BMRB Entry 18883
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18883
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Title: TICAM-1 TIR domain structure PubMed: 24255114
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: 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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 750 |
| 15N chemical shifts | 186 |
| 1H chemical shifts | 1203 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TICAM-1 TIR domain | 1 |
Entities:
Entity 1, TICAM-1 TIR domain 168 residues - 18061.678 Da.
| 1 | MET | GLU | SER | SER | SER | GLU | GLN | LYS | PHE | TYR | ||||
| 2 | ASN | PHE | VAL | ILE | LEU | HIS | ALA | ARG | ALA | ASP | ||||
| 3 | GLU | HIS | ILE | ALA | LEU | ARG | VAL | ARG | GLU | LYS | ||||
| 4 | LEU | GLU | ALA | LEU | GLY | VAL | PRO | ASP | GLY | ALA | ||||
| 5 | THR | PHE | CYS | GLU | ASP | PHE | GLN | VAL | HIS | GLY | ||||
| 6 | ARG | GLY | GLU | LEU | SER | CYS | LEU | GLN | ASP | ALA | ||||
| 7 | ILE | ASP | HIS | SER | ALA | PHE | ILE | ILE | LEU | LEU | ||||
| 8 | LEU | THR | SER | ASN | PHE | ASP | CYS | ARG | LEU | SER | ||||
| 9 | LEU | HIS | GLN | VAL | ASN | GLN | ALA | MET | MET | SER | ||||
| 10 | ASN | LEU | THR | ARG | GLN | GLY | SER | PRO | ASP | CYS | ||||
| 11 | VAL | ILE | PRO | PHE | LEU | PRO | LEU | GLU | SER | SER | ||||
| 12 | PRO | ALA | GLN | LEU | SER | SER | ASP | THR | ALA | SER | ||||
| 13 | LEU | LEU | SER | GLY | LEU | VAL | ARG | LEU | ASP | GLU | ||||
| 14 | HIS | SER | GLN | ILE | PHE | ALA | ARG | LYS | VAL | ALA | ||||
| 15 | ASN | THR | PHE | LYS | PRO | HIS | ARG | LEU | GLN | ALA | ||||
| 16 | ARG | LYS | ALA | MET | TRP | ARG | LYS | GLU | GLN | ASP | ||||
| 17 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | CN | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | CN | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | CN | isotropic | sample_conditions_1 |
| 3D HNCO | CN | isotropic | sample_conditions_1 |
| 3D HNCA | CN | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | CN | isotropic | sample_conditions_1 |
| 3D HNCACB | CN | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | CN | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | CN | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | CN | isotropic | sample_conditions_1 |
| 3D C(CO)NH | CN | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | CN | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | CN | isotropic | sample_conditions_1 |
| 3D HCACO | CN | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | CN | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | CN | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | CN | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts