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Database: PDB
Entry: 1WKL
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Original site: 1WKL 
HEADER    TRANSFERASE                             01-JUN-04   1WKL              
TITLE     CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE FROM THERMUS       
TITLE    2 THERMOPHILUS HB8 IN COMPLEX WITH ATP AND ADP                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOTIDE 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    NUCLEOTIDE DIPHOSPHATE KINASE, COMPLEX WITH ATP AND ADP, REACTION     
KEYWDS   2 INTERMEDIATE, THERMUS THERMOPHILUS 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   4   23-APR-14 1WKL    1       REMARK                                   
REVDAT   3   13-JUL-11 1WKL    1       VERSN                                    
REVDAT   2   24-FEB-09 1WKL    1       VERSN                                    
REVDAT   1   23-AUG-05 1WKL    0                                                
JRNL        AUTH   S.TAKEISHI,N.NAKAGAWA,R.MASUI,S.KURAMITSU                    
JRNL        TITL   CRYSTAL STRUCTURE OF NUCLEOSIDE DIPHOSPHATE KINASE FROM      
JRNL        TITL 2 THERMUS THERMOPHILUS HB8                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
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)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23548                          
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2326                            
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          : 63                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.25900                                             
REMARK   3    B22 (A**2) : -2.25900                                             
REMARK   3    B33 (A**2) : 4.51800                                              
REMARK   3    B12 (A**2) : 1.32500                                              
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
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 1WKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023678.                                      
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                             : 4.5                                
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   : 497844                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 20.300                             
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 72.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
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) : 0.22800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 20.000                             
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: 14% PEG4000, 0.09M AMMONIUM ACETATE,     
REMARK 280  18% GLYCEROL, 0.1M SODIUM CITRATE, PH 4.5, VAPOR DIFFUSION,         
REMARK 280  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       52.74600            
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       52.74600            
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       52.74600            
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       52.74600            
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       52.74600            
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       52.74600            
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 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 AND   
REMARK 300 -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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 15890 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 KCAL/MOL                       
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       61.44850            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -61.44850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 35900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -279.0 KCAL/MOL                       
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       61.44850            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -61.44850            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000       61.44850            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      158.23800            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      158.23800            
REMARK 350   BIOMT1   6  0.500000  0.866025  0.000000      -61.44850            
REMARK 350   BIOMT2   6  0.866025 -0.500000  0.000000      106.43192            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      158.23800            
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      141.47   -172.47                                   
REMARK 500    LYS A  55      167.09    -48.92                                   
REMARK 500    VAL A 113      -40.36     58.27                                   
REMARK 500    LYS B  36      145.09   -171.24                                   
REMARK 500    PRO B  56      -79.22    -87.16                                   
REMARK 500    PHE B  57       -2.91    -47.62                                   
REMARK 500    ASN B 112       31.05    -96.00                                   
REMARK 500    VAL B 113      -37.14     56.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 900  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B 856   O3G                                                    
REMARK 620 2 GLY B 116   O   116.2                                              
REMARK 620 3 ARG B  85   NH2 116.1  54.4                                        
REMARK 620 4 GLY B 116   N   105.9  55.2 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHS A 138                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 646                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 856                 
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: 1WKK   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH GDP                                  
REMARK 900 RELATED ID: TTK003000088.6   RELATED DB: TARGETDB                    
DBREF  1WKL A    1   137  UNP    Q5SLV5   NDK_THET8        1    137             
DBREF  1WKL 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     MG  B 900       1                                                       
HET    PHS  A 138       4                                                       
HET    ADP  A 646      27                                                       
HET    ATP  B 856      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PHS PHOSPHONIC ACID                                                  
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  PHS    H3 O3 P                                                      
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  ATP    C10 H16 N5 O13 P3                                            
FORMUL   7  HOH   *89(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 HIS A   92  ALA A   96  5                                   5    
HELIX    8   8 THR A  100  ALA A  106  1                                   7    
HELIX    9   9 THR A  119  PHE A  131  1                                  13    
HELIX   10  10 ARG A  132  LEU A  136  5                                   5    
HELIX   11  11 LYS B    9  ARG B   15  1                                   7    
HELIX   12  12 LEU B   17  GLY B   29  1                                  13    
HELIX   13  13 SER B   41  TYR B   49  1                                   9    
HELIX   14  14 GLU B   51  LYS B   55  5                                   5    
HELIX   15  15 PHE B   57  THR B   66  1                                  10    
HELIX   16  16 GLY B   79  GLY B   89  1                                  11    
HELIX   17  17 HIS B   92  ALA B   96  5                                   5    
HELIX   18  18 THR B  100  ALA B  106  1                                   7    
HELIX   19  19 THR B  119  PHE B  131  1                                  13    
HELIX   20  20 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  ILE A   8   O  VAL A  71           
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           
LINK         O3G ATP B 856                MG    MG B 900     1555   1555  1.84  
LINK        MG    MG B 900                 O   GLY B 116     1555   1555  3.09  
LINK        MG    MG B 900                 NH2 ARG B  85     1555   1555  3.11  
LINK        MG    MG B 900                 N   GLY B 116     1555   1555  2.82  
SITE     1 AC1  6 ARG B  85  MET B  88  ARG B 102  HIS B 115                    
SITE     2 AC1  6 GLY B 116  ATP B 856                                          
SITE     1 AC2  6 MET A   7  LYS A   9  HIS A  48  TYR A  49                    
SITE     2 AC2  6 HIS A 115  ADP A 646                                          
SITE     1 AC3 11 LYS A   9  TYR A  49  HIS A  52  PHE A  57                    
SITE     2 AC3 11 ARG A  85  THR A  91  ARG A 102  ILE A 109                    
SITE     3 AC3 11 ASP A 110  ASN A 112  PHS A 138                               
SITE     1 AC4 11 LYS B   9  HIS B  52  PHE B  57  LEU B  61                    
SITE     2 AC4 11 ARG B  85  THR B  91  ILE B 109  ASP B 110                    
SITE     3 AC4 11 HIS B 115   MG B 900  HOH B 927                               
CRYST1  122.897  122.897  105.492  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      0.008137  0.004698  0.000000        0.00000                         
SCALE2      0.000000  0.009396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009479        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system