BMRB Entry 51860

Name: 1H, 13C and 15N backbone chemical shifts for N-terminal domain of FtsQ (FtsQ1-99) from Mycobacterium tuberculosis
Published: 2023-03-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51860

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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:

1H, 13C and 15N backbone chemical shifts for N-terminal domain of FtsQ (FtsQ1-99) from Mycobacterium tuberculosis

Deposition date:

2023-02-27

Original release date:

2023-03-27

Authors:

Smrt, Sean; Escobar, Cristian; Dey, Souvik; Cross, Timothy; Zhou, Huan-Xiang

Citation:

Citation: Smrt, Sean; Escobar, Cristian; Dey, Souvik; Cross, Timothy; Zhou, Huan-Xiang. "An Arg/Ala-rich helix in the N-terminal region of M. tuberculosis FtsQ is a potential membrane anchor of the Z-ring" Commun. Biol. 6, 311-311 (2023).
PubMed: 36959324

Assembly members:

Assembly members:
entity_1, polymer, 99 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: pTBSG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTEHNEDPQIERVADDAADE EAVTEPLATESKDEPAEHPE FEGPRRRARRERAERRAAQA RATAIEQARRAAKRRARGQI VSEQNPAKPAARGVVRGLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	266
15N chemical shifts	92
1H chemical shifts	92
T1 relaxation values	83
T2 relaxation values	80
heteronuclear NOE values	85

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FtsQ1-99	1

Entities:

Entity 1, FtsQ1-99 99 residues - Formula weight is not available

1

MET

THR

GLU

HIS

ASN

GLU

ASP

PRO

GLN

ILE

2

GLU

ARG

VAL

ALA

ASP

ALA

ASP

GLU

3

GLU

ALA

VAL

THR

GLU

PRO

LEU

ALA

THR

GLU

4

SER

LYS

ASP

GLU

PRO

ALA

GLU

HIS

PRO

GLU

5

PHE

GLU

GLY

PRO

ARG

ALA

ARG

6

GLU

ARG

ALA

GLU

ARG

ALA

GLN

ALA

7

ARG

ALA

THR

ALA

ILE

GLU

GLN

ALA

ARG

8

ALA

LYS

ARG

ALA

ARG

GLY

GLN

ILE

9

VAL

SER

GLU

GLN

ASN

PRO

ALA

LYS

PRO

ALA

10

ALA

ARG

GLY

VAL

ARG

GLY

LEU

LYS

Samples:

sample_1: FtsQ1-99, [U-100% 13C; U-100% 15N], 370 uM

sample_2: FtsQ1-99, [U-100% 15N], 400 uM

sample_conditions_1: pH: 6.85; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
T1rho/R1rho relaxation	sample_2	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_1
T1/R1 relaxation	sample_2	isotropic	sample_conditions_1
T2/R2 relaxation	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - data analysis

X-PLOR NIH - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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