BMRB Entry 51335
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51335
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Title: MDM2 AD in complex with p53 DBD 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
entity_2, polymer, 223 residues, Formula weight is not available
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: pET-32
Entity Sequences (FASTA):
entity_1: STGTPSNPDLDAGVSEHSGD
WLDQDSVSDQFSVEFEVESL
DSEDYSLSEEGQELSDEDDE
VYQVTVYQAGESDTDSFEED
PEISLA
entity_2: GSHMSSSVPSQKTYQGSYGF
RLGFLHSGTAKSVTCTYSPA
LNKMFCQLAKTCPVQLWVDS
TPPPGTRVRAMAIYKQSQHM
TEVVRRCPHHERCSDSDGLA
PPQHLIRVEGNLRVEYLDDR
NTFRHSVVVPYEPPEVGSDC
TTIHYNYMCNSSCMGGMNRR
PILTIITLEDSSGNLLGRNS
FEVRVCVCPGRDRRTEEENL
RKKGEPHHELPPGSTKRALP
NNT
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 159 |
15N chemical shifts | 76 |
1H chemical shifts | 76 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MDM2 Acid Domain | 1 |
2 | p53 DBD | 2 |
3 | Zinc | 3 |
Entities:
Entity 1, MDM2 Acid Domain 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 |
Entity 2, p53 DBD 223 residues - Formula weight is not available
1 | GLY | SER | HIS | MET | SER | SER | SER | VAL | PRO | SER | ||||
2 | GLN | LYS | THR | TYR | GLN | GLY | SER | TYR | GLY | PHE | ||||
3 | ARG | LEU | GLY | PHE | LEU | HIS | SER | GLY | THR | ALA | ||||
4 | LYS | SER | VAL | THR | CYS | THR | TYR | SER | PRO | ALA | ||||
5 | LEU | ASN | LYS | MET | PHE | CYS | GLN | LEU | ALA | LYS | ||||
6 | THR | CYS | PRO | VAL | GLN | LEU | TRP | VAL | ASP | SER | ||||
7 | THR | PRO | PRO | PRO | GLY | THR | ARG | VAL | ARG | ALA | ||||
8 | MET | ALA | ILE | TYR | LYS | GLN | SER | GLN | HIS | MET | ||||
9 | THR | GLU | VAL | VAL | ARG | ARG | CYS | PRO | HIS | HIS | ||||
10 | GLU | ARG | CYS | SER | ASP | SER | ASP | GLY | LEU | ALA | ||||
11 | PRO | PRO | GLN | HIS | LEU | ILE | ARG | VAL | GLU | GLY | ||||
12 | ASN | LEU | ARG | VAL | GLU | TYR | LEU | ASP | ASP | ARG | ||||
13 | ASN | THR | PHE | ARG | HIS | SER | VAL | VAL | VAL | PRO | ||||
14 | TYR | GLU | PRO | PRO | GLU | VAL | GLY | SER | ASP | CYS | ||||
15 | THR | THR | ILE | HIS | TYR | ASN | TYR | MET | CYS | ASN | ||||
16 | SER | SER | CYS | MET | GLY | GLY | MET | ASN | ARG | ARG | ||||
17 | PRO | ILE | LEU | THR | ILE | ILE | THR | LEU | GLU | ASP | ||||
18 | SER | SER | GLY | ASN | LEU | LEU | GLY | ARG | ASN | SER | ||||
19 | PHE | GLU | VAL | ARG | VAL | CYS | VAL | CYS | PRO | GLY | ||||
20 | ARG | ASP | ARG | ARG | THR | GLU | GLU | GLU | ASN | LEU | ||||
21 | ARG | LYS | LYS | GLY | GLU | PRO | HIS | HIS | GLU | LEU | ||||
22 | PRO | PRO | GLY | SER | THR | LYS | ARG | ALA | LEU | PRO | ||||
23 | ASN | ASN | THR |
Entity 3, Zinc - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: MDM2 AD, [U-95% 13C; U-95% 15N], 300 uM; p53DBD 330 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; TCEP 1 mM
sample_conditions_1: ionic strength: 82 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1D 1H | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment, data analysis, peak picking
NMRPipe - processing
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts