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:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

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

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_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