BMRB Entry 51355
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51355
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Title: Backbone and side-chain NMR assignment of the human TRPV3 ion channel N-terminal intrinsically disordered region PubMed: 35666427
Deposition date: 2022-03-09 Original release date: 2022-06-06
Authors: Wiedemann, Christoph; Goretzki, Benedikt; Merz, Zoe; Schmitt, Pauline; Tebbe, Frederike; Hellmich, Ute
Citation: Wiedemann, Christoph; Goretzki, Benedikt; Merz, Zoe; Tebbe, Frederike; Schmitt, Pauline; Hellmich, Ute. "Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels" Biomol. NMR Assignments 16, 289-296 (2022).
Assembly members:
entity_1, polymer, 118 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: pET11a
Entity Sequences (FASTA):
entity_1: KAHPKEMVPLMGKRVAAPSG
NPAILPEKRPAEITPTKKSA
HFFLEIEGFEPNPTVAKTSP
PVFSKPMDSNIRQCISGNCD
DMDSPQSPQDDVTETPSNPN
SPSAQLAKEEQRRKKRRL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 458 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 620 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hsTRPV3-IDR | 1 |
Entities:
Entity 1, hsTRPV3-IDR 118 residues - Formula weight is not available
| 1 | LYS | ALA | HIS | PRO | LYS | GLU | MET | VAL | PRO | LEU | ||||
| 2 | MET | GLY | LYS | ARG | VAL | ALA | ALA | PRO | SER | GLY | ||||
| 3 | ASN | PRO | ALA | ILE | LEU | PRO | GLU | LYS | ARG | PRO | ||||
| 4 | ALA | GLU | ILE | THR | PRO | THR | LYS | LYS | SER | ALA | ||||
| 5 | HIS | PHE | PHE | LEU | GLU | ILE | GLU | GLY | PHE | GLU | ||||
| 6 | PRO | ASN | PRO | THR | VAL | ALA | LYS | THR | SER | PRO | ||||
| 7 | PRO | VAL | PHE | SER | LYS | PRO | MET | ASP | SER | ASN | ||||
| 8 | ILE | ARG | GLN | CYS | ILE | SER | GLY | ASN | CYS | ASP | ||||
| 9 | ASP | MET | ASP | SER | PRO | GLN | SER | PRO | GLN | ASP | ||||
| 10 | ASP | VAL | THR | GLU | THR | PRO | SER | ASN | PRO | ASN | ||||
| 11 | SER | PRO | SER | ALA | GLN | LEU | ALA | LYS | GLU | GLU | ||||
| 12 | GLN | ARG | ARG | LYS | LYS | ARG | ARG | LEU |
Samples:
sample_1: hsTRPV3-IDR, [U-99% 13C; U-99% 15N], 300 uM; D2O, [U-99% 2H], 10%; DSS 0.1 mM; H2O 90%; sodium phosphate 10 mM; sodium chloride 300 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.31 M; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection, processing
CcpNMR - data analysis
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts