HEADER    SUGAR BINDING PROTEIN                   22-JUN-04   1WLC              
TITLE     CONGERIN II Y16S/T88I DOUBLE MUTANT                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CONGERIN II;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BETA-GALACTOSIDE-BINDING LECTIN 2;                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CONGER MYRIASTER;                               
SOURCE   3 ORGANISM_COMMON: WHITESPOTTED CONGER;                                
SOURCE   4 ORGANISM_TAXID: 7943;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PTV118N                                   
KEYWDS    GALECTIN, BETA-SANDWICH, THERMOSTABILITY, DOUBLE-MUTANT, SUGAR        
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SHIONYU-MITSUYAMA,Y.ITO,A.KONNO,Y.MIWA,T.OGAWA,K.MURAMOTO,T.SHIRAI  
REVDAT   4   10-NOV-21 1WLC    1       REMARK SEQADV                            
REVDAT   3   11-FEB-15 1WLC    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 1WLC    1       VERSN                                    
REVDAT   1   07-JUN-05 1WLC    0                                                
JRNL        AUTH   C.SHIONYU-MITSUYAMA,Y.ITO,A.KONNO,Y.MIWA,T.OGAWA,K.MURAMOTO, 
JRNL        AUTH 2 T.SHIRAI                                                     
JRNL        TITL   IN VITRO EVOLUTIONARY THERMOSTABILIZATION OF CONGERIN II: A  
JRNL        TITL 2 LIMITED REPRODUCTION OF NATURAL PROTEIN EVOLUTION BY         
JRNL        TITL 3 ARTIFICIAL SELECTION PRESSURE                                
JRNL        REF    J.MOL.BIOL.                   V. 347   385 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15740748                                                     
JRNL        DOI    10.1016/J.JMB.2005.01.027                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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             : 9452                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 480                             
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            : 1073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1WLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023702.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10418                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M MAGNESIUM SULFATE, 0.05M MES, PH    
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.41500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.41500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.77500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.41500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.41500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.77500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.41500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.41500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       39.77500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.41500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.41500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       39.77500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     SER A     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   5   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG A  29   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 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    VAL A  67      -58.81   -128.77                                   
REMARK 500    GLN A  70     -144.51    -93.41                                   
REMARK 500    ASP A  93     -167.34   -124.30                                   
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 MES A 777                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WLD   RELATED DB: PDB                                   
REMARK 900 CONGERIN II T88I SINGLE MUTANT                                       
REMARK 900 RELATED ID: 1IS3   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF WILD TYPE CONGERIN II                                   
DBREF  1WLC A    1   135  UNP    Q9YIC2   LEG2_CONMY       1    135             
SEQADV 1WLC SER A   16  UNP  Q9YIC2    TYR    16 ENGINEERED MUTATION            
SEQADV 1WLC ILE A   88  UNP  Q9YIC2    THR    88 ENGINEERED MUTATION            
SEQRES   1 A  135  SER ASP ARG ALA GLU VAL ARG ASN ILE PRO PHE LYS LEU          
SEQRES   2 A  135  GLY MET SER LEU THR VAL GLY GLY VAL VAL ASN SER ASN          
SEQRES   3 A  135  ALA THR ARG PHE SER ILE ASN VAL GLY GLU SER THR ASP          
SEQRES   4 A  135  SER ILE ALA MET HIS MET ASP HIS ARG PHE SER TYR GLY          
SEQRES   5 A  135  ALA ASP GLN ASN VAL LEU VAL LEU ASN SER LEU VAL HIS          
SEQRES   6 A  135  ASN VAL GLY TRP GLN GLN GLU GLU ARG SER LYS LYS PHE          
SEQRES   7 A  135  PRO PHE THR LYS GLY ASP HIS PHE GLN ILE THR ILE THR          
SEQRES   8 A  135  PHE ASP THR HIS THR PHE TYR ILE GLN LEU SER ASN GLY          
SEQRES   9 A  135  GLU THR VAL GLU PHE PRO ASN ARG ASN LYS ASP ALA ALA          
SEQRES  10 A  135  PHE ASN LEU ILE TYR LEU ALA GLY ASP ALA ARG LEU THR          
SEQRES  11 A  135  PHE VAL ARG LEU GLU                                          
HET    MES  A 777      12                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
FORMUL   2  MES    C6 H13 N O4 S                                                
FORMUL   3  HOH   *93(H2 O)                                                     
SHEET    1   A 6 ALA A   4  LYS A  12  0                                        
SHEET    2   A 6 ALA A 117  GLY A 125 -1  O  ASN A 119   N  ASN A   8           
SHEET    3   A 6 ARG A  29  SER A  37 -1  N  GLY A  35   O  LEU A 120           
SHEET    4   A 6 SER A  40  TYR A  51 -1  O  SER A  40   N  GLU A  36           
SHEET    5   A 6 ASP A  54  VAL A  64 -1  O  VAL A  59   N  ASP A  46           
SHEET    6   A 6 GLY A  68  TRP A  69 -1  O  GLY A  68   N  VAL A  64           
SHEET    1   B 6 ALA A   4  LYS A  12  0                                        
SHEET    2   B 6 ALA A 117  GLY A 125 -1  O  ASN A 119   N  ASN A   8           
SHEET    3   B 6 ARG A  29  SER A  37 -1  N  GLY A  35   O  LEU A 120           
SHEET    4   B 6 SER A  40  TYR A  51 -1  O  SER A  40   N  GLU A  36           
SHEET    5   B 6 ASP A  54  VAL A  64 -1  O  VAL A  59   N  ASP A  46           
SHEET    6   B 6 GLU A  73  SER A  75 -1  O  GLU A  73   N  LEU A  60           
SHEET    1   C 5 THR A 106  PRO A 110  0                                        
SHEET    2   C 5 THR A  96  GLN A 100 -1  N  PHE A  97   O  PHE A 109           
SHEET    3   C 5 HIS A  85  PHE A  92 -1  N  THR A  91   O  TYR A  98           
SHEET    4   C 5 LEU A  17  VAL A  23 -1  N  LEU A  17   O  ILE A  90           
SHEET    5   C 5 ALA A 127  LEU A 134 -1  O  ARG A 133   N  THR A  18           
SITE     1 AC1  7 ARG A   3  THR A  38  ASP A  39  HIS A  65                    
SITE     2 AC1  7 TRP A  69  TYR A 122  ALA A 124                               
CRYST1   60.830   60.830   79.550  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016430  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012570        0.00000                         
ATOM      1  N   ASP A   2      32.828  22.008   2.717  1.00 43.84           N  
ATOM      2  CA  ASP A   2      33.135  21.209   3.962  1.00 43.08           C  
ATOM      3  C   ASP A   2      31.869  20.597   4.565  1.00 39.31           C  
ATOM      4  O   ASP A   2      31.570  19.394   4.497  1.00 37.32           O  
ATOM      5  CB  ASP A   2      33.893  22.120   4.905  1.00 47.62           C  
ATOM      6  CG  ASP A   2      34.208  21.730   6.325  1.00 51.06           C  
ATOM      7  OD1 ASP A   2      34.349  20.517   6.624  1.00 52.90           O  
ATOM      8  OD2 ASP A   2      34.348  22.639   7.199  1.00 52.26           O  
ATOM      9  N   ARG A   3      31.074  21.472   5.195  1.00 33.09           N  
ATOM     10  CA  ARG A   3      29.824  21.026   5.811  1.00 26.94           C  
ATOM     11  C   ARG A   3      28.878  20.535   4.715  1.00 21.09           C  
ATOM     12  O   ARG A   3      28.904  20.998   3.572  1.00 18.61           O  
ATOM     13  CB  ARG A   3      29.227  22.185   6.590  1.00 27.42           C  
ATOM     14  CG  ARG A   3      28.435  23.183   5.783  1.00 28.88           C  
ATOM     15  CD  ARG A   3      28.059  24.387   6.650  1.00 30.70           C  
ATOM     16  NE  ARG A   3      29.203  25.265   6.811  1.00 31.54           N  
ATOM     17  CZ  ARG A   3      29.501  26.301   6.023  1.00 30.68           C  
ATOM     18  NH1 ARG A   3      28.703  26.608   5.012  1.00 32.36           N  
ATOM     19  NH2 ARG A   3      30.561  27.053   6.227  1.00 28.58           N  
ATOM     20  N   ALA A   4      27.952  19.687   5.103  1.00 16.80           N  
ATOM     21  CA  ALA A   4      26.841  19.295   4.247  1.00 13.16           C  
ATOM     22  C   ALA A   4      25.710  20.303   4.431  1.00 14.25           C  
ATOM     23  O   ALA A   4      25.264  20.483   5.568  1.00 12.64           O  
ATOM     24  CB  ALA A   4      26.399  17.893   4.578  1.00 13.08           C  
ATOM     25  N   GLU A   5      25.191  20.851   3.335  1.00 12.76           N  
ATOM     26  CA  GLU A   5      24.067  21.774   3.551  1.00 14.89           C  
ATOM     27  C   GLU A   5      23.038  21.717   2.439  1.00 14.44           C  
ATOM     28  O   GLU A   5      23.215  21.254   1.304  1.00 12.15           O  
ATOM     29  CB  GLU A   5      24.626  23.172   3.765  1.00 18.73           C  
ATOM     30  CG  GLU A   5      25.423  23.798   2.671  1.00 20.64           C  
ATOM     31  CD  GLU A   5      26.399  24.890   3.054  1.00 23.56           C  
ATOM     32  OE1 GLU A   5      27.215  25.227   2.161  1.00 26.36           O  
ATOM     33  OE2 GLU A   5      26.542  25.483   4.130  1.00 23.72           O  
ATOM     34  N   VAL A   6      21.840  22.157   2.842  1.00 13.88           N  
ATOM     35  CA  VAL A   6      20.733  22.443   1.944  1.00 11.77           C  
ATOM     36  C   VAL A   6      20.412  23.933   2.100  1.00 10.93           C  
ATOM     37  O   VAL A   6      19.966  24.350   3.170  1.00  9.97           O  
ATOM     38  CB  VAL A   6      19.486  21.604   2.252  1.00 13.08           C  
ATOM     39  CG1 VAL A   6      18.380  21.947   1.255  1.00 10.71           C  
ATOM     40  CG2 VAL A   6      19.816  20.109   2.299  1.00 12.48           C  
ATOM     41  N   ARG A   7      20.562  24.691   1.038  1.00  8.94           N  
ATOM     42  CA  ARG A   7      20.474  26.164   1.161  1.00 10.86           C  
ATOM     43  C   ARG A   7      19.444  26.693   0.191  1.00 10.00           C  
ATOM     44  O   ARG A   7      19.427  26.297  -0.991  1.00  9.33           O  
ATOM     45  CB  ARG A   7      21.852  26.743   0.839  1.00 14.65           C  
ATOM     46  CG  ARG A   7      22.134  28.191   1.109  1.00 20.00           C  
ATOM     47  CD  ARG A   7      23.587  28.579   0.805  1.00 22.14           C  
ATOM     48  NE  ARG A   7      24.547  28.139   1.806  1.00 24.50           N  
ATOM     49  CZ  ARG A   7      24.850  28.843   2.908  1.00 24.38           C  
ATOM     50  NH1 ARG A   7      25.715  28.387   3.811  1.00 21.30           N  
ATOM     51  NH2 ARG A   7      24.219  30.002   3.090  1.00 25.58           N  
ATOM     52  N   ASN A   8      18.605  27.605   0.635  1.00  7.41           N  
ATOM     53  CA  ASN A   8      17.605  28.279  -0.155  1.00  9.07           C  
ATOM     54  C   ASN A   8      16.545  27.350  -0.742  1.00  8.88           C  
ATOM     55  O   ASN A   8      15.948  27.617  -1.788  1.00  8.59           O  
ATOM     56  CB  ASN A   8      18.264  29.120  -1.262  1.00 11.11           C  
ATOM     57  CG  ASN A   8      19.097  30.254  -0.717  1.00 13.28           C  
ATOM     58  OD1 ASN A   8      20.088  30.725  -1.318  1.00 16.84           O  
ATOM     59  ND2 ASN A   8      18.754  30.754   0.449  1.00 11.42           N  
ATOM     60  N   ILE A   9      16.365  26.186  -0.146  1.00  6.92           N  
ATOM     61  CA  ILE A   9      15.113  25.458  -0.369  1.00 10.83           C  
ATOM     62  C   ILE A   9      14.287  25.595   0.912  1.00 10.69           C  
ATOM     63  O   ILE A   9      14.594  24.939   1.928  1.00 11.56           O  
ATOM     64  CB  ILE A   9      15.362  23.976  -0.683  1.00 11.90           C  
ATOM     65  CG1 ILE A   9      16.341  23.819  -1.877  1.00 10.10           C  
ATOM     66  CG2 ILE A   9      14.035  23.265  -0.958  1.00  9.86           C  
ATOM     67  CD1 ILE A   9      16.765  22.386  -2.082  1.00 11.18           C  
ATOM     68  N   PRO A  10      13.299  26.472   0.891  1.00  9.47           N  
ATOM     69  CA  PRO A  10      12.673  26.906   2.134  1.00  9.51           C  
ATOM     70  C   PRO A  10      12.138  25.720   2.910  1.00 10.21           C  
ATOM     71  O   PRO A  10      11.377  24.916   2.387  1.00 10.55           O  
ATOM     72  CB  PRO A  10      11.570  27.866   1.702  1.00 10.32           C  
ATOM     73  CG  PRO A  10      12.051  28.390   0.364  1.00  9.65           C  
ATOM     74  CD  PRO A  10      12.814  27.253  -0.257  1.00  9.52           C  
ATOM     75  N   PHE A  11      12.479  25.637   4.190  1.00 10.05           N  
ATOM     76  CA  PHE A  11      11.941  24.609   5.079  1.00  9.87           C  
ATOM     77  C   PHE A  11      10.802  25.289   5.848  1.00 10.37           C  
ATOM     78  O   PHE A  11      11.154  26.092   6.721  1.00  8.94           O  
ATOM     79  CB  PHE A  11      13.039  24.086   6.003  1.00  9.40           C  
ATOM     80  CG  PHE A  11      12.626  23.095   7.065  1.00  8.20           C  
ATOM     81  CD1 PHE A  11      11.470  22.335   6.987  1.00  7.36           C  
ATOM     82  CD2 PHE A  11      13.409  22.937   8.192  1.00  7.73           C  
ATOM     83  CE1 PHE A  11      11.103  21.458   7.987  1.00  7.76           C  
ATOM     84  CE2 PHE A  11      13.071  22.066   9.212  1.00  5.26           C  
ATOM     85  CZ  PHE A  11      11.935  21.325   9.099  1.00  5.88           C  
ATOM     86  N   LYS A  12       9.581  25.074   5.421  1.00  8.41           N  
ATOM     87  CA  LYS A  12       8.439  25.905   5.798  1.00 14.03           C  
ATOM     88  C   LYS A  12       7.527  25.172   6.782  1.00 13.21           C  
ATOM     89  O   LYS A  12       7.686  23.983   6.968  1.00 10.92           O  
ATOM     90  CB  LYS A  12       7.548  26.200   4.550  1.00 14.81           C  
ATOM     91  CG  LYS A  12       8.342  27.091   3.591  1.00 18.81           C  
ATOM     92  CD  LYS A  12       7.519  27.599   2.435  1.00 23.88           C  
ATOM     93  CE  LYS A  12       8.270  28.693   1.664  1.00 29.25           C  
ATOM     94  NZ  LYS A  12       8.874  29.758   2.540  1.00 31.20           N  
ATOM     95  N   LEU A  13       6.618  25.896   7.440  1.00 15.41           N  
ATOM     96  CA  LEU A  13       5.696  25.265   8.364  1.00 17.48           C  
ATOM     97  C   LEU A  13       4.937  24.154   7.645  1.00 16.99           C  
ATOM     98  O   LEU A  13       4.456  24.402   6.542  1.00 15.41           O  
ATOM     99  CB  LEU A  13       4.601  26.240   8.842  1.00 20.34           C  
ATOM    100  CG  LEU A  13       5.088  27.450   9.625  1.00 21.47           C  
ATOM    101  CD1 LEU A  13       3.964  28.504   9.665  1.00 22.21           C  
ATOM    102  CD2 LEU A  13       5.448  27.035  11.034  1.00 21.96           C  
ATOM    103  N   GLY A  14       4.938  22.971   8.252  1.00 17.16           N  
ATOM    104  CA  GLY A  14       4.116  21.891   7.681  1.00 17.95           C  
ATOM    105  C   GLY A  14       4.940  20.990   6.762  1.00 16.64           C  
ATOM    106  O   GLY A  14       4.430  19.943   6.307  1.00 19.10           O  
ATOM    107  N   MET A  15       6.179  21.394   6.502  1.00 11.26           N  
ATOM    108  CA  MET A  15       7.077  20.482   5.783  1.00 10.08           C  
ATOM    109  C   MET A  15       7.780  19.567   6.768  1.00 10.67           C  
ATOM    110  O   MET A  15       7.882  19.807   7.959  1.00  9.58           O  
ATOM    111  CB  MET A  15       8.093  21.289   4.962  1.00  8.97           C  
ATOM    112  CG  MET A  15       7.331  21.958   3.779  1.00  6.54           C  
ATOM    113  SD  MET A  15       8.507  23.027   2.943  1.00  5.90           S  
ATOM    114  CE  MET A  15       9.597  21.769   2.262  1.00  5.64           C  
ATOM    115  N   SER A  16       8.416  18.533   6.260  1.00  9.46           N  
ATOM    116  CA  SER A  16       9.240  17.656   7.067  1.00 12.37           C  
ATOM    117  C   SER A  16      10.648  17.586   6.504  1.00 10.97           C  
ATOM    118  O   SER A  16      10.821  17.543   5.295  1.00 10.04           O  
ATOM    119  CB  SER A  16       8.560  16.254   6.971  1.00 13.52           C  
ATOM    120  OG  SER A  16       9.237  15.443   7.879  1.00 20.03           O  
ATOM    121  N   LEU A  17      11.627  17.497   7.374  1.00 11.36           N  
ATOM    122  CA  LEU A  17      13.032  17.386   6.967  1.00 10.73           C  
ATOM    123  C   LEU A  17      13.511  16.051   7.539  1.00 12.15           C  
ATOM    124  O   LEU A  17      13.542  15.900   8.783  1.00 11.80           O  
ATOM    125  CB  LEU A  17      13.866  18.548   7.541  1.00  9.57           C  
ATOM    126  CG  LEU A  17      15.387  18.365   7.513  1.00 10.88           C  
ATOM    127  CD1 LEU A  17      15.904  18.338   6.081  1.00  8.53           C  
ATOM    128  CD2 LEU A  17      16.120  19.466   8.312  1.00 11.41           C  
ATOM    129  N   THR A  18      13.833  15.085   6.696  1.00 11.22           N  
ATOM    130  CA  THR A  18      14.490  13.853   7.154  1.00 10.16           C  
ATOM    131  C   THR A  18      15.920  13.798   6.610  1.00 11.69           C  
ATOM    132  O   THR A  18      16.129  13.957   5.406  1.00 11.21           O  
ATOM    133  CB  THR A  18      13.723  12.589   6.736  1.00 10.91           C  
ATOM    134  OG1 THR A  18      12.393  12.726   7.267  1.00 11.10           O  
ATOM    135  CG2 THR A  18      14.385  11.346   7.334  1.00  8.84           C  
ATOM    136  N   VAL A  19      16.915  13.674   7.498  1.00 10.80           N  
ATOM    137  CA  VAL A  19      18.296  13.559   7.143  1.00 11.59           C  
ATOM    138  C   VAL A  19      18.816  12.195   7.654  1.00 13.99           C  
ATOM    139  O   VAL A  19      18.516  11.805   8.770  1.00 12.76           O  
ATOM    140  CB  VAL A  19      19.209  14.690   7.616  1.00 11.96           C  
ATOM    141  CG1 VAL A  19      18.773  16.034   6.988  1.00 11.73           C  
ATOM    142  CG2 VAL A  19      19.279  14.791   9.131  1.00 11.12           C  
ATOM    143  N   GLY A  20      19.576  11.508   6.810  1.00 12.87           N  
ATOM    144  CA  GLY A  20      20.271  10.285   7.218  1.00 11.28           C  
ATOM    145  C   GLY A  20      21.773  10.523   7.085  1.00 11.97           C  
ATOM    146  O   GLY A  20      22.142  11.310   6.189  1.00 11.49           O  
ATOM    147  N   GLY A  21      22.574   9.923   7.955  1.00 10.18           N  
ATOM    148  CA  GLY A  21      24.028   9.923   7.694  1.00 12.27           C  
ATOM    149  C   GLY A  21      24.732   8.861   8.524  1.00 11.75           C  
ATOM    150  O   GLY A  21      24.170   7.874   9.016  1.00 11.70           O  
ATOM    151  N   VAL A  22      26.036   9.090   8.743  1.00 10.39           N  
ATOM    152  CA  VAL A  22      26.923   8.128   9.377  1.00 11.09           C  
ATOM    153  C   VAL A  22      27.806   8.923  10.352  1.00  8.38           C  
ATOM    154  O   VAL A  22      28.417   9.892   9.916  1.00  8.66           O  
ATOM    155  CB  VAL A  22      27.850   7.341   8.421  1.00 10.77           C  
ATOM    156  CG1 VAL A  22      28.689   6.316   9.172  1.00 11.92           C  
ATOM    157  CG2 VAL A  22      27.088   6.568   7.357  1.00 12.24           C  
ATOM    158  N   VAL A  23      27.854   8.590  11.606  1.00  9.26           N  
ATOM    159  CA  VAL A  23      28.793   9.228  12.552  1.00  9.77           C  
ATOM    160  C   VAL A  23      30.238   8.768  12.337  1.00 11.08           C  
ATOM    161  O   VAL A  23      30.444   7.548  12.134  1.00  8.37           O  
ATOM    162  CB  VAL A  23      28.353   8.808  13.971  1.00 10.37           C  
ATOM    163  CG1 VAL A  23      29.152   9.650  14.969  1.00  7.88           C  
ATOM    164  CG2 VAL A  23      26.841   9.052  14.095  1.00  8.47           C  
ATOM    165  N   ASN A  24      31.231   9.658  12.335  1.00  8.09           N  
ATOM    166  CA  ASN A  24      32.608   9.208  12.163  1.00 10.75           C  
ATOM    167  C   ASN A  24      33.021   8.270  13.283  1.00 10.98           C  
ATOM    168  O   ASN A  24      32.514   8.416  14.399  1.00 10.62           O  
ATOM    169  CB  ASN A  24      33.625  10.358  12.216  1.00 10.84           C  
ATOM    170  CG  ASN A  24      33.496  11.391  11.131  1.00 12.51           C  
ATOM    171  OD1 ASN A  24      34.202  12.421  11.135  1.00 15.44           O  
ATOM    172  ND2 ASN A  24      32.590  11.300  10.203  1.00  8.54           N  
ATOM    173  N   SER A  25      34.023   7.427  13.058  1.00 13.17           N  
ATOM    174  CA  SER A  25      34.389   6.400  14.027  1.00 13.73           C  
ATOM    175  C   SER A  25      34.909   6.913  15.366  1.00 14.79           C  
ATOM    176  O   SER A  25      34.799   6.176  16.384  1.00 16.36           O  
ATOM    177  CB  SER A  25      35.523   5.510  13.475  1.00 15.07           C  
ATOM    178  OG  SER A  25      35.011   4.928  12.289  1.00 15.93           O  
ATOM    179  N   ASN A  26      35.670   7.995  15.262  1.00 13.32           N  
ATOM    180  CA  ASN A  26      36.235   8.589  16.492  1.00 14.81           C  
ATOM    181  C   ASN A  26      35.636   9.962  16.761  1.00 11.38           C  
ATOM    182  O   ASN A  26      36.288  10.846  17.312  1.00 13.47           O  
ATOM    183  CB  ASN A  26      37.764   8.698  16.323  1.00 15.93           C  
ATOM    184  CG  ASN A  26      38.286   7.254  16.186  1.00 19.05           C  
ATOM    185  OD1 ASN A  26      38.078   6.430  17.090  1.00 18.32           O  
ATOM    186  ND2 ASN A  26      38.868   6.978  15.037  1.00 19.13           N  
ATOM    187  N   ALA A  27      34.377  10.114  16.398  1.00  9.43           N  
ATOM    188  CA  ALA A  27      33.703  11.414  16.529  1.00  9.34           C  
ATOM    189  C   ALA A  27      33.798  12.013  17.913  1.00  9.91           C  
ATOM    190  O   ALA A  27      33.509  11.285  18.883  1.00  8.33           O  
ATOM    191  CB  ALA A  27      32.244  11.215  16.122  1.00  8.87           C  
ATOM    192  N   THR A  28      34.040  13.324  18.046  1.00 10.55           N  
ATOM    193  CA  THR A  28      33.834  14.022  19.316  1.00 10.71           C  
ATOM    194  C   THR A  28      32.389  14.516  19.436  1.00 10.48           C  
ATOM    195  O   THR A  28      31.663  14.307  20.434  1.00  8.46           O  
ATOM    196  CB  THR A  28      34.763  15.241  19.547  1.00 12.32           C  
ATOM    197  OG1 THR A  28      34.544  16.174  18.481  1.00 12.14           O  
ATOM    198  CG2 THR A  28      36.244  14.904  19.574  1.00 13.38           C  
ATOM    199  N   ARG A  29      31.957  15.185  18.366  1.00  9.76           N  
ATOM    200  CA  ARG A  29      30.580  15.700  18.327  1.00 10.36           C  
ATOM    201  C   ARG A  29      30.251  16.125  16.893  1.00  9.40           C  
ATOM    202  O   ARG A  29      31.175  16.466  16.170  1.00  8.18           O  
ATOM    203  CB  ARG A  29      30.449  16.899  19.264  1.00 10.87           C  
ATOM    204  CG  ARG A  29      31.487  17.976  18.991  1.00 13.41           C  
ATOM    205  CD  ARG A  29      31.578  19.045  20.071  1.00 16.63           C  
ATOM    206  NE  ARG A  29      30.581  20.091  20.026  1.00 17.90           N  
ATOM    207  CZ  ARG A  29      30.623  21.349  19.636  1.00 19.93           C  
ATOM    208  NH1 ARG A  29      29.577  22.176  19.656  1.00 18.11           N  
ATOM    209  NH2 ARG A  29      31.753  21.920  19.199  1.00 19.95           N  
ATOM    210  N   PHE A  30      28.979  16.117  16.534  1.00  7.82           N  
ATOM    211  CA  PHE A  30      28.523  16.634  15.237  1.00  8.11           C  
ATOM    212  C   PHE A  30      27.157  17.286  15.486  1.00  9.10           C  
ATOM    213  O   PHE A  30      26.485  16.887  16.458  1.00 10.38           O  
ATOM    214  CB  PHE A  30      28.395  15.559  14.145  1.00  7.83           C  
ATOM    215  CG  PHE A  30      27.170  14.685  14.302  1.00 10.35           C  
ATOM    216  CD1 PHE A  30      27.201  13.557  15.098  1.00 10.30           C  
ATOM    217  CD2 PHE A  30      25.981  15.018  13.636  1.00  7.65           C  
ATOM    218  CE1 PHE A  30      26.037  12.772  15.268  1.00 10.71           C  
ATOM    219  CE2 PHE A  30      24.891  14.207  13.803  1.00  9.00           C  
ATOM    220  CZ  PHE A  30      24.889  13.093  14.628  1.00  8.22           C  
ATOM    221  N   SER A  31      26.757  18.293  14.709  1.00  8.09           N  
ATOM    222  CA  SER A  31      25.439  18.900  14.924  1.00  8.50           C  
ATOM    223  C   SER A  31      24.596  18.905  13.641  1.00  7.91           C  
ATOM    224  O   SER A  31      25.154  18.852  12.537  1.00  5.79           O  
ATOM    225  CB  SER A  31      25.593  20.340  15.462  1.00  8.02           C  
ATOM    226  OG  SER A  31      26.285  21.191  14.518  1.00  5.11           O  
ATOM    227  N   ILE A  32      23.263  18.899  13.757  1.00  8.64           N  
ATOM    228  CA  ILE A  32      22.315  19.357  12.732  1.00  7.73           C  
ATOM    229  C   ILE A  32      21.813  20.739  13.113  1.00  9.17           C  
ATOM    230  O   ILE A  32      21.460  20.993  14.273  1.00  6.65           O  
ATOM    231  CB  ILE A  32      21.149  18.384  12.635  1.00  9.69           C  
ATOM    232  CG1 ILE A  32      21.596  16.918  12.712  1.00 14.32           C  
ATOM    233  CG2 ILE A  32      20.371  18.522  11.326  1.00  8.47           C  
ATOM    234  CD1 ILE A  32      22.312  16.438  11.446  1.00 17.18           C  
ATOM    235  N   ASN A  33      21.789  21.599  12.123  1.00  7.39           N  
ATOM    236  CA  ASN A  33      21.389  22.986  12.317  1.00  7.40           C  
ATOM    237  C   ASN A  33      20.358  23.443  11.288  1.00  9.03           C  
ATOM    238  O   ASN A  33      20.480  23.160  10.096  1.00  9.67           O  
ATOM    239  CB  ASN A  33      22.633  23.856  12.184  1.00  9.22           C  
ATOM    240  CG  ASN A  33      23.752  23.390  13.111  1.00 10.64           C  
ATOM    241  OD1 ASN A  33      23.820  23.841  14.250  1.00 10.39           O  
ATOM    242  ND2 ASN A  33      24.638  22.501  12.689  1.00  8.21           N  
ATOM    243  N   VAL A  34      19.367  24.143  11.808  1.00  5.80           N  
ATOM    244  CA  VAL A  34      18.283  24.733  11.005  1.00  7.81           C  
ATOM    245  C   VAL A  34      18.239  26.211  11.327  1.00  7.44           C  
ATOM    246  O   VAL A  34      18.073  26.615  12.489  1.00 10.07           O  
ATOM    247  CB  VAL A  34      16.927  24.098  11.335  1.00  6.09           C  
ATOM    248  CG1 VAL A  34      15.773  24.714  10.530  1.00  6.77           C  
ATOM    249  CG2 VAL A  34      16.879  22.597  11.047  1.00  5.91           C  
ATOM    250  N   GLY A  35      18.393  27.022  10.316  1.00  8.35           N  
ATOM    251  CA  GLY A  35      18.384  28.447  10.542  1.00  9.27           C  
ATOM    252  C   GLY A  35      18.479  29.259   9.269  1.00 10.73           C  
ATOM    253  O   GLY A  35      17.857  28.931   8.246  1.00  9.76           O  
ATOM    254  N   GLU A  36      19.272  30.282   9.425  1.00 13.19           N  
ATOM    255  CA  GLU A  36      19.500  31.299   8.426  1.00 16.45           C  
ATOM    256  C   GLU A  36      20.959  31.294   7.855  1.00 17.85           C  
ATOM    257  O   GLU A  36      21.194  31.532   6.658  1.00 17.39           O  
ATOM    258  CB  GLU A  36      19.237  32.653   9.123  1.00 21.02           C  
ATOM    259  CG  GLU A  36      17.793  32.811   9.742  1.00 25.74           C  
ATOM    260  CD  GLU A  36      17.519  32.147  11.158  1.00 29.82           C  
ATOM    261  OE1 GLU A  36      18.396  32.158  12.121  1.00 27.38           O  
ATOM    262  OE2 GLU A  36      16.382  31.574  11.397  1.00 28.52           O  
ATOM    263  N   SER A  37      21.920  31.031   8.714  1.00 14.49           N  
ATOM    264  CA  SER A  37      23.354  31.029   8.332  1.00 12.66           C  
ATOM    265  C   SER A  37      24.161  30.316   9.403  1.00 12.99           C  
ATOM    266  O   SER A  37      23.620  29.871  10.411  1.00 12.57           O  
ATOM    267  CB  SER A  37      23.845  32.469   8.221  1.00 14.06           C  
ATOM    268  OG  SER A  37      24.022  33.011   9.525  1.00 13.29           O  
ATOM    269  N   THR A  38      25.463  30.211   9.190  1.00 13.88           N  
ATOM    270  CA  THR A  38      26.324  29.530  10.173  1.00 13.62           C  
ATOM    271  C   THR A  38      26.455  30.366  11.464  1.00 14.50           C  
ATOM    272  O   THR A  38      27.034  29.919  12.458  1.00 13.21           O  
ATOM    273  CB  THR A  38      27.726  29.268   9.621  1.00 14.28           C  
ATOM    274  OG1 THR A  38      28.325  30.480   9.205  1.00 13.03           O  
ATOM    275  CG2 THR A  38      27.721  28.315   8.425  1.00 13.71           C  
ATOM    276  N   ASP A  39      25.912  31.584  11.448  1.00 13.76           N  
ATOM    277  CA  ASP A  39      25.948  32.462  12.650  1.00 13.13           C  
ATOM    278  C   ASP A  39      24.522  32.847  13.090  1.00 13.51           C  
ATOM    279  O   ASP A  39      24.315  33.743  13.910  1.00 12.57           O  
ATOM    280  CB  ASP A  39      26.722  33.761  12.397  1.00 13.97           C  
ATOM    281  CG  ASP A  39      27.156  34.441  13.710  1.00 15.10           C  
ATOM    282  OD1 ASP A  39      27.118  35.726  13.824  1.00 17.49           O  
ATOM    283  OD2 ASP A  39      27.559  33.724  14.706  1.00 15.65           O  
ATOM    284  N   SER A  40      23.563  32.158  12.536  1.00 12.37           N  
ATOM    285  CA  SER A  40      22.142  32.391  12.838  1.00  9.88           C  
ATOM    286  C   SER A  40      21.416  31.056  12.725  1.00 10.51           C  
ATOM    287  O   SER A  40      20.991  30.656  11.639  1.00  8.30           O  
ATOM    288  CB  SER A  40      21.586  33.408  11.830  1.00 10.00           C  
ATOM    289  OG  SER A  40      20.317  33.882  12.246  1.00  9.38           O  
ATOM    290  N   ILE A  41      21.293  30.391  13.863  1.00  9.41           N  
ATOM    291  CA  ILE A  41      20.662  29.061  13.928  1.00  9.38           C  
ATOM    292  C   ILE A  41      19.504  29.043  14.937  1.00  9.74           C  
ATOM    293  O   ILE A  41      19.665  29.391  16.113  1.00  9.19           O  
ATOM    294  CB  ILE A  41      21.730  28.036  14.339  1.00  9.50           C  
ATOM    295  CG1 ILE A  41      23.018  28.172  13.496  1.00 10.41           C  
ATOM    296  CG2 ILE A  41      21.257  26.589  14.181  1.00  7.10           C  
ATOM    297  CD1 ILE A  41      24.179  27.298  13.987  1.00 12.91           C  
ATOM    298  N   ALA A  42      18.324  28.685  14.395  1.00  8.70           N  
ATOM    299  CA  ALA A  42      17.135  28.675  15.239  1.00  8.12           C  
ATOM    300  C   ALA A  42      17.064  27.363  16.003  1.00  7.80           C  
ATOM    301  O   ALA A  42      16.599  27.334  17.147  1.00  6.63           O  
ATOM    302  CB  ALA A  42      15.887  28.859  14.356  1.00  9.47           C  
ATOM    303  N   MET A  43      17.609  26.275  15.436  1.00  7.49           N  
ATOM    304  CA  MET A  43      17.581  24.990  16.165  1.00  9.68           C  
ATOM    305  C   MET A  43      18.937  24.325  15.911  1.00  9.75           C  
ATOM    306  O   MET A  43      19.195  23.888  14.786  1.00 11.42           O  
ATOM    307  CB  MET A  43      16.447  24.037  15.764  1.00  7.07           C  
ATOM    308  CG  MET A  43      16.200  22.898  16.777  1.00  9.55           C  
ATOM    309  SD  MET A  43      17.514  21.660  16.786  1.00  7.15           S  
ATOM    310  CE  MET A  43      17.476  21.145  15.076  1.00  5.25           C  
ATOM    311  N   HIS A  44      19.794  24.362  16.906  1.00  9.02           N  
ATOM    312  CA  HIS A  44      21.046  23.587  16.845  1.00  8.99           C  
ATOM    313  C   HIS A  44      20.947  22.325  17.677  1.00  9.14           C  
ATOM    314  O   HIS A  44      20.588  22.471  18.861  1.00  6.68           O  
ATOM    315  CB  HIS A  44      22.102  24.557  17.400  1.00  9.36           C  
ATOM    316  CG  HIS A  44      23.412  23.915  17.741  1.00  9.54           C  
ATOM    317  ND1 HIS A  44      24.303  23.518  16.782  1.00  7.60           N  
ATOM    318  CD2 HIS A  44      23.928  23.585  18.957  1.00 10.84           C  
ATOM    319  CE1 HIS A  44      25.359  23.013  17.427  1.00 11.80           C  
ATOM    320  NE2 HIS A  44      25.162  23.012  18.729  1.00  9.81           N  
ATOM    321  N   MET A  45      21.194  21.126  17.139  1.00  7.98           N  
ATOM    322  CA  MET A  45      21.163  19.945  17.996  1.00  9.52           C  
ATOM    323  C   MET A  45      22.531  19.280  17.911  1.00 11.56           C  
ATOM    324  O   MET A  45      22.969  18.834  16.845  1.00  9.07           O  
ATOM    325  CB  MET A  45      20.072  18.953  17.598  1.00 12.23           C  
ATOM    326  CG  MET A  45      20.044  17.764  18.570  1.00 13.77           C  
ATOM    327  SD  MET A  45      18.638  16.641  18.441  1.00 13.71           S  
ATOM    328  CE  MET A  45      18.890  16.021  16.773  1.00 13.60           C  
ATOM    329  N   ASP A  46      23.247  19.277  19.031  1.00 10.11           N  
ATOM    330  CA  ASP A  46      24.641  18.892  19.082  1.00 10.41           C  
ATOM    331  C   ASP A  46      24.701  17.488  19.668  1.00 10.02           C  
ATOM    332  O   ASP A  46      24.006  17.175  20.640  1.00 11.51           O  
ATOM    333  CB  ASP A  46      25.502  19.926  19.843  1.00 10.02           C  
ATOM    334  CG  ASP A  46      26.981  19.704  19.619  1.00 13.54           C  
ATOM    335  OD1 ASP A  46      27.395  19.123  18.578  1.00 14.10           O  
ATOM    336  OD2 ASP A  46      27.814  20.071  20.503  1.00 14.34           O  
ATOM    337  N   HIS A  47      25.454  16.588  19.043  1.00  8.63           N  
ATOM    338  CA  HIS A  47      25.484  15.181  19.413  1.00  9.26           C  
ATOM    339  C   HIS A  47      26.871  14.940  20.022  1.00  9.55           C  
ATOM    340  O   HIS A  47      27.845  14.926  19.282  1.00 10.47           O  
ATOM    341  CB  HIS A  47      25.237  14.273  18.191  1.00  9.63           C  
ATOM    342  CG  HIS A  47      23.941  14.416  17.472  1.00  9.55           C  
ATOM    343  ND1 HIS A  47      23.615  15.475  16.648  1.00 10.85           N  
ATOM    344  CD2 HIS A  47      22.894  13.552  17.369  1.00 10.56           C  
ATOM    345  CE1 HIS A  47      22.415  15.277  16.104  1.00 10.40           C  
ATOM    346  NE2 HIS A  47      21.939  14.110  16.526  1.00 11.19           N  
ATOM    347  N   ARG A  48      26.997  14.911  21.339  1.00  9.69           N  
ATOM    348  CA  ARG A  48      28.264  14.956  22.046  1.00 10.00           C  
ATOM    349  C   ARG A  48      28.664  13.568  22.531  1.00 12.36           C  
ATOM    350  O   ARG A  48      28.089  12.993  23.461  1.00 10.99           O  
ATOM    351  CB  ARG A  48      28.161  15.946  23.247  1.00 10.07           C  
ATOM    352  CG  ARG A  48      28.002  17.376  22.700  1.00  8.39           C  
ATOM    353  CD  ARG A  48      27.865  18.400  23.820  1.00  9.45           C  
ATOM    354  NE  ARG A  48      27.695  19.738  23.186  1.00  9.35           N  
ATOM    355  CZ  ARG A  48      27.828  20.859  23.890  1.00 11.01           C  
ATOM    356  NH1 ARG A  48      28.116  20.776  25.195  1.00 13.37           N  
ATOM    357  NH2 ARG A  48      27.695  22.069  23.358  1.00 11.20           N  
ATOM    358  N   PHE A  49      29.589  12.978  21.769  1.00 13.38           N  
ATOM    359  CA  PHE A  49      30.114  11.669  22.137  1.00 13.87           C  
ATOM    360  C   PHE A  49      31.122  11.923  23.253  1.00 16.32           C  
ATOM    361  O   PHE A  49      30.986  11.301  24.310  1.00 16.59           O  
ATOM    362  CB  PHE A  49      30.726  10.897  20.967  1.00 13.51           C  
ATOM    363  CG  PHE A  49      29.663  10.595  19.926  1.00 13.41           C  
ATOM    364  CD1 PHE A  49      29.371  11.547  18.967  1.00 13.65           C  
ATOM    365  CD2 PHE A  49      28.950   9.405  19.954  1.00 12.55           C  
ATOM    366  CE1 PHE A  49      28.368  11.309  18.019  1.00 14.61           C  
ATOM    367  CE2 PHE A  49      27.973   9.158  19.017  1.00 12.83           C  
ATOM    368  CZ  PHE A  49      27.668  10.113  18.059  1.00 14.31           C  
ATOM    369  N   SER A  50      32.036  12.885  23.043  1.00 17.02           N  
ATOM    370  CA  SER A  50      32.906  13.271  24.160  1.00 17.89           C  
ATOM    371  C   SER A  50      33.302  14.727  24.050  1.00 17.74           C  
ATOM    372  O   SER A  50      33.978  15.065  23.075  1.00 16.71           O  
ATOM    373  CB  SER A  50      34.119  12.341  24.221  1.00 20.27           C  
ATOM    374  OG  SER A  50      34.946  12.662  25.345  1.00 23.27           O  
ATOM    375  N   TYR A  51      32.882  15.552  25.009  1.00 16.78           N  
ATOM    376  CA  TYR A  51      33.052  17.004  24.851  1.00 18.16           C  
ATOM    377  C   TYR A  51      33.039  17.642  26.229  1.00 19.57           C  
ATOM    378  O   TYR A  51      31.972  17.807  26.831  1.00 19.60           O  
ATOM    379  CB  TYR A  51      31.920  17.623  24.010  1.00 17.12           C  
ATOM    380  CG  TYR A  51      32.070  19.104  23.709  1.00 18.45           C  
ATOM    381  CD1 TYR A  51      33.185  19.573  23.023  1.00 17.83           C  
ATOM    382  CD2 TYR A  51      31.123  20.037  24.116  1.00 18.35           C  
ATOM    383  CE1 TYR A  51      33.368  20.907  22.732  1.00 17.84           C  
ATOM    384  CE2 TYR A  51      31.277  21.392  23.856  1.00 18.04           C  
ATOM    385  CZ  TYR A  51      32.394  21.797  23.148  1.00 19.52           C  
ATOM    386  OH  TYR A  51      32.556  23.128  22.858  1.00 18.81           O  
ATOM    387  N   GLY A  52      34.199  17.961  26.779  1.00 22.02           N  
ATOM    388  CA  GLY A  52      34.331  18.428  28.153  1.00 23.59           C  
ATOM    389  C   GLY A  52      33.886  17.312  29.107  1.00 25.36           C  
ATOM    390  O   GLY A  52      34.271  16.159  28.970  1.00 27.57           O  
ATOM    391  N   ALA A  53      32.961  17.626  29.978  1.00 26.02           N  
ATOM    392  CA  ALA A  53      32.215  16.706  30.799  1.00 27.31           C  
ATOM    393  C   ALA A  53      31.064  15.998  30.075  1.00 28.62           C  
ATOM    394  O   ALA A  53      30.361  15.249  30.761  1.00 29.17           O  
ATOM    395  CB  ALA A  53      31.501  17.510  31.895  1.00 27.06           C  
ATOM    396  N   ASP A  54      30.812  16.346  28.813  1.00 26.61           N  
ATOM    397  CA  ASP A  54      29.608  15.884  28.141  1.00 25.06           C  
ATOM    398  C   ASP A  54      29.926  14.598  27.389  1.00 23.01           C  
ATOM    399  O   ASP A  54      30.732  14.605  26.469  1.00 21.00           O  
ATOM    400  CB  ASP A  54      29.127  16.949  27.152  1.00 24.52           C  
ATOM    401  CG  ASP A  54      28.442  18.101  27.851  1.00 25.22           C  
ATOM    402  OD1 ASP A  54      27.903  17.892  28.965  1.00 27.21           O  
ATOM    403  OD2 ASP A  54      28.378  19.220  27.324  1.00 25.31           O  
ATOM    404  N   GLN A  55      29.306  13.501  27.814  1.00 22.80           N  
ATOM    405  CA  GLN A  55      29.440  12.221  27.150  1.00 22.44           C  
ATOM    406  C   GLN A  55      28.073  11.598  26.849  1.00 20.36           C  
ATOM    407  O   GLN A  55      27.257  11.401  27.766  1.00 15.73           O  
ATOM    408  CB  GLN A  55      30.190  11.197  28.003  1.00 28.03           C  
ATOM    409  CG  GLN A  55      31.264  11.741  28.964  1.00 32.64           C  
ATOM    410  CD  GLN A  55      32.480  12.061  28.110  1.00 34.80           C  
ATOM    411  OE1 GLN A  55      32.652  11.210  27.224  1.00 38.05           O  
ATOM    412  NE2 GLN A  55      33.199  13.144  28.350  1.00 35.17           N  
ATOM    413  N   ASN A  56      27.896  11.246  25.563  1.00 16.41           N  
ATOM    414  CA  ASN A  56      26.626  10.686  25.145  1.00 18.50           C  
ATOM    415  C   ASN A  56      25.470  11.572  25.556  1.00 17.47           C  
ATOM    416  O   ASN A  56      24.502  11.137  26.168  1.00 17.79           O  
ATOM    417  CB  ASN A  56      26.497   9.257  25.705  1.00 21.05           C  
ATOM    418  CG  ASN A  56      27.483   8.331  25.002  1.00 25.56           C  
ATOM    419  OD1 ASN A  56      28.428   8.699  24.300  1.00 26.94           O  
ATOM    420  ND2 ASN A  56      27.260   7.020  25.181  1.00 28.92           N  
ATOM    421  N   VAL A  57      25.519  12.856  25.207  1.00 16.52           N  
ATOM    422  CA  VAL A  57      24.407  13.767  25.583  1.00 15.76           C  
ATOM    423  C   VAL A  57      24.018  14.570  24.358  1.00 12.40           C  
ATOM    424  O   VAL A  57      24.892  14.813  23.526  1.00  8.87           O  
ATOM    425  CB  VAL A  57      24.790  14.603  26.801  1.00 16.93           C  
ATOM    426  CG1 VAL A  57      26.185  15.200  26.652  1.00 17.92           C  
ATOM    427  CG2 VAL A  57      23.814  15.733  27.115  1.00 19.26           C  
ATOM    428  N   LEU A  58      22.731  14.890  24.207  1.00 11.82           N  
ATOM    429  CA  LEU A  58      22.345  15.844  23.170  1.00 11.44           C  
ATOM    430  C   LEU A  58      22.290  17.248  23.743  1.00 10.46           C  
ATOM    431  O   LEU A  58      21.685  17.376  24.816  1.00 12.20           O  
ATOM    432  CB  LEU A  58      20.967  15.506  22.634  1.00 12.34           C  
ATOM    433  CG  LEU A  58      20.777  14.256  21.766  1.00 13.51           C  
ATOM    434  CD1 LEU A  58      19.297  14.169  21.368  1.00 13.32           C  
ATOM    435  CD2 LEU A  58      21.707  14.348  20.570  1.00 12.16           C  
ATOM    436  N   VAL A  59      22.856  18.279  23.166  1.00 10.63           N  
ATOM    437  CA  VAL A  59      22.708  19.654  23.672  1.00 11.24           C  
ATOM    438  C   VAL A  59      22.014  20.489  22.601  1.00 12.15           C  
ATOM    439  O   VAL A  59      22.445  20.428  21.434  1.00 12.44           O  
ATOM    440  CB  VAL A  59      24.080  20.273  23.961  1.00 12.99           C  
ATOM    441  CG1 VAL A  59      23.957  21.752  24.294  1.00 13.60           C  
ATOM    442  CG2 VAL A  59      24.772  19.491  25.067  1.00 11.58           C  
ATOM    443  N   LEU A  60      20.907  21.146  22.906  1.00 11.29           N  
ATOM    444  CA  LEU A  60      20.156  21.931  21.939  1.00 12.58           C  
ATOM    445  C   LEU A  60      20.120  23.422  22.270  1.00 13.25           C  
ATOM    446  O   LEU A  60      20.027  23.745  23.477  1.00 11.60           O  
ATOM    447  CB  LEU A  60      18.703  21.433  21.863  1.00 13.31           C  
ATOM    448  CG  LEU A  60      18.521  20.067  21.167  1.00 13.66           C  
ATOM    449  CD1 LEU A  60      18.542  18.982  22.256  1.00 12.97           C  
ATOM    450  CD2 LEU A  60      17.202  20.064  20.423  1.00 13.63           C  
ATOM    451  N   ASN A  61      20.222  24.267  21.230  1.00 11.23           N  
ATOM    452  CA  ASN A  61      20.303  25.707  21.570  1.00 10.74           C  
ATOM    453  C   ASN A  61      20.040  26.518  20.296  1.00 11.46           C  
ATOM    454  O   ASN A  61      19.879  25.937  19.206  1.00 10.80           O  
ATOM    455  CB  ASN A  61      21.663  26.059  22.184  1.00 10.67           C  
ATOM    456  CG  ASN A  61      21.684  27.331  23.030  1.00 10.77           C  
ATOM    457  OD1 ASN A  61      20.686  28.074  23.072  1.00 10.89           O  
ATOM    458  ND2 ASN A  61      22.785  27.619  23.706  1.00  8.99           N  
ATOM    459  N   SER A  62      19.963  27.835  20.453  1.00 10.10           N  
ATOM    460  CA  SER A  62      19.852  28.728  19.301  1.00  9.23           C  
ATOM    461  C   SER A  62      21.040  29.671  19.330  1.00  9.85           C  
ATOM    462  O   SER A  62      21.625  29.966  20.384  1.00  7.61           O  
ATOM    463  CB  SER A  62      18.531  29.526  19.325  1.00 10.03           C  
ATOM    464  OG  SER A  62      18.397  30.209  20.577  1.00  6.82           O  
ATOM    465  N   LEU A  63      21.361  30.190  18.164  1.00 10.22           N  
ATOM    466  CA  LEU A  63      22.519  31.021  17.948  1.00 11.85           C  
ATOM    467  C   LEU A  63      22.039  32.286  17.228  1.00 12.26           C  
ATOM    468  O   LEU A  63      21.447  32.188  16.143  1.00 11.75           O  
ATOM    469  CB  LEU A  63      23.619  30.317  17.156  1.00 11.39           C  
ATOM    470  CG  LEU A  63      24.750  31.238  16.664  1.00 12.30           C  
ATOM    471  CD1 LEU A  63      25.540  31.767  17.848  1.00 12.56           C  
ATOM    472  CD2 LEU A  63      25.659  30.419  15.720  1.00 12.71           C  
ATOM    473  N   VAL A  64      22.303  33.420  17.862  1.00 11.67           N  
ATOM    474  CA  VAL A  64      21.829  34.706  17.324  1.00 11.32           C  
ATOM    475  C   VAL A  64      23.034  35.433  16.739  1.00 13.62           C  
ATOM    476  O   VAL A  64      24.078  35.555  17.348  1.00 14.35           O  
ATOM    477  CB  VAL A  64      21.197  35.568  18.419  1.00 12.04           C  
ATOM    478  CG1 VAL A  64      20.862  36.994  18.006  1.00  9.90           C  
ATOM    479  CG2 VAL A  64      19.968  34.821  18.935  1.00 11.42           C  
ATOM    480  N   HIS A  65      22.876  35.930  15.551  1.00 13.88           N  
ATOM    481  CA  HIS A  65      23.938  36.537  14.771  1.00 16.21           C  
ATOM    482  C   HIS A  65      24.597  37.677  15.498  1.00 14.69           C  
ATOM    483  O   HIS A  65      23.873  38.555  15.977  1.00 13.17           O  
ATOM    484  CB  HIS A  65      23.234  36.999  13.473  1.00 20.15           C  
ATOM    485  CG  HIS A  65      24.216  37.802  12.682  1.00 23.56           C  
ATOM    486  ND1 HIS A  65      25.501  37.342  12.495  1.00 25.42           N  
ATOM    487  CD2 HIS A  65      24.117  38.981  12.055  1.00 26.24           C  
ATOM    488  CE1 HIS A  65      26.177  38.229  11.776  1.00 27.47           C  
ATOM    489  NE2 HIS A  65      25.364  39.228  11.494  1.00 27.12           N  
ATOM    490  N   ASN A  66      25.907  37.704  15.686  1.00 12.84           N  
ATOM    491  CA  ASN A  66      26.558  38.809  16.358  1.00 14.53           C  
ATOM    492  C   ASN A  66      26.106  38.994  17.804  1.00 14.74           C  
ATOM    493  O   ASN A  66      26.356  40.062  18.403  1.00 14.21           O  
ATOM    494  CB  ASN A  66      26.414  40.138  15.592  1.00 15.51           C  
ATOM    495  CG  ASN A  66      27.528  41.138  15.922  1.00 15.30           C  
ATOM    496  OD1 ASN A  66      27.285  42.364  16.065  1.00 17.32           O  
ATOM    497  ND2 ASN A  66      28.760  40.670  16.052  1.00 10.21           N  
ATOM    498  N   VAL A  67      25.544  37.966  18.420  1.00 12.76           N  
ATOM    499  CA  VAL A  67      25.117  37.945  19.815  1.00 12.06           C  
ATOM    500  C   VAL A  67      25.713  36.706  20.487  1.00 13.86           C  
ATOM    501  O   VAL A  67      26.456  36.870  21.482  1.00 14.38           O  
ATOM    502  CB  VAL A  67      23.601  37.962  20.029  1.00  9.69           C  
ATOM    503  CG1 VAL A  67      23.168  37.584  21.452  1.00  9.57           C  
ATOM    504  CG2 VAL A  67      23.006  39.312  19.682  1.00 10.74           C  
ATOM    505  N   GLY A  68      25.411  35.504  19.981  1.00 13.38           N  
ATOM    506  CA  GLY A  68      25.871  34.281  20.630  1.00 13.94           C  
ATOM    507  C   GLY A  68      24.776  33.251  20.947  1.00 14.57           C  
ATOM    508  O   GLY A  68      23.624  33.291  20.513  1.00 11.90           O  
ATOM    509  N   TRP A  69      25.234  32.175  21.628  1.00 12.80           N  
ATOM    510  CA  TRP A  69      24.344  31.088  22.033  1.00 11.32           C  
ATOM    511  C   TRP A  69      23.436  31.537  23.158  1.00 12.28           C  
ATOM    512  O   TRP A  69      23.860  32.275  24.074  1.00 10.71           O  
ATOM    513  CB  TRP A  69      25.241  29.929  22.472  1.00 11.76           C  
ATOM    514  CG  TRP A  69      26.027  29.383  21.295  1.00 11.79           C  
ATOM    515  CD1 TRP A  69      27.347  29.597  21.000  1.00 11.85           C  
ATOM    516  CD2 TRP A  69      25.498  28.516  20.276  1.00 11.58           C  
ATOM    517  NE1 TRP A  69      27.667  28.909  19.847  1.00 10.81           N  
ATOM    518  CE2 TRP A  69      26.547  28.242  19.392  1.00 11.49           C  
ATOM    519  CE3 TRP A  69      24.224  27.986  20.013  1.00 11.81           C  
ATOM    520  CZ2 TRP A  69      26.367  27.453  18.255  1.00 11.70           C  
ATOM    521  CZ3 TRP A  69      24.038  27.165  18.900  1.00 11.91           C  
ATOM    522  CH2 TRP A  69      25.104  26.929  18.031  1.00 11.28           C  
ATOM    523  N   GLN A  70      22.179  31.107  23.124  1.00 11.12           N  
ATOM    524  CA  GLN A  70      21.183  31.451  24.122  1.00 11.04           C  
ATOM    525  C   GLN A  70      21.109  30.406  25.221  1.00 11.46           C  
ATOM    526  O   GLN A  70      22.137  29.768  25.449  1.00 12.55           O  
ATOM    527  CB  GLN A  70      19.850  31.616  23.361  1.00  9.83           C  
ATOM    528  CG  GLN A  70      20.013  32.743  22.304  1.00  7.88           C  
ATOM    529  CD  GLN A  70      20.484  34.023  22.981  1.00  7.96           C  
ATOM    530  OE1 GLN A  70      19.881  34.548  23.888  1.00  8.89           O  
ATOM    531  NE2 GLN A  70      21.583  34.620  22.565  1.00  6.03           N  
ATOM    532  N   GLN A  71      19.964  30.095  25.789  1.00 12.73           N  
ATOM    533  CA  GLN A  71      19.909  29.069  26.838  1.00 16.99           C  
ATOM    534  C   GLN A  71      20.004  27.632  26.308  1.00 15.80           C  
ATOM    535  O   GLN A  71      19.097  27.229  25.551  1.00 15.78           O  
ATOM    536  CB  GLN A  71      18.613  29.213  27.623  1.00 20.09           C  
ATOM    537  CG  GLN A  71      18.413  28.195  28.731  1.00 26.98           C  
ATOM    538  CD  GLN A  71      19.326  28.520  29.906  1.00 32.71           C  
ATOM    539  OE1 GLN A  71      20.341  27.819  30.045  1.00 36.81           O  
ATOM    540  NE2 GLN A  71      19.016  29.530  30.721  1.00 34.40           N  
ATOM    541  N   GLU A  72      20.930  26.817  26.799  1.00 13.72           N  
ATOM    542  CA  GLU A  72      21.015  25.430  26.331  1.00 16.41           C  
ATOM    543  C   GLU A  72      19.953  24.523  26.949  1.00 16.85           C  
ATOM    544  O   GLU A  72      19.635  24.747  28.114  1.00 16.96           O  
ATOM    545  CB  GLU A  72      22.292  24.662  26.688  1.00 16.62           C  
ATOM    546  CG  GLU A  72      23.491  25.113  25.896  1.00 20.19           C  
ATOM    547  CD  GLU A  72      24.757  24.426  26.390  1.00 19.92           C  
ATOM    548  OE1 GLU A  72      24.723  23.813  27.477  1.00 20.73           O  
ATOM    549  OE2 GLU A  72      25.735  24.540  25.641  1.00 19.29           O  
ATOM    550  N   GLU A  73      19.538  23.553  26.185  1.00 15.81           N  
ATOM    551  CA  GLU A  73      18.651  22.496  26.689  1.00 16.78           C  
ATOM    552  C   GLU A  73      19.372  21.172  26.501  1.00 16.31           C  
ATOM    553  O   GLU A  73      20.237  21.089  25.619  1.00 15.83           O  
ATOM    554  CB  GLU A  73      17.340  22.516  25.906  1.00 19.40           C  
ATOM    555  CG  GLU A  73      16.456  23.716  26.207  1.00 23.56           C  
ATOM    556  CD  GLU A  73      15.001  23.601  25.843  1.00 27.32           C  
ATOM    557  OE1 GLU A  73      14.341  24.681  25.904  1.00 30.74           O  
ATOM    558  OE2 GLU A  73      14.414  22.539  25.503  1.00 28.37           O  
ATOM    559  N   ARG A  74      19.146  20.162  27.317  1.00 16.45           N  
ATOM    560  CA  ARG A  74      19.889  18.915  27.126  1.00 18.94           C  
ATOM    561  C   ARG A  74      18.915  17.739  27.171  1.00 17.36           C  
ATOM    562  O   ARG A  74      17.892  17.902  27.822  1.00 14.17           O  
ATOM    563  CB  ARG A  74      20.986  18.651  28.135  1.00 21.26           C  
ATOM    564  CG  ARG A  74      22.183  19.566  28.108  1.00 24.86           C  
ATOM    565  CD  ARG A  74      23.015  19.324  29.383  1.00 28.07           C  
ATOM    566  NE  ARG A  74      24.455  19.313  29.025  1.00 30.86           N  
ATOM    567  CZ  ARG A  74      25.012  20.498  28.754  1.00 32.03           C  
ATOM    568  NH1 ARG A  74      24.212  21.563  28.874  1.00 33.42           N  
ATOM    569  NH2 ARG A  74      26.278  20.575  28.406  1.00 31.67           N  
ATOM    570  N   SER A  75      19.343  16.647  26.561  1.00 13.71           N  
ATOM    571  CA  SER A  75      18.630  15.388  26.638  1.00 14.14           C  
ATOM    572  C   SER A  75      19.676  14.271  26.802  1.00 16.25           C  
ATOM    573  O   SER A  75      20.764  14.261  26.223  1.00 13.10           O  
ATOM    574  CB  SER A  75      17.747  15.132  25.420  1.00 13.02           C  
ATOM    575  OG  SER A  75      17.138  13.850  25.470  1.00 15.42           O  
ATOM    576  N   LYS A  76      19.281  13.315  27.639  1.00 17.52           N  
ATOM    577  CA  LYS A  76      20.122  12.118  27.778  1.00 20.24           C  
ATOM    578  C   LYS A  76      19.739  11.050  26.781  1.00 19.12           C  
ATOM    579  O   LYS A  76      20.353   9.976  26.748  1.00 18.86           O  
ATOM    580  CB  LYS A  76      20.010  11.665  29.239  1.00 24.03           C  
ATOM    581  CG  LYS A  76      20.656  12.660  30.200  1.00 27.07           C  
ATOM    582  CD  LYS A  76      22.117  12.875  29.820  1.00 31.02           C  
ATOM    583  CE  LYS A  76      22.854  13.809  30.761  1.00 34.69           C  
ATOM    584  NZ  LYS A  76      22.732  15.267  30.478  1.00 36.54           N  
ATOM    585  N   LYS A  77      18.731  11.290  25.941  1.00 17.32           N  
ATOM    586  CA  LYS A  77      18.400  10.311  24.882  1.00 17.70           C  
ATOM    587  C   LYS A  77      19.538  10.258  23.875  1.00 17.66           C  
ATOM    588  O   LYS A  77      19.871  11.349  23.359  1.00 17.28           O  
ATOM    589  CB  LYS A  77      17.091  10.673  24.181  1.00 17.02           C  
ATOM    590  CG  LYS A  77      15.939  10.639  25.176  1.00 16.58           C  
ATOM    591  CD  LYS A  77      14.736  11.406  24.621  1.00 18.35           C  
ATOM    592  CE  LYS A  77      13.591  11.222  25.633  1.00 19.19           C  
ATOM    593  NZ  LYS A  77      12.288  11.635  25.072  1.00 20.33           N  
ATOM    594  N   PHE A  78      20.146   9.078  23.667  1.00 14.08           N  
ATOM    595  CA  PHE A  78      21.346   9.169  22.787  1.00 12.77           C  
ATOM    596  C   PHE A  78      21.480   7.880  22.013  1.00 11.15           C  
ATOM    597  O   PHE A  78      22.413   7.101  22.236  1.00 10.22           O  
ATOM    598  CB  PHE A  78      22.614   9.507  23.562  1.00 11.67           C  
ATOM    599  CG  PHE A  78      23.775  10.053  22.757  1.00 13.99           C  
ATOM    600  CD1 PHE A  78      24.846   9.264  22.409  1.00 13.09           C  
ATOM    601  CD2 PHE A  78      23.793  11.396  22.374  1.00 13.58           C  
ATOM    602  CE1 PHE A  78      25.906   9.772  21.701  1.00 15.92           C  
ATOM    603  CE2 PHE A  78      24.874  11.915  21.694  1.00 15.33           C  
ATOM    604  CZ  PHE A  78      25.942  11.111  21.313  1.00 15.79           C  
ATOM    605  N   PRO A  79      20.574   7.660  21.067  1.00 11.98           N  
ATOM    606  CA  PRO A  79      20.603   6.420  20.282  1.00 13.14           C  
ATOM    607  C   PRO A  79      21.597   6.496  19.143  1.00 13.36           C  
ATOM    608  O   PRO A  79      21.195   6.514  17.948  1.00 13.99           O  
ATOM    609  CB  PRO A  79      19.151   6.358  19.753  1.00 14.57           C  
ATOM    610  CG  PRO A  79      18.801   7.826  19.547  1.00 12.79           C  
ATOM    611  CD  PRO A  79      19.331   8.436  20.823  1.00 12.10           C  
ATOM    612  N   PHE A  80      22.869   6.738  19.367  1.00 11.43           N  
ATOM    613  CA  PHE A  80      23.819   7.125  18.329  1.00 11.37           C  
ATOM    614  C   PHE A  80      25.097   6.336  18.588  1.00 12.35           C  
ATOM    615  O   PHE A  80      25.418   6.175  19.775  1.00 12.58           O  
ATOM    616  CB  PHE A  80      24.134   8.636  18.283  1.00 11.57           C  
ATOM    617  CG  PHE A  80      22.914   9.473  17.987  1.00 12.82           C  
ATOM    618  CD1 PHE A  80      22.480   9.661  16.686  1.00 13.56           C  
ATOM    619  CD2 PHE A  80      22.207  10.067  19.013  1.00 11.09           C  
ATOM    620  CE1 PHE A  80      21.367  10.435  16.393  1.00 14.49           C  
ATOM    621  CE2 PHE A  80      21.079  10.812  18.720  1.00 12.00           C  
ATOM    622  CZ  PHE A  80      20.638  10.990  17.443  1.00 13.77           C  
ATOM    623  N   THR A  81      25.712   5.798  17.538  1.00 11.17           N  
ATOM    624  CA  THR A  81      26.950   5.079  17.626  1.00 12.65           C  
ATOM    625  C   THR A  81      27.950   5.517  16.560  1.00 12.89           C  
ATOM    626  O   THR A  81      27.652   5.514  15.364  1.00 12.66           O  
ATOM    627  CB  THR A  81      26.735   3.548  17.491  1.00 12.33           C  
ATOM    628  OG1 THR A  81      25.684   3.241  18.419  1.00 12.35           O  
ATOM    629  CG2 THR A  81      28.032   2.807  17.822  1.00 11.11           C  
ATOM    630  N   LYS A  82      29.145   5.858  17.050  1.00 10.59           N  
ATOM    631  CA  LYS A  82      30.239   6.244  16.174  1.00 10.21           C  
ATOM    632  C   LYS A  82      30.406   5.173  15.110  1.00  9.84           C  
ATOM    633  O   LYS A  82      30.362   4.011  15.515  1.00  8.01           O  
ATOM    634  CB  LYS A  82      31.540   6.345  17.002  1.00 10.87           C  
ATOM    635  CG  LYS A  82      31.525   7.525  17.991  1.00 10.59           C  
ATOM    636  CD  LYS A  82      32.882   7.754  18.644  1.00 11.17           C  
ATOM    637  CE  LYS A  82      33.187   6.665  19.661  1.00 11.30           C  
ATOM    638  NZ  LYS A  82      34.374   6.958  20.495  1.00 10.43           N  
ATOM    639  N   GLY A  83      30.595   5.529  13.832  1.00  8.80           N  
ATOM    640  CA  GLY A  83      30.750   4.490  12.833  1.00  9.45           C  
ATOM    641  C   GLY A  83      29.376   4.115  12.232  1.00 11.41           C  
ATOM    642  O   GLY A  83      29.369   3.463  11.178  1.00 10.66           O  
ATOM    643  N   ASP A  84      28.266   4.393  12.891  1.00  9.73           N  
ATOM    644  CA  ASP A  84      26.969   3.917  12.494  1.00 11.32           C  
ATOM    645  C   ASP A  84      26.112   5.037  11.874  1.00 11.59           C  
ATOM    646  O   ASP A  84      26.296   6.223  12.085  1.00  8.15           O  
ATOM    647  CB  ASP A  84      26.162   3.294  13.647  1.00 11.50           C  
ATOM    648  CG  ASP A  84      26.781   1.954  14.044  1.00 12.71           C  
ATOM    649  OD1 ASP A  84      26.334   1.334  15.021  1.00 13.76           O  
ATOM    650  OD2 ASP A  84      27.765   1.486  13.444  1.00 14.36           O  
ATOM    651  N   HIS A  85      25.186   4.546  11.066  1.00 12.17           N  
ATOM    652  CA  HIS A  85      24.113   5.299  10.477  1.00 14.13           C  
ATOM    653  C   HIS A  85      23.184   5.884  11.547  1.00 12.18           C  
ATOM    654  O   HIS A  85      22.975   5.297  12.607  1.00 10.51           O  
ATOM    655  CB  HIS A  85      23.250   4.409   9.540  1.00 15.59           C  
ATOM    656  CG  HIS A  85      23.995   4.184   8.255  1.00 18.18           C  
ATOM    657  ND1 HIS A  85      23.835   4.959   7.134  1.00 19.82           N  
ATOM    658  CD2 HIS A  85      24.940   3.263   7.923  1.00 20.12           C  
ATOM    659  CE1 HIS A  85      24.606   4.524   6.153  1.00 19.16           C  
ATOM    660  NE2 HIS A  85      25.315   3.515   6.623  1.00 20.35           N  
ATOM    661  N   PHE A  86      22.637   7.047  11.202  1.00  8.43           N  
ATOM    662  CA  PHE A  86      21.599   7.630  12.051  1.00 10.92           C  
ATOM    663  C   PHE A  86      20.529   8.211  11.119  1.00 11.89           C  
ATOM    664  O   PHE A  86      20.886   8.518   9.955  1.00 10.17           O  
ATOM    665  CB  PHE A  86      22.247   8.695  12.917  1.00 10.88           C  
ATOM    666  CG  PHE A  86      22.769   9.895  12.194  1.00 10.77           C  
ATOM    667  CD1 PHE A  86      24.115  10.005  11.937  1.00 12.52           C  
ATOM    668  CD2 PHE A  86      21.948  10.906  11.736  1.00 12.25           C  
ATOM    669  CE1 PHE A  86      24.652  11.111  11.290  1.00 12.45           C  
ATOM    670  CE2 PHE A  86      22.480  11.980  11.061  1.00 13.10           C  
ATOM    671  CZ  PHE A  86      23.823  12.108  10.849  1.00  8.99           C  
ATOM    672  N   GLN A  87      19.356   8.457  11.638  1.00 11.83           N  
ATOM    673  CA  GLN A  87      18.341   9.183  10.849  1.00 12.98           C  
ATOM    674  C   GLN A  87      17.600  10.103  11.811  1.00 14.37           C  
ATOM    675  O   GLN A  87      17.279   9.618  12.905  1.00 14.47           O  
ATOM    676  CB  GLN A  87      17.306   8.212  10.302  1.00 13.20           C  
ATOM    677  CG  GLN A  87      16.340   8.880   9.316  1.00 15.71           C  
ATOM    678  CD  GLN A  87      15.522   7.780   8.647  1.00 15.51           C  
ATOM    679  OE1 GLN A  87      14.321   7.759   8.870  1.00 17.76           O  
ATOM    680  NE2 GLN A  87      16.187   6.899   7.924  1.00 16.62           N  
ATOM    681  N   ILE A  88      17.368  11.328  11.385  1.00 12.82           N  
ATOM    682  CA  ILE A  88      16.703  12.349  12.204  1.00 13.03           C  
ATOM    683  C   ILE A  88      15.552  12.928  11.365  1.00 12.42           C  
ATOM    684  O   ILE A  88      15.810  13.196  10.170  1.00  9.60           O  
ATOM    685  CB  ILE A  88      17.652  13.533  12.555  1.00 11.53           C  
ATOM    686  CG1 ILE A  88      18.880  13.004  13.288  1.00 15.37           C  
ATOM    687  CG2 ILE A  88      16.915  14.539  13.463  1.00 11.70           C  
ATOM    688  CD1 ILE A  88      20.016  13.965  13.588  1.00 14.98           C  
ATOM    689  N   THR A  89      14.400  13.172  11.981  1.00 10.97           N  
ATOM    690  CA  THR A  89      13.345  13.905  11.255  1.00 12.40           C  
ATOM    691  C   THR A  89      12.947  15.148  12.040  1.00 11.99           C  
ATOM    692  O   THR A  89      12.754  15.015  13.275  1.00 12.79           O  
ATOM    693  CB  THR A  89      12.060  13.048  11.104  1.00 12.63           C  
ATOM    694  OG1 THR A  89      12.374  11.922  10.295  1.00 14.69           O  
ATOM    695  CG2 THR A  89      10.890  13.765  10.458  1.00 12.98           C  
ATOM    696  N   ILE A  90      12.808  16.278  11.359  1.00  9.18           N  
ATOM    697  CA  ILE A  90      12.424  17.518  12.048  1.00 10.43           C  
ATOM    698  C   ILE A  90      11.193  18.108  11.351  1.00 11.46           C  
ATOM    699  O   ILE A  90      11.028  18.075  10.115  1.00 10.95           O  
ATOM    700  CB  ILE A  90      13.569  18.525  12.045  1.00 10.85           C  
ATOM    701  CG1 ILE A  90      14.831  17.951  12.724  1.00 10.16           C  
ATOM    702  CG2 ILE A  90      13.243  19.885  12.665  1.00 10.66           C  
ATOM    703  CD1 ILE A  90      16.063  18.737  12.305  1.00 11.78           C  
ATOM    704  N   THR A  91      10.205  18.529  12.129  1.00 10.76           N  
ATOM    705  CA  THR A  91       9.103  19.363  11.678  1.00 11.60           C  
ATOM    706  C   THR A  91       9.001  20.499  12.712  1.00 10.32           C  
ATOM    707  O   THR A  91       9.648  20.430  13.764  1.00 10.32           O  
ATOM    708  CB  THR A  91       7.749  18.663  11.590  1.00 13.03           C  
ATOM    709  OG1 THR A  91       7.430  18.192  12.930  1.00 16.58           O  
ATOM    710  CG2 THR A  91       7.716  17.448  10.682  1.00 14.52           C  
ATOM    711  N   PHE A  92       8.198  21.517  12.479  1.00  9.70           N  
ATOM    712  CA  PHE A  92       8.114  22.634  13.405  1.00 10.49           C  
ATOM    713  C   PHE A  92       6.820  23.378  13.143  1.00 10.47           C  
ATOM    714  O   PHE A  92       6.298  23.348  12.025  1.00 10.74           O  
ATOM    715  CB  PHE A  92       9.287  23.611  13.325  1.00 11.54           C  
ATOM    716  CG  PHE A  92       9.320  24.382  12.031  1.00 12.67           C  
ATOM    717  CD1 PHE A  92       9.982  23.840  10.922  1.00 13.35           C  
ATOM    718  CD2 PHE A  92       8.738  25.623  11.898  1.00 12.96           C  
ATOM    719  CE1 PHE A  92      10.055  24.519   9.730  1.00 12.44           C  
ATOM    720  CE2 PHE A  92       8.783  26.321  10.707  1.00 14.39           C  
ATOM    721  CZ  PHE A  92       9.441  25.776   9.607  1.00 14.26           C  
ATOM    722  N   ASP A  93       6.277  24.039  14.155  1.00 10.91           N  
ATOM    723  CA  ASP A  93       5.218  25.032  13.915  1.00 10.18           C  
ATOM    724  C   ASP A  93       5.762  26.290  14.555  1.00 11.48           C  
ATOM    725  O   ASP A  93       6.946  26.333  14.967  1.00  8.76           O  
ATOM    726  CB  ASP A  93       3.897  24.622  14.572  1.00 13.41           C  
ATOM    727  CG  ASP A  93       3.973  24.365  16.087  1.00 14.17           C  
ATOM    728  OD1 ASP A  93       3.155  23.567  16.586  1.00 16.10           O  
ATOM    729  OD2 ASP A  93       4.814  24.922  16.805  1.00 12.01           O  
ATOM    730  N   THR A  94       4.960  27.329  14.749  1.00 12.61           N  
ATOM    731  CA  THR A  94       5.584  28.599  15.157  1.00 15.33           C  
ATOM    732  C   THR A  94       6.121  28.542  16.579  1.00 13.98           C  
ATOM    733  O   THR A  94       6.917  29.422  16.952  1.00 13.17           O  
ATOM    734  CB  THR A  94       4.594  29.753  14.919  1.00 19.18           C  
ATOM    735  OG1 THR A  94       3.413  29.478  15.653  1.00 20.35           O  
ATOM    736  CG2 THR A  94       4.239  29.736  13.419  1.00 21.58           C  
ATOM    737  N   HIS A  95       5.723  27.550  17.384  1.00 10.53           N  
ATOM    738  CA  HIS A  95       6.124  27.517  18.775  1.00 12.82           C  
ATOM    739  C   HIS A  95       7.213  26.513  19.054  1.00 11.76           C  
ATOM    740  O   HIS A  95       7.936  26.693  20.028  1.00 10.53           O  
ATOM    741  CB  HIS A  95       4.877  27.237  19.635  1.00 17.11           C  
ATOM    742  CG  HIS A  95       4.052  28.501  19.596  1.00 21.94           C  
ATOM    743  ND1 HIS A  95       2.827  28.578  19.008  1.00 24.65           N  
ATOM    744  CD2 HIS A  95       4.361  29.757  20.025  1.00 24.03           C  
ATOM    745  CE1 HIS A  95       2.355  29.813  19.090  1.00 25.17           C  
ATOM    746  NE2 HIS A  95       3.275  30.538  19.704  1.00 25.56           N  
ATOM    747  N   THR A  96       7.282  25.430  18.260  1.00  9.40           N  
ATOM    748  CA  THR A  96       8.118  24.293  18.629  1.00  8.86           C  
ATOM    749  C   THR A  96       8.837  23.596  17.480  1.00  8.29           C  
ATOM    750  O   THR A  96       8.172  23.412  16.462  1.00  7.06           O  
ATOM    751  CB  THR A  96       7.136  23.187  19.183  1.00  8.87           C  
ATOM    752  OG1 THR A  96       6.398  23.823  20.234  1.00 10.40           O  
ATOM    753  CG2 THR A  96       7.941  22.004  19.711  1.00  5.43           C  
ATOM    754  N   PHE A  97      10.057  23.130  17.675  1.00  8.82           N  
ATOM    755  CA  PHE A  97      10.708  22.190  16.786  1.00  8.60           C  
ATOM    756  C   PHE A  97      10.512  20.774  17.351  1.00  8.88           C  
ATOM    757  O   PHE A  97      10.685  20.540  18.549  1.00  8.32           O  
ATOM    758  CB  PHE A  97      12.201  22.433  16.652  1.00  7.64           C  
ATOM    759  CG  PHE A  97      12.576  23.675  15.862  1.00  8.39           C  
ATOM    760  CD1 PHE A  97      12.776  23.599  14.503  1.00  8.28           C  
ATOM    761  CD2 PHE A  97      12.794  24.876  16.509  1.00  9.57           C  
ATOM    762  CE1 PHE A  97      13.136  24.734  13.773  1.00  7.78           C  
ATOM    763  CE2 PHE A  97      13.175  26.022  15.820  1.00  7.73           C  
ATOM    764  CZ  PHE A  97      13.324  25.912  14.442  1.00  9.99           C  
ATOM    765  N   TYR A  98      10.044  19.909  16.484  1.00 10.23           N  
ATOM    766  CA  TYR A  98       9.718  18.524  16.816  1.00 11.06           C  
ATOM    767  C   TYR A  98      10.786  17.610  16.198  1.00 11.74           C  
ATOM    768  O   TYR A  98      10.922  17.562  14.956  1.00 11.49           O  
ATOM    769  CB  TYR A  98       8.348  18.226  16.216  1.00 11.44           C  
ATOM    770  CG  TYR A  98       7.204  18.895  16.957  1.00 10.38           C  
ATOM    771  CD1 TYR A  98       6.483  19.938  16.411  1.00 11.41           C  
ATOM    772  CD2 TYR A  98       6.858  18.470  18.231  1.00 10.58           C  
ATOM    773  CE1 TYR A  98       5.439  20.530  17.099  1.00  8.71           C  
ATOM    774  CE2 TYR A  98       5.802  19.035  18.912  1.00 10.04           C  
ATOM    775  CZ  TYR A  98       5.102  20.072  18.358  1.00 11.22           C  
ATOM    776  OH  TYR A  98       4.063  20.658  19.039  1.00  9.09           O  
ATOM    777  N   ILE A  99      11.589  17.015  17.048  1.00 10.91           N  
ATOM    778  CA  ILE A  99      12.778  16.277  16.569  1.00 12.31           C  
ATOM    779  C   ILE A  99      12.574  14.801  16.903  1.00 13.14           C  
ATOM    780  O   ILE A  99      12.190  14.483  18.036  1.00 13.75           O  
ATOM    781  CB  ILE A  99      14.059  16.846  17.170  1.00 12.82           C  
ATOM    782  CG1 ILE A  99      14.211  18.355  16.869  1.00 11.01           C  
ATOM    783  CG2 ILE A  99      15.311  16.122  16.659  1.00 13.42           C  
ATOM    784  CD1 ILE A  99      14.846  19.059  18.059  1.00 13.51           C  
ATOM    785  N   GLN A 100      12.663  13.936  15.891  1.00 12.45           N  
ATOM    786  CA  GLN A 100      12.594  12.510  16.138  1.00 11.91           C  
ATOM    787  C   GLN A 100      13.946  11.888  15.788  1.00 11.81           C  
ATOM    788  O   GLN A 100      14.540  12.119  14.723  1.00  8.65           O  
ATOM    789  CB  GLN A 100      11.476  11.829  15.348  1.00 14.45           C  
ATOM    790  CG  GLN A 100      11.324  10.387  15.851  1.00 17.49           C  
ATOM    791  CD  GLN A 100      10.077   9.685  15.316  1.00 21.62           C  
ATOM    792  OE1 GLN A 100       9.924   9.671  14.077  1.00 22.20           O  
ATOM    793  NE2 GLN A 100       9.207   9.132  16.186  1.00 16.78           N  
ATOM    794  N   LEU A 101      14.478  11.142  16.740  1.00  9.98           N  
ATOM    795  CA  LEU A 101      15.763  10.471  16.641  1.00 10.63           C  
ATOM    796  C   LEU A 101      15.734   9.122  15.961  1.00 10.81           C  
ATOM    797  O   LEU A 101      14.656   8.661  15.576  1.00 11.21           O  
ATOM    798  CB  LEU A 101      16.344  10.283  18.056  1.00 10.97           C  
ATOM    799  CG  LEU A 101      16.375  11.520  18.944  1.00 10.93           C  
ATOM    800  CD1 LEU A 101      16.958  11.134  20.291  1.00 10.63           C  
ATOM    801  CD2 LEU A 101      17.184  12.674  18.311  1.00 10.09           C  
ATOM    802  N   SER A 102      16.896   8.471  15.781  1.00 10.97           N  
ATOM    803  CA  SER A 102      17.014   7.218  15.086  1.00 11.82           C  
ATOM    804  C   SER A 102      16.198   6.072  15.697  1.00 13.20           C  
ATOM    805  O   SER A 102      15.844   5.199  14.914  1.00 10.48           O  
ATOM    806  CB  SER A 102      18.467   6.701  14.991  1.00 13.52           C  
ATOM    807  OG  SER A 102      19.316   7.708  14.487  1.00 14.22           O  
ATOM    808  N   ASN A 103      15.990   6.035  17.013  1.00 11.11           N  
ATOM    809  CA  ASN A 103      15.213   4.963  17.608  1.00 12.11           C  
ATOM    810  C   ASN A 103      13.735   5.260  17.768  1.00 10.85           C  
ATOM    811  O   ASN A 103      12.964   4.553  18.399  1.00  9.73           O  
ATOM    812  CB  ASN A 103      15.839   4.702  19.007  1.00 11.79           C  
ATOM    813  CG  ASN A 103      15.781   5.904  19.924  1.00 13.77           C  
ATOM    814  OD1 ASN A 103      15.595   7.082  19.560  1.00 12.69           O  
ATOM    815  ND2 ASN A 103      16.018   5.641  21.234  1.00 11.90           N  
ATOM    816  N   GLY A 104      13.248   6.386  17.248  1.00  9.64           N  
ATOM    817  CA  GLY A 104      11.884   6.853  17.368  1.00  9.44           C  
ATOM    818  C   GLY A 104      11.636   7.753  18.595  1.00  8.09           C  
ATOM    819  O   GLY A 104      10.530   8.280  18.703  1.00  9.69           O  
ATOM    820  N   GLU A 105      12.592   7.913  19.481  1.00  6.39           N  
ATOM    821  CA  GLU A 105      12.474   8.808  20.625  1.00  9.13           C  
ATOM    822  C   GLU A 105      12.469  10.233  20.095  1.00  9.07           C  
ATOM    823  O   GLU A 105      12.913  10.493  18.968  1.00  8.15           O  
ATOM    824  CB  GLU A 105      13.588   8.669  21.661  1.00  9.09           C  
ATOM    825  CG  GLU A 105      13.415   7.365  22.451  1.00 12.90           C  
ATOM    826  CD  GLU A 105      14.407   7.302  23.609  1.00 14.64           C  
ATOM    827  OE1 GLU A 105      13.907   7.210  24.774  1.00 17.18           O  
ATOM    828  OE2 GLU A 105      15.625   7.318  23.342  1.00 13.73           O  
ATOM    829  N   THR A 106      11.887  11.147  20.836  1.00 10.60           N  
ATOM    830  CA  THR A 106      11.763  12.522  20.354  1.00 11.12           C  
ATOM    831  C   THR A 106      12.281  13.522  21.378  1.00 11.79           C  
ATOM    832  O   THR A 106      12.345  13.224  22.585  1.00 12.95           O  
ATOM    833  CB  THR A 106      10.299  12.881  20.062  1.00 13.15           C  
ATOM    834  OG1 THR A 106       9.599  12.955  21.318  1.00 13.84           O  
ATOM    835  CG2 THR A 106       9.559  11.874  19.218  1.00 13.73           C  
ATOM    836  N   VAL A 107      12.670  14.689  20.904  1.00 11.05           N  
ATOM    837  CA  VAL A 107      12.988  15.846  21.726  1.00 11.36           C  
ATOM    838  C   VAL A 107      12.285  17.038  21.067  1.00 12.92           C  
ATOM    839  O   VAL A 107      12.046  17.016  19.854  1.00 10.27           O  
ATOM    840  CB  VAL A 107      14.482  16.131  21.826  1.00 11.97           C  
ATOM    841  CG1 VAL A 107      15.208  14.938  22.489  1.00 13.21           C  
ATOM    842  CG2 VAL A 107      15.121  16.280  20.442  1.00 15.76           C  
ATOM    843  N   GLU A 108      11.931  18.039  21.862  1.00 12.91           N  
ATOM    844  CA  GLU A 108      11.218  19.220  21.381  1.00 13.20           C  
ATOM    845  C   GLU A 108      12.042  20.432  21.803  1.00 13.29           C  
ATOM    846  O   GLU A 108      12.767  20.321  22.793  1.00 14.55           O  
ATOM    847  CB  GLU A 108       9.793  19.302  21.922  1.00 14.84           C  
ATOM    848  CG  GLU A 108       8.789  18.339  21.295  1.00 15.76           C  
ATOM    849  CD  GLU A 108       8.893  16.963  21.931  1.00 17.34           C  
ATOM    850  OE1 GLU A 108       8.937  16.915  23.177  1.00 17.58           O  
ATOM    851  OE2 GLU A 108       8.988  15.937  21.210  1.00 18.19           O  
ATOM    852  N   PHE A 109      12.038  21.514  21.040  1.00 11.95           N  
ATOM    853  CA  PHE A 109      12.856  22.667  21.402  1.00  9.96           C  
ATOM    854  C   PHE A 109      12.117  23.895  20.904  1.00 12.37           C  
ATOM    855  O   PHE A 109      11.492  23.844  19.833  1.00 10.48           O  
ATOM    856  CB  PHE A 109      14.183  22.581  20.642  1.00 10.64           C  
ATOM    857  CG  PHE A 109      15.108  23.738  20.917  1.00  9.50           C  
ATOM    858  CD1 PHE A 109      15.763  23.789  22.140  1.00  7.59           C  
ATOM    859  CD2 PHE A 109      15.287  24.734  19.965  1.00  8.67           C  
ATOM    860  CE1 PHE A 109      16.622  24.855  22.402  1.00  8.13           C  
ATOM    861  CE2 PHE A 109      16.164  25.787  20.206  1.00  7.76           C  
ATOM    862  CZ  PHE A 109      16.802  25.845  21.447  1.00  8.91           C  
ATOM    863  N   PRO A 110      12.199  24.978  21.666  1.00 12.14           N  
ATOM    864  CA  PRO A 110      11.320  26.112  21.365  1.00 13.63           C  
ATOM    865  C   PRO A 110      11.766  26.764  20.076  1.00 12.08           C  
ATOM    866  O   PRO A 110      12.952  26.900  19.783  1.00 13.41           O  
ATOM    867  CB  PRO A 110      11.485  27.027  22.579  1.00 13.14           C  
ATOM    868  CG  PRO A 110      12.796  26.561  23.158  1.00 15.22           C  
ATOM    869  CD  PRO A 110      12.616  25.043  23.088  1.00 13.21           C  
ATOM    870  N   ASN A 111      10.780  27.191  19.291  1.00 11.90           N  
ATOM    871  CA  ASN A 111      11.031  28.024  18.109  1.00 11.22           C  
ATOM    872  C   ASN A 111      11.087  29.430  18.680  1.00 10.63           C  
ATOM    873  O   ASN A 111      10.064  30.116  18.737  1.00 13.65           O  
ATOM    874  CB  ASN A 111       9.898  27.887  17.110  1.00  9.90           C  
ATOM    875  CG  ASN A 111      10.037  28.632  15.807  1.00 12.85           C  
ATOM    876  OD1 ASN A 111       9.332  28.340  14.806  1.00 12.57           O  
ATOM    877  ND2 ASN A 111      10.893  29.619  15.806  1.00  8.44           N  
ATOM    878  N   ARG A 112      12.232  29.851  19.146  1.00 10.07           N  
ATOM    879  CA  ARG A 112      12.335  31.109  19.888  1.00 11.98           C  
ATOM    880  C   ARG A 112      12.005  32.321  19.039  1.00 12.65           C  
ATOM    881  O   ARG A 112      11.526  33.283  19.626  1.00 12.71           O  
ATOM    882  CB  ARG A 112      13.735  31.163  20.515  1.00 11.68           C  
ATOM    883  CG  ARG A 112      13.902  30.056  21.572  1.00 11.60           C  
ATOM    884  CD  ARG A 112      15.349  29.945  22.002  1.00 10.47           C  
ATOM    885  NE  ARG A 112      15.480  29.118  23.193  1.00  9.04           N  
ATOM    886  CZ  ARG A 112      16.585  28.611  23.719  1.00  8.41           C  
ATOM    887  NH1 ARG A 112      16.515  27.896  24.843  1.00  6.18           N  
ATOM    888  NH2 ARG A 112      17.758  28.774  23.124  1.00  4.65           N  
ATOM    889  N   ASN A 113      12.186  32.375  17.724  1.00 13.17           N  
ATOM    890  CA  ASN A 113      11.924  33.552  16.925  1.00 15.39           C  
ATOM    891  C   ASN A 113      10.503  33.559  16.384  1.00 15.21           C  
ATOM    892  O   ASN A 113      10.115  34.547  15.784  1.00 14.50           O  
ATOM    893  CB  ASN A 113      12.808  33.661  15.669  1.00 17.82           C  
ATOM    894  CG  ASN A 113      14.282  33.782  15.888  1.00 18.88           C  
ATOM    895  OD1 ASN A 113      14.999  34.043  14.898  1.00 22.24           O  
ATOM    896  ND2 ASN A 113      14.730  33.646  17.123  1.00 17.29           N  
ATOM    897  N   LYS A 114       9.827  32.415  16.502  1.00 13.83           N  
ATOM    898  CA  LYS A 114       8.508  32.275  15.916  1.00 15.54           C  
ATOM    899  C   LYS A 114       8.638  32.338  14.391  1.00 15.07           C  
ATOM    900  O   LYS A 114       7.719  32.729  13.703  1.00 16.20           O  
ATOM    901  CB  LYS A 114       7.487  33.281  16.454  1.00 18.05           C  
ATOM    902  CG  LYS A 114       7.351  33.203  17.975  1.00 20.01           C  
ATOM    903  CD  LYS A 114       6.205  34.012  18.518  1.00 21.53           C  
ATOM    904  CE  LYS A 114       4.827  33.381  18.280  1.00 19.81           C  
ATOM    905  NZ  LYS A 114       3.800  34.460  18.310  1.00 20.04           N  
ATOM    906  N   ASP A 115       9.720  31.822  13.822  1.00 15.44           N  
ATOM    907  CA  ASP A 115       9.954  31.752  12.397  1.00 15.02           C  
ATOM    908  C   ASP A 115       9.035  30.769  11.688  1.00 14.99           C  
ATOM    909  O   ASP A 115       8.727  29.697  12.229  1.00 12.70           O  
ATOM    910  CB  ASP A 115      11.388  31.217  12.147  1.00 17.06           C  
ATOM    911  CG  ASP A 115      12.448  32.231  12.508  1.00 19.00           C  
ATOM    912  OD1 ASP A 115      13.356  31.869  13.311  1.00 21.42           O  
ATOM    913  OD2 ASP A 115      12.379  33.363  11.992  1.00 17.52           O  
ATOM    914  N   ALA A 116       8.665  31.070  10.436  1.00 12.81           N  
ATOM    915  CA  ALA A 116       7.737  30.164   9.752  1.00 11.84           C  
ATOM    916  C   ALA A 116       8.473  29.479   8.591  1.00 11.44           C  
ATOM    917  O   ALA A 116       7.882  28.607   7.951  1.00 13.67           O  
ATOM    918  CB  ALA A 116       6.497  30.911   9.251  1.00 11.79           C  
ATOM    919  N   ALA A 117       9.736  29.828   8.395  1.00 10.76           N  
ATOM    920  CA  ALA A 117      10.527  29.208   7.318  1.00 11.63           C  
ATOM    921  C   ALA A 117      12.003  29.488   7.530  1.00 12.50           C  
ATOM    922  O   ALA A 117      12.386  30.466   8.193  1.00 11.58           O  
ATOM    923  CB  ALA A 117      10.130  29.781   5.943  1.00 13.01           C  
ATOM    924  N   PHE A 118      12.849  28.615   6.988  1.00 10.70           N  
ATOM    925  CA  PHE A 118      14.276  28.602   7.236  1.00 10.80           C  
ATOM    926  C   PHE A 118      14.965  28.292   5.915  1.00 12.59           C  
ATOM    927  O   PHE A 118      14.541  27.317   5.271  1.00 11.00           O  
ATOM    928  CB  PHE A 118      14.667  27.459   8.229  1.00 10.38           C  
ATOM    929  CG  PHE A 118      14.061  27.701   9.590  1.00  8.73           C  
ATOM    930  CD1 PHE A 118      14.519  28.735  10.379  1.00  8.13           C  
ATOM    931  CD2 PHE A 118      12.995  26.923  10.003  1.00 10.01           C  
ATOM    932  CE1 PHE A 118      13.933  28.982  11.604  1.00  8.69           C  
ATOM    933  CE2 PHE A 118      12.411  27.160  11.240  1.00  9.39           C  
ATOM    934  CZ  PHE A 118      12.887  28.177  12.045  1.00  9.16           C  
ATOM    935  N   ASN A 119      15.980  29.091   5.558  1.00 13.21           N  
ATOM    936  CA  ASN A 119      16.643  28.801   4.291  1.00 15.61           C  
ATOM    937  C   ASN A 119      17.944  28.056   4.374  1.00 14.79           C  
ATOM    938  O   ASN A 119      18.646  27.998   3.342  1.00 16.94           O  
ATOM    939  CB  ASN A 119      16.913  30.120   3.516  1.00 18.60           C  
ATOM    940  CG  ASN A 119      15.535  30.586   3.022  1.00 21.74           C  
ATOM    941  OD1 ASN A 119      15.100  31.537   3.679  1.00 26.18           O  
ATOM    942  ND2 ASN A 119      14.939  29.976   2.032  1.00 17.93           N  
ATOM    943  N   LEU A 120      18.290  27.512   5.532  1.00 12.78           N  
ATOM    944  CA  LEU A 120      19.574  26.833   5.623  1.00 11.33           C  
ATOM    945  C   LEU A 120      19.483  25.655   6.575  1.00 11.90           C  
ATOM    946  O   LEU A 120      19.034  25.817   7.714  1.00  8.73           O  
ATOM    947  CB  LEU A 120      20.684  27.763   6.144  1.00 10.46           C  
ATOM    948  CG  LEU A 120      22.030  27.021   6.312  1.00 12.02           C  
ATOM    949  CD1 LEU A 120      22.555  26.474   5.001  1.00 10.48           C  
ATOM    950  CD2 LEU A 120      23.085  28.001   6.851  1.00 12.50           C  
ATOM    951  N   ILE A 121      19.896  24.506   6.046  1.00 11.17           N  
ATOM    952  CA  ILE A 121      20.011  23.341   6.917  1.00 10.93           C  
ATOM    953  C   ILE A 121      21.434  22.824   6.737  1.00 11.92           C  
ATOM    954  O   ILE A 121      21.935  22.749   5.608  1.00 11.17           O  
ATOM    955  CB  ILE A 121      19.012  22.270   6.454  1.00 10.55           C  
ATOM    956  CG1 ILE A 121      17.559  22.717   6.699  1.00  8.88           C  
ATOM    957  CG2 ILE A 121      19.275  20.979   7.208  1.00  9.36           C  
ATOM    958  CD1 ILE A 121      16.696  22.090   5.627  1.00 12.70           C  
ATOM    959  N   TYR A 122      22.121  22.522   7.832  1.00 10.67           N  
ATOM    960  CA  TYR A 122      23.480  22.029   7.662  1.00  9.88           C  
ATOM    961  C   TYR A 122      23.897  21.108   8.798  1.00  9.59           C  
ATOM    962  O   TYR A 122      23.451  21.198   9.924  1.00 10.36           O  
ATOM    963  CB  TYR A 122      24.538  23.098   7.492  1.00  9.07           C  
ATOM    964  CG  TYR A 122      24.999  23.983   8.606  1.00 11.22           C  
ATOM    965  CD1 TYR A 122      26.142  23.694   9.364  1.00 11.31           C  
ATOM    966  CD2 TYR A 122      24.346  25.181   8.905  1.00 11.96           C  
ATOM    967  CE1 TYR A 122      26.599  24.542  10.347  1.00 10.76           C  
ATOM    968  CE2 TYR A 122      24.794  26.040   9.903  1.00 12.60           C  
ATOM    969  CZ  TYR A 122      25.917  25.705  10.628  1.00 11.53           C  
ATOM    970  OH  TYR A 122      26.374  26.566  11.605  1.00 10.42           O  
ATOM    971  N   LEU A 123      24.834  20.244   8.452  1.00 10.83           N  
ATOM    972  CA  LEU A 123      25.505  19.373   9.407  1.00 12.05           C  
ATOM    973  C   LEU A 123      26.952  19.822   9.519  1.00 13.59           C  
ATOM    974  O   LEU A 123      27.595  20.087   8.496  1.00 13.85           O  
ATOM    975  CB  LEU A 123      25.404  17.916   8.918  1.00 13.06           C  
ATOM    976  CG  LEU A 123      26.230  16.929   9.757  1.00 14.78           C  
ATOM    977  CD1 LEU A 123      25.448  15.656  10.006  1.00 14.90           C  
ATOM    978  CD2 LEU A 123      27.522  16.610   9.005  1.00 18.38           C  
ATOM    979  N   ALA A 124      27.424  19.857  10.754  1.00 13.01           N  
ATOM    980  CA  ALA A 124      28.807  20.211  10.991  1.00 11.69           C  
ATOM    981  C   ALA A 124      29.425  19.199  11.957  1.00 11.73           C  
ATOM    982  O   ALA A 124      28.694  18.426  12.604  1.00  8.80           O  
ATOM    983  CB  ALA A 124      28.868  21.614  11.559  1.00 10.54           C  
ATOM    984  N   GLY A 125      30.764  19.177  11.955  1.00  9.74           N  
ATOM    985  CA  GLY A 125      31.445  18.380  12.996  1.00 11.80           C  
ATOM    986  C   GLY A 125      31.699  16.948  12.462  1.00 13.02           C  
ATOM    987  O   GLY A 125      31.789  16.736  11.218  1.00 13.09           O  
ATOM    988  N   ASP A 126      31.732  15.961  13.368  1.00  8.94           N  
ATOM    989  CA  ASP A 126      32.344  14.690  12.986  1.00  9.06           C  
ATOM    990  C   ASP A 126      31.363  13.674  12.437  1.00 10.78           C  
ATOM    991  O   ASP A 126      31.194  12.550  12.969  1.00  8.09           O  
ATOM    992  CB  ASP A 126      32.988  14.195  14.288  1.00 12.14           C  
ATOM    993  CG  ASP A 126      34.238  14.949  14.681  1.00 13.11           C  
ATOM    994  OD1 ASP A 126      34.608  14.978  15.873  1.00 11.97           O  
ATOM    995  OD2 ASP A 126      34.910  15.463  13.755  1.00 10.87           O  
ATOM    996  N   ALA A 127      30.728  13.992  11.300  1.00  8.80           N  
ATOM    997  CA  ALA A 127      29.850  13.034  10.647  1.00  9.26           C  
ATOM    998  C   ALA A 127      29.646  13.464   9.190  1.00 10.02           C  
ATOM    999  O   ALA A 127      30.141  14.530   8.826  1.00  9.06           O  
ATOM   1000  CB  ALA A 127      28.492  12.993  11.372  1.00  8.03           C  
ATOM   1001  N   ARG A 128      28.792  12.753   8.491  1.00 10.30           N  
ATOM   1002  CA  ARG A 128      28.528  13.014   7.086  1.00  9.11           C  
ATOM   1003  C   ARG A 128      27.071  12.682   6.803  1.00  8.91           C  
ATOM   1004  O   ARG A 128      26.476  11.854   7.500  1.00  7.64           O  
ATOM   1005  CB  ARG A 128      29.489  12.217   6.214  1.00 11.68           C  
ATOM   1006  CG  ARG A 128      29.452  10.708   6.305  1.00 13.72           C  
ATOM   1007  CD  ARG A 128      30.662  10.083   5.575  1.00 14.64           C  
ATOM   1008  NE  ARG A 128      30.665   8.634   5.730  1.00 16.92           N  
ATOM   1009  CZ  ARG A 128      29.942   7.786   4.991  1.00 19.60           C  
ATOM   1010  NH1 ARG A 128      29.148   8.260   4.031  1.00 18.46           N  
ATOM   1011  NH2 ARG A 128      29.977   6.456   5.171  1.00 18.81           N  
ATOM   1012  N   LEU A 129      26.489  13.401   5.848  1.00  7.06           N  
ATOM   1013  CA  LEU A 129      25.115  13.059   5.481  1.00  7.54           C  
ATOM   1014  C   LEU A 129      25.154  12.111   4.280  1.00  5.50           C  
ATOM   1015  O   LEU A 129      26.054  12.198   3.457  1.00  3.80           O  
ATOM   1016  CB  LEU A 129      24.367  14.357   5.144  1.00  9.02           C  
ATOM   1017  CG  LEU A 129      23.993  15.276   6.314  1.00  9.90           C  
ATOM   1018  CD1 LEU A 129      23.100  16.421   5.849  1.00  9.15           C  
ATOM   1019  CD2 LEU A 129      23.271  14.478   7.408  1.00  9.43           C  
ATOM   1020  N   THR A 130      24.179  11.219   4.233  1.00  6.12           N  
ATOM   1021  CA  THR A 130      23.945  10.323   3.135  1.00  8.35           C  
ATOM   1022  C   THR A 130      22.637  10.476   2.393  1.00  7.61           C  
ATOM   1023  O   THR A 130      22.637  10.083   1.226  1.00  8.31           O  
ATOM   1024  CB  THR A 130      24.049   8.838   3.581  1.00 10.12           C  
ATOM   1025  OG1 THR A 130      23.084   8.620   4.604  1.00 11.73           O  
ATOM   1026  CG2 THR A 130      25.479   8.568   4.058  1.00  8.57           C  
ATOM   1027  N   PHE A 131      21.547  11.044   2.917  1.00  8.75           N  
ATOM   1028  CA  PHE A 131      20.374  11.288   2.087  1.00  6.67           C  
ATOM   1029  C   PHE A 131      19.644  12.451   2.721  1.00  7.84           C  
ATOM   1030  O   PHE A 131      19.861  12.722   3.908  1.00  6.80           O  
ATOM   1031  CB  PHE A 131      19.482  10.058   2.000  1.00  8.16           C  
ATOM   1032  CG  PHE A 131      18.685   9.631   3.189  1.00 10.30           C  
ATOM   1033  CD1 PHE A 131      19.168   8.735   4.108  1.00 12.26           C  
ATOM   1034  CD2 PHE A 131      17.389  10.129   3.362  1.00 12.27           C  
ATOM   1035  CE1 PHE A 131      18.397   8.329   5.205  1.00 13.15           C  
ATOM   1036  CE2 PHE A 131      16.624   9.753   4.450  1.00 13.89           C  
ATOM   1037  CZ  PHE A 131      17.121   8.841   5.358  1.00 12.50           C  
ATOM   1038  N   VAL A 132      18.734  13.060   1.977  1.00  7.78           N  
ATOM   1039  CA  VAL A 132      17.879  14.077   2.619  1.00  7.31           C  
ATOM   1040  C   VAL A 132      16.527  14.049   1.945  1.00  8.15           C  
ATOM   1041  O   VAL A 132      16.461  13.922   0.711  1.00  8.53           O  
ATOM   1042  CB  VAL A 132      18.524  15.471   2.572  1.00  7.56           C  
ATOM   1043  CG1 VAL A 132      18.821  15.842   1.110  1.00  6.73           C  
ATOM   1044  CG2 VAL A 132      17.620  16.496   3.256  1.00  7.65           C  
ATOM   1045  N   ARG A 133      15.425  14.124   2.673  1.00  8.10           N  
ATOM   1046  CA  ARG A 133      14.130  14.423   2.116  1.00  7.23           C  
ATOM   1047  C   ARG A 133      13.629  15.706   2.763  1.00  9.02           C  
ATOM   1048  O   ARG A 133      13.514  15.743   4.001  1.00  8.03           O  
ATOM   1049  CB  ARG A 133      13.105  13.307   2.431  1.00  9.92           C  
ATOM   1050  CG  ARG A 133      13.487  12.029   1.690  1.00 11.67           C  
ATOM   1051  CD  ARG A 133      12.346  11.032   1.764  1.00 14.91           C  
ATOM   1052  NE  ARG A 133      11.993  10.603   3.110  1.00 15.96           N  
ATOM   1053  CZ  ARG A 133      12.531   9.616   3.805  1.00 18.95           C  
ATOM   1054  NH1 ARG A 133      13.525   8.880   3.322  1.00 17.59           N  
ATOM   1055  NH2 ARG A 133      12.072   9.305   5.028  1.00 17.31           N  
ATOM   1056  N   LEU A 134      13.386  16.746   1.978  1.00  6.90           N  
ATOM   1057  CA  LEU A 134      12.796  17.987   2.529  1.00  7.97           C  
ATOM   1058  C   LEU A 134      11.556  18.284   1.703  1.00  8.55           C  
ATOM   1059  O   LEU A 134      11.651  18.609   0.505  1.00  7.67           O  
ATOM   1060  CB  LEU A 134      13.835  19.119   2.399  1.00  8.08           C  
ATOM   1061  CG  LEU A 134      13.388  20.534   2.758  1.00 10.29           C  
ATOM   1062  CD1 LEU A 134      12.923  20.516   4.241  1.00 10.95           C  
ATOM   1063  CD2 LEU A 134      14.510  21.552   2.544  1.00  7.46           C  
ATOM   1064  N   GLU A 135      10.370  18.133   2.298  1.00 10.28           N  
ATOM   1065  CA  GLU A 135       9.164  18.070   1.491  1.00 10.68           C  
ATOM   1066  C   GLU A 135       7.946  18.253   2.391  1.00 13.13           C  
ATOM   1067  O   GLU A 135       6.949  18.743   1.840  1.00 12.76           O  
ATOM   1068  CB  GLU A 135       9.079  16.782   0.683  1.00 13.95           C  
ATOM   1069  CG  GLU A 135       8.885  15.513   1.493  1.00 13.58           C  
ATOM   1070  CD  GLU A 135       8.939  14.292   0.611  1.00 15.54           C  
ATOM   1071  OE1 GLU A 135       9.515  13.306   1.125  1.00 15.66           O  
ATOM   1072  OE2 GLU A 135       8.526  14.331  -0.587  1.00 16.97           O  
ATOM   1073  OXT GLU A 135       8.036  17.923   3.590  1.00  9.39           O  
TER    1074      GLU A 135                                                      
HETATM 1075  O1  MES A 777      27.809  26.268  15.528  1.00 21.20           O  
HETATM 1076  C2  MES A 777      27.957  27.444  14.676  1.00 18.45           C  
HETATM 1077  C3  MES A 777      29.090  27.090  13.691  1.00 20.33           C  
HETATM 1078  N4  MES A 777      28.707  25.858  13.083  1.00 22.09           N  
HETATM 1079  C5  MES A 777      28.515  24.704  13.858  1.00 20.61           C  
HETATM 1080  C6  MES A 777      27.337  25.101  14.808  1.00 21.81           C  
HETATM 1081  C7  MES A 777      29.787  25.185  12.363  1.00 22.68           C  
HETATM 1082  C8  MES A 777      30.102  25.929  11.096  1.00 24.42           C  
HETATM 1083  S   MES A 777      31.369  25.026  10.099  1.00 25.01           S  
HETATM 1084  O1S MES A 777      31.076  25.636   8.846  1.00 26.54           O  
HETATM 1085  O2S MES A 777      30.470  24.095   9.451  1.00 25.64           O  
HETATM 1086  O3S MES A 777      32.398  24.397  10.912  1.00 24.85           O  
HETATM 1087  O   HOH A 801      25.172  25.489  23.060  1.00 13.98           O  
HETATM 1088  O   HOH A 802      32.089  18.211   8.494  1.00 35.93           O  
HETATM 1089  O   HOH A 803      32.125  20.908  10.124  1.00 24.22           O  
HETATM 1090  O   HOH A 804      28.306  14.937   4.354  1.00  8.60           O  
HETATM 1091  O   HOH A 805      30.869  14.840   0.596  1.00 24.14           O  
HETATM 1092  O   HOH A 806      17.353  25.336   2.509  1.00 12.77           O  
HETATM 1093  O   HOH A 807      10.758  28.281  -2.893  1.00  5.76           O  
HETATM 1094  O   HOH A 808       9.778  24.991   0.104  1.00  9.78           O  
HETATM 1095  O   HOH A 809       9.110  27.372  -1.020  1.00 12.17           O  
HETATM 1096  O   HOH A 810       3.808  18.760   9.475  1.00 40.57           O  
HETATM 1097  O   HOH A 811       7.479  22.022   9.553  1.00 15.82           O  
HETATM 1098  O   HOH A 812      11.063  14.359   5.494  1.00 13.92           O  
HETATM 1099  O   HOH A 813      19.296   4.961  11.508  1.00 25.55           O  
HETATM 1100  O   HOH A 814      16.177   5.208  12.231  1.00 23.91           O  
HETATM 1101  O   HOH A 815      21.005   6.586   7.717  1.00 20.43           O  
HETATM 1102  O   HOH A 816      31.080   9.244   8.964  1.00 20.97           O  
HETATM 1103  O   HOH A 817      34.215   3.311  16.794  1.00 19.32           O  
HETATM 1104  O   HOH A 818      37.903   3.794  16.683  1.00 24.53           O  
HETATM 1105  O   HOH A 819      32.522   6.568   8.443  1.00 35.13           O  
HETATM 1106  O   HOH A 820      37.491   9.311  12.151  1.00 16.58           O  
HETATM 1107  O   HOH A 821      36.903  15.656  23.099  1.00 32.82           O  
HETATM 1108  O   HOH A 822      38.532  20.062  15.705  1.00 28.26           O  
HETATM 1109  O   HOH A 823      37.748  18.282  17.499  1.00 20.50           O  
HETATM 1110  O   HOH A 824      35.986  18.145  21.787  1.00 28.18           O  
HETATM 1111  O   HOH A 825      29.301  19.598  16.636  1.00 10.81           O  
HETATM 1112  O   HOH A 826      27.185  23.525  20.525  1.00 13.15           O  
HETATM 1113  O   HOH A 827      27.569  25.013  22.986  1.00 11.09           O  
HETATM 1114  O   HOH A 828      18.759  32.452  15.500  1.00 10.20           O  
HETATM 1115  O   HOH A 829      14.160  35.259  12.306  1.00 13.02           O  
HETATM 1116  O   HOH A 830      20.324  35.798  14.231  1.00 10.71           O  
HETATM 1117  O   HOH A 831      26.334  31.066   5.926  1.00 26.40           O  
HETATM 1118  O   HOH A 832      17.224  32.521  20.145  1.00  8.15           O  
HETATM 1119  O   HOH A 833      30.555   7.448  22.779  1.00 27.28           O  
HETATM 1120  O   HOH A 834      32.405   8.747  24.988  1.00 23.04           O  
HETATM 1121  O   HOH A 835      29.522   5.370  19.906  1.00 14.67           O  
HETATM 1122  O   HOH A 836      22.910  27.765  28.500  1.00 18.94           O  
HETATM 1123  O   HOH A 837      27.839  23.540  26.276  1.00 11.38           O  
HETATM 1124  O   HOH A 838      19.347  38.286  14.398  1.00 21.30           O  
HETATM 1125  O   HOH A 839      29.556  38.555  14.632  1.00 36.25           O  
HETATM 1126  O   HOH A 840      17.530  31.304  25.711  1.00 19.30           O  
HETATM 1127  O   HOH A 841      24.316  26.420  30.262  1.00 35.66           O  
HETATM 1128  O   HOH A 842      17.102  20.605  29.540  1.00 30.46           O  
HETATM 1129  O   HOH A 843      24.567   6.586  15.054  1.00 11.01           O  
HETATM 1130  O   HOH A 844      21.593   6.371  15.358  1.00 16.85           O  
HETATM 1131  O   HOH A 845       9.312  15.813  18.684  1.00 16.64           O  
HETATM 1132  O   HOH A 846      15.155  20.565  24.104  1.00 24.88           O  
HETATM 1133  O   HOH A 847      12.166  17.499  24.640  1.00 24.62           O  
HETATM 1134  O   HOH A 848      30.329  16.318   5.742  1.00 35.92           O  
HETATM 1135  O   HOH A 849      30.221  28.551  18.195  1.00 36.76           O  
HETATM 1136  O   HOH A 850      13.408  30.392  15.761  1.00 18.42           O  
HETATM 1137  O   HOH A 851      14.532  31.933   9.164  1.00 21.30           O  
HETATM 1138  O   HOH A 852       5.514  33.762  12.308  1.00 48.34           O  
HETATM 1139  O   HOH A 853      35.483  18.499  19.334  1.00 16.49           O  
HETATM 1140  O   HOH A 854      35.703  25.914  24.704  1.00 47.60           O  
HETATM 1141  O   HOH A 855      28.661  30.006   3.101  1.00 37.06           O  
HETATM 1142  O   HOH A 856       5.901  28.926   6.146  1.00 22.44           O  
HETATM 1143  O   HOH A 857      29.831  31.713  11.335  1.00 20.80           O  
HETATM 1144  O   HOH A 858      28.803  31.483  13.747  1.00 18.85           O  
HETATM 1145  O   HOH A 859      13.858  32.307   5.913  1.00 31.24           O  
HETATM 1146  O   HOH A 860      33.777  14.906   8.963  1.00 29.21           O  
HETATM 1147  O   HOH A 861      30.310  12.551   2.474  1.00 21.92           O  
HETATM 1148  O   HOH A 862       6.004  24.644  -1.056  1.00 45.37           O  
HETATM 1149  O   HOH A 863       6.570  21.498  -0.996  1.00 32.97           O  
HETATM 1150  O   HOH A 864       6.463  15.933  13.906  1.00 36.47           O  
HETATM 1151  O   HOH A 865       4.658  20.225  13.133  1.00 30.34           O  
HETATM 1152  O   HOH A 866      22.446   2.756  13.015  1.00 31.73           O  
HETATM 1153  O   HOH A 867      25.069   1.240  10.549  1.00 22.85           O  
HETATM 1154  O   HOH A 868      11.822   2.601  12.550  1.00 33.32           O  
HETATM 1155  O   HOH A 869      12.915   3.653  15.074  1.00 32.98           O  
HETATM 1156  O   HOH A 870      34.564   7.319  10.150  1.00 21.56           O  
HETATM 1157  O   HOH A 871      28.163   2.079   9.146  1.00 30.35           O  
HETATM 1158  O   HOH A 872      37.481  15.455  15.651  1.00 37.99           O  
HETATM 1159  O   HOH A 873      15.859  37.786  12.433  1.00 22.28           O  
HETATM 1160  O   HOH A 874      12.824  39.027  11.666  1.00 18.97           O  
HETATM 1161  O   HOH A 875      10.552  36.999  14.961  1.00 12.63           O  
HETATM 1162  O   HOH A 876      14.203  34.429   9.061  1.00 27.56           O  
HETATM 1163  O   HOH A 877      19.611  40.365  16.245  1.00 18.10           O  
HETATM 1164  O   HOH A 878      21.438  22.506  30.121  1.00 42.48           O  
HETATM 1165  O   HOH A 879      16.104  31.666   7.072  1.00 12.90           O  
HETATM 1166  O   HOH A 880      38.033  26.974  26.869  1.00 34.34           O  
HETATM 1167  O   HOH A 881      27.825   4.280   3.563  1.00 28.96           O  
HETATM 1168  O   HOH A 882       8.227  30.445  20.561  1.00 20.99           O  
HETATM 1169  O   HOH A 883      16.620   2.219  15.443  1.00 28.07           O  
HETATM 1170  O   HOH A 884       9.513  15.326  13.854  1.00 22.46           O  
HETATM 1171  O   HOH A 885      24.414   6.185  24.123  1.00 25.97           O  
HETATM 1172  O   HOH A 886      27.687  32.444  22.910  1.00 20.94           O  
HETATM 1173  O   HOH A 887      11.174  31.343   2.760  1.00 40.94           O  
HETATM 1174  O   HOH A 888      13.170  29.568  25.286  1.00 20.97           O  
HETATM 1175  O   HOH A 889      30.227   1.348  14.576  1.00 19.19           O  
HETATM 1176  O   HOH A 890      31.888   2.873  17.616  1.00 27.22           O  
HETATM 1177  O   HOH A 891      36.019  12.058  13.633  1.00 21.30           O  
HETATM 1178  O   HOH A 892      14.953  14.194  27.419  1.00 23.72           O  
HETATM 1179  O   HOH A 893      16.187  13.091  29.255  1.00 36.53           O  
CONECT 1075 1076 1080                                                           
CONECT 1076 1075 1077                                                           
CONECT 1077 1076 1078                                                           
CONECT 1078 1077 1079 1081                                                      
CONECT 1079 1078 1080                                                           
CONECT 1080 1075 1079                                                           
CONECT 1081 1078 1082                                                           
CONECT 1082 1081 1083                                                           
CONECT 1083 1082 1084 1085 1086                                                 
CONECT 1084 1083                                                                
CONECT 1085 1083                                                                
CONECT 1086 1083                                                                
MASTER      293    0    1    0   17    0    2    6 1178    1   12   11          
END                                                                             
