[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER TRANSFERASE 24-JUL-97 1PMR TITLE LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE TITLE 2 COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME TITLE 3 COMPLEX OF ESCHERICHIA COLI, NMR, 25 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOYL SUCCINYLTRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIPOYL DOMAIN; COMPND 5 EC: 2.3.1.61; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 CELL_LINE: BL21; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET11C KEYWDS TRANSFERASE, 2-OXOGLUTARATE DEHYDROGENASE, LIPOYL DOMAIN, KEYWDS 2 COMPLEX, NMR, GLYCOLYSIS EXPDTA NMR, 25 STRUCTURES AUTHOR P.M.RICAUD,M.J.HOWARD,E.L.ROBERTS,R.W.BROADHURST,R.N.PERHAM REVDAT 1 29-JUL-98 1PMR 0 JRNL AUTH P.M.RICAUD,M.J.HOWARD,E.L.ROBERTS,R.W.BROADHURST, JRNL AUTH 2 R.N.PERHAM JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN JRNL TITL 2 FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE JRNL TITL 3 COMPONENT OF THE 2-OXOGLUTARATE DEHYDROGENASE JRNL TITL 4 MULTIENZYME COMPLEX OF ESCHERICHIA COLI. JRNL REF J.MOL.BIOL. V. 264 179 1996 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 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 1PMR COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) 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 : 72 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21 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 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 M RES CSSEQI PSI PHI REMARK 500 1 ASP A 53 -86.50 69.81 REMARK 500 2 ASP A 33 80.45 146.68 REMARK 500 3 ASP A 33 84.70 145.04 REMARK 500 4 ASP A 53 -88.43 60.63 REMARK 500 5 ASP A 33 102.69 143.96 REMARK 500 5 ASP A 53 -117.37 106.65 REMARK 500 6 ASP A 33 80.88 149.60 REMARK 500 7 ALA A 52 160.81 88.81 REMARK 500 7 ASP A 53 -76.95 79.97 REMARK 500 9 ALA A 52 136.95 98.53 REMARK 500 9 ASP A 53 -76.47 101.34 REMARK 500 10 GLU A 12 -93.66 39.05 REMARK 500 10 ALA A 52 162.35 101.58 REMARK 500 11 ASP A 53 -73.82 78.91 REMARK 500 12 ALA A 52 160.99 105.43 REMARK 500 12 ASP A 53 -89.45 74.95 REMARK 500 13 ASP A 33 100.60 146.00 REMARK 500 13 ASP A 53 -93.93 65.84 REMARK 500 14 ASP A 16 163.02 55.64 REMARK 500 14 ASP A 33 84.14 145.32 REMARK 500 15 ASP A 53 -88.80 66.75 REMARK 500 16 ALA A 52 169.37 93.23 REMARK 500 16 ASP A 53 -101.59 69.74 REMARK 500 17 ASP A 33 88.10 144.94 REMARK 500 19 ASP A 53 -81.89 75.34 REMARK 500 20 ALA A 52 164.93 90.65 REMARK 500 20 ASP A 53 -100.54 67.65 REMARK 500 21 ASP A 33 91.02 147.81 REMARK 500 21 ASP A 53 -87.87 67.85 REMARK 500 22 ASP A 53 -77.36 78.26 REMARK 500 23 ASP A 53 -88.43 60.63 REMARK 500 24 ASP A 33 99.16 149.65 REMARK 500 24 ASP A 53 -73.41 79.10 REMARK 500 25 ALA A 52 168.45 94.48 DBREF 1PMR A 1 80 UNP P07016 ODO2_ECOLI 1 80 SEQRES 1 A 80 SER SER VAL ASP ILE LEU VAL PRO ASP LEU PRO GLU SER SEQRES 2 A 80 VAL ALA ASP ALA THR VAL ALA THR TRP HIS LYS LYS PRO SEQRES 3 A 80 GLY ASP ALA VAL VAL ARG ASP GLU VAL LEU VAL GLU ILE SEQRES 4 A 80 GLU THR ASP LYS VAL VAL LEU GLU VAL PRO ALA SER ALA SEQRES 5 A 80 ASP GLY ILE LEU ASP ALA VAL LEU GLU ASP GLU GLY THR SEQRES 6 A 80 THR VAL THR SER ARG GLN ILE LEU GLY ARG LEU ARG GLU SEQRES 7 A 80 GLY ASN SHEET 1 S1 4 GLY A 27 VAL A 30 0 SHEET 2 S1 4 GLY A 54 VAL A 59 -1 SHEET 3 S1 4 GLN A 71 LEU A 76 -1 SHEET 4 S1 4 VAL A 3 VAL A 7 -1 SHEET 1 S2 4 VAL A 44 ALA A 50 0 SHEET 2 S2 4 GLU A 34 THR A 41 -1 SHEET 3 S2 4 ALA A 17 TRP A 22 -1 SHEET 4 S2 4 THR A 65 THR A 68 -1 TURN 1 T1 PRO A 8 ASP A 16 BETA-TURN TURN 2 T2 HIS A 23 PRO A 26 BETA-TURN TURN 3 T3 VAL A 31 ASP A 33 BETA-TURN TURN 4 T4 ASP A 42 LYS A 43 BETA-TURN TURN 5 T5 SER A 51 ASP A 53 BETA-TURN TURN 6 T6 LEU A 60 GLY A 64 BETA-TURN TURN 7 T7 SER A 69 ARG A 70 BETA-TURN 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