BMRB Entry 19800

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19800
MolProbity Validation Chart

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Title:
Structure of the PrgK first periplasmic domain
Deposition date:
2014-02-14
Original release date:
2014-10-27
Authors:
Bergeron, Julien; McIntosh, Lawrence; Strynadka, Natalie
Citation:

Citation: Bergeron, Julien; Worrall, Liam; De, Soumya; Sgourakis, Nikolaos; Cheung, Adrienne; Lameignere, Emilie; Okon, Mark; Baker, David; McIntosh, Lawrence; Strynadka, Natalie. "The structure of PrgK reveals structural rearrangements upon assembly of the type III secretion system basal body."  Structure ., .-..

Assembly members:

Assembly members:
entity, polymer, 58 residues, 6532.430 Da.

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 90371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: KDKDLLKGLDQEQANEVIAV LQMHNIEANKIDSGKLGYSI TVAEPDFTAAVYWIKTYQ

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts57
1H chemical shifts400

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PrgK first periplasmic domain1

Entities:

Entity 1, PrgK first periplasmic domain 58 residues - 6532.430 Da.

1   LYSASPLYSASPLEULEULYSGLYLEUASP
2   GLNGLUGLNALAASNGLUVALILEALAVAL
3   LEUGLNMETHISASNILEGLUALAASNLYS
4   ILEASPSERGLYLYSLEUGLYTYRSERILE
5   THRVALALAGLUPROASPPHETHRALAALA
6   VALTYRTRPILELYSTHRTYRGLN

Samples:

sample_1: PrgK, [U-100% 13C; U-100% 15N], 1 mM; D2O 10%; H2O 90%; HEPES 25 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAJ37863 BAP08776
EMBL CAD05978 CAR34291 CAR38583 CAR60779 CBG25840
GB AAB60191 AAL21751 AAO70334 AAV78586 AAX66709
PIR AC0849
REF NP_457265 NP_461792 WP_000001630 WP_000621236 WP_000621237
SP P41786
AlphaFold P41786

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