BMRB Entry 27698
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27698
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Title: p15CCSS PubMed: 31479228
Deposition date: 2018-11-21 Original release date: 2019-09-24
Authors: Blanco, Francisco; Ibanez de Opakua, Alain; Gonzalez-magana, Amaia
Citation: Gonzalez-Magana, Amaia; de Opakua, Alain Ibanez; Merino, Nekane; Monteiro, Hugo; Diercks, Tammo; Murciano-Calles, Javier; Luque, Irene; Bernado, Pau; Cordeiro, Tiago; Biasio, Alfredo De; Blanco, Francisco. "Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1" ACS Chem. Biol. 14, 2315-2326 (2019).
Assembly members:
p15CSS, polymer, 110 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: pET11d
Entity Sequences (FASTA):
p15CSS: VRTKADSVPGTYRCVVAARA
PRCVLGSSTSATNSTSVSSR
KAENKYAGGNPVSVRPTPKW
QKGIGEFFRLSPKDSEKENQ
IPEEAGSSGLGKAKRKASPL
QPDHTNDEKE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 208 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | p15CSS | 1 |
Entities:
Entity 1, p15CSS 110 residues - Formula weight is not available
The protein lacks the initial methionine and thus it starts with Val2.
| 1 | VAL | ARG | THR | LYS | ALA | ASP | SER | VAL | PRO | GLY | |
| 2 | THR | TYR | ARG | CYS | VAL | VAL | ALA | ALA | ARG | ALA | |
| 3 | PRO | ARG | CYS | VAL | LEU | GLY | SER | SER | THR | SER | |
| 4 | ALA | THR | ASN | SER | THR | SER | VAL | SER | SER | ARG | |
| 5 | LYS | ALA | GLU | ASN | LYS | TYR | ALA | GLY | GLY | ASN | |
| 6 | PRO | VAL | SER | VAL | ARG | PRO | THR | PRO | LYS | TRP | |
| 7 | GLN | LYS | GLY | ILE | GLY | GLU | PHE | PHE | ARG | LEU | |
| 8 | SER | PRO | LYS | ASP | SER | GLU | LYS | GLU | ASN | GLN | |
| 9 | ILE | PRO | GLU | GLU | ALA | GLY | SER | SER | GLY | LEU | |
| 10 | GLY | LYS | ALA | LYS | ARG | LYS | ALA | SER | PRO | LEU | |
| 11 | GLN | PRO | ASP | HIS | THR | ASN | ASP | GLU | LYS | GLU |
Samples:
sample_1: p15CSS, [U-100% 13C; U-100% 15N], 50 uM; D2O, [U-100% 2H], 5%; DTT 1 mM; sodium azide 0.01%; DSS 50 uM; sodium phosphate 10 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts