BMRB Entry 27580

Name: Backbone 1H, 15N and 13C Chemical shifts of N-terminal domain of antitoxin VapB46 from Mycobacterium tuberculosis
Published: 2019-01-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27580

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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:

Backbone 1H, 15N and 13C Chemical shifts of N-terminal domain of antitoxin VapB46 from Mycobacterium tuberculosis

Deposition date:

2018-08-18

Original release date:

2019-01-02

Authors:

Roy, Madhurima; De, Soumya; Das, Amit

Citation:

Citation: Roy, Madhurima; Kundu, Anirban; Bhunia, Anirban; Das Gupta, Sujoy; De, Soumya; Das, Amit Kumar. "Structural characterization of VapB46 antitoxin from Mycobacterium tuberculosis: insights into VapB46-DNA binding." FEBS J. 286, 1174-1190 (2019).
PubMed: 30576065

Assembly members:

Assembly members:
VapB46, polymer, 66 residues, Formula weight is not available

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 Vector: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VapB46: MRGSHHHHHHGSMTPTACAT VSTMTSVGVRALRQRASELL RRVEAGETIEITDRGRPVAL LSPLPQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	148
15N chemical shifts	46
1H chemical shifts	46

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VapB46	1

Entities:

Entity 1, VapB46 66 residues - Formula weight is not available

1

MET

ARG

GLY

SER

HIS

2

GLY

SER

MET

THR

PRO

THR

ALA

CYS

ALA

THR

3

VAL

SER

THR

MET

THR

SER

VAL

GLY

VAL

ARG

4

ALA

LEU

ARG

GLN

ARG

ALA

SER

GLU

LEU

5

ARG

VAL

GLU

ALA

GLY

GLU

THR

ILE

GLU

6

ILE

THR

ASP

ARG

GLY

ARG

PRO

VAL

ALA

LEU

7

LEU

SER

PRO

LEU

PRO

GLN

Samples:

sample_1: VapB46, [U-13C; U-15N], 0.3 mM; potassium phosphate 50 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz

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