BMRB Entry 52289

Name: Mdm2aa111-333 phosphorylated by CK1d
Published: 2024-02-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52289

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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:

Mdm2aa111-333 phosphorylated by CK1d

Deposition date:

2024-01-28

Original release date:

2024-02-02

Authors:

Luo, Yingyue; Theillet, Francois-Xavier

Citation:

Citation: Luo, Yingyue; 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, 224 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-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNQQESSDSGTSVSENRAHL EGGSDQKDLVQELQEEKPSS SHLVSRPSTSSRRRAISETE ENSDELSGERQRKRHKSDSI SLXFDESLALAVIREIAAER SSSSEXTGXPXNPDLDAGVX EHSGDWLDQDXVXDQFXVEF EVEXLDXEDYXLXEEGQELS DEDDEVYQVXVYQAGEXDTD SFEEDPEISLADYWKCTSCN EMNPPLPSHCNRCWALRENW LPED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	528
15N chemical shifts	175
1H chemical shifts	175

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mdm2aa111-333 phosphorylated by CK1d	1

Entities:

Entity 1, Mdm2aa111-333 phosphorylated by CK1d 224 residues - Formula weight is not available

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

SEP

PHE

ASP

GLU

SER

LEU

ALA

LEU

10

ALA

VAL

ILE

ARG

GLU

ILE

ALA

GLU

ARG

11

SER

GLU

SEP

THR

GLY

TPO

PRO

12

SEP

ASN

PRO

ASP

LEU

ASP

ALA

GLY

VAL

SEP

13

GLU

HIS

SER

GLY

ASP

TRP

LEU

ASP

GLN

ASP

14

SEP

VAL

SEP

ASP

GLN

PHE

SEP

VAL

GLU

PHE

15

GLU

VAL

GLU

SEP

LEU

ASP

SEP

GLU

ASP

TYR

16

SEP

LEU

SEP

GLU

GLY

GLN

GLU

LEU

SER

17

ASP

GLU

ASP

GLU

VAL

TYR

GLN

VAL

TPO

18

VAL

TYR

GLN

ALA

GLY

GLU

SEP

ASP

THR

ASP

19

SER

PHE

GLU

ASP

PRO

GLU

ILE

SER

LEU

20

ALA

ASP

TYR

TRP

LYS

CYS

THR

SER

CYS

ASN

21

GLU

MET

ASN

PRO

LEU

PRO

SER

HIS

CYS

22

ASN

ARG

CYS

TRP

ALA

LEU

ARG

GLU

ASN

TRP

23

LEU

PRO

GLU

ASP

Samples:

sample_1: Mdm2aa111-333 phosphorylated by CK1d, [U-98% 13C; U-98% 15N], 180 ± 20 uM; D2O, [U-2H], 1.5 M; DSS 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; protease inhibitors cocktail 1 tablet/100mL

sample_conditions_1: ionic strength: 0.19 M; pH: 7.4; 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 HN(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3 - collection

CcpNMR v2.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz

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