BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18668

Title: Solution Structure of Escherichia coli Ferrous Iron transport protein A (FeoA)   PubMed: 23104801

Deposition date: 2012-08-16 Original release date: 2012-11-12

Authors: Lau, Cheryl; Ishida, Hiroaki; Liu, Zhihong; Vogel, Hans

Citation: Lau, Cheryl; Ishida, Hiroaki; Liu, Zhihong; Vogel, Hans. "Solution structure of Escherichia coli FeoA and its potential role in bacterial ferrous iron transport."  J. Bacteriol. 195, 46-55 (2013).

Assembly members:
FeoA, polymer, 83 residues, 9436.995 Da.

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

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

Entity Sequences (FASTA):
FeoA: MQYTPDTAWKITGFSREISP AYRQKLLSLGMLPGSSFNVV RVAPLGDPIHIETRRVSLVL RKKDLALLEVEAVSSLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts223
15N chemical shifts69
1H chemical shifts69

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FeoA1

Entities:

Entity 1, FeoA 83 residues - 9436.995 Da.

Residues 76-83 represents vector artefact and His-tag

1   METGLNTYRTHRPROASPTHRALATRPLYS
2   ILETHRGLYPHESERARGGLUILESERPRO
3   ALATYRARGGLNLYSLEULEUSERLEUGLY
4   METLEUPROGLYSERSERPHEASNVALVAL
5   ARGVALALAPROLEUGLYASPPROILEHIS
6   ILEGLUTHRARGARGVALSERLEUVALLEU
7   ARGLYSLYSASPLEUALALEULEUGLUVAL
8   GLUALAVALSERSERLEUGLUHISHISHIS
9   HISHISHIS

Samples:

sample_1: HEPES 20 mM; DSS 1 mM; D2O, [U-100% 2H], 10%; sodium chloride 100 mM; FeoA, [U-95% 13C; U-95% 15N], 0.8 mM; H2O 90%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAB37673 BAE77883 BAG79198 BAI27666 BAI32836
EMBL CAA50386 CAQ33729 CAR00351 CAR05009 CAR10059
GB AAA58206 AAC76433 AAG58509 AAN44888 AAN82623
REF NP_312277 NP_417867 NP_709181 WP_001200452 WP_001200453
SP P0AEL3 P0AEL4 P0AEL5

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts