BMRB Entry 18668

Name: Solution Structure of Escherichia coli Ferrous Iron transport protein A (FeoA)
Published: 2012-11-12

Click here to enlarge.

PDB ID: 2lx9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18668
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution Structure of Escherichia coli Ferrous Iron transport protein A (FeoA)

Deposition date:

2012-08-16

Original release date:

2012-11-12

Authors:

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

Citation:

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).
PubMed: 23104801

Assembly members:

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

Natural source:

Natural source: Common Name: enterobacteria 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: pET30a

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	223
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

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

SER

LEU

GLY

4

MET

LEU

PRO

GLY

SER

PHE

ASN

VAL

5

ARG

VAL

ALA

PRO

LEU

GLY

ASP

PRO

ILE

HIS

6

ILE

GLU

THR

ARG

VAL

SER

LEU

VAL

LEU

7

ARG

LYS

ASP

LEU

ALA

LEU

GLU

VAL

8

GLU

ALA

VAL

SER

LEU

GLU

HIS

9

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

PDB	2LX9
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
AlphaFold	P0AEL3 P0AEL4 P0AEL5