BMRB Entry 17075

Name: Chemical shift assignments for Bacillus subtilis TatAd protein, the channel-forming component of the Tat protein transport system
Published: 2010-08-24

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17075

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

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Title: Chemical shift assignments for Bacillus subtilis TatAd protein, the channel-forming component of the Tat protein transport system PubMed: 20726548

Deposition date: 2010-07-23 Original release date: 2010-08-24

Authors: Hu, Yunfei; Jin, Changwen

Citation: Hu, Yunfei; Zhao, Enwei; Li, Hongwei; Xia, Bin; Jin, Changwen. "Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis." J. Am. Chem. Soc. 132, 15942-15944 (2010).

Assembly members:
TatAd, polymer, 78 residues, Formula weight is not available

Natural source: Common Name: B. subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

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

Entity Sequences (FASTA):
TatAd: MFSNIGIPGLILIFVIALII FGPSKLPEIGRAAGRTLLEF KSATKSLVSGDEKEEKSAEL TAVKQDKNAGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	324
15N chemical shifts	75
1H chemical shifts	493

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pept	1

Entities:

Entity 1, pept 78 residues - Formula weight is not available

1

MET

PHE

SER

ASN

ILE

GLY

ILE

PRO

GLY

LEU

2

ILE

LEU

ILE

PHE

VAL

ILE

ALA

LEU

ILE

3

PHE

GLY

PRO

SER

LYS

LEU

PRO

GLU

ILE

GLY

4

ARG

ALA

GLY

ARG

THR

LEU

GLU

PHE

5

LYS

SER

ALA

THR

LYS

SER

LEU

VAL

SER

GLY

6

ASP

GLU

LYS

GLU

LYS

SER

ALA

GLU

LEU

7

THR

ALA

VAL

LYS

GLN

ASP

LYS

ASN

ALA

GLY

8

LEU

GLU

HIS

Samples:

sample_1: TatAd, [U-15N], 1 mM; H2O 90%; D2O 10%; DSS 0.01%; sodium phosphate 50 mM; DPC 5%; sodium azide 0.01%

sample_2: TatAd, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; DSS 0.01%; sodium phosphate 50 mM; DPC, [U-2H], 5%; sodium azide 0.01%

sample_conditions_1: ionic strength: 0.300 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	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 HN(CA)CO	sample_2	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz

PDB	2L16
DBJ	BAI83717 BAM49193 BAM56463 GAK80268
EMBL	CAB12057 CCU56717 CEI55381 CEJ75806 CJN29131
GB	ADM36327 ADV95193 AEP85179 AEP89324 AFI26807
REF	NP_388145 WP_003223835 WP_010332899
SP	O31467

Biological Magnetic Resonance Data Bank