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Database: PDB
Entry: 1X0X
LinkDB: 1X0X
Original site: 1X0X 
HEADER    OXIDOREDUCTASE                          31-MAR-05   1X0X              
TITLE     CO-STRUCTURE OF HOMO SAPIENS GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1     
TITLE    2 COMPLEX WITH NAD                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD+], CYTOPLASMIC;    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GPD-C, GPDH-C;                                              
COMPND   5 EC: 1.1.1.8;                                                         
COMPND   6 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;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DE3(BL21);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    NAD, CO-ENZYME, GPD1, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.RAO,X.OU                                                            
REVDAT   4   13-JUL-11 1X0X    1       VERSN                                    
REVDAT   3   24-FEB-09 1X0X    1       VERSN                                    
REVDAT   2   20-JUN-06 1X0X    1       TITLE                                    
REVDAT   1   11-APR-06 1X0X    0                                                
JRNL        AUTH   X.OU,C.JI,X.HAN,X.ZHAO,X.LI,Y.MAO,L.L.WONG,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   2                                                                      
REMARK   2 RESOLUTION.    2.75 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) : 2.75                           
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             : 13788                          
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) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 656                             
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            : 2638                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 210                                     
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) : 0.120                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.59                            
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 1X0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024240.                                      
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26614                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
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) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE DIHYDRATE,       
REMARK 280  0.5M AMMONIUM SULFATE, 1.0M LITHIUM SULFATE MONOHYDRATE, PH 5.6,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-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       58.29950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       58.29950            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.87100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       38.43550            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       58.29950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      115.30650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      115.30650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.29950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.43550            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       58.29950            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       76.87100            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       58.29950            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       76.87100            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       58.29950            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      115.30650            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       38.43550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       58.29950            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       38.43550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      115.30650            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       58.29950            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       58.29950            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       76.87100            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 7860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL                       
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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       58.29950            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -269.04850            
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     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 320   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES          
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    MET A   1      149.59     50.69                                   
REMARK 500    SER A  11       20.52   -158.26                                   
REMARK 500    ASN A  60       67.06   -107.09                                   
REMARK 500    LYS A 106      120.40    -39.97                                   
REMARK 500    PRO A 126      -19.90    -45.90                                   
REMARK 500    ASN A 127       78.10   -150.72                                   
REMARK 500    ASN A 293       47.30     33.17                                   
REMARK 500    HIS A 312        3.52    -67.59                                   
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 A2187        DISTANCE =  5.04 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 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WPQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HOMO SAPIENS GLYCEROL-3-PHOSPHATE               
REMARK 900 DEHYDROGENASE 1 COMPLEXED WITH NAD AND HIHYDROXYACTONE               
REMARK 900 RELATED ID: 1X0V   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HOMO SAPIENS GLYCEROL-3-PHOSPHATE               
REMARK 900 DEHYDROGENASE 1                                                      
DBREF  1X0X A    1   349  UNP    P21695   GPDA_HUMAN       1    349             
SEQADV 1X0X GLY A   -4  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0X PRO A   -3  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0X LEU A   -2  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0X GLY A   -1  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0X SER A    0  UNP  P21695              CLONING ARTIFACT               
SEQRES   1 A  354  GLY PRO LEU GLY SER MET ALA SER LYS LYS VAL CYS ILE          
SEQRES   2 A  354  VAL GLY SER GLY ASN TRP GLY SER ALA ILE ALA LYS ILE          
SEQRES   3 A  354  VAL GLY GLY ASN ALA ALA GLN LEU ALA GLN PHE ASP PRO          
SEQRES   4 A  354  ARG VAL THR MET TRP VAL PHE GLU GLU ASP ILE GLY GLY          
SEQRES   5 A  354  LYS LYS LEU THR GLU ILE ILE ASN THR GLN HIS GLU ASN          
SEQRES   6 A  354  VAL LYS TYR LEU PRO GLY HIS LYS LEU PRO PRO ASN VAL          
SEQRES   7 A  354  VAL ALA VAL PRO ASP VAL VAL GLN ALA ALA GLU ASP ALA          
SEQRES   8 A  354  ASP ILE LEU ILE PHE VAL VAL PRO HIS GLN PHE ILE GLY          
SEQRES   9 A  354  LYS ILE CYS ASP GLN LEU LYS GLY HIS LEU LYS ALA ASN          
SEQRES  10 A  354  ALA THR GLY ILE SER LEU ILE LYS GLY VAL ASP GLU GLY          
SEQRES  11 A  354  PRO ASN GLY LEU LYS LEU ILE SER GLU VAL ILE GLY GLU          
SEQRES  12 A  354  ARG LEU GLY ILE PRO MET SER VAL LEU MET GLY ALA ASN          
SEQRES  13 A  354  ILE ALA SER GLU VAL ALA ASP GLU LYS PHE CYS GLU THR          
SEQRES  14 A  354  THR ILE GLY CYS LYS ASP PRO ALA GLN GLY GLN LEU LEU          
SEQRES  15 A  354  LYS GLU LEU MET GLN THR PRO ASN PHE ARG ILE THR VAL          
SEQRES  16 A  354  VAL GLN GLU VAL ASP THR VAL GLU ILE CYS GLY ALA LEU          
SEQRES  17 A  354  LYS ASN VAL VAL ALA VAL GLY ALA GLY PHE CYS ASP GLY          
SEQRES  18 A  354  LEU GLY PHE GLY ASP ASN THR LYS ALA ALA VAL ILE ARG          
SEQRES  19 A  354  LEU GLY LEU MET GLU MET ILE ALA PHE ALA LYS LEU PHE          
SEQRES  20 A  354  CYS SER GLY PRO VAL SER SER ALA THR PHE LEU GLU SER          
SEQRES  21 A  354  CYS GLY VAL ALA ASP LEU ILE THR THR CYS TYR GLY GLY          
SEQRES  22 A  354  ARG ASN ARG LYS VAL ALA GLU ALA PHE ALA ARG THR GLY          
SEQRES  23 A  354  LYS SER ILE GLU GLN LEU GLU LYS GLU LEU LEU ASN GLY          
SEQRES  24 A  354  GLN LYS LEU GLN GLY PRO GLU THR ALA ARG GLU LEU TYR          
SEQRES  25 A  354  SER ILE LEU GLN HIS LYS GLY LEU VAL ASP LYS PHE PRO          
SEQRES  26 A  354  LEU PHE MET ALA VAL TYR LYS VAL CYS TYR GLU GLY GLN          
SEQRES  27 A  354  PRO VAL GLY GLU PHE ILE HIS CYS LEU GLN ASN HIS PRO          
SEQRES  28 A  354  GLU HIS MET                                                  
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  A1004       5                                                       
HET    SO4  A1005       5                                                       
HET    NAD  A2001      44                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   2  SO4    5(O4 S 2-)                                                   
FORMUL   7  NAD    C21 H27 N7 O14 P2                                            
FORMUL   8  HOH   *210(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 LEU A  131  GLY A  141  1                                  11    
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  248  GLU A  254  5                                   7    
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  HIS A  312  1                                  15    
HELIX   16  16 LYS A  313  GLY A  314  5                                   2    
HELIX   17  17 LEU A  315  LYS A  318  5                                   4    
HELIX   18  18 PHE A  319  TYR A  330  1                                  12    
HELIX   19  19 PRO A  334  GLY A  336  5                                   3    
HELIX   20  20 GLU A  337  ASN A  344  1                                   8    
SHEET    1   A 8 VAL A  73  VAL A  76  0                                        
SHEET    2   A 8 VAL A  36  TRP A  39  1  N  MET A  38   O  VAL A  74           
SHEET    3   A 8 VAL A   6  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  VAL A 191   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 ASP A 123  GLY A 125  0                                        
SHEET    2   C 2 GLY A 128  LYS A 130 -1  O  GLY A 128   N  GLY A 125           
SITE     1 AC1  3 LYS A  20  HIS A  67  LYS A  68                               
SITE     1 AC2 12 LYS A 204  ASN A 205  THR A 264  GLY A 268                    
SITE     2 AC2 12 ARG A 269  ASN A 270  HOH A2010  HOH A2022                    
SITE     3 AC2 12 HOH A2039  HOH A2049  HOH A2076  HOH A2134                    
SITE     1 AC3  6 LYS A 240  VAL A 247  SER A 248  SER A 249                    
SITE     2 AC3  6 HOH A2175  HOH A2179                                          
SITE     1 AC4  3 ARG A 271  LYS A 272  HOH A2017                               
SITE     1 AC5  5 ASN A  13  GLN A 295  HOH A2065  HOH A2096                    
SITE     2 AC5  5 HOH A2211                                                     
SITE     1 AC6 29 SER A  11  GLY A  12  ASN A  13  TRP A  14                    
SITE     2 AC6 29 GLY A  15  PHE A  41  TYR A  63  VAL A  93                    
SITE     3 AC6 29 PRO A  94  PHE A  97  ILE A 119  LYS A 120                    
SITE     4 AC6 29 ASN A 151  ALA A 153  ARG A 269  GLY A 294                    
SITE     5 AC6 29 GLN A 295  LYS A 296  GLN A 298  HOH A2007                    
SITE     6 AC6 29 HOH A2011  HOH A2012  HOH A2022  HOH A2023                    
SITE     7 AC6 29 HOH A2039  HOH A2044  HOH A2087  HOH A2134                    
SITE     8 AC6 29 HOH A2135                                                     
CRYST1  116.599  116.599  153.742  90.00  90.00  90.00 I 41 2 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      0.008576  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006504        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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