GenomeNet

Database: PDB
Entry: 3KQK
LinkDB: 3KQK
Original site: 3KQK 
HEADER    HYDROLASE/DNA                           17-NOV-09   3KQK              
TITLE     THREE CONFORMATIONAL SNAPSHOTS OF THE HEPATITIS C VIRUS NS3 HELICASE  
TITLE    2 REVEAL A RATCHET TRANSLOCATION MECHANISM                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE PROTEASE/NTPASE/HELICASE NS3;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CORE PROTEIN P21, CAPSID PROTEIN C, P21, CORE PROTEIN P19,  
COMPND   5 ENVELOPE GLYCOPROTEIN E1, GP32, GP35, ENVELOPE GLYCOPROTEIN E2, NS1, 
COMPND   6 GP68, GP70, P7, PROTEASE NS2-3, P23, SERINE PROTEASE/NTPASE/HELICASE 
COMPND   7 NS3, HEPACIVIRIN, NS3P, P70, NON-STRUCTURAL PROTEIN 4A, NS4A, P8,    
COMPND   8 NON-STRUCTURAL PROTEIN 4B, NS4B, P27, NON-STRUCTURAL PROTEIN 5A,     
COMPND   9 NS5A, P56, RNA-DIRECTED RNA POLYMERASE, NS5B, P68;                   
COMPND  10 EC: 3.4.21.98, 3.6.1.15, 3.6.1.-;                                    
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: 5'-D(*TP*TP*TP*TP*TP*T)-3';                                
COMPND  14 CHAIN: C, D;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;                              
SOURCE   3 ORGANISM_COMMON: HCV;                                                
SOURCE   4 ORGANISM_TAXID: 333284;                                              
SOURCE   5 STRAIN: CON1;                                                        
SOURCE   6 GENE: NS3;                                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES                                                       
KEYWDS    HELICASE-SUBSTRATE BINARY COMPLEX, HCV, NS3 PROTEIN, HELICASE, DNA-   
KEYWDS   2 BINDING, HYDROLASE-DNA COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GU,C.M.RICE                                                         
REVDAT   3   21-FEB-24 3KQK    1       REMARK                                   
REVDAT   2   01-NOV-17 3KQK    1       REMARK                                   
REVDAT   1   26-JAN-10 3KQK    0                                                
JRNL        AUTH   M.GU,C.M.RICE                                                
JRNL        TITL   THREE CONFORMATIONAL SNAPSHOTS OF THE HEPATITIS C VIRUS NS3  
JRNL        TITL 2 HELICASE REVEAL A RATCHET TRANSLOCATION MECHANISM.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107   521 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20080715                                                     
JRNL        DOI    10.1073/PNAS.0913380107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 24872                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6550                                    
REMARK   3   NUCLEIC ACID ATOMS       : 234                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.40                          
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 3KQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056322.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28955                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08000                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 22% (V/V) GLYCEROL,    
REMARK 280  10% (W/V) PEG 8000 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.74350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.36950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.69050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.36950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.74350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.69050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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    SER A 208      -47.78   -175.73                                   
REMARK 500    THR A 212      -59.74   -127.95                                   
REMARK 500    VAL A 256      -75.19    -67.06                                   
REMARK 500    ALA A 283      -22.03   -143.40                                   
REMARK 500    CYS A 292        3.22    -61.18                                   
REMARK 500    PHE A 349     -130.95   -119.81                                   
REMARK 500    TYR A 350       58.89   -101.87                                   
REMARK 500    LYS A 380       -9.45    -50.77                                   
REMARK 500    LEU A 384       17.95   -143.05                                   
REMARK 500    SER A 403     -158.71   -141.67                                   
REMARK 500    MET A 415       48.86   -100.11                                   
REMARK 500    ASP A 421       94.82     63.18                                   
REMARK 500    THR A 443     -100.63   -125.65                                   
REMARK 500    LEU A 602       70.89   -115.19                                   
REMARK 500    THR B 206       81.46     48.66                                   
REMARK 500    SER B 208      -57.77   -167.11                                   
REMARK 500    THR B 212      -60.32   -138.21                                   
REMARK 500    SER B 297      -46.94    -29.66                                   
REMARK 500    ALA B 310      -72.73    -44.98                                   
REMARK 500    ASN B 335       45.31   -102.23                                   
REMARK 500    PHE B 349     -108.34   -127.40                                   
REMARK 500    LYS B 360      -80.59    -45.81                                   
REMARK 500    TYR B 392      159.28    177.94                                   
REMARK 500    THR B 411     -148.05    -92.39                                   
REMARK 500    PHE B 418      119.10   -173.11                                   
REMARK 500    LEU B 440       40.13     39.64                                   
REMARK 500    THR B 443      -97.20   -106.03                                   
REMARK 500    ARG B 469     -145.00   -110.38                                   
REMARK 500    PRO B 478      -77.45    -76.04                                   
REMARK 500    PHE B 557       71.91   -114.50                                   
REMARK 500    LYS B 583      -18.03    -48.40                                   
REMARK 500    GLN B 606      -61.70    -94.96                                   
REMARK 500    ASN B 607      169.77    -48.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KQH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3KQL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3KQN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3KQU   RELATED DB: PDB                                   
DBREF  3KQK A  189   624  UNP    Q9WMX2   POLG_HCVCO    1215   1650             
DBREF  3KQK B  189   624  UNP    Q9WMX2   POLG_HCVCO    1215   1650             
DBREF  3KQK C    1     6  PDB    3KQK     3KQK             1      6             
DBREF  3KQK D    1     6  PDB    3KQK     3KQK             1      6             
SEQRES   1 A  436  SER PRO PRO ALA VAL PRO GLN THR PHE GLN VAL ALA HIS          
SEQRES   2 A  436  LEU HIS ALA PRO THR GLY SER GLY LYS SER THR LYS VAL          
SEQRES   3 A  436  PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL LEU VAL          
SEQRES   4 A  436  LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE GLY ALA          
SEQRES   5 A  436  TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN ILE ARG          
SEQRES   6 A  436  THR GLY VAL ARG THR ILE THR THR GLY ALA PRO ILE THR          
SEQRES   7 A  436  TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY GLY CYS          
SEQRES   8 A  436  SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP GLU CYS          
SEQRES   9 A  436  HIS SER THR ASP SER THR THR ILE LEU GLY ILE GLY THR          
SEQRES  10 A  436  VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG LEU VAL          
SEQRES  11 A  436  VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL THR VAL          
SEQRES  12 A  436  PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER SER THR          
SEQRES  13 A  436  GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO ILE GLU          
SEQRES  14 A  436  THR ILE LYS GLY GLY ARG HIS LEU ILE PHE CYS HIS SER          
SEQRES  15 A  436  LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU SER GLY          
SEQRES  16 A  436  LEU GLY LEU ASN ALA VAL ALA TYR TYR ARG GLY LEU ASP          
SEQRES  17 A  436  VAL SER VAL ILE PRO THR SER GLY ASP VAL ILE VAL VAL          
SEQRES  18 A  436  ALA THR ASP ALA LEU MET THR GLY PHE THR GLY ASP PHE          
SEQRES  19 A  436  ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR GLN THR          
SEQRES  20 A  436  VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE GLU THR          
SEQRES  21 A  436  THR THR VAL PRO GLN ASP ALA VAL SER ARG SER GLN ARG          
SEQRES  22 A  436  ARG GLY ARG THR GLY ARG GLY ARG MET GLY ILE TYR ARG          
SEQRES  23 A  436  PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET PHE ASP          
SEQRES  24 A  436  SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY CYS ALA          
SEQRES  25 A  436  TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL ARG LEU          
SEQRES  26 A  436  ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL CYS GLN          
SEQRES  27 A  436  ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR GLY LEU          
SEQRES  28 A  436  THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR LYS GLN          
SEQRES  29 A  436  ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR GLN ALA          
