HEADER ELECTRON TRANSPORT 03-JUL-96 1OCD
TITLE CYTOCHROME C (OXIDIZED) FROM EQUUS CABALLUS, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: OXIDIZED
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 ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR P.X.QI,R.A.BECKMAN,A.J.WAND
REVDAT 4 14-MAR-18 1OCD 1 JRNL REMARK
REVDAT 3 29-NOV-17 1OCD 1 REMARK HELIX
REVDAT 2 24-FEB-09 1OCD 1 VERSN
REVDAT 1 16-JUN-97 1OCD 0
JRNL AUTH P.X.QI,R.A.BECKMAN,A.J.WAND
JRNL TITL SOLUTION STRUCTURE OF HORSE HEART FERRICYTOCHROME C AND
JRNL TITL 2 DETECTION OF REDOX-RELATED STRUCTURAL CHANGES BY
JRNL TITL 3 HIGH-RESOLUTION 1H NMR.
JRNL REF BIOCHEMISTRY V. 35 12275 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8823161
JRNL DOI 10.1021/BI961042W
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.X.QI,J.L.URBAUER,E.J.FUENTES,M.F.LEOPOLD,A.J.WAND
REMARK 1 TITL STRUCTURAL WATER IN OXIDIZED AND REDUCED HORSE HEART
REMARK 1 TITL 2 CYTOCHROME C
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 378 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 7664051
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.X.QI,D.L.DI STEFANO,A.J.WAND
REMARK 1 TITL SOLUTION STRUCTURE OF HORSE HEART FERROCYTOCHROME C
REMARK 1 TITL 2 DETERMINED BY HIGH-RESOLUTION NMR AND RESTRAINED SIMULATED
REMARK 1 TITL 3 ANNEALING
REMARK 1 REF BIOCHEMISTRY V. 33 6408 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8204573
REMARK 1 REFERENCE 3
REMARK 1 AUTH Y.FENG,H.RODER,S.W.ENGLANDER,A.J.WAND,D.L.DI STEFANO
REMARK 1 TITL PROTON RESONANCE ASSIGNMENTS OF HORSE FERRICYTOCHROME C
REMARK 1 REF BIOCHEMISTRY V. 28 195 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 2539855
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OCD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175428.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : [U-15N] 7-10 MM CYTOCHROME C, 50
REMARK 210 MM POTASSIUM PHOSPHATE; [U-13C;
REMARK 210 U-15N] 15 MM CYTOCHROME C, 50 MM
REMARK 210 POTASSIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY; 3D NOESY
REMARK 210 -TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 300 MHZ
REMARK 210 SPECTROMETER MODEL : AM; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DSPACE, X-PLOR, FELIX
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 64
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 H ALA A 43 H1 HOH A 203 1.31
REMARK 500 HA ASN A 31 H2 HOH A 200 1.32
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 VAL A 3 -68.05 -107.75
REMARK 500 CYS A 14 40.96 -101.92
REMARK 500 VAL A 20 -55.26 -136.19
REMARK 500 LYS A 27 -142.21 -58.62
REMARK 500 LEU A 35 175.81 -47.72
REMARK 500 PHE A 36 72.10 -2.41
REMARK 500 ARG A 38 -42.63 81.49
REMARK 500 THR A 40 -61.99 -100.04
REMARK 500 GLN A 42 -101.01 -55.51
REMARK 500 PRO A 44 -17.87 -48.01
REMARK 500 PHE A 46 -109.32 -64.29
REMARK 500 THR A 47 18.67 -150.47
REMARK 500 TYR A 48 157.94 -44.23
REMARK 500 THR A 49 -155.31 -78.57
REMARK 500 ASP A 50 54.70 -90.04
REMARK 500 ALA A 51 -57.25 -167.32
REMARK 500 LYS A 55 -152.48 -54.87
REMARK 500 ILE A 57 -151.85 -89.66
REMARK 500 TRP A 59 50.32 -145.57
REMARK 500 LYS A 60 -132.06 -89.98
REMARK 500 GLU A 61 -85.85 -80.52
REMARK 500 MET A 65 -35.44 -30.28
REMARK 500 PRO A 71 -78.36 -51.64
REMARK 500 LYS A 72 -28.45 -39.80
REMARK 500 ILE A 75 92.67 -161.35
REMARK 500 PHE A 82 107.92 179.91
REMARK 500 ALA A 83 73.23 -105.46
REMARK 500 LYS A 87 -99.73 -48.33
REMARK 500 LYS A 88 -73.83 179.98
REMARK 500 ILE A 95 -76.46 -57.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 38 0.31 SIDE CHAIN
REMARK 500 ARG A 91 0.31 SIDE CHAIN
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 HEC A 105 NA 92.0
REMARK 620 3 HEC A 105 NB 78.6 89.8
REMARK 620 4 HEC A 105 NC 80.6 172.5 89.6
REMARK 620 5 HEC A 105 ND 93.9 89.3 172.4 90.3
REMARK 620 6 MET A 80 SD 152.0 112.5 113.4 74.5 73.8
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 105
DBREF 1OCD 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
FORMUL 3 HOH *6(H2 O)
HELIX 1 NR VAL A 3 CYS A 14 1 12
HELIX 2 60R LYS A 60 LEU A 68 1 9
HELIX 3 70R ASN A 70 ILE A 75 5 6
HELIX 4 CR LYS A 88 THR A 102 1 15
LINK CAB HEC A 105 SG CYS A 14 1555 1555 1.81
LINK CAC HEC A 105 SG CYS A 17 1555 1555 1.81
LINK FE HEC A 105 NE2 HIS A 18 1555 1555 2.06
LINK FE HEC A 105 SD MET A 80 1555 1555 2.44
SITE 1 AC1 20 CYS A 14 CYS A 17 HIS A 18 PRO A 30
SITE 2 AC1 20 THR A 40 GLN A 42 THR A 47 TYR A 48
SITE 3 AC1 20 THR A 49 ASN A 52 TRP A 59 LEU A 64
SITE 4 AC1 20 TYR A 67 LEU A 68 THR A 78 LYS A 79
SITE 5 AC1 20 MET A 80 PHE A 82 ILE A 85 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.)
END
