BMRB Entry 18992

Title:
Backbone resonance assignment of [2Fe-2S]-ferredoxin in its reduced state
Deposition date:
2013-01-30
Original release date:
2014-02-14
Authors:
Kim, Jin Hae; Markley, John
Citation:

Citation: Kim, Jin Hae; Frederick, Ronnie; Reinen, Nichole; Troupis, Andrew; Markley, John. "[2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin."  J. Am. Chem. Soc. 135, 8117-8120 (2013).
PubMed: 23682711

Assembly members:

Assembly members:
ferredoxin, polymer, 111 residues, Formula weight is not available
entity_FES, non-polymer, 175.820 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST42

Data sets:
Data typeCount
13C chemical shifts174
15N chemical shifts79
1H chemical shifts79

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ferredoxin1
22Fe-2S cluster2

Entities:

Entity 1, ferredoxin 111 residues - Formula weight is not available

1   METPROLYSILEVALILELEUPROHISGLN
2   ASPLEUCYSPROASPGLYALAVALLEUGLU
3   ALAASNSERGLYGLUTHRILELEUASPALA
4   ALALEUARGASNGLYILEGLUILEGLUHIS
5   ALACYSGLULYSSERCYSALACYSTHRTHR
6   CYSHISCYSILEVALARGGLUGLYPHEASP
7   SERLEUPROGLUSERSERGLUGLNGLUASP
8   ASPMETLEUASPLYSALATRPGLYLEUGLU
9   PROGLUSERARGLEUSERCYSGLNALAARG
10   VALTHRASPGLUASPLEUVALVALGLUILE
11   PROARGTYRTHRILEASNHISALAARGGLU
12   HIS

Entity 2, 2Fe-2S cluster - Fe2 S2 - 175.820 Da.

1   FES

Samples:

sample_1: ferredoxin, [U-13C; U-15N], 1 mM; 2Fe-2S cluster 1 mM; TRIS 20 mM; EDTA 0.5 mM; sodium chloride 150 mM; DTT 5 mM; sodium azide 0.02%; DSS 0.7 mM; sodium dithionite 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 18991 19273
PDB
DBJ BAA16415 BAB36814 BAG78335 BAI26770 BAI31799
EMBL CAP76977 CAQ32898 CAQ88191 CAQ99416 CAR03967
GB AAA23755 AAC75578 AAG57639 AAN44071 AAN81500
REF NP_311418 NP_417020 NP_708364 WP_001124467 WP_001124468
SP P0A9R4 P0A9R5 P0A9R6
AlphaFold P0A9R4 P0A9R6 P0A9R5

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks