BMRB Entry 28032

Name: Chemical shifts of mouse BTNL2 IgV1 domain
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28032

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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:

Chemical shifts of mouse BTNL2 IgV1 domain

Deposition date:

2019-10-19

Original release date:

2021-07-16

Authors:

Basak, Aditya; De, Soumya

Citation:

Citation: Basak, Aditya; Maiti, Snigdha; Hansda, Anita; Mahata, Dhrubajyoti; Duraivelan, Kheerthana; Kundapura, Shankar; Lee, Woonghee; Mukherjee, Gayatri; De, Soumya; Samanta, Dibyendu. "Structural Insights into N-terminal IgV Domain of BTNL2, a T Cell Inhibitory Molecule, Suggests a Non-canonical Binding Interface for Its Putative Receptors" J. Mol. Biol. 432, 5938-5950 (2020).
PubMed: 32976909

Assembly members:

Assembly members:
BTNL2, polymer, 117 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BTNL2: MDFRVVGPNLPILAKVGEDA LLTCQLLPKRTTAHMEVRWY RSDPDMPVIMYRDGAEVTGL PMEGYGGRAEWMEDSTEEGS VALKIRQVQPSDDGQYWCRF QEGDYWRETSVLLQVAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	452
15N chemical shifts	113
1H chemical shifts	663

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BTNL2 Igv1 monomer	1

Entities:

Entity 1, BTNL2 Igv1 monomer 117 residues - Formula weight is not available

1

MET

ASP

PHE

ARG

VAL

GLY

PRO

ASN

LEU

2

PRO

ILE

LEU

ALA

LYS

VAL

GLY

GLU

ASP

ALA

3

LEU

THR

CYS

GLN

LEU

PRO

LYS

ARG

4

THR

ALA

HIS

MET

GLU

VAL

ARG

TRP

TYR

5

ARG

SER

ASP

PRO

ASP

MET

PRO

VAL

ILE

MET

6

TYR

ARG

ASP

GLY

ALA

GLU

VAL

THR

GLY

LEU

7

PRO

MET

GLU

GLY

TYR

GLY

ARG

ALA

GLU

8

TRP

MET

GLU

ASP

SER

THR

GLU

GLY

SER

9

VAL

ALA

LEU

LYS

ILE

ARG

GLN

VAL

GLN

PRO

10

SER

ASP

GLY

GLN

TYR

TRP

CYS

ARG

PHE

11

GLN

GLU

GLY

ASP

TYR

TRP

ARG

GLU

THR

SER

12

VAL

LEU

GLN

VAL

ALA

Samples:

sample_1: BTNL2, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 90 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

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