BMRB Entry 26610

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the active domains of the type II topoisomerases from Streptococcus pneumoniae
Deposition date:
2015-07-13
Original release date:
2015-12-18
Authors:
Li, Yan; Ng, Hui Qi; Lee, Michelle Yueqi; Huang, Qiwei; Wong, Ying Lei; Kang, CongBao
Citation:

Citation: Kang, CongBao; Li, Yan; Cherian, Joseph; Liu, Boping; Ng, Hui Qi; Lee, Michelle Yueqi; Poh, Zhi Ying; Wong, Yun Xuan; Huang, Qiwei; Wong, Ying Lei; Hung, Alvin; Hill, Jeffrey; Keller, Thomas H. "Biophysical Studies of Bacterial Topoisomerases Substantiate Their Binding Modes to an Inhibitor"  Biophys. J. 109, 1969-1977 (2015).
PubMed: 26536273

Assembly members:

Assembly members:
Streptococcus_pneumoniae_active_domains_of_the_type_II_topoisomerases, polymer, 235 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Data sets:
Data typeCount
13C chemical shifts652
15N chemical shifts223
1H chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1active domains of the type II topoisomerases1

Entities:

Entity 1, active domains of the type II topoisomerases 235 residues - Formula weight is not available

1   METSERLYSLYSGLUILEASNILEASNASN
2   TYRASNASPASPALAILEGLNVALLEUGLU
3   GLYLEUASPALAVALARGLYSARGPROGLY
4   METTYRILEGLYSERTHRASPGLYALAGLY
5   LEUHISHISLEUVALTRPGLUILEVALASP
6   ASNALAVALASPGLUALALEUSERGLYPHE
7   GLYASPARGILEASPVALTHRILEASNLYS
8   ASPGLYSERLEUTHRVALGLNASPHISGLY
9   ARGGLYMETPROTHRGLYMETHISALAMET
10   GLYILEPROTHRVALGLUVALILEPHETHR
11   ILELEUHISALAGLYGLYLYSPHEGLYGLN
12   GLYGLYTYRLYSTHRSERGLYGLYLEUHIS
13   GLYVALGLYSERSERVALVALASNALALEU
14   SERSERTRPLEUGLUVALGLUILETHRARG
15   ASPGLYALAVALTYRLYSGLNARGPHEGLU
16   ASNGLYGLYLYSPROVALTHRTHRLEULYS
17   LYSILEGLYTHRALALEULYSSERLYSTHR
18   GLYTHRLYSVALTHRPHEMETPROASPALA
19   THRILEPHESERTHRTHRASPPHELYSTYR
20   ASNTHRILESERGLUARGLEUASNGLUSER
21   ALAPHELEULEULYSASNVALTHRLEUSER
22   LEUTHRASPLYSARGTHRASPGLUALAILE
23   GLUPHEHISTYRGLUASNGLYLEUGLUHIS
24   HISHISHISHISHIS

Samples:

sample_1: Streptococcus pneumoniae active domains of the type II topoisomerases, [U-13C; U-15N; U-2H], 0.8 mM; sodium phosphate 20 mM; potassium chloride 80 mM; DTT 2 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 80 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing

NMR spectrometers:

  • Bruker Avance 700 MHz

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