BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 28032

Title: Chemical shifts of mouse BTNL2 IgV1 domain   PubMed: 32976909

Deposition date: 2019-10-19 Original release date: 2021-07-16

Authors: Basak, Aditya; De, Soumya

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts113
1H chemical shifts663

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BTNL2 Igv1 monomer1

Entities:

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

1   METASPPHEARGVALVALGLYPROASNLEU
2   PROILELEUALALYSVALGLYGLUASPALA
3   LEULEUTHRCYSGLNLEULEUPROLYSARG
4   THRTHRALAHISMETGLUVALARGTRPTYR
5   ARGSERASPPROASPMETPROVALILEMET
6   TYRARGASPGLYALAGLUVALTHRGLYLEU
7   PROMETGLUGLYTYRGLYGLYARGALAGLU
8   TRPMETGLUASPSERTHRGLUGLUGLYSER
9   VALALALEULYSILEARGGLNVALGLNPRO
10   SERASPASPGLYGLNTYRTRPCYSARGPHE
11   GLNGLUGLYASPTYRTRPARGGLUTHRSER
12   VALLEULEUGLNVALALAALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts