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Database: PDB
Entry: 2HUR
LinkDB: 2HUR
Original site: 2HUR 
HEADER    SIGNALING PROTEIN,TRANSFERASE           27-JUL-06   2HUR              
TITLE     ESCHERICHIA COLI NUCLEOSIDE DIPHOSPHATE KINASE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;                             
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: NDK; NDP KINASE; NUCLEOSIDE-2-P KINASE;                     
COMPND   5 EC: 2.7.4.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: NDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJC20                                     
KEYWDS    TYPE II TETRAMER, SIGNALING PROTEIN,TRANSFERASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.MOYNIE,M.-F.GIRAUD,F.GEORGESCAULD,I.LASCU,A.DAUTANT                 
REVDAT   4   13-JUL-11 2HUR    1       VERSN                                    
REVDAT   3   24-FEB-09 2HUR    1       VERSN                                    
REVDAT   2   05-JUN-07 2HUR    1       JRNL                                     
REVDAT   1   10-APR-07 2HUR    0                                                
JRNL        AUTH   L.MOYNIE,M.-F.GIRAUD,F.GEORGESCAULD,I.LASCU,A.DAUTANT        
JRNL        TITL   THE STRUCTURE OF THE ESCHERICHIA COLI NUCLEOSIDE DIPHOSPHATE 
JRNL        TITL 2 KINASE REVEALS A NEW QUATERNARY ARCHITECTURE FOR THIS ENZYME 
JRNL        TITL 3 FAMILY                                                       
JRNL        REF    PROTEINS                      V.  67   755 2007              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17330300                                                     
JRNL        DOI    10.1002/PROT.21316                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   N.ALMAULA,Q.LU,J.DELGADO,S.BELKIN,M.INOUYE                   
REMARK   1  TITL   NUCLEOSIDE DIPHOSPHATE KINASE FROM ESCHERICHIA COLI          
REMARK   1  REF    J.BACTERIOL.                  V. 177  2524 1995              
REMARK   1  REFN                   ISSN 0021-9193                               
REMARK   1  PMID   7730286                                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.L.WILLIAMS,D.A.OREN,S.INOUYE,M.INOUYE,E.ARNOLD             
REMARK   1  TITL   CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE           
REMARK   1  TITL 2 DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE     
REMARK   1  TITL 3 SUBSTRATE AT 2.0 A RESOLUTION                                
REMARK   1  REF    J.MOL.BIOL.                   V. 234  1230 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   8263923                                                      
REMARK   1  DOI    10.1006/JMBI.1993.1673                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.LEBRAS,I.LASCU,M.L.LACOMBE,J.JANIN                         
REMARK   1  TITL   REFINED X-RAY STRUCTURE OF DICTYOSTELIUM DISCOIDEUM          
REMARK   1  TITL 2 NUCLEOSIDE DIPHOSPHATE KINASE AT 1.8 A RESOLUTION.           
REMARK   1  REF    J.MOL.BIOL.                   V. 243   873 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   7966307                                                      
REMARK   1  DOI    10.1006/JMBI.1994.1689                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 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) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2343463.170                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 108681                         
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) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5451                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 16974                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 894                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6492                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 717                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.81000                                             
REMARK   3    B22 (A**2) : 1.33000                                              
REMARK   3    B33 (A**2) : -0.52000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.96000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
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) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 45.02                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038785.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 107.0                              
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108681                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.050                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB FILE 2NCK                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM SULPHATE, 25% PEG 4000    
REMARK 280  0.1 M SODIUM ACETATE/ACETIC ACID, PH 4.6, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.45200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.04750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.45200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.04750            
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, 3, 4, 5                                           
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 -1.000000  0.000000  0.000000      -40.84898            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       96.28089            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 7980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 219  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 261  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 296  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 297  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH E 303  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH F 280  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH F 323  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  37      149.09   -171.23                                   
REMARK 500    GLU A  53       -6.06    -59.54                                   
REMARK 500    GLU A 113       64.13   -106.82                                   
REMARK 500    ASP C  55       81.79    -67.45                                   
REMARK 500    GLU C 113       62.57   -107.98                                   
REMARK 500    GLU D 135      109.11    -41.87                                   
REMARK 500    GLU E 113       62.50   -102.28                                   
REMARK 500    GLU F 135      118.74    -38.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 254        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 281        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B 265        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH B 360        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH C 273        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C 304        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH C 321        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH D 313        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH E 301        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH E 336        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH E 342        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH F 333        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH F 376        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH F 377        DISTANCE =  6.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NCK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYXOCOCCUS XANTHUS NUCLEOSIDE                   
REMARK 900 DIPHOSPHATE KINASE AND ITS INTERACTION WITH A NUCLEOTIDE             
REMARK 900 SUBSTRATE AT 2.0 ANGSTROMS                                           
REMARK 900 RELATED ID: 1NPK   RELATED DB: PDB                                   
REMARK 900 REFINED X-RAY STRUCTURE OF DICTYOSTELIUM NUCLEOSIDE                  
REMARK 900 DIPHOSPHATE KINASE AT 1.8 ANGSTROMS RESOLUTION                       
DBREF  2HUR A    2   143  UNP    P0A763   NDK_ECOLI        1    142             
DBREF  2HUR B    2   143  UNP    P0A763   NDK_ECOLI        1    142             
DBREF  2HUR C    2   143  UNP    P0A763   NDK_ECOLI        1    142             
DBREF  2HUR D    2   143  UNP    P0A763   NDK_ECOLI        1    142             
DBREF  2HUR E    2   143  UNP    P0A763   NDK_ECOLI        1    142             
DBREF  2HUR F    2   143  UNP    P0A763   NDK_ECOLI        1    142             
SEQRES   1 A  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 A  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 A  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 A  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 A  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 A  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 A  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 A  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 A  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 A  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 A  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
SEQRES   1 B  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 B  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 B  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 B  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 B  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 B  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 B  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 B  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 B  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 B  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 B  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
SEQRES   1 C  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 C  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 C  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 C  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 C  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 C  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 C  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 C  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 C  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 C  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 C  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
SEQRES   1 D  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 D  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 D  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 D  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 D  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 D  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 D  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 D  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 D  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 D  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 D  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
SEQRES   1 E  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 E  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 E  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 E  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 E  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 E  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 E  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 E  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 E  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 E  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 E  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
SEQRES   1 F  142  ALA ILE GLU ARG THR PHE SER ILE ILE LYS PRO ASN ALA          
SEQRES   2 F  142  VAL ALA LYS ASN VAL ILE GLY ASN ILE PHE ALA ARG PHE          
SEQRES   3 F  142  GLU ALA ALA GLY PHE LYS ILE VAL GLY THR LYS MET LEU          
SEQRES   4 F  142  HIS LEU THR VAL GLU GLN ALA ARG GLY PHE TYR ALA GLU          
SEQRES   5 F  142  HIS ASP GLY LYS PRO PHE PHE ASP GLY LEU VAL GLU PHE          
SEQRES   6 F  142  MET THR SER GLY PRO ILE VAL VAL SER VAL LEU GLU GLY          
SEQRES   7 F  142  GLU ASN ALA VAL GLN ARG HIS ARG ASP LEU LEU GLY ALA          
SEQRES   8 F  142  THR ASN PRO ALA ASN ALA LEU ALA GLY THR LEU ARG ALA          
SEQRES   9 F  142  ASP TYR ALA ASP SER LEU THR GLU ASN GLY THR HIS GLY          
SEQRES  10 F  142  SER ASP SER VAL GLU SER ALA ALA ARG GLU ILE ALA TYR          
SEQRES  11 F  142  PHE PHE GLY GLU GLY GLU VAL CYS PRO ARG THR ARG              
HET    SO4  A 200       5                                                       
HET    SO4  B 200       5                                                       
HET    SO4  C 200       5                                                       
HET    SO4  D 200       5                                                       
HET    SO4  E 200       5                                                       
HET    SO4  F 200       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    6(O4 S 2-)                                                   
FORMUL  13  HOH   *717(H2 O)                                                    
HELIX    1   1 LYS A   11  LYS A   17  1ALPHA 0 CHAIN A                    7    
HELIX    2   2 VAL A   19  ALA A   30  1ALPHA 1 CHAIN A                   12    
HELIX    3   3 THR A   43  TYR A   51  1ALPHA A CHAIN A                    9    
HELIX    4   4 ALA A   52  ASP A   55  5                                   4    
HELIX    5   5 PHE A   59  THR A   68  1ALPHA 2 CHAIN A                   10    
HELIX    6   6 ASN A   81  GLY A   91  1ALPHA 3 CHAIN A                   11    
HELIX    7   7 THR A  102  ALA A  108  1ALPHA 3' CHAIN A                   7    
HELIX    8   8 SER A  121  PHE A  133  1ALPHA 4 CHAIN A                   13    
HELIX    9   9 LYS B   11  LYS B   17  1ALPHA 0 CHAIN B                    7    
HELIX   10  10 VAL B   19  ALA B   30  1ALPHA 1 CHAIN B                   12    
HELIX   11  11 THR B   43  TYR B   51  1ALPHA A CHAIN B                    9    
HELIX   12  12 ALA B   52  ASP B   55  5                                   4    
HELIX   13  13 PHE B   59  THR B   68  1ALPHA 2 CHAIN B                   10    
HELIX   14  14 ASN B   81  GLY B   91  1ALPHA 3 CHAIN B                   11    
HELIX   15  15 THR B  102  ALA B  108  1ALPHA 3' CHAIN B                   7    
HELIX   16  16 SER B  121  PHE B  133  1ALPHA 4 CHAIN B                   13    
HELIX   17  17 LYS C   11  LYS C   17  1ALPHA 0 CHAIN C                    7    
HELIX   18  18 VAL C   19  ALA C   30  1ALPHA 1 CHAIN C                   12    
HELIX   19  19 THR C   43  TYR C   51  1ALPHA A CHAIN C                    9    
HELIX   20  20 ALA C   52  ASP C   55  5                                   4    
HELIX   21  21 PHE C   59  THR C   68  1ALPHA 2 CHAIN C                   10    
HELIX   22  22 ASN C   81  GLY C   91  1ALPHA 3 CHAIN C                   11    
HELIX   23  23 THR C  102  ALA C  108  1ALPHA 3' CHAIN C                   7    
HELIX   24  24 SER C  121  PHE C  133  1ALPHA 4 CHAIN C                   13    
HELIX   25  25 LYS D   11  LYS D   17  1ALPHA 0 CHAIN D                    7    
HELIX   26  26 VAL D   19  ALA D   30  1ALPHA 1 CHAIN D                   12    
HELIX   27  27 THR D   43  TYR D   51  1ALPHA A CHAIN D                    9    
HELIX   28  28 ALA D   52  ASP D   55  5                                   4    
HELIX   29  29 PHE D   59  THR D   68  1ALPHA 2 CHAIN D                   10    
HELIX   30  30 ASN D   81  GLY D   91  1ALPHA 3 CHAIN D                   11    
HELIX   31  31 ASN D   94  ALA D   98  5                                   5    
HELIX   32  32 THR D  102  ALA D  108  1ALPHA 3' CHAIN D                   7    
HELIX   33  33 SER D  121  PHE D  133  1ALPHA 4 CHAIN D                   13    
HELIX   34  34 LYS E   11  LYS E   17  1ALPHA 0 CHAIN E                    7    
HELIX   35  35 VAL E   19  ALA E   30  1ALPHA 1 CHAIN E                   12    
HELIX   36  36 THR E   43  TYR E   51  1ALPHA A CHAIN E                    9    
HELIX   37  37 ALA E   52  ASP E   55  5                                   4    
HELIX   38  38 PHE E   59  THR E   68  1ALPHA 2 CHAIN E                   10    
HELIX   39  39 ASN E   81  GLY E   91  1ALPHA 3 CHAIN E                   11    
HELIX   40  40 THR E  102  ALA E  108  1ALPHA 3' CHAIN E                   7    
HELIX   41  41 SER E  121  PHE E  133  1ALPHA 4 CHAIN E                   13    
HELIX   42  42 LYS F   11  LYS F   17  1ALPHA 0 CHAIN F                    7    
HELIX   43  43 VAL F   19  ALA F   30  1ALPHA 1 CHAIN F                   12    
HELIX   44  44 THR F   43  TYR F   51  1ALPHA A CHAIN F                    9    
HELIX   45  45 ALA F   52  ASP F   55  5                                   4    
HELIX   46  46 PHE F   59  THR F   68  1ALPHA 2 CHAIN F                   10    
HELIX   47  47 ASN F   81  GLY F   91  1ALPHA 3 CHAIN F                   11    
HELIX   48  48 THR F  102  ALA F  108  1ALPHA 3' CHAIN F                   7    
HELIX   49  49 SER F  121  PHE F  133  1ALPHA 4 CHAIN F                   13    
SHEET    1   A 4 LYS A  33  LEU A  40  0                                        
SHEET    2   A 4 ILE A  72  GLU A  80 -1  O  ILE A  72   N  LEU A  40           
SHEET    3   A 4 ILE A   3  ILE A  10 -1  N  GLU A   4   O  GLY A  79           
SHEET    4   A 4 THR A 116  GLY A 118 -1  O  HIS A 117   N  ILE A   9           
SHEET    1   B 4 LYS B  33  LEU B  40  0                                        
SHEET    2   B 4 ILE B  72  GLU B  80 -1  O  ILE B  72   N  LEU B  40           
SHEET    3   B 4 ILE B   3  ILE B  10 -1  N  GLU B   4   O  GLY B  79           
SHEET    4   B 4 THR B 116  GLY B 118 -1  O  HIS B 117   N  ILE B   9           
SHEET    1   C 4 LYS C  33  LEU C  40  0                                        
SHEET    2   C 4 ILE C  72  GLU C  80 -1  O  GLU C  78   N  LYS C  33           
SHEET    3   C 4 ILE C   3  ILE C  10 -1  N  GLU C   4   O  GLY C  79           
SHEET    4   C 4 THR C 116  GLY C 118 -1  O  HIS C 117   N  ILE C   9           
SHEET    1   D 4 LYS D  33  LEU D  40  0                                        
SHEET    2   D 4 ILE D  72  GLU D  80 -1  O  ILE D  72   N  LEU D  40           
SHEET    3   D 4 ILE D   3  ILE D  10 -1  N  SER D   8   O  SER D  75           
SHEET    4   D 4 THR D 116  GLY D 118 -1  O  HIS D 117   N  ILE D   9           
SHEET    1   E 4 LYS E  33  LEU E  40  0                                        
SHEET    2   E 4 ILE E  72  GLU E  80 -1  O  ILE E  72   N  LEU E  40           
SHEET    3   E 4 ILE E   3  ILE E  10 -1  N  ILE E  10   O  VAL E  73           
SHEET    4   E 4 THR E 116  GLY E 118 -1  O  HIS E 117   N  ILE E   9           
SHEET    1   F 4 LYS F  33  LEU F  40  0                                        
SHEET    2   F 4 ILE F  72  GLU F  80 -1  O  ILE F  72   N  LEU F  40           
SHEET    3   F 4 ILE F   3  ILE F  10 -1  N  THR F   6   O  LEU F  77           
SHEET    4   F 4 THR F 116  GLY F 118 -1  O  HIS F 117   N  ILE F   9           
SITE     1 AC1  8 LYS A  11  THR A  93  ARG A 104  ASN A 114                    
SITE     2 AC1  8 HIS A 117  HOH A 226  HOH A 237  HOH A 264                    
SITE     1 AC2  8 LYS B  11  THR B  93  ARG B 104  ASN B 114                    
SITE     2 AC2  8 HIS B 117  HOH B 246  HOH B 276  HOH B 322                    
SITE     1 AC3  7 LYS C  11  THR C  93  ARG C 104  ASN C 114                    
SITE     2 AC3  7 HIS C 117  HOH C 247  HOH C 258                               
SITE     1 AC4 11 LYS D  11  THR D  93  ARG D 104  ASN D 114                    
SITE     2 AC4 11 HIS D 117  HOH D 327  HOH D 334  HOH D 397                    
SITE     3 AC4 11 HOH D 408  HOH D 443  HOH F 360                               
SITE     1 AC5  6 LYS E  11  THR E  93  ARG E 104  ASN E 114                    
SITE     2 AC5  6 HIS E 117  HOH E 287                                          
SITE     1 AC6 11 HOH D 343  LYS F  11  THR F  93  ARG F 104                    
SITE     2 AC6 11 ASN F 114  HIS F 117  HOH F 290  HOH F 302                    
SITE     3 AC6 11 HOH F 329  HOH F 332  HOH F 344                               
CRYST1  118.904   76.095  104.588  90.00 112.99  90.00 C 1 2 1      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      0.008410  0.000000  0.003568        0.00000                         
SCALE2      0.000000  0.013141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010386        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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