BMRB Entry 51613

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51613

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Title:
p53 C-terminal
Deposition date:
2022-09-02
Original release date:
2024-08-27
Authors:
Krois, Alexander; Park, Sangho; Martinez-Yamout, Maria; Dyson, H. Jane; Wright, Peter
Citation:

Citation: Krois, Alexander; Park, Sangho; Martinez-Yamout, Maria; Dyson, H. Jane; Wright, Peter. "Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR"  Biochemistry 61, 2709-2719 (2022).
PubMed: 36380579

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TKRALPNNTSSSPQPKKKPL DGEYFTLQIRGRERFEMFRE LNEALELKDAQAGKEPGGSR AHSSHLKSKKGQSTSRHKKL MFKTEGPDSD

Data sets:
Data typeCount
13C chemical shifts98
15N chemical shifts41
1H chemical shifts41

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p53 Cterm1

Entities:

Entity 1, p53 Cterm 90 residues - Formula weight is not available

1   THRLYSARGALALEUPROASNASNTHRSER
2   SERSERPROGLNPROLYSLYSLYSPROLEU
3   ASPGLYGLUTYRPHETHRLEUGLNILEARG
4   GLYARGGLUARGPHEGLUMETPHEARGGLU
5   LEUASNGLUALALEUGLULEULYSASPALA
6   GLNALAGLYLYSGLUPROGLYGLYSERARG
7   ALAHISSERSERHISLEULYSSERLYSLYS
8   GLYGLNSERTHRSERARGHISLYSLYSLEU
9   METPHELYSTHRGLUGLYPROASPSERASP

Samples:

sample_1: C-terminal region of p53, [U-99% 15N], 90 uM; TRIS 20 mM; NaCl 150 mM; DTT 2 mM

sample_2: C-terminal region of p53, [U-99% 15N], 90 uM; TRIS 20 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRViewJ - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

UniProt P04637

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