BMRB Entry 18668
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18668
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 69 |
| 1H chemical shifts | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FeoA | 1 |
Entities:
Entity 1, FeoA 83 residues - 9436.995 Da.
Residues 76-83 represents vector artefact and His-tag
| 1 | MET | GLN | TYR | THR | PRO | ASP | THR | ALA | TRP | LYS | ||||
| 2 | ILE | THR | GLY | PHE | SER | ARG | GLU | ILE | SER | PRO | ||||
| 3 | ALA | TYR | ARG | GLN | LYS | LEU | LEU | SER | LEU | GLY | ||||
| 4 | MET | LEU | PRO | GLY | SER | SER | PHE | ASN | VAL | VAL | ||||
| 5 | ARG | VAL | ALA | PRO | LEU | GLY | ASP | PRO | ILE | HIS | ||||
| 6 | ILE | GLU | THR | ARG | ARG | VAL | SER | LEU | VAL | LEU | ||||
| 7 | ARG | LYS | LYS | ASP | LEU | ALA | LEU | LEU | GLU | VAL | ||||
| 8 | GLU | ALA | VAL | SER | SER | LEU | GLU | HIS | HIS | HIS | ||||
| 9 | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_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:
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