BMRB Entry 52016

Name: Mdm2_aa111-293_human
Published: 2023-07-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52016

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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_aa111-293_human

Deposition date:

2023-07-07

Original release date:

2023-07-10

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, 184 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: pET41(b+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNQQESSDSGTSVSENRCHL EGGSDQKDLVQELQEEKPSS SHLVSRPSTSSRRRAISETE ENSDELSGERQRKRHKSDSI SLSFDESLALCVIREICCER SSSSESTGTPSNPDLDAGVS EHSGDWLDQDSVSDQFSVEF EVESLDSEDYSLSEEGQELS DEDDEVYQVTVYQAGESDTD SFEE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	536
15N chemical shifts	178
1H chemical shifts	178

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mdm2_aa111-293	1

Entities:

Entity 1, Mdm2_aa111-293 184 residues - Formula weight is not available

One supplementary Glycine in N-terminal, remaining from Tev-motif (ENLYFQG) after cleavage by Tev-protease.

1

GLY

ASN

GLN

GLU

SER

ASP

SER

GLY

2

THR

SER

VAL

SER

GLU

ASN

ARG

CYS

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

CYS

VAL

ILE

ARG

GLU

ILE

CYS

GLU

ARG

11

SER

GLU

SER

THR

GLY

THR

PRO

12

SER

ASN

PRO

ASP

LEU

ASP

ALA

GLY

VAL

SER

13

GLU

HIS

SER

GLY

ASP

TRP

LEU

ASP

GLN

ASP

14

SER

VAL

SER

ASP

GLN

PHE

SER

VAL

GLU

PHE

15

GLU

VAL

GLU

SER

LEU

ASP

SER

GLU

ASP

TYR

16

SER

LEU

SER

GLU

GLY

GLN

GLU

LEU

SER

17

ASP

GLU

ASP

GLU

VAL

TYR

GLN

VAL

THR

18

VAL

TYR

GLN

ALA

GLY

GLU

SER

ASP

THR

ASP

19

SER

PHE

GLU

Samples:

sample_1: Mdm2_aa111-293, [U-98% 13C; U-98% 15N], 600 uM; DSS 0.1 mM; HEPES 10 mM; sodium chloride 50 mM; TCEP 4 mM; cocktail protease inhibitors 2 tablet/100mL

sample_conditions_1: ionic strength: 0.06 M; pH: 6.2; 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 HNCACO	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