Header list of 1e8e.pdb file
Complete list - n 15 2 Bytes
HEADER OXIDOREDUCTASE(CYTOCHROME) 20-SEP-00 1E8E
TITLE SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS CYTOCHROME C''.
TITLE 2 INSIGHTS INTO THE STRUCTURAL BASIS OF HAEM-LIGAND DETACHMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C'';
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: C-TYPE CYTOCHROME, FULLY OXIDISED FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOPHILUS METHYLOTROPHUS;
SOURCE 3 ORGANISM_COMMON: BACTERIUM W3A1;
SOURCE 4 ORGANISM_TAXID: 17
KEYWDS OXIDOREDUCTASE(CYTOCHROME), CYTOCHROME C'', LIGAND DETACHMENT, REDOX-
KEYWDS 2 BOHR EFFECT, PARAMAGNETIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BRENNAN,D.L.TURNER,P.FARELEIRA,H.SANTOS
REVDAT 3 15-JAN-20 1E8E 1 LINK
REVDAT 2 24-FEB-09 1E8E 1 VERSN
REVDAT 1 20-SEP-01 1E8E 0
JRNL AUTH L.BRENNAN,D.L.TURNER,P.FARELEIRA,H.SANTOS
JRNL TITL SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOTROPHUS
JRNL TITL 2 CYTOCHROME C": INSIGHTS INTO THE STRUCTURAL BASIS OF
JRNL TITL 3 HAEM-LIGAND DETACHMENT
JRNL REF J.MOL.BIOL. V. 308 353 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11327772
JRNL DOI 10.1006/JMBI.2001.4600
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.S.COSTA,H.SANTOS,D.L.TURNER
REMARK 1 TITL CHARACTERIZATION OF THE HAEM ENVIRONMENT IN METHYLOPHILUS
REMARK 1 TITL 2 METHYLOTROPHUS FERRICYTOCHROME C'' BY 1H-NMR
REMARK 1 REF EUR.J.BIOCHEM. V. 215 817 1993
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 8394812
REMARK 1 DOI 10.1111/J.1432-1033.1993.TB18097.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.S.COSTA,H.SANTOS,D.L.TURNER,A.V.XAVIER
REMARK 1 TITL INVOLVEMENT OF A LABILE AXIAL HISTIDINE IN COUPLING ELECTRON
REMARK 1 TITL 2 AND PROTON TRANSFER IN METHYLOPHILUS METHYLOTROPHUS
REMARK 1 TITL 3 CYTOCHROME C''
REMARK 1 REF EUR.J.BIOCHEM. V. 208 427 1992
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 1325909
REMARK 1 DOI 10.1111/J.1432-1033.1992.TB17204.X
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.SANTOS,D.L.TURNER
REMARK 1 TITL CHARACTERIZATION AND NMR STUDIES OF A NOVEL CYTOCHROME C
REMARK 1 TITL 2 ISOLATED FROM METHYLOPHILUS METHYLOTROPHUS WHICH SHOWS A
REMARK 1 TITL 3 REDOX-LINKED CHANGE OS SPIN-STATE
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 954 277 1988
REMARK 1 REFN ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PARADYANA
REMARK 3 AUTHORS : D.L.TURNER,L.BRENNAN,S.G.CHAMBERLIN, R.O.LOURO,
REMARK 3 A.V.XAVIER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DIPOLAR SHIFTS WERE USED AS RESTRAINTS
REMARK 3 IN AN EXTENDED VERSION OF DYANA CALLED PARADYANA. D.L.TURNER,L,
REMARK 3 BRENNAN,S.G.CHAMBERLIN, R.O.LOURO,A.V.XAVIER (1998)DETERMINATION
REMARK 3 OF SOLUTION STRUCTURES OF PARAMAGNETIC PROTEINS BY
REMARK 3 NMR.EUR.BIOPHYS.J.27,367-375.
REMARK 4
REMARK 4 1E8E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1290005380.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 10 MM PHOSPATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-NOESY; 2D-1H-TOCSY; 2D-1H
REMARK 210 -COSY; 3D(15N; 1H)-TOCSY-HSQC;
REMARK 210 1H)-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PARADYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS WITH
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
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 ALA A 16 H ASN A 20 1.51
REMARK 500 O VAL A 2 H GLU A 6 1.52
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 VAL A 2 -41.47 87.08
REMARK 500 1 LYS A 11 -71.76 -96.28
REMARK 500 1 LYS A 32 -66.55 -141.21
REMARK 500 1 ASN A 36 22.62 -140.21
REMARK 500 1 LYS A 38 96.24 -56.42
REMARK 500 1 LYS A 45 124.79 172.49
REMARK 500 1 THR A 54 172.02 50.27
REMARK 500 1 LYS A 68 -94.44 -81.97
REMARK 500 1 GLU A 69 123.13 -177.99
REMARK 500 1 PRO A 71 167.83 -48.94
REMARK 500 1 PRO A 72 131.46 -37.76
REMARK 500 1 ALA A 74 98.42 -37.89
REMARK 500 1 LYS A 80 43.72 -107.82
REMARK 500 1 PHE A 82 64.76 36.44
REMARK 500 1 THR A 83 -64.26 -101.51
REMARK 500 1 ASP A 90 -50.35 178.39
REMARK 500 1 ILE A 99 -51.63 -121.71
REMARK 500 1 THR A 118 -67.61 -127.49
REMARK 500 2 VAL A 2 49.10 -145.91
REMARK 500 2 LYS A 11 -72.79 -100.20
REMARK 500 2 ILE A 28 38.16 -92.60
REMARK 500 2 THR A 29 34.68 -148.47
REMARK 500 2 ASP A 30 -49.94 -137.23
REMARK 500 2 LYS A 32 -72.16 -51.98
REMARK 500 2 LYS A 38 94.27 -51.66
REMARK 500 2 LYS A 45 112.34 178.68
REMARK 500 2 THR A 54 170.61 50.26
REMARK 500 2 LYS A 68 -94.54 -79.08
REMARK 500 2 GLU A 69 123.94 -179.47
REMARK 500 2 PRO A 71 167.08 -49.00
REMARK 500 2 PRO A 72 132.05 -37.18
REMARK 500 2 ALA A 74 113.41 -39.28
REMARK 500 2 PHE A 82 62.78 36.60
REMARK 500 2 ASP A 84 79.70 -174.86
REMARK 500 2 ASP A 90 -66.94 176.69
REMARK 500 2 LEU A 117 33.32 -91.98
REMARK 500 2 THR A 118 -68.02 -141.62
REMARK 500 3 VAL A 2 -21.65 87.35
REMARK 500 3 LYS A 11 -72.72 -97.90
REMARK 500 3 PRO A 26 -167.45 -75.25
REMARK 500 3 THR A 29 35.82 -162.21
REMARK 500 3 ASP A 30 -49.46 -143.99
REMARK 500 3 LYS A 32 -74.02 -46.44
REMARK 500 3 ASN A 36 28.37 -140.99
REMARK 500 3 LYS A 38 95.69 -44.50
REMARK 500 3 LYS A 45 123.13 -175.22
REMARK 500 3 THR A 54 170.39 50.25
REMARK 500 3 LYS A 62 131.75 176.10
REMARK 500 3 ALA A 74 97.80 -37.73
REMARK 500 3 LYS A 80 43.82 -104.93
REMARK 500
REMARK 500 THIS ENTRY HAS 426 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 125 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 53 NE2
REMARK 620 2 HEC A 125 NA 91.6
REMARK 620 3 HEC A 125 NB 90.3 90.1
REMARK 620 4 HEC A 125 NC 91.0 177.4 90.5
REMARK 620 5 HEC A 125 ND 87.1 89.5 177.4 90.0
REMARK 620 6 HIS A 95 NE2 178.8 88.4 90.9 89.0 91.7
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 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4837 RELATED DB: BMRB
DBREF 1E8E A 1 124 UNP Q9RQB9 Q9RQB9 21 144
SEQRES 1 A 124 ASP VAL THR ASN ALA GLU LYS LEU VAL TYR LYS TYR THR
SEQRES 2 A 124 ASN ILE ALA HIS SER ALA ASN PRO MET TYR GLU ALA PRO
SEQRES 3 A 124 SER ILE THR ASP GLY LYS ILE PHE PHE ASN ARG LYS PHE
SEQRES 4 A 124 LYS THR PRO SER GLY LYS GLU ALA ALA CYS ALA SER CYS
SEQRES 5 A 124 HIS THR ASN ASN PRO ALA ASN VAL GLY LYS ASN ILE VAL
SEQRES 6 A 124 THR GLY LYS GLU ILE PRO PRO LEU ALA PRO ARG VAL ASN
SEQRES 7 A 124 THR LYS ARG PHE THR ASP ILE ASP LYS VAL GLU ASP GLU
SEQRES 8 A 124 PHE THR LYS HIS CYS ASN ASP ILE LEU GLY ALA ASP CYS
SEQRES 9 A 124 SER PRO SER GLU LYS ALA ASN PHE ILE ALA TYR LEU LEU
SEQRES 10 A 124 THR GLU THR LYS PRO THR LYS
HET HEC A 125 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 VAL A 2 ASN A 20 1 19
HELIX 2 2 LYS A 32 ASN A 36 5 5
HELIX 3 3 LYS A 87 LEU A 100 1 14
HELIX 4 4 SER A 105 LEU A 117 1 13
SHEET 1 A 2 PHE A 39 THR A 41 0
SHEET 2 A 2 LYS A 45 ALA A 47 -1 N ALA A 47 O PHE A 39
SSBOND 1 CYS A 96 CYS A 104 1555 1555 1.99
LINK SG CYS A 49 CAB HEC A 125 1555 1555 1.88
LINK SG CYS A 52 CAC HEC A 125 1555 1555 1.81
LINK NE2 HIS A 53 FE HEC A 125 1555 1555 1.94
LINK NE2 HIS A 95 FE HEC A 125 1555 1555 1.95
SITE 1 AC1 11 ALA A 48 CYS A 49 SER A 51 CYS A 52
SITE 2 AC1 11 HIS A 53 ASN A 63 ILE A 70 LEU A 73
SITE 3 AC1 11 PHE A 92 HIS A 95 PHE A 112
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
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