Header list of 1ehj.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 21-FEB-00 1EHJ TITLE A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM TITLE 2 DESULFUROMONAS ACETOXIDANS CAVEAT 1EHJ ONE RESIDUE HAS INCORRECT CHIRALITY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C7; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DESULFUROMONAS ACETOXIDANS; SOURCE 3 ORGANISM_TAXID: 891 KEYWDS MULTI-HEME, ELECTRON TRANSPORT EXPDTA SOLUTION NMR AUTHOR M.ASSFALG,L.BANCI,I.BERTINI,M.BRUSCHI,M.T.GIUDICI-ORTICONI REVDAT 3 16-FEB-22 1EHJ 1 REMARK LINK REVDAT 2 24-FEB-09 1EHJ 1 VERSN REVDAT 1 10-MAY-00 1EHJ 0 JRNL AUTH M.ASSFALG,L.BANCI,I.BERTINI,M.BRUSCHI,M.T.GIUDICI-ORTICONI JRNL TITL A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME JRNL TITL 2 C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE JRNL TITL 3 REDUCED AND THE OXIDIZED FORMS. JRNL REF EUR.J.BIOCHEM. V. 266 634 1999 JRNL REFN ISSN 0014-2956 JRNL PMID 10561607 JRNL DOI 10.1046/J.1432-1327.1999.00904.X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.ASSFALG,L.BANCI,I.BERTINI,M.BRUSCHI,P.TURANO REMARK 1 TITL 800 MHZ 1H NMR SOLUTION STRUCTURE REFINEMENT OF OXIDIZED REMARK 1 TITL 2 CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. REMARK 1 REF EUR.J.BIOCHEM. V. (2) 261 1998 REMARK 1 REFN ISSN 0014-2956 REMARK 1 DOI 10.1046/J.1432-1327.1998.2560261.X REMARK 1 REFERENCE 2 REMARK 1 AUTH L.BANCI,I.BERTINI,M.BRUSCHI,P.SOMPORNPISUT,P.TURANO REMARK 1 TITL NMR CHARACTERIZATION AND SOLUTION STRUCTURE DETERMINATION OF REMARK 1 TITL 2 THE OXIDIZED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. REMARK 1 REF PROC.NATL.ACAD.SCI.USA V.(25) 14396 1996 REMARK 1 REFN ISSN 0027-8424 REMARK 1 DOI 10.1073/PNAS.93.25.14396 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER 4.1 REMARK 3 AUTHORS : REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1352 NOE-DERIVED CONSTRAINTS REMARK 4 REMARK 4 1EHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-00. REMARK 100 THE DEPOSITION ID IS D_1000010578. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 292; 292; 292 REMARK 210 PH : 5.5; 6.5; 8.0 REMARK 210 IONIC STRENGTH : NULL; NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2-3MM CYTOCHROME 1H; 100MM REMARK 210 PHOSPHATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 3.1, XWINNMR REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED REMARK 210 WITH TORSION ANGLE DYNAMICS REMARK 210 RESTRAINED ENERGY MINIMIZATION 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES. 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 16 75.76 -68.45 REMARK 500 CYS A 26 -51.53 176.85 REMARK 500 ALA A 35 58.11 -155.81 REMARK 500 LYS A 36 -171.98 59.11 REMARK 500 ILE A 37 -50.10 -134.76 REMARK 500 ALA A 38 70.78 73.16 REMARK 500 LYS A 46 -72.63 -84.18 REMARK 500 ALA A 48 -86.69 -147.46 REMARK 500 LYS A 50 39.23 -82.63 REMARK 500 THR A 51 -52.59 -134.50 REMARK 500 LYS A 61 -93.86 -92.89 REMARK 500 CYS A 62 -155.23 -132.66 REMARK 500 CYS A 65 -56.03 -120.90 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 HEC A1030 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 17 NE2 REMARK 620 2 HEC A1030 NA 93.1 REMARK 620 3 HEC A1030 NB 90.3 90.7 REMARK 620 4 HEC A1030 NC 87.6 177.7 91.5 REMARK 620 5 HEC A1030 ND 89.0 88.5 178.9 89.3 REMARK 620 6 HIS A 30 NE2 174.2 92.7 89.4 86.6 91.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A1053 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 20 NE2 REMARK 620 2 HEC A1053 NA 93.0 REMARK 620 3 HEC A1053 NB 92.4 90.0 REMARK 620 4 HEC A1053 NC 89.2 177.1 91.7 REMARK 620 5 HEC A1053 ND 89.6 91.0 177.7 87.1 REMARK 620 6 HIS A 53 NE2 177.1 89.1 89.6 88.6 88.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A1066 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 45 NE2 REMARK 620 2 HEC A1066 NA 90.6 REMARK 620 3 HEC A1066 NB 91.4 90.7 REMARK 620 4 HEC A1066 NC 89.5 179.8 89.4 REMARK 620 5 HEC A1066 ND 93.2 90.7 175.2 89.2 REMARK 620 6 HIS A 66 NE2 177.8 91.4 89.6 88.5 85.8 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 1030 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 1053 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 1066 DBREF 1EHJ A 1 68 UNP P00137 CYC3_DESAC 1 68 SEQRES 1 A 68 ALA ASP VAL VAL THR TYR GLU ASN LYS LYS GLY ASN VAL SEQRES 2 A 68 THR PHE ASP HIS LYS ALA HIS ALA GLU LYS LEU GLY CYS SEQRES 3 A 68 ASP ALA CYS HIS GLU GLY THR PRO ALA LYS ILE ALA ILE SEQRES 4 A 68 ASP LYS LYS SER ALA HIS LYS ASP ALA CYS LYS THR CYS SEQRES 5 A 68 HIS LYS SER ASN ASN GLY PRO THR LYS CYS GLY GLY CYS SEQRES 6 A 68 HIS ILE LYS HET HEC A1030 75 HET HEC A1053 75 HET HEC A1066 75 HETNAM HEC HEME C FORMUL 2 HEC 3(C34 H34 FE N4 O4) HELIX 1 1 ASP A 16 GLY A 25 1 10 HELIX 2 2 ASP A 40 ALA A 48 1 9 HELIX 3 3 ALA A 48 HIS A 53 1 6 HELIX 4 4 LYS A 54 ASN A 56 5 3 SHEET 1 A 2 VAL A 4 TYR A 6 0 SHEET 2 A 2 VAL A 13 PHE A 15 -1 N VAL A 13 O TYR A 6 LINK SG CYS A 26 CAB HEC A1030 1555 1555 1.82 LINK SG CYS A 29 CAC HEC A1030 1555 1555 1.81 LINK SG CYS A 49 CAB HEC A1053 1555 1555 1.82 LINK SG CYS A 52 CAC HEC A1053 1555 1555 1.82 LINK SG CYS A 62 CAB HEC A1066 1555 1555 1.81 LINK SG CYS A 65 CAC HEC A1066 1555 1555 1.81 LINK NE2 HIS A 17 FE HEC A1030 1555 1555 1.91 LINK NE2 HIS A 20 FE HEC A1053 1555 1555 1.98 LINK NE2 HIS A 30 FE HEC A1030 1555 1555 1.94 LINK NE2 HIS A 45 FE HEC A1066 1555 1555 1.98 LINK NE2 HIS A 53 FE HEC A1053 1555 1555 1.96 LINK NE2 HIS A 66 FE HEC A1066 1555 1555 1.94 SITE 1 AC1 12 TYR A 6 HIS A 17 HIS A 20 ALA A 21 SITE 2 AC1 12 GLY A 25 CYS A 26 CYS A 29 HIS A 30 SITE 3 AC1 12 PRO A 34 LYS A 36 ILE A 37 ALA A 38 SITE 1 AC2 12 VAL A 13 THR A 14 HIS A 20 LYS A 23 SITE 2 AC2 12 LEU A 24 ALA A 48 CYS A 49 CYS A 52 SITE 3 AC2 12 HIS A 53 ASN A 56 ASN A 57 GLY A 64 SITE 1 AC3 15 ASN A 8 LYS A 9 LYS A 10 VAL A 13 SITE 2 AC3 15 ASP A 40 LYS A 41 ALA A 44 HIS A 45 SITE 3 AC3 15 CYS A 49 LYS A 50 HIS A 53 LYS A 61 SITE 4 AC3 15 CYS A 62 CYS A 65 HIS A 66 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 - 16 20 Bytes