SEQRES  30 A  436  THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO SER TRP          
SEQRES  31 A  436  ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS PRO THR          
SEQRES  32 A  436  LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU GLY ALA          
SEQRES  33 A  436  VAL GLN ASN GLU VAL THR THR THR HIS PRO ILE THR LYS          
SEQRES  34 A  436  TYR ILE MET ALA CYS MET SER                                  
SEQRES   1 B  436  SER PRO PRO ALA VAL PRO GLN THR PHE GLN VAL ALA HIS          
SEQRES   2 B  436  LEU HIS ALA PRO THR GLY SER GLY LYS SER THR LYS VAL          
SEQRES   3 B  436  PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL LEU VAL          
SEQRES   4 B  436  LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE GLY ALA          
SEQRES   5 B  436  TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN ILE ARG          
SEQRES   6 B  436  THR GLY VAL ARG THR ILE THR THR GLY ALA PRO ILE THR          
SEQRES   7 B  436  TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY GLY CYS          
SEQRES   8 B  436  SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP GLU CYS          
SEQRES   9 B  436  HIS SER THR ASP SER THR THR ILE LEU GLY ILE GLY THR          
SEQRES  10 B  436  VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG LEU VAL          
SEQRES  11 B  436  VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL THR VAL          
SEQRES  12 B  436  PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER SER THR          
SEQRES  13 B  436  GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO ILE GLU          
SEQRES  14 B  436  THR ILE LYS GLY GLY ARG HIS LEU ILE PHE CYS HIS SER          
SEQRES  15 B  436  LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU SER GLY          
SEQRES  16 B  436  LEU GLY LEU ASN ALA VAL ALA TYR TYR ARG GLY LEU ASP          
SEQRES  17 B  436  VAL SER VAL ILE PRO THR SER GLY ASP VAL ILE VAL VAL          
SEQRES  18 B  436  ALA THR ASP ALA LEU MET THR GLY PHE THR GLY ASP PHE          
SEQRES  19 B  436  ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR GLN THR          
SEQRES  20 B  436  VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE GLU THR          
SEQRES  21 B  436  THR THR VAL PRO GLN ASP ALA VAL SER ARG SER GLN ARG          
SEQRES  22 B  436  ARG GLY ARG THR GLY ARG GLY ARG MET GLY ILE TYR ARG          
SEQRES  23 B  436  PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET PHE ASP          
SEQRES  24 B  436  SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY CYS ALA          
SEQRES  25 B  436  TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL ARG LEU          
SEQRES  26 B  436  ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL CYS GLN          
SEQRES  27 B  436  ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR GLY LEU          
SEQRES  28 B  436  THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR LYS GLN          
SEQRES  29 B  436  ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR GLN ALA          
SEQRES  30 B  436  THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO SER TRP          
SEQRES  31 B  436  ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS PRO THR          
SEQRES  32 B  436  LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU GLY ALA          
SEQRES  33 B  436  VAL GLN ASN GLU VAL THR THR THR HIS PRO ILE THR LYS          
SEQRES  34 B  436  TYR ILE MET ALA CYS MET SER                                  
SEQRES   1 C    6   DT  DT  DT  DT  DT  DT                                      
SEQRES   1 D    6   DT  DT  DT  DT  DT  DT                                      
FORMUL   5  HOH   *138(H2 O)                                                    
HELIX    1   1 THR A  212  GLN A  221  1                                  10    
HELIX    2   2 SER A  231  GLY A  247  1                                  17    
HELIX    3   3 TYR A  270  ASP A  276  1                                   7    
HELIX    4   4 ASP A  296  GLY A  314  1                                  19    
HELIX    5   5 PRO A  355  ILE A  359  5                                   5    
HELIX    6   6 LYS A  371  GLY A  383  1                                  13    
HELIX    7   7 ASP A  396  ILE A  400  5                                   5    
HELIX    8   8 ASP A  454  GLY A  463  1                                  10    
HELIX    9   9 ASP A  487  TRP A  501  1                                  15    
HELIX   10  10 THR A  505  ASN A  518  1                                  14    
HELIX   11  11 HIS A  528  LEU A  539  1                                  12    
HELIX   12  12 ASP A  543  ALA A  553  1                                  11    
