BMRB Entry 51604

Title:
Backbone 1H, 15N, 13C chemical Shift Assignments for the mutant human MDMX acidic domain, residues 170-260 W200S/W201G
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

Data sets:
Data typeCount
13C chemical shifts272
15N chemical shifts91
1H chemical shifts91

Additional metadata:

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  • Samples and Experiments
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  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1MDMX1

Entities:

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

The MDMX acidic domain, residues 170-260 mutated at W200S/W201G; 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   GLYPROLEUGLYSERGLUASPGLUASPLEU
2   ILEGLUASNLEUALAGLNASPGLUTHRSER
3   ARGLEUASPLEUGLYPHEGLUGLUTRPASP
4   VALALAGLYLEUPROSERGLYPHELEUGLY
5   ASNLEUARGSERASNTYRTHRPROARGSER
6   ASNGLYSERTHRASPLEUGLNTHRASNGLN
7   ASPVALGLYTHRALAILEVALSERASPTHR
8   THRASPASPLEUTRPPHELEUASNGLUSER
9   VALSERGLUGLNLEUGLYVALGLYILELYS
10   VALGLUALAALAASPTHR

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