Header list of 1iyv.pdb file
Complete list - b 23 2 Bytes
HEADER ACYLTRANSFERASE 25-SEP-96 1IYV
TITLE LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, 29 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE
COMPND 3 DEHYDROGENASE COMPLEX;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: LIPOYL DOMAIN, RESIDUES 1 - 79;
COMPND 6 SYNONYM: E2P;
COMPND 7 EC: 2.3.1.12
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;
SOURCE 3 ORGANISM_TAXID: 354
KEYWDS GLYCOLYSIS, TRANSFERASE, ACYLTRANSFERASE, LIPOYL
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR A.BERG,J.VERVOORT,A.DE KOK
REVDAT 3 23-FEB-22 1IYV 1 REMARK
REVDAT 2 24-FEB-09 1IYV 1 VERSN
REVDAT 1 12-MAR-97 1IYV 0
JRNL AUTH A.BERG,J.VERVOORT,A.DE KOK
JRNL TITL THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE N-TERMINAL
JRNL TITL 2 LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE COMPLEX FROM
JRNL TITL 3 AZOTOBACTER VINELANDII.
JRNL REF EUR.J.BIOCHEM. V. 244 352 1997
JRNL REFN ISSN 0014-2956
JRNL PMID 9119000
JRNL DOI 10.1111/J.1432-1033.1997.00352.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.BERG,J.VERVOORT,A.DE KOK
REMARK 1 TITL SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE
REMARK 1 TITL 2 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER
REMARK 1 TITL 3 VINELANDII
REMARK 1 REF J.MOL.BIOL. V. 261 432 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
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 1 REFERENCE 3
REMARK 1 AUTH A.BERG,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 N-TERMINAL LIPOYL DOMAIN OF
REMARK 1 TITL 3 THE DIHYDROLIPOYL TRANSACETYLASE COMPONENT OF THE PYRUVATE
REMARK 1 TITL 4 DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELANDII
REMARK 1 REF EUR.J.BIOCHEM. V. 221 87 1994
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 1IYV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174292.
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 : 29
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 1 ILE A 9 -61.66 -105.35
REMARK 500 1 LEU A 19 49.76 -101.98
REMARK 500 1 VAL A 28 91.45 -50.28
REMARK 500 1 GLU A 29 -60.66 162.78
REMARK 500 1 LEU A 32 -40.45 -143.43
REMARK 500 1 LYS A 39 54.55 -140.86
REMARK 500 1 ALA A 40 146.16 -174.65
REMARK 500 1 PRO A 45 -168.40 -77.56
REMARK 500 1 ILE A 69 -71.46 -103.34
REMARK 500 1 ALA A 75 -169.07 70.26
REMARK 500 2 LEU A 19 30.55 -90.26
REMARK 500 2 GLU A 29 -58.55 162.94
REMARK 500 2 GLN A 30 157.88 -44.29
REMARK 500 2 LEU A 32 -73.42 -159.87
REMARK 500 2 ALA A 40 -166.58 -174.10
REMARK 500 2 PRO A 45 -168.65 -79.28
REMARK 500 2 ILE A 69 -67.24 -140.90
REMARK 500 2 ALA A 75 -172.05 49.60
REMARK 500 2 ALA A 78 104.62 -51.35
REMARK 500 3 PRO A 7 -168.79 -78.06
REMARK 500 3 LEU A 19 52.15 -106.10
REMARK 500 3 GLU A 29 -32.86 162.83
REMARK 500 3 LEU A 32 -68.59 -148.22
REMARK 500 3 ALA A 40 173.63 173.89
REMARK 500 3 PRO A 45 -168.44 -78.44
REMARK 500 3 SER A 54 145.34 171.12
REMARK 500 3 ALA A 68 175.38 -48.50
REMARK 500 3 ILE A 69 -47.97 -146.93
REMARK 500 3 ALA A 75 -79.60 -123.90
REMARK 500 3 ALA A 76 81.65 44.71
REMARK 500 4 ASP A 12 -179.20 49.76
REMARK 500 4 GLU A 29 -40.60 169.21
REMARK 500 4 ALA A 40 -179.54 177.15
REMARK 500 4 PRO A 45 -168.69 -77.43
REMARK 500 4 ILE A 69 -67.28 -134.13
REMARK 500 4 ALA A 75 -54.00 -137.89
REMARK 500 4 ALA A 76 133.30 -174.87
REMARK 500 5 VAL A 6 104.47 -44.83
REMARK 500 5 GLU A 17 149.06 -172.98
REMARK 500 5 LEU A 19 48.62 -90.71
REMARK 500 5 GLU A 29 -43.69 82.99
REMARK 500 5 LYS A 39 50.87 -156.21
REMARK 500 5 PRO A 45 -169.10 -77.57
REMARK 500 5 ILE A 69 -55.55 -135.41
REMARK 500 5 ALA A 78 24.04 -158.03
REMARK 500 6 GLU A 17 137.91 -175.47
REMARK 500 6 GLU A 29 -27.03 162.92
REMARK 500 6 LEU A 32 -62.93 -137.15
REMARK 500 6 LYS A 39 37.04 -157.95
REMARK 500 6 ALA A 40 88.33 -152.69
REMARK 500
REMARK 500 THIS ENTRY HAS 250 RAMACHANDRAN OUTLIERS.
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 1 ARG A 5 0.29 SIDE CHAIN
REMARK 500 1 ARG A 79 0.21 SIDE CHAIN
REMARK 500 2 ARG A 5 0.17 SIDE CHAIN
REMARK 500 2 ARG A 79 0.31 SIDE CHAIN
REMARK 500 3 ARG A 5 0.30 SIDE CHAIN
REMARK 500 3 ARG A 79 0.26 SIDE CHAIN
REMARK 500 4 ARG A 5 0.23 SIDE CHAIN
REMARK 500 4 ARG A 79 0.29 SIDE CHAIN
REMARK 500 5 ARG A 5 0.16 SIDE CHAIN
REMARK 500 5 ARG A 79 0.22 SIDE CHAIN
REMARK 500 6 ARG A 5 0.32 SIDE CHAIN
REMARK 500 6 ARG A 79 0.11 SIDE CHAIN
REMARK 500 7 ARG A 5 0.29 SIDE CHAIN
REMARK 500 7 ARG A 79 0.28 SIDE CHAIN
REMARK 500 8 ARG A 5 0.25 SIDE CHAIN
REMARK 500 8 ARG A 79 0.26 SIDE CHAIN
REMARK 500 9 ARG A 5 0.32 SIDE CHAIN
REMARK 500 9 ARG A 79 0.25 SIDE CHAIN
REMARK 500 10 ARG A 5 0.08 SIDE CHAIN
REMARK 500 10 ARG A 79 0.32 SIDE CHAIN
REMARK 500 11 ARG A 5 0.27 SIDE CHAIN
REMARK 500 11 ARG A 79 0.26 SIDE CHAIN
REMARK 500 12 ARG A 5 0.09 SIDE CHAIN
REMARK 500 12 ARG A 79 0.23 SIDE CHAIN
REMARK 500 13 ARG A 5 0.21 SIDE CHAIN
REMARK 500 13 ARG A 79 0.21 SIDE CHAIN
REMARK 500 14 ARG A 5 0.30 SIDE CHAIN
REMARK 500 14 ARG A 79 0.30 SIDE CHAIN
REMARK 500 15 ARG A 5 0.30 SIDE CHAIN
REMARK 500 15 ARG A 79 0.19 SIDE CHAIN
REMARK 500 16 ARG A 5 0.21 SIDE CHAIN
REMARK 500 16 ARG A 79 0.32 SIDE CHAIN
REMARK 500 17 ARG A 5 0.21 SIDE CHAIN
REMARK 500 17 ARG A 79 0.32 SIDE CHAIN
REMARK 500 18 ARG A 5 0.11 SIDE CHAIN
REMARK 500 18 ARG A 79 0.24 SIDE CHAIN
REMARK 500 19 ARG A 79 0.32 SIDE CHAIN
REMARK 500 20 ARG A 5 0.25 SIDE CHAIN
REMARK 500 20 ARG A 79 0.29 SIDE CHAIN
REMARK 500 21 ARG A 5 0.27 SIDE CHAIN
REMARK 500 21 ARG A 79 0.14 SIDE CHAIN
REMARK 500 22 ARG A 79 0.31 SIDE CHAIN
REMARK 500 23 ARG A 5 0.31 SIDE CHAIN
REMARK 500 23 ARG A 79 0.30 SIDE CHAIN
REMARK 500 24 ARG A 5 0.11 SIDE CHAIN
REMARK 500 24 ARG A 79 0.32 SIDE CHAIN
REMARK 500 25 ARG A 5 0.31 SIDE CHAIN
REMARK 500 25 ARG A 79 0.32 SIDE CHAIN
REMARK 500 26 ARG A 5 0.27 SIDE CHAIN
REMARK 500 26 ARG A 79 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 56 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LIP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LYS 39 IS THE LIPOYLATION SITE WHERE LIPOIC ACID
REMARK 800 (6,8 THIOCTIC ACID) IS COVALENTLY ATTACHED VIA AN AMIDE LINKAGE
REMARK 800 TO THE LYSINE SIDE CHAIN.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IYU RELATED DB: PDB
DBREF 1IYV A 1 78 UNP P10802 ODP2_AZOVI 1 78
SEQRES 1 A 79 SER GLU ILE ILE ARG VAL PRO ASP ILE GLY GLY ASP GLY
SEQRES 2 A 79 GLU VAL ILE GLU LEU LEU VAL LYS THR GLY ASP LEU ILE
SEQRES 3 A 79 GLU VAL GLU GLN GLY LEU VAL VAL LEU GLU SER ALA LYS
SEQRES 4 A 79 ALA SER MET GLU VAL PRO SER PRO LYS ALA GLY VAL VAL
SEQRES 5 A 79 LYS SER VAL SER VAL LYS LEU GLY ASP LYS LEU LYS GLU
SEQRES 6 A 79 GLY ASP ALA ILE ILE GLU LEU GLU PRO ALA ALA GLY ALA
SEQRES 7 A 79 ARG
SHEET 1 A 2 ASP A 12 GLU A 14 0
SHEET 2 A 2 LYS A 62 LYS A 64 -1 N LEU A 63 O GLY A 13
SHEET 1 B 3 GLU A 2 ARG A 5 0
SHEET 2 B 3 ALA A 68 GLU A 73 -1 N LEU A 72 O GLU A 2
SHEET 3 B 3 VAL A 51 VAL A 55 -1 N SER A 54 O GLU A 71
SITE 1 LIP 1 LYS A 39
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
MODEL 1
Complete list - b 23 2 Bytes