Header list of 2giw.pdb file
Complete list - r 9 2 Bytes
HEADER ELECTRON TRANSPORT 25-JUN-98 2GIW
TITLE SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C, NMR, 40
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: REDUCED
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, CYTOCHROME C
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR L.BANCI,I.BERTINI,J.G.HUBER,G.A.SPYROULIAS,P.TURANO
REVDAT 4 09-MAR-22 2GIW 1 REMARK LINK
REVDAT 3 24-FEB-09 2GIW 1 VERSN
REVDAT 2 27-JAN-99 2GIW 3 ATOM REMARK JRNL
REVDAT 1 09-DEC-98 2GIW 0
JRNL AUTH L.BANCI,I.BERTINI,J.G.HUBER,G.A.SPYROULIAS,P.TURANO
JRNL TITL SOLUTION STRUCTURE OF REDUCED HORSE HEART CYTOCHROME C.
JRNL REF J.BIOL.INORG.CHEM. V. 4 21 1999
JRNL REFN ISSN 0949-8257
JRNL PMID 10499099
JRNL DOI 10.1007/S007750050285
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BANCI,I.BERTINI,H.B.GRAY,C.LUCHINAT,T.REDDIG,A.ROSATO,
REMARK 1 AUTH 2 P.TURANO
REMARK 1 TITL SOLUTION STRUCTURE OF OXIDIZED HORSE HEART CYTOCHROME C
REMARK 1 REF BIOCHEMISTRY V. 36 9867 1997
REMARK 1 REFN ISSN 0006-2960
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 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2GIW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178137.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE
REMARK 210 PRESSURE : 1013 MBAR
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE 800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, AMBER
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS, RESTRAINED
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING NOES OF 1H NMR.
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 1 LYS A 13 -0.22 -140.17
REMARK 500 1 GLU A 21 30.64 -151.69
REMARK 500 1 LYS A 22 -179.84 179.18
REMARK 500 1 LYS A 27 -80.33 -77.33
REMARK 500 1 LEU A 35 -80.67 69.58
REMARK 500 1 GLN A 42 78.89 -166.80
REMARK 500 1 THR A 47 35.80 -98.61
REMARK 500 1 TYR A 48 -162.57 63.91
REMARK 500 1 GLU A 61 43.76 -75.48
REMARK 500 1 GLU A 62 -60.31 -137.68
REMARK 500 1 PHE A 82 75.06 -161.98
REMARK 500 1 LYS A 86 -64.02 -170.90
REMARK 500 1 LYS A 87 -57.65 -167.89
REMARK 500 1 LYS A 88 -50.27 -171.24
REMARK 500 2 LYS A 13 31.38 -146.81
REMARK 500 2 CYS A 14 -47.60 -138.40
REMARK 500 2 VAL A 20 109.47 -51.34
REMARK 500 2 GLU A 21 41.63 -163.62
REMARK 500 2 LYS A 22 56.84 34.99
REMARK 500 2 HIS A 26 -91.46 -119.44
REMARK 500 2 LYS A 27 -61.77 75.93
REMARK 500 2 PHE A 36 98.08 -69.32
REMARK 500 2 LYS A 39 106.50 -39.77
REMARK 500 2 GLN A 42 78.76 -175.77
REMARK 500 2 TYR A 48 -167.31 53.34
REMARK 500 2 ILE A 57 -158.83 -98.99
REMARK 500 2 TRP A 59 102.38 50.13
REMARK 500 2 GLU A 61 35.14 -71.67
REMARK 500 2 GLU A 62 -56.77 -137.91
REMARK 500 2 ASN A 70 74.37 -154.94
REMARK 500 2 ALA A 83 -69.16 -123.21
REMARK 500 2 ILE A 85 -83.63 -122.64
REMARK 500 2 LYS A 86 74.05 -170.00
REMARK 500 2 LYS A 87 -75.19 64.91
REMARK 500 2 LYS A 88 -35.81 -157.44
REMARK 500 3 ASP A 2 -45.76 -139.54
REMARK 500 3 VAL A 3 -36.44 100.67
REMARK 500 3 VAL A 20 108.24 -46.07
REMARK 500 3 GLU A 21 35.80 -157.42
REMARK 500 3 LYS A 22 56.36 31.36
REMARK 500 3 HIS A 26 -88.83 -86.23
REMARK 500 3 LYS A 27 75.19 65.47
REMARK 500 3 LEU A 35 -81.76 60.06
REMARK 500 3 PHE A 36 99.61 -48.85
REMARK 500 3 GLN A 42 102.45 -173.74
REMARK 500 3 THR A 47 36.92 -84.59
REMARK 500 3 TYR A 48 -177.06 52.63
REMARK 500 3 TRP A 59 60.41 31.67
REMARK 500 3 GLU A 61 39.20 -71.96
REMARK 500 3 GLU A 62 -57.69 -140.36
REMARK 500
REMARK 500 THIS ENTRY HAS 777 RAMACHANDRAN OUTLIERS.
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 1 HIS A 18 0.07 SIDE CHAIN
REMARK 500 1 PHE A 36 0.08 SIDE CHAIN
REMARK 500 1 TYR A 48 0.12 SIDE CHAIN
REMARK 500 1 TYR A 74 0.10 SIDE CHAIN
REMARK 500 2 PHE A 10 0.09 SIDE CHAIN
REMARK 500 2 ARG A 38 0.08 SIDE CHAIN
REMARK 500 2 TYR A 74 0.10 SIDE CHAIN
REMARK 500 2 TYR A 97 0.12 SIDE CHAIN
REMARK 500 3 PHE A 10 0.11 SIDE CHAIN
REMARK 500 3 TYR A 48 0.08 SIDE CHAIN
REMARK 500 4 TYR A 48 0.12 SIDE CHAIN
REMARK 500 4 TYR A 67 0.09 SIDE CHAIN
REMARK 500 4 TYR A 74 0.13 SIDE CHAIN
REMARK 500 5 HIS A 18 0.08 SIDE CHAIN
REMARK 500 5 TYR A 48 0.10 SIDE CHAIN
REMARK 500 5 TYR A 67 0.07 SIDE CHAIN
REMARK 500 6 PHE A 10 0.08 SIDE CHAIN
REMARK 500 6 HIS A 18 0.08 SIDE CHAIN
REMARK 500 6 TYR A 48 0.14 SIDE CHAIN
REMARK 500 6 TYR A 74 0.12 SIDE CHAIN
REMARK 500 7 TYR A 48 0.11 SIDE CHAIN
REMARK 500 7 TYR A 67 0.08 SIDE CHAIN
REMARK 500 7 TYR A 74 0.10 SIDE CHAIN
REMARK 500 8 PHE A 10 0.08 SIDE CHAIN
REMARK 500 8 TYR A 74 0.10 SIDE CHAIN
REMARK 500 9 TYR A 74 0.24 SIDE CHAIN
REMARK 500 10 PHE A 10 0.08 SIDE CHAIN
REMARK 500 11 PHE A 10 0.09 SIDE CHAIN
REMARK 500 11 HIS A 18 0.08 SIDE CHAIN
REMARK 500 11 TYR A 48 0.07 SIDE CHAIN
REMARK 500 11 TYR A 74 0.11 SIDE CHAIN
REMARK 500 11 ARG A 91 0.09 SIDE CHAIN
REMARK 500 11 TYR A 97 0.07 SIDE CHAIN
REMARK 500 12 PHE A 10 0.10 SIDE CHAIN
REMARK 500 12 HIS A 18 0.07 SIDE CHAIN
REMARK 500 12 TYR A 67 0.10 SIDE CHAIN
REMARK 500 13 TYR A 48 0.11 SIDE CHAIN
REMARK 500 13 TYR A 74 0.11 SIDE CHAIN
REMARK 500 13 PHE A 82 0.09 SIDE CHAIN
REMARK 500 14 PHE A 10 0.08 SIDE CHAIN
REMARK 500 14 TYR A 48 0.09 SIDE CHAIN
REMARK 500 14 TYR A 67 0.07 SIDE CHAIN
REMARK 500 15 PHE A 36 0.07 SIDE CHAIN
REMARK 500 15 ARG A 91 0.16 SIDE CHAIN
REMARK 500 16 PHE A 10 0.07 SIDE CHAIN
REMARK 500 16 TYR A 48 0.07 SIDE CHAIN
REMARK 500 16 TYR A 67 0.09 SIDE CHAIN
REMARK 500 16 TYR A 74 0.07 SIDE CHAIN
REMARK 500 17 HIS A 18 0.08 SIDE CHAIN
REMARK 500 17 TYR A 48 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 118 PLANE DEVIATIONS.
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 92.7
REMARK 620 3 HEC A 105 NB 88.6 92.9
REMARK 620 4 HEC A 105 NC 88.9 176.0 90.9
REMARK 620 5 HEC A 105 ND 90.9 87.9 179.0 88.3
REMARK 620 6 MET A 80 SD 171.1 84.8 100.1 93.0 80.5
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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GIW RELATED DB: PDB
DBREF 2GIW 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 GLU A 4 LYS A 13 1 10
HELIX 2 2 ASP A 50 LYS A 53 1 4
HELIX 3 3 THR A 63 GLU A 69 1 7
HELIX 4 4 PRO A 71 TYR A 74 1 4
HELIX 5 5 THR A 89 ALA A 101 1 13
LINK SG CYS A 14 CAB HEC A 105 1555 1555 1.81
LINK SG CYS A 17 CAC HEC A 105 1555 1555 1.82
LINK NE2 HIS A 18 FE HEC A 105 1555 1555 1.93
LINK SD MET A 80 FE HEC A 105 1555 1555 2.35
SITE 1 AC1 17 PHE A 10 LYS A 13 CYS A 14 CYS A 17
SITE 2 AC1 17 HIS A 18 THR A 28 PRO A 30 LEU A 35
SITE 3 AC1 17 THR A 40 TYR A 48 ASN A 52 TRP A 59
SITE 4 AC1 17 TYR A 67 LEU A 68 LYS A 79 MET A 80
SITE 5 AC1 17 PHE A 82
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 9 2 Bytes