HEADER ELECTRON TRANSPORT 06-FEB-97 2CJN
TITLE STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: 2FE-2S
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 32046;
SOURCE 4 OTHER_DETAILS: CYANOBACTERIUM
KEYWDS FERREDOXIN, ELECTRON TRANSPORT, IRON-SULFUR PROTEIN
EXPDTA SOLUTION NMR
AUTHOR H.HATANAKA,R.TANIMURA,S.KATOH,F.INAGAKI
REVDAT 3 09-MAR-22 2CJN 1 REMARK
REVDAT 2 24-FEB-09 2CJN 1 VERSN
REVDAT 1 15-MAY-97 2CJN 0
SPRSDE 15-MAY-97 2CJN 1CJN
JRNL AUTH H.HATANAKA,R.TANIMURA,S.KATOH,F.INAGAKI
JRNL TITL SOLUTION STRUCTURE OF FERREDOXIN FROM THE THERMOPHILIC
JRNL TITL 2 CYANOBACTERIUM SYNECHOCOCCUS ELONGATUS AND ITS
JRNL TITL 3 THERMOSTABILITY.
JRNL REF J.MOL.BIOL. V. 268 922 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9180381
JRNL DOI 10.1006/JMBI.1997.1001
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CJN 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_1000177924.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : ALPHA-600
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : F(NOE) + F(REPEL)
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NMR DATA WERE COLLECTED IN H2O IN 0.010 M SODIUM PHOSPHATE
REMARK 210 BUFFER PH 7.2 CONTAINING 10 PERCENT D2O AND 0.050 M SODIUM
REMARK 210 CHLORIDE AT 20 DEGREES CELSIUS.
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 THR A 2 100.71 -44.53
REMARK 500 SER A 13 -173.33 177.74
REMARK 500 ASP A 35 71.90 26.26
REMARK 500 PHE A 38 155.13 172.26
REMARK 500 SER A 39 -58.82 -151.10
REMARK 500 LYS A 51 87.73 177.17
REMARK 500 LEU A 52 102.64 -58.15
REMARK 500 SER A 60 37.40 -90.29
REMARK 500 GLN A 62 -172.04 -52.06
REMARK 500 ASP A 68 -71.15 -77.37
REMARK 500 PHE A 74 -172.90 -51.80
REMARK 500 VAL A 75 96.43 167.50
REMARK 500 LEU A 76 108.93 -43.71
REMARK 500 VAL A 79 42.42 -143.76
REMARK 500 SER A 84 162.53 160.95
REMARK 500 LEU A 89 95.67 -59.62
REMARK 500 ASN A 91 105.08 63.50
REMARK 500 GLN A 92 51.01 -152.36
REMARK 500 GLU A 93 45.71 -86.16
REMARK 500 GLU A 94 -36.71 -153.69
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 9 0.12 SIDE CHAIN
REMARK 500 ARG A 41 0.22 SIDE CHAIN
REMARK 500 ARG A 83 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CJO RELATED DB: PDB
DBREF 2CJN A 1 97 UNP P0A3C9 FER_SYNEL 1 97
SEQRES 1 A 97 ALA THR TYR LYS VAL THR LEU VAL ARG PRO ASP GLY SER
SEQRES 2 A 97 GLU THR THR ILE ASP VAL PRO GLU ASP GLU TYR ILE LEU
SEQRES 3 A 97 ASP VAL ALA GLU GLU GLN GLY LEU ASP LEU PRO PHE SER
SEQRES 4 A 97 CYS ARG ALA GLY ALA CYS SER THR CYS ALA GLY LYS LEU
SEQRES 5 A 97 LEU GLU GLY GLU VAL ASP GLN SER ASP GLN SER PHE LEU
SEQRES 6 A 97 ASP ASP ASP GLN ILE GLU LYS GLY PHE VAL LEU THR CYS
SEQRES 7 A 97 VAL ALA TYR PRO ARG SER ASP CYS LYS ILE LEU THR ASN
SEQRES 8 A 97 GLN GLU GLU GLU LEU TYR
HELIX 1 A ILE A 25 GLN A 32 1 8
HELIX 2 B ASP A 67 LYS A 72 1 6
HELIX 3 C GLU A 94 TYR A 97 1 4
SHEET 1 A 4 SER A 13 GLU A 21 0
SHEET 2 A 4 THR A 2 PRO A 10 -1 O LEU A 7 N THR A 15
SHEET 3 A 4 SER A 84 THR A 90 1 O ILE A 88 N VAL A 8
SHEET 4 A 4 LYS A 51 LEU A 53 -1 O LYS A 51 N LEU A 89
SHEET 1 B 2 GLU A 56 GLN A 59 0
SHEET 2 B 2 ALA A 80 ARG A 83 -1 O TYR A 81 N ASP A 58
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
