BMRB Entry 19714

Name: Transport protein A
Published: 2015-04-13

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PDB ID: 2mn6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19714
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Transport protein A PubMed: 25090434

Deposition date: 2014-01-02 Original release date: 2015-04-13

Authors: Zhang, Yi; Hu, Yunfei; Jin, Changwen

Citation: Zhang, Yi; Hu, Yunfei; Li, Hongwei; Jin, Changwen. "Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure" Plos One 9, e103157-e103157 (2014).

Assembly members:
entity, polymer, 100 residues, Formula weight is not available

Natural source: Common Name: E. coli 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):
entity: MCGMGGISIWQLLIIAVIVV LLFGTKKLGSIGSDLGASIK GFKKAMSDDEPKQDKTSQDA DFTAKTIADKQADTNQEQAK TEDAKRHDKEQVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	378
15N chemical shifts	90
1H chemical shifts	628

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Transport protein A	1

Entities:

Entity 1, Transport protein A 100 residues - Formula weight is not available

1	MET	CYS	GLY	MET	GLY	GLY	ILE	SER	ILE	TRP
2	GLN	LEU	LEU	ILE	ILE	ALA	VAL	ILE	VAL	VAL
3	LEU	LEU	PHE	GLY	THR	LYS	LYS	LEU	GLY	SER
4	ILE	GLY	SER	ASP	LEU	GLY	ALA	SER	ILE	LYS
5	GLY	PHE	LYS	LYS	ALA	MET	SER	ASP	ASP	GLU
6	PRO	LYS	GLN	ASP	LYS	THR	SER	GLN	ASP	ALA
7	ASP	PHE	THR	ALA	LYS	THR	ILE	ALA	ASP	LYS
8	GLN	ALA	ASP	THR	ASN	GLN	GLU	GLN	ALA	LYS
9	THR	GLU	ASP	ALA	LYS	ARG	HIS	ASP	LYS	GLU
10	GLN	VAL	LEU	GLU	HIS	HIS	HIS	HIS	HIS	HIS

Samples:

sample_1: transport protein A, [U-100% 15N], 1 mM; sodium phosphate 50 mM; DPC 80 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: transport protein A, [U-100% 15N], 1 mM; sodium phosphate 50 mM; DPC 80 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 700 MHz

BMRB	19881
PDB	2MN6 2MN7
DBJ	BAB38189 BAE77465 BAG79648 BAI27909 BAI33032
EMBL	CAA06724 CAP78301 CAQ34195 CAR00812 CAR05477
GB	AAA67633 AAC19240 AAC76839 AAG59032 AAN45349
PIR	D86071
REF	NP_312793 NP_418280 NP_709642 WP_000508967 WP_001234791
SP	P69428 P69429 P69430 P69431

Biological Magnetic Resonance Data Bank