HEADER ELECTRON TRANSPORT 14-SEP-95 1DOY
TITLE 1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY
TITLE 2 FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN [2FE-2S];
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: PLANT TYPE FERREDOXIN, WITH DISULFIDE BOND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803
KEYWDS IRON-SULFUR PROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 3
AUTHOR C.LELONG,P.SETIF,H.BOTTIN,F.ANDRE,J.M.NEUMANN
REVDAT 4 13-JUL-11 1DOY 1 VERSN
REVDAT 3 24-FEB-09 1DOY 1 VERSN
REVDAT 2 01-APR-03 1DOY 1 JRNL
REVDAT 1 08-MAR-96 1DOY 0
JRNL AUTH C.LELONG,P.SETIF,H.BOTTIN,F.ANDRE,J.M.NEUMANN
JRNL TITL 1H AND 15N NMR SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE,
JRNL TITL 2 AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS
JRNL TITL 3 SP. PCC 6803.
JRNL REF BIOCHEMISTRY V. 34 14462 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7578051
JRNL DOI 10.1021/BI00044A024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.BOTTIN,B.LAGOUTTE
REMARK 1 TITL FERREDOXIN AND FLAVODOXIN FROM THE CYANOBACTERIUM
REMARK 1 TITL 2 SYNECHOCYSTIS SP. PCC 6803
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1101 48 1992
REMARK 1 REFN ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : 3
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 SER A 2 168.51 58.17
REMARK 500 1 TYR A 3 79.61 37.11
REMARK 500 1 THR A 4 -35.64 -165.87
REMARK 500 1 VAL A 5 -131.87 -51.84
REMARK 500 1 ILE A 8 108.18 -173.54
REMARK 500 1 THR A 9 -160.70 -125.86
REMARK 500 1 PRO A 10 -18.99 -48.60
REMARK 500 1 ASP A 11 69.64 -111.34
REMARK 500 1 CYS A 18 56.14 22.10
REMARK 500 1 SER A 19 39.31 -89.22
REMARK 500 1 ASP A 20 37.73 -165.03
REMARK 500 1 ASP A 21 164.27 71.13
REMARK 500 1 THR A 22 -123.66 103.24
REMARK 500 1 TYR A 23 -47.18 81.69
REMARK 500 1 ILE A 24 161.89 -14.53
REMARK 500 1 ALA A 28 -73.74 -96.22
REMARK 500 1 GLU A 29 -14.35 -45.93
REMARK 500 1 ASP A 34 109.89 22.92
REMARK 500 1 SER A 38 -45.62 -164.40
REMARK 500 1 CYS A 39 -30.07 -35.15
REMARK 500 1 ARG A 40 163.33 69.60
REMARK 500 1 ALA A 48 47.21 -98.66
REMARK 500 1 ILE A 51 57.13 74.17
REMARK 500 1 ALA A 53 29.73 33.66
REMARK 500 1 GLN A 58 -56.79 81.83
REMARK 500 1 SER A 59 48.06 -85.19
REMARK 500 1 GLN A 61 -148.64 42.18
REMARK 500 1 ASP A 65 -74.78 -165.71
REMARK 500 1 ASP A 66 19.68 -144.78
REMARK 500 1 ASP A 67 -44.80 82.47
REMARK 500 1 GLN A 68 -38.25 -160.13
REMARK 500 1 ILE A 69 26.69 172.33
REMARK 500 1 GLU A 70 73.59 175.36
REMARK 500 1 ALA A 71 76.92 -171.63
REMARK 500 1 LEU A 75 93.03 -65.64
REMARK 500 1 CYS A 77 7.85 -65.79
REMARK 500 1 TYR A 80 -93.76 -136.66
REMARK 500 1 ASP A 84 144.11 81.08
REMARK 500 1 LYS A 91 92.27 178.34
REMARK 500 1 ASP A 94 -44.92 -147.36
REMARK 500 1 LEU A 95 50.98 75.57
REMARK 500 2 SER A 2 -102.06 -86.37
REMARK 500 2 TYR A 3 -94.06 -84.21
REMARK 500 2 VAL A 5 131.99 -4.27
REMARK 500 2 LEU A 7 -103.86 143.88
REMARK 500 2 ILE A 8 -99.81 55.34
REMARK 500 2 THR A 9 -73.63 117.71
REMARK 500 2 ASP A 11 78.56 -114.37
REMARK 500 2 SER A 15 81.74 -150.73
REMARK 500 2 ILE A 16 -85.32 -140.89
REMARK 500
REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1 FES A 97
REMARK 610 2 FES A 97
REMARK 610 3 FES A 97
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 1 FES A 97 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 CYS A 44 SG 83.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 FES A 97 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 47 SG
REMARK 620 2 CYS A 77 SG 122.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 97
DBREF 1DOY A 1 96 UNP P27320 FER_SYNY3 1 96
SEQRES 1 A 96 ALA SER TYR THR VAL LYS LEU ILE THR PRO ASP GLY GLU
SEQRES 2 A 96 SER SER ILE GLU CYS SER ASP ASP THR TYR ILE LEU ASP
SEQRES 3 A 96 ALA ALA GLU GLU ALA GLY LEU ASP LEU PRO TYR SER CYS
SEQRES 4 A 96 ARG ALA GLY ALA CYS SER THR CYS ALA GLY LYS ILE THR
SEQRES 5 A 96 ALA GLY SER VAL ASP GLN SER ASP GLN SER PHE LEU ASP
SEQRES 6 A 96 ASP ASP GLN ILE GLU ALA GLY TYR VAL LEU THR CYS VAL
SEQRES 7 A 96 ALA TYR PRO THR SER ASP CYS THR ILE GLU THR HIS LYS
SEQRES 8 A 96 GLU GLU ASP LEU TYR
HET FES A 97 2
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 ASP A 26 ASP A 34 1 9
HELIX 2 2 ASP A 66 GLU A 70 1 5
HELIX 3 3 GLU A 93 TYR A 96 1 4
SHEET 1 A 2 LYS A 6 ILE A 8 0
SHEET 2 A 2 GLU A 13 SER A 15 -1 N SER A 14 O LEU A 7
SSBOND 1 CYS A 18 CYS A 85 1555 1555 2.02
LINK SG CYS A 39 FE1 FES A 97 1555 1555 2.28
LINK SG CYS A 44 FE1 FES A 97 1555 1555 2.28
LINK SG CYS A 47 FE2 FES A 97 1555 1555 2.35
LINK SG CYS A 77 FE2 FES A 97 1555 1555 2.26
SITE 1 S2 4 CYS A 39 CYS A 44 CYS A 47 CYS A 77
SITE 1 AC1 6 CYS A 39 ARG A 40 CYS A 44 CYS A 47
SITE 2 AC1 6 LEU A 75 CYS A 77
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
(ATOM LINES ARE NOT SHOWN.)
END
