Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6522
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Galea, Charles; Bowman, Prentice; Kriwacki, Richard. "Disruption of an intermonomer salt bridge in the p53 tetramerization domain
results in an increased propensity to form amyloid fibrils." Protein Sci. 14, 2993-3003 (2005).
PubMed: 16260757
Assembly members:
Mutant_p53_tetramerization_domain_polypeptide, polymer, 54 residues, 6131.8 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Mutant_p53_tetramerization_domain_polypeptide: GSHMNTSSSPQPKKKPLDGE
YFTLQIRGRERFEMFRELNE
ALELKDAQAGKEPG
Data type | Count |
13C chemical shifts | 105 |
15N chemical shifts | 95 |
1H chemical shifts | 95 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | subunit A | 1 |
2 | subunit B | 1 |
3 | subunit C | 1 |
4 | subunit D | 1 |
Entity 1, subunit A 54 residues - 6131.8 Da.
Residues 11 to 60 correspond to residues 310 to 360 of p53. Arg337 has been substituted by His.
1 | GLY | SER | HIS | MET | ASN | THR | SER | SER | SER | PRO | ||||
2 | GLN | PRO | LYS | LYS | LYS | PRO | LEU | ASP | GLY | GLU | ||||
3 | TYR | PHE | THR | LEU | GLN | ILE | ARG | GLY | ARG | GLU | ||||
4 | ARG | PHE | GLU | MET | PHE | ARG | GLU | LEU | ASN | GLU | ||||
5 | ALA | LEU | GLU | LEU | LYS | ASP | ALA | GLN | ALA | GLY | ||||
6 | LYS | GLU | PRO | GLY |
sample_1: p53tet-R337H, [U-15N], 4.0 mM; Na2HPO4 10.0 mM; NaCl 50.0 mM; NaN3 0.02%
sample_2: p53tet-R337H, U-13C; U-15N, 4.0 mM; Na2HPO4 10.0 mM; NaCl 50.0 mM; NaN3 0.02%
conditions_1: pH: 6.0; temperature: 293.0 K
conditions_2: pH: 4.0; temperature: 293.0 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H15N_HSQC | not available | not available | not available |
HNCA | not available | not available | not available |
HN(CO)CA | not available | not available | not available |
HNCACB | not available | not available | not available |
CBCA(CO)NH | not available | not available | not available |
1H15N_NOESY | not available | not available | not available |
Felix, Accelrys - Chemical Shift Assignments
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks