BMRB Entry 50511

Name: Backbone chemical shift assignments of the p53 1-95 (S6A and S46A) peptide with phosphorylation of T55
Published: 2025-06-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50511

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone chemical shift assignments of the p53 1-95 (S6A and S46A) peptide with phosphorylation of T55

Deposition date:

2020-10-13

Original release date:

2025-06-04

Authors:

Sun, Xun; Dyson, H.; Wright, Peter

Citation:

Citation: Sun, Xun; Dyson, H.; Wright, Peter. "A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA binding" Proc. Natl. Acad. Sci. U. S. A. 118, e2021456118-e2021456118 (2021).
PubMed: 33443163

Assembly members:

Assembly members:
entity_1, polymer, 95 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEEPQADPSVEPPLSQETFS DLWKLLPENNVLSPLPSQAM DDLMLAPDDIEQWFXEDPGP DEAPRMPEAAPPVAPAPAAP TPAAPAPAPSWPLSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	263
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	phosphorylated T55, p53 NTAD-PRD	1

Entities:

Entity 1, phosphorylated T55, p53 NTAD-PRD 95 residues - Formula weight is not available

1

MET

GLU

PRO

GLN

ALA

ASP

PRO

SER

VAL

2

GLU

PRO

LEU

SER

GLN

GLU

THR

PHE

SER

3

ASP

LEU

TRP

LYS

LEU

PRO

GLU

ASN

4

VAL

LEU

SER

PRO

LEU

PRO

SER

GLN

ALA

MET

5

ASP

LEU

MET

LEU

ALA

PRO

ASP

ILE

6

GLU

GLN

TRP

PHE

TPO

GLU

ASP

PRO

GLY

PRO

7

ASP

GLU

ALA

PRO

ARG

MET

PRO

GLU

ALA

8

PRO

VAL

ALA

PRO

ALA

PRO

ALA

PRO

9

THR

PRO

ALA

PRO

ALA

PRO

ALA

PRO

SER

10

TRP

PRO

LEU

SER

Samples:

sample_1: p53 1-95 S6A-S46A pT55, [U-13C; U-15N], 300 uM; sodium chloride 150 mM; TRIS/HCl 20 mM; DTT 2 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ - chemical shift assignment

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

Bruker Avance 700 MHz

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