HEADER ELECTRON TRANSPORT 04-APR-02 1LC1
TITLE SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C IN
TITLE 2 30% ACETONITRILE SOLUTION, NMR MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FERROCYTOCHROME C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 ORGAN: HEART
KEYWDS CYTOCHROME C, ORGANIC SOLVENT, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR S.G.SIVAKOLUNDU,P.A.MABROUK
REVDAT 2 24-FEB-09 1LC1 1 VERSN
REVDAT 1 03-JUN-03 1LC1 0
JRNL AUTH S.G.SIVAKOLUNDU,P.A.MABROUK
JRNL TITL STRUCTURE FUNCTION RELATIONSHIP OF REDUCED
JRNL TITL 2 CYTOCHROME C PROBED BY COMPLETE SOLUTION STRUCTURE
JRNL TITL 3 DETERMINATION IN 30% ACETONITRILE/WATER SOLUTION
JRNL REF J.BIOL.INORG.CHEM. V. 8 527 2003
JRNL REFN ISSN 0949-8257
JRNL PMID 12764601
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 5.0
REMARK 3 AUTHORS : CASE, PEARLMAN, CALDWELL, CHEATHAM III, ROSS,
REMARK 3 SIMMERLING, DARDEN, MERZ, STANTON, CHENG,
REMARK 3 VINCENT, CROWLEY, FERGUSON, RADMER, SEIBEL,
REMARK 3 SINGH, WEINER, KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF
REMARK 3 2232 NOE-BASED DISTANCE RESTRAINTS AND 73 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1LC1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015826.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5MM FERROCYTOCHROME C 1H;
REMARK 210 50MM PHOSPHATE BUFFER; 70%
REMARK 210 H2O, 30% CD3CN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 591.1 MHZ
REMARK 210 SPECTROMETER MODEL : HOME BUILT
REMARK 210 SPECTROMETER MANUFACTURER : HOME BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : RNMR 1.0, FELIX 2000, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS, RESTRAINED
REMARK 210 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 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 CYS A 17 -41.31 -141.58
REMARK 500 HIS A 18 70.22 -104.11
REMARK 500 THR A 28 3.91 -154.02
REMARK 500 HIS A 33 89.40 -54.64
REMARK 500 PHE A 46 98.04 -63.66
REMARK 500 ILE A 57 -4.23 -54.37
REMARK 500 THR A 58 117.73 56.69
REMARK 500 ASN A 70 56.18 -163.22
REMARK 500 MET A 80 94.57 -64.07
REMARK 500 PHE A 82 -37.97 -163.38
REMARK 500 ALA A 83 -17.68 46.91
REMARK 500 LYS A 86 -84.09 160.93
REMARK 500 ALA A 101 -8.68 -58.45
REMARK 500 ASN A 103 -10.12 -153.87
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 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 MET A 80 SD 173.2
REMARK 620 N 1
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 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LC2 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C IN
REMARK 900 30% ACETONITRILE SOLUTION, NMR 30 STRUCTURES
DBREF 1LC1 A 1 104 UNP P00004 CYC_HORSE 1 104
SEQRES 1 A 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 A 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 A 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 A 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 A 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 A 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 A 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 A 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
HET HEC A 105 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 ASP A 50 GLY A 56 1 7
HELIX 3 3 LYS A 60 ASN A 70 1 11
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 ALA A 101 1 15
LINK FE HEC A 105 NE2 HIS A 18 1555 1555 1.97
LINK FE HEC A 105 SD MET A 80 1555 1555 2.68
LINK CAB HEC A 105 SG CYS A 14 1555 1555 1.80
LINK CAC HEC A 105 SG CYS A 17 1555 1555 1.82
SITE 1 AC1 17 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 17 THR A 28 PRO A 30 LEU A 35 THR A 40
SITE 3 AC1 17 ASN A 52 TRP A 59 TYR A 67 LEU A 68
SITE 4 AC1 17 THR A 78 LYS A 79 MET A 80 PHE A 82
SITE 5 AC1 17 LEU A 94
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
(ATOM LINES ARE NOT SHOWN.)
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