Header list of 1w3d.pdb file
Complete list - n 24 2 Bytes
HEADER TRANSFERASE 14-JUL-04 1W3D TITLE NMR STRUCTURE OF THE PERIPHERAL-SUBUNIT BINDING DOMAIN OF BACILLUS TITLE 2 STEAROTHERMOPHILUS E2P COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF COMPND 3 PYRUVATE DEHYDROGENASE; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: RESIDUES 118-170; COMPND 6 SYNONYM: COMPLEX DIHYDROPOAMIDE ACETYLTRANSFERASE; COMPND 7 EC: 2.3.1.12; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS; SOURCE 3 ORGANISM_TAXID: 1422; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET11C KEYWDS TRANSFERASE, PERIPHERAL-SUBUNIT BINDING DOMAIN, DIHYDROLIPOAMIDE KEYWDS 2 ACETYLTRANSFERASE, DIHYDROLIPOAMIDE DEHYDROGENASE, PROTEIN- PROTEIN KEYWDS 3 INTERACTION, PROTEIN STRUCTURE, MULTIENZYME COMPLEX, BACILLUS KEYWDS 4 STEROTHERMOPHILUS, GLYCOLYSIS, ACYLTRANSFERASE, LIPOYL EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.D.ALLEN,R.W.BROADHURST,R.G.SOLOMON,R.N.PERHAM REVDAT 6 24-JAN-18 1W3D 1 SOURCE REVDAT 5 24-FEB-09 1W3D 1 VERSN REVDAT 4 16-FEB-06 1W3D 1 AUTHOR REVDAT 3 12-JAN-05 1W3D 1 JRNL REVDAT 2 02-AUG-04 1W3D 1 REMARK REVDAT 1 20-JUL-04 1W3D 0 JRNL AUTH M.D.ALLEN,R.W.BROADHURST,R.G.SOLOMON,R.N.PERHAM JRNL TITL INTERACTION OF THE E2 AND E3 COMPONENTS OF THE PYRUVATE JRNL TITL 2 DEHYDROGENASE MULTIENZYME COMPLEX OF BACILLUS JRNL TITL 3 STEAROTHERMOPHILUS. USE OF A TRUNCATED PROTEIN DOMAIN IN NMR JRNL TITL 4 SPECTROSCOPY JRNL REF FEBS J. V. 272 259 2005 JRNL REFN ISSN 1742-464X JRNL PMID 15634348 JRNL DOI 10.1111/J.1432-1033.2004.04405.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 1W3D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUL-04. REMARK 100 THE DEPOSITION ID IS D_1290020460. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20 REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AM REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AZARA, ANSIG, CNS REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATION > 0.25A REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NONE 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 400 REMARK 400 COMPOUND REMARK 400 CATALYTIC ACTIVITY: ACETYL-COA + ENZYME N(6)-(DIHYDROLIPOYL)LYSINE REMARK 400 = COA + ENZYME N(6)-(S-ACETYLDIHYDROLIPOYL)LYSINE. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 117 REMARK 465 SER A 118 REMARK 465 ALA A 119 REMARK 465 GLU A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 ALA A 123 REMARK 465 GLY A 124 REMARK 465 PRO A 125 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 ALA A 171 CA C O CB 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 ARG A 127 82.64 -175.54 REMARK 500 2 LEU A 167 -76.39 -86.88 REMARK 500 3 THR A 152 30.09 -148.19 REMARK 500 3 LYS A 154 -49.73 73.55 REMARK 500 3 ASN A 155 27.12 -155.50 REMARK 500 3 LEU A 167 -80.10 -105.69 REMARK 500 3 ALA A 168 100.08 53.41 REMARK 500 5 LEU A 167 -73.60 -75.81 REMARK 500 6 ALA A 131 -169.86 -113.15 REMARK 500 6 LYS A 154 -78.69 63.48 REMARK 500 6 LEU A 167 -75.66 -71.95 REMARK 500 7 ILE A 130 52.98 -108.34 REMARK 500 7 LYS A 154 -75.08 64.83 REMARK 500 7 LEU A 167 -76.21 -72.52 REMARK 500 7 ALA A 168 -78.45 -67.12 REMARK 500 8 THR A 152 42.81 -140.67 REMARK 500 8 LYS A 154 102.62 55.69 REMARK 500 8 LEU A 167 -71.90 -74.61 REMARK 500 9 LYS A 154 -70.87 67.16 REMARK 500 10 LYS A 154 -90.55 42.72 REMARK 500 10 LEU A 167 -77.80 -90.44 REMARK 500 10 ALA A 168 -80.71 -73.33 REMARK 500 13 ALA A 168 -74.39 -58.12 REMARK 500 14 LEU A 167 -83.18 -96.33 REMARK 500 14 ALA A 168 -177.64 50.45 REMARK 500 15 LYS A 154 97.94 56.17 REMARK 500 15 ASN A 155 -66.15 70.16 REMARK 500 16 ARG A 128 -177.35 -64.70 REMARK 500 17 LYS A 154 -90.90 38.97 REMARK 500 18 ARG A 127 63.12 -119.43 REMARK 500 18 LEU A 167 -72.53 -71.15 REMARK 500 19 ARG A 127 55.52 -97.39 REMARK 500 19 ARG A 128 175.80 61.06 REMARK 500 19 ILE A 130 50.03 -93.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1B5S RELATED DB: PDB REMARK 900 DIHYDROLIPOYL TRANSACETYLASE CATALYTIC DOMAIN ( RESIDUES 184-425) REMARK 900 FROM BACILLUS STEAROTHERMOPHILUS REMARK 900 RELATED ID: 1EBD RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF REMARK 900 THE DIHYDROLIPOAMIDE ACETYLASE REMARK 900 RELATED ID: 1LAB RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE REMARK 900 DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (LIPOYLATED DOMAIN, REMARK 900 RESIDUES 1 - 80) (NMR, 11 STRUCTURES) REMARK 900 RELATED ID: 1LAC RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE REMARK 900 DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (LIPOYLATED DOMAIN, REMARK 900 RESIDUES 1 - 80) (NMR, AVERAGE STRUCTURE) REMARK 900 RELATED ID: 2PDD RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE REMARK 900 DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (PYRUVATE DECARBOXYLASE REMARK 900 (E1P ) / DIHYDROLIPOAMIDE DEHYDROGENASE (E3) 43 RESIDUE BINDING REMARK 900 DOMAIN) (NMR, 35 STRUCTURES) REMARK 900 RELATED ID: 2PDE RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) SUBUNIT OF THE PYRUVATE REMARK 900 DEHYDROGENASE (PDH) MULTIENZYME COMPLEX (PYRUVATE DECARBOXYLASE REMARK 900 (E1P ) / DIHYDROLIPOAMIDE DEHYDROGENASE (E3) 43 RESIDUE BINDING REMARK 900 DOMAIN) (NMR, AVERAGE STRUCTURE) DBREF 1W3D A 117 118 PDB 1W3D 1W3D 117 118 DBREF 1W3D A 119 171 UNP P11961 ODP2_BACST 118 170 SEQRES 1 A 55 GLY SER ALA GLU ALA GLU ALA GLY PRO ASN ARG ARG VAL SEQRES 2 A 55 ILE ALA MET PRO SER VAL ARG LYS TYR ALA ARG GLU LYS SEQRES 3 A 55 GLY VAL ASP ILE ARG LEU VAL GLN GLY THR GLY LYS ASN SEQRES 4 A 55 GLY ARG VAL LEU LYS GLU ASP ILE ASP ALA PHE LEU ALA SEQRES 5 A 55 GLY GLY ALA HELIX 1 1 MET A 132 GLY A 143 1 12 HELIX 2 2 ASP A 145 VAL A 149 5 5 HELIX 3 3 LEU A 159 ALA A 168 1 10 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 - n 24 2 Bytes