BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17760

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   Vector: NA

Entity Sequences (FASTA):
p53_TAD: MEEPQSDPSVEPPLSQETFS DLWKLLPENNVLSPLPSQAM DDLMLSPDDIEQWFTEDPGP DEAPRMPEAAPPVAPAPAAP TPAAPAPAPSWPL

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts67
1H chemical shifts67

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1p53_TAD1

Entities:

Entity 1, p53_TAD 93 residues - Formula weight is not available

1   METGLUGLUPROGLNSERASPPROSERVAL
2   GLUPROPROLEUSERGLNGLUTHRPHESER
3   ASPLEUTRPLYSLEULEUPROGLUASNASN
4   VALLEUSERPROLEUPROSERGLNALAMET
5   ASPASPLEUMETLEUSERPROASPASPILE
6   GLUGLNTRPPHETHRGLUASPPROGLYPRO
7   ASPGLUALAPROARGMETPROGLUALAALA
8   PROPROVALALAPROALAPROALAALAPRO
9   THRPROALAALAPROALAPROALAPROSER
10   TRPPROLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_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
AlphaFold P04637

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts