BMRB Entry 52028

Name: Mdm2 aa111-230 4C4A human
Published: 2023-07-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52028

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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:

Mdm2 aa111-230 4C4A human

Deposition date:

2023-07-12

Original release date:

2023-07-21

Authors:

Theillet, Francois-Xavier

Citation:

Citation: Theillet, Francois-Xavier. "Structural characterization of the MDM2 NLS/NES/arrestin-binding/acidic domain in phospho- and unmodified-forms" .

Assembly members:

Assembly members:
entity_1, polymer, 121 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: pET41b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNQQESSDSGTSVSENRAHL EGGSDQKDLVQELQEEKPSS SHLVSRPSTSSRRRAISETE ENSDELSGERQRKRHKSDSI SLSFDESLALAVIREIAAER SSSSESTGTPSNPDLDAGVS E

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	353
15N chemical shifts	115
1H chemical shifts	115

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mdm2 aa111-230 4C4A	1

Entities:

Entity 1, Mdm2 aa111-230 4C4A 121 residues - Formula weight is not available

One supplementary Glycine in N-terminal, remaining from Tev-motif (ENLYFQG) after cleavage by Tev-protease. Four Alanine-mutations of the 4 cysteine residues : C127A-C200A-C206A-C207A.

1

GLY

ASN

GLN

GLU

SER

ASP

SER

GLY

2

THR

SER

VAL

SER

GLU

ASN

ARG

ALA

HIS

LEU

3

GLU

GLY

SER

ASP

GLN

LYS

ASP

LEU

VAL

4

GLN

GLU

LEU

GLN

GLU

LYS

PRO

SER

5

SER

HIS

LEU

VAL

SER

ARG

PRO

SER

THR

SER

6

SER

ARG

ALA

ILE

SER

GLU

THR

GLU

7

GLU

ASN

SER

ASP

GLU

LEU

SER

GLY

GLU

ARG

8

GLN

ARG

LYS

ARG

HIS

LYS

SER

ASP

SER

ILE

9

SER

LEU

SER

PHE

ASP

GLU

SER

LEU

ALA

LEU

10

ALA

VAL

ILE

ARG

GLU

ILE

ALA

GLU

ARG

11

SER

GLU

SER

THR

GLY

THR

PRO

12

SER

ASN

PRO

ASP

LEU

ASP

ALA

GLY

VAL

SER

13

GLU

Samples:

sample_1: Mdm2 aa111-230 4C4A, [U-98% 13C; U-98% 15N], 600 uM; DSS 100 uM; HEPES 10 mM; NaCl 50 mM; cocktail protease inhibitors 2 tablet/100mL

sample_conditions_1: ionic strength: 0.06 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(NCA)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3 - collection, processing

CcpNMR v2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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