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HEADER TRANSFERASE 21-FEB-97 1FYC TITLE INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) TITLE 2 COMPLEX, NMR, 1 STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIPOYL DOMAIN; COMPND 5 EC: 2.3.1.12; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: DIHYDROLIPOAMIDE ACETYLTRANSFERASE SUBUNIT COMPND 8 OF THE PYRUVATE DEHYDROGENASE (PDH) MULTIENZYME COMPLEX COMPND 9 (UNLIPOYLATED DOMAIN) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGAN: LIVER; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: HLIP; SOURCE 8 OTHER_DETAILS: EXPRESSED AS A GST FUSION PROTEIN KEYWDS TRANSFERASE, ACYLTRANSFERASE DIHYDROLIPOAMIDE, SUBUNIT, KEYWDS 2 UNLIPOYLATED EXPDTA NMR AUTHOR M.J.HOWARD,C.FULLER,R.W.BROADHURST,J.QUINN,S.J.YEAMAN, AUTHOR 2 R.N.PERHAM REVDAT 1 04-SEP-97 1FYC 0 JRNL AUTH M.J.HOWARD,C.FULLER,R.W.BROADHURST,R.N.PERHAM, JRNL AUTH 2 J.G.TANG,J.QUINN,A.G.DIAMOND,S.J.YEAMAN JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE MAJOR JRNL TITL 2 AUTOANTIGEN IN PRIMARY BILIARY CIRRHOSIS. JRNL REF GASTROENTEROLOGY V. 115 139 1998 JRNL REFN ASTM GASTAB US ISSN 0016-5085 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: REFINEMENT DETAILS CAM BE FOUND IN REMARK 3 P.M. RICAUD ET AL., JOURNAL OF MOLECULAR BIOLOGY, 264, 179- REMARK 3 190, 1996 REMARK 4 REMARK 4 1FYC 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) : 308 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, COSY, TCOSY, HSQC- REMARK 210 NOESY, HSQC-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AM500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ANSIG 3.3 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : MEAN STRUCTURE FROM 26 CHOSEN REMARK 210 HAVING LEAST RESTRAINT REMARK 210 VIOLATION 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 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 TYR A 6 151.58 59.89 REMARK 500 ALA A 89 138.28 75.17 DBREF 1FYC A 1 106 UNP P10515 ODP2_HUMAN 179 282 SEQADV 1FYC ASN A 3 UNP P10515 INSERTION SEQADV 1FYC MET A 4 UNP P10515 INSERTION SEQRES 1 A 106 GLY SER ASN MET SER TYR PRO PRO HIS MET GLN VAL LEU SEQRES 2 A 106 LEU PRO ALA LEU SER PRO THR MET THR MET GLY THR VAL SEQRES 3 A 106 GLN ARG TRP GLU LYS LYS VAL GLY GLU LYS LEU SER GLU SEQRES 4 A 106 GLY ASP LEU LEU ALA GLU ILE GLU THR ASP LYS ALA THR SEQRES 5 A 106 ILE GLY PHE GLU VAL GLN GLU GLU GLY TYR LEU ALA LYS SEQRES 6 A 106 ILE LEU VAL PRO GLU GLY THR ARG ASP VAL PRO LEU GLY SEQRES 7 A 106 THR PRO LEU CYS ILE ILE VAL GLU LYS GLU ALA ASP ILE SEQRES 8 A 106 SER ALA PHE ALA ASP TYR ARG PRO THR GLU VAL THR ASP SEQRES 9 A 106 LEU LYS SHEET 1 S1 4 MET A 10 LEU A 13 0 SHEET 2 S1 4 PRO A 80 VAL A 85 -1 SHEET 3 S1 4 GLU A 60 ILE A 66 -1 SHEET 4 S1 4 GLY A 34 SER A 38 -1 SHEET 1 S2 4 THR A 52 VAL A 57 0 SHEET 2 S2 4 ASP A 41 THR A 48 -1 SHEET 3 S2 4 THR A 25 TRP A 29 -1 SHEET 4 S2 4 THR A 72 VAL A 75 -1 TURN 1 T1 GLU A 30 VAL A 33 TURN 2 T2 GLU A 39 GLY A 40 TURN 3 T3 ASP A 49 ALA A 51 TURN 4 T4 GLN A 58 GLU A 59 TURN 5 T5 LEU A 67 GLY A 71 TURN 6 T6 PRO A 76 THR A 79 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