BMRB Entry 25377
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25377
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Title: MDMX-P53
Deposition date: 2014-12-03 Original release date: 2016-01-25
Authors: Grace, Christy
Citation: Grace, Christy; Kriwacki, Richard; Ban, David. "Monitoring ligand induced protein ordering in drug discovery" J. Mol. Biol. ., .-..
Assembly members:
entity_1, polymer, 89 residues, 10160.976 Da.
entity_2, polymer, 15 residues, 1807.993 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
Entity Sequences (FASTA):
entity_1: QINQVRPKLPLLKILHAAGA
QGEMFTVKEVMHYLGQYIMV
KQLYDQQEQHMVYCGGDLLG
ELLGRQSFSVKDPSPLYDML
RKNLVTLAT
entity_2: SQETFSDLWKLLPEN
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 585 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 89 residues - 10160.976 Da.
Residue 1 corresponds to 23 in MDMX
| 1 | GLN | ILE | ASN | GLN | VAL | ARG | PRO | LYS | LEU | PRO | ||||
| 2 | LEU | LEU | LYS | ILE | LEU | HIS | ALA | ALA | GLY | ALA | ||||
| 3 | GLN | GLY | GLU | MET | PHE | THR | VAL | LYS | GLU | VAL | ||||
| 4 | MET | HIS | TYR | LEU | GLY | GLN | TYR | ILE | MET | VAL | ||||
| 5 | LYS | GLN | LEU | TYR | ASP | GLN | GLN | GLU | GLN | HIS | ||||
| 6 | MET | VAL | TYR | CYS | GLY | GLY | ASP | LEU | LEU | GLY | ||||
| 7 | GLU | LEU | LEU | GLY | ARG | GLN | SER | PHE | SER | VAL | ||||
| 8 | LYS | ASP | PRO | SER | PRO | LEU | TYR | ASP | MET | LEU | ||||
| 9 | ARG | LYS | ASN | LEU | VAL | THR | LEU | ALA | THR |
Entity 2, entity_2 15 residues - 1807.993 Da.
Peptide is TAD of p53 from 15 to 29
| 1 | SER | GLN | GLU | THR | PHE | SER | ASP | LEU | TRP | LYS | ||||
| 2 | LEU | LEU | PRO | GLU | ASN |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 1.0 mM; entity_2 1.2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G??ntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz