BMRB Entry 34610

Title:
Solution structure of toll like receptor 1 (TLR1) TIR domain
Deposition date:
2021-03-09
Original release date:
2021-08-17
Authors:
Mineev, K.; Lushpa, V.; Goncharuk, M.
Citation:

Citation: Lushpa, Vladislav; Goncharuk, Marina; Lin, Cong; Zalevsky, Arthur; Talyzina, Irina; Luginina, Aleksandra; Vakhrameev, Daniil; Shevtsov, Mikhail; Goncharuk, Sergey; Arseniev, Alexander; Borshchevskiy, Valentin; Wang, Xiaohui; Mineev, Konstantin. "Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn 2+ ions"  Commun. Biol. 4, 1003-1003 (2021).
PubMed: 34429510

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 19204.139 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts729
15N chemical shifts160
1H chemical shifts1192

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 163 residues - 19204.139 Da.

1   SERASNILEPROLEUGLUGLULEUGLNARG
2   ASNLEUGLNPHEHISALAPHEILESERTYR
3   SERGLYHISASPSERPHETRPVALLYSASN
4   GLULEULEUPROASNLEUGLULYSGLUGLY
5   METGLNILECYSLEUHISGLUARGASNPHE
6   VALPROGLYLYSSERILEVALGLUASNILE
7   ILETHRCYSILEGLULYSSERTYRLYSSER
8   ILEPHEVALLEUSERPROASNPHEVALGLN
9   SERGLUTRPCYSHISTYRGLULEUTYRPHE
10   ALAHISHISASNLEUPHEHISGLUGLYSER
11   ASNSERLEUILELEUILELEULEUGLUPRO
12   ILEPROGLNTYRSERILEPROSERSERTYR
13   HISLYSLEULYSSERLEUMETALAARGARG
14   THRTYRLEUGLUTRPPROLYSGLULYSSER
15   LYSARGGLYLEUPHETRPALAASNLEUARG
16   ALAALAILEASNILELYSLEUTHRGLUGLN
17   ALALYSLYS

Samples:

sample_1: TLR1-TIR, [U-100% 13C; U-100% 15N], 0.8 mM; PIPES 20 mM; sodium chloride 25 mM; TCEP 3 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment, peak picking

qMDD v2.7, Orekhov, Mayzel - processing

TopSpin, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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