BMRB Entry 51797
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51797
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone assignment of the extended C-terminal domain of Tetrahymena telomerase protein p65 PubMed: 37330293
Deposition date: 2023-01-23 Original release date: 2023-06-19
Authors: Yang, Yuan; Eichhorn, Catherine; Jiang, Yi Xiao; Wang, Yaqiang; Feigon, Juli
Citation: Wang, Yaqiang; He, Yao; Wang, Yanjiao; Yang, Yuan; Singh, Mahavir; Eichhorn, Catherine; Cheng, Xinyi; Jiang, Yi Xiao; Zhou, Z. Hong; Feigon, Juli. "Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR" J. Mol. Biol. 435, 168044-168044 (2023).
Assembly members:
entity_1, polymer, 169 residues, Formula weight is not available
Natural source: Common Name: Tetrahymena Thermophila Taxonomy ID: 5911 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tetrahymena Thermophila
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETDUET
Entity Sequences (FASTA):
entity_1: GQKNKNMNQSRKASDEFVSI
DVEIKQNCLIKIINIPQGTL
KAEVVLAVRHLGYEFYCDYI
DENSNQINSNLIQQDQHPQL
NDLLKEGQAMIRFQNSDEQR
LAIQKLLNHNNNKLQIEIRG
QICDVISTIPEDEEKNYWNY
IKFKKNEFRKFFFMKKQQKK
QNITQNYNK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 212 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p65-aL-xRRM2 | 1 |
Entities:
Entity 1, p65-aL-xRRM2 169 residues - Formula weight is not available
The first amino acid, 352 Glycine, is a non-native residue resulted from TEV protease cleavage site. There is a loop truncation between amino acids 420 and 443.
| 1 | GLY | GLN | LYS | ASN | LYS | ASN | MET | ASN | GLN | SER | ||||
| 2 | ARG | LYS | ALA | SER | ASP | GLU | PHE | VAL | SER | ILE | ||||
| 3 | ASP | VAL | GLU | ILE | LYS | GLN | ASN | CYS | LEU | ILE | ||||
| 4 | LYS | ILE | ILE | ASN | ILE | PRO | GLN | GLY | THR | LEU | ||||
| 5 | LYS | ALA | GLU | VAL | VAL | LEU | ALA | VAL | ARG | HIS | ||||
| 6 | LEU | GLY | TYR | GLU | PHE | TYR | CYS | ASP | TYR | ILE | ||||
| 7 | ASP | GLU | ASN | SER | ASN | GLN | ILE | ASN | SER | ASN | ||||
| 8 | LEU | ILE | GLN | GLN | ASP | GLN | HIS | PRO | GLN | LEU | ||||
| 9 | ASN | ASP | LEU | LEU | LYS | GLU | GLY | GLN | ALA | MET | ||||
| 10 | ILE | ARG | PHE | GLN | ASN | SER | ASP | GLU | GLN | ARG | ||||
| 11 | LEU | ALA | ILE | GLN | LYS | LEU | LEU | ASN | HIS | ASN | ||||
| 12 | ASN | ASN | LYS | LEU | GLN | ILE | GLU | ILE | ARG | GLY | ||||
| 13 | GLN | ILE | CYS | ASP | VAL | ILE | SER | THR | ILE | PRO | ||||
| 14 | GLU | ASP | GLU | GLU | LYS | ASN | TYR | TRP | ASN | TYR | ||||
| 15 | ILE | LYS | PHE | LYS | LYS | ASN | GLU | PHE | ARG | LYS | ||||
| 16 | PHE | PHE | PHE | MET | LYS | LYS | GLN | GLN | LYS | LYS | ||||
| 17 | GLN | ASN | ILE | THR | GLN | ASN | TYR | ASN | LYS |
Samples:
sample_1: extended C-terminal domain of Tetrahymena telomerase protein p65, [U-98% 13C; U-98% 15N], 0.8 mM; H2O 95%; D2O, [U-100% 2H], 5%; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 80 mM; pH: 6.1; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN vv3.5pl7 - collection
NMRPipe - processing
NMRFAM-SPARKY vv1.470 - data analysis
NMR spectrometers:
- Bruker AVANCE III HD 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts