Header list of 2btg.pdb file
Complete list - n 24 2 Bytes
HEADER TRANSFERASE 31-MAY-05 2BTG 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 2BTG 1 SOURCE REVDAT 3 19-APR-17 2BTG 1 REMARK REVDAT 2 24-FEB-09 2BTG 1 VERSN REVDAT 1 24-MAY-06 2BTG 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 2BTG 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_1290024184. 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 D2O 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 : SIMULATED ANNEALING 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 LYS A 169 33.11 -97.89 REMARK 500 2 ASN A 128 -46.57 -147.33 REMARK 500 3 ALA A 130 -38.51 -179.97 REMARK 500 3 VAL A 154 70.64 -107.40 REMARK 500 4 ASN A 128 102.98 60.47 REMARK 500 4 ALA A 130 -54.18 -174.83 REMARK 500 5 ASN A 127 54.13 -170.54 REMARK 500 5 ASN A 128 -58.80 75.58 REMARK 500 5 ASP A 129 135.85 76.00 REMARK 500 5 THR A 152 51.82 -118.69 REMARK 500 5 VAL A 154 35.52 -152.34 REMARK 500 6 ASN A 127 107.45 -172.24 REMARK 500 6 LYS A 169 30.11 -98.39 REMARK 500 7 ASN A 143 57.09 70.05 REMARK 500 7 VAL A 154 33.13 -99.14 REMARK 500 8 ASN A 127 168.73 60.76 REMARK 500 8 VAL A 154 76.51 -67.30 REMARK 500 9 ASN A 128 -41.03 -174.15 REMARK 500 9 ALA A 130 -66.92 -166.60 REMARK 500 10 ASN A 127 -39.88 -177.13 REMARK 500 11 ASN A 127 174.93 64.17 REMARK 500 11 LYS A 169 -68.67 -107.20 REMARK 500 12 VAL A 154 75.91 -68.53 REMARK 500 13 ALA A 130 -56.46 78.04 REMARK 500 13 VAL A 154 80.26 -65.15 REMARK 500 14 THR A 152 45.03 -147.96 REMARK 500 14 VAL A 154 49.94 -91.46 REMARK 500 15 ASN A 128 -46.53 -141.03 REMARK 500 15 ALA A 130 -49.97 -171.39 REMARK 500 16 ASP A 129 37.78 -164.89 REMARK 500 17 ASN A 128 31.91 -152.18 REMARK 500 17 ASN A 143 61.73 65.69 REMARK 500 17 THR A 152 27.53 -147.71 REMARK 500 17 VAL A 154 30.61 -99.08 REMARK 500 18 ASN A 128 -177.18 -59.48 REMARK 500 18 ALA A 130 -51.65 -156.92 REMARK 500 19 ASN A 127 -69.05 68.23 REMARK 500 19 VAL A 154 76.37 -69.80 REMARK 500 19 LYS A 169 66.14 -117.77 REMARK 500 20 ASN A 128 73.54 -68.22 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: 2BTH RELATED DB: PDB REMARK 900 PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, REMARK 900 AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- REMARK 900 STATE TRANSITIONS 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 2BTG A 124 125 PDB 2BTG 2BTG 124 125 DBREF 2BTG A 126 170 UNP P07016 ODO2_ECOLI 108 152 SEQADV 2BTG 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