BMRB Entry 27979

Title:
Chemical shifts of Bordetella pertussis effector BteA
Deposition date:
2019-07-18
Original release date:
2019-07-30
Authors:
Yahalom, Adi; Shaked, Hadassa; Chill, Jordan
Citation:

Citation: Yahalom, Adi; Davidov, Geula; Kolusheva, Sofiya; Shaked, Hadassa; Barber-Zucker, Shiran; Zarivach, Raz; Chill, Jordan. "Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain"  Biochim. Biophys. Acta Biomembr. 1861, 183054-183054 (2019).
PubMed: 31487494

Assembly members:

Assembly members:
BteA131, polymer, 134 residues, 14940.66 Da.

Natural source:

Natural source:   Common Name: Bordetella pertussis   Taxonomy ID: 520   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella pertussis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts101
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BteA1311

Entities:

Entity 1, BteA131 134 residues - 14940.66 Da.

1   GLYSERHISMETLEUSERSERASNVALASN
2   PROVALVALGLYLEUSERTYRARGPROLEU
3   PROGLUTHRPROPROSERGLYGLNALAALA
4   ALAHISPROSERMETARGLEULEUGLUPRO
5   ASNASNASPGLUPHEVALARGSERVALALA
6   SERPROARGLEUHISHISSERSERGLUALA
7   LEUARGGLUVALLYSHISASPVALARGGLN
8   PHEGLNALASERGLYASPARGSERLEUGLN
9   GLNLEUARGASPLEUGLUVALALALEUASN
10   HISTRPGLUALASERGLNPROARGGLUPHE
11   ALALYSARGGLYGLYMETVALALAGLULEU
12   ARGTHRALAILEASPALATYRLYSGLNGLN
13   LEUHISGLUGLNALAPROSERHISALAASN
14   LEUASPVALLYS

Samples:

sample_1: BteA131 mM; bis-Tris 20 ± 0.2 mM; NaCl 100 ± 1 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.3; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, peak picking, processing

NMR spectrometers:

  • Bruker DRX 700 MHz

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