HEADER TRANSFERASE (ACYLTRANSFERASE) 02-SEP-92 1LAB TITLE THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM TITLE 2 BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE TITLE 3 MULTIENZYME COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOAMIDE ACETYLTRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 EC: 2.3.1.12; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS; SOURCE 3 GENE: BACILLUS STEAROTHERMOPHILUS; SOURCE 4 EXPRESSION_SYSTEM_GENE: BACILLUS STEAROTHERMOPHILUS KEYWDS TRANSFERASE (ACYLTRANSFERASE) EXPDTA NMR, 11 STRUCTURES AUTHOR F.DARDEL,A.L.DAVIS,E.D.LAUE,R.N.PERHAM REVDAT 2 15-OCT-94 1LAB 1 COMPND SOURCE REVDAT 1 15-JUL-93 1LAB 0 JRNL AUTH F.DARDEL,A.L.DAVIS,E.D.LAUE,R.N.PERHAM JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN JRNL TITL 2 FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE JRNL TITL 3 DEHYDROGENASE MULTIENZYME COMPLEX. JRNL REF J.MOL.BIOL. V. 229 1037 1993 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH F.DARDEL,E.D.LAUE,R.N.PERHAM REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS AND SECONDARY REMARK 1 TITL 2 STRUCTURE OF THE LIPOYL DOMAIN OF THE BACILLUS REMARK 1 TITL 3 STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE REMARK 1 TITL 4 MULTIENZYME COMPLEX REMARK 1 REF EUR.J.BIOCHEM. V. 201 203 1991 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LAB 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 : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : NULL 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 3 PHE A 2 N - CA - C ANGL. DEV. =-22.2 DEGREES REMARK 500 3 GLU A 31 CA - C - N ANGL. DEV. =-22.1 DEGREES REMARK 500 4 GLU A 31 N - CA - C ANGL. DEV. = 40.6 DEGREES REMARK 500 4 GLU A 31 CA - C - N ANGL. DEV. =-23.0 DEGREES REMARK 500 5 GLU A 31 OE1 - CD - OE2 ANGL. DEV. =-39.7 DEGREES REMARK 500 5 GLU A 31 CG - CD - OE1 ANGL. DEV. = 47.4 DEGREES REMARK 500 5 GLU A 31 CG - CD - OE2 ANGL. DEV. =-35.8 DEGREES REMARK 500 6 GLU A 31 N - CA - C ANGL. DEV. = 27.2 DEGREES REMARK 500 7 GLU A 31 N - CA - C ANGL. DEV. = 24.2 DEGREES REMARK 500 9 GLU A 31 N - CA - C ANGL. DEV. = 23.9 DEGREES 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 33 -137.74 18.13 REMARK 500 4 GLU A 31 123.08 20.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 24 PRO A 25 1 -70.90 REMARK 500 ILE A 47 PRO A 48 3 82.65 REMARK 500 ILE A 47 PRO A 48 4 90.04 REMARK 500 LEU A 6 PRO A 7 5 148.03 REMARK 500 ALA A 77 PRO A 78 5 -143.90 REMARK 500 ILE A 47 PRO A 48 6 83.39 REMARK 500 LEU A 6 PRO A 7 7 148.60 REMARK 500 ILE A 47 PRO A 48 7 84.30 REMARK 500 LYS A 24 PRO A 25 8 -60.08 REMARK 500 ALA A 77 PRO A 78 8 -62.64 REMARK 500 ILE A 47 PRO A 48 9 87.58 REMARK 500 LEU A 6 PRO A 7 11 145.93 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LAC RELATED DB: PDB DBREF 1LAB A 1 80 UNP P11961 ODP2_BACST 1 80 SEQRES 1 A 80 ALA PHE GLU PHE LYS LEU PRO ASP ILE GLY GLU GLY ILE SEQRES 2 A 80 HIS GLU GLY GLU ILE VAL LYS TRP PHE VAL LYS PRO GLY SEQRES 3 A 80 ASP GLU VAL ASN GLU ASP ASP VAL LEU CYS GLU VAL GLN SEQRES 4 A 80 ASN ASP LYS ALA VAL VAL GLU ILE PRO SER PRO VAL LYS SEQRES 5 A 80 GLY LYS VAL LEU GLU ILE LEU VAL PRO GLU GLY THR VAL SEQRES 6 A 80 ALA THR VAL GLY GLN THR LEU ILE THR LEU ASP ALA PRO SEQRES 7 A 80 GLY TYR SHEET 1 A 4 ALA A 1 PHE A 4 0 SHEET 2 A 4 ILE A 73 PRO A 78 -1 SHEET 3 A 4 GLY A 53 LEU A 59 -1 SHEET 4 A 4 ASP A 27 VAL A 29 -1 SHEET 1 B 4 ALA A 43 ILE A 47 0 SHEET 2 B 4 CYS A 36 ASN A 40 -1 SHEET 3 B 4 GLU A 15 VAL A 19 -1 SHEET 4 B 4 GLY A 63 VAL A 68 -1 TURN 1 A ASN A 40 ALA A 43 CISPEP 1 LYS A 24 PRO A 25 2 13.21 CISPEP 2 ALA A 77 PRO A 78 2 -22.73 CISPEP 3 ALA A 77 PRO A 78 3 -22.09 CISPEP 4 LYS A 24 PRO A 25 10 29.71 CISPEP 5 ALA A 77 PRO A 78 10 -24.56 SITE 1 LIP 1 LYS A 42 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