BMRB Entry 17760
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17760
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Title: backbone resonance assignments of p53 N-terminal transactivation domain (1-93) PubMed: 19755502
Deposition date: 2011-07-05 Original release date: 2011-07-18
Authors: Wong, Tuck; Rutherford, Trevor; Freund, Stefan; Fersht, Alan
Citation: Wong, Tuck; Rajagopalan, Sridharan; Freund, Stefan; Rutherford, Trevor; Andreeva, Antonina; Townsley, Fiona; Petrovich, Miriana; Fersht, Alan. "Biophysical characterizations of human mitochondrial travscription factor A and its binding to tumor suppressor p53" Nucleic Acids Res. 37, 6765-6783 (2009).
Assembly members:
p53_TAD, polymer, 93 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
Entity Sequences (FASTA):
p53_TAD: MEEPQSDPSVEPPLSQETFS
DLWKLLPENNVLSPLPSQAM
DDLMLSPDDIEQWFTEDPGP
DEAPRMPEAAPPVAPAPAAP
TPAAPAPAPSWPL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 251 |
15N chemical shifts | 67 |
1H chemical shifts | 67 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | p53_TAD | 1 |
Entities:
Entity 1, p53_TAD 93 residues - Formula weight is not available
1 | MET | GLU | GLU | PRO | GLN | SER | ASP | PRO | SER | VAL | ||||
2 | GLU | PRO | PRO | LEU | SER | GLN | GLU | THR | PHE | SER | ||||
3 | ASP | LEU | TRP | LYS | LEU | LEU | PRO | GLU | ASN | ASN | ||||
4 | VAL | LEU | SER | PRO | LEU | PRO | SER | GLN | ALA | MET | ||||
5 | ASP | ASP | LEU | MET | LEU | SER | PRO | ASP | ASP | ILE | ||||
6 | GLU | GLN | TRP | PHE | THR | GLU | ASP | PRO | GLY | PRO | ||||
7 | ASP | GLU | ALA | PRO | ARG | MET | PRO | GLU | ALA | ALA | ||||
8 | PRO | PRO | VAL | ALA | PRO | ALA | PRO | ALA | ALA | PRO | ||||
9 | THR | PRO | ALA | ALA | PRO | ALA | PRO | ALA | PRO | SER | ||||
10 | TRP | PRO | LEU |
Samples:
sample_1: p53_TAD, [U-100% 13C; U-100% 15N], 200 uM; TRIS 25 mM; sodium chloride 150 mM; DTT 1 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 175 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.1, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
PDB | |
DBJ | BAC16799 BAG35463 BAG64357 BAI45431 BAJ52715 |
EMBL | CAA26306 CAA38095 CAA42625 CAA42626 CAA42627 |
GB | AAA59987 AAA59988 AAA59989 AAA61211 AAA61212 |
REF | NP_000537 NP_001119584 NP_001119585 NP_001119586 NP_001119590 |
SP | P04637 Q9TTA1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts