BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51332

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51332

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Title: Structural insights into the mechanism of p53 regulation by MDM2 acidic domain   PubMed: 35780910

Deposition date: 2022-02-19 Original release date: 2022-10-11

Authors: Song, Qinyan; Rainey, Jan; Liu, Paul

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).

Assembly members:
entity_1, polymer, 221 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32

Entity Sequences (FASTA):
entity_1: HMSSSVPSQKTYQGSYGFRL GFLHSGTAKSVTCTYSPALN KMFCQLAKTCPVQLWVDSTP PPGTRVRAMAIYKQSQHMTE VVRRCPHHERCSDSDGLAPP QHLIRVEGNLRVEYLDDRNT FRHSVVVPYEPPEVGSDCTT IHYNYMCNSSCMGGMNRRPI LTIITLEDSSGNLLGRNSFE VRVCACPGRDRRTEEENLRK KGEPHHELPPGSTKRALPNN T

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts199
1H chemical shifts198

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1p53 DNA-binding domain1

Entities:

Entity 1, p53 DNA-binding domain 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

Samples:

sample_1: p53 DNA-binding domain, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM; H2O 90%; D2O, [U-99% 2H], 10%; DSS 1 mM; TCEP 1 mM; sodium azide 0.05 % w/v; sodium phosphate 20 mM; sodium chloride 40 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
1D 1Hsample_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 shifts
SPARKY: Backbone or all simulated shifts