Header list of 1ghj.pdb file
Complete list - 29 20 Bytes
HEADER ACYLTRANSFERASE 16-JAN-96 1GHJ
TITLE SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE
TITLE 2 DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED
TITLE 3 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E2, THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE COMPONENT OF
COMPND 3 2-OXOGLUTARATE DEHYDROGENASE COMPLEX;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: LIPOYL DOMAIN, RESIDUES 1-79;
COMPND 6 SYNONYM: E2;
COMPND 7 EC: 2.3.1.61;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;
SOURCE 3 ORGANISM_TAXID: 354;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCOLYSIS, TRANSFERASE, ACYLTRANSFERASE, LIPOYL
EXPDTA SOLUTION NMR
AUTHOR A.BERG,J.VERVOORT,A.DE KOK
REVDAT 4 29-NOV-17 1GHJ 1 REMARK HELIX
REVDAT 3 24-FEB-09 1GHJ 1 VERSN
REVDAT 2 01-APR-03 1GHJ 1 JRNL
REVDAT 1 11-JAN-97 1GHJ 0
JRNL AUTH A.BERG,J.VERVOORT,A.DE KOK
JRNL TITL SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE
JRNL TITL 2 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER
JRNL TITL 3 VINELANDII.
JRNL REF J.MOL.BIOL. V. 261 432 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8780784
JRNL DOI 10.1006/JMBI.1996.0474
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.BERG,O.SMITS,A.DE KOK,J.VERVOORT
REMARK 1 TITL SEQUENTIAL 1H AND 15N NUCLEAR MAGNETIC RESONANCE ASSIGNMENTS
REMARK 1 TITL 2 AND SECONDARY STRUCTURE OF THE LIPOYL DOMAIN OF THE
REMARK 1 TITL 3 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER
REMARK 1 TITL 4 VINELANDII. EVIDENCE FOR HIGH STRUCTURAL SIMILARITY WITH THE
REMARK 1 TITL 5 LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE COMPLEX
REMARK 1 REF EUR.J.BIOCHEM. V. 234 148 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GHJ 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_1000173574.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO A 10 -160.00 -78.00
REMARK 500 ASP A 15 -170.89 -176.59
REMARK 500 VAL A 18 159.92 -48.22
REMARK 500 ALA A 19 -74.70 -104.22
REMARK 500 ASP A 32 37.78 70.01
REMARK 500 LEU A 34 158.96 -40.42
REMARK 500 ILE A 35 -41.83 -141.27
REMARK 500 LYS A 42 28.58 -153.22
REMARK 500 ALA A 51 145.38 166.53
REMARK 500 ASP A 52 170.82 -58.87
REMARK 500 GLU A 57 148.21 -179.56
REMARK 500 GLU A 77 -168.97 -60.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 31 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GHK RELATED DB: PDB
DBREF 1GHJ A 1 79 UNP P20708 ODO2_AZOVI 2 80
SEQRES 1 A 79 ALA ILE ASP ILE LYS ALA PRO THR PHE PRO GLU SER ILE
SEQRES 2 A 79 ALA ASP GLY THR VAL ALA THR TRP HIS LYS LYS PRO GLY
SEQRES 3 A 79 GLU ALA VAL LYS ARG ASP GLU LEU ILE VAL ASP ILE GLU
SEQRES 4 A 79 THR ASP LYS VAL VAL MET GLU VAL LEU ALA GLU ALA ASP
SEQRES 5 A 79 GLY VAL ILE ALA GLU ILE VAL LYS ASN GLU GLY ASP THR
SEQRES 6 A 79 VAL LEU SER GLY GLU LEU LEU GLY LYS LEU THR GLU GLY
SEQRES 7 A 79 GLY
SHEET 1 A 4 ILE A 2 LYS A 5 0
SHEET 2 A 4 LEU A 71 THR A 76 -1 N LEU A 75 O ILE A 2
SHEET 3 A 4 GLY A 53 ILE A 58 -1 O VAL A 54 N THR A 76
SHEET 4 A 4 GLU A 27 VAL A 29 -1 N VAL A 29 O GLY A 53
SHEET 1 B 4 VAL A 44 LEU A 48 0
SHEET 2 B 4 LEU A 34 GLU A 39 -1 N ILE A 38 O MET A 45
SHEET 3 B 4 GLY A 16 TRP A 21 -1 O THR A 17 N GLU A 39
SHEET 4 B 4 ASP A 64 VAL A 66 -1 N VAL A 66 O GLY A 16
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 29 20 Bytes