BMRB Entry 54060

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR54060

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Title:
Mdm2_aa111-333_3C3S
Deposition date:
2026-10-17
Original release date:
2026-10-22
Authors:
Theillet, Francois-Xavier; Procaccia, Jehanne; Cuzin, Clemence
Citation:

Citation: Luo, Yingyue; Procaccia, Jehanne; Bouguechtouli, Chafiaa; Cuzin, Clemence; Alik, Ania; Aumont-Nicaise, Magali; Theillet, Francois-Xavier. "The disordered region 1 of Mdm2 weakens p53-binding in both its unmodified and hyperphospho-forms "  .

Assembly members:

Assembly members:
Mdm2_aa111-333_1C1A_3C3S, polymer, 224 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-45b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mdm2_aa111-333_1C1A_3C3S: GNQQESSDSGTSVSENRAHL EGGSDQKDLVQELQEEKPSS SHLVSRPSTSSRRRAISETE ENSDELSGERQRKRHKSDSI SLSFDESLALSVIREISSER SSSSESTGTPSNPDLDAGVS EHSGDWLDQDSVSDQFSVEF EVESLDSEDYSLSEEGQELS DEDDEVYQVTVYQAGESDTD SFEEDPEISLADYWKCTSCN EMNPPLPSHCNRCWALRENW LPED

Data sets:
Data typeCount
13C chemical shifts588
15N chemical shifts193
1H chemical shifts193

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Mdm2_aa111-333_1C1A_3C3S1

Entities:

Entity 1, Mdm2_aa111-333_1C1A_3C3S 224 residues - Formula weight is not available

1   GLYASNGLNGLNGLUSERSERASPSERGLY
2   THRSERVALSERGLUASNARGALAHISLEU
3   GLUGLYGLYSERASPGLNLYSASPLEUVAL
4   GLNGLULEUGLNGLUGLULYSPROSERSER
5   SERHISLEUVALSERARGPROSERTHRSER
6   SERARGARGARGALAILESERGLUTHRGLU
7   GLUASNSERASPGLULEUSERGLYGLUARG
8   GLNARGLYSARGHISLYSSERASPSERILE
9   SERLEUSERPHEASPGLUSERLEUALALEU
10   SERVALILEARGGLUILESERSERGLUARG
11   SERSERSERSERGLUSERTHRGLYTHRPRO
12   SERASNPROASPLEUASPALAGLYVALSER
13   GLUHISSERGLYASPTRPLEUASPGLNASP
14   SERVALSERASPGLNPHESERVALGLUPHE
15   GLUVALGLUSERLEUASPSERGLUASPTYR
16   SERLEUSERGLUGLUGLYGLNGLULEUSER
17   ASPGLUASPASPGLUVALTYRGLNVALTHR
18   VALTYRGLNALAGLYGLUSERASPTHRASP
19   SERPHEGLUGLUASPPROGLUILESERLEU
20   ALAASPTYRTRPLYSCYSTHRSERCYSASN
21   GLUMETASNPROPROLEUPROSERHISCYS
22   ASNARGCYSTRPALALEUARGGLUASNTRP
23   LEUPROGLUASP

Samples:

sample_1: Mdm2_aa111-333_1C1A_3C3S, [U-98% 13C; U-98% 15N], 200 ± 20 uM; D2O 3%; DSS 100 uM; sodium azide 0.05%; sodium chloride 150 mM; sodium phosphate 20 mM; cocktail protease inhibitors 4 tablet/100mL

sample_conditions_1: ionic strength: 0.19 M; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4 - chemical shift assignment

TOPSPIN v3.5pl7 - collection

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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