BMRB: 7255

1H chemical shift assignments for p53 tetramerization domain mutant Y327S T329E Q331G

Authors

Carbajo, R.J., Mora, P., Sanchez del Pino, M.M., Perez Paya, E., Pineda-Lucena, A.

Assembly

p53 tetramerization domain

Entity

1. p53 tetramerization domain (polymer, Thiol state: not present), 31 monomers, 3642.017 × 4 Da Detail

ESFELGIRGR ERFEMFRELN EALELKDAQA G

Total weight

14568.068 Da

Max. entity weight

3642.017 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 96.4 %, Completeness (bb): 100.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	96.4 % (190 of 197)	96.4 % (190 of 197)
Backbone	100.0 % (65 of 65)	100.0 % (65 of 65)
Sidechain	94.7 % (125 of 132)	94.7 % (125 of 132)
Aromatic	100.0 % (15 of 15)	100.0 % (15 of 15)
Methyl	100.0 % (13 of 13)	100.0 % (13 of 13)

1. p53TD

ESFELGIRGR ERFEMFRELN EALELKDAQA G

Show sample condition

Sample

Temperature 300 (±0.1) K, pH 7.2 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	p53TD mutant Y327S T329E Q331G		protein	0.5 mM
2	phosphate buffer		buffer	40 mM

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Release date

2008-02-04

Citation

Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53--a structural and combinatorial approach
Mora, P., Carbajo, R.J., Pineda-Lucena, A., Sanchez del Pino, M.M., Perez Paya, E.
Proteins (2008), 71, 1670-1685, PubMed 18076077 , DOI 10.1002/prot.21854 , Abstract

Related entities 1. p53 tetramerization domain, : 1 : 36 : 63 entities Detail

Interaction partners 1. p53 tetramerization domain, : 1 interactors Detail

Experiments performed 2 experiments Detail

Chemical shift validation 3 contents Detail