BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 7252

Title: 1H chemical shift assignments for p53 tetramerization domain mutant T329F Q331K   PubMed: 18076077

Authors: Carbajo, Rodrigo; Mora, Puig; Sanchez del Pino, Manuel; Perez Paya, Enrique; Pineda-Lucena, Antonio

Citation: Mora, Puig; Carbajo, Rodrigo; Pineda-Lucena, Antonio; Sanchez del Pino, Manuel; Perez Paya, Enrique. "Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach"  Proteins 71, 1670-1685 (2008).

Assembly members:
p53TD, polymer, 31 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: chemical synthesis

Entity Sequences (FASTA):
p53TD: EYFFLKIRGRERFEMFRELN EALELKDAQAG

Data sets:
Data typeCount
1H chemical shifts231

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21
3subunit 31
4subunit 41

Entities:

Entity 1, subunit 1 31 residues - Formula weight is not available

residues 326-356 p53 tetramerization domain mutant T329F Q331K

1   GLUTYRPHEPHELEULYSILEARGGLYARG
2   GLUARGPHEGLUMETPHEARGGLULEUASN
3   GLUALALEUGLULEULYSASPALAGLNALA
4   GLY

Samples:

sample_1: p53TD 0.5 mM; phosphate buffer 40 mM

conditions_1: pH: 7.2; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
1H,1H NOESYsample_1not availableconditions_1
1H,1H TOCSYsample_1not availableconditions_1

Software:

TOPSPIN v1.3, Bruker - Processing

SPARKY v3.110 - Assignment

CNS v1.1, Bruker - Structure calculations

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAP30003 EAW90141