BMRB Entry 34359

Name: NMR solution structure of LSR2-T112D binding domain.
Published: 2019-10-03

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PDB ID: 6qkq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34359
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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 solution structure of LSR2-T112D binding domain.

Deposition date:

2019-01-30

Original release date:

2019-10-03

Authors:

Barthe, P.; Cohen-Gonsaud, M.; Mukamolova, G.

Citation:

Citation: Alqaseer, Kawther; Turapov, Obolbek; Barthe, Philippe; Jagatia, Heena; De Visch, Angelique; Roumestand, Christian; Wegrzyn, Malgorzata; Bartek, Iona; Voskuil, Martin; O'Hare, Helen; Ajuh, Paul; Bottrill, Andrew; Witney, Adam; Cohen-Gonsaud, Martin; Waddell, Simon; Mukamolova, Galina. "Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112" Mol. Microbiol. 112, 1847-1862 (2019).
PubMed: 31562654

Assembly members:

Assembly members:
entity_1, polymer, 51 residues, 5508.020 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 83332 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_1: GPHMSGSGRGRGAIDREQSA AIREWARRNGHNVSTRGRIP ADVIDAYHAAD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	53
1H chemical shifts	299

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 51 residues - 5508.020 Da.

1

GLY

PRO

HIS

MET

SER

GLY

SER

GLY

ARG

GLY

2

ARG

GLY

ALA

ILE

ASP

ARG

GLU

GLN

SER

ALA

3

ALA

ILE

ARG

GLU

TRP

ALA

ARG

ASN

GLY

4

HIS

ASN

VAL

SER

THR

ARG

GLY

ARG

ILE

PRO

5

ALA

ASP

VAL

ILE

ASP

ALA

TYR

HIS

ALA

6

ASP

Samples:

sample_1: LSR2-T112D protein, [U-15N], 0.5 mM

sample_2: LSR2-T112D protein, [U-15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CINDY, Padilla - chemical shift assignment

Gifa, Delsuc - peak picking

NMR spectrometers:

Bruker AVANCE III 700 MHz

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