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 25137

Title: Ligand-induced folding of a receiver domain   PubMed: 25629646

Deposition date: 2014-08-08 Original release date: 2015-02-09

Authors: Ocasio, Victor; Correa, Fernando; Gardner, Kevin

Citation: Ocasio, Victor; Correa, Fernando; Gardner, Kevin. "Ligand-induced folding of a two-component signaling receiver domain"  Biochemistry 54, 1353-1363 (2015).

Assembly members:
EL_LovR, polymer, 125 residues, 13259.346 Da.
BERYLLIUM TRIFLUORIDE ION, non-polymer, 66.007 Da.
MAGNESIUM ION, non-polymer, 24.305 Da.

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 314225   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Erythrobacter litoralis

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

Entity Sequences (FASTA):
EL_LovR: GAMGMPKVLVLEDEPLIAMN LQYAFEDEGAEVVVAATCEQ ALKSLADNPIDVAVLDVNLG PKSHCGPVADALKQRAIPFI LHTGDLDRHGELLRKIDAPV MAKPADTSDVAKRALEMCGG DKEPA

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts121
1H chemical shifts877

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EL_LovR1
2BERYLLIUM TRIFLUORIDE ION2
3Magnesium3

Entities:

Entity 1, EL_LovR 125 residues - 13259.346 Da.

Residues 1-4 is residual TEV protease tag

1   GLYALAMETGLYMETPROLYSVALLEUVAL
2   LEUGLUASPGLUPROLEUILEALAMETASN
3   LEUGLNTYRALAPHEGLUASPGLUGLYALA
4   GLUVALVALVALALAALATHRCYSGLUGLN
5   ALALEULYSSERLEUALAASPASNPROILE
6   ASPVALALAVALLEUASPVALASNLEUGLY
7   PROLYSSERHISCYSGLYPROVALALAASP
8   ALALEULYSGLNARGALAILEPROPHEILE
9   LEUHISTHRGLYASPLEUASPARGHISGLY
10   GLULEULEUARGLYSILEASPALAPROVAL
11   METALALYSPROALAASPTHRSERASPVAL
12   ALALYSARGALALEUGLUMETCYSGLYGLY
13   ASPLYSGLUPROALA

Entity 2, BERYLLIUM TRIFLUORIDE ION - Be F3 - 66.007 Da.

1   BEF

Entity 3, Magnesium - Mg - 24.305 Da.

1   MG

Samples:

sample_1: sodium azide 3 mM; DTT 1 mM; HEPES 20 mM; AEBSF protease inhibitor 1.8 mg/mL; D2O 10%; EL_LovR, [U-100% 13C; U-100% 15N], 500 uM; Beryllium fluoride 15 mM; Magnesium Chloride 10 mM; H2O 90%

sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement, structure solution

NMRView v9.0.0-b114, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

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