Header list of 2bth.pdb file
Complete list - n 24 2 Bytes
HEADER TRANSFERASE 31-MAY-05 2BTH TITLE PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND TITLE 2 HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TITLE 3 TRANSITIONS COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT COMPND 3 OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: RESIDUES 108-152; COMPND 6 SYNONYM: E3-BINDING DOMAIN, E2; COMPND 7 EC: 2.3.1.61; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; 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: MODIFIED PRSETA KEYWDS ACYLTRANSFERASE, LIPOYL, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.FERGUSON,M.D.ALLEN REVDAT 4 24-JAN-18 2BTH 1 SOURCE REVDAT 3 19-APR-17 2BTH 1 REMARK REVDAT 2 24-FEB-09 2BTH 1 VERSN REVDAT 1 24-MAY-06 2BTH 0 JRNL AUTH N.FERGUSON,T.D.SHARPE,P.J.SCHARTAU,S.SATO,M.D.ALLEN, JRNL AUTH 2 C.M.JOHNSON,T.J.RUTHERFORD,A.R.FERSHT JRNL TITL ULTRA-FAST BARRIER-LIMITED FOLDING IN THE PERIPHERAL JRNL TITL 2 SUBUNIT-BINDING DOMAIN FAMILY. JRNL REF J.MOL.BIOL. V. 353 427 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 16168437 JRNL DOI 10.1016/J.JMB.2005.08.031 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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 ABOVE REMARK 4 REMARK 4 2BTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1290024183. 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 : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 50 MM POTASSIUM PHOSPHATE, 10% REMARK 210 D2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE 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 : ACCEPTED 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 ENGINEERED RESIDUE IN CHAIN A, HIS 166 TO TRP 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 124 REMARK 465 SER A 125 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 ASN A 127 32.04 -99.03 REMARK 500 1 ALA A 130 -68.96 -128.93 REMARK 500 1 LYS A 150 175.11 -48.83 REMARK 500 1 THR A 152 35.00 -145.01 REMARK 500 1 LYS A 169 39.86 -98.52 REMARK 500 2 VAL A 154 91.35 -64.12 REMARK 500 3 ALA A 130 -36.99 178.35 REMARK 500 3 LYS A 150 175.11 -51.30 REMARK 500 3 THR A 152 69.12 -112.51 REMARK 500 3 VAL A 154 34.16 -153.61 REMARK 500 3 LYS A 169 87.44 -150.23 REMARK 500 4 ALA A 130 -59.68 -134.60 REMARK 500 4 VAL A 154 38.04 -154.33 REMARK 500 5 ASN A 127 30.72 -98.62 REMARK 500 5 LYS A 150 175.05 -48.27 REMARK 500 5 LYS A 169 31.88 -98.02 REMARK 500 6 ASN A 127 -78.19 -90.13 REMARK 500 6 ALA A 130 -64.67 -155.91 REMARK 500 6 ASN A 143 67.08 68.81 REMARK 500 6 LYS A 150 175.08 -49.48 REMARK 500 6 VAL A 154 35.25 -145.12 REMARK 500 7 ASN A 128 -177.36 -66.42 REMARK 500 7 ASN A 143 55.86 70.16 REMARK 500 7 THR A 152 42.80 -100.04 REMARK 500 7 VAL A 154 36.56 -153.42 REMARK 500 7 LYS A 169 36.32 -97.67 REMARK 500 8 ASN A 143 55.48 70.03 REMARK 500 8 LYS A 150 175.03 -48.57 REMARK 500 8 VAL A 154 32.51 -97.97 REMARK 500 9 ASN A 127 81.72 60.69 REMARK 500 9 VAL A 154 67.17 -70.00 REMARK 500 10 ASN A 127 91.31 60.54 REMARK 500 10 ASP A 129 -178.93 -59.55 REMARK 500 10 ALA A 130 -38.50 -177.15 REMARK 500 11 ASN A 127 -39.71 -177.35 REMARK 500 11 ASN A 143 55.86 70.48 REMARK 500 11 LYS A 150 175.11 -50.20 REMARK 500 11 VAL A 154 71.39 -68.84 REMARK 500 12 ASN A 127 -68.02 -134.09 REMARK 500 12 LYS A 150 175.19 -50.23 REMARK 500 12 THR A 152 33.17 -142.36 REMARK 500 13 ASN A 127 -177.18 58.95 REMARK 500 13 ASP A 129 28.67 -145.65 REMARK 500 13 THR A 152 44.50 -93.34 REMARK 500 13 VAL A 154 85.21 -61.30 REMARK 500 14 ASN A 128 170.25 61.04 REMARK 500 14 LYS A 169 68.31 -159.04 REMARK 500 15 ASN A 128 70.24 -176.77 REMARK 500 15 LYS A 150 175.14 -50.79 REMARK 500 16 ASP A 129 46.14 -94.75 REMARK 500 REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BAL RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E3-BINDING DOMAIN) CORE FROM REMARK 900 THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF (NMR, 56 REMARK 900 SIMULATED ANNEALING STRUCTURES) REMARK 900 RELATED ID: 1BBL RELATED DB: PDB REMARK 900 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E3-BINDING DOMAIN) CORE FROM REMARK 900 THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA REMARK 900 COLI (NMR, MINIMIZED AVERAGE STRUCTURE) REMARK 900 RELATED ID: 1C4T RELATED DB: PDB REMARK 900 CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE REMARK 900 RELATED ID: 1E2O RELATED DB: PDB REMARK 900 CATALYTIC DOMAIN FROM DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE REMARK 900 RELATED ID: 1PMR RELATED DB: PDB REMARK 900 LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT REMARK 900 OF THE 2- OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF REMARK 900 ESCHERICHIA COLI, NMR, 25 STRUCTURES REMARK 900 RELATED ID: 1SCZ RELATED DB: PDB REMARK 900 IMPROVED STRUCTURAL MODEL FOR THE CATALYTIC DOMAIN OFE.COLI REMARK 900 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE REMARK 900 RELATED ID: 2BTG RELATED DB: PDB REMARK 900 LIPOYL DOMAIN FROM THE DIHYDROLIPOYL SUCCINYLTRANSFERASE COMPONENT REMARK 900 OF THE 2- OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF REMARK 900 ESCHERICHIA COLI, NMR, 20 STRUCTURES REMARK 999 REMARK 999 SEQUENCE REMARK 999 GLY-SER AT THE N-TERMINUS IS THE REMAINS OF A THROMBIN REMARK 999 CLEAVAGE SITE. HIS TO TRP MUTATION IS A DELIBERATE REMARK 999 MUTATION TO ALLOW FOR FOLDING STUDIES DBREF 2BTH A 124 125 PDB 2BTH 2BTH 124 125 DBREF 2BTH A 126 170 UNP P07016 ODO2_ECOLI 108 152 SEQADV 2BTH TRP A 166 UNP P07016 HIS 149 ENGINEERED MUTATION SEQRES 1 A 47 GLY SER GLN ASN ASN ASP ALA LEU SER PRO ALA ILE ARG SEQRES 2 A 47 ARG LEU LEU ALA GLU HIS ASN LEU ASP ALA SER ALA ILE SEQRES 3 A 47 LYS GLY THR GLY VAL GLY GLY ARG LEU THR ARG GLU ASP SEQRES 4 A 47 VAL GLU LYS TRP LEU ALA LYS ALA HELIX 1 1 SER A 132 ASN A 143 1 12 HELIX 2 2 ASP A 145 ILE A 149 5 5 HELIX 3 3 THR A 159 LYS A 169 1 11 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