BMRB Entry 16067

Name: Backbone assignment of RelB antitoxin C-terminal peptide (RelBc) in the RelE-free state
Published: 2009-04-22

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16067

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone assignment of RelB antitoxin C-terminal peptide (RelBc) in the RelE-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:
RelBc, polymer, 36 residues, 4128.7 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: PGEX2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RelBc: GSHKQTLLSDEDAELVEIVK ERLRNPKPVRVTLDEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	66
15N chemical shifts	31
1H chemical shifts	31

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	chain A	1

Entities:

Entity 1, chain A 36 residues - 4128.7 Da.

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

1

GLY

SER

HIS

LYS

GLN

THR

LEU

SER

ASP

2

GLU

ASP

ALA

GLU

LEU

VAL

GLU

ILE

VAL

LYS

3

GLU

ARG

LEU

ARG

ASN

PRO

LYS

PRO

VAL

ARG

4

VAL

THR

LEU

ASP

GLU

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_h2o	isotropic	sample_conditions_1
3D HNCACB	sample_h2o	isotropic	sample_conditions_1
3D C(CO)NH	sample_h2o	isotropic	sample_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

PDB	2KC8 4FXE
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
AlphaFold	P0C079 P0C080