BMRB Entry 51090
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51090
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Title: Sequence-specific 1H, 15N, and 13C chemical shift assignment of the acidic domain of the human oncoprotein MDMX PubMed: 35359247
Deposition date: 2021-09-19 Original release date: 2022-04-13
Authors: Song, Qinyan; Rainey, Jan; Liu, Xiang-Qin
Citation: Song, Qinyan; Liu, Xiang-Qin; Rainey, Jan. "1H, 15N and 13C backbone resonance assignments of the acidic domain of the human MDMX protein" Biomol. NMR Assignments 16, 171-178 (2022).
Assembly members:
entity_1, polymer, 120 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-30a
Entity Sequences (FASTA):
entity_1: DETSRLDLGFEEWDVAGLPW
WFLGNLRSNYTPRSNGSTDL
QTNQDVGTAIVSDTTDDLWF
LNESVSEQLGVGIKVEAADT
EQTSEEVGKVSDKKVIEVGK
NDDLEDSKSLSDDTDVEVTS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 343 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 116 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acidic domain of human MDMX | 1 |
Entities:
Entity 1, acidic domain of human MDMX 120 residues - Formula weight is not available
Acidic domain of human MDMX containing residues that span 181-300 (120 residues).
| 1 | ASP | GLU | THR | SER | ARG | LEU | ASP | LEU | GLY | PHE | |
| 2 | GLU | GLU | TRP | ASP | VAL | ALA | GLY | LEU | PRO | TRP | |
| 3 | TRP | PHE | LEU | GLY | ASN | LEU | ARG | SER | ASN | TYR | |
| 4 | THR | PRO | ARG | SER | ASN | GLY | SER | THR | ASP | LEU | |
| 5 | GLN | THR | ASN | GLN | ASP | VAL | GLY | THR | ALA | ILE | |
| 6 | VAL | SER | ASP | THR | THR | ASP | ASP | LEU | TRP | PHE | |
| 7 | LEU | ASN | GLU | SER | VAL | SER | GLU | GLN | LEU | GLY | |
| 8 | VAL | GLY | ILE | LYS | VAL | GLU | ALA | ALA | ASP | THR | |
| 9 | GLU | GLN | THR | SER | GLU | GLU | VAL | GLY | LYS | VAL | |
| 10 | SER | ASP | LYS | LYS | VAL | ILE | GLU | VAL | GLY | LYS | |
| 11 | ASN | ASP | ASP | LEU | GLU | ASP | SER | LYS | SER | LEU | |
| 12 | SER | ASP | ASP | THR | ASP | VAL | GLU | VAL | THR | SER |
Samples:
sample_1: Acidic domain of human MDMX, [U-99% 13C; U-99% 15N], 380 uM; DSS 1 mM; sodium phosphate 20 mM; sodium azide 0.05 % v/v; sodium chloride 40 mM; D2O, [U-99% 2H], 10 % v/v; H2O 90 % v/v
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 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:
NMRbox - chemical shift assignment, data analysis, peak picking, processing
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts