BMRB Entry 51124

Name: Backbone 1H, 15N chemical shift assignments of human p53 1-94
Published: 2021-11-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51124

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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 1H, 15N chemical shift assignments of human p53 1-94

Deposition date:

2021-10-04

Original release date:

2021-11-21

Authors:

Bourgeois, Benjamin

Citation:

Citation: Usluer, Sinem; Spreitzer, Emil; Bourgeois, Benjamin; Madl, Tobias. "p53 Transactivation Domain Mediates Binding and Phase Separation with Poly-PR/GR" Int. J. Mol. Sci 22, 11431-11431 (2021).
PubMed: 34768862

Assembly members:

Assembly members:
entity_1, polymer, 94 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEEPQSDPSVEPPLSQETFS DLWKLLPENNVLSPLPSQAM DDLMLSPDDIEQWFTEDPGP DEAPRMPEAAPPVAPAPAAP TPAAPAPAPSWPLS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	64
1H chemical shifts	63

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p53 1-94	1

Entities:

Entity 1, p53 1-94 94 residues - Formula weight is not available

1

MET

GLU

PRO

GLN

SER

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

SER

PRO

ASP

ILE

6

GLU

GLN

TRP

PHE

THR

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 1-94, [U-99% 13C; U-99% 15N], 300 uM; D2O 5%; HEPES 20 mM; sodium chloride 50 mM; TCEP 2 mM; sodium azide 0.04%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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