BMRB Entry 51625
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51625
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Title: Backbone 1H, 13C, and 15N chemical shift assignments for the N-terminal fragment of human YY1
Deposition date: 2022-09-14 Original release date: 2022-12-29
Authors: Luchinat, Enrico; Banci, Lucia; Gorecki, Andrzej
Citation: Figiel, Malgorzata; Szubert, Filip; Luchinat, Enrico; Bonarek, Piotr; Baranowska, Anna; Wajda-Nikiel, Katarzyna; Wilamowski, Mateusz; Milek, Piotr; Dziedzicka-Wasylewska, Marta; Banci, Lucia; Gorecki, Andrzej. "Zinc controls operator affinity of human transcription factor YY1 by mediating dimerization via its N-terminal region" Biochim. Biophys. Acta Gene Regul. Mech. 1866, 194905-194905 (2023).
Assembly members:
entity_1, polymer, 295 residues, 31189 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: pET21a
Entity Sequences (FASTA):
entity_1: MASGDTLYIATDGSEMPAEI
VELHEIEVETIPVETIETTV
VGEEEEEDDDDEDGGGGDHG
GGGGHGHAGHHHHHHHHHHH
PPMIALQPLVTDDPTQVHHH
QEVILVQTREEVVGGDDSDG
LRAEDGFEDQILIPVPAPAG
GDDDYIEQTLVTVAAAGKSG
GGGSSSSGGGRVKKGGGKKS
GKKSYLSGGAGAAGGGGADP
GNKKWEQKQVQIKTLEGEFS
VTMWSSDEKKDIDHETVVEE
QIIGENSPPDYSEYMTGKKL
PPGGIPGIDLSDPKQLAEFA
RMKPRKIKEDDAPRT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 723 |
| 15N chemical shifts | 268 |
| 1H chemical shifts | 240 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | monomeric polypeptide | 1 |
Entities:
Entity 1, monomeric polypeptide 295 residues - 31189 Da.
Residues 1-295 of the human protein Ying Yang 1 (YY1), corresponding to the N-terminal fragment.
| 1 | MET | ALA | SER | GLY | ASP | THR | LEU | TYR | ILE | ALA | ||||
| 2 | THR | ASP | GLY | SER | GLU | MET | PRO | ALA | GLU | ILE | ||||
| 3 | VAL | GLU | LEU | HIS | GLU | ILE | GLU | VAL | GLU | THR | ||||
| 4 | ILE | PRO | VAL | GLU | THR | ILE | GLU | THR | THR | VAL | ||||
| 5 | VAL | GLY | GLU | GLU | GLU | GLU | GLU | ASP | ASP | ASP | ||||
| 6 | ASP | GLU | ASP | GLY | GLY | GLY | GLY | ASP | HIS | GLY | ||||
| 7 | GLY | GLY | GLY | GLY | HIS | GLY | HIS | ALA | GLY | HIS | ||||
| 8 | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 9 | PRO | PRO | MET | ILE | ALA | LEU | GLN | PRO | LEU | VAL | ||||
| 10 | THR | ASP | ASP | PRO | THR | GLN | VAL | HIS | HIS | HIS | ||||
| 11 | GLN | GLU | VAL | ILE | LEU | VAL | GLN | THR | ARG | GLU | ||||
| 12 | GLU | VAL | VAL | GLY | GLY | ASP | ASP | SER | ASP | GLY | ||||
| 13 | LEU | ARG | ALA | GLU | ASP | GLY | PHE | GLU | ASP | GLN | ||||
| 14 | ILE | LEU | ILE | PRO | VAL | PRO | ALA | PRO | ALA | GLY | ||||
| 15 | GLY | ASP | ASP | ASP | TYR | ILE | GLU | GLN | THR | LEU | ||||
| 16 | VAL | THR | VAL | ALA | ALA | ALA | GLY | LYS | SER | GLY | ||||
| 17 | GLY | GLY | GLY | SER | SER | SER | SER | GLY | GLY | GLY | ||||
| 18 | ARG | VAL | LYS | LYS | GLY | GLY | GLY | LYS | LYS | SER | ||||
| 19 | GLY | LYS | LYS | SER | TYR | LEU | SER | GLY | GLY | ALA | ||||
| 20 | GLY | ALA | ALA | GLY | GLY | GLY | GLY | ALA | ASP | PRO | ||||
| 21 | GLY | ASN | LYS | LYS | TRP | GLU | GLN | LYS | GLN | VAL | ||||
| 22 | GLN | ILE | LYS | THR | LEU | GLU | GLY | GLU | PHE | SER | ||||
| 23 | VAL | THR | MET | TRP | SER | SER | ASP | GLU | LYS | LYS | ||||
| 24 | ASP | ILE | ASP | HIS | GLU | THR | VAL | VAL | GLU | GLU | ||||
| 25 | GLN | ILE | ILE | GLY | GLU | ASN | SER | PRO | PRO | ASP | ||||
| 26 | TYR | SER | GLU | TYR | MET | THR | GLY | LYS | LYS | LEU | ||||
| 27 | PRO | PRO | GLY | GLY | ILE | PRO | GLY | ILE | ASP | LEU | ||||
| 28 | SER | ASP | PRO | LYS | GLN | LEU | ALA | GLU | PHE | ALA | ||||
| 29 | ARG | MET | LYS | PRO | ARG | LYS | ILE | LYS | GLU | ASP | ||||
| 30 | ASP | ALA | PRO | ARG | THR |
Samples:
sample_1: YY1-NTF, [U-98% 13C; U-98% 15N], 210 uM; TRIS 50 mM; sodium chloride 100 mM
sample_conditions_1: pH: 7.2; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C-detected CON | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-detected CBCACON | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-detected CBCANCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-detected COCON | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0 - collection
NMRPipe - processing
CARA v1.9.1.7 - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE NEO 900 MHz
- Bruker AVANCE NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts