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 15691

Title: Structure of the DBD domain of E. coli antitoxin RelB   PubMed: 18501926

Deposition date: 2008-03-23 Original release date: 2008-06-27

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

Citation: Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko. "Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module"  J. Mol. Biol. 380, 107-119 (2008).

Assembly members:
RelB, polymer, 53 residues, 5993.9 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):
RelB: GSHMGSINLRIDDELKARSY AALEKMGVTPSEALRLMLEY IADNERLPFKQTL

Data sets:
Data typeCount
15N chemical shifts52
1H chemical shifts362
residual dipolar couplings42

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 53 residues - 5993.9 Da.

Residues 1-3 represent a non-native affinity tag. This is a DNA binding domain of a antitoxin protein.

1   GLYSERHISMETGLYSERILEASNLEUARG
2   ILEASPASPGLULEULYSALAARGSERTYR
3   ALAALALEUGLULYSMETGLYVALTHRPRO
4   SERGLUALALEUARGLEUMETLEUGLUTYR
5   ILEALAASPASNGLUARGLEUPROPHELYS
6   GLNTHRLEU

Samples:

sample_1: RelBN, [U-100% 13C; U-100% 15N], 0.5-1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 1 uM

sample_2: RelBN, [U-100% 13C; U-100% 15N], 0.5-1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 1 uM

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

VNMR v6.1C, Varian - collection

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA15263 BAI25453 BAJ43364 BAN94923
EMBL CAA26250 CAQ98463 CBG34538 CBK86917 CCF87937
GB AAC74637 AAN43138 AAP17029 AAS76441 ABF03723
REF NP_416082 NP_707431 WP_000534857 WP_000534858 WP_001408098
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