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- PDB-1fct: NMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM C... -

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Basic information

Entry
Database: PDB / ID: 1fct
TitleNMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM CHLAMYDOMONAS REINHARDTII PROMOTED BY TRIFLUOROETHANOL IN AQUEOUS SOLUTION
ComponentsFERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE FROM THE GREEN ALGA
KeywordsTRANSIT PEPTIDE
Function / homology
Function and homology information


iron-sulfur cluster binding / chloroplast / 2 iron, 2 sulfur cluster binding / electron transfer activity / metal ion binding
Similarity search - Function
Ferredoxin, chloroplast transit peptide / Ferredoxin chloroplastic transit peptide / Ferredoxin [2Fe-2S], plant / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / 2Fe-2S iron-sulfur cluster binding domain / Beta-grasp domain superfamily / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily
Similarity search - Domain/homology
Ferredoxin, chloroplastic
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
MethodSOLUTION NMR
AuthorsLancelin, J.-M. / Blackledge, M.
Citation
Journal: FEBS Lett. / Year: 1994
Title: NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution.
Authors: Lancelin, J.M. / Bally, I. / Arlaud, G.J. / Blackledge, M. / Gans, P. / Stein, M. / Jacquot, J.P.
#1: Journal: Plant Physiol. / Year: 1993
Title: A Cdna Clone Encoding Chlamydomonas Reinhardtii Preferredoxin
Authors: Stein, M. / Jacquot, J.-P. / Miginiac-Maslow, M.
History
DepositionMar 30, 1994Processing site: BNL
Revision 1.0Jun 22, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE FROM THE GREEN ALGA


Theoretical massNumber of molelcules
Total (without water)3,3481
Polymers3,3481
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: MET 31 - ALA 32 MODEL 4 OMEGA =145.82 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
2: MET 28 - SER 29 MODEL 5 OMEGA =138.81 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: MET 31 - ALA 32 MODEL 7 OMEGA =142.17 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: ARG 12 - VAL 13 MODEL 8 OMEGA =215.92 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
5: ARG 23 - PRO 24 MODEL 8 OMEGA =146.16 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
6: ARG 23 - PRO 24 MODEL 10 OMEGA =147.21 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
7: MET 31 - ALA 32 MODEL 13 OMEGA =142.69 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
8: MET 31 - ALA 32 MODEL 14 OMEGA =137.65 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
9: ALA 15 - LYS 16 MODEL 15 OMEGA =144.36 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
10: LYS 16 - PRO 17 MODEL 15 OMEGA =148.98 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
11: PRO 17 - ALA 18 MODEL 15 OMEGA =139.25 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
12: ALA 18 - VAL 19 MODEL 15 OMEGA =214.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
13: MET 31 - ALA 32 MODEL 15 OMEGA =142.29 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
14: MET 31 - ALA 32 MODEL 20 OMEGA =141.96 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
15: LYS 16 - PRO 17 MODEL 21 OMEGA =144.71 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
16: MET 31 - ALA 32 MODEL 22 OMEGA =139.05 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
17: MET 3 - ALA 4 MODEL 23 OMEGA =225.83 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
18: MET 28 - SER 29 MODEL 24 OMEGA =144.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
19: MET 31 - ALA 32 MODEL 24 OMEGA =142.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
20: MET 31 - ALA 32 MODEL 27 OMEGA =142.57 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)27 / -
Representative

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Components

#1: Protein/peptide FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE FROM THE GREEN ALGA


Mass: 3348.091 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Chlamydomonas reinhardtii (plant) / Gene: CDNA / References: UniProt: P07839

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

SoftwareName: AMBER / Classification: refinement
NMR softwareName: Discover / Version: 2.9 / Developer: BIOSYM, INC. / Classification: refinement
NMR ensembleConformers submitted total number: 27

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