Header list of 1hrq.pdb file
Complete list - 23 20 Bytes
HEADER ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 17-JAN-95 1HRQ TITLE THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL TITLE 2 IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIGH POTENTIAL IRON SULFUR PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALLOCHROMATIUM VINOSUM; SOURCE 3 ORGANISM_TAXID: 1049 KEYWDS ELECTRON TRANSFER (IRON-SULFUR PROTEIN) EXPDTA SOLUTION NMR AUTHOR L.BANCI,I.BERTINI,A.DIKIY,D.H.W.KASTRAU,C.LUCHINAT,P.SOMPORNPISUT REVDAT 5 23-FEB-22 1HRQ 1 REMARK REVDAT 4 24-MAR-09 1HRQ 1 ATOM CONECT REVDAT 3 24-FEB-09 1HRQ 1 VERSN REVDAT 2 01-APR-03 1HRQ 1 JRNL REVDAT 1 03-JUN-95 1HRQ 0 JRNL AUTH L.BANCI,I.BERTINI,A.DIKIY,D.H.KASTRAU,C.LUCHINAT, JRNL AUTH 2 P.SOMPORNPISUT JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED JRNL TITL 2 HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM JRNL TITL 3 THROUGH NMR. JRNL REF BIOCHEMISTRY V. 34 206 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 7819198 JRNL DOI 10.1021/BI00001A025 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.GAILLARD,J.-P.ALBRAND,J.-M.MOULIS,D.E.WEMMER REMARK 1 TITL SEQUENCE-SPECIFIC ASSIGNMENTS OF THE 1H NUCLEAR MAGNETIC REMARK 1 TITL 2 RESONANCE SPECTRA OF REDUCED HIGH-POTENTIAL FERREDOXIN REMARK 1 TITL 3 (HIPIP) FROM CHROMATIUM VINOSUM REMARK 1 REF BIOCHEMISTRY V. 31 5632 1992 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH I.BERTINI,F.CAPOZZI,S.CIURLI,C.LUCHINAT,L.MESSORI,M.PICCIOLI REMARK 1 TITL IDENTIFICATION OF THE IRON IONS OF HIGH POTENTIAL IRON REMARK 1 TITL 2 PROTEIN FROM CHROMATIUM VINOSUM WITHIN THE PROTEIN FRAME REMARK 1 TITL 3 THROUGH TWO-DIMENSIONAL NMR EXPERIMENTS REMARK 1 REF J.AM.CHEM.SOC. V. 9 3332 1992 REMARK 1 REFN ISSN 0002-7863 REMARK 1 REFERENCE 3 REMARK 1 AUTH C.W.CARTER JUNIOR,J.KRAUT,S.T.FREER,N.-H.XUONG,R.A.ALDEN, REMARK 1 AUTH 2 R.G.BARTSCH REMARK 1 TITL TWO-ANGSTROM CRYSTAL STRUCTURE OF OXIDIZED CHROMATIUM HIGH REMARK 1 TITL 2 POTENTIAL IRON PROTEIN REMARK 1 REF J.BIOL.CHEM. V. 249 4212 1974 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : GUENTERT,BRAUN,WUTHRICH (DIANA), REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN REMARK 3 (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173982. 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 : 1 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 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 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 ASP A 22 85.87 -69.47 REMARK 500 LYS A 83 104.30 -36.32 REMARK 500 ALA A 84 -144.24 -88.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 86 FE1 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 43 SG REMARK 620 2 SF4 A 86 S2 112.7 REMARK 620 3 SF4 A 86 S3 111.9 106.0 REMARK 620 4 SF4 A 86 S4 112.8 105.7 107.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 86 FE2 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 46 SG REMARK 620 2 SF4 A 86 S1 112.8 REMARK 620 3 SF4 A 86 S3 112.8 106.4 REMARK 620 4 SF4 A 86 S4 110.6 106.7 107.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 86 FE3 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 63 SG REMARK 620 2 SF4 A 86 S1 110.3 REMARK 620 3 SF4 A 86 S2 114.0 107.0 REMARK 620 4 SF4 A 86 S4 112.6 106.4 106.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 SF4 A 86 FE4 REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 77 SG REMARK 620 2 SF4 A 86 S1 108.4 REMARK 620 3 SF4 A 86 S2 112.4 107.1 REMARK 620 4 SF4 A 86 S3 115.8 106.0 106.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 86 DBREF 1HRQ A 1 85 UNP P00260 HIP_CHRVI 38 122 SEQRES 1 A 85 SER ALA PRO ALA ASN ALA VAL ALA ALA ASP ASP ALA THR SEQRES 2 A 85 ALA ILE ALA LEU LYS TYR ASN GLN ASP ALA THR LYS SER SEQRES 3 A 85 GLU ARG VAL ALA ALA ALA ARG PRO GLY LEU PRO PRO GLU SEQRES 4 A 85 GLU GLN HIS CYS ALA ASN CYS GLN PHE MET GLN ALA ASP SEQRES 5 A 85 ALA ALA GLY ALA THR ASP GLU TRP LYS GLY CYS GLN LEU SEQRES 6 A 85 PHE PRO GLY LYS LEU ILE ASN VAL ASN GLY TRP CYS ALA SEQRES 7 A 85 SER TRP THR LEU LYS ALA GLY HET SF4 A 86 8 HETNAM SF4 IRON/SULFUR CLUSTER FORMUL 2 SF4 FE4 S4 HELIX 1 1 ALA A 12 LEU A 17 1 6 HELIX 2 2 GLU A 27 ALA A 31 5 5 HELIX 3 3 PRO A 38 GLU A 40 5 3 HELIX 4 4 CYS A 43 ASN A 45 5 3 SHEET 1 A 3 MET A 49 GLN A 50 0 SHEET 2 A 3 TRP A 60 CYS A 63 -1 N GLY A 62 O GLN A 50 SHEET 3 A 3 PHE A 66 ASN A 72 -1 N PHE A 66 O CYS A 63 LINK SG CYS A 43 FE1 SF4 A 86 1555 1555 2.03 LINK SG CYS A 46 FE2 SF4 A 86 1555 1555 2.02 LINK SG CYS A 63 FE3 SF4 A 86 1555 1555 2.03 LINK SG CYS A 77 FE4 SF4 A 86 1555 1555 2.03 SITE 1 AC1 6 CYS A 43 CYS A 46 PHE A 48 CYS A 63 SITE 2 AC1 6 PHE A 66 CYS A 77 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
Complete list - 23 20 Bytes