BMRB Entry 16066

Title:
Structure of E. coli toxin RelE(R81A/R83A) mutant in the free state
Deposition date:
2008-12-17
Original release date:
2009-04-22
Authors:
Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko
Citation:

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).
PubMed: 19297318

Assembly members:

Assembly members:
RelE, polymer, 98 residues, 11336.2 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts409
15N chemical shifts94
1H chemical shifts726

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chain A1

Entities:

Entity 1, chain A 98 residues - 11336.2 Da.

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

1   GLYSERHISMETALATYRPHELEUASPPHE
2   ASPGLUARGALALEULYSGLUTRPARGLYS
3   LEUGLYSERTHRVALARGGLUGLNLEULYS
4   LYSLYSLEUVALGLUVALLEUGLUSERPRO
5   ARGILEGLUALAASNLYSLEUARGGLYMET
6   PROASPCYSTYRLYSILELYSLEUARGSER
7   SERGLYTYRARGLEUVALTYRGLNVALILE
8   ASPGLULYSVALVALVALPHEVALILESER
9   VALGLYLYSALAGLUALASERGLUVALTYR
10   SERGLUALAVALLYSARGILELEU

Samples:

sample_h2o: RelE, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 0 mM; sodium chloride 500 ± 0 mM; DTT 1 mM; sodium azide 0.5 mM

sample_d2o: RelE, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 0 mM; sodium chloride 500 ± 0 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
2D 1H-15N HSQCsample_h2oisotropicsample_conditions_1
3D HNCACBsample_h2oisotropicsample_conditions_1
3D C(CO)NHsample_h2oisotropicsample_conditions_1
3D HNCOsample_h2oisotropicsample_conditions_1
3D H(CCO)NHsample_h2oisotropicsample_conditions_1
3D 1H-15N NOESYsample_h2oisotropicsample_conditions_1
2D 1H-13C HSQCsample_d2oisotropicsample_conditions_1
3D HCCH-TOCSYsample_d2oisotropicsample_conditions_1
3D HCCH-COSYsample_d2oisotropicsample_conditions_1
3D 1H-13C NOESYsample_d2oisotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

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

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - automated NOE peak assignments, structure solution

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

Molmol, Koradi, Billeter and Wuthrich - structure analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16065
PDB
DBJ BAA15262 BAI25452 BAJ43363
EMBL CAA26251 CBG34537 CCF87938 CDJ71963 CDP71409
GB AAC74636 AAN43137 AAP17028 AAS76442 ABQ02944
REF NP_416081 NP_707430 WP_000323024 WP_000323025 WP_001513653
SP P0C077 P0C078
AlphaFold P0C077 P0C078

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