Header list of 1qn0.pdb file
Complete list - v 6 2 Bytes
HEADER ELECTRON TRANSPORT 11-OCT-99 1QN0
TITLE SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS FERROCYTOCHROME C3, NMR, 20
TITLE 2 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 GIGAS;
SOURCE 3 ORGANISM_TAXID: 879;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM
KEYWDS ELECTRON TRANSPORT, HEMEPROTEIN, CYTOCHROME C3, REDOX-BOHR EFFECT,
KEYWDS 2 REDOX COOPERATIVITY, ENERGY TRANSDUCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.C.MESSIAS,M.L.TEODORO,L.BRENNAN,J.LEGALL,H.SANTOS,A.V.XAVIER,
AUTHOR 2 D.L.TURNER
REVDAT 4 06-NOV-19 1QN0 1 SEQADV LINK
REVDAT 3 24-FEB-09 1QN0 1 VERSN
REVDAT 2 16-FEB-06 1QN0 1 JRNL REMARK
REVDAT 1 12-OCT-00 1QN0 0
JRNL AUTH L.BRENNAN,D.L.TURNER,A.C.MESSIAS,M.L.TEODORO,J.LEGALL,
JRNL AUTH 2 H.SANTOS,A.V.XAVIER
JRNL TITL STRUCTURAL BASIS FOR THE NETWORK OF FUNCTIONAL
JRNL TITL 2 COOPERATIVITIES IN CYTOCHROME C3 FROM DESULFOVIBRIO GIGAS:
JRNL TITL 3 SOLUTION STRUCTURES OF THE OXIDISED AND REDUCED STATES
JRNL REF J.MOL.BIOL. V. 298 61 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10756105
JRNL DOI 10.1006/JMBI.2000.3652
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.O.LOURO,T.CATARINO,D.L.TURNER,M.A.PICARRA-PEREIRA,
REMARK 1 AUTH 2 I.PACHECO,J.LEGALL,A.V.XAVIER
REMARK 1 TITL FUNCTIONAL AND MECHANISTIC STUDIES OF CYTOCHROME C3 FROM
REMARK 1 TITL 2 DESULFOVIBRIO GIGAS: THERMODYNAMICS OF A 'PROTON THRUSTER'
REMARK 1 REF BIOCHEMISTRY V. 37 15808 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9843386
REMARK 1 DOI 10.1021/BI981505T
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.M.MATIAS,J.MORAIS,M.A.CARRONDO,K.WILSON,Z.DAUTER,L.SIEKER
REMARK 1 TITL CYTOCHROMES C3 FROM DESULFOVIBRIO GIGAS: CRYSTAL STRUCTURE
REMARK 1 TITL 2 AT 1.8 A RESOLUTION AND EVIDENCE FOR A SPECIFIC
REMARK 1 TITL 3 CALCIUM-BINDING SITE
REMARK 1 REF PROTEIN SCI. V. 5 1342 1996
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 8819167
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INDYANA
REMARK 3 AUTHORS : D.L.TURNER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION MENTIONED. INDYANA REFERENCE:D.L.TURNER, L.BRENNAN,
REMARK 3 H.E.MEYER,C.LOHAUS, C.SIETHOFF,H.S.COSTA,B.GONZALEZ, H.SANTOS,
REMARK 3 J.E.SUAREZ(1999) EUR.J.BIOCHEM., 264,833-839.
REMARK 4
REMARK 4 1QN0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1290002904.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.3
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 : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : INDYANA
REMARK 210 METHOD USED : RESTRAINED TORSION ANGLE
REMARK 210 DYNAMICS 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 : 1
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 O HIS A 29 H VAL A 32 1.52
REMARK 500 OD1 ASN A 25 H SER A 27 1.54
REMARK 500 HE1 TRP A 68 O1D HEC A 116 1.58
REMARK 500 HG1 THR A 82 OG SER A 85 1.59
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 ASP A 2 115.98 58.11
REMARK 500 1 PRO A 4 163.48 -41.23
REMARK 500 1 ASP A 6 -162.14 -57.33
REMARK 500 1 ASP A 11 86.42 -163.07
REMARK 500 1 GLU A 17 24.53 -146.91
REMARK 500 1 ASN A 19 124.22 178.48
REMARK 500 1 CYS A 37 -49.27 -131.73
REMARK 500 1 HIS A 39 43.94 -94.74
REMARK 500 1 ASP A 43 -57.84 76.27
REMARK 500 1 GLN A 45 -38.91 -39.52
REMARK 500 1 CYS A 54 -135.07 -131.95
REMARK 500 1 HIS A 55 47.40 -89.84
REMARK 500 1 LYS A 60 46.73 -87.09
REMARK 500 1 ALA A 61 58.32 178.37
REMARK 500 1 ASP A 93 -56.16 160.71
REMARK 500 1 LYS A 99 46.66 -142.92
REMARK 500 1 LYS A 100 -45.63 -167.83
REMARK 500 2 ASP A 2 119.84 59.00
REMARK 500 2 PRO A 4 163.65 -40.80
REMARK 500 2 ASP A 6 -179.35 -69.44
REMARK 500 2 ASP A 11 95.75 -164.09
REMARK 500 2 LYS A 18 -156.92 -145.78
REMARK 500 2 ASN A 19 130.84 170.18
REMARK 500 2 CYS A 37 -49.02 -131.31
REMARK 500 2 HIS A 39 45.07 -104.92
REMARK 500 2 LYS A 44 37.92 -91.30
REMARK 500 2 CYS A 54 -132.74 -130.84
REMARK 500 2 HIS A 55 46.64 -92.55
REMARK 500 2 ASP A 59 78.08 -116.67
REMARK 500 2 ALA A 61 46.84 80.05
REMARK 500 2 VAL A 65 38.20 -88.40
REMARK 500 2 ASP A 93 -56.51 160.93
REMARK 500 2 LYS A 99 45.84 -140.81
REMARK 500 2 LYS A 100 -43.72 -167.00
REMARK 500 3 ASP A 2 77.20 161.54
REMARK 500 3 VAL A 3 109.83 -53.88
REMARK 500 3 PRO A 4 163.04 -48.93
REMARK 500 3 ASP A 6 -171.29 -54.30
REMARK 500 3 ASP A 11 92.96 -161.49
REMARK 500 3 ALA A 14 174.77 -59.40
REMARK 500 3 GLU A 17 28.80 48.74
REMARK 500 3 LYS A 18 45.72 -163.22
REMARK 500 3 CYS A 37 -49.11 -131.77
REMARK 500 3 ASP A 43 -65.10 69.93
REMARK 500 3 TYR A 46 66.77 -112.82
REMARK 500 3 CYS A 54 -132.35 -131.98
REMARK 500 3 HIS A 55 48.14 -93.09
REMARK 500 3 ASP A 59 78.41 -116.57
REMARK 500 3 ALA A 61 42.82 77.99
REMARK 500 3 ASP A 93 -58.02 167.55
REMARK 500
REMARK 500 THIS ENTRY HAS 323 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 113 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 26 NE2
REMARK 620 2 HEC A 113 NA 90.6
REMARK 620 3 HEC A 113 NB 90.8 89.5
REMARK 620 4 HEC A 113 NC 87.7 178.3 90.9
REMARK 620 5 HEC A 113 ND 90.9 90.3 178.3 89.4
REMARK 620 6 HIS A 38 NE2 178.1 90.8 90.6 90.9 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 115 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 29 NE2
REMARK 620 2 HEC A 115 NA 90.0
REMARK 620 3 HEC A 115 NB 90.3 89.5
REMARK 620 4 HEC A 115 NC 89.8 179.8 90.6
REMARK 620 5 HEC A 115 ND 90.0 90.2 179.6 89.7
REMARK 620 6 HIS A 87 NE2 179.7 90.2 89.9 90.0 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 114 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEC A 114 NA 90.0
REMARK 620 3 HEC A 114 NB 91.3 89.5
REMARK 620 4 HEC A 114 NC 88.4 178.3 90.8
REMARK 620 5 HEC A 114 ND 90.4 89.7 178.2 90.0
REMARK 620 6 HIS A 55 NE2 176.4 90.8 92.2 90.8 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 116 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 73 NE2
REMARK 620 2 HEC A 116 NA 87.0
REMARK 620 3 HEC A 116 NB 90.8 90.3
REMARK 620 4 HEC A 116 NC 91.0 177.9 90.3
REMARK 620 5 HEC A 116 ND 91.2 89.6 178.0 89.8
REMARK 620 6 HIS A 110 NE2 178.3 91.3 89.4 90.7 88.6
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 113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 116
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WAD RELATED DB: PDB
REMARK 900 CYTOCHROME C3 WITH 4 HEME GROUPS AND ONE CALCIUM ION
REMARK 900 RELATED ID: 1A2I RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH)
REMARK 900 FERROCYTOCHROME C3, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1QN1 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS FERRICYTOCHROME C3, NMR,
REMARK 900 15 STRUCTURES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 40 WAS FOUND TO BE GLN
DBREF 1QN0 A 1 112 UNP P00133 CYC3_DESGI 1 112
SEQADV 1QN0 GLN A 40 UNP P00133 ASP 40 CONFLICT
SEQRES 1 A 112 VAL ASP VAL PRO ALA ASP GLY ALA LYS ILE ASP PHE ILE
SEQRES 2 A 112 ALA GLY GLY GLU LYS ASN LEU THR VAL VAL PHE ASN HIS
SEQRES 3 A 112 SER THR HIS LYS ASP VAL LYS CYS ASP ASP CYS HIS HIS
SEQRES 4 A 112 GLN PRO GLY ASP LYS GLN TYR ALA GLY CYS THR THR ASP
SEQRES 5 A 112 GLY CYS HIS ASN ILE LEU ASP LYS ALA ASP LYS SER VAL
SEQRES 6 A 112 ASN SER TRP TYR LYS VAL VAL HIS ASP ALA LYS GLY GLY
SEQRES 7 A 112 ALA LYS PRO THR CYS ILE SER CYS HIS LYS ASP LYS ALA
SEQRES 8 A 112 GLY ASP ASP LYS GLU LEU LYS LYS LYS LEU THR GLY CYS
SEQRES 9 A 112 LYS GLY SER ALA CYS HIS PRO SER
HET HEC A 113 75
HET HEC A 114 75
HET HEC A 115 75
HET HEC A 116 75
HETNAM HEC HEME C
FORMUL 2 HEC 4(C34 H34 FE N4 O4)
HELIX 1 1 SER A 85 LYS A 90 1 6
HELIX 2 2 GLU A 96 LYS A 99 5 4
SHEET 1 A 2 ALA A 8 ILE A 10 0
SHEET 2 A 2 VAL A 22 PHE A 24 -1 N PHE A 24 O ALA A 8
LINK NE2 HIS A 26 FE HEC A 113 1555 1555 1.93
LINK NE2 HIS A 29 FE HEC A 115 1555 1555 1.93
LINK SG CYS A 34 CAB HEC A 113 1555 1555 1.82
LINK SG CYS A 37 CAC HEC A 113 1555 1555 1.81
LINK NE2 HIS A 38 FE HEC A 113 1555 1555 1.92
LINK NE2 HIS A 39 FE HEC A 114 1555 1555 1.96
LINK SG CYS A 49 CAB HEC A 114 1555 1555 1.86
LINK SG CYS A 54 CAC HEC A 114 1555 1555 1.81
LINK NE2 HIS A 55 FE HEC A 114 1555 1555 1.90
LINK NE2 HIS A 73 FE HEC A 116 1555 1555 1.91
LINK SG CYS A 83 CAB HEC A 115 1555 1555 1.80
LINK SG CYS A 86 CAC HEC A 115 1555 1555 1.81
LINK NE2 HIS A 87 FE HEC A 115 1555 1555 1.95
LINK SG CYS A 104 CAB HEC A 116 1555 1555 1.84
LINK SG CYS A 109 CAC HEC A 116 1555 1555 1.81
LINK NE2 HIS A 110 FE HEC A 116 1555 1555 1.93
SITE 1 AC1 13 VAL A 3 PRO A 4 ILE A 10 PHE A 12
SITE 2 AC1 13 PHE A 24 HIS A 26 VAL A 32 LYS A 33
SITE 3 AC1 13 CYS A 34 CYS A 37 HIS A 38 TYR A 46
SITE 4 AC1 13 CYS A 49
SITE 1 AC2 8 HIS A 39 GLN A 40 GLY A 48 CYS A 49
SITE 2 AC2 8 CYS A 54 HIS A 55 VAL A 65 PRO A 81
SITE 1 AC3 11 VAL A 23 PHE A 24 HIS A 29 ASP A 36
SITE 2 AC3 11 THR A 82 CYS A 83 CYS A 86 HIS A 87
SITE 3 AC3 11 LYS A 90 LEU A 101 ALA A 108
SITE 1 AC4 17 ILE A 10 ASP A 11 PHE A 12 ILE A 13
SITE 2 AC4 17 LEU A 20 LYS A 60 TRP A 68 TYR A 69
SITE 3 AC4 17 VAL A 72 HIS A 73 CYS A 83 HIS A 87
SITE 4 AC4 17 LEU A 101 THR A 102 CYS A 104 CYS A 109
SITE 5 AC4 17 HIS A 110
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 - v 6 2 Bytes