BMRB Entry 17075

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

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Title:
Chemical shift assignments for Bacillus subtilis TatAd protein, the channel-forming component of the Tat protein transport system
Deposition date:
2010-07-23
Original release date:
2010-08-24
Authors:
Hu, Yunfei; Jin, Changwen
Citation:

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).
PubMed: 20726548

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a(+)

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts75
1H chemical shifts493

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pept1

Entities:

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

1   METPHESERASNILEGLYILEPROGLYLEU
2   ILELEUILEPHEVALILEALALEUILEILE
3   PHEGLYPROSERLYSLEUPROGLUILEGLY
4   ARGALAALAGLYARGTHRLEULEUGLUPHE
5   LYSSERALATHRLYSSERLEUVALSERGLY
6   ASPGLULYSGLUGLULYSSERALAGLULEU
7   THRALAVALLYSGLNASPLYSASNALAGLY
8   LEUGLUHISHISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_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

Related Database Links:

PDB
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
AlphaFold O31467

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks