BMRB Entry 27525
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27525
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Citation: Gandhi, Amit; Kim, Walter; Sun, Zhen-Yu; Huang, Yu-Hwa; Bonsor, Daniel; Sundberg, Eric; Wagner, Gerhard; Kuchroo, Vijay; Petsko, Greg; Blumberg, Richard. "High resolution X-ray and NMR structural study of human T-cell immunoglobulin and mucin domain containing protein-3" Sci. Rep. 8, 17512-17512 (2018).
Assembly members:
hTIM3, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21d
Entity Sequences (FASTA):
hTIM3: MVEYRAEVGQNAYLPCFYTP
AAPGNLVPVCWGKGACPVFE
CGNVVLRTDERDVNYWTSRY
WLNGDFRKGDVSLTIENVTL
ADSGIYCCRIQIPGIMNDEK
FNLKLVIK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 216 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 77 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hTIM3 | 1 |
Entities:
Entity 1, hTIM3 108 residues - Formula weight is not available
N-terminal Met residue (start codon) is artificial.
| 1 | MET | VAL | GLU | TYR | ARG | ALA | GLU | VAL | GLY | GLN | ||||
| 2 | ASN | ALA | TYR | LEU | PRO | CYS | PHE | TYR | THR | PRO | ||||
| 3 | ALA | ALA | PRO | GLY | ASN | LEU | VAL | PRO | VAL | CYS | ||||
| 4 | TRP | GLY | LYS | GLY | ALA | CYS | PRO | VAL | PHE | GLU | ||||
| 5 | CYS | GLY | ASN | VAL | VAL | LEU | ARG | THR | ASP | GLU | ||||
| 6 | ARG | ASP | VAL | ASN | TYR | TRP | THR | SER | ARG | TYR | ||||
| 7 | TRP | LEU | ASN | GLY | ASP | PHE | ARG | LYS | GLY | ASP | ||||
| 8 | VAL | SER | LEU | THR | ILE | GLU | ASN | VAL | THR | LEU | ||||
| 9 | ALA | ASP | SER | GLY | ILE | TYR | CYS | CYS | ARG | ILE | ||||
| 10 | GLN | ILE | PRO | GLY | ILE | MET | ASN | ASP | GLU | LYS | ||||
| 11 | PHE | ASN | LEU | LYS | LEU | VAL | ILE | LYS |
Samples:
sample_1: hTIM3, [U-100% 13C; U-100% 15N], 0.85 mM; HEPES 10 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA, Keller and Wuthrich - data analysis
NMR spectrometers:
- Agilent DD2 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks