Header list of 1a2i.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 05-JAN-98 1A2I TITLE SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) TITLE 2 FERROCYTOCHROME C3, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYTOCHROME C3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TETRAHEME CYTOCHROME; COMPND 5 OTHER_DETAILS: CLASS III OF C-TYPE CYTOCHROMES, FULLY REDUCED FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP. VULGARIS STR. SOURCE 3 HILDENBOROUGH; SOURCE 4 ORGANISM_TAXID: 882; SOURCE 5 STRAIN: HILDENBOROUGH; SOURCE 6 CELLULAR_LOCATION: PERIPLASM KEYWDS ELECTRON TRANSPORT, HEMEPROTEIN, ELECTRON TRANSFER, REDOX-BOHR KEYWDS 2 EFFECT, COOPERATIVITY, ENERGY TRANSDUCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.C.MESSIAS,D.H.K.KASTRAU,H.S.COSTA,J.LEGALL,D.L.TURNER,H.SANTOS, AUTHOR 2 A.V.XAVIER REVDAT 4 16-FEB-22 1A2I 1 REMARK LINK REVDAT 3 24-FEB-09 1A2I 1 VERSN REVDAT 2 01-APR-03 1A2I 1 JRNL REVDAT 1 08-JUL-98 1A2I 0 JRNL AUTH A.C.MESSIAS,D.H.KASTRAU,H.S.COSTA,J.LEGALL,D.L.TURNER, JRNL AUTH 2 H.SANTOS,A.V.XAVIER JRNL TITL SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) JRNL TITL 2 FERROCYTOCHROME C3: STRUCTURAL BASIS FOR FUNCTIONAL JRNL TITL 3 COOPERATIVITY. JRNL REF J.MOL.BIOL. V. 281 719 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9710542 JRNL DOI 10.1006/JMBI.1998.1974 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH P.SIMOES,P.M.MATIAS,J.MORAIS,K.WILSON,Z.DAUTER,M.A.CARRONDO REMARK 1 TITL REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURES OF REMARK 1 TITL 2 CYTOCHROMES C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH AT REMARK 1 TITL 3 1.67 A RESOLUTION AND FROM DESULFOVIBRIO DESULFURICANS REMARK 1 TITL 4 ATCC27774 AT 1.6 A RESOLUTION REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH R.O.LOURO,T.CATARINO,J.LEGALL,A.V.XAVIER REMARK 1 TITL REDOX-BOHR EFFECT IN ELECTRON/PROTON ENERGY TRANSDUCTION: REMARK 1 TITL 2 CYTOCHROME C3 COUPLED TO HYDROGENASE WORKS AS A 'PROTON REMARK 1 TITL 3 THRUSTER' IN DESULFOVIBRIO VULGARIS REMARK 1 REF J.BIOL.INORG.CHEM. V. 2 488 1997 REMARK 1 REFN ISSN 0949-8257 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.L.TURNER,C.A.SALGUEIRO,T.CATARINO,J.LEGALL,A.V.XAVIER REMARK 1 TITL NMR STUDIES OF COOPERATIVITY IN THE TETRAHAEM CYTOCHROME C3 REMARK 1 TITL 2 FROM DESULFOVIBRIO VULGARIS REMARK 1 REF EUR.J.BIOCHEM. V. 241 723 1996 REMARK 1 REFN ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 1A2I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170311. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 8.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-NOESY 2D-1H-TOCSY 2D-1H REMARK 210 -COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS REMARK 210 WITH SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 600 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HG1 THR A 14 O1D HEC A 111 1.44 REMARK 500 O HIS A 83 H ALA A 87 1.50 REMARK 500 O VAL A 80 H VAL A 84 1.56 REMARK 500 REMARK 500 REMARK: NULL 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 3 -172.49 47.51 REMARK 500 1 GLU A 12 67.33 -108.19 REMARK 500 1 HIS A 25 34.66 -99.23 REMARK 500 1 ASN A 38 -1.13 82.55 REMARK 500 1 ALA A 49 102.37 -54.92 REMARK 500 1 CYS A 51 -92.25 -108.74 REMARK 500 1 HIS A 52 74.60 -107.11 REMARK 500 1 LYS A 57 -64.81 69.64 REMARK 500 1 ASP A 59 -51.15 -140.63 REMARK 500 1 LYS A 60 90.51 41.99 REMARK 500 1 SER A 61 -54.65 -157.87 REMARK 500 1 ALA A 62 -54.48 -179.44 REMARK 500 1 HIS A 70 -60.06 -132.91 REMARK 500 1 ASP A 71 132.14 -39.00 REMARK 500 1 ALA A 89 60.93 -113.13 REMARK 500 1 ALA A 91 146.01 61.37 REMARK 500 1 ALA A 92 -50.41 84.03 REMARK 500 1 LYS A 102 46.03 72.15 REMARK 500 2 PRO A 2 -89.65 -74.96 REMARK 500 2 LYS A 3 157.82 176.29 REMARK 500 2 ALA A 6 -170.56 -56.27 REMARK 500 2 GLU A 12 67.21 -108.63 REMARK 500 2 ASN A 38 35.03 -98.88 REMARK 500 2 ALA A 49 108.74 -54.69 REMARK 500 2 CYS A 51 -90.53 -105.53 REMARK 500 2 HIS A 52 70.80 -109.55 REMARK 500 2 ASP A 59 90.56 -171.91 REMARK 500 2 SER A 61 -66.94 174.12 REMARK 500 2 ALA A 62 -45.51 -176.25 REMARK 500 2 HIS A 70 -61.91 -132.49 REMARK 500 2 ASP A 71 132.01 -38.87 REMARK 500 2 ALA A 89 89.92 40.25 REMARK 500 2 ASP A 90 -43.28 -165.05 REMARK 500 2 ALA A 91 144.11 75.20 REMARK 500 2 ALA A 92 -48.19 84.49 REMARK 500 2 LYS A 102 42.51 74.09 REMARK 500 3 PRO A 2 -87.01 -74.94 REMARK 500 3 LYS A 3 155.82 172.71 REMARK 500 3 ALA A 6 -172.17 -54.96 REMARK 500 3 GLU A 12 68.50 -108.84 REMARK 500 3 HIS A 25 33.45 -97.55 REMARK 500 3 ASN A 38 32.21 -94.82 REMARK 500 3 ALA A 49 108.53 -54.83 REMARK 500 3 CYS A 51 -91.10 -105.51 REMARK 500 3 HIS A 52 69.66 -109.00 REMARK 500 3 ASP A 59 -58.09 -122.95 REMARK 500 3 LYS A 60 -139.60 63.21 REMARK 500 3 SER A 61 -71.55 72.16 REMARK 500 3 ALA A 62 -42.51 -178.69 REMARK 500 3 HIS A 70 -63.35 -132.60 REMARK 500 REMARK 500 THIS ENTRY HAS 302 RAMACHANDRAN OUTLIERS. 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 A 108 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 22 NE2 REMARK 620 2 HEC A 108 NA 90.5 REMARK 620 3 HEC A 108 NB 90.2 89.8 REMARK 620 4 HEC A 108 NC 89.0 179.4 90.4 REMARK 620 5 HEC A 108 ND 90.4 90.1 179.4 89.7 REMARK 620 6 HIS A 34 NE2 179.7 89.6 90.2 91.0 89.2 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 110 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 25 NE2 REMARK 620 2 HEC A 110 NA 91.4 REMARK 620 3 HEC A 110 NB 91.8 89.8 REMARK 620 4 HEC A 110 NC 89.3 179.2 90.2 REMARK 620 5 HEC A 110 ND 87.4 90.0 179.2 89.9 REMARK 620 6 HIS A 83 NE2 177.8 88.7 90.4 90.6 90.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 109 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 35 NE2 REMARK 620 2 HEC A 109 NA 90.6 REMARK 620 3 HEC A 109 NB 90.4 89.6 REMARK 620 4 HEC A 109 NC 88.3 178.8 90.9 REMARK 620 5 HEC A 109 ND 90.7 90.1 178.8 89.5 REMARK 620 6 HIS A 52 NE2 178.5 90.7 90.3 90.4 88.6 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEC A 111 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 70 NE2 REMARK 620 2 HEC A 111 NA 91.4 REMARK 620 3 HEC A 111 NB 90.4 90.1 REMARK 620 4 HEC A 111 NC 87.2 178.6 90.3 REMARK 620 5 HEC A 111 ND 90.9 89.8 178.7 89.9 REMARK 620 6 HIS A 106 NE2 177.6 90.9 90.0 90.4 88.7 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 108 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 110 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 111 DBREF 1A2I A 1 107 UNP P00131 CYC3_DESVH 23 129 SEQRES 1 A 107 ALA PRO LYS ALA PRO ALA ASP GLY LEU LYS MET GLU ALA SEQRES 2 A 107 THR LYS GLN PRO VAL VAL PHE ASN HIS SER THR HIS LYS SEQRES 3 A 107 SER VAL LYS CYS GLY ASP CYS HIS HIS PRO VAL ASN GLY SEQRES 4 A 107 LYS GLU ASP TYR ARG LYS CYS GLY THR ALA GLY CYS HIS SEQRES 5 A 107 ASP SER MET ASP LYS LYS ASP LYS SER ALA LYS GLY TYR SEQRES 6 A 107 TYR HIS VAL MET HIS ASP LYS ASN THR LYS PHE LYS SER SEQRES 7 A 107 CYS VAL GLY CYS HIS VAL GLU VAL ALA GLY ALA ASP ALA SEQRES 8 A 107 ALA LYS LYS LYS ASP LEU THR GLY CYS LYS LYS SER LYS SEQRES 9 A 107 CYS HIS GLU HET HEC A 108 75 HET HEC A 109 75 HET HEC A 110 75 HET HEC A 111 75 HETNAM HEC HEME C FORMUL 2 HEC 4(C34 H34 FE N4 O4) HELIX 1 1 LYS A 29 HIS A 34 1 6 HELIX 2 2 GLY A 64 VAL A 68 5 5 HELIX 3 3 SER A 78 GLY A 88 1 11 HELIX 4 4 ALA A 92 LYS A 94 1 3 SHEET 1 A 2 LEU A 9 MET A 11 0 SHEET 2 A 2 VAL A 18 PHE A 20 -1 N PHE A 20 O LEU A 9 LINK SG CYS A 30 CAB HEC A 108 1555 1555 1.85 LINK SG CYS A 33 CAC HEC A 108 1555 1555 1.81 LINK SG CYS A 46 CAB HEC A 109 1555 1555 1.83 LINK SG CYS A 51 CAC HEC A 109 1555 1555 1.81 LINK SG CYS A 79 CAB HEC A 110 1555 1555 1.85 LINK SG CYS A 82 CAC HEC A 110 1555 1555 1.81 LINK SG CYS A 100 CAB HEC A 111 1555 1555 1.87 LINK SG CYS A 105 CAC HEC A 111 1555 1555 1.81 LINK NE2 HIS A 22 FE HEC A 108 1555 1555 1.93 LINK NE2 HIS A 25 FE HEC A 110 1555 1555 1.91 LINK NE2 HIS A 34 FE HEC A 108 1555 1555 1.94 LINK NE2 HIS A 35 FE HEC A 109 1555 1555 1.93 LINK NE2 HIS A 52 FE HEC A 109 1555 1555 1.93 LINK NE2 HIS A 70 FE HEC A 111 1555 1555 1.92 LINK NE2 HIS A 83 FE HEC A 110 1555 1555 1.94 LINK NE2 HIS A 106 FE HEC A 111 1555 1555 1.93 SITE 1 AC1 19 LYS A 3 ALA A 4 PRO A 5 LEU A 9 SITE 2 AC1 19 MET A 11 PHE A 20 HIS A 22 HIS A 25 SITE 3 AC1 19 VAL A 28 LYS A 29 CYS A 30 CYS A 33 SITE 4 AC1 19 HIS A 34 TYR A 43 ARG A 44 LYS A 45 SITE 5 AC1 19 CYS A 46 HEC A 109 HEC A 110 SITE 1 AC2 15 CYS A 33 HIS A 35 LYS A 45 CYS A 46 SITE 2 AC2 15 CYS A 51 HIS A 52 SER A 61 ALA A 62 SITE 3 AC2 15 HIS A 67 VAL A 68 ASN A 73 THR A 74 SITE 4 AC2 15 LYS A 75 PHE A 76 HEC A 108 SITE 1 AC3 13 PHE A 20 THR A 24 HIS A 25 ASP A 32 SITE 2 AC3 13 CYS A 33 LYS A 77 CYS A 79 CYS A 82 SITE 3 AC3 13 HIS A 83 VAL A 86 LEU A 97 LYS A 104 SITE 4 AC3 13 HEC A 108 SITE 1 AC4 16 MET A 11 ALA A 13 THR A 14 GLN A 16 SITE 2 AC4 16 VAL A 18 TYR A 65 TYR A 66 HIS A 70 SITE 3 AC4 16 VAL A 80 HIS A 83 LEU A 97 THR A 98 SITE 4 AC4 16 GLY A 99 CYS A 100 CYS A 105 HIS A 106 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 - b 16 2 Bytes