BMRB Entry 51605

Name: Backbone 1H, 15N, 13C chemical Shift Assignments for the mutant human MDMX acidic domain, residues 170-260 W239S/W240S
Published: 2022-10-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51605

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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, 15N, 13C chemical Shift Assignments for the mutant human MDMX acidic domain, residues 170-260 W239S/W240S

Deposition date:

2022-08-31

Original release date:

2022-10-07

Authors:

Fenton, Malissa; Borcherds, Wade; Chen, Lihong; Anbanandam, Asokan; Chen, Jiandong; Daughdrill, Gary

Citation:

Citation: Fenton, Malissa; Borcherds, Wade; Chen, Lihong; Anbanandam, Asokan; Levy, Robin; Chen, Jiandong; Daughdrill, Gary. "Two short linear motifs in the MDMX acidic domain bind overlapping sites on MDMX and p53" J. Mol. Biol. 434, 167844-167844 (2022).
PubMed: 36181774

Assembly members:

Assembly members:
entity_1, polymer, 96 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: pGEX-6p-2 vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPLGSEDEDLIENLAQDETS RLDLGFEEWDVAGLPWWFLG NLRSNYTPRSNGSTDLQTNQ DVGTAIVSDTTDDLSSLNES VSEQLGVGIKVEAADT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	274
15N chemical shifts	92
1H chemical shifts	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MDMX	1

Entities:

Entity 1, MDMX 96 residues - Formula weight is not available

The MDMX acidic domain, residues 170-260 mutated at W239S/W240S; including five residues that are left over after the HRV3C cleavage and remain intact N-terminally to the MDMX protein sequence, designated as residues 166-169.

1

GLY

PRO

LEU

GLY

SER

GLU

ASP

GLU

ASP

LEU

2

ILE

GLU

ASN

LEU

ALA

GLN

ASP

GLU

THR

SER

3

ARG

LEU

ASP

LEU

GLY

PHE

GLU

TRP

ASP

4

VAL

ALA

GLY

LEU

PRO

TRP

PHE

LEU

GLY

5

ASN

LEU

ARG

SER

ASN

TYR

THR

PRO

ARG

SER

6

ASN

GLY

SER

THR

ASP

LEU

GLN

THR

ASN

GLN

7

ASP

VAL

GLY

THR

ALA

ILE

VAL

SER

ASP

THR

8

THR

ASP

LEU

SER

LEU

ASN

GLU

SER

9

VAL

SER

GLU

GLN

LEU

GLY

VAL

GLY

ILE

LYS

10

VAL

GLU

ALA

ASP

THR

Samples:

sample_1: Apo MDMX, [U-13C; U-15N], 100 uM; D2O, [U-100% 2H], 10 % v/v; H2O 90 % v/v; DTT 4 mM; sodium phosphate 10 mM; sodium chloride 66 mM; sodium azide 0.02 % v/v

sample_conditions_1: ionic strength: 66 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ v9.2.b20 - chemical shift assignment, data analysis, peak picking

NMRFx Processor - processing

VNMRj - collection

NMR spectrometers:

Agilent VNMRS 800 MHz

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