BMRB Entry 51090

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51090

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Title:
Sequence-specific 1H, 15N, and 13C chemical shift assignment of the acidic domain of the human oncoprotein MDMX
Deposition date:
2021-09-19
Original release date:
2022-04-13
Authors:
Song, Qinyan; Rainey, Jan; Liu, Xiang-Qin
Citation:

Citation: Song, Qinyan; Liu, Xiang-Qin; Rainey, Jan. "1H, 15N and 13C backbone resonance assignments of the acidic domain of the human MDMX protein"  Biomol. NMR Assignments 16, 171-178 (2022).
PubMed: 35359247

Assembly members:

Assembly members:
entity_1, polymer, 120 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-30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DETSRLDLGFEEWDVAGLPW WFLGNLRSNYTPRSNGSTDL QTNQDVGTAIVSDTTDDLWF LNESVSEQLGVGIKVEAADT EQTSEEVGKVSDKKVIEVGK NDDLEDSKSLSDDTDVEVTS

Data sets:
Data typeCount
13C chemical shifts343
15N chemical shifts116
1H chemical shifts116

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1acidic domain of human MDMX1

Entities:

Entity 1, acidic domain of human MDMX 120 residues - Formula weight is not available

Acidic domain of human MDMX containing residues that span 181-300 (120 residues).

1   ASPGLUTHRSERARGLEUASPLEUGLYPHE
2   GLUGLUTRPASPVALALAGLYLEUPROTRP
3   TRPPHELEUGLYASNLEUARGSERASNTYR
4   THRPROARGSERASNGLYSERTHRASPLEU
5   GLNTHRASNGLNASPVALGLYTHRALAILE
6   VALSERASPTHRTHRASPASPLEUTRPPHE
7   LEUASNGLUSERVALSERGLUGLNLEUGLY
8   VALGLYILELYSVALGLUALAALAASPTHR
9   GLUGLNTHRSERGLUGLUVALGLYLYSVAL
10   SERASPLYSLYSVALILEGLUVALGLYLYS
11   ASNASPASPLEUGLUASPSERLYSSERLEU
12   SERASPASPTHRASPVALGLUVALTHRSER

Samples:

sample_1: Acidic domain of human MDMX, [U-99% 13C; U-99% 15N], 380 uM; DSS 1 mM; sodium phosphate 20 mM; sodium azide 0.05 % v/v; sodium chloride 40 mM; D2O, [U-99% 2H], 10 % v/v; H2O 90 % v/v

sample_conditions_1: ionic strength: 82 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRbox - chemical shift assignment, data analysis, peak picking, processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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