BMRB Entry 6538
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6538
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Title: 1H, 13C, and 15N Chemical Shift Assignments for 2B4
Deposition date: 2005-03-07 Original release date: 2005-05-27
Authors: Ames, James
Citation: Ames, J.; Vyas, V.; Lusin, J.; Mariuzza, R.. "NMR Structure of the Natural Killer Cell Receptor 2B4 (CD244): Implications for Ligand Recognition" Biochemistry. 44, 6416-6423 (2005).
Assembly members:
D1 domain of 2B4, polymer, 109 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
D1 domain of 2B4: DCPDSSEEVVGVSGKPVQLR
PSNIQTKDVSVQWKKTEQGS
HRKIEILNWYNDGPSWSNVS
FSDIYGFDYGDFALSIKSAK
LQDSGHYLLEITNTGGKVCN
KNFQLLILD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 437 |
15N chemical shifts | 98 |
1H chemical shifts | 641 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | 2B4_polypeptide | 1 |
Entities:
Entity 1, 2B4_polypeptide 109 residues - Formula weight is not available
D1 domain of 2B4 starts at residue D21 in the mouse gene sequence. Amino acid sequence was renumbered in this study so that the first residue (D21) now becomes D1.
1 | ASP | CYS | PRO | ASP | SER | SER | GLU | GLU | VAL | VAL | ||||
2 | GLY | VAL | SER | GLY | LYS | PRO | VAL | GLN | LEU | ARG | ||||
3 | PRO | SER | ASN | ILE | GLN | THR | LYS | ASP | VAL | SER | ||||
4 | VAL | GLN | TRP | LYS | LYS | THR | GLU | GLN | GLY | SER | ||||
5 | HIS | ARG | LYS | ILE | GLU | ILE | LEU | ASN | TRP | TYR | ||||
6 | ASN | ASP | GLY | PRO | SER | TRP | SER | ASN | VAL | SER | ||||
7 | PHE | SER | ASP | ILE | TYR | GLY | PHE | ASP | TYR | GLY | ||||
8 | ASP | PHE | ALA | LEU | SER | ILE | LYS | SER | ALA | LYS | ||||
9 | LEU | GLN | ASP | SER | GLY | HIS | TYR | LEU | LEU | GLU | ||||
10 | ILE | THR | ASN | THR | GLY | GLY | LYS | VAL | CYS | ASN | ||||
11 | LYS | ASN | PHE | GLN | LEU | LEU | ILE | LEU | ASP |
Samples:
sample_1: D1 domain of 2B4, [U-95% 13C; U-90% 15N], 0.4 mM; sodium phosphate 50 mM
conditions_1: ionic strength: 0.05 M; pH: 7.2; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
HSQC | not available | isotropic | not available |
HNCO | not available | not available | not available |
HNCACB | not available | not available | not available |
CBCACONH | not available | not available | not available |
HNCOCACB | not available | not available | not available |
HBHACONH | not available | not available | not available |
15N-edited NOESY and TOCSY-HSQC | not available | not available | not available |
13C-edited NOESY-HSQC | not available | not available | not available |
HCCH-TOCSY | not available | not available | not available |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts