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 25863

Title: Adenylate cyclase toxin RTX domain from Bordetella pertussis   PubMed: 27058787

Deposition date: 2015-10-27 Original release date: 2016-06-15

Authors: Veverka, Vaclav

Citation: Bumba, Ladislav; Masin, Jiri; Macek, Pavel; Wald, Tomas; Motlova, Lucia; Bibova, Ilona; Klimova, Nela; Bednarova, Lucie; Veverka, Vaclav; Kachala, Michael; Svergun, Dmitri; Barinka, Cyril; Sebo, Peter. "Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts"  Mol. Cell. 62, 47-62 (2016).

Assembly members:
RTX_domain, polymer, 153 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
RTX_domain: GSARDDVLIGDAGANVLNGL AGNDVLSGGAGDDVLLGDEG SDLLSGDAGNDDLFGGQGDD TYLFGVGYGHDTIYESGGGH DTIRINAGADQLWFARQGND LEIRILGTDDALTVHDWYRD ADHRVEIIHAANQAVDQAGI EKLVEAMAQYPDP

Data sets:
Data typeCount
13C chemical shifts717
15N chemical shifts241
1H chemical shifts241

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ACT RTX domain1

Entities:

Entity 1, ACT RTX domain 153 residues - Formula weight is not available

1   GLYSERALAARGASPASPVALLEUILEGLY
2   ASPALAGLYALAASNVALLEUASNGLYLEU
3   ALAGLYASNASPVALLEUSERGLYGLYALA
4   GLYASPASPVALLEULEUGLYASPGLUGLY
5   SERASPLEULEUSERGLYASPALAGLYASN
6   ASPASPLEUPHEGLYGLYGLNGLYASPASP
7   THRTYRLEUPHEGLYVALGLYTYRGLYHIS
8   ASPTHRILETYRGLUSERGLYGLYGLYHIS
9   ASPTHRILEARGILEASNALAGLYALAASP
10   GLNLEUTRPPHEALAARGGLNGLYASNASP
11   LEUGLUILEARGILELEUGLYTHRASPASP
12   ALALEUTHRVALHISASPTRPTYRARGASP
13   ALAASPHISARGVALGLUILEILEHISALA
14   ALAASNGLNALAVALASPGLNALAGLYILE
15   GLULYSLEUVALGLUALAMETALAGLNTYR
16   PROASPPRO

Samples:

sample_Ca+: RTX_domain, [U-13C; U-15N], 0.5 mM; TRIS 5 mM; sodium chloride 50 mM; calcium chloride 10 mM; D2O, [U-2H], 5%; H2O 95%

sample_Ca-: RTX_domain, [U-13C; U-15N], 0.5 mM; TRIS 5 mM; sodium chloride 50 mM; D2O, [U-2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 0.05 M; pH: 8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_Ca+isotropicsample_conditions_1
2D 1H-15N HSQCsample_Ca-isotropicsample_conditions_1
3D HNCACBsample_Ca+isotropicsample_conditions_1
3D HNCACBsample_Ca-isotropicsample_conditions_1
3D CBCA(CO)NHsample_Ca+isotropicsample_conditions_1
3D CBCA(CO)NHsample_Ca-isotropicsample_conditions_1
3D HNCOsample_Ca+isotropicsample_conditions_1
3D HNCOsample_Ca-isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz
  • 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