BMRB Entry 18882

Title:
TICAM-2 TIR domain
Deposition date:
2012-12-07
Original release date:
2014-01-13
Authors:
Enokizono, Yoshiaki; Kumeta, Hiroyuki; Funami, Kenji; Horiuchi, Masataka; Sarmiento, Joy; Yamashita, Kazuo; Standley, Daron; Matsumoto, Misako; Seya, Tsukasa; Inagaki, Fuyuhiko
Citation:

Citation: Enokizono, Yoshiaki; Kumeta, Hiroyuki; Funami, Kenji; Horiuchi, Masataka; Sarmiento, Joy; Yamashita, Kazuo; Standley, Daron; Matsumoto, Misako; Seya, Tsukasa; Inagaki, Fuyuhiko. "Structures and interface mapping of the TIR domain-containing adaptor molecules involved in interferon signaling"  Proc. Natl. Acad. Sci. U. S. A. 110, 19908-19913 (2013).
PubMed: 24255114

Assembly members:

Assembly members:
TICAM-2_TIR, polymer, 166 residues, 19386.037 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   Vector: pGEX6p-1

Data sets:
Data typeCount
13C chemical shifts696
15N chemical shifts169
1H chemical shifts1193

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TICAM-2 TIR domain1

Entities:

Entity 1, TICAM-2 TIR domain 166 residues - 19386.037 Da.

1   GLYPROLEUGLYSERGLUGLUVALPHELEU
2   LYSPHEVALILELEUHISALAGLUASPASP
3   THRASPGLUALALEUARGVALGLNASNLEU
4   LEUGLNASPASPPHEGLYILELYSPROGLY
5   ILEILEPHEALAGLUMETPROHISGLYARG
6   GLNHISLEUGLNASNLEUASPASPALAVAL
7   ASNGLYSERALATRPTHRILELEULEULEU
8   THRGLUASNPHELEUARGASPTHRTRPCYS
9   ASNPHEGLNPHETYRTHRSERLEUMETASN
10   SERVALASNARGGLNHISLYSTYRASNSER
11   VALILEPROMETARGPROLEUASNASNPRO
12   LEUPROARGGLUARGTHRPROPHEALALEU
13   GLNTHRILEASNALALEUGLUGLUGLUSER
14   ARGGLYPHEPROTHRGLNVALGLUARGILE
15   PHEGLNGLUSERVALTYRLYSTHRGLNGLN
16   THRILETRPLYSGLUTHRARGASNMETVAL
17   GLNARGGLNPHEILEALA

Samples:

CN: TICAM-2 TIR, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES-NaOH 50 mM; DTT 10 mM; glycerol, [U-100% 2H], 5%; DSS 0.02 mg/mL

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCNisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticCNisotropicsample_conditions_1
2D 1H-13C HSQC aromaticCNisotropicsample_conditions_1
3D HNCOCNisotropicsample_conditions_1
3D HNCACNisotropicsample_conditions_1
3D HN(CO)CACNisotropicsample_conditions_1
3D HNCACBCNisotropicsample_conditions_1
3D CBCA(CO)NHCNisotropicsample_conditions_1
3D HBHA(CO)NHCNisotropicsample_conditions_1
3D HN(CA)HACNisotropicsample_conditions_1
3D H(CCO)NHCNisotropicsample_conditions_1
3D C(CO)NHCNisotropicsample_conditions_1
3D HCCH-TOCSYCNisotropicsample_conditions_1
3D 1H-15N-NOESYCNisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticCNisotropicsample_conditions_1
3D 1H-13C NOESY aromaticCNisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v2007.068.09.07, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking, refinement

TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAB21882 BAC77375 BAC98397 BAC98399 BAE88603
GB AAI09266 AAI09267 AAO74498 AAP81748 AAQ97430
REF NP_001157940 NP_001182133 NP_001182430 NP_001191270 NP_001191272
SP Q86XR7
AlphaFold Q86XR7

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