HEADER OXIDOREDUCTASE 01-JUL-75 1GPD
TITLE STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-
TITLE 2 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: G, R;
COMPND 4 EC: 1.2.1.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMARUS AMERICANUS;
SOURCE 3 ORGANISM_COMMON: AMERICAN LOBSTER;
SOURCE 4 ORGANISM_TAXID: 6706
KEYWDS OXIDO-REDUCTASE(ALDEHYDE/DONR, NAD/ACCPT), OXIDO-REDUCTASE(ALDEHYDE-
KEYWDS 2 DONR, NAD-ACCPT) COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MORAS,K.W.OLSEN,M.N.SABESAN,M.BUEHNER,G.C.FORD,M.G.ROSSMANN
REVDAT 14 27-SEP-23 1GPD 1 REMARK LINK CRYST1 SCALE
REVDAT 14 2 1 MTRIX ATOM
REVDAT 13 29-OCT-14 1GPD 1 LINK
REVDAT 12 13-JUL-11 1GPD 1 VERSN
REVDAT 11 24-FEB-09 1GPD 1 VERSN
REVDAT 10 15-JUL-92 1GPD 1 COMPND
REVDAT 9 30-SEP-83 1GPD 1 REVDAT
REVDAT 8 01-MAR-82 1GPD 1 REMARK
REVDAT 7 20-APR-81 1GPD 3 SEQRES ATOM
REVDAT 6 31-DEC-80 1GPD 1 REMARK
REVDAT 5 01-OCT-80 1GPD 1 REMARK
REVDAT 4 05-FEB-79 1GPD 1 SITE
REVDAT 3 20-JUL-78 1GPD 2 CONECT
REVDAT 2 01-NOV-77 1GPD 1 COMPND SOURCE AUTHOR JRNL
REVDAT 2 2 1 REMARK FORMUL
REVDAT 1 17-FEB-77 1GPD 0
JRNL AUTH D.MORAS,K.W.OLSEN,M.N.SABESAN,M.BUEHNER,G.C.FORD,
JRNL AUTH 2 M.G.ROSSMANN
JRNL TITL STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF
JRNL TITL 2 LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE.
JRNL REF J.BIOL.CHEM. V. 250 9137 1975
JRNL REFN ISSN 0021-9258
JRNL PMID 127793
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.W.OLSEN,R.M.GARAVITO,M.N.SABESAN,M.G.ROSSMANN
REMARK 1 TITL ANION BINDING SITES IN THE ACTIVE CENTER OF
REMARK 1 TITL 2 D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
REMARK 1 REF J.MOL.BIOL. V. 107 571 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.W.OLSEN,R.M.GARAVITO,M.N.SABESAN,M.G.ROSSMANN
REMARK 1 TITL STUDIES ON COENZYME BINDING TO GLYCERALDEHYDE-3-PHOSPHATE
REMARK 1 TITL 2 DEHYDROGENASE
REMARK 1 REF J.MOL.BIOL. V. 107 577 1976
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.G.ROSSMANN
REMARK 1 TITL A COMPARISON OF THE BINDING AND FUNCTION OF NAD WITH RESPECT
REMARK 1 TITL 2 TO LACTATE DEHYDROGENASE AND GLYCERALDEHYDE-3-PHOSPHATE
REMARK 1 TITL 3 DEHYDROGENASE
REMARK 1 EDIT M.SUNDARALINGAM, S.T.RAO
REMARK 1 REF STRUCTURE AND CONFORMATION 353 1975
REMARK 1 REF 2 OF NUCLEIC ACIDS AND
REMARK 1 REF 3 PROTEIN-NUCLEIC ACID
REMARK 1 REF 4 INTERACTIONS : PROCEEDINGS
REMARK 1 REF 5 OF THE FOURTH ANNUAL HARRY
REMARK 1 REF 6 STEENBOCK SYMPOSIUM, JUNE
REMARK 1 REF 7 16-19, 1974, MADISON,
REMARK 1 REF 8 WISCONSIN
REMARK 1 PUBL UNIVERSITY PARK PRESS,BALTIMORE,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.W.OLSEN,D.MORAS,M.G.ROSSMANN,J.I.HARRIS
REMARK 1 TITL SEQUENCE VARIABILITY AND STRUCTURE OF
REMARK 1 TITL 2 D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
REMARK 1 REF J.BIOL.CHEM. V. 250 9313 1975
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.BUEHNER,G.C.FORD,D.MORAS,K.W.OLSEN,M.G.ROSSMANN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE
REMARK 1 TITL 2 DEHYDROGENASE
REMARK 1 REF J.MOL.BIOL. V. 90 25 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.BUEHNER,G.C.FORD,D.MORAS,K.W.OLSEN,M.G.ROSSMANN
REMARK 1 TITL STRUCTURE DETERMINATION OF CRYSTALLINE LOBSTER
REMARK 1 TITL 2 D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
REMARK 1 REF J.MOL.BIOL. V. 82 563 1974
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 7
REMARK 1 AUTH M.BUEHNER,G.C.FORD,D.MORAS,K.W.OLSEN,M.G.ROSSMANN
REMARK 1 TITL D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE,THREE DIMENSIONAL
REMARK 1 TITL 2 STRUCTURE AND EVOLUTIONARY SIGNIFICANCE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 70 3052 1973
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 8
REMARK 1 AUTH P.ARGOS,G.C.FORD,M.G.ROSSMANN
REMARK 1 TITL AN APPLICATION OF THE MOLECULAR REPLACEMENT TECHNIQUE IN
REMARK 1 TITL 2 DIRECT SPACE TO A KNOWN PROTEIN STRUCTURE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.A V. 31 499 1975
REMARK 1 REFN ISSN 0108-7673
REMARK 1 REFERENCE 9
REMARK 1 EDIT R.J.FELDMANN
REMARK 1 REF ATLAS OF MACROMOLECULAR 347 1976
REMARK 1 REF 2 STRUCTURE ON MICROFICHE
REMARK 1 PUBL TRACOR JITCO INC.,ROCKVILLE,MD.
REMARK 1 REFN
REMARK 1 REFERENCE 10
REMARK 1 EDIT M.O.DAYHOFF
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 75 1976
REMARK 1 REF 2 AND STRUCTURE,SUPPLEMENT 2
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.
REMARK 1 REFN ISSN 0-912466-05-7
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : NULL
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) : NULL
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 : 5020
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 0
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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: NULL
REMARK 4
REMARK 4 1GPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173656.
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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) : 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 74.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.35000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.35000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.55000
REMARK 290 SMTRY3 4 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 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 APPLY THE FOLLOWING TO CHAINS: G, R
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 -0.170476 -0.748321 -0.640255 96.24453
REMARK 350 BIOMT2 2 -0.748780 -0.324519 0.577934 70.94252
REMARK 350 BIOMT3 2 -0.641323 0.578543 -0.505006 41.77925
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PO4 R 335
REMARK 610 PO4 R 336
REMARK 610 PO4 R 337
REMARK 610 PO4 R 338
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET SUBSTRUCTURE OF THE CATALYTIC DOMAIN IS
REMARK 700 BIFURCATED. TO REPRESENT THIS FEATURE REDUNDANT SHEETS
REMARK 700 ARE DEFINED FOR EACH OF THE TWO SUBUNITS. STRANDS 1-7 OF
REMARK 700 SHEETS GC1 AND RC1 ARE IDENTICAL TO STRANDS 1-7 OF SHEETS
REMARK 700 GC2 AND RC2.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ABG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENINE BASE OF
REMARK 800 THE COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: ABR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENINE BASE OF
REMARK 800 THE COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: ARG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE
REMARK 800 OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: ARR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE
REMARK 800 OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: APG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PHOSPHATE OF THE
REMARK 800 ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: APR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PHOSPHATE OF THE
REMARK 800 ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NPG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PHOSPHATE OF THE
REMARK 800 NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NPR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PHOSPHATE OF THE
REMARK 800 NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NRG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE RIBOSE OF THE
REMARK 800 NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NRR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE RIBOSE OF THE
REMARK 800 NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NBG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE
REMARK 800 OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: NBR
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE
REMARK 800 OF THE NAD COFACTOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD R 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 338
DBREF 1GPD G 1 334 UNP P00357 G3P_HOMAM 1 333
DBREF 1GPD R 1 334 UNP P00357 G3P_HOMAM 1 333
SEQRES 1 G 334 ACE SER LYS ILE GLY ILE ASN GLY PHE GLY ARG ILE GLY
SEQRES 2 G 334 ARG LEU VAL LEU ARG ALA ALA LEU SER CYS GLY ALA GLN
SEQRES 3 G 334 VAL VAL ALA VAL ASN ASP PRO PHE ILE ALA LEU GLU TYR
SEQRES 4 G 334 MET VAL TYR MET PHE LYS TYR ASP SER THR HIS GLY VAL
SEQRES 5 G 334 PHE LYS GLY GLU VAL LYS MET GLU ASP GLY ALA LEU VAL
SEQRES 6 G 334 VAL ASP GLY LYS LYS ILE THR VAL PHE ASN GLU MET LYS
SEQRES 7 G 334 PRO GLU ASN ILE PRO TRP SER LYS ALA GLY ALA GLU TYR
SEQRES 8 G 334 ILE VAL GLU SER THR GLY VAL PHE THR THR ILE GLU LYS
SEQRES 9 G 334 ALA SER ALA HIS PHE LYS GLY GLY ALA LYS LYS VAL VAL
SEQRES 10 G 334 ILE SER ALA PRO SER ALA ASP ALA PRO MET PHE VAL CYS
SEQRES 11 G 334 GLY VAL ASN LEU GLU LYS TYR SER LYS ASP MET THR VAL
SEQRES 12 G 334 VAL SER ASN ALA SER CYS THR THR ASN CYS LEU ALA PRO
SEQRES 13 G 334 VAL ALA LYS VAL LEU HIS GLU ASN PHE GLU ILE VAL GLU
SEQRES 14 G 334 GLY LEU MET THR THR VAL HIS ALA VAL THR ALA THR GLN
SEQRES 15 G 334 LYS THR VAL ASP GLY PRO SER ALA LYS ASP TRP ARG GLY
SEQRES 16 G 334 GLY ARG GLY ALA ALA GLN ASN ILE ILE PRO SER SER THR
SEQRES 17 G 334 GLY ALA ALA LYS ALA VAL GLY LYS VAL ILE PRO GLU LEU
SEQRES 18 G 334 ASP GLY LYS LEU THR GLY MET ALA PHE ARG VAL PRO THR
SEQRES 19 G 334 PRO ASP VAL SER VAL VAL ASP LEU THR VAL ARG LEU GLY
SEQRES 20 G 334 LYS GLU CYS SER TYR ASP ASP ILE LYS ALA ALA MET LYS
SEQRES 21 G 334 THR ALA SER GLU GLY PRO LEU GLN GLY PHE LEU GLY TYR
SEQRES 22 G 334 THR GLU ASP ASP VAL VAL SER SER ASP PHE ILE GLY ASP
SEQRES 23 G 334 ASN ARG SER SER ILE PHE ASP ALA LYS ALA GLY ILE GLN
SEQRES 24 G 334 LEU SER LYS THR PHE VAL LYS VAL VAL SER TRP TYR ASP
SEQRES 25 G 334 ASN GLU PHE GLY TYR SER GLN ARG VAL ILE ASP LEU LEU
SEQRES 26 G 334 LYS HIS MET GLN LYS VAL ASP SER ALA
SEQRES 1 R 334 ACE SER LYS ILE GLY ILE ASN GLY PHE GLY ARG ILE GLY
SEQRES 2 R 334 ARG LEU VAL LEU ARG ALA ALA LEU SER CYS GLY ALA GLN
SEQRES 3 R 334 VAL VAL ALA VAL ASN ASP PRO PHE ILE ALA LEU GLU TYR
SEQRES 4 R 334 MET VAL TYR MET PHE LYS TYR ASP SER THR HIS GLY VAL
SEQRES 5 R 334 PHE LYS GLY GLU VAL LYS MET GLU ASP GLY ALA LEU VAL
SEQRES 6 R 334 VAL ASP GLY LYS LYS ILE THR VAL PHE ASN GLU MET LYS
SEQRES 7 R 334 PRO GLU ASN ILE PRO TRP SER LYS ALA GLY ALA GLU TYR
SEQRES 8 R 334 ILE VAL GLU SER THR GLY VAL PHE THR THR ILE GLU LYS
SEQRES 9 R 334 ALA SER ALA HIS PHE LYS GLY GLY ALA LYS LYS VAL VAL
SEQRES 10 R 334 ILE SER ALA PRO SER ALA ASP ALA PRO MET PHE VAL CYS
SEQRES 11 R 334 GLY VAL ASN LEU GLU LYS TYR SER LYS ASP MET THR VAL
SEQRES 12 R 334 VAL SER ASN ALA SER CYS THR THR ASN CYS LEU ALA PRO
SEQRES 13 R 334 VAL ALA LYS VAL LEU HIS GLU ASN PHE GLU ILE VAL GLU
SEQRES 14 R 334 GLY LEU MET THR THR VAL HIS ALA VAL THR ALA THR GLN
SEQRES 15 R 334 LYS THR VAL ASP GLY PRO SER ALA LYS ASP TRP ARG GLY
SEQRES 16 R 334 GLY ARG GLY ALA ALA GLN ASN ILE ILE PRO SER SER THR
SEQRES 17 R 334 GLY ALA ALA LYS ALA VAL GLY LYS VAL ILE PRO GLU LEU
SEQRES 18 R 334 ASP GLY LYS LEU THR GLY MET ALA PHE ARG VAL PRO THR
SEQRES 19 R 334 PRO ASP VAL SER VAL VAL ASP LEU THR VAL ARG LEU GLY
SEQRES 20 R 334 LYS GLU CYS SER TYR ASP ASP ILE LYS ALA ALA MET LYS
SEQRES 21 R 334 THR ALA SER GLU GLY PRO LEU GLN GLY PHE LEU GLY TYR
SEQRES 22 R 334 THR GLU ASP ASP VAL VAL SER SER ASP PHE ILE GLY ASP
SEQRES 23 R 334 ASN ARG SER SER ILE PHE ASP ALA LYS ALA GLY ILE GLN
SEQRES 24 R 334 LEU SER LYS THR PHE VAL LYS VAL VAL SER TRP TYR ASP
SEQRES 25 R 334 ASN GLU PHE GLY TYR SER GLN ARG VAL ILE ASP LEU LEU
SEQRES 26 R 334 LYS HIS MET GLN LYS VAL ASP SER ALA
HET ACE G 0 3
HET ACE R 0 3
HET NAD G 335 44
HET PO4 R 335 1
HET PO4 R 336 1
HET PO4 R 337 1
HET PO4 R 338 1
HET NAD R 339 44
HETNAM ACE ACETYL GROUP
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM PO4 PHOSPHATE ION
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 4 PO4 4(O4 P 3-)
HELIX 1 B GLY G 9 CYS G 22 1 14
HELIX 2 C ALA G 36 TYR G 46 1 11
HELIX 3 E THR G 101 GLY G 112 1 12
HELIX 4 H4 SER G 148 GLU G 166 1IRREGULAR NEAR RES 154-157 19
HELIX 5 H5 GLY G 209 ILE G 218 1 10
HELIX 6 H6 SER G 251 GLY G 265 1 15
HELIX 7 H7 ASN G 313 ALA G 334 1 22
HELIX 8 B GLY R 9 CYS R 22 1 14
HELIX 9 C ALA R 36 TYR R 46 1 11
HELIX 10 E THR R 101 GLY R 112 1 12
HELIX 11 H4 SER R 148 GLU R 166 1IRREGULAR NEAR RES 154-157 19
HELIX 12 H5 GLY R 209 ILE R 218 1 10
HELIX 13 H6 SER R 251 GLY R 265 1 15
HELIX 14 H7 ASN R 313 ALA R 334 1 22
SHEET 1 GBD 9 GLU G 56 GLU G 60 0
SHEET 2 GBD 9 ALA G 63 ASP G 67 -1
SHEET 3 GBD 9 THR G 72 PHE G 74 -1
SHEET 4 GBD 9 VAL G 27 ASP G 32 1
SHEET 5 GBD 9 LYS G 2 GLY G 7 1
SHEET 6 GBD 9 GLU G 90 SER G 95 1
SHEET 7 GBD 9 LYS G 115 ALA G 120 1
SHEET 8 GBD 9 THR G 142 ALA G 147 1
SHEET 9 GBD 9 PRO G 126 PHE G 128 1
SHEET 1 GC1 8 VAL G 185 LYS G 191 0
SHEET 2 GC1 8 ASP G 192 ARG G 194 -1
SHEET 3 GC1 8 ILE G 204 THR G 208 -1
SHEET 4 GC1 8 LYS G 224 PRO G 233 -1
SHEET 5 GC1 8 VAL G 168 THR G 179 1
SHEET 6 GC1 8 ASP G 236 LEU G 246 -1
SHEET 7 GC1 8 THR G 303 ASP G 312 -1
SHEET 8 GC1 8 GLN G 299 SER G 301 -1
SHEET 1 GC2 9 VAL G 185 LYS G 191 0
SHEET 2 GC2 9 ASP G 192 ARG G 194 -1
SHEET 3 GC2 9 ILE G 204 THR G 208 -1
SHEET 4 GC2 9 LYS G 224 PRO G 233 -1
SHEET 5 GC2 9 VAL G 168 THR G 179 1
SHEET 6 GC2 9 ASP G 236 LEU G 246 -1
SHEET 7 GC2 9 THR G 303 ASP G 312 -1
SHEET 8 GC2 9 SER G 290 ASP G 293 -1
SHEET 9 GC2 9 LEU G 271 TYR G 273 1
SHEET 1 RBD 9 GLU R 56 GLU R 60 0
SHEET 2 RBD 9 ALA R 63 ASP R 67 -1
SHEET 3 RBD 9 THR R 72 PHE R 74 -1
SHEET 4 RBD 9 VAL R 27 ASP R 32 1
SHEET 5 RBD 9 LYS R 2 GLY R 7 1
SHEET 6 RBD 9 GLU R 90 SER R 95 1
SHEET 7 RBD 9 LYS R 115 ALA R 120 1
SHEET 8 RBD 9 THR R 142 ALA R 147 1
SHEET 9 RBD 9 PRO R 126 PHE R 128 1
SHEET 1 RC1 8 VAL R 185 LYS R 191 0
SHEET 2 RC1 8 ASP R 192 ARG R 194 -1
SHEET 3 RC1 8 ILE R 204 THR R 208 -1
SHEET 4 RC1 8 LYS R 224 PRO R 233 -1
SHEET 5 RC1 8 VAL R 168 THR R 179 1
SHEET 6 RC1 8 ASP R 236 LEU R 246 -1
SHEET 7 RC1 8 THR R 303 ASP R 312 -1
SHEET 8 RC1 8 GLN R 299 SER R 301 -1
SHEET 1 RC2 9 VAL R 185 LYS R 191 0
SHEET 2 RC2 9 ASP R 192 ARG R 194 -1
SHEET 3 RC2 9 ILE R 204 THR R 208 -1
SHEET 4 RC2 9 LYS R 224 PRO R 233 -1
SHEET 5 RC2 9 VAL R 168 THR R 179 1
SHEET 6 RC2 9 ASP R 236 LEU R 246 -1
SHEET 7 RC2 9 THR R 303 ASP R 312 -1
SHEET 8 RC2 9 SER R 290 ASP R 293 -1
SHEET 9 RC2 9 LEU R 271 TYR R 273 1
LINK C ACE G 0 N SER G 1 1555 1555 1.32
LINK C ACE R 0 N SER R 1 1555 1555 1.32
SITE 1 ABG 6 ASN G 6 ASN G 31 ASP G 32 PHE G 34
SITE 2 ABG 6 THR G 96 PHE G 99
SITE 1 ABR 6 ASN R 6 ASN R 31 ASP R 32 PHE R 34
SITE 2 ABR 6 THR R 96 PHE R 99
SITE 1 ARG 3 GLY G 7 ASP G 32 PRO R 188
SITE 1 ARR 4 GLY R 7 PHE R 8 ASP R 32 PRO G 188
SITE 1 APG 2 ARG G 10 ALA G 180
SITE 1 APR 2 ARG R 10 ALA R 180
SITE 1 NPG 1 ILE G 11
SITE 1 NPR 1 ILE R 11
SITE 1 NRG 4 THR G 96 GLY G 97 SER G 119 ALA G 120
SITE 1 NRR 4 THR R 96 GLY R 97 SER R 119 ALA R 120
SITE 1 NBG 4 ILE G 11 CYS G 149 ASN G 313 TYR G 317
SITE 1 NBR 4 ILE R 11 CYS R 149 ASN R 313 TYR R 317
SITE 1 AC3 11 GLY G 7 PHE G 8 GLY G 9 ARG G 10
SITE 2 AC3 11 ILE G 11 ASP G 32 PHE G 34 ILE G 35
SITE 3 AC3 11 PHE G 99 SER G 119 GLU G 314
SITE 1 AC4 10 PHE R 8 ARG R 10 ASP R 32 THR R 96
SITE 2 AC4 10 PHE R 99 SER R 119 ALA R 120 CYS R 149
SITE 3 AC4 10 ASN R 313 TYR R 317
SITE 1 AC7 1 THR R 179
SITE 1 AC8 3 THR R 150 THR R 208 GLY R 209
CRYST1 149.000 139.100 80.700 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 -0.644212 0.581149 0.497224 22.35172
ORIGX2 0.710721 0.695637 0.107094 -61.11378
ORIGX3 -0.283862 0.422406 -0.860346 16.64914
SCALE1 0.006711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007189 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012392 0.00000
MTRIX1 1 -0.170476 -0.748321 -0.640255 96.24453
MTRIX2 1 -0.748780 -0.324519 0.577934 70.94252
MTRIX3 1 -0.641323 0.578543 -0.505006 41.77925
MTRIX1 2 0.009415 0.987991 0.152101 38.22796 1
MTRIX2 2 0.988613 -0.032369 0.148967 -40.04659 1
MTRIX3 2 0.152335 0.149102 -0.977046 6.42870 1
MTRIX1 3 -0.838939 -0.239670 0.488153 115.57931 1
MTRIX2 3 -0.239833 -0.643112 -0.726901 59.02943 1
MTRIX3 3 0.488987 -0.727645 0.482051 -9.15240 1
HETATM 1 C ACE G 0 87.167 48.604 -9.856 1.00 0.00 C
HETATM 2 O ACE G 0 87.476 49.485 -10.674 1.00 0.00 O
HETATM 3 CH3 ACE G 0 87.265 48.859 -8.351 1.00 0.00 C
(ATOM LINES ARE NOT SHOWN.)
END
