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Database: PDB
Entry: 1WPQ
LinkDB: 1WPQ
Original site: 1WPQ 
HEADER    OXIDOREDUCTASE                          10-SEP-04   1WPQ              
TITLE     TERNARY COMPLEX OF GLYCEROL 3-PHOSPHATE DEHYDROGENASE 1               
TITLE    2 WITH NAD AND DIHYDROXYACTONE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD+],                 
COMPND   3 CYTOPLASMIC;                                                         
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: GPD-C, GPDH-C;                                              
COMPND   6 EC: 1.1.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NAD, GPD1, DEHYDROGENASE, DIHYDROXYACTONE COMPLEX,                    
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.OU,X.HAN,Z.RAO                                                      
REVDAT   2   24-FEB-09 1WPQ    1       VERSN                                    
REVDAT   1   11-APR-06 1WPQ    0                                                
JRNL        AUTH   X.OU,C.JI,X.HAN,X.ZHAO,X.LI,Y.MAO,L.L.WONG,                  
JRNL        AUTH 2 M.BARTLAM,Z.RAO                                              
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN GLYCEROL 3-PHOSPHATE             
JRNL        TITL 2 DEHYDROGENASE 1 (GPD1)                                       
JRNL        REF    J.MOL.BIOL.                   V. 357   858 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16460752                                                     
JRNL        DOI    10.1016/J.JMB.2005.12.074                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 34850                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1745                            
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            : 5248                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 143                                     
REMARK   3   SOLVENT ATOMS            : 602                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.31                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023858.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73285                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 500.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-SODIUM CITRATE DEHYDRATE,            
REMARK 280  AMMONIUM SULFATE, LITHIUM SULFATE MONOHYDRATE, PH 5.6, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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 -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       76.86000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       57.99750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       57.99750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      115.29000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       57.99750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       57.99750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       38.43000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       57.99750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.99750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      115.29000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       57.99750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.99750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.43000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       76.86000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 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 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     1                                                      
REMARK 465     MET B     1                                                      
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     PRO A 113    CG   CD                                             
REMARK 470     PRO B 113    CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY B    99     O    HOH B  3050              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  11       32.36   -152.77                                   
REMARK 500    GLU A  84      -58.29    -29.84                                   
REMARK 500    PRO A 126      -75.97    -36.85                                   
REMARK 500    ASN A 293       58.44     29.58                                   
REMARK 500    SER B  11       26.26   -154.45                                   
REMARK 500    GLU B  59      144.43   -170.79                                   
REMARK 500    GLU B  84      -66.79    -22.65                                   
REMARK 500    GLN B  96        2.11    -67.48                                   
REMARK 500    ASP B 103      -80.10    -51.33                                   
REMARK 500    ALA B 111      -72.09    -48.97                                   
REMARK 500    ASN B 112       38.70    -96.61                                   
REMARK 500    PRO B 126      -15.45    -46.66                                   
REMARK 500    ALA B 150       86.72    -68.45                                   
REMARK 500    PRO B 246      129.21    -34.79                                   
REMARK 500    ASN B 293       51.25     34.81                                   
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 SO4 A 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1005                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1006                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P B 2001                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13P A 2002                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 3001                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 3002                
DBREF  1WPQ A    1   349  UNP    P21695   GPDA_HUMAN       1    348             
DBREF  1WPQ B    1   349  UNP    P21695   GPDA_HUMAN       1    348             
SEQRES   1 A  349  MET ALA SER LYS LYS VAL CYS ILE VAL GLY SER GLY ASN          
SEQRES   2 A  349  TRP GLY SER ALA ILE ALA LYS ILE VAL GLY GLY ASN ALA          
SEQRES   3 A  349  ALA GLN LEU ALA GLN PHE ASP PRO ARG VAL THR MET TRP          
SEQRES   4 A  349  VAL PHE GLU GLU ASP ILE GLY GLY LYS LYS LEU THR GLU          
SEQRES   5 A  349  ILE ILE ASN THR GLN HIS GLU ASN VAL LYS TYR LEU PRO          
SEQRES   6 A  349  GLY HIS LYS LEU PRO PRO ASN VAL VAL ALA VAL PRO ASP          
SEQRES   7 A  349  VAL VAL GLN ALA ALA GLU ASP ALA ASP ILE LEU ILE PHE          
SEQRES   8 A  349  VAL VAL PRO HIS GLN PHE ILE GLY LYS ILE CYS ASP GLN          
SEQRES   9 A  349  LEU LYS GLY HIS LEU LYS ALA ASN PRO THR GLY ILE SER          
SEQRES  10 A  349  LEU ILE LYS GLY VAL ASP GLU GLY PRO ASN GLY LEU LYS          
SEQRES  11 A  349  LEU ILE SER GLU VAL ILE GLY GLU ARG LEU GLY ILE PRO          
SEQRES  12 A  349  MET SER VAL LEU MET GLY ALA ASN ILE ALA SER GLU VAL          
SEQRES  13 A  349  ALA ASP GLU LYS PHE CYS GLU THR THR ILE GLY CYS LYS          
SEQRES  14 A  349  ASP PRO ALA GLN GLY GLN LEU LEU LYS GLU LEU MET GLN          
SEQRES  15 A  349  THR PRO ASN PHE ARG ILE THR VAL VAL GLN GLU VAL ASP          
SEQRES  16 A  349  THR VAL GLU ILE CYS GLY ALA LEU LYS ASN VAL VAL ALA          
SEQRES  17 A  349  VAL GLY ALA GLY PHE CYS ASP GLY LEU GLY PHE GLY ASP          
SEQRES  18 A  349  ASN THR LYS ALA ALA VAL ILE ARG LEU GLY LEU MET GLU          
SEQRES  19 A  349  MET ILE ALA PHE ALA LYS LEU PHE CYS SER GLY PRO VAL          
SEQRES  20 A  349  SER SER ALA THR PHE LEU GLU SER CYS GLY VAL ALA ASP          
SEQRES  21 A  349  LEU ILE THR THR CYS TYR GLY GLY ARG ASN ARG LYS VAL          
SEQRES  22 A  349  ALA GLU ALA PHE ALA ARG THR GLY LYS SER ILE GLU GLN          
SEQRES  23 A  349  LEU GLU LYS GLU LEU LEU ASN GLY GLN LYS LEU GLN GLY          
SEQRES  24 A  349  PRO GLU THR ALA ARG GLU LEU TYR SER ILE LEU GLN HIS          
SEQRES  25 A  349  LYS GLY LEU VAL ASP LYS PHE PRO LEU PHE MET ALA VAL          
SEQRES  26 A  349  TYR LYS VAL CYS TYR GLU GLY GLN PRO VAL GLY GLU PHE          
SEQRES  27 A  349  ILE HIS CYS LEU GLN ASN HIS PRO GLU HIS MET                  
SEQRES   1 B  349  MET ALA SER LYS LYS VAL CYS ILE VAL GLY SER GLY ASN          
SEQRES   2 B  349  TRP GLY SER ALA ILE ALA LYS ILE VAL GLY GLY ASN ALA          
SEQRES   3 B  349  ALA GLN LEU ALA GLN PHE ASP PRO ARG VAL THR MET TRP          
SEQRES   4 B  349  VAL PHE GLU GLU ASP ILE GLY GLY LYS LYS LEU THR GLU          
SEQRES   5 B  349  ILE ILE ASN THR GLN HIS GLU ASN VAL LYS TYR LEU PRO          
SEQRES   6 B  349  GLY HIS LYS LEU PRO PRO ASN VAL VAL ALA VAL PRO ASP          
SEQRES   7 B  349  VAL VAL GLN ALA ALA GLU ASP ALA ASP ILE LEU ILE PHE          
SEQRES   8 B  349  VAL VAL PRO HIS GLN PHE ILE GLY LYS ILE CYS ASP GLN          
SEQRES   9 B  349  LEU LYS GLY HIS LEU LYS ALA ASN PRO THR GLY ILE SER          
SEQRES  10 B  349  LEU ILE LYS GLY VAL ASP GLU GLY PRO ASN GLY LEU LYS          
SEQRES  11 B  349  LEU ILE SER GLU VAL ILE GLY GLU ARG LEU GLY ILE PRO          
SEQRES  12 B  349  MET SER VAL LEU MET GLY ALA ASN ILE ALA SER GLU VAL          
SEQRES  13 B  349  ALA ASP GLU LYS PHE CYS GLU THR THR ILE GLY CYS LYS          
SEQRES  14 B  349  ASP PRO ALA GLN GLY GLN LEU LEU LYS GLU LEU MET GLN          
SEQRES  15 B  349  THR PRO ASN PHE ARG ILE THR VAL VAL GLN GLU VAL ASP          
SEQRES  16 B  349  THR VAL GLU ILE CYS GLY ALA LEU LYS ASN VAL VAL ALA          
SEQRES  17 B  349  VAL GLY ALA GLY PHE CYS ASP GLY LEU GLY PHE GLY ASP          
SEQRES  18 B  349  ASN THR LYS ALA ALA VAL ILE ARG LEU GLY LEU MET GLU          
SEQRES  19 B  349  MET ILE ALA PHE ALA LYS LEU PHE CYS SER GLY PRO VAL          
SEQRES  20 B  349  SER SER ALA THR PHE LEU GLU SER CYS GLY VAL ALA ASP          
SEQRES  21 B  349  LEU ILE THR THR CYS TYR GLY GLY ARG ASN ARG LYS VAL          
SEQRES  22 B  349  ALA GLU ALA PHE ALA ARG THR GLY LYS SER ILE GLU GLN          
SEQRES  23 B  349  LEU GLU LYS GLU LEU LEU ASN GLY GLN LYS LEU GLN GLY          
SEQRES  24 B  349  PRO GLU THR ALA ARG GLU LEU TYR SER ILE LEU GLN HIS          
SEQRES  25 B  349  LYS GLY LEU VAL ASP LYS PHE PRO LEU PHE MET ALA VAL          
SEQRES  26 B  349  TYR LYS VAL CYS TYR GLU GLY GLN PRO VAL GLY GLU PHE          
SEQRES  27 B  349  ILE HIS CYS LEU GLN ASN HIS PRO GLU HIS MET                  
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  A1004       5                                                       
HET    SO4  B1005       5                                                       
HET    SO4  A1006       5                                                       
HET    SO4  A1007       5                                                       
HET    13P  B2001      10                                                       
HET    13P  A2002      10                                                       
HET    NAD  A3001      44                                                       
HET    NAD  B3002      44                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     13P 1,3-DIHYDROXYACETONEPHOSPHATE                                    
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  SO4    7(O4 S 2-)                                                   
FORMUL  10  13P    2(C3 H7 O6 P)                                                
FORMUL  12  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL  14  HOH   *602(H2 O)                                                    
HELIX    1   1 GLY A   12  LEU A   29  1                                  18    
HELIX    2   2 LEU A   50  HIS A   58  1                                   9    
HELIX    3   3 ASP A   78  GLU A   84  1                                   7    
HELIX    4   4 PRO A   94  GLN A   96  5                                   3    
HELIX    5   5 PHE A   97  LYS A  106  1                                  10    
HELIX    6   6 ILE A  132  GLY A  141  1                                  10    
HELIX    7   7 ILE A  152  ASP A  158  1                                   7    
HELIX    8   8 ASP A  170  GLN A  182  1                                  13    
HELIX    9   9 GLU A  193  LEU A  217  1                                  25    
HELIX   10  10 GLY A  220  CYS A  243  1                                  24    
HELIX   11  11 SER A  249  GLU A  254  5                                   6    
HELIX   12  12 GLY A  257  GLY A  268  1                                  12    
HELIX   13  13 GLY A  268  GLY A  281  1                                  14    
HELIX   14  14 SER A  283  LEU A  292  1                                  10    
HELIX   15  15 GLN A  298  GLY A  314  1                                  17    
HELIX   16  16 LEU A  315  LYS A  318  5                                   4    
HELIX   17  17 PHE A  319  GLU A  331  1                                  13    
HELIX   18  18 PRO A  334  GLU A  337  5                                   4    
HELIX   19  19 PHE A  338  ASN A  344  1                                   7    
HELIX   20  20 GLY B   12  LEU B   29  1                                  18    
HELIX   21  21 LEU B   50  HIS B   58  1                                   9    
HELIX   22  22 ASP B   78  GLU B   84  1                                   7    
HELIX   23  23 PRO B   94  LYS B  106  1                                  13    
HELIX   24  24 LEU B  131  LEU B  140  1                                  10    
HELIX   25  25 ILE B  152  ASP B  158  1                                   7    
HELIX   26  26 ASP B  170  GLN B  182  1                                  13    
HELIX   27  27 GLU B  193  LEU B  217  1                                  25    
HELIX   28  28 GLY B  220  CYS B  243  1                                  24    
HELIX   29  29 SER B  248  GLU B  254  5                                   7    
HELIX   30  30 GLY B  257  GLY B  268  1                                  12    
HELIX   31  31 GLY B  268  GLY B  281  1                                  14    
HELIX   32  32 SER B  283  LEU B  292  1                                  10    
HELIX   33  33 GLN B  298  HIS B  312  1                                  15    
HELIX   34  34 LYS B  313  GLY B  314  5                                   2    
HELIX   35  35 LEU B  315  LYS B  318  5                                   4    
HELIX   36  36 PHE B  319  GLU B  331  1                                  13    
HELIX   37  37 PRO B  334  GLY B  336  5                                   3    
HELIX   38  38 GLU B  337  ASN B  344  1                                   8    
SHEET    1   A 8 VAL A  73  VAL A  76  0                                        
SHEET    2   A 8 PHE A  32  TRP A  39  1  N  MET A  38   O  VAL A  76           
SHEET    3   A 8 LYS A   4  VAL A   9  1  N  ILE A   8   O  THR A  37           
SHEET    4   A 8 ILE A  88  PHE A  91  1  O  ILE A  90   N  VAL A   9           
SHEET    5   A 8 THR A 114  SER A 117  1  O  ILE A 116   N  PHE A  91           
SHEET    6   A 8 MET A 144  MET A 148  1  O  SER A 145   N  SER A 117           
SHEET    7   A 8 CYS A 162  GLY A 167 -1  O  THR A 165   N  MET A 148           
SHEET    8   A 8 PHE A 186  VAL A 191  1  O  THR A 189   N  ILE A 166           
SHEET    1   B 2 ASP A  44  ILE A  45  0                                        
SHEET    2   B 2 LYS A  48  LYS A  49 -1  O  LYS A  48   N  ILE A  45           
SHEET    1   C 2 VAL A 122  GLY A 125  0                                        
SHEET    2   C 2 GLY A 128  LEU A 131 -1  O  GLY A 128   N  GLY A 125           
SHEET    1   D 8 VAL B  73  VAL B  76  0                                        
SHEET    2   D 8 PHE B  32  TRP B  39  1  N  VAL B  36   O  VAL B  74           
SHEET    3   D 8 LYS B   4  VAL B   9  1  N  LYS B   4   O  ASP B  33           
SHEET    4   D 8 ILE B  88  PHE B  91  1  O  ILE B  90   N  VAL B   9           
SHEET    5   D 8 THR B 114  SER B 117  1  O  ILE B 116   N  PHE B  91           
SHEET    6   D 8 MET B 144  MET B 148  1  O  SER B 145   N  SER B 117           
SHEET    7   D 8 CYS B 162  GLY B 167 -1  O  THR B 165   N  MET B 148           
SHEET    8   D 8 PHE B 186  VAL B 191  1  O  VAL B 191   N  ILE B 166           
SHEET    1   E 2 ASP B  44  ILE B  45  0                                        
SHEET    2   E 2 LYS B  48  LYS B  49 -1  O  LYS B  48   N  ILE B  45           
SHEET    1   F 2 ASP B 123  GLY B 125  0                                        
SHEET    2   F 2 GLY B 128  LYS B 130 -1  O  LYS B 130   N  ASP B 123           
SITE     1 AC1  9 LYS A  20  GLY A  66  HIS A  67  LYS A  68                    
SITE     2 AC1  9 HOH A3042  HOH A3047  HOH A3135  HOH A3175                    
SITE     3 AC1  9 HOH A3245                                                     
SITE     1 AC2  6 HOH A3132  HOH A3195  HOH A3293  LYS B  20                    
SITE     2 AC2  6 HIS B  67  LYS B  68                                          
SITE     1 AC3  3 ARG A 271  LYS A 272  HOH A3214                               
SITE     1 AC4  5 LYS A 178  GLN A 182  ARG A 187  HOH A3102                    
SITE     2 AC4  5 HOH A3256                                                     
SITE     1 AC5  5 LYS B 240  VAL B 247  SER B 248  SER B 249                    
SITE     2 AC5  5 HOH B3102                                                     
SITE     1 AC6  5 VAL A 247  SER A 248  HOH A3003  HOH A3033                    
SITE     2 AC6  5 HOH A3288                                                     
SITE     1 AC7  5 PRO A 346  GLU A 347  HIS A 348  HOH A3101                    
SITE     2 AC7  5 HOH A3149                                                     
SITE     1 AC8 12 LYS B 120  LYS B 204  ASN B 205  THR B 264                    
SITE     2 AC8 12 GLY B 268  ARG B 269  ASN B 270  NAD B3002                    
SITE     3 AC8 12 HOH B3012  HOH B3013  HOH B3161  HOH B3191                    
SITE     1 AC9 15 LYS A 120  GLY A 149  LYS A 204  ASN A 205                    
SITE     2 AC9 15 ASP A 260  THR A 264  GLY A 268  ARG A 269                    
SITE     3 AC9 15 ASN A 270  NAD A3001  HOH A3005  HOH A3037                    
SITE     4 AC9 15 HOH A3058  HOH A3136  HOH A3197                               
SITE     1 BC1 27 SER A  11  GLY A  12  ASN A  13  TRP A  14                    
SITE     2 BC1 27 GLY A  15  PHE A  41  TYR A  63  VAL A  92                    
SITE     3 BC1 27 PRO A  94  PHE A  97  LEU A 118  LYS A 120                    
SITE     4 BC1 27 ASN A 151  ILE A 152  ALA A 153  ARG A 269                    
SITE     5 BC1 27 GLY A 294  GLN A 295  LYS A 296  GLN A 298                    
SITE     6 BC1 27 13P A2002  HOH A3026  HOH A3038  HOH A3054                    
SITE     7 BC1 27 HOH A3056  HOH A3058  HOH A3197                               
SITE     1 BC2 28 SER B  11  GLY B  12  ASN B  13  TRP B  14                    
SITE     2 BC2 28 GLY B  15  PHE B  41  TYR B  63  VAL B  93                    
SITE     3 BC2 28 PRO B  94  PHE B  97  LEU B 118  ILE B 119                    
SITE     4 BC2 28 LYS B 120  ASN B 151  ILE B 152  ALA B 153                    
SITE     5 BC2 28 ARG B 269  GLY B 294  GLN B 295  LYS B 296                    
SITE     6 BC2 28 GLN B 298  13P B2001  HOH B3011  HOH B3013                    
SITE     7 BC2 28 HOH B3020  HOH B3023  HOH B3037  HOH B3120                    
CRYST1  115.995  115.995  153.720  90.00  90.00  90.00 P 43 21 2    16          
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      0.008621  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008621  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006505        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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