BMRB Entry 51353
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51353
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Title: Backbone NMR assignment of the human TRPV1 ion channel N-terminal intrinsically disordered region PubMed: 35666427
Deposition date: 2022-03-09 Original release date: 2022-06-06
Authors: Goretzki, Benedikt; Wiedemann, Christoph; 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, 99 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: KKWSSTDLGAAADPLQKDTC
PDPLDGDPNSRPPPAKPQLS
TAKSRTRLFGKGDSEEAFPV
DCPHEEGELDSCPTITVSPV
ITIQRPGDGPTGARLLSQD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 280 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 319 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hsTRPV1-IDR | 1 |
Entities:
Entity 1, hsTRPV1-IDR 99 residues - Formula weight is not available
| 1 | LYS | LYS | TRP | SER | SER | THR | ASP | LEU | GLY | ALA | ||||
| 2 | ALA | ALA | ASP | PRO | LEU | GLN | LYS | ASP | THR | CYS | ||||
| 3 | PRO | ASP | PRO | LEU | ASP | GLY | ASP | PRO | ASN | SER | ||||
| 4 | ARG | PRO | PRO | PRO | ALA | LYS | PRO | GLN | LEU | SER | ||||
| 5 | THR | ALA | LYS | SER | ARG | THR | ARG | LEU | PHE | GLY | ||||
| 6 | LYS | GLY | ASP | SER | GLU | GLU | ALA | PHE | PRO | VAL | ||||
| 7 | ASP | CYS | PRO | HIS | GLU | GLU | GLY | GLU | LEU | ASP | ||||
| 8 | SER | CYS | PRO | THR | ILE | THR | VAL | SER | PRO | VAL | ||||
| 9 | ILE | THR | ILE | GLN | ARG | PRO | GLY | ASP | GLY | PRO | ||||
| 10 | THR | GLY | ALA | ARG | LEU | LEU | SER | GLN | ASP |
Samples:
sample_1: hsTRPV1-IDR, [U-99% 13C; U-99% 15N], 300 uM; D2O, [U-99% 2H], 10%; DSS 0.1 mM; H2O 90%; TRIS 10 mM; sodium chloride 100 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.11 M; pH: 7; 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
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