BMRB Entry 16066

Name: Structure of E. coli toxin RelE(R81A/R83A) mutant in the free state
Published: 2009-04-22

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PDB ID: 2kc9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16066
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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:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RelE: GSHMAYFLDFDERALKEWRK LGSTVREQLKKKLVEVLESP RIEANKLRGMPDCYKIKLRS SGYRLVYQVIDEKVVVFVIS VGKAEASEVYSEAVKRIL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	409
15N chemical shifts	94
1H chemical shifts	726

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 98 residues - 11336.2 Da.

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

1

GLY

SER

HIS

MET

ALA

TYR

PHE

LEU

ASP

PHE

2

ASP

GLU

ARG

ALA

LEU

LYS

GLU

TRP

ARG

LYS

3

LEU

GLY

SER

THR

VAL

ARG

GLU

GLN

LEU

LYS

4

LYS

LEU

VAL

GLU

VAL

LEU

GLU

SER

PRO

5

ARG

ILE

GLU

ALA

ASN

LYS

LEU

ARG

GLY

MET

6

PRO

ASP

CYS

TYR

LYS

ILE

LYS

LEU

ARG

SER

7

SER

GLY

TYR

ARG

LEU

VAL

TYR

GLN

VAL

ILE

8

ASP

GLU

LYS

VAL

PHE

VAL

ILE

SER

9

VAL

GLY

LYS

ALA

GLU

ALA

SER

GLU

VAL

TYR

10

SER

GLU

ALA

VAL

LYS

ARG

ILE

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_h2o	isotropic	sample_conditions_1
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
3D HNCO	sample_h2o	isotropic	sample_conditions_1
3D H(CCO)NH	sample_h2o	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_h2o	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_d2o	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_d2o	isotropic	sample_conditions_1
3D HCCH-COSY	sample_d2o	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_d2o	isotropic	sample_conditions_1

BMRB	16065
PDB	2KC8 2KC9 3KIQ 3KIS 3KIU 3KIX 4FXE 4FXH 4FXI
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

BMRB Entry 16066

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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