BMRB Entry 51984

Name: 1H, 13C, and 15N Chemical Shift Assignments for p53 (1-100)
Published: 2023-10-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51984

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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:

1H, 13C, and 15N Chemical Shift Assignments for p53 (1-100)

Deposition date:

2023-05-31

Original release date:

2023-10-20

Authors:

Sebak, Fanni; Bodor, Andrea

Citation:

Citation: Sebak, Fanni; Ecsedi, Peter; Nyitray, Laszlo; Bodor, Andrea. "Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1Ha-detected NMR measurements" Biomol. NMR Assign. 17, 309-314 (2023).
PubMed: 37861971

Assembly members:

Assembly members:
entity_1, polymer, 102 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: pETARA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMEEPQSDPSVEPPLSQET FSDLWKLLPENNVLSPLPSQ AMDDLMLSPDDIEQWFTEDP GPDEAPRMPEAAPRVAPAPA APTPAAPAPAPSWPLSSSVP SQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	288
15N chemical shifts	99
1H chemical shifts	168

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p53(1-100)	1

Entities:

Entity 1, p53(1-100) 102 residues - Formula weight is not available

Residues -1 - 0 represent a cloning artifact.

1

GLY

SER

MET

GLU

PRO

GLN

SER

ASP

PRO

2

SER

VAL

GLU

PRO

LEU

SER

GLN

GLU

THR

3

PHE

SER

ASP

LEU

TRP

LYS

LEU

PRO

GLU

4

ASN

VAL

LEU

SER

PRO

LEU

PRO

SER

GLN

5

ALA

MET

ASP

LEU

MET

LEU

SER

PRO

ASP

6

ASP

ILE

GLU

GLN

TRP

PHE

THR

GLU

ASP

PRO

7

GLY

PRO

ASP

GLU

ALA

PRO

ARG

MET

PRO

GLU

8

ALA

PRO

ARG

VAL

ALA

PRO

ALA

PRO

ALA

9

ALA

PRO

THR

PRO

ALA

PRO

ALA

PRO

ALA

10

PRO

SER

TRP

PRO

LEU

SER

VAL

PRO

11

SER

GLN

Samples:

sample_1: p53(1-100), [U-100% 13C; U-100% 15N], 1 mM; MES 20 mM; sodium chloride 20 mM; TCEP 10 mM; sodium azide 3 mM; D2O, [U-2H], 10%; DSS 1 % v/v

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D SHACA-HSQC	sample_1	isotropic	sample_conditions_1
3D HCAN	sample_1	isotropic	sample_conditions_1
3D HCACON	sample_1	isotropic	sample_conditions_1
3D Pro-(H)CBCGCAHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - collection, processing

CARA v1.8.4.2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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