BMRB Entry 51341

Title:
NMR Assignment of Backbone (1H, 15N, and 13C) resonances of Histone Like DNA binding protein of Helicobacter pylori (Hup-P64A) variant
Deposition date:
2022-03-01
Original release date:
2022-05-27
Authors:
Agarwal, Nipanshu; Kumar, Dinesh; Poluri, Krishna Mohan
Citation:

Citation: Agarwal, Nipanshu; Nagar, Nupur; Raj, Ritu; Kumar, Dinesh; Poluri, Krishna Mohan. "Conserved Apical Proline Regulating the Structure and DNA Binding Properties of Helicobacter pylori Histone-like DNA Binding Protein (Hup)"  ACS Omega 7, 15231-15246 (2022).
PubMed: 35572751

Assembly members:

Assembly members:
entity_1, polymer, 98 residues, 10772 Da.

Natural source:

Natural source:   Common Name: Helicobacter pylori   Taxonomy ID: 210   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Helicobacter pylori

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE 80L

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts86
1H chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Chain A1
2Chain B1

Entities:

Entity 1, Chain A 98 residues - 10772 Da.

Residue -4 to -1 represent cloning artifacts Protein has 6X-His tag at N terminus

1   GLYALAMETGLUMETASNLYSALAGLUPHE
2   ILEASPLEUVALLYSGLUALAGLYLYSTYR
3   ASNSERLYSARGGLUALAGLUGLUALAILE
4   SERALAPHETHRLEUALAVALGLUTHRALA
5   LEUSERLYSGLYGLUSERVALGLULEUILE
6   GLYPHEGLYLYSPHEGLUTHRALAGLUGLN
7   LYSGLYLYSGLUGLYLYSVALALAGLYSER
8   ASPLYSTHRTYRLYSTHRGLUASPLYSARG
9   VALPROLYSPHELYSPROGLYLYSTHRLEU
10   LYSGLNLYSVALGLUGLUGLYLYS

Samples:

sample_1: Histone Like DNA binding protein of Helicobacter pylori (Hup-P64A) variant, [U-99% 13C; U-99% 15N], 0.75 mM; D2O, [U-100% 15N], 10%; sodium chloride 200 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.079 M; pH: 6; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CARA v1.9.1 - chemical shift assignment, data analysis

TOPSPIN v3.6.1 - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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