Header list of 1hko.pdb file
Complete list - r 19 2 Bytes
HEADER ELECTRON TRANSPORT 10-MAR-03 1HKO
TITLE NMR STRUCTURE OF BOVINE CYTOCHROME B5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEME BINDING DOMAIN, RESIDUES 1-104;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET21D
KEYWDS CYTOCHROME, ELECTRON TRANSFER PROTEIN, HEME, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 42
AUTHOR F.W.MUSKETT,D.WHITFORD
REVDAT 3 19-APR-17 1HKO 1 REMARK
REVDAT 2 24-FEB-09 1HKO 1 VERSN
REVDAT 1 18-MAR-03 1HKO 0
SPRSDE 10-MAR-03 1HKO 1WDB
JRNL AUTH F.W.MUSKETT,G.P.KELLY,D.WHITFORD
JRNL TITL THE SOLUTION STRUCTURE OF BOVINE FERRICYTOCHROME B5
JRNL TITL 2 DETERMINED USING HETERONUCLEAR NMR METHODS.
JRNL REF J.MOL.BIOL. V. 258 172 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8613986
JRNL DOI 10.1006/JMBI.1996.0241
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: 5 CYCLES OF REDAC PROCEDURE
REMARK 4
REMARK 4 1HKO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12345.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-1H HSQC; 15N-1H TOCSY-HSQC;
REMARK 210 15N-1H NOESY HSQC; CBCANH;
REMARK 210 CBCA(CO)NH; HCCH-TOCSY; (HB)
REMARK 210 CB(CGCD)HD/HE; 13C-EDITED NOESY
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; UNITY; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 42
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED FROM A COMBINATION OF TRIPLE
REMARK 210 RESONANCE NMR EXPERIMENTS ON 13C, 15N LABELED CYTOCHROME B5
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 400
REMARK 400 COMPOUND
REMARK 400 CYTOCHROME B5 IS A MEMBRANE BOUND HEMOPROTEIN WHICH
REMARK 400 FUNCTIONS AS AN ELECTRON CARRIER FOR SEVERAL MEMBRANE BOUND
REMARK 400 OXYGENASES.
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 HE2 HIS A 67 FE HEM A 105 1.02
REMARK 500 HE2 HIS A 43 FE HEM A 105 1.28
REMARK 500 HE2 HIS A 30 HE ARG A 72 1.33
REMARK 500 O VAL A 49 HE21 GLN A 53 1.33
REMARK 500 O GLU A 48 H GLU A 52 1.40
REMARK 500 O ALA A 58 H PHE A 62 1.57
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 GLU A 2 77.88 -166.97
REMARK 500 1 GLU A 3 166.51 179.52
REMARK 500 1 SER A 5 142.45 -177.88
REMARK 500 1 ALA A 7 93.52 69.26
REMARK 500 1 LYS A 9 -60.89 75.62
REMARK 500 1 ASN A 20 19.95 -141.54
REMARK 500 1 HIS A 30 -60.90 68.90
REMARK 500 1 TYR A 31 1.89 -176.60
REMARK 500 1 LEU A 40 -70.10 -60.51
REMARK 500 1 GLU A 42 -176.00 -51.18
REMARK 500 1 HIS A 43 136.33 84.57
REMARK 500 1 VAL A 49 -31.18 -38.70
REMARK 500 1 HIS A 67 -178.69 -68.86
REMARK 500 1 ASP A 87 40.39 -163.87
REMARK 500 1 ILE A 91 -47.73 -131.69
REMARK 500 1 THR A 92 144.31 -33.36
REMARK 500 1 LYS A 93 108.54 67.04
REMARK 500 1 SER A 95 146.50 -179.03
REMARK 500 1 THR A 101 75.03 -159.15
REMARK 500 1 ASP A 103 91.40 -169.41
REMARK 500 2 GLU A 2 111.57 -177.74
REMARK 500 2 GLU A 3 171.74 172.19
REMARK 500 2 SER A 5 172.59 176.84
REMARK 500 2 LYS A 6 108.61 175.03
REMARK 500 2 ALA A 7 93.36 -173.76
REMARK 500 2 VAL A 8 -73.93 -38.48
REMARK 500 2 LYS A 9 -53.38 78.74
REMARK 500 2 ASN A 20 30.28 -147.74
REMARK 500 2 HIS A 30 -51.60 73.41
REMARK 500 2 TYR A 31 -9.14 177.20
REMARK 500 2 LEU A 40 -71.97 -70.43
REMARK 500 2 GLU A 42 177.31 -48.72
REMARK 500 2 HIS A 43 134.24 88.87
REMARK 500 2 VAL A 49 -26.77 -39.46
REMARK 500 2 HIS A 84 -176.77 -65.93
REMARK 500 2 ASP A 87 51.88 -179.07
REMARK 500 2 ILE A 91 -43.48 -140.68
REMARK 500 2 SER A 95 123.89 -176.44
REMARK 500 2 GLU A 96 145.66 177.97
REMARK 500 2 ASP A 103 136.23 66.91
REMARK 500 3 SER A 5 153.02 179.11
REMARK 500 3 LYS A 6 144.40 -175.28
REMARK 500 3 ALA A 7 108.99 -165.11
REMARK 500 3 LYS A 9 -55.92 77.56
REMARK 500 3 ASN A 20 24.75 -144.45
REMARK 500 3 HIS A 30 -57.79 71.89
REMARK 500 3 TYR A 31 0.24 -177.66
REMARK 500 3 GLU A 42 -154.26 -89.73
REMARK 500 3 HIS A 43 171.45 68.38
REMARK 500 3 HIS A 84 -177.23 -65.94
REMARK 500
REMARK 500 THIS ENTRY HAS 757 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 HEM A 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 67 NE2
REMARK 620 2 HEM A 105 NA 97.1
REMARK 620 3 HEM A 105 NB 82.2 90.2
REMARK 620 4 HEM A 105 NC 82.3 179.4 89.8
REMARK 620 5 HEM A 105 ND 97.4 90.7 179.1 89.4
REMARK 620 6 HIS A 43 NE2 169.6 73.4 93.3 107.1 87.3
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 HEM A 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CYO RELATED DB: PDB
REMARK 900 BOVINE CYTOCHROME B(5)
REMARK 900 RELATED ID: 1EHB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN- SOLUBILIZED FRAGMENT OF
REMARK 900 CYTOCHROME B5
REMARK 900 RELATED ID: 1ES1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED
REMARK 900 FRAGMENT OF CYTOCHROME B5
REMARK 900 RELATED ID: 1F03 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5
REMARK 900 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME
REMARK 900 C
REMARK 900 RELATED ID: 1F04 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5
REMARK 900 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME
REMARK 900 C
REMARK 900 RELATED ID: 1I5U RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE MUTANT(E48A/E56A/D60A)
REMARK 900 RELATED ID: 1LQX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF V45E MUTANT OF CYTOCHROME B5
REMARK 900 RELATED ID: 1LR6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF V45Y MUTANT OF CYTOCHROME B5
REMARK 900 RELATED ID: 1M20 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF F35Y MUTANT OF TRYPSIN -SOLUBILIZEDFRAGMENT OF
REMARK 900 CYTOCHROME B5
REMARK 900 RELATED ID: 1WDB RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF BOVINE CYTOCHROME B5, MINIMIZED AVERAGE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 5745 RELATED DB: BMRB
DBREF 1HKO A 1 104 UNP P00171 CYB5_BOVIN 1 104
SEQRES 1 A 104 ALA GLU GLU SER SER LYS ALA VAL LYS TYR TYR THR LEU
SEQRES 2 A 104 GLU GLU ILE GLN LYS HIS ASN ASN SER LYS SER THR TRP
SEQRES 3 A 104 LEU ILE LEU HIS TYR LYS VAL TYR ASP LEU THR LYS PHE
SEQRES 4 A 104 LEU GLU GLU HIS PRO GLY GLY GLU GLU VAL LEU ARG GLU
SEQRES 5 A 104 GLN ALA GLY GLY ASP ALA THR GLU ASN PHE GLU ASP VAL
SEQRES 6 A 104 GLY HIS SER THR ASP ALA ARG GLU LEU SER LYS THR PHE
SEQRES 7 A 104 ILE ILE GLY GLU LEU HIS PRO ASP ASP ARG SER LYS ILE
SEQRES 8 A 104 THR LYS PRO SER GLU SER ILE ILE THR THR ILE ASP SER
HET HEM A 105 63
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 THR A 12 HIS A 19 1 8
HELIX 2 2 LEU A 36 LEU A 40 1 5
HELIX 3 3 GLU A 47 GLU A 52 1 6
HELIX 4 4 ALA A 58 GLU A 63 1 6
HELIX 5 5 SER A 68 LYS A 76 1 9
SHEET 1 AA 5 LYS A 9 TYR A 11 0
SHEET 2 AA 5 ILE A 79 LEU A 83 1 O ILE A 80 N LYS A 9
SHEET 3 AA 5 LYS A 32 ASP A 35 -1 O VAL A 33 N ILE A 80
SHEET 4 AA 5 TRP A 26 LEU A 29 -1 O LEU A 27 N TYR A 34
SHEET 5 AA 5 GLY A 56 ASP A 57 1 O GLY A 56 N ILE A 28
LINK NE2 HIS A 67 FE HEM A 105 1555 1555 1.92
LINK FE HEM A 105 NE2 HIS A 43 1555 1555 2.22
SITE 1 AC1 17 LEU A 27 LEU A 29 PHE A 39 HIS A 43
SITE 2 AC1 17 PRO A 44 VAL A 49 GLU A 52 GLN A 53
SITE 3 AC1 17 ALA A 58 ASN A 61 PHE A 62 VAL A 65
SITE 4 AC1 17 HIS A 67 SER A 68 ALA A 71 LEU A 74
SITE 5 AC1 17 SER A 75
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 - r 19 2 Bytes