Header list of 1w4k.pdb file
Complete list - n 12 2 Bytes
HEADER TRANSFERASE 23-JUL-04 1W4K TITLE PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, TITLE 2 THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY TITLE 3 ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PYRUVATE DEHYDROGENASE E2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 93-141; COMPND 5 SYNONYM: DIHYDROLIPOAMIDE ACETYLTRANSFERASE; COMPND 6 EC: 2.3.1.12; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PYROBACULUM AEROPHILUM; SOURCE 3 ORGANISM_TAXID: 13773; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRSETA KEYWDS ULTRAFAST FOLDING, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR N.FERGUSON,T.D.SHARPE,P.J.SCHARTAU,M.D.ALLEN,C.M.JOHNSON, AUTHOR 2 S.SATO,A.R.FERSHT REVDAT 3 22-MAY-13 1W4K 1 KEYWDS REMARK VERSN DBREF REVDAT 3 2 ATOM TER MASTER REVDAT 2 24-FEB-09 1W4K 1 VERSN REVDAT 1 20-JUL-05 1W4K 0 JRNL AUTH N.FERGUSON,T.D.SHARPE,P.J.SCHARTAU,S.SATO, JRNL AUTH 2 M.D.ALLEN,C.M.JOHNSON,T.J.RUTHERFORD,A.R.FERSHT JRNL TITL ULTRA-FAST BARRIER-LIMITED FOLDING IN THE JRNL TITL 2 PERIPHERAL 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 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, REMARK 3 RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE REMARK 4 REMARK 4 1W4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-04. REMARK 100 THE PDBE ID CODE IS EBI-20578. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0 REMARK 210 PH : 6.2 REMARK 210 IONIC STRENGTH : 100 REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 95% H2O/ 5% D2O, REMARK 210 3MM SAMPLE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : 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 VIOLATIONS >0.25 REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE REMARK 210 NMR SPECTROSCOPY ON 13C, 15N LABELED PROTEIN 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 MUTATION LEU 112 ALA AND TYR 132 TRP 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 GLU A 128 169.63 56.57 REMARK 500 1 MET A 132 167.42 -46.31 REMARK 500 1 ASP A 145 103.12 -58.94 REMARK 500 1 LYS A 150 92.86 -50.92 REMARK 500 1 PRO A 154 106.83 -44.72 REMARK 500 2 SER A 126 177.98 60.54 REMARK 500 2 MET A 132 163.60 -45.08 REMARK 500 2 LYS A 150 92.48 -50.82 REMARK 500 2 PRO A 154 106.14 -44.34 REMARK 500 2 THR A 174 79.10 53.22 REMARK 500 3 MET A 132 166.26 -48.33 REMARK 500 3 ASP A 145 101.07 -56.52 REMARK 500 3 LYS A 150 100.97 -50.90 REMARK 500 3 PRO A 154 104.40 -44.68 REMARK 500 3 THR A 174 -74.84 -123.73 REMARK 500 4 MET A 132 164.64 -46.42 REMARK 500 4 LYS A 150 91.33 -50.96 REMARK 500 4 PRO A 154 102.95 -43.85 REMARK 500 5 ARG A 127 -65.07 -125.86 REMARK 500 5 MET A 132 167.77 -47.11 REMARK 500 5 LYS A 150 100.27 -50.78 REMARK 500 5 PRO A 154 107.74 -44.91 REMARK 500 6 SER A 126 -55.03 -140.68 REMARK 500 6 ARG A 127 -63.25 -156.11 REMARK 500 6 GLU A 128 -81.82 -149.39 REMARK 500 6 MET A 132 167.08 -46.82 REMARK 500 6 ASP A 145 101.07 -57.82 REMARK 500 6 LYS A 150 91.41 -50.81 REMARK 500 6 PRO A 154 104.92 -44.70 REMARK 500 7 SER A 126 -56.07 -142.67 REMARK 500 7 GLU A 128 -176.43 48.24 REMARK 500 7 MET A 132 166.75 -46.35 REMARK 500 7 ASP A 145 101.02 -59.06 REMARK 500 7 LYS A 150 91.34 -50.94 REMARK 500 7 PRO A 154 103.53 -43.74 REMARK 500 8 GLU A 128 -80.08 -77.73 REMARK 500 8 MET A 132 166.47 -46.28 REMARK 500 8 ASP A 145 101.15 -58.33 REMARK 500 8 LYS A 150 96.50 -50.87 REMARK 500 8 PRO A 154 106.59 -44.76 REMARK 500 9 GLU A 128 156.87 62.73 REMARK 500 9 MET A 132 166.78 -46.74 REMARK 500 9 LYS A 150 107.52 -50.76 REMARK 500 9 PRO A 154 106.50 -44.37 REMARK 500 10 MET A 132 167.25 -47.02 REMARK 500 10 ASP A 145 101.03 -57.07 REMARK 500 10 LYS A 150 95.82 -50.72 REMARK 500 10 PRO A 154 105.00 -44.69 REMARK 500 11 SER A 126 31.31 -159.57 REMARK 500 11 ARG A 127 127.10 -172.90 REMARK 500 REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1W4E RELATED DB: PDB REMARK 900 PERIPHERAL-SUBUNIT BINDING DOMAINS FROM REMARK 900 MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC REMARK 900 BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- REMARK 900 STATE TRANSITIONS REMARK 900 RELATED ID: 1W4G RELATED DB: PDB REMARK 900 PERIPHERAL-SUBUNIT BINDING DOMAINS FROM REMARK 900 MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC REMARK 900 BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- REMARK 900 STATE FOLDING TRANSITIONS REMARK 900 RELATED ID: 1W4I RELATED DB: PDB REMARK 900 PERIPHERAL-SUBUNIT BINDING DOMAINS FROM REMARK 900 MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC REMARK 900 BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- REMARK 900 STATE TRANSITIONS REMARK 900 RELATED ID: 1W4J RELATED DB: PDB REMARK 900 PERIPHERAL-SUBUNIT BINDING DOMAINS FROM REMARK 900 MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC REMARK 900 BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO- REMARK 900 STATE TRANSITIONS REMARK 999 REMARK 999 SEQUENCE REMARK 999 L146A DESTABILISATION FOR BIOPHYSICAL STUDIES Y166W REMARK 999 ENGINEERED FLUOROPHORE DBREF 1W4K A 125 126 PDB 1W4K 1W4K 125 126 DBREF 1W4K A 127 175 UNP Q8ZUR6 Q8ZUR6_PYRAE 93 141 SEQADV 1W4K ALA A 146 UNP Q8ZUR6 LEU 112 ENGINEERED MUTATION SEQADV 1W4K TRP A 166 UNP Q8ZUR6 TYR 132 ENGINEERED MUTATION SEQRES 1 A 51 GLY SER ARG GLU VAL ALA ALA MET PRO ALA ALA ARG ARG SEQRES 2 A 51 LEU ALA LYS GLU LEU GLY ILE ASP ALA SER LYS VAL LYS SEQRES 3 A 51 GLY THR GLY PRO GLY GLY VAL ILE THR VAL GLU ASP VAL SEQRES 4 A 51 LYS ARG TRP ALA GLU GLU THR ALA LYS ALA THR ALA HELIX 1 1 MET A 132 GLY A 143 1 12 HELIX 2 2 THR A 159 ALA A 173 1 15 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 12 2 Bytes