HELIX   13  13 PHE A  557  ALA A  571  1                                  15    
HELIX   14  14 ASP A  579  LEU A  592  5                                  14    
HELIX   15  15 HIS A  613  MET A  623  1                                  11    
HELIX   16  16 SER B  208  SER B  211  5                                   4    
HELIX   17  17 THR B  212  ALA B  220  1                                   9    
HELIX   18  18 SER B  231  HIS B  246  1                                  16    
HELIX   19  19 TYR B  270  ASP B  276  1                                   7    
HELIX   20  20 ASP B  296  GLY B  314  1                                  19    
HELIX   21  21 SER B  370  LEU B  381  1                                  12    
HELIX   22  22 SER B  382  GLY B  385  5                                   4    
HELIX   23  23 ASP B  396  ILE B  400  5                                   5    
HELIX   24  24 ASP B  454  GLY B  463  1                                  10    
HELIX   25  25 ASP B  487  TRP B  501  1                                  15    
HELIX   26  26 THR B  505  THR B  519  1                                  15    
HELIX   27  27 HIS B  528  GLY B  538  1                                  11    
HELIX   28  28 ASP B  543  GLY B  554  1                                  12    
HELIX   29  29 PHE B  557  GLN B  572  1                                  16    
HELIX   30  30 ASP B  579  LYS B  589  5                                  11    
HELIX   31  31 HIS B  613  SER B  624  1                                  12    
SHEET    1   A 7 GLN A 198  HIS A 203  0                                        
SHEET    2   A 7 LEU A 317  THR A 322  1  O  VAL A 318   N  ALA A 200           
SHEET    3   A 7 ILE A 286  CYS A 289  1  N  CYS A 289   O  VAL A 319           
SHEET    4   A 7 VAL A 225  ASN A 229  1  N  LEU A 228   O  ILE A 288           
SHEET    5   A 7 ILE A 265  THR A 269  1  O  THR A 266   N  VAL A 227           
SHEET    6   A 7 ASN A 251  ARG A 253  1  N  ASN A 251   O  TYR A 267           
SHEET    7   A 7 THR A 258  ILE A 259 -1  O  ILE A 259   N  ILE A 252           
SHEET    1   B 6 ILE A 336  ALA A 340  0                                        
SHEET    2   B 6 GLY A 471  PHE A 475  1  O  TYR A 473   N  VAL A 339           
SHEET    3   B 6 SER A 424  ASP A 427  1  N  VAL A 425   O  ARG A 474           
SHEET    4   B 6 ARG A 363  PHE A 367  1  N  LEU A 365   O  ILE A 426           
SHEET    5   B 6 VAL A 406  ALA A 410  1  O  VAL A 408   N  ILE A 366           
SHEET    6   B 6 ALA A 388  TYR A 391  1  N  TYR A 391   O  VAL A 409           
SHEET    1   C 2 THR A 430  ASP A 437  0                                        
SHEET    2   C 2 THR A 445  PRO A 452 -1  O  GLU A 447   N  THR A 435           
SHEET    1   D 2 THR A 596  PRO A 597  0                                        
SHEET    2   D 2 VAL A 609  THR A 610  1  O  THR A 610   N  THR A 596           
SHEET    1   E 7 VAL B 199  HIS B 203  0                                        
SHEET    2   E 7 LEU B 317  THR B 322  1  O  LEU B 320   N  ALA B 200           
SHEET    3   E 7 ILE B 286  ASP B 290  1  N  CYS B 289   O  VAL B 319           
SHEET    4   E 7 VAL B 225  ASN B 229  1  N  LEU B 228   O  ILE B 288           
SHEET    5   E 7 ILE B 265  THR B 269  1  O  THR B 266   N  VAL B 227           
SHEET    6   E 7 ASN B 251  ARG B 253  1  N  ASN B 251   O  TYR B 267           
SHEET    7   E 7 THR B 258  ILE B 259 -1  O  ILE B 259   N  ILE B 252           
SHEET    1   F 6 ILE B 336  ALA B 340  0                                        
SHEET    2   F 6 GLY B 471  PHE B 475  1  O  TYR B 473   N  GLU B 337           
SHEET    3   F 6 SER B 424  ASP B 427  1  N  VAL B 425   O  ILE B 472           
SHEET    4   F 6 ARG B 363  PHE B 367  1  N  LEU B 365   O  ILE B 426           
SHEET    5   F 6 VAL B 406  ALA B 410  1  O  VAL B 408   N  ILE B 366           
SHEET    6   F 6 ALA B 388  TYR B 391  1  N  TYR B 391   O  VAL B 409           
SHEET    1   G 2 THR B 430  ASP B 437  0                                        
SHEET    2   G 2 THR B 445  PRO B 452 -1  O  GLU B 447   N  THR B 435           
SHEET    1   H 2 THR B 596  PRO B 597  0                                        
SHEET    2   H 2 VAL B 609  THR B 610  1  O  THR B 610   N  THR B 596           
CISPEP   1 ASP A  441    PRO A  442          0        -1.10                     
CISPEP   2 ASP B  441    PRO B  442          0         0.66                     
CRYST1   45.487  115.381  198.739  90.00  90.00  90.00 P 21 21 21    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      0.021984  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005032        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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