BMRB Entry 28020

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Mdm2 (residues 284 to 434) phosphorylated by DNA-PK
Published: 2019-10-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR28020

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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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Mdm2 (residues 284 to 434) phosphorylated by DNA-PK PubMed: 32181947

Deposition date: 2019-09-24 Original release date: 2019-10-15

Authors: Theillet, Francois-Xavier

Citation: Alik, Ania; Bouguechtouli, Chafiaa; Julien, Manon; Bermel, Wolfgang; Ghouil, Rania; Zinn-Justin, Sophie; Theillet, Francois-Xavier. "Sensitivity-Enhanced 13 C-NMR Spectroscopy for Monitoring Multisite Phosphorylation at Physiological Temperature and pH" Angew. Chem. Int. Ed. Engl. 59, 10411-10415 (2020).

Assembly members:
pMdm2, polymer, 151 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET41

Entity Sequences (FASTA):
pMdm2: GESDTDSFEEDPEISLADYW KCTSCNEMNPPLPSHCNRCW ALRENWLPEDKGKDKGEISE KAKLENSTQAEEGFDVPDAK KTIVNDSRESAVEENDDKIT QASQSQESEDYSQPSTSSSI IYSSQEDVKEFEREETQDKE ESVESSLPLNA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	415
15N chemical shifts	133
1H chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pMdm2	1
2	Zn2+	2

Entities:

Entity 1, pMdm2 151 residues - Formula weight is not available

1

GLY

GLU

SER

ASP

THR

ASP

SER

PHE

GLU

2

ASP

PRO

GLU

ILE

SER

LEU

ALA

ASP

TYR

TRP

3

LYS

CYS

THR

SER

CYS

ASN

GLU

MET

ASN

PRO

4

PRO

LEU

PRO

SER

HIS

CYS

ASN

ARG

CYS

TRP

5

ALA

LEU

ARG

GLU

ASN

TRP

LEU

PRO

GLU

ASP

6

LYS

GLY

LYS

ASP

LYS

GLY

GLU

ILE

SER

GLU

7

LYS

ALA

LYS

LEU

GLU

ASN

SER

THR

GLN

ALA

8

GLU

GLY

PHE

ASP

VAL

PRO

ASP

ALA

LYS

9

LYS

THR

ILE

VAL

ASN

ASP

SER

ARG

GLU

SER

10

ALA

VAL

GLU

ASN

ASP

LYS

ILE

THR

11

GLN

ALA

SER

GLN

SER

GLN

GLU

SER

GLU

ASP

12

TYR

SER

GLN

PRO

SER

THR

SER

ILE

13

ILE

TYR

SER

GLN

GLU

ASP

VAL

LYS

GLU

14

PHE

GLU

ARG

GLU

THR

GLN

ASP

LYS

GLU

15

GLU

SER

VAL

GLU

SER

LEU

PRO

LEU

ASN

16

ALA

Entity 2, Zn2+ - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: pMdm2, [U-99% 13C; U-99% 15N], 200 uM; Zn2+ 1 mM; HEPES 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

TOPSPIN v4.0.4, Bruker Biospin - collection, processing

ccpnmr_analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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