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Database: PDB
Entry: 1BDG
LinkDB: 1BDG
Original site: 1BDG 
HEADER    HEXOKINASE                              08-MAY-98   1BDG              
TITLE     HEXOKINASE FROM SCHISTOSOMA MANSONI COMPLEXED WITH GLUCOSE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATP/:D-HEXOSE-6-PHOSPHOTRANSFERASE;                         
COMPND   5 EC: 2.7.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA MANSONI;                            
SOURCE   3 ORGANISM_TAXID: 6183;                                                
SOURCE   4 ORGAN: BLOOD;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HEXOKINASE, PHOSPHOTRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.MULICHAK,R.M.GARAVITO                                             
REVDAT   2   24-FEB-09 1BDG    1       VERSN                                    
REVDAT   1   11-MAY-99 1BDG    0                                                
JRNL        AUTH   A.M.MULICHAK,J.E.WILSON,K.PADMANABHAN,R.M.GARAVITO           
JRNL        TITL   THE STRUCTURE OF MAMMALIAN HEXOKINASE-1.                     
JRNL        REF    NAT.STRUCT.BIOL.              V.   5   555 1998              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9665168                                                      
JRNL        DOI    10.1038/811                                                  
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 65.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 12325                          
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) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 615                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 7                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 55.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1227                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.044                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3352                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 104                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.34                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BDG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NOV-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 153                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MSC FOCUSSING MIRRORS              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1HKG AND YHK PI MUTANT P152K COMPLEX       
REMARK 200  WITH GLC PROVIDED BY H. BARTUNIK                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       51.73333            
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      103.46667            
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       77.60000            
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      129.33333            
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       25.86667            
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       51.73333            
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      103.46667            
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      129.33333            
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       77.60000            
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       25.86667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     THR A   461                                                      
REMARK 465     ARG A   462                                                      
REMARK 465     GLN A   463                                                      
REMARK 465     ASN A   464                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A  13    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A  14    OG                                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 195    CD   CE   NZ                                        
REMARK 470     ASN A 199    CG   OD1  ND2                                       
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     SER A 243    OG                                                  
REMARK 470     ASP A 249    CG   OD1  OD2                                       
REMARK 470     LYS A 290    CG   CD   CE   NZ                                   
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 329    CD   CE   NZ                                        
REMARK 470     ARG A 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 337    CD   NE   CZ   NH1  NH2                             
REMARK 470     HIS A 348    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     LEU A 349    CB   CG   CD1  CD2                                  
REMARK 470     LEU A 350    CB   CG   CD1  CD2                                  
REMARK 470     LYS A 380    CE   NZ                                             
REMARK 470     ASN A 404    CG   OD1  ND2                                       
REMARK 470     SER A 406    OG                                                  
REMARK 470     LYS A 422    CD   CE   NZ                                        
REMARK 470     LYS A 437    CG   CD   CE   NZ                                   
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 447    CG   OD1  OD2                                       
REMARK 470     SER A 449    OG                                                  
REMARK 470     LYS A 451    CD   CE   NZ                                        
REMARK 470     CYS A 460    SG                                                  
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    GLU A  99       98.78   -160.55                                   
REMARK 500    LYS A 103     -168.03   -100.21                                   
REMARK 500    MET A 143       52.58   -148.79                                   
REMARK 500    LYS A 144      -72.42    -77.49                                   
REMARK 500    ASP A 145      -16.47    -49.37                                   
REMARK 500    SER A 155       52.36    -65.24                                   
REMARK 500    LYS A 161       76.75   -117.46                                   
REMARK 500    LYS A 173     -137.41     67.61                                   
REMARK 500    SER A 176       41.24   -163.70                                   
REMARK 500    LYS A 195        2.56    -66.76                                   
REMARK 500    SER A 242       12.73    -69.56                                   
REMARK 500    ASP A 249      174.83     74.15                                   
REMARK 500    PHE A 320       37.78     39.18                                   
REMARK 500    ARG A 321       26.20     49.97                                   
REMARK 500    LEU A 328       16.69    -66.12                                   
REMARK 500    LEU A 339       -9.74    -58.17                                   
REMARK 500    ALA A 347      -72.03    -61.05                                   
REMARK 500    LEU A 349       88.18   -170.82                                   
REMARK 500    LEU A 350       53.46   -105.96                                   
REMARK 500    ARG A 396      -63.27    -95.78                                   
REMARK 500    ASN A 404       -7.64     69.01                                   
REMARK 500    LYS A 422      -13.45     86.39                                   
REMARK 500    ALA A 458       -8.14    -49.01                                   
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 GLC A 501                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 RESIDUE NUMBERING IS BASED ON MAMMALIAN HEXOKINASE TYPE I            
DBREF  1BDG A   11   464  UNP    Q26609   HXK_SCHMA        1    451             
SEQADV 1BDG MET A   43  UNP  Q26609    THR    33 SEQUENCING ERROR               
SEQRES   1 A  451  MET VAL PHE SER ASP GLN GLN LEU PHE GLU LYS VAL VAL          
SEQRES   2 A  451  GLU ILE LEU LYS PRO PHE ASP LEU SER VAL VAL ASP TYR          
SEQRES   3 A  451  GLU GLU ILE CYS ASP ARG MET GLY GLU SER MET ARG LEU          
SEQRES   4 A  451  GLY LEU GLN LYS SER THR ASN GLU LYS SER SER ILE LYS          
SEQRES   5 A  451  MET PHE PRO SER TYR VAL THR LYS THR PRO ASN GLY THR          
SEQRES   6 A  451  GLU THR GLY ASN PHE LEU ALA LEU ASP LEU GLY GLY THR          
SEQRES   7 A  451  ASN TYR ARG VAL LEU SER VAL THR LEU GLU GLY LYS GLY          
SEQRES   8 A  451  LYS SER PRO ARG ILE GLN GLU ARG THR TYR CYS ILE PRO          
SEQRES   9 A  451  ALA GLU LYS MET SER GLY SER GLY THR GLU LEU PHE LYS          
SEQRES  10 A  451  TYR ILE ALA GLU THR LEU ALA ASP PHE LEU GLU ASN ASN          
SEQRES  11 A  451  GLY MET LYS ASP LYS LYS PHE ASP LEU GLY PHE THR PHE          
SEQRES  12 A  451  SER PHE PRO CYS VAL GLN LYS GLY LEU THR HIS ALA THR          
SEQRES  13 A  451  LEU VAL ARG TRP THR LYS GLY PHE SER ALA ASP GLY VAL          
SEQRES  14 A  451  GLU GLY HIS ASN VAL ALA GLU LEU LEU GLN THR GLU LEU          
SEQRES  15 A  451  ASP LYS ARG GLU LEU ASN VAL LYS CYS VAL ALA VAL VAL          
SEQRES  16 A  451  ASN ASP THR VAL GLY THR LEU ALA SER CYS ALA LEU GLU          
SEQRES  17 A  451  ASP PRO LYS CYS ALA VAL GLY LEU ILE VAL GLY THR GLY          
SEQRES  18 A  451  THR ASN VAL ALA TYR ILE GLU ASP SER SER LYS VAL GLU          
SEQRES  19 A  451  LEU MET ASP GLY VAL LYS GLU PRO GLU VAL VAL ILE ASN          
SEQRES  20 A  451  THR GLU TRP GLY ALA PHE GLY GLU LYS GLY GLU LEU ASP          
SEQRES  21 A  451  CYS TRP ARG THR GLN PHE ASP LYS SER MET ASP ILE ASP          
SEQRES  22 A  451  SER LEU HIS PRO GLY LYS GLN LEU TYR GLU LYS MET VAL          
SEQRES  23 A  451  SER GLY MET TYR LEU GLY GLU LEU VAL ARG HIS ILE ILE          
SEQRES  24 A  451  VAL TYR LEU VAL GLU GLN LYS ILE LEU PHE ARG GLY ASP          
SEQRES  25 A  451  LEU PRO GLU ARG LEU LYS VAL ARG ASN SER LEU LEU THR          
SEQRES  26 A  451  ARG TYR LEU THR ASP VAL GLU ARG ASP PRO ALA HIS LEU          
SEQRES  27 A  451  LEU TYR ASN THR HIS TYR MET LEU THR ASP ASP LEU HIS          
SEQRES  28 A  451  VAL PRO VAL VAL GLU PRO ILE ASP ASN ARG ILE VAL ARG          
SEQRES  29 A  451  TYR ALA CYS GLU MET VAL VAL LYS ARG ALA ALA TYR LEU          
SEQRES  30 A  451  ALA GLY ALA GLY ILE ALA CYS ILE LEU ARG ARG ILE ASN          
SEQRES  31 A  451  ARG SER GLU VAL THR VAL GLY VAL ASP GLY SER LEU TYR          
SEQRES  32 A  451  LYS PHE HIS PRO LYS PHE CYS GLU ARG MET THR ASP MET          
SEQRES  33 A  451  VAL ASP LYS LEU LYS PRO LYS ASN THR ARG PHE CYS LEU          
SEQRES  34 A  451  ARG LEU SER GLU ASP GLY SER GLY LYS GLY ALA ALA ALA          
SEQRES  35 A  451  ILE ALA ALA SER CYS THR ARG GLN ASN                          
HET    GLC  A 501      12                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  GLC    C6 H12 O6                                                    
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *104(H2 O)                                                    
HELIX    1   1 ASP A   15  PHE A   29  1                                  15    
HELIX    2   2 VAL A   33  LEU A   51  1                                  19    
HELIX    3   3 LYS A   53  ASN A   56  1                                   4    
HELIX    4   4 ALA A  116  MET A  119  5                                   4    
HELIX    5   5 GLY A  123  ASN A  141  1                                  19    
HELIX    6   6 VAL A  185  ARG A  196  1                                  12    
HELIX    7   7 ASP A  209  GLU A  220  1                                  12    
HELIX    8   8 GLU A  246  MET A  248  5                                   3    
HELIX    9   9 TRP A  261  ALA A  263  5                                   3    
HELIX   10  10 GLN A  276  ASP A  284  1                                   9    
HELIX   11  11 GLU A  294  VAL A  297  1                                   4    
HELIX   12  12 GLY A  299  GLU A  315  1                                  17    
HELIX   13  13 GLU A  326  LYS A  329  5                                   4    
HELIX   14  14 ARG A  337  GLU A  343  1                                   7    
HELIX   15  15 TYR A  351  ASP A  359  1                                   9    
HELIX   16  16 PRO A  365  ILE A  397  1                                  33    
HELIX   17  17 SER A  415  PHE A  419  1                                   5    
HELIX   18  18 PHE A  423  LEU A  434  1                                  12    
HELIX   19  19 SER A  449  SER A  459  1                                  11    
SHEET    1   A 5 VAL A 201  VAL A 207  0                                        
SHEET    2   A 5 PHE A 148  PHE A 154  1  N  PHE A 148   O  LYS A 202           
SHEET    3   A 5 GLY A  78  LEU A  85  1  N  LEU A  81   O  GLY A 151           
SHEET    4   A 5 TYR A  90  LEU A  97 -1  N  LEU A  97   O  GLY A  78           
SHEET    5   A 5 ARG A 106  TYR A 112 -1  N  TYR A 112   O  TYR A  90           
SHEET    1   B 2 CYS A 158  LYS A 161  0                                        
SHEET    2   B 2 HIS A 165  LEU A 168 -1  N  THR A 167   O  VAL A 159           
SHEET    1   C 5 GLU A 254A ASN A 258  0                                        
SHEET    2   C 5 THR A 234  ASP A 241 -1  N  GLU A 240   O  VAL A 255           
SHEET    3   C 5 CYS A 224  VAL A 230 -1  N  ILE A 229   O  ASN A 235           
SHEET    4   C 5 GLU A 407  ASP A 413  1  N  THR A 409   O  ALA A 225           
SHEET    5   C 5 ARG A 440  LEU A 444  1  N  ARG A 440   O  VAL A 408           
SSBOND   1 CYS A  217    CYS A  224                          1555   1555  2.03  
SSBOND   2 CYS A  272    CYS A  272                          1555  12556  2.40  
SITE     1 AC1 14 SER A 155  PHE A 156  PRO A 157  THR A 172                    
SITE     2 AC1 14 LYS A 173  ASN A 208  ASP A 209  ILE A 229                    
SITE     3 AC1 14 GLY A 233  THR A 234  ASN A 235  GLU A 260                    
SITE     4 AC1 14 GLU A 294  HOH A 652                                          
SITE     1 AC2  6 GLY A  87  THR A  88  THR A 232  SER A 415                    
SITE     2 AC2  6 HOH A 630  HOH A 652                                          
SITE     1 AC3  1 ARG A 426                                                     
SITE     1 AC4  4 ARG A  48  LYS A 244  ARG A 396  HOH A 771                    
CRYST1  114.300  114.300  155.200  90.00  90.00 120.00 P 61 2 2     12          
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      0.008749  0.005051  0.000000        0.00000                         
SCALE2      0.000000  0.010102  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006443        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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