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 6522

Title: Characterization of an amyloid fibril intermediate   PubMed: 16260757

Deposition date: 2005-02-23 Original release date: 2007-01-29

Authors: Galea, Charles; Bowman, Prentice; Kriwacki, Richard

Citation: Galea, Charles; Bowman, Prentice; Kriwacki, Richard. "Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils."  Protein Sci. 14, 2993-3003 (2005).

Assembly members:
Mutant_p53_tetramerization_domain_polypeptide, polymer, 54 residues, 6131.8 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: homo sapiens

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Mutant_p53_tetramerization_domain_polypeptide: GSHMNTSSSPQPKKKPLDGE YFTLQIRGRERFEMFRELNE ALELKDAQAGKEPG

Data sets:
Data typeCount
13C chemical shifts105
15N chemical shifts95
1H chemical shifts95

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit A1
2subunit B1
3subunit C1
4subunit D1

Entities:

Entity 1, subunit A 54 residues - 6131.8 Da.

Residues 11 to 60 correspond to residues 310 to 360 of p53. Arg337 has been substituted by His.

1   GLYSERHISMETASNTHRSERSERSERPRO
2   GLNPROLYSLYSLYSPROLEUASPGLYGLU
3   TYRPHETHRLEUGLNILEARGGLYARGGLU
4   ARGPHEGLUMETPHEARGGLULEUASNGLU
5   ALALEUGLULEULYSASPALAGLNALAGLY
6   LYSGLUPROGLY

Samples:

sample_1: p53tet-R337H, [U-15N], 4.0 mM; Na2HPO4 10.0 mM; NaCl 50.0 mM; NaN3 0.02%

sample_2: p53tet-R337H, U-13C; U-15N, 4.0 mM; Na2HPO4 10.0 mM; NaCl 50.0 mM; NaN3 0.02%

conditions_1: pH: 6.0; temperature: 293.0 K

conditions_2: pH: 4.0; temperature: 293.0 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCnot availablenot availablenot available
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
1H15N_NOESYnot availablenot availablenot available

Software:

Felix, Accelrys - Chemical Shift Assignments

NMR spectrometers:

  • Varian INOVA 600 600 MHz

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