BMRB Entry 36403

Name: Solution structure of TGS domain of the Mycobacterium tuberculosis Rel protein
Published: 2025-10-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36403

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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:

Solution structure of TGS domain of the Mycobacterium tuberculosis Rel protein

Deposition date:

2020-12-14

Original release date:

2025-10-25

Authors:

Shin, J.; Singal, B.; Grueber, G.

Citation:

Citation: Shin, Joon; Singal, Bharti; Gruber, Ardina; Wong, David; Ragunathan, Priya; Gruber, Gerhard. "Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA." FEBS Lett. 595, 3006-3018 (2021).
PubMed: 34808002

Assembly members:

Assembly members:
GTP pyrophosphokinase, polymer, 77 residues, 8607.881 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GTP pyrophosphokinase: MKHHHHHHPMVDLAVQEIFV FTPKGDVITLPTGSTPVDFA YAVHTEVGHRCIGARVNGRL VALERKLENGEVVEVFT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	203
15N chemical shifts	53
1H chemical shifts	439

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 77 residues - 8607.881 Da.

1

MET

LYS

HIS

PRO

MET

2

VAL

ASP

LEU

ALA

VAL

GLN

GLU

ILE

PHE

VAL

3

PHE

THR

PRO

LYS

GLY

ASP

VAL

ILE

THR

LEU

4

PRO

THR

GLY

SER

THR

PRO

VAL

ASP

PHE

ALA

5

TYR

ALA

VAL

HIS

THR

GLU

VAL

GLY

HIS

ARG

6

CYS

ILE

GLY

ALA

ARG

VAL

ASN

GLY

ARG

LEU

7

VAL

ALA

LEU

GLU

ARG

LYS

LEU

GLU

ASN

GLY

8

GLU

VAL

GLU

VAL

PHE

THR

Samples:

15N_sample: TGS domain of Rel protein, [U-15N], 0.3 mM; DTT 1 mM; sodium chloride 350 mM; TRIS 50 mM; H2O 90 % v/v; D2O, [U-2H], 10 % v/v

13C_15N_sample: TGS domain of Rel protein, [U-13C; U-15N], 0.3 mM; DTT 1 mM; sodium chloride 350 mM; TRIS 50 mM; H2O 90 % v/v; D2O, [U-2H], 10 % v/v

sample_conditions_1: ionic strength: 350 mM; pH: 8.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C_15N_sample	isotropic	sample_conditions_1
3D HNCA	not available	isotropic	sample_conditions_1
3D HN(CO)CA	not available	isotropic	sample_conditions_1
3D HCCH-TOCSY	not available	isotropic	sample_conditions_1
3D 1H-15N NOESY	not available	isotropic	sample_conditions_1
3D 1H-13C NOESY	not available	isotropic	sample_conditions_1

Software:

TopSpin v3.2, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMR spectrometers:

Bruker AVANCE 700 MHz

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