BMRB Entry 16065

Name: Structure of E. coli toxin RelE(R81A/R83A)mutant in complex with antitoxin RelBc (K47-L79) peptide
Published: 2009-04-22

Click here to enlarge.

PDB ID: 2kc8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16065
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Structure of E. coli toxin RelE(R81A/R83A)mutant in complex with antitoxin RelBc (K47-L79) peptide 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:
RelE, polymer, 98 residues, 11336.2 Da.
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):
RelE: GSHMAYFLDFDERALKEWRK LGSTVREQLKKKLVEVLESP RIEANKLRGMPDCYKIKLRS SGYRLVYQVIDEKVVVFVIS VGKAEASEVYSEAVKRIL
RelBc: GSHKQTLLSDEDAELVEIVK ERLRNPKPVRVTLDEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	496
15N chemical shifts	127
1H chemical shifts	993

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Entity Assembly ID	Entity Name	Entity ID
1	subunit A	1
2	subunit B	2

Samples:

sample_1: RelE, [U-13C; U-15N], 0.5 ± 0.2 mM; RelBc 0.5 ± 0.2 mM; sodium phosphate 25 ± 0 mM; sodium chloride 500 ± 0 mM; DTT 1 ± 0 mM; sodium azide 0.5 ± 0 mM

sample_2: RelE 0.5 ± 0.1 mM; RelBc, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 mM

sample_3: RelE, [U-13C; U-15N], 0.5 ± 0.1 mM; RelBc 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 mM

sample_4: RelE 0.5 ± 0.1 mM; RelBc, [U-13C; U-15N], 0.5 ± 0.1 mM; sodium phosphate 25 ± 2.5 mM; sodium chloride 500 ± 50 mM; DTT 1 ± 0.1 mM; sodium azide 0.5 ± 0.1 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_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D HCCH-COSY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1
3D X-filtered 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D X-filtered 1H-13C NOESY	sample_4	isotropic	sample_conditions_1

BMRB	16066 16067
PDB	2KC8 2KC9 3KIQ 3KIS 3KIU 3KIX 4FXE 4FXH 4FXI 2KC8 4FXE
DBJ	BAA15262 BAI25452 BAJ43363 BAA15263 BAI25453 BAJ43364
EMBL	CAA26251 CBG34537 CCF87938 CDJ71963 CDP71409 CAA26250 CAQ98463 CBG34538 CBK86917 CCF87937
GB	AAC74636 AAN43137 AAP17028 AAS76442 ABQ02944 AAC74637 AAN43138 AAP17029 ABF03723 ABP62831
REF	NP_416081 NP_707430 WP_000323024 WP_000323025 WP_001513653 NP_416082 NP_707431 NP_837222 WP_000534858 WP_001413280
SP	P0C077 P0C078 P0C079 P0C080

Biological Magnetic Resonance Data Bank

BMRB Entry 16065

Title: Structure of E. coli toxin RelE(R81A/R83A)mutant in complex with antitoxin RelBc (K47-L79) peptide PubMed: 19297318

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: