Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52221

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Nicholas Rego and David Koes
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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 (I19G mutant) in Apo form, Apo-MDM2-Lid-I19G (residues 6 to 125)
Published: 2026-02-11

Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain human Mdm2 (I19G mutant) in Apo form, Apo-MDM2-Lid-I19G (residues 6 to 125)

Deposition date:

2023-11-30

Original release date:

2026-02-11

Authors:

Gupta, Arun; Michel, Julien

Citation:

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

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 13524.45 Da.

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: MCNTNMSVPTDGAVTTSQGP ASEQETLVRPKPLLLKLLKS VGAQKDTYTMKEVLFYLGQY IMTKRLYDEKQQHIVYCSND LLGDLFGVPSFSVKEHRKIY TMIYRNLVVVNQQESSDSGT SVSEN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	191
15N chemical shifts	98
1H chemical shifts	163

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human Mdm2 (6-125) I19G mutant	1

Entities:

Entity 1, human Mdm2 (6-125) I19G mutant 125 residues - 13524.45 Da.

Ubiquitin-protein ligase E3 Mdm2

1

MET

CYS

ASN

THR

ASN

MET

SER

VAL

PRO

THR

2

ASP

GLY

ALA

VAL

THR

SER

GLN

GLY

PRO

3

ALA

SER

GLU

GLN

GLU

THR

LEU

VAL

ARG

PRO

4

LYS

PRO

LEU

LYS

LEU

LYS

SER

5

VAL

GLY

ALA

GLN

LYS

ASP

THR

TYR

THR

MET

6

LYS

GLU

VAL

LEU

PHE

TYR

LEU

GLY

GLN

TYR

7

ILE

MET

THR

LYS

ARG

LEU

TYR

ASP

GLU

LYS

8

GLN

HIS

ILE

VAL

TYR

CYS

SER

ASN

ASP

9

LEU

GLY

ASP

LEU

PHE

GLY

VAL

PRO

SER

10

PHE

SER

VAL

LYS

GLU

HIS

ARG

LYS

ILE

TYR

11

THR

MET

ILE

TYR

ARG

ASN

LEU

VAL

12

ASN

GLN

GLU

SER

ASP

SER

GLY

THR

13

SER

VAL

SER

GLU

ASN

Samples:

sample_1: human Mdm2 (6-125) I19G mutant, [U-98% 15N], 75 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 1 mM

sample_2: human Mdm2 (6-125) I19G mutant, [U-98% 13C; U-98% 15N], 135 uM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 1 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 CBCACONH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN vTopSpin 3.5 pl 7 - collection

NMRPipe v2023 - processing

NMRFAM-SPARKY - data analysis

POKY - data analysis

AutoAssign - chemical shift assignment

PINE - chemical shift assignment refinement

NMR spectrometers:

Bruker Avance 800 MHz

BMRB Entry 52221