BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27424

Title: Chemical shifts of PrgK (19-92)   PubMed: 30095200

Deposition date: 2018-03-12 Original release date: 2018-08-15

Authors: Bergeron, Julien; McIntosh, Lawrence; Brockerman, Jacob

Citation: Bergeron, Julien; Brockerman, Jacob; Vuckovic, Marija; Deng, Wanyin; Okon, Mark; McIntosh, Lawrence; Finlay, Brett; Strynadka, Natalie. "Characterization of the two conformations adopted by the T3SS inner-membrane protein PrgK"  Protein Sci. 27, 1680-1691 (2018).

Assembly members:
PrgK, polymer, 74 residues, Formula weight is not available

Natural source:   Common Name: Salmonella enterica   Taxonomy ID: 28901   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

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

Entity Sequences (FASTA):
PrgK: KDKDLLKGLDQEQANEVIAV LQMHNIEANKIDSGKLGYSI TVAEPDFTAAVYWIKTYQLP PRPRVEIAQMFPAD

Data sets:
Data typeCount
13C chemical shifts454
15N chemical shifts137
1H chemical shifts183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PrgK, conformer a1
2PrgK, conformer b1

Entities:

Entity 1, PrgK, conformer a 74 residues - Formula weight is not available

1   LYSASPLYSASPLEULEULYSGLYLEUASP
2   GLNGLUGLNALAASNGLUVALILEALAVAL
3   LEUGLNMETHISASNILEGLUALAASNLYS
4   ILEASPSERGLYLYSLEUGLYTYRSERILE
5   THRVALALAGLUPROASPPHETHRALAALA
6   VALTYRTRPILELYSTHRTYRGLNLEUPRO
7   PROARGPROARGVALGLUILEALAGLNMET
8   PHEPROALAASP

Samples:

PrgK19-92: PrgK, [U-100% 13C; U-100% 15N], 1 mM; HEPES 50 mM; NaCl 50 mM

sample_conditions_PrgK19-92: ionic strength: 0.2 M; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCPrgK19-92isotropicsample_conditions_PrgK19-92
3D HNCACBPrgK19-92isotropicsample_conditions_PrgK19-92
3D CBCA(CO)NHPrgK19-92isotropicsample_conditions_PrgK19-92
3D HNCOPrgK19-92isotropicsample_conditions_PrgK19-92
3D HCACOPrgK19-92isotropicsample_conditions_PrgK19-92
3D HCCH-TOCSYPrgK19-92isotropicsample_conditions_PrgK19-92

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts