BMRB Entry 51333

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51333

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Title:
Structural insights into the mechanism of p53 regulation by MDM2 acidic domain
Deposition date:
2022-02-19
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, 221 residues, Formula weight is not available
entity_2, polymer, 86 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-32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HMSSSVPSQKTYQGSYGFRL GFLHSGTAKSVTCTYSPALN KMFCQLAKTCPVQLWVDSTP PPGTRVRAMAIYKQSQHMTE VVRRCPHHERCSDSDGLAPP QHLIRVEGNLRVEYLDDRNT FRHSVVVPYEPPEVGSDCTT IHYNYMCNSSCMGGMNRRPI LTIITLEDSSGNLLGRNSFE VRVCACPGRDRRTEEENLRK KGEPHHELPPGSTKRALPNN T
entity_2: STGTPSNPDLDAGVSEHSGD WLDQDSVSDQFSVEFEVESL DSEDYSLSEEGQELSDEDDE VYQVTVYQAGESDTDSFEED PEISLA

Data sets:
Data typeCount
13C chemical shifts559
15N chemical shifts195
1H chemical shifts194

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p53 DBD1
2MDM2 AD2

Entities:

Entity 1, p53 DBD 221 residues - Formula weight is not available

1   HISMETSERSERSERVALPROSERGLNLYS
2   THRTYRGLNGLYSERTYRGLYPHEARGLEU
3   GLYPHELEUHISSERGLYTHRALALYSSER
4   VALTHRCYSTHRTYRSERPROALALEUASN
5   LYSMETPHECYSGLNLEUALALYSTHRCYS
6   PROVALGLNLEUTRPVALASPSERTHRPRO
7   PROPROGLYTHRARGVALARGALAMETALA
8   ILETYRLYSGLNSERGLNHISMETTHRGLU
9   VALVALARGARGCYSPROHISHISGLUARG
10   CYSSERASPSERASPGLYLEUALAPROPRO
11   GLNHISLEUILEARGVALGLUGLYASNLEU
12   ARGVALGLUTYRLEUASPASPARGASNTHR
13   PHEARGHISSERVALVALVALPROTYRGLU
14   PROPROGLUVALGLYSERASPCYSTHRTHR
15   ILEHISTYRASNTYRMETCYSASNSERSER
16   CYSMETGLYGLYMETASNARGARGPROILE
17   LEUTHRILEILETHRLEUGLUASPSERSER
18   GLYASNLEULEUGLYARGASNSERPHEGLU
19   VALARGVALCYSALACYSPROGLYARGASP
20   ARGARGTHRGLUGLUGLUASNLEUARGLYS
21   LYSGLYGLUPROHISHISGLULEUPROPRO
22   GLYSERTHRLYSARGALALEUPROASNASN
23   THR

Entity 2, MDM2 AD 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

Samples:

sample_1: p53 DBD, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM; MDM2 AD 600 uM; D2O, [U-99% 2H], 10%; H2O 90%; DSS 1 mM; sodium chloride 40 mM; sodium phosphate 20 mM; TCEP 1 mM; sodium azide 0.05 % w/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 TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis, peak picking

NMRPipe - 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