Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52216

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain human Mdm2 in Apo form, Apo-MDM2-Lid-wt (residues 6 to 125)
Published: 2026-02-11

Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain human Mdm2 in Apo form, Apo-MDM2-Lid-wt (residues 6 to 125)

Deposition date:

2023-11-26

Original release date:

2026-02-11

Authors:

Gupta, Arun; Michel, Julien

Citation:

Citation: Gupta, Arun. "Protein disorder-order transitions in MDM2 and its mutants upon binding: an experimental/computational study" Commun. Chem. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 120 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-20b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSVPTDGAVTTSQIPASEQE TLVRPKPLLLKLLKSVGAQK DTYTMKEVLFYLGQYIMTKR LYDEKQQHIVYCSNDLLGDL FGVPSFSVKEHRKIYTMIYR NLVVVNQQESSDSGTSVSEN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	298
15N chemical shifts	106
1H chemical shifts	223

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ubiquitin-protein ligase E3 Mdm2 in Apo form, Apo-MDM2-Lid-wt	1

Entities:

Entity 1, Ubiquitin-protein ligase E3 Mdm2 in Apo form, Apo-MDM2-Lid-wt 120 residues - Formula weight is not available

1	MET	SER	VAL	PRO	THR	ASP	GLY	ALA	VAL	THR
2	THR	SER	GLN	ILE	PRO	ALA	SER	GLU	GLN	GLU
3	THR	LEU	VAL	ARG	PRO	LYS	PRO	LEU	LEU	LEU
4	LYS	LEU	LEU	LYS	SER	VAL	GLY	ALA	GLN	LYS
5	ASP	THR	TYR	THR	MET	LYS	GLU	VAL	LEU	PHE
6	TYR	LEU	GLY	GLN	TYR	ILE	MET	THR	LYS	ARG
7	LEU	TYR	ASP	GLU	LYS	GLN	GLN	HIS	ILE	VAL
8	TYR	CYS	SER	ASN	ASP	LEU	LEU	GLY	ASP	LEU
9	PHE	GLY	VAL	PRO	SER	PHE	SER	VAL	LYS	GLU
10	HIS	ARG	LYS	ILE	TYR	THR	MET	ILE	TYR	ARG
11	ASN	LEU	VAL	VAL	VAL	ASN	GLN	GLN	GLU	SER
12	SER	ASP	SER	GLY	THR	SER	VAL	SER	GLU	ASN

Samples:

sample_1: E3 ubiquitin-protein ligase Mdm2, [U-98% 15N], 75 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 1 mM; TSP 0.01 - 0.5 mM

sample_2: E3 ubiquitin-protein ligase Mdm2, [U-98% 13C; U-98% 15N], 483 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 1 mM; TSP 0.01 - 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HMQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 15N TOCSY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe v2023 - processing

PINE vPINE-SPARKY.2 - chemical shift assignment

TOPSPIN vTopSpin 3.5 pl 7 - collection

NMRFAM-SPARKY - data analysis

NMR spectrometers:

Bruker Avance 800 MHz

BMRB Entry 52216