BMRB Entry 51335

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51335

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Title:
MDM2 AD in complex with p53 DBD
Deposition date:
2022-02-20
Original release date:
2022-10-11
Authors:
Song, Qinyan; Rainey, Jan; Liu, Paul
Citation:

Citation: Song, Qinyan; Liu, Xiang-Qin; Rainey, Jan. "The MDMX acidic domain competes with the p53 transactivation domain for MDM2 N-terminal domain binding"  Biochim. Biophys. Acta Mol. Cell Res. 1869, 119319-119319 (2022).
PubMed: 35780910

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, Formula weight is not available
entity_2, polymer, 223 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

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-32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STGTPSNPDLDAGVSEHSGD WLDQDSVSDQFSVEFEVESL DSEDYSLSEEGQELSDEDDE VYQVTVYQAGESDTDSFEED PEISLA
entity_2: GSHMSSSVPSQKTYQGSYGF RLGFLHSGTAKSVTCTYSPA LNKMFCQLAKTCPVQLWVDS TPPPGTRVRAMAIYKQSQHM TEVVRRCPHHERCSDSDGLA PPQHLIRVEGNLRVEYLDDR NTFRHSVVVPYEPPEVGSDC TTIHYNYMCNSSCMGGMNRR PILTIITLEDSSGNLLGRNS FEVRVCVCPGRDRRTEEENL RKKGEPHHELPPGSTKRALP NNT

Data sets:
Data typeCount
13C chemical shifts159
15N chemical shifts76
1H chemical shifts76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MDM2 Acid Domain1
2p53 DBD2
3Zinc3

Entities:

Entity 1, MDM2 Acid Domain 86 residues - Formula weight is not available

1   SERTHRGLYTHRPROSERASNPROASPLEU
2   ASPALAGLYVALSERGLUHISSERGLYASP
3   TRPLEUASPGLNASPSERVALSERASPGLN
4   PHESERVALGLUPHEGLUVALGLUSERLEU
5   ASPSERGLUASPTYRSERLEUSERGLUGLU
6   GLYGLNGLULEUSERASPGLUASPASPGLU
7   VALTYRGLNVALTHRVALTYRGLNALAGLY
8   GLUSERASPTHRASPSERPHEGLUGLUASP
9   PROGLUILESERLEUALA

Entity 2, p53 DBD 223 residues - Formula weight is not available

1   GLYSERHISMETSERSERSERVALPROSER
2   GLNLYSTHRTYRGLNGLYSERTYRGLYPHE
3   ARGLEUGLYPHELEUHISSERGLYTHRALA
4   LYSSERVALTHRCYSTHRTYRSERPROALA
5   LEUASNLYSMETPHECYSGLNLEUALALYS
6   THRCYSPROVALGLNLEUTRPVALASPSER
7   THRPROPROPROGLYTHRARGVALARGALA
8   METALAILETYRLYSGLNSERGLNHISMET
9   THRGLUVALVALARGARGCYSPROHISHIS
10   GLUARGCYSSERASPSERASPGLYLEUALA
11   PROPROGLNHISLEUILEARGVALGLUGLY
12   ASNLEUARGVALGLUTYRLEUASPASPARG
13   ASNTHRPHEARGHISSERVALVALVALPRO
14   TYRGLUPROPROGLUVALGLYSERASPCYS
15   THRTHRILEHISTYRASNTYRMETCYSASN
16   SERSERCYSMETGLYGLYMETASNARGARG
17   PROILELEUTHRILEILETHRLEUGLUASP
18   SERSERGLYASNLEULEUGLYARGASNSER
19   PHEGLUVALARGVALCYSVALCYSPROGLY
20   ARGASPARGARGTHRGLUGLUGLUASNLEU
21   ARGLYSLYSGLYGLUPROHISHISGLULEU
22   PROPROGLYSERTHRLYSARGALALEUPRO
23   ASNASNTHR

Entity 3, Zinc - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: MDM2 AD, [U-95% 13C; U-95% 15N], 300 uM; p53DBD 330 uM; D2O, [U-99% 2H], 10%; H2O 90%; DSS 1 mM; sodium azide 0.05 % w/v; sodium chloride 40 mM; sodium phosphate 20 mM; TCEP 1 mM

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 TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis, peak picking

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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