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 16067

Title: Backbone assignment of RelB antitoxin C-terminal peptide (RelBc) in the RelE-free state   PubMed: 19297318

Deposition date: 2008-12-17 Original release date: 2009-04-22

Authors: Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko

Citation: Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko. "Inhibitory mechanism of E. coli RelE/RelB toxin/antitoxin module involves a helix displacement near a mRNA interferase active site"  J. Biol. Chem. 284, 14628-14636 (2009).

Assembly members:
RelBc, polymer, 36 residues, 4128.7 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
RelBc: GSHKQTLLSDEDAELVEIVK ERLRNPKPVRVTLDEL

Data sets:
Data typeCount
13C chemical shifts66
15N chemical shifts31
1H chemical shifts31

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1chain A1

Entities:

Entity 1, chain A 36 residues - 4128.7 Da.

Residues 1-3 represent a cloning artifact from the affinity tag.

1   GLYSERHISLYSGLNTHRLEULEUSERASP
2   GLUASPALAGLULEUVALGLUILEVALLYS
3   GLUARGLEUARGASNPROLYSPROVALARG
4   VALTHRLEUASPGLULEU

Samples:

sample_h2o: RelBc, [U-13C; U-15N], 1 ± 0.2 mM; sodium phosphate 25 mM; sodium chloride 300 mM; DTT 1 mM; sodium azide 0.5 mM

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 296.5 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_h2oisotropicsample_conditions_1
3D HNCACBsample_h2oisotropicsample_conditions_1
3D C(CO)NHsample_h2oisotropicsample_conditions_1

Software:

VNMR, Varian - collection

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAA15263 BAI25453 BAJ43364
EMBL CAA26250 CAQ98463 CBG34538 CBK86917 CCF87937
GB AAC74637 AAN43138 AAP17029 ABF03723 ABP62831
REF NP_416082 NP_707431 WP_000534858 WP_001413280 WP_001625283
SP P0C079 P0C080

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