BMRB Entry 7252
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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/BMR7252
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Title: 1H chemical shift assignments for p53 tetramerization domain mutant T329F Q331K PubMed: 18076077
Deposition date: 2006-08-08 Original release date: 2008-02-05
Authors: Carbajo, Rodrigo; Mora, Puig; Sanchez del Pino, Manuel; Perez Paya, Enrique; Pineda-Lucena, Antonio
Citation: Mora, Puig; Carbajo, Rodrigo; Pineda-Lucena, Antonio; Sanchez del Pino, Manuel; Perez Paya, Enrique. "Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach" Proteins 71, 1670-1685 (2008).
Assembly members:
p53TD, polymer, 31 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: chemical synthesis
Entity Sequences (FASTA):
p53TD: EYFFLKIRGRERFEMFRELN
EALELKDAQAG
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 231 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 1 |
| 3 | subunit 3 | 1 |
| 4 | subunit 4 | 1 |
Entities:
Entity 1, subunit 1 31 residues - Formula weight is not available
residues 326-356 p53 tetramerization domain mutant T329F Q331K
| 1 | GLU | TYR | PHE | PHE | LEU | LYS | ILE | ARG | GLY | ARG | ||||
| 2 | GLU | ARG | PHE | GLU | MET | PHE | ARG | GLU | LEU | ASN | ||||
| 3 | GLU | ALA | LEU | GLU | LEU | LYS | ASP | ALA | GLN | ALA | ||||
| 4 | GLY |
Samples:
sample_1: p53TD 0.5 mM; phosphate buffer 40 mM
conditions_1: pH: 7.2; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H,1H NOESY | sample_1 | not available | conditions_1 |
| 1H,1H TOCSY | sample_1 | not available | conditions_1 |
Software:
TOPSPIN v1.3, Bruker - Processing
SPARKY v3.110 - Assignment
CNS v1.1, Bruker - Structure calculations
NMR spectrometers:
- Bruker Avance 600 MHz