BMRB Entry 34341

Title:
Structural investigation of the TasA anchoring protein TapA from Bacillus subtilis
Deposition date:
2018-12-20
Original release date:
2020-01-24
Authors:
Higman, V.; Schmieder, P.; Diehl, A.; Oschkinat, H.
Citation:

Citation: Roske, Yvette; Lindemann, Florian; Diehl, Anne; Cremer, Nils; Higman, Victoria; Schlegel, Brigitte; Leidert, Martina; Driller, Kristina; Turgay, Kursad; Schmieder, Peter; Heinemann, Udo; Oschkinat, Hartmut. "TapA acts as specific chaperone in TasA filament formation by strand complementation"  Proc. Natl. Acad. Sci. U.S.A. 120, e2217070120-e2217070120 (2023).
PubMed: 37068239

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 17010.301 Da.

Natural source:

Natural source:   Common Name: Bacillus 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 BL21(DE3)

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts114
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 147 residues - 17010.301 Da.

1   ALAPHEHISASPILEGLUTHRPHEASPVAL
2   SERLEUGLNTHRCYSLYSASPPHEGLNHIS
3   THRASPLYSASNCYSHISTYRASPLYSARG
4   TRPASPGLNSERASPLEUHISILESERASP
5   GLNTHRASPTHRLYSGLYTHRVALCYSSER
6   PROPHEALALEUPHEALAVALLEUGLUASN
7   THRGLYGLULYSLEULYSLYSSERLYSTRP
8   LYSTRPGLULEUHISLYSLEUGLUASNALA
9   ARGLYSPROLEULYSASPGLYASNVALILE
10   GLULYSGLYPHEVALSERASNGLNILEGLY
11   ASPSERLEUTYRLYSILEGLUTHRLYSLYS
12   LYSMETLYSPROGLYILETYRALAPHELYS
13   VALTYRLYSPROALAGLYTYRPROALAASN
14   GLYSERTHRPHEGLUTRPSERGLUPROMET
15   ARGLEUALALYSCYSASPGLU

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