Header list of 2pac.pdb file
Complete list - 10 20 Bytes
HEADER ELECTRON TRANSPORT 05-MAY-93 2PAC
TITLE SOLUTION STRUCTURE OF FE(II) CYTOCHROME C551 FROM PSEUDOMONAS
TITLE 2 AERUGINOSA AS DETERMINED BY TWO-DIMENSIONAL 1H NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C551;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.J.DETLEFSEN,V.THANABAL,V.L.PECORARO,G.WAGNER
REVDAT 3 10-MAR-21 2PAC 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK ATOM
REVDAT 2 24-FEB-09 2PAC 1 VERSN
REVDAT 1 31-OCT-93 2PAC 0
JRNL AUTH D.J.DETLEFSEN,V.THANABAL,V.L.PECORARO,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF FE(II) CYTOCHROME C551 FROM
JRNL TITL 2 PSEUDOMONAS AERUGINOSA AS DETERMINED BY TWO-DIMENSIONAL 1H
JRNL TITL 3 NMR.
JRNL REF BIOCHEMISTRY V. 30 9040 1991
JRNL REFN ISSN 0006-2960
JRNL PMID 1654086
JRNL DOI 10.1021/BI00101A019
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.J.DETLEFSEN,V.THANABAL,V.L.PECORARO,G.WAGNER
REMARK 1 TITL SEQUENTIAL 1H NMR ASSIGNMENTS OF IRON(II) CYTOCHROME C551
REMARK 1 TITL 2 FROM PSEUDOMONAS AERUGINOSA
REMARK 1 REF BIOCHEMISTRY V. 29 9377 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PAC 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_1000178434.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 1 LYS A 10 -91.75 -109.41
REMARK 500 1 CYS A 15 20.29 -163.13
REMARK 500 1 HIS A 16 -69.00 -100.33
REMARK 500 1 ALA A 17 151.73 70.24
REMARK 500 1 ILE A 18 33.80 -99.39
REMARK 500 1 ASP A 19 9.83 174.51
REMARK 500 1 MET A 22 -85.20 -157.55
REMARK 500 1 LYS A 33 -78.80 -124.49
REMARK 500 1 ALA A 35 86.98 37.18
REMARK 500 1 ALA A 40 -105.14 -131.20
REMARK 500 1 GLU A 41 -35.57 84.98
REMARK 500 1 SER A 52 -165.56 -72.77
REMARK 500 1 PRO A 62 109.51 -41.33
REMARK 500 1 ASN A 64 134.91 72.35
REMARK 500 1 ALA A 65 -42.54 -170.27
REMARK 500 1 VAL A 66 -146.73 -141.01
REMARK 500 1 SER A 67 -92.44 -98.84
REMARK 500 1 ASP A 68 34.46 -172.25
REMARK 500 1 ASP A 69 -56.93 -130.77
REMARK 500 1 SER A 80 62.05 -118.56
REMARK 500 2 ASP A 2 62.80 -170.25
REMARK 500 2 CYS A 15 17.71 -157.44
REMARK 500 2 ALA A 17 156.23 179.09
REMARK 500 2 MET A 22 -145.93 -177.56
REMARK 500 2 LYS A 33 -50.86 -122.40
REMARK 500 2 ALA A 35 -157.84 50.00
REMARK 500 2 ALA A 38 -179.84 58.22
REMARK 500 2 ALA A 42 -66.17 -101.59
REMARK 500 2 GLN A 53 106.26 -170.61
REMARK 500 2 VAL A 55 -65.19 -131.39
REMARK 500 2 PRO A 58 -155.89 -68.21
REMARK 500 2 ILE A 59 111.60 73.81
REMARK 500 2 PRO A 62 107.32 -47.33
REMARK 500 2 PRO A 63 99.07 -69.02
REMARK 500 2 ASN A 64 -167.40 -65.26
REMARK 500 2 VAL A 66 -143.22 -121.80
REMARK 500 2 SER A 67 41.20 -163.93
REMARK 500 2 ASP A 68 148.38 70.17
REMARK 500 2 ASP A 69 88.05 69.77
REMARK 500 2 GLU A 70 -37.71 140.37
REMARK 500 2 LEU A 79 -71.44 -50.67
REMARK 500 3 ASN A 9 -74.69 -45.75
REMARK 500 3 LYS A 10 80.37 174.35
REMARK 500 3 CYS A 15 21.55 -165.35
REMARK 500 3 HIS A 16 -74.34 -97.44
REMARK 500 3 ALA A 17 158.11 72.00
REMARK 500 3 MET A 22 -88.94 -130.21
REMARK 500 3 LYS A 33 -61.34 -122.45
REMARK 500 3 GLN A 37 -164.67 81.19
REMARK 500 3 ALA A 38 104.13 78.56
REMARK 500
REMARK 500 THIS ENTRY HAS 179 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 ARG A 47 0.25 SIDE CHAIN
REMARK 500 2 ARG A 47 0.16 SIDE CHAIN
REMARK 500 3 ARG A 47 0.30 SIDE CHAIN
REMARK 500 5 ARG A 47 0.20 SIDE CHAIN
REMARK 500 6 ARG A 47 0.12 SIDE CHAIN
REMARK 500 7 ARG A 47 0.23 SIDE CHAIN
REMARK 500 8 ARG A 47 0.29 SIDE CHAIN
REMARK 500 9 ARG A 47 0.18 SIDE CHAIN
REMARK 500 10 ARG A 47 0.30 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 83 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 HEC A 83 NA 106.3
REMARK 620 3 HEC A 83 NB 89.5 90.9
REMARK 620 4 HEC A 83 NC 76.8 176.7 90.1
REMARK 620 5 HEC A 83 ND 93.0 89.2 177.4 89.7
REMARK 620 6 MET A 61 SD 164.6 89.0 91.9 87.9 85.6
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 83
DBREF 2PAC A 1 82 UNP P00099 CY551_PSEAE 23 104
SEQRES 1 A 82 GLU ASP PRO GLU VAL LEU PHE LYS ASN LYS GLY CYS VAL
SEQRES 2 A 82 ALA CYS HIS ALA ILE ASP THR LYS MET VAL GLY PRO ALA
SEQRES 3 A 82 TYR LYS ASP VAL ALA ALA LYS PHE ALA GLY GLN ALA GLY
SEQRES 4 A 82 ALA GLU ALA GLU LEU ALA GLN ARG ILE LYS ASN GLY SER
SEQRES 5 A 82 GLN GLY VAL TRP GLY PRO ILE PRO MET PRO PRO ASN ALA
SEQRES 6 A 82 VAL SER ASP ASP GLU ALA GLN THR LEU ALA LYS TRP VAL
SEQRES 7 A 82 LEU SER GLN LYS
HET HEC A 83 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 2 PHE A 7 1 6
HELIX 2 2 GLY A 11 CYS A 15 5 5
HELIX 3 3 ALA A 26 ALA A 32 1 7
HELIX 4 4 GLU A 41 GLN A 46 1 6
HELIX 5 5 ASP A 69 SER A 80 1 12
LINK SG CYS A 12 CAB HEC A 83 1555 1555 1.88
LINK SG CYS A 15 CAC HEC A 83 1555 1555 1.90
LINK NE2 HIS A 16 FE HEC A 83 1555 1555 2.03
LINK SD MET A 61 FE HEC A 83 1555 1555 2.45
SITE 1 AC1 18 GLY A 11 CYS A 12 CYS A 15 HIS A 16
SITE 2 AC1 18 VAL A 23 GLY A 24 PRO A 25 TYR A 27
SITE 3 AC1 18 PHE A 34 ILE A 48 SER A 52 VAL A 55
SITE 4 AC1 18 TRP A 56 GLY A 57 ILE A 59 MET A 61
SITE 5 AC1 18 LEU A 74 VAL A 78
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 - 10 20 Bytes