BMRB Entry 26010

Name: NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain.
Published: 2016-09-08

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PDB ID: 2nc8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26010
MolProbity Validation Chart

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

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Title:

NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain.

Deposition date:

2016-03-22

Original release date:

2016-09-08

Authors:

Barthe, Philippe; Cohen-Gonsaud, Martin

Citation:

Citation: Barthe, Philippe; Veyron-Churlet, Romain; de Vish, Angelique; Gilleron, Martine; Saliou, Jean-Michel; Nigou, Jerome; Brodin, Priscille; Cohen-Gonsaud, Martin. "Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization" Structure 24, 1788-1794 (2016).
PubMed: 27568926

Assembly members:

Assembly members:
entity, polymer, 171 residues, 18229.328 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GRENLYFQGHMLRVRASITI SPDDLVSGEIIAAAKPKNSK DTGPALDGDVPFSQKVAVSN YDSDGYVGSQAVFSDLTFAE LPQLANMNSDAAGVNLSLRR NGNIVILEGRADLTSVSDPD ADVELTVAFPAAVTSTNGDR IEPEVVQWKLKPGVVSTMSA QARYTDPNTRS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	461
15N chemical shifts	169
1H chemical shifts	1052

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 171 residues - 18229.328 Da.

1

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

GLY

HIS

2

MET

LEU

ARG

VAL

ARG

ALA

SER

ILE

THR

ILE

3

SER

PRO

ASP

LEU

VAL

SER

GLY

GLU

ILE

4

ILE

ALA

LYS

PRO

LYS

ASN

SER

LYS

5

ASP

THR

GLY

PRO

ALA

LEU

ASP

GLY

ASP

VAL

6

PRO

PHE

SER

GLN

LYS

VAL

ALA

VAL

SER

ASN

7

TYR

ASP

SER

ASP

GLY

TYR

VAL

GLY

SER

GLN

8

ALA

VAL

PHE

SER

ASP

LEU

THR

PHE

ALA

GLU

9

LEU

PRO

GLN

LEU

ALA

ASN

MET

ASN

SER

ASP

10

ALA

GLY

VAL

ASN

LEU

SER

LEU

ARG

11

ASN

GLY

ASN

ILE

VAL

ILE

LEU

GLU

GLY

ARG

12

ALA

ASP

LEU

THR

SER

VAL

SER

ASP

PRO

ASP

13

ALA

ASP

VAL

GLU

LEU

THR

VAL

ALA

PHE

PRO

14

ALA

VAL

THR

SER

THR

ASN

GLY

ASP

ARG

15

ILE

GLU

PRO

GLU

VAL

GLN

TRP

LYS

LEU

16

LYS

PRO

GLY

VAL

SER

THR

MET

SER

ALA

17

GLN

ALA

ARG

TYR

THR

ASP

PRO

ASN

THR

ARG

18

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 26010

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: