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Database: PDB
Entry: 1GAD
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HEADER    OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A))    24-OCT-95   1GAD              
TITLE     COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF       
TITLE    2 ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES:          
TITLE    3 IMPLICATION FOR NAD BINDING AND COOPERATIVITY                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE;                
COMPND   3 CHAIN: O, P;                                                         
COMPND   4 EC: 1.2.1.12;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: WILD TYPE, HOLO FORM                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DF221 (GAPDH-);                            
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PBR322;                                   
SOURCE   8 EXPRESSION_SYSTEM_GENE: ESCHERICHIA COLI GAPA                        
KEYWDS    OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A))                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DUEE,L.OLIVIER-DEYRIS,E.FANCHON,C.CORBIER,G.BRANLANT,O.DIDEBERG     
REVDAT   3   13-JUL-11 1GAD    1       VERSN                                    
REVDAT   2   24-FEB-09 1GAD    1       VERSN                                    
REVDAT   1   08-MAR-96 1GAD    0                                                
JRNL        AUTH   E.DUEE,L.OLIVIER-DEYRIS,E.FANCHON,C.CORBIER,G.BRANLANT,      
JRNL        AUTH 2 O.DIDEBERG                                                   
JRNL        TITL   COMPARISON OF THE STRUCTURES OF WILD-TYPE AND A N313T MUTANT 
JRNL        TITL 2 OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE               
JRNL        TITL 3 DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND              
JRNL        TITL 4 COOPERATIVITY.                                               
JRNL        REF    J.MOL.BIOL.                   V. 257   814 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8636984                                                      
JRNL        DOI    10.1006/JMBI.1996.0204                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.OLIVIER,G.BUISSON,E.FANCHON,C.CORBIER,G.BRANLANT,          
REMARK   1  AUTH 2 O.DIDEBERG                                                   
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF 
REMARK   1  TITL 2 ESCHERICHIA COLI GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE    
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  51   245 1995              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.BRANLANT,C.BRANLANT                                        
REMARK   1  TITL   NUCLEOTIDE SEQUENCE OF THE ESCHERICHIA COLI GAP GENE.        
REMARK   1  TITL 2 DIFFERENT EVOLUTIONARY BEHAVIOR OF THE NAD+ BINDING DOMAIN   
REMARK   1  TITL 3 AND OF THE CATALYTIC DOMAIN OF D-GLYCERALDEHYDE-3-PHOSPHATE  
REMARK   1  TITL 4 DEHYDROGENASE                                                
REMARK   1  REF    EUR.J.BIOCHEM.                V. 150    61 1985              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : ARP/WARP, X-PLOR                                     
REMARK   3   AUTHORS     : LAMZIN,PERRAKIS,MORRIS,BRUNGER                       
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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)   (%) : 69.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58328                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 4976                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 290                                     
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.62                            
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  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:                                           
REMARK   3  ATOMS FOR WHICH NO DENSITY WAS OBSERVED IN THE ELECTRON             
REMARK   3  DENSITY MAP WERE GIVEN AN OCCUPANCY OF 0.0.                         
REMARK   4                                                                      
REMARK   4 1GAD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62943                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.8                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: ARP/WARP, X-PLOR                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.09000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.09000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.57000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       94.78000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.57000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       94.78000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.09000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.57000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       94.78000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.09000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.57000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       94.78000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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 300 REMARK: THE MOLECULAR TWO-FOLD SYMMETRY AXIS R COINCIDES WITH A      
REMARK 300 CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS PARALLEL TO THE B            
REMARK 300 AXIS.  THE COMPLETE TETRAMER IS GENERATED FROM THE                   
REMARK 300 ASYMMETRIC UNIT BY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION:          
REMARK 300   - X , Y , 1/2 -Z.                                                  
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 19610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P                                  
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        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.09000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH O 471  LIES ON A SPECIAL POSITION.                          
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS O    2   CE   NZ                                             
REMARK 480     LYS O   21   CE   NZ                                             
REMARK 480     ASP O   36   OD1  OD2                                            
REMARK 480     GLU O   58   CD   OE1  OE2                                       
REMARK 480     LYS O   60   CG   CD   CE   NZ                                   
REMARK 480     ASP O   61   CB   CG   OD1  OD2                                  
REMARK 480     LYS O   69   CD   CE   NZ                                        
REMARK 480     LYS O   70   CD   CE   NZ                                        
REMARK 480     GLU O   76   CG   CD   OE1  OE2                                  
REMARK 480     ARG O   77   CZ   NH1  NH2                                       
REMARK 480     LYS O   83   CD   CE   NZ                                        
REMARK 480     GLU O   86   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU O  103   CG   CD   OE1  OE2                                  
REMARK 480     LYS O  114   CE   NZ                                             
REMARK 480     LYS O  122A  CE   NZ                                             
REMARK 480     HIS O  190   ND1  CD2  CE1  NE2                                  
REMARK 480     LYS O  191   CB   CG   CD   CE   NZ                              
REMARK 480     LYS O  212   CD   CE   NZ                                        
REMARK 480     LYS O  216   NZ                                                  
REMARK 480     LYS O  248   CD   CE   NZ                                        
REMARK 480     GLU O  264   CG   CD   OE1  OE2                                  
REMARK 480     GLU O  266   CG   CD   OE1  OE2                                  
REMARK 480     LYS O  268   NZ                                                  
REMARK 480     LYS O  330   CG   CD   CE   NZ                                   
REMARK 480     THR P    0   OG1  CG2                                            
REMARK 480     ASP P   36   OD1  OD2                                            
REMARK 480     LYS P   69   CD   CE   NZ                                        
REMARK 480     LYS P   70   CD   CE   NZ                                        
REMARK 480     ARG P   77   CZ   NH1  NH2                                       
REMARK 480     LYS P   83   CD   CE   NZ                                        
REMARK 480     GLU P   86   CG   CD   OE1  OE2                                  
REMARK 480     GLU P  103   OE1  OE2                                            
REMARK 480     LYS P  114   CE   NZ                                             
REMARK 480     LYS P  122A  NZ                                                  
REMARK 480     ASN P  124   ND2                                                 
REMARK 480     HIS P  190   CE1  NE2                                            
REMARK 480     LYS P  191   CG   CD   CE   NZ                                   
REMARK 480     LYS P  212   CG   CD   CE   NZ                                   
REMARK 480     LYS P  216   NZ                                                  
REMARK 480     LYS P  248   CE   NZ                                             
REMARK 480     GLU P  266   CG   CD   OE1  OE2                                  
REMARK 480     LYS P  268   CE   NZ                                             
REMARK 480     LYS P  330   CE   NZ                                             
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    ILE P 203   N   -  CA  -  C   ANGL. DEV. = -16.4 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    PHE O   8       52.87    -94.34                                   
REMARK 500    PHE O  99       74.82   -108.59                                   
REMARK 500    THR O 119       39.08    -94.20                                   
REMARK 500    ASP O 123     -146.01   -111.35                                   
REMARK 500    ASN O 133       26.55   -150.64                                   
REMARK 500    ALA O 147     -154.81     59.14                                   
REMARK 500    ASP O 186      109.99    -45.69                                   
REMARK 500    SER O 189       75.97   -161.34                                   
REMARK 500    PRO O 233       52.98    -67.91                                   
REMARK 500    VAL O 237      126.88     81.42                                   
REMARK 500    PHE P   8       54.59    -91.55                                   
REMARK 500    ASP P  32     -160.84   -161.20                                   
REMARK 500    PHE P  99       68.74   -113.86                                   
REMARK 500    ALA P 111        2.66    -67.65                                   
REMARK 500    ASP P 123     -144.26   -120.19                                   
REMARK 500    ASN P 133       29.15   -148.85                                   
REMARK 500    ALA P 147     -153.13     66.23                                   
REMARK 500    SER P 189       74.66   -158.24                                   
REMARK 500    ASP P 192       82.62   -164.51                                   
REMARK 500    PRO P 233       60.80    -69.29                                   
REMARK 500    VAL P 237      127.68     82.81                                   
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 NAD O 336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD P 336                 
DBREF  1GAD O    0   330  UNP    P0A9B2   G3P1_ECOLI       1    330             
DBREF  1GAD P    0   330  UNP    P0A9B2   G3P1_ECOLI       1    330             
SEQRES   1 O  330  THR ILE LYS VAL GLY ILE ASN GLY PHE GLY ARG ILE GLY          
SEQRES   2 O  330  ARG ILE VAL PHE ARG ALA ALA GLN LYS ARG SER ASP ILE          
SEQRES   3 O  330  GLU ILE VAL ALA ILE ASN ASP LEU LEU ASP ALA ASP TYR          
SEQRES   4 O  330  MET ALA TYR MET LEU LYS TYR ASP SER THR HIS GLY ARG          
SEQRES   5 O  330  PHE ASP GLY THR VAL GLU VAL LYS ASP GLY HIS LEU ILE          
SEQRES   6 O  330  VAL ASN GLY LYS LYS ILE ARG VAL THR ALA GLU ARG ASP          
SEQRES   7 O  330  PRO ALA ASN LEU LYS TRP ASP GLU VAL GLY VAL ASP VAL          
SEQRES   8 O  330  VAL ALA GLU ALA THR GLY LEU PHE LEU THR ASP GLU THR          
SEQRES   9 O  330  ALA ARG LYS HIS ILE THR ALA GLY ALA LYS LYS VAL VAL          
SEQRES  10 O  330  MET THR GLY PRO SER LYS ASP ASN THR PRO MET PHE VAL          
SEQRES  11 O  330  LYS GLY ALA ASN PHE ASP LYS TYR ALA GLY GLN ASP ILE          
SEQRES  12 O  330  VAL SER ASN ALA SER CYS THR THR ASN CYS LEU ALA PRO          
SEQRES  13 O  330  LEU ALA LYS VAL ILE ASN ASP ASN PHE GLY ILE ILE GLU          
SEQRES  14 O  330  GLY LEU MET THR THR VAL HIS ALA THR THR ALA THR GLN          
SEQRES  15 O  330  LYS THR VAL ASP GLY PRO SER HIS LYS ASP TRP ARG GLY          
SEQRES  16 O  330  GLY ARG GLY ALA SER GLN ASN ILE ILE PRO SER SER THR          
SEQRES  17 O  330  GLY ALA ALA LYS ALA VAL GLY LYS VAL LEU PRO GLU LEU          
SEQRES  18 O  330  ASN GLY LYS LEU THR GLY MET ALA PHE ARG VAL PRO THR          
SEQRES  19 O  330  PRO ASN VAL SER VAL VAL ASP LEU THR VAL ARG LEU GLU          
SEQRES  20 O  330  LYS ALA ALA THR TYR GLU GLN ILE LYS ALA ALA VAL LYS          
SEQRES  21 O  330  ALA ALA ALA GLU GLY GLU MET LYS GLY VAL LEU GLY TYR          
SEQRES  22 O  330  THR GLU ASP ASP VAL VAL SER THR ASP PHE ASN GLY GLU          
SEQRES  23 O  330  VAL CYS THR SER VAL PHE ASP ALA LYS ALA GLY ILE ALA          
SEQRES  24 O  330  LEU ASN ASP ASN PHE VAL LYS LEU VAL SER TRP TYR ASP          
SEQRES  25 O  330  ASN GLU THR GLY TYR SER ASN LYS VAL LEU ASP LEU ILE          
SEQRES  26 O  330  ALA HIS ILE SER LYS                                          
SEQRES   1 P  330  THR ILE LYS VAL GLY ILE ASN GLY PHE GLY ARG ILE GLY          
SEQRES   2 P  330  ARG ILE VAL PHE ARG ALA ALA GLN LYS ARG SER ASP ILE          
SEQRES   3 P  330  GLU ILE VAL ALA ILE ASN ASP LEU LEU ASP ALA ASP TYR          
SEQRES   4 P  330  MET ALA TYR MET LEU LYS TYR ASP SER THR HIS GLY ARG          
SEQRES   5 P  330  PHE ASP GLY THR VAL GLU VAL LYS ASP GLY HIS LEU ILE          
SEQRES   6 P  330  VAL ASN GLY LYS LYS ILE ARG VAL THR ALA GLU ARG ASP          
SEQRES   7 P  330  PRO ALA ASN LEU LYS TRP ASP GLU VAL GLY VAL ASP VAL          
SEQRES   8 P  330  VAL ALA GLU ALA THR GLY LEU PHE LEU THR ASP GLU THR          
SEQRES   9 P  330  ALA ARG LYS HIS ILE THR ALA GLY ALA LYS LYS VAL VAL          
SEQRES  10 P  330  MET THR GLY PRO SER LYS ASP ASN THR PRO MET PHE VAL          
SEQRES  11 P  330  LYS GLY ALA ASN PHE ASP LYS TYR ALA GLY GLN ASP ILE          
SEQRES  12 P  330  VAL SER ASN ALA SER CYS THR THR ASN CYS LEU ALA PRO          
SEQRES  13 P  330  LEU ALA LYS VAL ILE ASN ASP ASN PHE GLY ILE ILE GLU          
SEQRES  14 P  330  GLY LEU MET THR THR VAL HIS ALA THR THR ALA THR GLN          
SEQRES  15 P  330  LYS THR VAL ASP GLY PRO SER HIS LYS ASP TRP ARG GLY          
SEQRES  16 P  330  GLY ARG GLY ALA SER GLN ASN ILE ILE PRO SER SER THR          
SEQRES  17 P  330  GLY ALA ALA LYS ALA VAL GLY LYS VAL LEU PRO GLU LEU          
SEQRES  18 P  330  ASN GLY LYS LEU THR GLY MET ALA PHE ARG VAL PRO THR          
SEQRES  19 P  330  PRO ASN VAL SER VAL VAL ASP LEU THR VAL ARG LEU GLU          
SEQRES  20 P  330  LYS ALA ALA THR TYR GLU GLN ILE LYS ALA ALA VAL LYS          
SEQRES  21 P  330  ALA ALA ALA GLU GLY GLU MET LYS GLY VAL LEU GLY TYR          
SEQRES  22 P  330  THR GLU ASP ASP VAL VAL SER THR ASP PHE ASN GLY GLU          
SEQRES  23 P  330  VAL CYS THR SER VAL PHE ASP ALA LYS ALA GLY ILE ALA          
SEQRES  24 P  330  LEU ASN ASP ASN PHE VAL LYS LEU VAL SER TRP TYR ASP          
SEQRES  25 P  330  ASN GLU THR GLY TYR SER ASN LYS VAL LEU ASP LEU ILE          
SEQRES  26 P  330  ALA HIS ILE SER LYS                                          
HET    NAD  O 336      44                                                       
HET    NAD  P 336      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   5  HOH   *290(H2 O)                                                    
HELIX    1  BO ARG O   10  GLN O   20  1                                  11    
HELIX    2  CO ALA O   37  LYS O   45  1                                   9    
HELIX    3  DO TRP O   84  VAL O   87  1                                   4    
HELIX    4  EO ASP O  102  THR O  110  1                                   9    
HELIX    5  1O CYS O  149  PHE O  165  1                                  17    
HELIX    6  2O TYR O  252  GLU O  264  1                                  13    
HELIX    7  3O THR O  315  HIS O  327  1                                  13    
HELIX    8  BP ARG P   10  GLN P   20  1                                  11    
HELIX    9  CP ALA P   37  LYS P   45  1                                   9    
HELIX   10  DP TRP P   84  VAL P   87  1                                   4    
HELIX   11  EP ASP P  102  THR P  110  1                                   9    
HELIX   12  1P CYS P  149  PHE P  165  1                                  17    
HELIX   13  2P TYR P  252  GLU P  264  1                                  13    
HELIX   14  3P THR P  315  HIS P  327  1                                  13    
SHEET    1  BO 8 VAL O  57  LYS O  60  0                                        
SHEET    2  BO 8 HIS O  63  VAL O  66 -1                                        
SHEET    3  BO 8 LYS O  69  THR O  74 -1                                        
SHEET    4  BO 8 GLU O  26  ASN O  31  1                                        
SHEET    5  BO 8 LYS O   2  ASN O   6  1                                        
SHEET    6  BO 8 VAL O  91  GLU O  94  1                                        
SHEET    7  BO 8 LYS O 115  MET O 118  1                                        
SHEET    8  BO 8 ILE O 143  SER O 145  1                                        
SHEET    1  CO 7 ILE O 204  SER O 207  0                                        
SHEET    2  CO 7 LEU O 225  ARG O 231 -1                                        
SHEET    3  CO 7 ILE O 167  HIS O 176  1                                        
SHEET    4  CO 7 SER O 238  LEU O 246 -1                                        
SHEET    5  CO 7 PHE O 304  TYR O 311 -1                                        
SHEET    6  CO 7 SER O 290  ASN O 301 -1                                        
SHEET    7  CO 7 LEU O 271  THR O 274  1                                        
SHEET    1  BP 8 VAL P  57  LYS P  60  0                                        
SHEET    2  BP 8 HIS P  63  VAL P  66 -1                                        
SHEET    3  BP 8 LYS P  69  THR P  74 -1                                        
SHEET    4  BP 8 GLU P  26  ASN P  31  1                                        
SHEET    5  BP 8 LYS P   2  ASN P   6  1                                        
SHEET    6  BP 8 VAL P  91  GLU P  94  1                                        
SHEET    7  BP 8 LYS P 115  MET P 118  1                                        
SHEET    8  BP 8 ILE P 143  SER P 145  1                                        
SHEET    1  CP 7 ILE P 204  SER P 207  0                                        
SHEET    2  CP 7 LEU P 225  ARG P 231 -1                                        
SHEET    3  CP 7 ILE P 167  HIS P 176  1                                        
SHEET    4  CP 7 SER P 238  LEU P 246 -1                                        
SHEET    5  CP 7 PHE P 304  TYR P 311 -1                                        
SHEET    6  CP 7 SER P 290  ASN P 301 -1                                        
SHEET    7  CP 7 LEU P 271  THR P 274  1                                        
SITE     1 AC1 23 GLY O   9  ARG O  10  ILE O  11  ASN O  31                    
SITE     2 AC1 23 ASP O  32  ARG O  77  ALA O  95  THR O  96                    
SITE     3 AC1 23 GLY O  97  LEU O  98  THR O 119  CYS O 149                    
SITE     4 AC1 23 ASN O 313  TYR O 317  HOH O 344  HOH O 345                    
SITE     5 AC1 23 HOH O 347  HOH O 356  HOH O 359  HOH O 366                    
SITE     6 AC1 23 HOH O 383  HOH O 384  HOH O 460                               
SITE     1 AC2 25 GLY P   7  GLY P   9  ARG P  10  ILE P  11                    
SITE     2 AC2 25 ASN P  31  ASP P  32  ARG P  77  ALA P  95                    
SITE     3 AC2 25 THR P  96  GLY P  97  LEU P  98  THR P 119                    
SITE     4 AC2 25 ALA P 180  ASN P 313  TYR P 317  HOH P 350                    
SITE     5 AC2 25 HOH P 351  HOH P 353  HOH P 366  HOH P 372                    
SITE     6 AC2 25 HOH P 378  HOH P 394  HOH P 421  HOH P 456                    
SITE     7 AC2 25 HOH P 483                                                     
CRYST1   79.140  189.560  122.180  90.00  90.00  90.00 C 2 2 21     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      0.012636  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008185        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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