BMRB: 7251

1H chemical shift assignments for wild type p53 tetramerization domain

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, 3761.180 × 4 Da Detail

EYFTLQIRGR ERFEMFRELN EALELKDAQA G

Total weight

15044.72 Da

Max. entity weight

3761.18 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

CNS

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 97.5 %, Completeness (bb): 100.0 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H
All	97.5 % (199 of 204)	97.5 % (199 of 204)
Backbone	100.0 % (64 of 64)	100.0 % (64 of 64)
Sidechain	96.4 % (135 of 140)	96.4 % (135 of 140)
Aromatic	100.0 % (19 of 19)	100.0 % (19 of 19)
Methyl	100.0 % (14 of 14)	100.0 % (14 of 14)

1. p53TD

EYFTLQIRGR ERFEMFRELN EALELKDAQA G

Show sample condition

Sample

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

#	Name	Isotope labeling	Type	Concentration
1	p53TD wild type		protein	0.5 mM
2	phosphate buffer		buffer	40 mM

Hide sample codition

Protein Blocks Logo

Calculated from 30 models in PDB: 2J0Z, Strand ID: A, B, C, D Detail

---

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

Entries sharing articles BMRB: 4 entries Detail

Related entities 1. p53 tetramerization domain, : 1 : 23 : 1 : 12 : 62 entities Detail

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

Experiments performed 2 experiments Detail