CG  GLU A 123      17.623  51.206  55.394  1.00 17.19           C  
ATOM    927  CD  GLU A 123      18.211  52.081  56.468  1.00 18.73           C  
ATOM    928  OE1 GLU A 123      18.106  53.282  56.411  1.00 19.48           O  
ATOM    929  OE2 GLU A 123      18.802  51.568  57.382  1.00 22.75           O  
ATOM    930  N   ALA A 124      14.651  52.114  53.306  1.00 15.72           N  
ATOM    931  CA  ALA A 124      13.240  52.153  53.703  1.00 16.66           C  
ATOM    932  C   ALA A 124      12.406  51.057  53.038  1.00 16.81           C  
ATOM    933  O   ALA A 124      11.669  50.306  53.685  1.00 15.49           O  
ATOM    934  CB  ALA A 124      12.614  53.493  53.328  1.00 17.04           C  
ATOM    935  N   TYR A 125      12.565  50.925  51.713  1.00 16.70           N  
ATOM    936  CA  TYR A 125      11.850  49.955  50.931  1.00 15.84           C  
ATOM    937  C   TYR A 125      12.174  48.546  51.385  1.00 17.62           C  
ATOM    938  O   TYR A 125      11.246  47.755  51.609  1.00 16.98           O  
ATOM    939  CB  TYR A 125      12.221  50.118  49.474  1.00 17.57           C  
ATOM    940  CG  TYR A 125      11.492  49.149  48.556  1.00 18.73           C  
ATOM    941  CD1 TYR A 125      10.229  49.481  48.108  1.00 21.69           C  
ATOM    942  CD2 TYR A 125      12.064  47.929  48.209  1.00 21.28           C  
ATOM    943  CE1 TYR A 125       9.520  48.600  47.317  1.00 21.29           C  
ATOM    944  CE2 TYR A 125      11.362  47.033  47.428  1.00 21.54           C  
ATOM    945  CZ  TYR A 125      10.100  47.389  46.999  1.00 23.42           C  
ATOM    946  OH  TYR A 125       9.393  46.508  46.234  1.00 25.79           O  
ATOM    947  N   ALA A 126      13.465  48.220  51.477  1.00 16.28           N  
ATOM    948  CA  ALA A 126      13.914  46.867  51.815  1.00 15.86           C  
ATOM    949  C   ALA A 126      13.535  46.530  53.254  1.00 17.88           C  
ATOM    950  O   ALA A 126      13.114  45.409  53.550  1.00 17.60           O  
ATOM    951  CB  ALA A 126      15.429  46.760  51.659  1.00 13.67           C  
ATOM    952  N   ASN A 127      13.584  47.480  54.192  1.00 18.64           N  
ATOM    953  CA  ASN A 127      13.228  47.199  55.570  1.00 19.84           C  
ATOM    954  C   ASN A 127      11.763  46.869  55.683  1.00 21.74           C  
ATOM    955  O   ASN A 127      11.416  45.814  56.233  1.00 23.77           O  
ATOM    956  CB  ASN A 127      13.525  48.374  56.475  1.00 19.02           C  
ATOM    957  CG  ASN A 127      14.962  48.413  56.937  1.00 19.57           C  
ATOM    958  OD1 ASN A 127      15.363  49.317  57.645  1.00 25.04           O  
ATOM    959  ND2 ASN A 127      15.883  47.506  56.745  1.00 19.49           N  
ATOM    960  N   ASP A 128      10.894  47.685  55.085  1.00 21.57           N  
ATOM    961  CA  ASP A 128       9.462  47.410  55.168  1.00 21.82           C  
ATOM    962  C   ASP A 128       9.039  46.140  54.433  1.00 22.87           C  
ATOM    963  O   ASP A 128       8.348  45.286  55.000  1.00 23.68           O  
ATOM    964  CB  ASP A 128       8.647  48.592  54.604  1.00 20.12           C  
ATOM    965  CG  ASP A 128       8.786  49.867  55.384  1.00 24.66           C  
ATOM    966  OD1 ASP A 128       9.309  49.895  56.485  1.00 28.55           O  
ATOM    967  OD2 ASP A 128       8.374  50.883  54.902  1.00 26.01           O  
ATOM    968  N   ASN A 129       9.544  45.976  53.210  1.00 20.90           N  
ATOM    969  CA  ASN A 129       9.065  44.911  52.351  1.00 21.18           C  
ATOM    970  C   ASN A 129       9.745  43.582  52.418  1.00 19.10           C  
ATOM    971  O   ASN A 129       9.159  42.560  52.058  1.00 19.18           O  
ATOM    972  CB  ASN A 129       9.099  45.360  50.895  1.00 21.98           C  
ATOM    973  CG  ASN A 129       8.154  46.528  50.670  1.00 27.57           C  
ATOM    974  OD1 ASN A 129       6.949  46.339  50.658  1.00 31.51           O  
ATOM    975  ND2 ASN A 129       8.549  47.791  50.546  1.00 28.55           N  
ATOM    976  N   TRP A 130      11.009  43.602  52.816  1.00 17.94           N  
ATOM    977  CA  TRP A 130      11.821  42.414  52.753  1.00 17.44           C  
ATOM    978  C   TRP A 130      12.323  42.004  54.124  1.00 19.98           C  
ATOM    979  O   TRP A 130      12.173  40.823  54.479  1.00 20.55           O  
ATOM    980  CB  TRP A 130      13.046  42.618  51.797  1.00 16.76           C  
ATOM    981  CG  TRP A 130      12.731  42.849  50.309  1.00 18.85           C  
ATOM    982  CD1 TRP A 130      11.505  42.538  49.762  1.00 20.79           C  
ATOM    983  CD2 TRP A 130      13.589  43.390  49.364  1.00 18.32           C  
ATOM    984  NE1 TRP A 130      11.582  42.892  48.494  1.00 23.69           N  
ATOM    985  CE2 TRP A 130      12.798  43.388  48.214  1.00 20.70           C  
ATOM    986  CE3 TRP A 130      14.880  43.870  49.313  1.00 18.40           C  
ATOM    987  CZ2 TRP A 130      13.244  43.847  46.987  1.00 16.30           C  
ATOM    988  CZ3 TRP A 130      15.344  44.321  48.087  1.00 21.34           C  
ATOM    989  CH2 TRP A 130      14.528  44.327  46.956  1.00 19.28           C  
ATOM    990  N   ARG A 131      12.889  42.905  54.936  1.00 18.42           N  
ATOM    991  CA  ARG A 131      13.462  42.523  56.215  1.00 19.21           C  
ATOM    992  C   ARG A 131      12.389  41.923  57.119  1.00 19.46           C  
ATOM    993  O   ARG A 131      12.659  40.896  57.734  1.00 19.58           O  
ATOM    994  CB  ARG A 131      14.090  43.734  56.898  1.00 19.53           C  
ATOM    995  CG  ARG A 131      14.772  43.426  58.228  1.00 28.62           C  
ATOM    996  CD  ARG A 131      15.296  44.713  58.910  1.00 34.05           C  
ATOM    997  NE  ARG A 131      14.935  44.731  60.332  1.00 41.70           N  
ATOM    998  CZ  ARG A 131      15.601  44.010  61.259  1.00 45.19           C  
ATOM    999  NH1 ARG A 131      16.648  43.245  60.916  1.00 46.77           N  
ATOM   1000  NH2 ARG A 131      15.176  43.968  62.530  1.00 46.36           N  
ATOM   1001  N   THR A 132      11.161  42.449  57.131  1.00 18.11           N  
ATOM   1002  CA  THR A 132      10.107  41.951  58.003  1.00 19.57           C  
ATOM   1003  C   THR A 132       9.737  40.510  57.646  1.00 20.83           C  
ATOM   1004  O   THR A 132       9.306  39.743  58.513  1.00 20.00           O  
ATOM   1005  CB  THR A 132       8.848  42.832  57.880  1.00 19.44           C  
ATOM   1006  OG1 THR A 132       8.580  42.877  56.479  1.00 23.19           O  
ATOM   1007  CG2 THR A 132       9.017  44.256  58.413  1.00 22.74           C  
ATOM   1008  N   LYS A 133       9.934  40.123  56.382  1.00 19.72           N  
ATOM   1009  CA  LYS A 133       9.536  38.822  55.898  1.00 20.53           C  
ATOM   1010  C   LYS A 133      10.691  37.849  55.853  1.00 21.74           C  
ATOM   1011  O   LYS A 133      10.606  36.808  55.210  1.00 22.84           O  
ATOM   1012  CB  LYS A 133       8.965  38.967  54.529  1.00 21.23           C  
ATOM   1013  CG  LYS A 133       7.830  39.952  54.365  1.00 23.82           C  
ATOM   1014  CD  LYS A 133       6.624  39.521  55.148  1.00 27.50           C  
ATOM   1015  CE  LYS A 133       5.672  40.687  55.149  1.00 31.75           C  
ATOM   1016  NZ  LYS A 133       4.407  40.232  55.679  1.00 39.10           N  
ATOM   1017  N   GLY A 134      11.809  38.140  56.486  1.00 21.87           N  
ATOM   1018  CA  GLY A 134      12.904  37.212  56.579  1.00 22.84           C  
ATOM   1019  C   GLY A 134      14.001  37.353  55.545  1.00 22.89           C  
ATOM   1020  O   GLY A 134      14.765  36.389  55.366  1.00 25.41           O  
ATOM   1021  N   VAL A 135      14.103  38.440  54.794  1.00 20.53           N  
ATOM   1022  CA  VAL A 135      15.261  38.605  53.919  1.00 17.46           C  
ATOM   1023  C   VAL A 135      16.310  39.197  54.840  1.00 18.15           C  
ATOM   1024  O   VAL A 135      15.950  40.031  55.672  1.00 19.12           O  
ATOM   1025  CB  VAL A 135      14.968  39.591  52.791  1.00 18.26           C  
ATOM   1026  CG1 VAL A 135      16.203  39.823  51.897  1.00 17.09           C  
ATOM   1027  CG2 VAL A 135      13.783  39.035  52.019  1.00 16.92           C  
ATOM   1028  N   ASP A 136      17.594  38.820  54.759  1.00 17.46           N  
ATOM   1029  CA  ASP A 136      18.611  39.440  55.600  1.00 17.71           C  
ATOM   1030  C   ASP A 136      19.062  40.769  54.968  1.00 16.70           C  
ATOM   1031  O   ASP A 136      20.042  40.813  54.220  1.00 17.96           O  
ATOM   1032  CB  ASP A 136      19.811  38.483  55.759  1.00 19.49           C  
ATOM   1033  CG  ASP A 136      20.934  39.009  56.646  1.00 23.88           C  
ATOM   1034  OD1 ASP A 136      20.635  39.645  57.658  1.00 24.89           O  
ATOM   1035  OD2 ASP A 136      22.111  38.799  56.326  1.00 26.01           O  
ATOM   1036  N   VAL A 137      18.398  41.859  55.314  1.00 14.35           N  
ATOM   1037  CA  VAL A 137      18.718  43.175  54.772  1.00 15.33           C  
ATOM   1038  C   VAL A 137      19.762  43.766  55.704  1.00 15.73           C  
ATOM   1039  O   VAL A 137      19.490  43.925  56.897  1.00 17.81           O  
ATOM   1040  CB  VAL A 137      17.429  44.074  54.729  1.00 15.55           C  
ATOM   1041  CG1 VAL A 137      17.824  45.493  54.291  1.00 18.06           C  
ATOM   1042  CG2 VAL A 137      16.407  43.548  53.739  1.00 13.38           C  
ATOM   1043  N   VAL A 138      20.918  44.128  55.178  1.00 14.44           N  
ATOM   1044  CA  VAL A 138      22.026  44.652  55.935  1.00 14.78           C  
ATOM   1045  C   VAL A 138      22.225  46.116  55.547  1.00 15.19           C  
ATOM   1046  O   VAL A 138      22.420  46.386  54.358  1.00 16.58           O  
ATOM   1047  CB  VAL A 138      23.288  43.860  55.601  1.00 16.13           C  
ATOM   1048  CG1 VAL A 138      24.385  44.339  56.540  1.00 18.41           C  
ATOM   1049  CG2 VAL A 138      23.051  42.334  55.716  1.00 18.05           C  
ATOM   1050  N   ALA A 139      22.223  47.064  56.495  1.00 15.67           N  
ATOM   1051  CA  ALA A 139      22.393  48.491  56.213  1.00 15.40           C  
ATOM   1052  C   ALA A 139      23.857  48.874  56.336  1.00 16.35           C  
ATOM   1053  O   ALA A 139      24.540  48.452  57.278  1.00 18.29           O  
ATOM   1054  CB  ALA A 139      21.581  49.337  57.204  1.00 15.25           C  
ATOM   1055  N   TYR A 140      24.372  49.659  55.392  1.00 16.15           N  
ATOM   1056  CA  TYR A 140      25.787  50.013  55.363  1.00 16.64           C  
ATOM   1057  C   TYR A 140      26.002  51.515  55.487  1.00 16.25           C  
ATOM   1058  O   TYR A 140      25.166  52.290  55.011  1.00 15.77           O  
ATOM   1059  CB  TYR A 140      26.466  49.563  54.046  1.00 15.82           C  
ATOM   1060  CG  TYR A 140      26.721  48.076  53.929  1.00 16.34           C  
ATOM   1061  CD1 TYR A 140      25.678  47.182  53.727  1.00 16.62           C  
ATOM   1062  CD2 TYR A 140      28.023  47.626  54.062  1.00 18.35           C  
ATOM   1063  CE1 TYR A 140      25.948  45.817  53.678  1.00 16.95           C  
ATOM   1064  CE2 TYR A 140      28.300  46.264  54.008  1.00 17.09           C  
ATOM   1065  CZ  TYR A 140      27.256  45.365  53.830  1.00 18.82           C  
ATOM   1066  OH  TYR A 140      27.542  43.998  53.825  1.00 18.19           O  
ATOM   1067  N   ALA A 141      27.136  51.924  56.059  1.00 14.65           N  
ATOM   1068  CA  ALA A 141      27.472  53.331  56.230  1.00 16.10           C  
ATOM   1069  C   ALA A 141      27.685  54.031  54.886  1.00 16.09           C  
ATOM   1070  O   ALA A 141      27.349  55.218  54.751  1.00 16.52           O  
ATOM   1071  CB  ALA A 141      28.767  53.546  57.026  1.00 15.32           C  
ATOM   1072  N   ASN A 142      28.224  53.340  53.865  1.00 16.14           N  
ATOM   1073  CA  ASN A 142      28.432  53.972  52.554  1.00 16.69           C  
ATOM   1074  C   ASN A 142      28.365  52.898  51.470  1.00 16.56           C  
ATOM   1075  O   ASN A 142      28.449  51.685  51.772  1.00 15.82           O  
ATOM   1076  CB  ASN A 142      29.778  54.680  52.512  1.00 15.79           C  
ATOM   1077  CG  ASN A 142      30.995  53.777  52.526  1.00 17.53           C  
ATOM   1078  OD1 ASN A 142      31.326  53.075  51.566  1.00 17.61           O  
ATOM   1079  ND2 ASN A 142      31.699  53.683  53.616  1.00 20.23           N  
ATOM   1080  N   GLN A 143      28.192  53.315  50.209  1.00 15.12           N  
ATOM   1081  CA  GLN A 143      28.013  52.375  49.097  1.00 15.82           C  
ATOM   1082  C   GLN A 143      29.252  51.591  48.674  1.00 17.28           C  
ATOM   1083  O   GLN A 143      29.155  50.451  48.181  1.00 16.72           O  
ATOM   1084  CB  GLN A 143      27.468  53.151  47.912  1.00 14.81           C  
ATOM   1085  CG  GLN A 143      27.029  52.353  46.692  1.00 13.78           C  
ATOM   1086  CD  GLN A 143      25.832  51.437  46.895  1.00 16.22           C  
ATOM   1087  OE1 GLN A 143      25.746  50.354  46.291  1.00 19.42           O  
ATOM   1088  NE2 GLN A 143      24.853  51.835  47.681  1.00 10.31           N  
ATOM   1089  N   ASP A 144      30.440  52.143  48.900  1.00 16.99           N  
ATOM   1090  CA  ASP A 144      31.635  51.403  48.548  1.00 20.29           C  
ATOM   1091  C   ASP A 144      31.779  50.153  49.389  1.00 19.66           C  
ATOM   1092  O   ASP A 144      32.178  49.111  48.850  1.00 20.86           O  
ATOM   1093  CB  ASP A 144      32.862  52.256  48.733  1.00 23.50           C  
ATOM   1094  CG  ASP A 144      32.993  53.374  47.700  1.00 27.97           C  
ATOM   1095  OD1 ASP A 144      32.362  53.320  46.626  1.00 27.11           O  
ATOM   1096  OD2 ASP A 144      33.740  54.319  48.008  1.00 32.39           O  
ATOM   1097  N   LEU A 145      31.414  50.226  50.678  1.00 19.53           N  
ATOM   1098  CA  LEU A 145      31.400  49.045  51.556  1.00 21.54           C  
ATOM   1099  C   LEU A 145      30.452  47.987  50.999  1.00 20.60           C  
ATOM   1100  O   LEU A 145      30.801  46.802  51.056  1.00 20.94           O  
ATOM   1101  CB  LEU A 145      30.911  49.337  52.980  1.00 21.61           C  
ATOM   1102  CG  LEU A 145      31.816  50.123  53.909  1.00 25.60           C  
ATOM   1103  CD1 LEU A 145      31.020  50.588  55.177  1.00 24.65           C  
ATOM   1104  CD2 LEU A 145      33.026  49.253  54.219  1.00 23.98           C  
ATOM   1105  N   ILE A 146      29.314  48.388  50.407  1.00 18.34           N  
ATOM   1106  CA  ILE A 146      28.381  47.426  49.829  1.00 18.85           C  
ATOM   1107  C   ILE A 146      29.023  46.674  48.657  1.00 18.80           C  
ATOM   1108  O   ILE A 146      28.974  45.436  48.577  1.00 18.19           O  
ATOM   1109  CB  ILE A 146      27.107  48.136  49.341  1.00 17.16           C  
ATOM   1110  CG1 ILE A 146      26.421  48.773  50.531  1.00 14.82           C  
ATOM   1111  CG2 ILE A 146      26.222  47.159  48.586  1.00 16.06           C  
ATOM   1112  CD1 ILE A 146      25.040  49.362  50.263  1.00 12.17           C  
ATOM   1113  N   TYR A 147      29.629  47.403  47.724  1.00 17.00           N  
ATOM   1114  CA  TYR A 147      30.289  46.758  46.594  1.00 19.09           C  
ATOM   1115  C   TYR A 147      31.429  45.837  47.059  1.00 19.72           C  
ATOM   1116  O   TYR A 147      31.583  44.723  46.552  1.00 21.91           O  
ATOM   1117  CB  TYR A 147      30.852  47.828  45.648  1.00 17.78           C  
ATOM   1118  CG  TYR A 147      29.827  48.712  44.952  1.00 16.03           C  
ATOM   1119  CD1 TYR A 147      28.644  48.206  44.452  1.00 16.38           C  
ATOM   1120  CD2 TYR A 147      30.144  50.047  44.801  1.00 17.92           C  
ATOM   1121  CE1 TYR A 147      27.762  49.028  43.778  1.00 15.09           C  
ATOM   1122  CE2 TYR A 147      29.279  50.870  44.122  1.00 15.59           C  
ATOM   1123  CZ  TYR A 147      28.105  50.354  43.625  1.00 15.34           C  
ATOM   1124  OH  TYR A 147      27.262  51.209  42.961  1.00 17.03           O  
ATOM   1125  N   SER A 148      32.203  46.225  48.059  1.00 19.82           N  
ATOM   1126  CA  SER A 148      33.267  45.375  48.545  1.00 23.42           C  
ATOM   1127  C   SER A 148      32.729  44.080  49.125  1.00 23.14           C  
ATOM   1128  O   SER A 148      33.269  43.008  48.844  1.00 23.60           O  
ATOM   1129  CB  SER A 148      34.070  46.057  49.628  1.00 25.53           C  
ATOM   1130  OG  SER A 148      34.473  47.341  49.151  1.00 36.18           O  
ATOM   1131  N   ASP A 149      31.656  44.121  49.896  1.00 22.29           N  
ATOM   1132  CA  ASP A 149      31.142  42.910  50.456  1.00 22.37           C  
ATOM   1133  C   ASP A 149      30.459  42.034  49.443  1.00 23.99           C  
ATOM   1134  O   ASP A 149      30.506  40.804  49.597  1.00 24.17           O  
ATOM   1135  CB  ASP A 149      30.213  43.266  51.574  1.00 23.71           C  
ATOM   1136  CG  ASP A 149      30.951  43.395  52.904  1.00 25.93           C  
ATOM   1137  OD1 ASP A 149      32.195  43.381  52.948  1.00 24.74           O  
ATOM   1138  OD2 ASP A 149      30.244  43.480  53.910  1.00 26.28           O  
ATOM   1139  N   LEU A 150      29.879  42.624  48.397  1.00 23.46           N  
ATOM   1140  CA  LEU A 150      29.266  41.847  47.335  1.00 24.51           C  
ATOM   1141  C   LEU A 150      30.373  41.088  46.636  1.00 25.74           C  
ATOM   1142  O   LEU A 150      30.277  39.870  46.574  1.00 26.41           O  
ATOM   1143  CB  LEU A 150      28.531  42.768  46.339  1.00 25.41           C  
ATOM   1144  CG  LEU A 150      27.714  42.107  45.220  1.00 26.97           C  
ATOM   1145  CD1 LEU A 150      26.389  41.548  45.762  1.00 27.10           C  
ATOM   1146  CD2 LEU A 150      27.443  43.139  44.145  1.00 27.43           C  
ATOM   1147  N   THR A 151      31.476  41.709  46.228  1.00 24.72           N  
ATOM   1148  CA  THR A 151      32.523  40.983  45.540  1.00 28.20           C  
ATOM   1149  C   THR A 151      33.226  39.991  46.474  1.00 29.98           C  
ATOM   1150  O   THR A 151      33.789  38.986  46.034  1.00 33.26           O  
ATOM   1151  CB  THR A 151      33.489  42.025  44.950  1.00 28.91           C  
ATOM   1152  OG1 THR A 151      33.936  42.849  46.026  1.00 33.68           O  
ATOM   1153  CG2 THR A 151      32.831  42.865  43.863  1.00 27.94           C  
ATOM   1154  N   ALA A 152      33.235  40.245  47.783  1.00 30.31           N  
ATOM   1155  CA  ALA A 152      33.755  39.301  48.760  1.00 30.80           C  
ATOM   1156  C   ALA A 152      32.803  38.128  48.950  1.00 29.74           C  
ATOM   1157  O   ALA A 152      33.148  37.173  49.644  1.00 32.44           O  
ATOM   1158  CB  ALA A 152      33.940  39.946  50.137  1.00 29.33           C  
ATOM   1159  N   GLY A 153      31.597  38.123  48.417  1.00 27.40           N  
ATOM   1160  CA  GLY A 153      30.705  37.021  48.624  1.00 27.69           C  
ATOM   1161  C   GLY A 153      30.018  37.124  49.966  1.00 28.43           C  
ATOM   1162  O   GLY A 153      29.395  36.141  50.343  1.00 29.72           O  
ATOM   1163  N   ARG A 154      30.065  38.233  50.728  1.00 26.53           N  
ATOM   1164  CA  ARG A 154      29.287  38.334  51.953  1.00 25.64           C  
ATOM   1165  C   ARG A 154      27.858  38.777  51.661  1.00 25.32           C  
ATOM   1166  O   ARG A 154      26.960  38.610  52.500  1.00 28.40           O  
ATOM   1167  CB  ARG A 154      29.897  39.321  52.898  1.00 28.31           C  
ATOM   1168  CG  ARG A 154      31.315  38.946  53.226  1.00 35.00           C  
ATOM   1169  CD  ARG A 154      31.893  39.919  54.221  1.00 39.39           C  
ATOM   1170  NE  ARG A 154      33.298  39.599  54.362  1.00 46.95           N  
ATOM   1171  CZ  ARG A 154      34.240  40.526  54.568  1.00 50.14           C  
ATOM   1172  NH1 ARG A 154      33.941  41.827  54.666  1.00 51.66           N  
ATOM   1173  NH2 ARG A 154      35.514  40.128  54.667  1.00 50.19           N  
ATOM   1174  N   LEU A 155      27.584  39.383  50.494  1.00 21.56           N  
ATOM   1175  CA  LEU A 155      26.221  39.760  50.144  1.00 20.05           C  
ATOM   1176  C   LEU A 155      25.885  38.992  48.877  1.00 19.18           C  
ATOM   1177  O   LEU A 155      26.793  38.673  48.112  1.00 20.42           O  
ATOM   1178  CB  LEU A 155      26.074  41.265  49.836  1.00 19.67           C  
ATOM   1179  CG  LEU A 155      26.313  42.287  50.953  1.00 18.66           C  
ATOM   1180  CD1 LEU A 155      26.334  43.693  50.349  1.00 16.63           C  
ATOM   1181  CD2 LEU A 155      25.243  42.157  52.011  1.00 17.17           C  
ATOM   1182  N   ASP A 156      24.603  38.654  48.712  1.00 18.49           N  
ATOM   1183  CA  ASP A 156      24.083  38.007  47.520  1.00 18.80           C  
ATOM   1184  C   ASP A 156      23.567  39.064  46.556  1.00 18.87           C  
ATOM   1185  O   ASP A 156      23.577  38.838  45.338  1.00 19.19           O  
ATOM   1186  CB  ASP A 156      22.915  37.114  47.815  1.00 20.51           C  
ATOM   1187  CG  ASP A 156      23.310  36.024  48.781  1.00 24.98           C  
ATOM   1188  OD1 ASP A 156      24.138  35.185  48.430  1.00 27.70           O  
ATOM   1189  OD2 ASP A 156      22.804  36.043  49.893  1.00 22.80           O  
ATOM   1190  N   ALA A 157      23.115  40.215  47.060  1.00 15.84           N  
ATOM   1191  CA  ALA A 157      22.536  41.229  46.203  1.00 14.76           C  
ATOM   1192  C   ALA A 157      22.653  42.613  46.859  1.00 15.68           C  
ATOM   1193  O   ALA A 157      22.907  42.691  48.071  1.00 16.35           O  
ATOM   1194  CB  ALA A 157      21.070  40.901  45.971  1.00 14.33           C  
ATOM   1195  N   ALA A 158      22.515  43.706  46.098  1.00 14.90           N  
ATOM   1196  CA  ALA A 158      22.533  45.063  46.646  1.00 15.50           C  
ATOM   1197  C   ALA A 158      21.502  45.915  45.896  1.00 15.73           C  
ATOM   1198  O   ALA A 158      21.274  45.709  44.685  1.00 17.08           O  
ATOM   1199  CB  ALA A 158      23.916  45.640  46.465  1.00 13.40           C  
ATOM   1200  N   LEU A 159      20.790  46.814  46.585  1.00 14.11           N  
ATOM   1201  CA  LEU A 159      19.777  47.656  45.971  1.00 13.69           C  
ATOM   1202  C   LEU A 159      20.299  49.090  46.135  1.00 14.53           C  
ATOM   1203  O   LEU A 159      20.701  49.497  47.238  1.00 14.36           O  
ATOM   1204  CB  LEU A 159      18.440  47.506  46.699  1.00 13.94           C  
ATOM   1205  CG  LEU A 159      17.207  48.226  46.092  1.00 17.44           C  
ATOM   1206  CD1 LEU A 159      16.806  47.542  44.771  1.00 15.25           C  
ATOM   1207  CD2 LEU A 159      16.041  48.194  47.083  1.00 15.10           C  
ATOM   1208  N   GLN A 160      20.307  49.883  45.063  1.00 12.40           N  
ATOM   1209  CA  GLN A 160      20.830  51.250  45.076  1.00 10.85           C  
ATOM   1210  C   GLN A 160      20.286  51.905  43.805  1.00 13.21           C  
ATOM   1211  O   GLN A 160      19.534  51.233  43.057  1.00 13.68           O  
ATOM   1212  CB  GLN A 160      22.372  51.311  45.022  1.00  8.73           C  
ATOM   1213  CG  GLN A 160      23.060  50.621  43.804  1.00 14.16           C  
ATOM   1214  CD  GLN A 160      22.964  49.088  43.911  1.00 16.96           C  
ATOM   1215  OE1 GLN A 160      23.524  48.516  44.844  1.00 15.94           O  
ATOM   1216  NE2 GLN A 160      22.240  48.359  43.059  1.00 14.85           N  
ATOM   1217  N   ASP A 161      20.609  53.186  43.527  1.00 11.53           N  
ATOM   1218  CA  ASP A 161      20.179  53.811  42.282  1.00 11.31           C  
ATOM   1219  C   ASP A 161      20.855  53.106  41.095  1.00 12.04           C  
ATOM   1220  O   ASP A 161      22.062  52.818  41.068  1.00 11.40           O  
ATOM   1221  CB  ASP A 161      20.550  55.302  42.271  1.00 10.47           C  
ATOM   1222  CG  ASP A 161      19.799  56.195  43.264  1.00 11.98           C  
ATOM   1223  OD1 ASP A 161      18.784  55.799  43.855  1.00 12.05           O  
ATOM   1224  OD2 ASP A 161      20.246  57.326  43.423  1.00 12.18           O  
ATOM   1225  N   GLU A 162      20.023  52.833  40.090  1.00 14.48           N  
ATOM   1226  CA  GLU A 162      20.423  52.147  38.856  1.00 15.08           C  
ATOM   1227  C   GLU A 162      21.681  52.703  38.171  1.00 14.56           C  
ATOM   1228  O   GLU A 162      22.680  51.995  37.968  1.00 13.47           O  
ATOM   1229  CB  GLU A 162      19.228  52.209  37.942  1.00 15.85           C  
ATOM   1230  CG  GLU A 162      19.394  51.353  36.698  1.00 21.89           C  
ATOM   1231  CD  GLU A 162      18.139  51.224  35.830  1.00 24.31           C  
ATOM   1232  OE1 GLU A 162      17.078  51.734  36.176  1.00 29.90           O  
ATOM   1233  OE2 GLU A 162      18.219  50.589  34.786  1.00 23.08           O  
ATOM   1234  N   VAL A 163      21.692  54.005  37.847  1.00 14.14           N  
ATOM   1235  CA  VAL A 163      22.849  54.633  37.202  1.00 14.82           C  
ATOM   1236  C   VAL A 163      24.093  54.580  38.072  1.00 14.31           C  
ATOM   1237  O   VAL A 163      25.173  54.397  37.512  1.00 14.70           O  
ATOM   1238  CB  VAL A 163      22.537  56.143  36.795  1.00 13.75           C  
ATOM   1239  CG1 VAL A 163      23.724  56.734  36.067  1.00 13.53           C  
ATOM   1240  CG2 VAL A 163      21.329  56.214  35.855  1.00 13.85           C  
ATOM   1241  N   ALA A 164      23.992  54.700  39.406  1.00 13.81           N  
ATOM   1242  CA  ALA A 164      25.195  54.612  40.244  1.00 14.98           C  
ATOM   1243  C   ALA A 164      25.780  53.192  40.118  1.00 14.87           C  
ATOM   1244  O   ALA A 164      26.969  53.025  39.822  1.00 15.21           O  
ATOM   1245  CB  ALA A 164      24.860  54.879  41.721  1.00 12.07           C  
ATOM   1246  N   ALA A 165      24.934  52.150  40.242  1.00 14.71           N  
ATOM   1247  CA  ALA A 165      25.396  50.758  40.102  1.00 15.88           C  
ATOM   1248  C   ALA A 165      26.003  50.506  38.705  1.00 16.74           C  
ATOM   1249  O   ALA A 165      27.097  49.918  38.596  1.00 16.95           O  
ATOM   1250  CB  ALA A 165      24.227  49.765  40.309  1.00 12.94           C  
ATOM   1251  N   SER A 166      25.336  51.010  37.655  1.00 15.95           N  
ATOM   1252  CA  SER A 166      25.784  50.812  36.281  1.00 17.27           C  
ATOM   1253  C   SER A 166      27.144  51.463  36.004  1.00 19.48           C  
ATOM   1254  O   SER A 166      28.156  50.767  35.792  1.00 19.50           O  
ATOM   1255  CB  SER A 166      24.739  51.375  35.332  1.00 19.03           C  
ATOM   1256  OG  SER A 166      25.142  51.015  34.035  1.00 23.36           O  
ATOM   1257  N   GLU A 167      27.197  52.796  36.139  1.00 18.91           N  
ATOM   1258  CA  GLU A 167      28.404  53.529  35.852  1.00 19.74           C  
ATOM   1259  C   GLU A 167      29.476  53.395  36.908  1.00 20.84           C  
ATOM   1260  O   GLU A 167      30.678  53.308  36.609  1.00 20.87           O  
ATOM   1261  CB  GLU A 167      28.038  55.007  35.641  1.00 19.20           C  
ATOM   1262  CG  GLU A 167      27.066  55.237  34.462  1.00 21.93           C  
ATOM   1263  CD  GLU A 167      27.604  54.853  33.072  1.00 25.53           C  
ATOM   1264  OE1 GLU A 167      28.828  54.760  32.902  1.00 24.17           O  
ATOM   1265  OE2 GLU A 167      26.790  54.670  32.157  1.00 27.89           O  
ATOM   1266  N   GLY A 168      29.066  53.353  38.172  1.00 19.49           N  
ATOM   1267  CA  GLY A 168      30.013  53.311  39.243  1.00 19.03           C  
ATOM   1268  C   GLY A 168      30.470  51.900  39.495  1.00 20.33           C  
ATOM   1269  O   GLY A 168      31.482  51.787  40.184  1.00 22.17           O  
ATOM   1270  N   PHE A 169      29.864  50.805  39.000  1.00 19.07           N  
ATOM   1271  CA  PHE A 169      30.350  49.482  39.379  1.00 18.99           C  
ATOM   1272  C   PHE A 169      30.319  48.492  38.225  1.00 19.83           C  
ATOM   1273  O   PHE A 169      31.372  47.956  37.858  1.00 19.36           O  
ATOM   1274  CB  PHE A 169      29.506  48.933  40.558  1.00 19.07           C  
ATOM   1275  CG  PHE A 169      29.849  47.537  41.093  1.00 20.32           C  
ATOM   1276  CD1 PHE A 169      31.074  47.283  41.713  1.00 23.35           C  
ATOM   1277  CD2 PHE A 169      28.939  46.493  40.931  1.00 21.20           C  
ATOM   1278  CE1 PHE A 169      31.391  45.999  42.161  1.00 21.23           C  
ATOM   1279  CE2 PHE A 169      29.265  45.222  41.379  1.00 21.70           C  
ATOM   1280  CZ  PHE A 169      30.488  44.976  41.992  1.00 22.26           C  
ATOM   1281  N   LEU A 170      29.147  48.253  37.636  1.00 20.03           N  
ATOM   1282  CA  LEU A 170      28.984  47.238  36.621  1.00 21.18           C  
ATOM   1283  C   LEU A 170      29.903  47.485  35.441  1.00 23.61           C  
ATOM   1284  O   LEU A 170      30.540  46.531  34.987  1.00 24.04           O  
ATOM   1285  CB  LEU A 170      27.527  47.179  36.138  1.00 19.68           C  
ATOM   1286  CG  LEU A 170      26.517  46.698  37.147  1.00 18.56           C  
ATOM   1287  CD1 LEU A 170      25.147  46.481  36.520  1.00 15.59           C  
ATOM   1288  CD2 LEU A 170      27.049  45.384  37.720  1.00 21.12           C  
ATOM   1289  N   LYS A 171      30.047  48.737  35.006  1.00 22.20           N  
ATOM   1290  CA  LYS A 171      30.941  49.071  33.904  1.00 25.73           C  
ATOM   1291  C   LYS A 171      32.386  49.267  34.341  1.00 26.81           C  
ATOM   1292  O   LYS A 171      33.228  49.751  33.577  1.00 30.69           O  
ATOM   1293  CB  LYS A 171      30.421  50.336  33.201  1.00 24.58           C  
ATOM   1294  CG  LYS A 171      29.183  49.910  32.475  1.00 24.86           C  
ATOM   1295  CD  LYS A 171      28.249  51.021  32.071  1.00 30.93           C  
ATOM   1296  CE  LYS A 171      28.841  51.850  30.970  1.00 34.83           C  
ATOM   1297  NZ  LYS A 171      27.768  52.562  30.305  1.00 37.91           N  
ATOM   1298  N   GLN A 172      32.724  48.904  35.574  1.00 28.23           N  
ATOM   1299  CA  GLN A 172      34.076  49.066  36.074  1.00 29.46           C  
ATOM   1300  C   GLN A 172      34.702  47.682  36.167  1.00 30.44           C  
ATOM   1301  O   GLN A 172      33.962  46.693  36.286  1.00 30.39           O  
ATOM   1302  CB  GLN A 172      34.069  49.709  37.458  1.00 30.05           C  
ATOM   1303  CG  GLN A 172      33.449  51.099  37.474  1.00 32.57           C  
ATOM   1304  CD  GLN A 172      34.127  52.065  36.515  1.00 38.17           C  
ATOM   1305  OE1 GLN A 172      35.359  52.088  36.423  1.00 40.77           O  
ATOM   1306  NE2 GLN A 172      33.404  52.886  35.752  1.00 38.90           N  
ATOM   1307  N   PRO A 173      36.041  47.553  36.146  1.00 32.74           N  
ATOM   1308  CA  PRO A 173      36.798  46.328  36.428  1.00 33.07           C  
ATOM   1309  C   PRO A 173      36.180  45.405  37.467  1.00 33.42           C  
ATOM   1310  O   PRO A 173      35.834  44.246  37.194  1.00 33.64           O  
ATOM   1311  CB  PRO A 173      38.156  46.852  36.832  1.00 34.18           C  
ATOM   1312  CG  PRO A 173      38.346  47.982  35.846  1.00 34.12           C  
ATOM   1313  CD  PRO A 173      36.968  48.626  35.778  1.00 33.57           C  
ATOM   1314  N   ALA A 174      35.956  46.007  38.646  1.00 33.37           N  
ATOM   1315  CA  ALA A 174      35.352  45.304  39.767  1.00 32.17           C  
ATOM   1316  C   ALA A 174      33.974  44.701  39.513  1.00 31.76           C  
ATOM   1317  O   ALA A 174      33.690  43.673  40.138  1.00 33.51           O  
ATOM   1318  CB  ALA A 174      35.224  46.233  40.952  1.00 31.89           C  
ATOM   1319  N   GLY A 175      33.129  45.210  38.607  1.00 28.86           N  
ATOM   1320  CA  GLY A 175      31.795  44.667  38.448  1.00 27.66           C  
ATOM   1321  C   GLY A 175      31.596  43.768  37.237  1.00 26.90           C  
ATOM   1322  O   GLY A 175      30.459  43.391  36.911  1.00 25.04           O  
ATOM   1323  N   LYS A 176      32.689  43.379  36.593  1.00 27.86           N  
ATOM   1324  CA  LYS A 176      32.641  42.566  35.380  1.00 29.25           C  
ATOM   1325  C   LYS A 176      31.841  41.273  35.511  1.00 29.30           C  
ATOM   1326  O   LYS A 176      31.130  40.865  34.597  1.00 29.81           O  
ATOM   1327  CB  LYS A 176      34.074  42.214  34.948  1.00 29.61           C  
ATOM   1328  N   GLU A 177      31.889  40.641  36.685  1.00 30.78           N  
ATOM   1329  CA  GLU A 177      31.156  39.405  36.935  1.00 31.84           C  
ATOM   1330  C   GLU A 177      29.787  39.611  37.598  1.00 30.91           C  
ATOM   1331  O   GLU A 177      29.226  38.672  38.187  1.00 29.43           O  
ATOM   1332  CB  GLU A 177      32.022  38.497  37.821  1.00 33.49           C  
ATOM   1333  N   TYR A 178      29.229  40.830  37.525  1.00 28.32           N  
ATOM   1334  CA  TYR A 178      27.967  41.126  38.173  1.00 25.23           C  
ATOM   1335  C   TYR A 178      27.083  41.718  37.137  1.00 22.85           C  
ATOM   1336  O   TYR A 178      27.580  42.135  36.097  1.00 24.09           O  
ATOM   1337  CB  TYR A 178      28.151  42.119  39.320  1.00 25.32           C  
ATOM   1338  CG  TYR A 178      28.985  41.462  40.402  1.00 27.25           C  
ATOM   1339  CD1 TYR A 178      28.376  40.647  41.326  1.00 27.95           C  
ATOM   1340  CD2 TYR A 178      30.358  41.623  40.394  1.00 27.92           C  
ATOM   1341  CE1 TYR A 178      29.148  39.961  42.235  1.00 28.46           C  
ATOM   1342  CE2 TYR A 178      31.132  40.948  41.298  1.00 30.28           C  
ATOM   1343  CZ  TYR A 178      30.515  40.115  42.202  1.00 30.23           C  
ATOM   1344  OH  TYR A 178      31.304  39.396  43.071  1.00 35.82           O  
ATOM   1345  N   ALA A 179      25.795  41.727  37.415  1.00 20.18           N  
ATOM   1346  CA  ALA A 179      24.812  42.263  36.510  1.00 18.12           C  
ATOM   1347  C   ALA A 179      23.586  42.696  37.279  1.00 17.93           C  
ATOM   1348  O   ALA A 179      23.438  42.406  38.462  1.00 20.24           O  
ATOM   1349  CB  ALA A 179      24.368  41.216  35.519  1.00 18.57           C  
ATOM   1350  N   PHE A 180      22.706  43.453  36.652  1.00 18.23           N  
ATOM   1351  CA  PHE A 180      21.406  43.768  37.199  1.00 17.42           C  
ATOM   1352  C   PHE A 180      20.586  42.506  37.322  1.00 18.63           C  
ATOM   1353  O   PHE A 180      20.618  41.606  36.475  1.00 19.37           O  
ATOM   1354  CB  PHE A 180      20.669  44.741  36.305  1.00 15.60           C  
ATOM   1355  CG  PHE A 180      21.206  46.161  36.408  1.00 18.70           C  
ATOM   1356  CD1 PHE A 180      21.254  46.808  37.645  1.00 17.11           C  
ATOM   1357  CD2 PHE A 180      21.595  46.849  35.270  1.00 19.39           C  
ATOM   1358  CE1 PHE A 180      21.686  48.122  37.725  1.00 18.11           C  
ATOM   1359  CE2 PHE A 180      22.026  48.168  35.365  1.00 20.24           C  
ATOM   1360  CZ  PHE A 180      22.072  48.802  36.589  1.00 18.24           C  
ATOM   1361  N   ALA A 181      19.848  42.391  38.407  1.00 18.55           N  
ATOM   1362  CA  ALA A 181      19.027  41.237  38.635  1.00 18.62           C  
ATOM   1363  C   ALA A 181      17.597  41.713  38.540  1.00 19.63           C  
ATOM   1364  O   ALA A 181      17.034  42.281  39.481  1.00 20.07           O  
ATOM   1365  CB  ALA A 181      19.344  40.672  40.013  1.00 19.88           C  
ATOM   1366  N   GLY A 182      16.971  41.481  37.380  1.00 16.82           N  
ATOM   1367  CA  GLY A 182      15.594  41.905  37.145  1.00 16.34           C  
ATOM   1368  C   GLY A 182      15.531  43.368  36.694  1.00 16.51           C  
ATOM   1369  O   GLY A 182      16.569  44.023  36.597  1.00 16.16           O  
ATOM   1370  N   PRO A 183      14.365  43.901  36.360  1.00 17.59           N  
ATOM   1371  CA  PRO A 183      14.169  45.288  35.936  1.00 19.21           C  
ATOM   1372  C   PRO A 183      14.179  46.275  37.121  1.00 18.05           C  
ATOM   1373  O   PRO A 183      14.200  45.822  38.274  1.00 17.25           O  
ATOM   1374  CB  PRO A 183      12.849  45.224  35.194  1.00 18.25           C  
ATOM   1375  CG  PRO A 183      12.058  44.274  36.072  1.00 18.92           C  
ATOM   1376  CD  PRO A 183      13.088  43.191  36.435  1.00 19.69           C  
ATOM   1377  N   SER A 184      14.149  47.590  36.883  1.00 19.38           N  
ATOM   1378  CA  SER A 184      14.063  48.598  37.930  1.00 21.43           C  
ATOM   1379  C   SER A 184      12.890  48.301  38.842  1.00 23.39           C  
ATOM   1380  O   SER A 184      11.845  47.838  38.355  1.00 25.12           O  
ATOM   1381  CB  SER A 184      13.811  49.967  37.361  1.00 21.05           C  
ATOM   1382  OG  SER A 184      14.721  50.155  36.308  1.00 28.81           O  
ATOM   1383  N   VAL A 185      13.052  48.555  40.140  1.00 24.11           N  
ATOM   1384  CA  VAL A 185      11.978  48.390  41.112  1.00 26.29           C  
ATOM   1385  C   VAL A 185      11.216  49.699  41.115  1.00 27.47           C  
ATOM   1386  O   VAL A 185      11.757  50.745  41.452  1.00 30.03           O  
ATOM   1387  CB  VAL A 185      12.536  48.123  42.525  1.00 25.39           C  
ATOM   1388  CG1 VAL A 185      11.385  47.916  43.494  1.00 25.20           C  
ATOM   1389  CG2 VAL A 185      13.455  46.910  42.484  1.00 27.95           C  
ATOM   1390  N   LYS A 186       9.991  49.722  40.675  1.00 30.59           N  
ATOM   1391  CA  LYS A 186       9.220  50.927  40.724  1.00 33.08           C  
ATOM   1392  C   LYS A 186       8.288  50.859  41.920  1.00 33.37           C  
ATOM   1393  O   LYS A 186       7.568  49.872  42.129  1.00 33.46           O  
ATOM   1394  CB  LYS A 186       8.415  51.077  39.446  1.00 36.88           C  
ATOM   1395  CG  LYS A 186       9.224  51.250  38.173  1.00 41.98           C  
ATOM   1396  CD  LYS A 186      10.166  52.454  38.224  1.00 47.15           C  
ATOM   1397  CE  LYS A 186      10.409  53.073  36.841  1.00 50.00           C  
ATOM   1398  NZ  LYS A 186      11.010  52.163  35.876  1.00 53.11           N  
ATOM   1399  N   ASP A 187       8.341  51.891  42.737  1.00 31.42           N  
ATOM   1400  CA  ASP A 187       7.404  52.070  43.811  1.00 31.81           C  
ATOM   1401  C   ASP A 187       7.380  53.560  44.069  1.00 32.75           C  
ATOM   1402  O   ASP A 187       8.287  54.094  44.723  1.00 31.79           O  
ATOM   1403  CB  ASP A 187       7.842  51.368  45.088  1.00 34.45           C  
ATOM   1404  CG  ASP A 187       6.687  51.316  46.062  1.00 37.37           C  
ATOM   1405  OD1 ASP A 187       6.144  52.357  46.437  1.00 39.15           O  
ATOM   1406  OD2 ASP A 187       6.323  50.208  46.436  1.00 40.11           O  
ATOM   1407  N   LYS A 188       6.310  54.245  43.666  1.00 33.78           N  
ATOM   1408  CA  LYS A 188       6.215  55.705  43.800  1.00 35.22           C  
ATOM   1409  C   LYS A 188       6.351  56.227  45.233  1.00 33.94           C  
ATOM   1410  O   LYS A 188       7.078  57.203  45.477  1.00 35.67           O  
ATOM   1411  CB  LYS A 188       4.868  56.210  43.240  1.00 36.11           C  
ATOM   1412  N   LYS A 189       5.723  55.508  46.166  1.00 30.42           N  
ATOM   1413  CA  LYS A 189       5.783  55.848  47.573  1.00 30.70           C  
ATOM   1414  C   LYS A 189       7.189  55.900  48.169  1.00 29.63           C  
ATOM   1415  O   LYS A 189       7.511  56.730  49.028  1.00 32.38           O  
ATOM   1416  CB  LYS A 189       5.004  54.840  48.422  1.00 30.74           C  
ATOM   1417  N   TYR A 190       8.039  54.972  47.765  1.00 24.34           N  
ATOM   1418  CA  TYR A 190       9.349  54.935  48.382  1.00 22.04           C  
ATOM   1419  C   TYR A 190      10.423  55.714  47.656  1.00 19.40           C  
ATOM   1420  O   TYR A 190      11.263  56.344  48.302  1.00 18.04           O  
ATOM   1421  CB  TYR A 190       9.831  53.506  48.511  1.00 20.93           C  
ATOM   1422  CG  TYR A 190       9.117  52.793  49.630  1.00 21.83           C  
ATOM   1423  CD1 TYR A 190       9.597  52.928  50.919  1.00 23.85           C  
ATOM   1424  CD2 TYR A 190       8.014  52.024  49.345  1.00 22.97           C  
ATOM   1425  CE1 TYR A 190       8.979  52.258  51.943  1.00 23.42           C  
ATOM   1426  CE2 TYR A 190       7.397  51.351  50.368  1.00 24.11           C  
ATOM   1427  CZ  TYR A 190       7.887  51.477  51.645  1.00 25.40           C  
ATOM   1428  OH  TYR A 190       7.230  50.811  52.649  1.00 28.69           O  
ATOM   1429  N   PHE A 191      10.391  55.692  46.324  1.00 16.82           N  
ATOM   1430  CA  PHE A 191      11.560  56.156  45.643  1.00 16.61           C  
ATOM   1431  C   PHE A 191      11.444  57.578  45.181  1.00 16.12           C  
ATOM   1432  O   PHE A 191      12.458  58.147  44.759  1.00 18.12           O  
ATOM   1433  CB  PHE A 191      11.853  55.180  44.485  1.00 16.63           C  
ATOM   1434  CG  PHE A 191      12.184  53.779  45.030  1.00 19.23           C  
ATOM   1435  CD1 PHE A 191      13.245  53.581  45.911  1.00 16.92           C  
ATOM   1436  CD2 PHE A 191      11.412  52.686  44.646  1.00 21.78           C  
ATOM   1437  CE1 PHE A 191      13.505  52.305  46.398  1.00 19.39           C  
ATOM   1438  CE2 PHE A 191      11.682  51.415  45.140  1.00 20.49           C  
ATOM   1439  CZ  PHE A 191      12.731  51.229  46.013  1.00 17.48           C  
ATOM   1440  N   GLY A 192      10.264  58.173  45.255  1.00 16.61           N  
ATOM   1441  CA  GLY A 192      10.106  59.585  44.918  1.00 19.20           C  
ATOM   1442  C   GLY A 192      10.229  59.937  43.437  1.00 21.15           C  
ATOM   1443  O   GLY A 192      10.094  59.049  42.579  1.00 22.09           O  
ATOM   1444  N   ASP A 193      10.520  61.208  43.117  1.00 21.12           N  
ATOM   1445  CA  ASP A 193      10.536  61.644  41.750  1.00 22.43           C  
ATOM   1446  C   ASP A 193      11.793  62.373  41.340  1.00 21.66           C  
ATOM   1447  O   ASP A 193      11.783  63.597  41.266  1.00 23.96           O  
ATOM   1448  CB  ASP A 193       9.329  62.543  41.516  1.00 27.65           C  
ATOM   1449  CG  ASP A 193       8.904  62.712  40.053  1.00 33.07           C  
ATOM   1450  OD1 ASP A 193       9.442  62.057  39.148  1.00 32.86           O  
ATOM   1451  OD2 ASP A 193       7.999  63.519  39.832  1.00 37.10           O  
ATOM   1452  N   GLY A 194      12.883  61.686  41.035  1.00 18.70           N  
ATOM   1453  CA  GLY A 194      14.104  62.370  40.663  1.00 14.44           C  
ATOM   1454  C   GLY A 194      14.769  62.897  41.916  1.00 12.79           C  
ATOM   1455  O   GLY A 194      14.264  62.707  43.034  1.00 14.84           O  
ATOM   1456  N   THR A 195      15.927  63.507  41.745  1.00 12.05           N  
ATOM   1457  CA  THR A 195      16.758  64.009  42.836  1.00 12.72           C  
ATOM   1458  C   THR A 195      16.763  65.538  42.822  1.00 13.17           C  
ATOM   1459  O   THR A 195      16.499  66.123  41.750  1.00 14.30           O  
ATOM   1460  CB  THR A 195      18.227  63.507  42.719  1.00 11.09           C  
ATOM   1461  OG1 THR A 195      18.877  64.097  41.588  1.00 11.70           O  
ATOM   1462  CG2 THR A 195      18.227  61.967  42.638  1.00  9.71           C  
ATOM   1463  N   GLY A 196      17.030  66.222  43.932  1.00 12.05           N  
ATOM   1464  CA  GLY A 196      17.052  67.677  43.913  1.00 13.22           C  
ATOM   1465  C   GLY A 196      17.981  68.145  45.021  1.00 13.89           C  
ATOM   1466  O   GLY A 196      18.536  67.330  45.778  1.00 12.86           O  
ATOM   1467  N   VAL A 197      18.281  69.447  45.042  1.00 13.21           N  
ATOM   1468  CA  VAL A 197      19.037  70.070  46.124  1.00 12.03           C  
ATOM   1469  C   VAL A 197      18.130  70.087  47.363  1.00 13.39           C  
ATOM   1470  O   VAL A 197      16.997  70.594  47.279  1.00 13.83           O  
ATOM   1471  CB  VAL A 197      19.457  71.556  45.797  1.00 11.87           C  
ATOM   1472  CG1 VAL A 197      20.420  72.014  46.887  1.00 11.57           C  
ATOM   1473  CG2 VAL A 197      20.098  71.696  44.429  1.00  9.82           C  
ATOM   1474  N   GLY A 198      18.585  69.505  48.485  1.00 12.85           N  
ATOM   1475  CA  GLY A 198      17.822  69.559  49.734  1.00 11.95           C  
ATOM   1476  C   GLY A 198      18.167  70.851  50.485  1.00 12.04           C  
ATOM   1477  O   GLY A 198      19.342  71.201  50.615  1.00 11.27           O  
ATOM   1478  N   LEU A 199      17.166  71.565  50.981  1.00 11.89           N  
ATOM   1479  CA  LEU A 199      17.340  72.869  51.605  1.00 12.85           C  
ATOM   1480  C   LEU A 199      16.418  72.967  52.797  1.00 11.83           C  
ATOM   1481  O   LEU A 199      15.412  72.262  52.861  1.00 12.21           O  
ATOM   1482  CB  LEU A 199      16.964  73.987  50.616  1.00 14.59           C  
ATOM   1483  CG  LEU A 199      17.778  74.005  49.332  1.00 13.67           C  
ATOM   1484  CD1 LEU A 199      16.885  74.460  48.228  1.00 17.88           C  
ATOM   1485  CD2 LEU A 199      19.066  74.773  49.550  1.00 15.96           C  
ATOM   1486  N   ARG A 200      16.732  73.805  53.790  1.00 14.36           N  
ATOM   1487  CA  ARG A 200      15.836  74.056  54.910  1.00 13.83           C  
ATOM   1488  C   ARG A 200      14.561  74.724  54.384  1.00 15.98           C  
ATOM   1489  O   ARG A 200      14.620  75.582  53.484  1.00 15.55           O  
ATOM   1490  CB  ARG A 200      16.518  74.980  55.918  1.00 16.47           C  
ATOM   1491  CG  ARG A 200      17.598  74.309  56.806  1.00 13.92           C  
ATOM   1492  CD  ARG A 200      18.183  75.347  57.768  1.00 15.10           C  
ATOM   1493  NE  ARG A 200      19.022  76.301  57.056  1.00 15.34           N  
ATOM   1494  CZ  ARG A 200      20.307  76.059  56.772  1.00 17.42           C  
ATOM   1495  NH1 ARG A 200      20.954  74.923  57.101  1.00 16.66           N  
ATOM   1496  NH2 ARG A 200      20.974  77.011  56.139  1.00 17.24           N  
ATOM   1497  N   LYS A 201      13.386  74.337  54.884  1.00 15.96           N  
ATOM   1498  CA  LYS A 201      12.117  74.919  54.462  1.00 18.27           C  
ATOM   1499  C   LYS A 201      12.008  76.434  54.438  1.00 21.07           C  
ATOM   1500  O   LYS A 201      11.376  77.032  53.570  1.00 21.89           O  
ATOM   1501  CB  LYS A 201      11.029  74.425  55.335  1.00 20.23           C  
ATOM   1502  CG  LYS A 201      10.815  72.938  55.181  1.00 22.19           C  
ATOM   1503  CD  LYS A 201       9.651  72.584  56.081  1.00 26.13           C  
ATOM   1504  CE  LYS A 201       9.012  71.323  55.619  1.00 26.50           C  
ATOM   1505  NZ  LYS A 201       7.810  71.077  56.385  1.00 32.22           N  
ATOM   1506  N   ASP A 202      12.586  77.088  55.430  1.00 20.31           N  
ATOM   1507  CA  ASP A 202      12.556  78.537  55.472  1.00 21.86           C  
ATOM   1508  C   ASP A 202      13.559  79.241  54.547  1.00 22.72           C  
ATOM   1509  O   ASP A 202      13.497  80.471  54.467  1.00 20.37           O  
ATOM   1510  CB  ASP A 202      12.767  78.971  56.922  1.00 21.87           C  
ATOM   1511  CG  ASP A 202      14.065  78.456  57.549  1.00 23.35           C  
ATOM   1512  OD1 ASP A 202      14.165  77.253  57.795  1.00 23.33           O  
ATOM   1513  OD2 ASP A 202      14.954  79.264  57.812  1.00 25.54           O  
ATOM   1514  N   ASP A 203      14.471  78.543  53.825  1.00 21.32           N  
ATOM   1515  CA  ASP A 203      15.444  79.205  52.974  1.00 20.39           C  
ATOM   1516  C   ASP A 203      14.922  79.309  51.558  1.00 21.00           C  
ATOM   1517  O   ASP A 203      15.503  78.888  50.556  1.00 17.78           O  
ATOM   1518  CB  ASP A 203      16.781  78.458  52.969  1.00 21.11           C  
ATOM   1519  CG  ASP A 203      17.753  78.861  54.085  1.00 25.82           C  
ATOM   1520  OD1 ASP A 203      17.469  79.833  54.791  1.00 29.84           O  
ATOM   1521  OD2 ASP A 203      18.808  78.238  54.261  1.00 24.89           O  
ATOM   1522  N   THR A 204      13.802  80.007  51.474  1.00 21.55           N  
ATOM   1523  CA  THR A 204      13.110  80.117  50.199  1.00 24.55           C  
ATOM   1524  C   THR A 204      13.916  80.975  49.206  1.00 23.35           C  
ATOM   1525  O   THR A 204      13.919  80.724  48.005  1.00 22.02           O  
ATOM   1526  CB  THR A 204      11.689  80.668  50.521  1.00 23.85           C  
ATOM   1527  OG1 THR A 204      11.837  81.857  51.267  1.00 28.68           O  
ATOM   1528  CG2 THR A 204      10.901  79.735  51.390  1.00 24.04           C  
ATOM   1529  N   GLU A 205      14.714  81.922  49.707  1.00 23.39           N  
ATOM   1530  CA  GLU A 205      15.517  82.787  48.867  1.00 26.00           C  
ATOM   1531  C   GLU A 205      16.618  81.915  48.244  1.00 25.34           C  
ATOM   1532  O   GLU A 205      16.932  82.021  47.041  1.00 23.31           O  
ATOM   1533  CB  GLU A 205      16.146  83.888  49.699  1.00 30.49           C  
ATOM   1534  CG  GLU A 205      16.616  85.044  48.821  1.00 42.46           C  
ATOM   1535  CD  GLU A 205      17.468  86.131  49.487  1.00 48.31           C  
ATOM   1536  OE1 GLU A 205      17.263  86.455  50.661  1.00 51.45           O  
ATOM   1537  OE2 GLU A 205      18.358  86.680  48.828  1.00 50.47           O  
ATOM   1538  N   LEU A 206      17.211  80.993  49.035  1.00 23.35           N  
ATOM   1539  CA  LEU A 206      18.243  80.118  48.497  1.00 20.92           C  
ATOM   1540  C   LEU A 206      17.632  79.135  47.484  1.00 17.88           C  
ATOM   1541  O   LEU A 206      18.240  78.894  46.421  1.00 17.82           O  
ATOM   1542  CB  LEU A 206      18.942  79.396  49.669  1.00 20.06           C  
ATOM   1543  CG  LEU A 206      20.179  78.569  49.325  1.00 21.55           C  
ATOM   1544  CD1 LEU A 206      21.230  79.407  48.602  1.00 20.00           C  
ATOM   1545  CD2 LEU A 206      20.751  78.021  50.623  1.00 22.99           C  
ATOM   1546  N   LYS A 207      16.433  78.601  47.746  1.00 15.64           N  
ATOM   1547  CA  LYS A 207      15.794  77.712  46.780  1.00 16.28           C  
ATOM   1548  C   LYS A 207      15.528  78.435  45.452  1.00 19.16           C  
ATOM   1549  O   LYS A 207      15.784  77.872  44.379  1.00 19.39           O  
ATOM   1550  CB  LYS A 207      14.448  77.174  47.302  1.00 15.14           C  
ATOM   1551  CG  LYS A 207      13.613  76.420  46.284  1.00 15.42           C  
ATOM   1552  CD  LYS A 207      12.339  75.906  46.845  1.00 15.46           C  
ATOM   1553  CE  LYS A 207      11.322  75.601  45.725  1.00 20.06           C  
ATOM   1554  NZ  LYS A 207      11.812  74.654  44.717  1.00 16.61           N  
ATOM   1555  N   ALA A 208      15.004  79.664  45.493  1.00 17.85           N  
ATOM   1556  CA  ALA A 208      14.729  80.420  44.303  1.00 16.84           C  
ATOM   1557  C   ALA A 208      15.992  80.648  43.485  1.00 15.81           C  
ATOM   1558  O   ALA A 208      15.924  80.527  42.260  1.00 16.05           O  
ATOM   1559  CB  ALA A 208      14.134  81.739  44.706  1.00 18.34           C  
ATOM   1560  N   ALA A 209      17.140  80.930  44.105  1.00 16.00           N  
ATOM   1561  CA  ALA A 209      18.394  81.118  43.410  1.00 15.91           C  
ATOM   1562  C   ALA A 209      18.892  79.831  42.741  1.00 18.90           C  
ATOM   1563  O   ALA A 209      19.381  79.861  41.588  1.00 16.19           O  
ATOM   1564  CB  ALA A 209      19.438  81.598  44.397  1.00 16.71           C  
ATOM   1565  N   PHE A 210      18.812  78.675  43.455  1.00 16.26           N  
ATOM   1566  CA  PHE A 210      19.185  77.391  42.860  1.00 15.72           C  
ATOM   1567  C   PHE A 210      18.241  77.073  41.702  1.00 13.86           C  
ATOM   1568  O   PHE A 210      18.708  76.635  40.642  1.00 15.63           O  
ATOM   1569  CB  PHE A 210      19.093  76.190  43.861  1.00 14.06           C  
ATOM   1570  CG  PHE A 210      20.340  75.992  44.704  1.00 14.70           C  
ATOM   1571  CD1 PHE A 210      21.519  75.597  44.084  1.00 12.75           C  
ATOM   1572  CD2 PHE A 210      20.301  76.214  46.070  1.00 13.04           C  
ATOM   1573  CE1 PHE A 210      22.666  75.410  44.829  1.00 16.42           C  
ATOM   1574  CE2 PHE A 210      21.472  76.019  46.793  1.00 13.55           C  
ATOM   1575  CZ  PHE A 210      22.654  75.614  46.197  1.00 13.97           C  
ATOM   1576  N   ASP A 211      16.926  77.278  41.834  1.00 14.80           N  
ATOM   1577  CA  ASP A 211      15.987  76.982  40.737  1.00 15.78           C  
ATOM   1578  C   ASP A 211      16.197  77.815  39.486  1.00 15.86           C  
ATOM   1579  O   ASP A 211      16.146  77.305  38.372  1.00 16.21           O  
ATOM   1580  CB  ASP A 211      14.572  77.164  41.217  1.00 14.46           C  
ATOM   1581  CG  ASP A 211      14.123  76.031  42.141  1.00 18.29           C  
ATOM   1582  OD1 ASP A 211      14.775  74.997  42.178  1.00 19.33           O  
ATOM   1583  OD2 ASP A 211      13.116  76.176  42.817  1.00 19.93           O  
ATOM   1584  N   LYS A 212      16.498  79.099  39.657  1.00 15.80           N  
ATOM   1585  CA  LYS A 212      16.771  80.002  38.557  1.00 15.16           C  
ATOM   1586  C   LYS A 212      18.069  79.586  37.868  1.00 14.44           C  
ATOM   1587  O   LYS A 212      18.086  79.430  36.652  1.00 16.26           O  
ATOM   1588  CB  LYS A 212      16.879  81.410  39.114  1.00 17.94           C  
ATOM   1589  CG  LYS A 212      17.252  82.413  38.040  1.00 22.86           C  
ATOM   1590  CD  LYS A 212      17.288  83.809  38.603  1.00 28.27           C  
ATOM   1591  CE  LYS A 212      17.576  84.840  37.504  1.00 31.97           C  
ATOM   1592  NZ  LYS A 212      19.005  84.940  37.226  1.00 35.22           N  
ATOM   1593  N   ALA A 213      19.161  79.317  38.598  1.00 14.79           N  
ATOM   1594  CA  ALA A 213      20.413  78.904  37.989  1.00 14.21           C  
ATOM   1595  C   ALA A 213      20.227  77.566  37.260  1.00 16.10           C  
ATOM   1596  O   ALA A 213      20.762  77.371  36.170  1.00 15.78           O  
ATOM   1597  CB  ALA A 213      21.456  78.725  39.052  1.00 14.47           C  
ATOM   1598  N   LEU A 214      19.444  76.620  37.800  1.00 17.23           N  
ATOM   1599  CA  LEU A 214      19.215  75.340  37.148  1.00 17.40           C  
ATOM   1600  C   LEU A 214      18.471  75.542  35.830  1.00 17.43           C  
ATOM   1601  O   LEU A 214      18.868  74.949  34.826  1.00 16.57           O  
ATOM   1602  CB  LEU A 214      18.396  74.424  38.060  1.00 17.50           C  
ATOM   1603  CG  LEU A 214      18.075  73.031  37.521  1.00 18.28           C  
ATOM   1604  CD1 LEU A 214      19.361  72.228  37.240  1.00 16.16           C  
ATOM   1605  CD2 LEU A 214      17.181  72.343  38.542  1.00 18.41           C  
ATOM   1606  N   THR A 215      17.376  76.306  35.797  1.00 18.16           N  
ATOM   1607  CA  THR A 215      16.690  76.652  34.551  1.00 20.51           C  
ATOM   1608  C   THR A 215      17.630  77.239  33.515  1.00 19.00           C  
ATOM   1609  O   THR A 215      17.639  76.763  32.384  1.00 18.86           O  
ATOM   1610  CB  THR A 215      15.588  77.661  34.823  1.00 22.50           C  
ATOM   1611  OG1 THR A 215      14.710  77.005  35.712  1.00 25.93           O  
ATOM   1612  CG2 THR A 215      14.786  78.064  33.587  1.00 24.86           C  
ATOM   1613  N   GLU A 216      18.445  78.222  33.903  1.00 20.57           N  
ATOM   1614  CA  GLU A 216      19.391  78.863  32.990  1.00 21.22           C  
ATOM   1615  C   GLU A 216      20.420  77.897  32.435  1.00 19.96           C  
ATOM   1616  O   GLU A 216      20.661  77.908  31.230  1.00 18.44           O  
ATOM   1617  CB  GLU A 216      20.137  80.006  33.685  1.00 21.50           C  
ATOM   1618  CG  GLU A 216      19.101  81.055  34.058  1.00 29.92           C  
ATOM   1619  CD  GLU A 216      19.577  82.280  34.841  1.00 33.39           C  
ATOM   1620  OE1 GLU A 216      20.739  82.326  35.284  1.00 34.17           O  
ATOM   1621  OE2 GLU A 216      18.735  83.182  34.996  1.00 36.34           O  
ATOM   1622  N   LEU A 217      21.037  77.024  33.234  1.00 17.53           N  
ATOM   1623  CA  LEU A 217      22.044  76.156  32.672  1.00 16.16           C  
ATOM   1624  C   LEU A 217      21.376  75.044  31.866  1.00 15.95           C  
ATOM   1625  O   LEU A 217      22.025  74.486  30.967  1.00 17.26           O  
ATOM   1626  CB  LEU A 217      22.937  75.638  33.828  1.00 18.28           C  
ATOM   1627  CG  LEU A 217      22.497  74.682  34.932  1.00 18.67           C  
ATOM   1628  CD1 LEU A 217      22.645  73.271  34.401  1.00 19.98           C  
ATOM   1629  CD2 LEU A 217      23.392  74.796  36.166  1.00 16.76           C  
ATOM   1630  N   ARG A 218      20.098  74.674  32.092  1.00 15.70           N  
ATOM   1631  CA  ARG A 218      19.438  73.702  31.225  1.00 18.57           C  
ATOM   1632  C   ARG A 218      19.110  74.314  29.854  1.00 20.33           C  
ATOM   1633  O   ARG A 218      19.403  73.786  28.790  1.00 19.43           O  
ATOM   1634  CB  ARG A 218      18.168  73.221  31.874  1.00 18.65           C  
ATOM   1635  CG  ARG A 218      18.478  72.145  32.951  1.00 21.46           C  
ATOM   1636  CD  ARG A 218      17.230  71.440  33.530  1.00 24.00           C  
ATOM   1637  NE  ARG A 218      16.324  70.838  32.541  1.00 24.70           N  
ATOM   1638  CZ  ARG A 218      16.669  69.856  31.688  1.00 30.33           C  
ATOM   1639  NH1 ARG A 218      17.895  69.314  31.647  1.00 29.28           N  
ATOM   1640  NH2 ARG A 218      15.737  69.387  30.847  1.00 34.65           N  
ATOM   1641  N   GLN A 219      18.611  75.540  29.926  1.00 22.28           N  
ATOM   1642  CA  GLN A 219      18.189  76.362  28.793  1.00 24.08           C  
ATOM   1643  C   GLN A 219      19.263  76.608  27.755  1.00 21.98           C  
ATOM   1644  O   GLN A 219      19.047  76.459  26.562  1.00 20.92           O  
ATOM   1645  CB  GLN A 219      17.723  77.662  29.371  1.00 28.30           C  
ATOM   1646  CG  GLN A 219      16.593  78.331  28.702  1.00 37.47           C  
ATOM   1647  CD  GLN A 219      15.747  79.103  29.708  1.00 44.32           C  
ATOM   1648  OE1 GLN A 219      14.617  78.710  30.013  1.00 48.19           O  
ATOM   1649  NE2 GLN A 219      16.254  80.197  30.271  1.00 46.48           N  
ATOM   1650  N   ASP A 220      20.446  77.001  28.180  1.00 20.54           N  
ATOM   1651  CA  ASP A 220      21.482  77.311  27.235  1.00 18.87           C  
ATOM   1652  C   ASP A 220      22.267  76.104  26.762  1.00 18.04           C  
ATOM   1653  O   ASP A 220      23.288  76.268  26.095  1.00 17.21           O  
ATOM   1654  CB  ASP A 220      22.373  78.365  27.900  1.00 19.23           C  
ATOM   1655  CG  ASP A 220      23.286  77.924  29.050  1.00 23.42           C  
ATOM   1656  OD1 ASP A 220      23.290  76.753  29.418  1.00 22.80           O  
ATOM   1657  OD2 ASP A 220      24.011  78.764  29.587  1.00 23.68           O  
ATOM   1658  N   GLY A 221      21.922  74.884  27.187  1.00 19.83           N  
ATOM   1659  CA  GLY A 221      22.672  73.698  26.771  1.00 17.89           C  
ATOM   1660  C   GLY A 221      23.852  73.292  27.659  1.00 17.23           C  
ATOM   1661  O   GLY A 221      24.516  72.274  27.378  1.00 18.00           O  
ATOM   1662  N   THR A 222      24.144  73.993  28.763  1.00 15.57           N  
ATOM   1663  CA  THR A 222      25.243  73.608  29.654  1.00 17.83           C  
ATOM   1664  C   THR A 222      24.951  72.265  30.348  1.00 16.81           C  
ATOM   1665  O   THR A 222      25.877  71.455  30.505  1.00 17.81           O  
ATOM   1666  CB  THR A 222      25.471  74.666  30.740  1.00 17.58           C  
ATOM   1667  OG1 THR A 222      25.830  75.838  30.025  1.00 21.57           O  
ATOM   1668  CG2 THR A 222      26.574  74.330  31.733  1.00 20.30           C  
ATOM   1669  N   TYR A 223      23.698  71.997  30.748  1.00 15.87           N  
ATOM   1670  CA  TYR A 223      23.401  70.735  31.418  1.00 17.53           C  
ATOM   1671  C   TYR A 223      23.796  69.556  30.518  1.00 20.13           C  
ATOM   1672  O   TYR A 223      24.437  68.596  30.970  1.00 18.91           O  
ATOM   1673  CB  TYR A 223      21.901  70.660  31.750  1.00 16.67           C  
ATOM   1674  CG  TYR A 223      21.464  69.385  32.495  1.00 17.85           C  
ATOM   1675  CD1 TYR A 223      21.303  68.191  31.800  1.00 17.60           C  
ATOM   1676  CD2 TYR A 223      21.205  69.433  33.859  1.00 18.43           C  
ATOM   1677  CE1 TYR A 223      20.897  67.048  32.457  1.00 18.75           C  
ATOM   1678  CE2 TYR A 223      20.790  68.298  34.524  1.00 14.29           C  
ATOM   1679  CZ  TYR A 223      20.643  67.119  33.813  1.00 17.21           C  
ATOM   1680  OH  TYR A 223      20.170  65.983  34.441  1.00 18.56           O  
ATOM   1681  N   ASP A 224      23.448  69.636  29.226  1.00 20.65           N  
ATOM   1682  CA  ASP A 224      23.708  68.507  28.362  1.00 22.43           C  
ATOM   1683  C   ASP A 224      25.185  68.404  28.088  1.00 21.52           C  
ATOM   1684  O   ASP A 224      25.675  67.282  28.021  1.00 22.58           O  
ATOM   1685  CB  ASP A 224      22.930  68.659  27.073  1.00 26.30           C  
ATOM   1686  CG  ASP A 224      21.442  68.602  27.320  1.00 30.89           C  
ATOM   1687  OD1 ASP A 224      20.987  67.677  27.979  1.00 34.40           O  
ATOM   1688  OD2 ASP A 224      20.728  69.486  26.871  1.00 34.35           O  
ATOM   1689  N   LYS A 225      25.928  69.509  28.005  1.00 21.51           N  
ATOM   1690  CA  LYS A 225      27.358  69.448  27.828  1.00 23.29           C  
ATOM   1691  C   LYS A 225      27.930  68.738  29.029  1.00 23.17           C  
ATOM   1692  O   LYS A 225      28.824  67.907  28.881  1.00 23.90           O  
ATOM   1693  CB  LYS A 225      28.086  70.767  27.860  1.00 29.23           C  
ATOM   1694  CG  LYS A 225      27.651  71.904  27.003  1.00 38.95           C  
ATOM   1695  CD  LYS A 225      28.150  71.824  25.580  1.00 47.14           C  
ATOM   1696  CE  LYS A 225      28.337  73.277  25.114  1.00 53.17           C  
ATOM   1697  NZ  LYS A 225      27.112  74.074  25.160  1.00 57.79           N  
ATOM   1698  N   MET A 226      27.468  69.059  30.243  1.00 22.07           N  
ATOM   1699  CA  MET A 226      28.022  68.430  31.430  1.00 21.54           C  
ATOM   1700  C   MET A 226      27.655  66.942  31.552  1.00 19.88           C  
ATOM   1701  O   MET A 226      28.500  66.098  31.881  1.00 18.59           O  
ATOM   1702  CB  MET A 226      27.548  69.194  32.649  1.00 23.31           C  
ATOM   1703  CG  MET A 226      28.230  70.550  32.806  1.00 27.53           C  
ATOM   1704  SD  MET A 226      27.883  71.352  34.411  1.00 32.33           S  
ATOM   1705  CE  MET A 226      26.130  71.539  34.310  1.00 29.69           C  
ATOM   1706  N   ALA A 227      26.420  66.590  31.220  1.00 18.25           N  
ATOM   1707  CA  ALA A 227      25.955  65.239  31.338  1.00 18.43           C  
ATOM   1708  C   ALA A 227      26.687  64.277  30.394  1.00 22.54           C  
ATOM   1709  O   ALA A 227      27.029  63.135  30.747  1.00 21.24           O  
ATOM   1710  CB  ALA A 227      24.482  65.275  31.058  1.00 15.89           C  
ATOM   1711  N   LYS A 228      27.029  64.784  29.198  1.00 23.50           N  
ATOM   1712  CA  LYS A 228      27.711  63.999  28.170  1.00 23.94           C  
ATOM   1713  C   LYS A 228      29.080  63.569  28.640  1.00 24.45           C  
ATOM   1714  O   LYS A 228      29.615  62.584  28.142  1.00 25.16           O  
ATOM   1715  CB  LYS A 228      27.866  64.820  26.870  1.00 23.59           C  
ATOM   1716  N   LYS A 229      29.690  64.254  29.610  1.00 24.18           N  
ATOM   1717  CA  LYS A 229      30.960  63.804  30.162  1.00 25.19           C  
ATOM   1718  C   LYS A 229      30.834  62.454  30.897  1.00 23.08           C  
ATOM   1719  O   LYS A 229      31.788  61.711  31.078  1.00 24.37           O  
ATOM   1720  CB  LYS A 229      31.440  64.922  31.082  1.00 30.10           C  
ATOM   1721  CG  LYS A 229      32.597  64.696  32.059  1.00 36.86           C  
ATOM   1722  CD  LYS A 229      32.895  66.034  32.699  1.00 42.57           C  
ATOM   1723  CE  LYS A 229      33.867  66.012  33.860  1.00 45.89           C  
ATOM   1724  NZ  LYS A 229      33.758  67.276  34.589  1.00 46.43           N  
ATOM   1725  N   TYR A 230      29.657  62.094  31.358  1.00 21.02           N  
ATOM   1726  CA  TYR A 230      29.476  60.876  32.105  1.00 20.48           C  
ATOM   1727  C   TYR A 230      28.535  59.885  31.436  1.00 22.44           C  
ATOM   1728  O   TYR A 230      28.709  58.678  31.607  1.00 24.84           O  
ATOM   1729  CB  TYR A 230      28.912  61.195  33.486  1.00 18.52           C  
ATOM   1730  CG  TYR A 230      29.725  62.183  34.299  1.00 17.85           C  
ATOM   1731  CD1 TYR A 230      30.801  61.710  35.018  1.00 17.09           C  
ATOM   1732  CD2 TYR A 230      29.388  63.536  34.313  1.00 17.11           C  
ATOM   1733  CE1 TYR A 230      31.559  62.585  35.768  1.00 18.68           C  
ATOM   1734  CE2 TYR A 230      30.150  64.417  35.067  1.00 15.75           C  
ATOM   1735  CZ  TYR A 230      31.230  63.934  35.786  1.00 17.58           C  
ATOM   1736  OH  TYR A 230      32.031  64.776  36.526  1.00 17.85           O  
ATOM   1737  N   PHE A 231      27.516  60.356  30.705  1.00 22.44           N  
ATOM   1738  CA  PHE A 231      26.392  59.526  30.288  1.00 23.19           C  
ATOM   1739  C   PHE A 231      26.167  59.615  28.800  1.00 25.38           C  
ATOM   1740  O   PHE A 231      26.395  60.675  28.202  1.00 26.25           O  
ATOM   1741  CB  PHE A 231      25.097  59.982  30.979  1.00 20.81           C  
ATOM   1742  CG  PHE A 231      25.253  60.208  32.477  1.00 20.23           C  
ATOM   1743  CD1 PHE A 231      25.563  59.139  33.325  1.00 17.99           C  
ATOM   1744  CD2 PHE A 231      25.107  61.493  32.991  1.00 19.03           C  
ATOM   1745  CE1 PHE A 231      25.724  59.372  34.685  1.00 18.33           C  
ATOM   1746  CE2 PHE A 231      25.269  61.707  34.356  1.00 19.02           C  
ATOM   1747  CZ  PHE A 231      25.583  60.651  35.203  1.00 18.14           C  
ATOM   1748  N   ASP A 232      25.644  58.553  28.202  1.00 26.45           N  
ATOM   1749  CA  ASP A 232      25.376  58.580  26.786  1.00 29.86           C  
ATOM   1750  C   ASP A 232      23.881  58.378  26.569  1.00 29.52           C  
ATOM   1751  O   ASP A 232      23.413  57.858  25.556  1.00 33.04           O  
ATOM   1752  CB  ASP A 232      26.224  57.482  26.121  1.00 35.81           C  
ATOM   1753  CG  ASP A 232      25.840  56.016  26.319  1.00 42.52           C  
ATOM   1754  OD1 ASP A 232      25.145  55.657  27.278  1.00 45.70           O  
ATOM   1755  OD2 ASP A 232      26.239  55.219  25.470  1.00 46.77           O  
ATOM   1756  N   PHE A 233      23.072  58.706  27.562  1.00 26.95           N  
ATOM   1757  CA  PHE A 233      21.623  58.547  27.493  1.00 24.89           C  
ATOM   1758  C   PHE A 233      21.086  59.769  28.248  1.00 25.66           C  
ATOM   1759  O   PHE A 233      21.874  60.454  28.931  1.00 25.02           O  
ATOM   1760  CB  PHE A 233      21.203  57.289  28.214  1.00 26.06           C  
ATOM   1761  CG  PHE A 233      21.709  57.181  29.659  1.00 25.59           C  
ATOM   1762  CD1 PHE A 233      22.971  56.668  29.901  1.00 24.04           C  
ATOM   1763  CD2 PHE A 233      20.901  57.611  30.698  1.00 26.12           C  
ATOM   1764  CE1 PHE A 233      23.425  56.605  31.189  1.00 24.57           C  
ATOM   1765  CE2 PHE A 233      21.378  57.542  31.980  1.00 23.77           C  
ATOM   1766  CZ  PHE A 233      22.629  57.043  32.214  1.00 24.13           C  
ATOM   1767  N   ASN A 234      19.803  60.091  28.229  1.00 23.98           N  
ATOM   1768  CA  ASN A 234      19.318  61.251  28.936  1.00 26.79           C  
ATOM   1769  C   ASN A 234      19.089  60.976  30.416  1.00 24.88           C  
ATOM   1770  O   ASN A 234      18.129  60.368  30.854  1.00 25.61           O  
ATOM   1771  CB  ASN A 234      18.086  61.702  28.168  1.00 29.07           C  
ATOM   1772  CG  ASN A 234      16.998  62.468  28.898  1.00 32.13           C  
ATOM   1773  OD1 ASN A 234      15.846  62.027  28.849  1.00 37.05           O  
ATOM   1774  ND2 ASN A 234      17.160  63.598  29.554  1.00 31.95           N  
ATOM   1775  N   VAL A 235      20.023  61.408  31.258  1.00 23.59           N  
ATOM   1776  CA  VAL A 235      19.968  61.185  32.696  1.00 21.04           C  
ATOM   1777  C   VAL A 235      18.826  61.978  33.326  1.00 20.80           C  
ATOM   1778  O   VAL A 235      18.266  61.613  34.362  1.00 20.04           O  
ATOM   1779  CB  VAL A 235      21.394  61.570  33.244  1.00 20.72           C  
ATOM   1780  CG1 VAL A 235      21.642  63.072  33.234  1.00 18.46           C  
ATOM   1781  CG2 VAL A 235      21.534  61.017  34.644  1.00 20.02           C  
ATOM   1782  N   TYR A 236      18.448  63.091  32.718  1.00 19.94           N  
ATOM   1783  CA  TYR A 236      17.432  63.926  33.293  1.00 18.69           C  
ATOM   1784  C   TYR A 236      16.112  63.178  33.339  1.00 22.21           C  
ATOM   1785  O   TYR A 236      15.291  63.424  34.216  1.00 20.62           O  
ATOM   1786  CB  TYR A 236      17.376  65.192  32.443  1.00 17.90           C  
ATOM   1787  CG  TYR A 236      16.414  66.193  33.019  1.00 19.16           C  
ATOM   1788  CD1 TYR A 236      16.809  66.993  34.083  1.00 19.98           C  
ATOM   1789  CD2 TYR A 236      15.151  66.275  32.466  1.00 21.14           C  
ATOM   1790  CE1 TYR A 236      15.918  67.879  34.636  1.00 19.79           C  
ATOM   1791  CE2 TYR A 236      14.254  67.154  33.016  1.00 23.95           C  
ATOM   1792  CZ  TYR A 236      14.666  67.944  34.076  1.00 23.42           C  
ATOM   1793  OH  TYR A 236      13.799  68.866  34.603  1.00 25.42           O  
ATOM   1794  N   GLY A 237      15.948  62.172  32.474  1.00 26.25           N  
ATOM   1795  CA  GLY A 237      14.670  61.532  32.250  1.00 32.94           C  
ATOM   1796  C   GLY A 237      13.995  62.688  31.559  1.00 40.20           C  
ATOM   1797  O   GLY A 237      14.636  63.388  30.767  1.00 43.31           O  
ATOM   1798  N   ASP A 238      12.752  62.964  31.816  1.00 45.63           N  
ATOM   1799  CA  ASP A 238      12.212  64.269  31.485  1.00 52.36           C  
ATOM   1800  C   ASP A 238      10.887  64.247  32.186  1.00 53.39           C  
ATOM   1801  O   ASP A 238      10.211  63.199  32.157  1.00 56.64           O  
ATOM   1802  CB  ASP A 238      12.039  64.530  29.952  1.00 56.07           C  
ATOM   1803  CG  ASP A 238      12.891  65.767  29.573  1.00 59.73           C  
ATOM   1804  OD1 ASP A 238      12.474  66.894  29.866  1.00 62.78           O  
ATOM   1805  OD2 ASP A 238      13.989  65.622  29.023  1.00 60.38           O  
TER    1806      ASP A 238                                                      
HETATM 1807  N   LYS A 240      18.663  58.231  45.771  1.00 10.52           N  
HETATM 1808  CA  LYS A 240      18.729  57.446  46.982  1.00 11.60           C  
HETATM 1809  C   LYS A 240      18.141  58.287  48.141  1.00 13.99           C  
HETATM 1810  O   LYS A 240      18.040  57.797  49.267  1.00 10.70           O  
HETATM 1811  CB  LYS A 240      20.183  57.087  47.258  1.00  9.82           C  
HETATM 1812  CG  LYS A 240      21.160  58.248  47.238  1.00 11.18           C  
HETATM 1813  CD  LYS A 240      22.442  57.774  47.856  1.00 10.09           C  
HETATM 1814  CE  LYS A 240      23.521  58.814  47.667  1.00  9.58           C  
HETATM 1815  NZ  LYS A 240      24.756  58.442  48.359  1.00 12.40           N  
HETATM 1816  OXT LYS A 240      17.791  59.453  47.900  1.00 12.31           O  
HETATM 1817  O   HOH A 401      20.737  65.844  45.608  1.00 11.65           O  
HETATM 1818  O   HOH A 402      18.914  75.522  53.480  1.00 14.83           O  
HETATM 1819  O   HOH A 403      25.554  61.475  44.768  1.00 12.89           O  
HETATM 1820  O   HOH A 404      21.500  53.849  47.639  1.00 14.49           O  
HETATM 1821  O   HOH A 405      27.624  57.479  53.221  1.00 12.10           O  
HETATM 1822  O   HOH A 406      21.320  65.250  42.838  1.00 18.08           O  
HETATM 1823  O   HOH A 407      16.035  44.893  40.162  1.00 17.72           O  
HETATM 1824  O   HOH A 408      20.444  58.223  38.798  1.00 16.71           O  
HETATM 1825  O   HOH A 409      19.500  55.652  38.735  1.00 14.92           O  
HETATM 1826  O   HOH A 410      18.593  60.084  54.950  1.00 33.02           O  
HETATM 1827  O   HOH A 411      15.196  56.939  45.408  1.00 16.25           O  
HETATM 1828  O   HOH A 412      13.917  72.359  57.043  1.00 17.62           O  
HETATM 1829  O   HOH A 413      26.044  76.133  57.248  1.00 18.73           O  
HETATM 1830  O   HOH A 414      20.324  82.206  40.536  1.00 20.65           O  
HETATM 1831  O   HOH A 415      15.980  55.437  43.212  1.00 15.95           O  
HETATM 1832  O   HOH A 416      22.222  51.326  48.601  1.00 13.63           O  
HETATM 1833  O   HOH A 417      30.824  72.791  36.985  1.00 24.79           O  
HETATM 1834  O   HOH A 418      24.789  56.457  55.695  1.00 14.49           O  
HETATM 1835  O   HOH A 419      28.343  53.902  42.879  1.00 21.14           O  
HETATM 1836  O   HOH A 420      20.317  62.110  55.450  1.00 20.32           O  
HETATM 1837  O   HOH A 421      17.534  55.605  36.355  1.00 27.49           O  
HETATM 1838  O   HOH A 422      15.839  50.334  32.985  1.00 30.67           O  
HETATM 1839  O   HOH A 423      27.035  55.907  49.464  1.00 22.31           O  
HETATM 1840  O   HOH A 424      21.443  58.713  41.401  1.00 14.28           O  
HETATM 1841  O   HOH A 425      14.235  70.654  36.584  1.00 19.47           O  
HETATM 1842  O   HOH A 426      26.031  60.562  47.318  1.00 17.08           O  
HETATM 1843  O   HOH A 427      29.074  43.985  34.690  1.00 29.82           O  
HETATM 1844  O   HOH A 428      25.052  37.192  43.631  1.00 26.28           O  
HETATM 1845  O   HOH A 429      34.198  73.228  56.123  1.00 25.00           O  
HETATM 1846  O   HOH A 430      15.555  60.294  54.569  1.00 28.08           O  
HETATM 1847  O   HOH A 431      12.429  69.774  59.943  1.00 32.03           O  
HETATM 1848  O   HOH A 432      14.031  71.636  60.928  1.00 31.21           O  
HETATM 1849  O   HOH A 433      12.794  53.055  40.949  1.00 25.35           O  
HETATM 1850  O   HOH A 434      13.922  76.372  50.806  1.00 26.38           O  
HETATM 1851  O   HOH A 435      18.668  58.982  35.235  1.00 32.12           O  
HETATM 1852  O   HOH A 436      13.284  59.448  38.938  1.00 25.84           O  
HETATM 1853  O   HOH A 437      14.348  48.184  34.092  1.00 22.71           O  
HETATM 1854  O   HOH A 438      20.614  50.656  32.890  1.00 52.50           O  
HETATM 1855  O   HOH A 439      17.306  81.544  51.838  1.00 23.49           O  
HETATM 1856  O   HOH A 440      34.162  71.660  43.839  1.00 61.89           O  
HETATM 1857  O   HOH A 441      14.613  75.158  37.956  1.00 26.11           O  
HETATM 1858  O   HOH A 442      32.034  60.587  40.875  1.00 26.11           O  
HETATM 1859  O   HOH A 443       8.005  58.918  50.812  1.00 29.24           O  
HETATM 1860  O   HOH A 444      22.525  39.150  38.082  1.00 42.28           O  
HETATM 1861  O   HOH A 445      22.062  46.422  59.381  1.00 26.33           O  
HETATM 1862  O   HOH A 446      23.103  44.108  33.967  1.00 30.69           O  
HETATM 1863  O   HOH A 447      10.127  71.366  48.118  1.00 27.98           O  
HETATM 1864  O   HOH A 448      30.476  54.458  44.583  1.00 29.13           O  
HETATM 1865  O   HOH A 449      10.997  70.013  43.449  1.00 29.90           O  
HETATM 1866  O   HOH A 450      31.426  61.090  52.383  1.00 33.65           O  
HETATM 1867  O   HOH A 451      26.657  56.278  58.866  1.00 36.37           O  
HETATM 1868  O   HOH A 452      19.729  67.877  63.318  1.00 34.31           O  
HETATM 1869  O   HOH A 453      34.383  75.970  56.698  1.00 33.59           O  
HETATM 1870  O   HOH A 454      31.504  43.405  56.323  1.00 36.85           O  
HETATM 1871  O   HOH A 455      18.035  41.599  58.665  1.00 40.16           O  
HETATM 1872  O   HOH A 456      34.930  72.646  48.078  1.00 39.83           O  
HETATM 1873  O   HOH A 457      42.243  60.205  40.209  1.00 58.02           O  
HETATM 1874  O   HOH A 458      18.540  46.941  58.291  1.00 51.18           O  
HETATM 1875  O   HOH A 459      17.658  78.672  57.497  1.00 25.69           O  
HETATM 1876  O   HOH A 460       9.510  53.893  41.415  1.00 41.33           O  
HETATM 1877  O   HOH A 461      14.234  59.092  42.677  1.00 25.80           O  
HETATM 1878  O   HOH A 462      17.009  84.376  45.359  1.00 27.32           O  
HETATM 1879  O   HOH A 463      14.559  73.392  35.949  1.00 35.11           O  
HETATM 1880  O   HOH A 464      33.759  66.790  38.552  1.00 19.61           O  
HETATM 1881  O   HOH A 465      21.156  82.707  38.097  1.00 35.45           O  
HETATM 1882  O   HOH A 466      13.512  80.677  40.892  1.00 38.65           O  
HETATM 1883  O   HOH A 467      31.546  77.529  41.312  1.00 36.52           O  
HETATM 1884  O   HOH A 468      19.661  64.247  30.067  1.00 36.60           O  
HETATM 1885  O   HOH A 469      16.093  54.947  55.307  1.00 26.21           O  
HETATM 1886  O   HOH A 470       9.024  70.983  50.828  1.00 37.14           O  
HETATM 1887  O   HOH A 471      15.518  57.668  55.878  1.00 52.71           O  
HETATM 1888  O   HOH A 472      26.675  56.246  29.703  1.00 40.98           O  
HETATM 1889  O   HOH A 473      10.872  57.078  51.027  1.00 41.98           O  
HETATM 1890  O   HOH A 474      45.663  59.393  47.582  1.00 39.96           O  
HETATM 1891  O   HOH A 475      34.660  67.700  53.651  1.00 41.92           O  
HETATM 1892  O   HOH A 476      29.000  61.886  58.372  1.00 50.06           O  
HETATM 1893  O   HOH A 477      26.709  53.835  61.430  1.00 52.48           O  
HETATM 1894  O   HOH A 478      18.195  37.684  37.469  1.00 63.22           O  
HETATM 1895  O   HOH A 479      32.626  78.837  44.772  1.00 55.03           O  
HETATM 1896  O   HOH A 480      11.692  61.934  56.225  1.00 42.19           O  
HETATM 1897  O   HOH A 481       9.871  42.806  46.160  1.00 37.88           O  
HETATM 1898  O   HOH A 482      19.197  80.903  30.053  1.00 40.71           O  
HETATM 1899  O   HOH A 483      12.083  61.541  37.675  1.00 41.72           O  
HETATM 1900  O   HOH A 484      34.508  49.486  46.823  1.00 44.00           O  
HETATM 1901  O   HOH A 485      15.005  39.473  58.296  1.00 26.80           O  
HETATM 1902  O   HOH A 486      11.885  78.688  44.024  1.00 55.51           O  
HETATM 1903  O   HOH A 487      33.071  71.085  38.907  1.00 36.60           O  
HETATM 1904  O   HOH A 488      34.925  59.040  50.600  1.00 49.57           O  
HETATM 1905  O   HOH A 489      14.604  82.870  52.539  1.00 40.32           O  
HETATM 1906  O   HOH A 490      11.562  55.478  40.731  1.00 46.48           O  
HETATM 1907  O   HOH A 491      39.333  65.192  50.608  1.00 46.55           O  
HETATM 1908  O   HOH A 492      21.202  71.475  28.560  1.00 23.75           O  
HETATM 1909  O   HOH A 493      22.569  48.198  31.836  1.00 61.29           O  
HETATM 1910  O   HOH A 494      12.057  59.334  51.917  1.00 21.33           O  
HETATM 1911  O   HOH A 495      27.312  41.739  55.454  1.00 40.78           O  
HETATM 1912  O   HOH A 496      15.777  82.708  34.650  1.00 54.35           O  
HETATM 1913  O   HOH A 497      19.747  84.514  42.094  1.00 41.79           O  
HETATM 1914  O   HOH A 498      30.222  66.251  57.715  1.00 50.79           O  
HETATM 1915  O   HOH A 499      24.312  53.216  32.338  1.00 46.44           O  
HETATM 1916  O   HOH A 500      10.816  45.166  39.080  1.00 61.84           O  
HETATM 1917  O   HOH A 501      11.462  41.392  38.661  1.00 69.31           O  
HETATM 1918  O   HOH A 502      26.987  59.080  60.116  1.00 53.95           O  
HETATM 1919  O   HOH A 503      37.247  69.267  46.501  1.00 48.77           O  
HETATM 1920  O   HOH A 504      33.410  41.008  39.045  1.00 51.78           O  
HETATM 1921  O   HOH A 505      22.884  33.627  51.223  1.00 82.89           O  
HETATM 1922  O   HOH A 506      30.517  58.295  53.126  1.00 33.91           O  
HETATM 1923  O   HOH A 507      29.211  59.302  27.262  1.00 59.36           O  
HETATM 1924  O   HOH A 508      35.206  57.764  47.122  1.00 45.41           O  
HETATM 1925  O   HOH A 510      31.256  55.927  54.926  1.00 45.88           O  
HETATM 1926  O   HOH A 511      24.936  65.029  61.382  1.00 45.67           O  
HETATM 1927  O   HOH A 512      24.045  71.351  24.616  1.00 40.62           O  
HETATM 1928  O   HOH A 513      28.848  79.511  32.700  1.00 66.68           O  
HETATM 1929  O   HOH A 514      10.778  49.369  35.497  1.00 71.73           O  
HETATM 1930  O   HOH A 515      31.495  75.573  36.741  1.00 47.60           O  
HETATM 1931  O   HOH A 516      32.362  56.149  37.979  1.00 65.56           O  
HETATM 1932  O   HOH A 518      10.199  82.014  54.747  1.00 68.92           O  
HETATM 1933  O   HOH A 519      12.498  33.734  55.685  1.00 75.12           O  
HETATM 1934  O   HOH A 521      10.386  65.938  40.058  1.00 41.21           O  
HETATM 1935  O   HOH A 522      35.073  69.632  55.734  1.00 56.00           O  
HETATM 1936  O   HOH A 523      18.078  73.258  26.285  1.00 52.48           O  
HETATM 1937  O   HOH A 525      10.372  68.507  41.343  1.00 49.48           O  
HETATM 1938  O   HOH A 526      10.477  72.771  43.128  1.00 54.90           O  
HETATM 1939  O   HOH A 527      32.700  45.975  33.295  1.00 69.92           O  
HETATM 1940  O   HOH A 528      30.465  67.642  33.386  1.00 52.17           O  
HETATM 1941  O   HOH A 529      33.221  57.269  53.532  1.00 57.41           O  
HETATM 1942  O   HOH A 530      26.715  79.364  55.711  1.00 43.15           O  
HETATM 1943  O   HOH A 531       8.989  62.494  57.511  1.00 55.77           O  
HETATM 1944  O   HOH A 532      16.690  83.789  42.084  1.00 51.30           O  
HETATM 1945  O   HOH A 534      22.644  37.769  35.504  1.00 50.33           O  
HETATM 1946  O   HOH A 535      11.906  79.673  46.532  1.00 67.46           O  
HETATM 1947  O   HOH A 536      18.681  67.285  29.538  1.00 46.08           O  
HETATM 1948  O   HOH A 537      33.528  60.283  38.377  1.00 62.73           O  
HETATM 1949  O   HOH A 538      35.250  68.721  40.281  1.00 41.55           O  
HETATM 1950  O   HOH A 539      25.422  38.848  55.502  1.00 76.30           O  
HETATM 1951  O   HOH A 540      18.881  60.675  57.836  1.00 64.51           O  
HETATM 1952  O   HOH A 541      21.935  53.446  33.828  1.00 41.65           O  
HETATM 1953  O   HOH A 542       6.301  69.146  45.270  1.00 71.23           O  
HETATM 1954  O   HOH A 543      35.902  58.006  40.780  1.00 48.52           O  
HETATM 1955  O   HOH A 544       4.619  52.571  42.030  1.00 57.01           O  
HETATM 1956  O   HOH A 545      24.928  86.674  44.540  1.00 55.46           O  
HETATM 1957  O   HOH A 547      41.364  59.890  47.619  1.00 55.57           O  
HETATM 1958  O   HOH A 548      22.216  60.353  61.294  1.00 64.14           O  
HETATM 1959  O   HOH A 549      39.170  68.238  48.619  1.00 54.79           O  
HETATM 1960  O   HOH A 550       7.243  47.613  44.796  1.00 49.64           O  
HETATM 1961  O   HOH A 551      22.990  51.107  63.150  1.00 51.14           O  
HETATM 1962  O   HOH A 552      11.209  69.870  38.925  1.00 62.38           O  
HETATM 1963  O   HOH A 553      17.759  66.003  63.126  1.00 68.13           O  
HETATM 1964  O   HOH A 554      29.006  57.609  61.421  1.00 64.72           O  
HETATM 1965  O   HOH A 556      11.014  76.486  50.463  1.00 53.04           O  
HETATM 1966  O   HOH A 557       9.202  55.748  53.306  1.00 69.20           O  
HETATM 1967  O   HOH A 558      36.150  71.191  49.958  1.00 74.33           O  
HETATM 1968  O   HOH A 559      24.181  53.706  62.443  1.00 59.43           O  
HETATM 1969  O   HOH A 560      22.272  52.455  30.085  1.00 70.23           O  
HETATM 1970  O   HOH A 561      31.692  55.766  57.446  1.00 79.71           O  
HETATM 1971  O   HOH A 562      23.517  81.987  33.545  1.00 61.21           O  
HETATM 1972  O   HOH A 563       9.798  65.133  37.232  1.00 65.30           O  
HETATM 1973  O   HOH A 564       8.372  47.427  40.593  1.00 62.34           O  
HETATM 1974  O   HOH A 565      18.175  50.730  31.130  1.00 55.50           O  
HETATM 1975  O   HOH A 566      27.288  82.846  34.930  1.00 59.71           O  
HETATM 1976  O   HOH A 567      31.112  80.301  43.026  1.00 56.22           O  
HETATM 1977  O   HOH A 568      26.285  34.959  46.556  1.00 82.53           O  
HETATM 1978  O   HOH A 569       9.350  69.542  45.998  1.00 60.21           O  
HETATM 1979  O   HOH A 570      26.260  44.237  33.765  1.00 54.60           O  
HETATM 1980  O   HOH A 571      28.035  37.591  45.471  1.00 59.76           O  
HETATM 1981  O   HOH A 572      15.888  36.983  34.207  1.00 70.58           O  
HETATM 1982  O   HOH A 573      11.651  61.573  34.720  1.00 56.97           O  
HETATM 1983  O   HOH A 574      29.872  40.658  56.780  1.00 66.67           O  
HETATM 1984  O   HOH A 575      23.653  67.043  63.696  1.00 58.02           O  
HETATM 1985  O   HOH A 576      33.588  50.869  30.583  1.00 81.86           O  
HETATM 1986  O   HOH A 577      34.951  71.489  53.771  1.00 63.75           O  
HETATM 1987  O   HOH A 578      21.744  64.864  28.541  1.00 65.33           O  
HETATM 1988  O   HOH A 579      30.851  74.293  33.168  1.00 68.47           O  
HETATM 1989  O   HOH A 580      34.056  38.948  42.416  1.00 57.72           O  
HETATM 1990  O   HOH A 581      36.353  69.677  43.500  1.00 74.22           O  
HETATM 1991  O   HOH A 583      19.974  51.868  60.533  1.00 65.35           O  
HETATM 1992  O   HOH A 584      19.063  54.687  32.574  1.00 63.67           O  
HETATM 1993  O   HOH A 586      19.686  72.255  23.632  1.00 80.10           O  
HETATM 1994  O   HOH A 587      17.428  71.120  28.598  1.00 56.33           O  
HETATM 1995  O   HOH A 588      24.025  65.098  26.802  1.00 69.83           O  
HETATM 1996  O   HOH A 589      28.887  34.866  37.832  1.00 60.97           O  
HETATM 1997  O   HOH A 590      33.421  51.907  44.640  1.00 72.95           O  
HETATM 1998  O   HOH A 592      30.379  57.471  33.995  1.00 50.35           O  
HETATM 1999  O   HOH A 593      11.878  75.919  34.602  1.00 63.86           O  
HETATM 2000  O   HOH A 594      36.528  43.109  48.768  1.00 67.97           O  
HETATM 2001  O   HOH A 596      14.121  52.483  34.679  1.00 64.64           O  
HETATM 2002  O   HOH A 598      24.287  78.610  57.694  1.00 75.94           O  
HETATM 2003  O   HOH A 599      27.416  81.998  31.423  1.00 68.14           O  
HETATM 2004  O   HOH A 600       9.535  53.378  55.633  1.00 68.15           O  
HETATM 2005  O   HOH A 601       8.626  83.164  57.408  1.00 71.48           O  
HETATM 2006  O   HOH A 602      18.094  58.366  27.054  1.00 57.57           O  
HETATM 2007  O   HOH A 604      25.314  48.605  32.844  1.00 70.80           O  
HETATM 2008  O   HOH A 605      34.778  52.465  54.172  1.00 74.85           O  
HETATM 2009  O   HOH A 606       1.474  40.308  55.070  1.00 62.11           O  
HETATM 2010  O   HOH A 607      32.768  58.845  34.177  1.00 57.07           O  
HETATM 2011  O   HOH A 608      13.564  51.283  57.999  1.00 84.87           O  
HETATM 2012  O   HOH A 611      16.726  58.613  32.906  1.00 62.15           O  
HETATM 2013  O   HOH A 612      25.733  85.149  36.836  1.00 67.75           O  
HETATM 2014  O   HOH A 613      35.911  42.254  41.855  1.00 61.32           O  
HETATM 2015  O   HOH A 615      23.139  34.579  43.264  1.00 85.05           O  
CONECT  283  342                                                                
CONECT  342  283                                                                
MASTER      314    0    1   10   10    0    4    6 2014    1    2   19          
END                                                                             



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