BMRB Entry 51753

Name: Human p53 DBD (94-293)
Published: 2024-03-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51753

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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:

Human p53 DBD (94-293)

Deposition date:

2022-12-29

Original release date:

2024-03-18

Authors:

Zoltsman, Guy; Rosenzweig, Rina

Citation:

Citation: Zoltsman, Guy; Dang, Lieu; Kuchersky, Miri; Faust, Ofrah; Silva, Micael; Ilani, Tal; Wentink, Anne; Bukau, Bernd; Rosenzweig, Rina. "A unique chaperoning mechanism in class A JDPs recognizes and stabilizes mutant p53" Mol. Cell 84, 1512-1526 (2024).
PubMed: 38508184

Assembly members:

Assembly members:
entity_1, polymer, 200 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-27

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSSVPSQKTYQGSYGFRLGF LHSGTAKSVTCTYSPALNKM FCQLAKTCPVQLWVDSTPPP GTRVRAMAIYKQSQHMTEVV RRCPHHERCSDSDGLAPPQH LIRVEGNLRVEYLDDRNTFR HSVVVPYEPPEVGSDCTTIH YNYMCNSSCMGGMNRRPILT IITLEDSSGNLLGRNSFEVR VCACPGRDRRTEEENLRKKG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	551
15N chemical shifts	173
1H chemical shifts	173

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p53 DBD	1

Entities:

Entity 1, p53 DBD 200 residues - Formula weight is not available

1	SER	SER	SER	VAL	PRO	SER	GLN	LYS	THR	TYR
2	GLN	GLY	SER	TYR	GLY	PHE	ARG	LEU	GLY	PHE
3	LEU	HIS	SER	GLY	THR	ALA	LYS	SER	VAL	THR
4	CYS	THR	TYR	SER	PRO	ALA	LEU	ASN	LYS	MET
5	PHE	CYS	GLN	LEU	ALA	LYS	THR	CYS	PRO	VAL
6	GLN	LEU	TRP	VAL	ASP	SER	THR	PRO	PRO	PRO
7	GLY	THR	ARG	VAL	ARG	ALA	MET	ALA	ILE	TYR
8	LYS	GLN	SER	GLN	HIS	MET	THR	GLU	VAL	VAL
9	ARG	ARG	CYS	PRO	HIS	HIS	GLU	ARG	CYS	SER
10	ASP	SER	ASP	GLY	LEU	ALA	PRO	PRO	GLN	HIS
11	LEU	ILE	ARG	VAL	GLU	GLY	ASN	LEU	ARG	VAL
12	GLU	TYR	LEU	ASP	ASP	ARG	ASN	THR	PHE	ARG
13	HIS	SER	VAL	VAL	VAL	PRO	TYR	GLU	PRO	PRO
14	GLU	VAL	GLY	SER	ASP	CYS	THR	THR	ILE	HIS
15	TYR	ASN	TYR	MET	CYS	ASN	SER	SER	CYS	MET
16	GLY	GLY	MET	ASN	ARG	ARG	PRO	ILE	LEU	THR
17	ILE	ILE	THR	LEU	GLU	ASP	SER	SER	GLY	ASN
18	LEU	LEU	GLY	ARG	ASN	SER	PHE	GLU	VAL	ARG
19	VAL	CYS	ALA	CYS	PRO	GLY	ARG	ASP	ARG	ARG
20	THR	GLU	GLU	GLU	ASN	LEU	ARG	LYS	LYS	GLY

Samples:

sample_1: p53 DBD, [U-13C; U-15N; U-2H], 500 uM

sample_conditions_1: pH: 7.2; 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

TOPSPIN - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

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

1	SER	SER	SER	VAL	PRO	SER	GLN	LYS	THR	TYR
2	GLN	GLY	SER	TYR	GLY	PHE	ARG	LEU	GLY	PHE
3	LEU	HIS	SER	GLY	THR	ALA	LYS	SER	VAL	THR
4	CYS	THR	TYR	SER	PRO	ALA	LEU	ASN	LYS	MET
5	PHE	CYS	GLN	LEU	ALA	LYS	THR	CYS	PRO	VAL
6	GLN	LEU	TRP	VAL	ASP	SER	THR	PRO	PRO	PRO
7	GLY	THR	ARG	VAL	ARG	ALA	MET	ALA	ILE	TYR
8	LYS	GLN	SER	GLN	HIS	MET	THR	GLU	VAL	VAL
9	ARG	ARG	CYS	PRO	HIS	HIS	GLU	ARG	CYS	SER
10	ASP	SER	ASP	GLY	LEU	ALA	PRO	PRO	GLN	HIS
11	LEU	ILE	ARG	VAL	GLU	GLY	ASN	LEU	ARG	VAL
12	GLU	TYR	LEU	ASP	ASP	ARG	ASN	THR	PHE	ARG
13	HIS	SER	VAL	VAL	VAL	PRO	TYR	GLU	PRO	PRO
14	GLU	VAL	GLY	SER	ASP	CYS	THR	THR	ILE	HIS
15	TYR	ASN	TYR	MET	CYS	ASN	SER	SER	CYS	MET
16	GLY	GLY	MET	ASN	ARG	ARG	PRO	ILE	LEU	THR
17	ILE	ILE	THR	LEU	GLU	ASP	SER	SER	GLY	ASN
18	LEU	LEU	GLY	ARG	ASN	SER	PHE	GLU	VAL	ARG
19	VAL	CYS	ALA	CYS	PRO	GLY	ARG	ASP	ARG	ARG
20	THR	GLU	GLU	GLU	ASN	LEU	ARG	LYS	LYS	GLY

1	SER	SER	SER	VAL	PRO	SER	GLN	LYS	THR	TYR
2	GLN	GLY	SER	TYR	GLY	PHE	ARG	LEU	GLY	PHE
3	LEU	HIS	SER	GLY	THR	ALA	LYS	SER	VAL	THR
4	CYS	THR	TYR	SER	PRO	ALA	LEU	ASN	LYS	MET
5	PHE	CYS	GLN	LEU	ALA	LYS	THR	CYS	PRO	VAL
6	GLN	LEU	TRP	VAL	ASP	SER	THR	PRO	PRO	PRO
7	GLY	THR	ARG	VAL	ARG	ALA	MET	ALA	ILE	TYR
8	LYS	GLN	SER	GLN	HIS	MET	THR	GLU	VAL	VAL
9	ARG	ARG	CYS	PRO	HIS	HIS	GLU	ARG	CYS	SER
10	ASP	SER	ASP	GLY	LEU	ALA	PRO	PRO	GLN	HIS
11	LEU	ILE	ARG	VAL	GLU	GLY	ASN	LEU	ARG	VAL
12	GLU	TYR	LEU	ASP	ASP	ARG	ASN	THR	PHE	ARG
13	HIS	SER	VAL	VAL	VAL	PRO	TYR	GLU	PRO	PRO
14	GLU	VAL	GLY	SER	ASP	CYS	THR	THR	ILE	HIS
15	TYR	ASN	TYR	MET	CYS	ASN	SER	SER	CYS	MET
16	GLY	GLY	MET	ASN	ARG	ARG	PRO	ILE	LEU	THR
17	ILE	ILE	THR	LEU	GLU	ASP	SER	SER	GLY	ASN
18	LEU	LEU	GLY	ARG	ASN	SER	PHE	GLU	VAL	ARG
19	VAL	CYS	ALA	CYS	PRO	GLY	ARG	ASP	ARG	ARG
20	THR	GLU	GLU	GLU	ASN	LEU	ARG	LYS	LYS	GLY

1	SER	SER	SER	VAL	PRO	SER	GLN	LYS	THR	TYR
2	GLN	GLY	SER	TYR	GLY	PHE	ARG	LEU	GLY	PHE
3	LEU	HIS	SER	GLY	THR	ALA	LYS	SER	VAL	THR
4	CYS	THR	TYR	SER	PRO	ALA	LEU	ASN	LYS	MET
5	PHE	CYS	GLN	LEU	ALA	LYS	THR	CYS	PRO	VAL
6	GLN	LEU	TRP	VAL	ASP	SER	THR	PRO	PRO	PRO
7	GLY	THR	ARG	VAL	ARG	ALA	MET	ALA	ILE	TYR
8	LYS	GLN	SER	GLN	HIS	MET	THR	GLU	VAL	VAL
9	ARG	ARG	CYS	PRO	HIS	HIS	GLU	ARG	CYS	SER
10	ASP	SER	ASP	GLY	LEU	ALA	PRO	PRO	GLN	HIS
11	LEU	ILE	ARG	VAL	GLU	GLY	ASN	LEU	ARG	VAL
12	GLU	TYR	LEU	ASP	ASP	ARG	ASN	THR	PHE	ARG
13	HIS	SER	VAL	VAL	VAL	PRO	TYR	GLU	PRO	PRO
14	GLU	VAL	GLY	SER	ASP	CYS	THR	THR	ILE	HIS
15	TYR	ASN	TYR	MET	CYS	ASN	SER	SER	CYS	MET
16	GLY	GLY	MET	ASN	ARG	ARG	PRO	ILE	LEU	THR
17	ILE	ILE	THR	LEU	GLU	ASP	SER	SER	GLY	ASN
18	LEU	LEU	GLY	ARG	ASN	SER	PHE	GLU	VAL	ARG
19	VAL	CYS	ALA	CYS	PRO	GLY	ARG	ASP	ARG	ARG
20	THR	GLU	GLU	GLU	ASN	LEU	ARG	LYS	LYS	GLY