BMRB Entry 52308
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52308
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Citation: Sahoo, Bikash; Kocman, Vojc; Clark, Nathan; Myers, Nikhil; Deng, Xiexiong; Wong, Ee; Yang, Harry; Kotar, Anita; Guzman, Bryan; Dominguez, Daniel; Plavec, Janez; Bardwell, James. "Effects of protein G-quadruplex interactions on phase transitions and protein aggregation." bioRxiv ., .-. (2023).
PubMed: 37790366
Assembly members:
entity_1, polymer, 76 residues, 8498 Da.
entity_ZN, non-polymer, 65.409 Da.
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: pET28
Entity Sequences (FASTA):
entity_1: MARGQQKIQSQQKNAKKQAG
QKKKQGHDQKAAAKAALIYT
CTVCRTQMPDPKTFKQHFES
KHPKTPLPPELADVQA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 178 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 62 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Human ZNF706 | 1 |
| 2 | ZINC ION | 2 |
Entities:
Entity 1, Human ZNF706 76 residues - 8498 Da.
| 1 | MET | ALA | ARG | GLY | GLN | GLN | LYS | ILE | GLN | SER | ||||
| 2 | GLN | GLN | LYS | ASN | ALA | LYS | LYS | GLN | ALA | GLY | ||||
| 3 | GLN | LYS | LYS | LYS | GLN | GLY | HIS | ASP | GLN | LYS | ||||
| 4 | ALA | ALA | ALA | LYS | ALA | ALA | LEU | ILE | TYR | THR | ||||
| 5 | CYS | THR | VAL | CYS | ARG | THR | GLN | MET | PRO | ASP | ||||
| 6 | PRO | LYS | THR | PHE | LYS | GLN | HIS | PHE | GLU | SER | ||||
| 7 | LYS | HIS | PRO | LYS | THR | PRO | LEU | PRO | PRO | GLU | ||||
| 8 | LEU | ALA | ASP | VAL | GLN | ALA |
Entity 2, ZINC ION - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: Human ZNF706, [U-15N], 750 uM; Human ZNF706, [U-13C], 750 uM; sodium phosphate 20 mM; NaCl 20 mM; D2O, [U-2H], 7.5%
sample_conditions_1: ionic strength: 0.02 M; pH: 7.4; pressure: 1 atm; temperature: 277.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, NMRFAM-SPARKY v4.1.4; 1.470 - chemical shift assignment, collection, data analysis
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks