BMRB Entry 26764
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26764
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for hTRF1 in urea PubMed: 27140645
Deposition date: 2016-03-21 Original release date: 2016-05-09
Authors: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis
Citation: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis. "Hsp70 biases the folding pathways of client proteins" Proc. Natl. Acad. Sci. U.S.A. 113, E2794-E2801 (2016).
Assembly members:
human_telomeric_protein_hTRF1, polymer, 53 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):
human_telomeric_protein_hTRF1: RKRQAWLWEEDKNLRSGVRK
YGEGNWSKILLHYKFNNRTS
VMLKDRWRTMKCL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 139 |
15N chemical shifts | 50 |
1H chemical shifts | 102 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hTRF1 | 1 |
Entities:
Entity 1, hTRF1 53 residues - Formula weight is not available
1 | ARG | LYS | ARG | GLN | ALA | TRP | LEU | TRP | GLU | GLU | ||||
2 | ASP | LYS | ASN | LEU | ARG | SER | GLY | VAL | ARG | LYS | ||||
3 | TYR | GLY | GLU | GLY | ASN | TRP | SER | LYS | ILE | LEU | ||||
4 | LEU | HIS | TYR | LYS | PHE | ASN | ASN | ARG | THR | SER | ||||
5 | VAL | MET | LEU | LYS | ASP | ARG | TRP | ARG | THR | MET | ||||
6 | LYS | CYS | LEU |
Samples:
sample_1: human telomeric protein hTRF1, [U-99% 13C; U-99% 15N], 0.6 mM; urea 3500 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts