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 18883

Title: TICAM-1 TIR domain structure   PubMed: 24255114

Authors: Enokizono, Yoshiaki; Kumeta, Hiroyuki; Funami, Kenji; Horiuchi, Masataka; Sarmiento, Joy; Yamashita, Kazuo; Standley, Daron; Matsumoto, Misako; Seya, Tsukasa; Inagaki, Fuyuhiko

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).

Assembly members:
TICAM1TIR, polymer, 168 residues, 18061.678 Da.

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

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

Entity Sequences (FASTA):
TICAM1TIR: MESSSEQKFYNFVILHARAD EHIALRVREKLEALGVPDGA TFCEDFQVHGRGELSCLQDA IDHSAFIILLLTSNFDCRLS LHQVNQAMMSNLTRQGSPDC VIPFLPLESSPAQLSSDTAS LLSGLVRLDEHSQIFARKVA NTFKPHRLQARKAMWRKEQD LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts750
15N chemical shifts186
1H chemical shifts1203

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TICAM-1 TIR domain1

Entities:

Entity 1, TICAM-1 TIR domain 168 residues - 18061.678 Da.

1   METGLUSERSERSERGLUGLNLYSPHETYR
2   ASNPHEVALILELEUHISALAARGALAASP
3   GLUHISILEALALEUARGVALARGGLULYS
4   LEUGLUALALEUGLYVALPROASPGLYALA
5   THRPHECYSGLUASPPHEGLNVALHISGLY
6   ARGGLYGLULEUSERCYSLEUGLNASPALA
7   ILEASPHISSERALAPHEILEILELEULEU
8   LEUTHRSERASNPHEASPCYSARGLEUSER
9   LEUHISGLNVALASNGLNALAMETMETSER
10   ASNLEUTHRARGGLNGLYSERPROASPCYS
11   VALILEPROPHELEUPROLEUGLUSERSER
12   PROALAGLNLEUSERSERASPTHRALASER
13   LEULEUSERGLYLEUVALARGLEUASPGLU
14   HISSERGLNILEPHEALAARGLYSVALALA
15   ASNTHRPHELYSPROHISARGLEUGLNALA
16   ARGLYSALAMETTRPARGLYSGLUGLNASP
17   LEUGLUHISHISHISHISHISHIS

Samples:

CN: TICAM-1 TIR, [U-99% 13C; U-99% 15N], 0.5 mM; AcOH Buffer 20 mM; DTT 5 mM; DSS 0.02 mg/mL; H20 90%; D20 10%

sample_conditions_1: ionic strength: 20 mM; pH: 5.0; pressure: 1 atm; temperature: 298 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 H(CCO)NHCNisotropicsample_conditions_1
3D HBHA(CO)NHCNisotropicsample_conditions_1
3D C(CO)NHCNisotropicsample_conditions_1
3D HCCH-TOCSYCNisotropicsample_conditions_1
3D HCCH-COSYCNisotropicsample_conditions_1
3D HCACOCNisotropicsample_conditions_1
3D 1H-15N NOESYCNisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticCNisotropicsample_conditions_1
2D 1H-13C HSQC 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, data analysis, 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: