Header list of 1a8c.pdb file
Complete list - 16 20 Bytes
HEADER HEMOPROTEIN 23-MAR-98 1A8C
TITLE PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552
TITLE 2 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT
TITLE 3 HYDROGEN BOND CONSTRAINTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERROCYTOCHROME C-552;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C-551
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NITROSOMONAS EUROPAEA;
SOURCE 3 ORGANISM_TAXID: 915
KEYWDS HEMOPROTEIN, CYTOCHROME, PROKARYOTIC ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR R.TIMKOVICH,D.BERGMANN,D.M.ARCIERO,A.B.HOOPER
REVDAT 4 16-FEB-22 1A8C 1 REMARK LINK
REVDAT 3 24-FEB-09 1A8C 1 VERSN
REVDAT 2 18-NOV-98 1A8C 1 HET COMPND REMARK TITLE
REVDAT 2 2 1 JRNL EXPDTA
REVDAT 1 21-OCT-98 1A8C 0
JRNL AUTH R.TIMKOVICH,D.BERGMANN,D.M.ARCIERO,A.B.HOOPER
JRNL TITL PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF
JRNL TITL 2 FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA.
JRNL REF BIOPHYS.J. V. 75 1964 1998
JRNL REFN ISSN 0006-3495
JRNL PMID 9746537
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE JOURNAL CITATION
REMARK 4
REMARK 4 1A8C 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_1000170519.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, X-PLOR
REMARK 210 METHOD USED : RESTRAINED DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMUM ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 ALA A 2 111.01 76.75
REMARK 500 ASP A 3 -49.13 -169.32
REMARK 500 ASN A 8 -87.93 -100.56
REMARK 500 ASN A 9 -22.76 -160.43
REMARK 500 CYS A 13 24.53 -144.74
REMARK 500 GLN A 15 -162.98 -79.87
REMARK 500 VAL A 20 -62.96 -125.21
REMARK 500 ASP A 27 -62.92 -98.46
REMARK 500 ALA A 33 36.10 -90.05
REMARK 500 LYS A 35 -96.25 -96.77
REMARK 500 ASP A 36 -137.60 -90.10
REMARK 500 ASP A 37 40.15 -92.41
REMARK 500 SER A 51 -56.43 -129.39
REMARK 500 GLN A 56 -158.98 -79.97
REMARK 500 VAL A 63 -74.22 -71.42
REMARK 500 ASN A 64 -57.60 -149.84
REMARK 500 VAL A 65 -85.15 -158.71
REMARK 500 SER A 66 -109.91 -138.91
REMARK 500 ASP A 67 -79.78 -90.07
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 82 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 14 NE2
REMARK 620 2 HEC A 82 NA 90.6
REMARK 620 3 HEC A 82 NB 90.0 90.0
REMARK 620 4 HEC A 82 NC 89.2 179.8 89.9
REMARK 620 5 HEC A 82 ND 89.6 90.0 179.6 90.1
REMARK 620 6 MET A 59 SD 179.8 89.4 89.8 90.8 90.6
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 82
DBREF 1A8C A 1 81 UNP P95339 C552_NITEU 23 103
SEQRES 1 A 81 ASP ALA ASP LEU ALA LYS LYS ASN ASN CYS ILE ALA CYS
SEQRES 2 A 81 HIS GLN VAL GLU THR LYS VAL VAL GLY PRO ALA LEU LYS
SEQRES 3 A 81 ASP ILE ALA ALA LYS TYR ALA ASP LYS ASP ASP ALA ALA
SEQRES 4 A 81 THR TYR LEU ALA GLY LYS ILE LYS GLY GLY SER SER GLY
SEQRES 5 A 81 VAL TRP GLY GLN ILE PRO MET PRO PRO ASN VAL ASN VAL
SEQRES 6 A 81 SER ASP ALA ASP ALA LYS ALA LEU ALA ASP TRP ILE LEU
SEQRES 7 A 81 THR LEU LYS
HET HEC A 82 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 LEU A 4 LYS A 7 1 4
HELIX 2 2 CYS A 10 CYS A 13 5 4
HELIX 3 3 LEU A 25 LYS A 31 1 7
HELIX 4 4 ALA A 38 GLY A 48 1 11
HELIX 5 5 ALA A 68 LEU A 78 1 11
LINK SG CYS A 10 CAB HEC A 82 1555 1555 1.82
LINK SG CYS A 13 CAC HEC A 82 1555 1555 1.81
LINK NE2 HIS A 14 FE HEC A 82 1555 1555 1.95
LINK SD MET A 59 FE HEC A 82 1555 1555 2.38
SITE 1 AC1 19 ASN A 9 CYS A 10 ALA A 12 CYS A 13
SITE 2 AC1 19 HIS A 14 VAL A 21 GLY A 22 PRO A 23
SITE 3 AC1 19 ILE A 46 SER A 50 VAL A 53 TRP A 54
SITE 4 AC1 19 GLY A 55 GLN A 56 ILE A 57 MET A 59
SITE 5 AC1 19 ASN A 62 VAL A 63 ASN A 64
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
Complete list - 16 20 Bytes