BMRB Entry 18316

Name: Solution structure of the C-terminal domain of the MgtC protein from Mycobacterium tuberculosis
Published: 2012-04-11

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PDB ID: 2lqj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18316
MolProbity Validation Chart

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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:

Solution structure of the C-terminal domain of the MgtC protein from Mycobacterium tuberculosis

Deposition date:

2012-03-07

Original release date:

2012-04-11

Authors:

Yang, Martin; Yang, Yishan; Labesse, Gilles; Blanc-Potard, Anne

Citation:

Citation: Yang, Yinshan; Labesse, Gilles; Carrere-Kremer, Severine; Esteves, Kevin; Kremer, Laurent; Cohen-Gonsaud, Martin; Blanc-Potard, Anne-Beatrice. "The C-terminal domain of the virulence factor MgtC is a divergent ACT domain." J. Bacteriol. 194, 6255-6263 (2012).
PubMed: 22984256

Assembly members:

Assembly members:
entity, polymer, 94 residues, 10414.866 Da.

Natural source:

Natural source: Common Name: High GC Gram + Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: VEDEGLQPYQVRVICRPKAE TYVRAHIVQRTSSNDITLRG IRTGPAGDDNITLTAHLLMV GHTPAKLERLVAELSLQPGV YAVHWYAGEHAQAE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	264
15N chemical shifts	89
1H chemical shifts	190

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of the MgtC protein	1

Entities:

Entity 1, C-terminal domain of the MgtC protein 94 residues - 10414.866 Da.

1

VAL

GLU

ASP

GLU

GLY

LEU

GLN

PRO

TYR

GLN

2

VAL

ARG

VAL

ILE

CYS

ARG

PRO

LYS

ALA

GLU

3

THR

TYR

VAL

ARG

ALA

HIS

ILE

VAL

GLN

ARG

4

THR

SER

ASN

ASP

ILE

THR

LEU

ARG

GLY

5

ILE

ARG

THR

GLY

PRO

ALA

GLY

ASP

ASN

6

ILE

THR

LEU

THR

ALA

HIS

LEU

MET

VAL

7

GLY

HIS

THR

PRO

ALA

LYS

LEU

GLU

ARG

LEU

8

VAL

ALA

GLU

LEU

SER

LEU

GLN

PRO

GLY

VAL

9

TYR

ALA

VAL

HIS

TRP

TYR

ALA

GLY

GLU

HIS

10

ALA

GLN

ALA

GLU

Samples:

sample_1: entity, [U-100% 15N], 0.3 mM; H20 90%; D20 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.3 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 4.6; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 700 MHz

PDB	2LQJ
DBJ	BAH26116 BAL65794 BAQ05835 GAA45520
EMBL	CAL71832 CCC26903 CCC44159 CCC64414 CCE37295
GB	AAK46132 ABQ73578 ABR06176 ACT25251 AEB04323
REF	NP_216327 NP_855493 WP_003409190 WP_003899032 WP_003900414