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Database: PDB
Entry: 1WKK
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Original site: 1WKK 
HEADER    TRANSFERASE                             01-JUN-04   1WKK              
TITLE     CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE FROM               
TITLE    2 THERMUS THERMOPHILUS HB8 IN COMPLEX WITH GDP                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.4.6;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 274;                                                 
SOURCE   4 GENE: NDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    NUCLEOSIDE DIPHOSPHATE KINASE, COMPLEX WITH GDP, THERMUS              
KEYWDS   2 THEMOPHILUS HB8, KINASE, RIKEN STRUCTURAL                            
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS,           
KEYWDS   4 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.TAKEISHI,N.NAKAGAWA,R.MASUI,S.KURAMITSU,RIKEN STRUCTURAL            
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
REVDAT   2   24-FEB-09 1WKK    1       VERSN                                    
REVDAT   1   23-AUG-05 1WKK    0                                                
JRNL        AUTH   S.TAKEISHI,N.NAKAGAWA,R.MASUI,S.KURAMITSU                    
JRNL        TITL   CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE           
JRNL        TITL 2 FROM THERMUS THERMOPHILUS HB8                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13048                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1347                            
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            : 2158                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.28200                                             
REMARK   3    B22 (A**2) : -1.28200                                             
REMARK   3    B33 (A**2) : 2.56400                                              
REMARK   3    B12 (A**2) : 2.94900                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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 1WKK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023677.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 161023                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 12.100                             
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 16.200                             
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: PDB ENTRY 1WKJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG4000, 0.09M AMMONIUM              
REMARK 280  ACETATE, 15% GLYCEROL, 0.1M SODIUM CITRATE, 0.001M GTP, PH          
REMARK 280  5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       52.15100            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       52.15100            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.15100            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       52.15100            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       52.15100            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       52.15100            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE      
REMARK 300 DIMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: -Y+1, X-Y+1, Z       
REMARK 300 AND -X+Y, -X+1, Z.                                                   
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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       61.91500            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      107.23993            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -61.91500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      107.23993            
REMARK 350   BIOMT3   3  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    LYS A  36      146.44   -170.57                                   
REMARK 500    ILE A  65       -8.46    -59.86                                   
REMARK 500    PRO A  78      106.87    -51.57                                   
REMARK 500    VAL A 113      -31.28     57.80                                   
REMARK 500    VAL B 113      -27.89     54.88                                   
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 GDP A 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WKJ   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, FREE FORM (NO LIGAND)                              
REMARK 900 RELATED ID: 1WKL   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH ATP AND ADP                         
REMARK 900 RELATED ID: TTK003000088.5   RELATED DB: TARGETDB                    
DBREF  1WKK A    1   137  UNP    Q5SLV5   NDK_THET8        1    137             
DBREF  1WKK B    1   137  UNP    Q5SLV5   NDK_THET8        1    137             
SEQRES   1 A  137  MET GLU ARG THR PHE VAL MET ILE LYS PRO ASP GLY VAL          
SEQRES   2 A  137  ARG ARG GLY LEU VAL GLY GLU ILE LEU ALA ARG PHE GLU          
SEQRES   3 A  137  ARG LYS GLY PHE ARG ILE ALA ALA LEU LYS LEU MET GLN          
SEQRES   4 A  137  ILE SER GLN GLU LEU ALA GLU ARG HIS TYR ALA GLU HIS          
SEQRES   5 A  137  ARG GLU LYS PRO PHE PHE PRO GLY LEU VAL ARG PHE ILE          
SEQRES   6 A  137  THR SER GLY PRO VAL VAL ALA MET VAL LEU GLU GLY PRO          
SEQRES   7 A  137  GLY VAL VAL ALA GLU VAL ARG LYS MET MET GLY ALA THR          
SEQRES   8 A  137  HIS PRO LYS ASP ALA LEU PRO GLY THR ILE ARG GLY ASP          
SEQRES   9 A  137  PHE ALA THR THR ILE ASP GLU ASN VAL ILE HIS GLY SER          
SEQRES  10 A  137  ALA THR LEU GLU ASP ALA GLN ARG GLU ILE ALA LEU PHE          
SEQRES  11 A  137  PHE ARG PRO GLU GLU LEU LEU                                  
SEQRES   1 B  137  MET GLU ARG THR PHE VAL MET ILE LYS PRO ASP GLY VAL          
SEQRES   2 B  137  ARG ARG GLY LEU VAL GLY GLU ILE LEU ALA ARG PHE GLU          
SEQRES   3 B  137  ARG LYS GLY PHE ARG ILE ALA ALA LEU LYS LEU MET GLN          
SEQRES   4 B  137  ILE SER GLN GLU LEU ALA GLU ARG HIS TYR ALA GLU HIS          
SEQRES   5 B  137  ARG GLU LYS PRO PHE PHE PRO GLY LEU VAL ARG PHE ILE          
SEQRES   6 B  137  THR SER GLY PRO VAL VAL ALA MET VAL LEU GLU GLY PRO          
SEQRES   7 B  137  GLY VAL VAL ALA GLU VAL ARG LYS MET MET GLY ALA THR          
SEQRES   8 B  137  HIS PRO LYS ASP ALA LEU PRO GLY THR ILE ARG GLY ASP          
SEQRES   9 B  137  PHE ALA THR THR ILE ASP GLU ASN VAL ILE HIS GLY SER          
SEQRES  10 B  137  ALA THR LEU GLU ASP ALA GLN ARG GLU ILE ALA LEU PHE          
SEQRES  11 B  137  PHE ARG PRO GLU GLU LEU LEU                                  
HET    GDP  A1001      28                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4  HOH   *49(H2 O)                                                     
HELIX    1   1 LYS A    9  ARG A   15  1                                   7    
HELIX    2   2 LEU A   17  GLY A   29  1                                  13    
HELIX    3   3 SER A   41  TYR A   49  1                                   9    
HELIX    4   4 ALA A   50  ARG A   53  5                                   4    
HELIX    5   5 PHE A   57  THR A   66  1                                  10    
HELIX    6   6 GLY A   79  GLY A   89  1                                  11    
HELIX    7   7 THR A  100  ALA A  106  1                                   7    
HELIX    8   8 THR A  119  PHE A  131  1                                  13    
HELIX    9   9 ARG A  132  LEU A  136  5                                   5    
HELIX   10  10 LYS B    9  ARG B   15  1                                   7    
HELIX   11  11 LEU B   17  GLY B   29  1                                  13    
HELIX   12  12 SER B   41  TYR B   49  1                                   9    
HELIX   13  13 ALA B   50  LYS B   55  5                                   6    
HELIX   14  14 PHE B   57  THR B   66  1                                  10    
HELIX   15  15 GLY B   79  GLY B   89  1                                  11    
HELIX   16  16 HIS B   92  ALA B   96  5                                   5    
HELIX   17  17 THR B  100  ALA B  106  1                                   7    
HELIX   18  18 THR B  119  PHE B  131  1                                  13    
HELIX   19  19 ARG B  132  LEU B  136  5                                   5    
SHEET    1   A 4 ARG A  31  MET A  38  0                                        
SHEET    2   A 4 VAL A  70  GLU A  76 -1  O  VAL A  70   N  MET A  38           
SHEET    3   A 4 ARG A   3  ILE A   8 -1  N  VAL A   6   O  MET A  73           
SHEET    4   A 4 ILE A 114  GLY A 116 -1  O  HIS A 115   N  MET A   7           
SHEET    1   B 4 ARG B  31  MET B  38  0                                        
SHEET    2   B 4 VAL B  70  GLU B  76 -1  O  VAL B  70   N  MET B  38           
SHEET    3   B 4 ARG B   3  ILE B   8 -1  N  ILE B   8   O  VAL B  71           
SHEET    4   B 4 ILE B 114  GLY B 116 -1  O  HIS B 115   N  MET B   7           
SITE     1 AC1 12 LYS A   9  TYR A  49  HIS A  52  PHE A  57                    
SITE     2 AC1 12 LEU A  61  ARG A  85  THR A  91  ILE A 109                    
SITE     3 AC1 12 ASP A 110  ASN A 112  HIS A 115  HOH A1005                    
CRYST1  123.830  123.830  104.302  90.00  90.00 120.00 P 63 2 2     24          
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      0.008076  0.004662  0.000000        0.00000                         
SCALE2      0.000000  0.009325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009588        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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