BMRB Entry 51855

Title:
Backbone and side-chain chemical shift assignments of the N terminal domain of the MazE9 (nMazE9) antitoxin in Mycobacterium tuberculosis
Deposition date:
2023-02-23
Original release date:
2023-11-21
Authors:
Basu Roy, Tanaya; Sarma, Siddhartha
Citation:

Citation: Basu Roy, Tanaya; Sarma, Siddhartha. "Insights into the solution structure and transcriptional regulation of the MazE9 antitoxin in Mycobacterium tuberculosis"  Proteins ., .-. (2023).
PubMed: 37737533

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGSMKLSVSLSDDDVAILDA YVKRAGLPSRSAGLQHAIRV LRY

Data sets:
Data typeCount
13C chemical shifts126
15N chemical shifts44
1H chemical shifts292

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nMazE9, Chain A1
2nMazE9, Chain B1

Entities:

Entity 1, nMazE9, Chain A 43 residues - Formula weight is not available

1   SERGLYSERMETLYSLEUSERVALSERLEU
2   SERASPASPASPVALALAILELEUASPALA
3   TYRVALLYSARGALAGLYLEUPROSERARG
4   SERALAGLYLEUGLNHISALAILEARGVAL
5   LEUARGTYR

Samples:

sample_1: nMazE9 450 uM; potassium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; D2O 10%

sample_2: nMazE9, [U-100% 13C; U-100% 15N], 430 uM; potassium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CC(CO)NH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

VNMRj v4.2 - NMR data acquisition

TopSpin (Bruker) v4.1.0 - NMR data acquisition

NMRPipe - NMR data processing

CcpNMR Analysis - NMR data analysis

NMR spectrometers:

  • Varian DDS2 600 MHz MHz
  • Bruker AVANCE III 700 MHz MHz

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