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 26068

Title: Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum

Deposition date: 2016-09-13 Original release date: 2016-11-03

Authors: Altukhov, Dmitry; Talyzina, Anna; Agapova, Yulia; Vlaskina, Anna; Korzhenevskiy, Dmitry; Bocharov, Eduard; Rakitina, Tatiana; Timofeev, Vladimir; Popov, Vladimir

Citation: Altukhov, Dmitry; Talyzina, Anna; Agapova, Yulia; Vlaskina, Anna; Korzhenevskiy, Dmitry; Bocharov, Eduard; Rakitina, Tatiana; Timofeev, Vladimir; Popov, Vladimir. "Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum"  Biochem. Biophys. Res. Commun. ., .-..

Assembly members:
entity, polymer, 99 residues, 10983.192 Da.

Natural source:   Common Name: Mycoplasma gallisepticum   Taxonomy ID: 2096   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycoplasma gallisepticum

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

Entity Sequences (FASTA):
entity: MAKIKSLSAAEYLKEMADET NIKVQDIRLVVTSLQKVLAK ELATTGEVRLFDIGKFKLVT TKPRTGINPKTKQKIQIPAG KKIKLTVSKILTDAVDSHK

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts94
1H chemical shifts163

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 99 residues - 10983.192 Da.

1   METALALYSILELYSSERLEUSERALAALA
2   GLUTYRLEULYSGLUMETALAASPGLUTHR
3   ASNILELYSVALGLNASPILEARGLEUVAL
4   VALTHRSERLEUGLNLYSVALLEUALALYS
5   GLULEUALATHRTHRGLYGLUVALARGLEU
6   PHEASPILEGLYLYSPHELYSLEUVALTHR
7   THRLYSPROARGTHRGLYILEASNPROLYS
8   THRLYSGLNLYSILEGLNILEPROALAGLY
9   LYSLYSILELYSLEUTHRVALSERLYSILE
10   LEUTHRASPALAVALASPSERHISLYS

Samples:

sample_1: entity, [U-13C; U-15N], 1 mM; D2O, [U-2H], 5%; sodium phosphate 50 mM; sodium azide 0.1 mM

sample_conditions_1: ionic strength: 0.375 M; pH: 6.7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TALOS++, Cornilescu, Delaglio and Bax - chemical shift assignment

GROMACS, Herman Berendsen's group, department of Biophysical Chemistry of Groningen University - refinement

NMR spectrometers:

  • Agilent Uniform NMR System 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts