BMRB Entry 52237

Name: 1H, 13C and 15N backbone and sidechain assignment of the BRCT domain of Mtb LigA
Published: 2024-01-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52237

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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 and sidechain assignment of the BRCT domain of Mtb LigA

Deposition date:

2023-12-12

Original release date:

2024-01-15

Authors:

Vaishnav, Jayanti; Ampapathi, Ravi

Citation:

Citation: Vaishnav, Jayanti; Ampapathi, Ravi. "1H, 15N & 13C resonance Backbone and side-chain assignments and secondary structure determination of the MtbLigA BRCT Domain" J. Biomol. NMR ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 116 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 DNA Technology for Protein expression Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASMTGGQQMGRGSEFDESV PRTLAGLTIVVTGSLTGFSR DDAKEAIVARGGKAAGSVSK KTNYVVAGDSPGSKYDKAVE LGVPILDEDGFRRLLADGPA SRTKLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	340
15N chemical shifts	84
1H chemical shifts	556

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BRCT	1

Entities:

Entity 1, BRCT 116 residues - Formula weight is not available

Residues 1-16 i.e., first sixteen residues are from cloning vector; D17 to T103 in provided sequence is BRCT domain corresponding to native sequence for BRCT domain of M.tb LigA that starts from ASP 605 and runs uptil THR 691. Residues K104 to H116 are again from cloning vector containing 6X-HIS tag.

1

MET

ALA

SER

MET

THR

GLY

GLN

MET

2

GLY

ARG

GLY

SER

GLU

PHE

ASP

GLU

SER

VAL

3

PRO

ARG

THR

LEU

ALA

GLY

LEU

THR

ILE

VAL

4

VAL

THR

GLY

SER

LEU

THR

GLY

PHE

SER

ARG

5

ASP

ALA

LYS

GLU

ALA

ILE

VAL

ALA

ARG

6

GLY

LYS

ALA

GLY

SER

VAL

SER

LYS

7

LYS

THR

ASN

TYR

VAL

ALA

GLY

ASP

SER

8

PRO

GLY

SER

LYS

TYR

ASP

LYS

ALA

VAL

GLU

9

LEU

GLY

VAL

PRO

ILE

LEU

ASP

GLU

ASP

GLY

10

PHE

ARG

LEU

ALA

ASP

GLY

PRO

ALA

11

SER

ARG

THR

LYS

LEU

ALA

LEU

GLU

12

HIS

Samples:

sample_1: BRCT, [U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_2: BRCT, [U-13C; U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_3: BRCT, [U-13C; U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_3	isotropic	sample_conditions_1

Software:

NMRDraw - processing

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Agilent DD2 700 MHz