BMRB Entry 28091
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28091
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Title: Retinoblastoma-like protein 1 / p107 PubMed: 34661528
Deposition date: 2020-03-03 Original release date: 2021-09-20
Authors: Wang, Xinru; Page, Rebecca; Peti, Wolfgang
Citation: Fowle, Holly; Zhao, Ziran; Xu, Qifang; Wasserman, Jason; Wang, Xinru; Adeyemi, Mary; Feiser, Felicity; Kurimchak, Alison; Atar, Diba; McEwan, Brennan; Kettenbach, Arminja; Page, Rebecca; Peti, Wolfgang; Dunbrack, Roland; Grana, Xavier. "B55/PP2A substrate recruitment as defined by the retinoblastoma-related protein p107" eLife 10, e63181-e63181 (2021).
Assembly members:
p107, polymer, 78 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: pTHMT
Entity Sequences (FASTA):
p107: GHMPMSPLMHPRVKEVRTDS
GSLRRDMQPLSPISVHERYS
SPTAGSAKRRLFGEDPPKEM
LMDKIITEGTKLKIAPSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 147 |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 65 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p107 | 1 |
Entities:
Entity 1, p107 78 residues - Formula weight is not available
Residue 1-2 represent a cloning artifact. Residue 3-78 represent human p107 residue 612-687.
| 1 | GLY | HIS | MET | PRO | MET | SER | PRO | LEU | MET | HIS | ||||
| 2 | PRO | ARG | VAL | LYS | GLU | VAL | ARG | THR | ASP | SER | ||||
| 3 | GLY | SER | LEU | ARG | ARG | ASP | MET | GLN | PRO | LEU | ||||
| 4 | SER | PRO | ILE | SER | VAL | HIS | GLU | ARG | TYR | SER | ||||
| 5 | SER | PRO | THR | ALA | GLY | SER | ALA | LYS | ARG | ARG | ||||
| 6 | LEU | PHE | GLY | GLU | ASP | PRO | PRO | LYS | GLU | MET | ||||
| 7 | LEU | MET | ASP | LYS | ILE | ILE | THR | GLU | GLY | THR | ||||
| 8 | LYS | LEU | LYS | ILE | ALA | PRO | SER | SER |
Samples:
sample_1: p107, [U-99% 13C; U-99% 15N], 0.7 mM; sodium chloride 50 mM; TCEP 0.5 mM; sodium phosphate 20 mM; D2O, [U-2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 70 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
cara v1.9.2, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Neo 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts