BMRB Entry 52703

Name: p53(1-93) apo form
Published: 2024-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52703

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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:

p53(1-93) apo form

Deposition date:

2024-11-18

Original release date:

2024-12-19

Authors:

Kohoutova, Klara; Srb, Pavel; Obsilova, Veronika; Veverka, Vaclav; Obsil, Tomas

Citation:

Citation: Kohoutova, Klara; Srb, Pavel; Obsilova, Veronika; Veverka, Vaclav; Obsil, Tomas. "Structural Plasticity of the FOXO-DBD:p53-TAD Interaction" Nat. Commun. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 93 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: pET21

Entity Sequences (FASTA):

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

Data sets:

heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
T1 relaxation values	64
T2 relaxation values	64

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p53(1-93)	1

Entities:

Entity 1, p53(1-93) 93 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

Samples:

sample_1: p53, [U-100% 15N], 100 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRFAM-SPARKY v3.1 - data analysis

NMR spectrometers:

Bruker AVANCE III 850 MHz