BMRB Entry 27565
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27565
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Title: Transmembrane protein 106B (TEM106B) PubMed: 30332472
Deposition date: 2018-07-30 Original release date: 2018-11-15
Authors: Lim, Liang Zhong; Kang, Jian; Song, Jianxing
Citation: Kang, Jian; Lim, Liang Zhong; Song, Jianxing. "TMEM106B, a risk factor for FTLD and aging, has an intrinsically disordered cytoplasmic domain" PLoS One 13, e0205856-e0205856 (2018).
Assembly members:
TMEM106B, polymer, 101 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: pET32a
Entity Sequences (FASTA):
TMEM106B: MGKSLSHLPLHSSKEDAYDG
VTSENMRNGLVNSEVHNEDG
RNGDVSQFPYVEFTGRDSVT
CPTCQGTGRIPRGQENQLVA
LIPYSDQRLRPRRLEHHHHH
H
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 179 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 307 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TMEM106B | 1 |
Entities:
Entity 1, TMEM106B 101 residues - Formula weight is not available
| 1 | MET | GLY | LYS | SER | LEU | SER | HIS | LEU | PRO | LEU | ||||
| 2 | HIS | SER | SER | LYS | GLU | ASP | ALA | TYR | ASP | GLY | ||||
| 3 | VAL | THR | SER | GLU | ASN | MET | ARG | ASN | GLY | LEU | ||||
| 4 | VAL | ASN | SER | GLU | VAL | HIS | ASN | GLU | ASP | GLY | ||||
| 5 | ARG | ASN | GLY | ASP | VAL | SER | GLN | PHE | PRO | TYR | ||||
| 6 | VAL | GLU | PHE | THR | GLY | ARG | ASP | SER | VAL | THR | ||||
| 7 | CYS | PRO | THR | CYS | GLN | GLY | THR | GLY | ARG | ILE | ||||
| 8 | PRO | ARG | GLY | GLN | GLU | ASN | GLN | LEU | VAL | ALA | ||||
| 9 | LEU | ILE | PRO | TYR | SER | ASP | GLN | ARG | LEU | ARG | ||||
| 10 | PRO | ARG | ARG | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 11 | HIS |
Samples:
sample_1: D2O 5%; TMEM106B, [U-100% 13C; U-100% 15N], 0.2 ± 0.005 mM; potassium phosphate 5 mM
sample_conditions_1: ionic strength: 0.02 Not defined; pH: 6.5; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, CCPN, Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, peak picking, processing
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts