BMRB Entry 50263
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50263
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Title: NMR backbone assignment of the transmembrane helix of TREM2, an Alzheimer linked disease protein PubMed: 32830336
Deposition date: 2020-05-08 Original release date: 2020-06-08
Authors: Steiner, Andrea; Hagn, Franz
Citation: Steiner, Andrea; Schlepckow, Kai; Brunner, Bettina; Steiner, Harald; Haass, Christian; Hagn, Franz. "gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics" EMBO J. 39, e104247-e104247 (2020).
Assembly members:
entity_1, polymer, 49 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
Entity Sequences (FASTA):
entity_1: GSGRSLLEGEIPFPPTSILL
LLACIFLIKILAASALWAAA
WHGQKPGTH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 103 |
| 15N chemical shifts | 32 |
| 1H chemical shifts | 32 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TREM2 | 1 |
Entities:
Entity 1, TREM2 49 residues - Formula weight is not available
| 1 | GLY | SER | GLY | ARG | SER | LEU | LEU | GLU | GLY | GLU | ||||
| 2 | ILE | PRO | PHE | PRO | PRO | THR | SER | ILE | LEU | LEU | ||||
| 3 | LEU | LEU | ALA | CYS | ILE | PHE | LEU | ILE | LYS | ILE | ||||
| 4 | LEU | ALA | ALA | SER | ALA | LEU | TRP | ALA | ALA | ALA | ||||
| 5 | TRP | HIS | GLY | GLN | LYS | PRO | GLY | THR | HIS |
Samples:
sample_1: TREM2, [U-13C; U-15N; U-2H], 500 ± 50 uM; DPC 200 mM; NaPi 20 mM; NaCl 50 mM; EDTA 0.5 mM; DTT 5 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5 - collection
NMRFAM-SPARKY - chemical shift assignment
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