BMRB Entry 51334
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51334
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Title: MDM2AD PubMed: 35780910
Deposition date: 2022-02-20 Original release date: 2022-10-11
Authors: Song, Qinyan; Rainey, Jan; Liu, Paul
Citation: Song, Qinyan; Liu, Xiang-Qin; Rainey, Jan. "The MDMX acidic domain competes with the p53 transactivation domain for MDM2 N-terminal domain binding" Biochim. Biophys. Acta Mol. Cell Res. 1869, 119319-119319 (2022).
Assembly members:
entity_1, polymer, 86 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: pET-32
Entity Sequences (FASTA):
entity_1: STGTPSNPDLDAGVSEHSGD
WLDQDSVSDQFSVEFEVESL
DSEDYSLSEEGQELSDEDDE
VYQVTVYQAGESDTDSFEED
PEISLA
- assigned_chemical_shifts
- heteronucl_NOEs
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 81 |
| heteronuclear NOE values | 83 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MDM2 | 1 |
Entities:
Entity 1, MDM2 86 residues - Formula weight is not available
| 1 | SER | THR | GLY | THR | PRO | SER | ASN | PRO | ASP | LEU | ||||
| 2 | ASP | ALA | GLY | VAL | SER | GLU | HIS | SER | GLY | ASP | ||||
| 3 | TRP | LEU | ASP | GLN | ASP | SER | VAL | SER | ASP | GLN | ||||
| 4 | PHE | SER | VAL | GLU | PHE | GLU | VAL | GLU | SER | LEU | ||||
| 5 | ASP | SER | GLU | ASP | TYR | SER | LEU | SER | GLU | GLU | ||||
| 6 | GLY | GLN | GLU | LEU | SER | ASP | GLU | ASP | ASP | GLU | ||||
| 7 | VAL | TYR | GLN | VAL | THR | VAL | TYR | GLN | ALA | GLY | ||||
| 8 | GLU | SER | ASP | THR | ASP | SER | PHE | GLU | GLU | ASP | ||||
| 9 | PRO | GLU | ILE | SER | LEU | ALA |
Samples:
sample_1: MDM2AD, [U-95% 13C; U-95% 15N], 800 uM; D2O, [U-99% 2H], 10%; H2O 90%; DSS 1 mM; sodium azide 0.05 % w/v; sodium chloride 40 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 82 mM; pH: 7.0; pressure: 1 atm; temperature: 293K K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment, data analysis, peak picking
NMRPipe - processing
VNMRJ v4.2A - collection
NMR spectrometers:
- Varian INOVA 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts