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Biological Magnetic Resonance Data Bank


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BMRB Entry 50960

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50960

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Title: The N-terminal region of human p53 (residues 1-312)   PubMed: 35481640

Deposition date: 2021-06-04 Original release date: 2022-05-06

Authors: Kohoutova, Klara

Citation: Mandal, Raju; Kohoutova, Klara; Petrvalska, Olivia; Horvath, Matej; Srb, Pavel; Veverka, Vaclav; Obsilova, Veronika; Obsil, Tomas. "FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA"  Protein Sci. 31, e4287-e4287 (2022).

Assembly members:
entity_1, polymer, 312 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

Entity Sequences (FASTA):
entity_1: MEEPQSDPSVEPPLSQETFS DLWKLLPENNVLSPLPSQAM DDLMLSPDDIEQWFTEDPGP DEAPRMPEAAPPVAPAPAAP TPAAPAPAPSWPLSSSVPSQ KTYQGSYGFRLGFLHSGTAK SVTCTYSPALNKMFCQLAKT CPVQLWVDSTPPPGTRVRAM AIYKQSQHMTEVVRRCPHHE RCSDSDGLAPPQHLIRVEGN LRVEYLDDRNTFRHSVVVPY EPPEVGSDCTTIHYNYMCNS SCMGGMNRRPILTIITLEDS SGNLLGRNSFEVRVCACPGR DRRTEEENLRKKGEPHHELP PGSTKRALPNNT

Data sets:
Data typeCount
13C chemical shifts781
15N chemical shifts225
1H chemical shifts225

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p531

Entities:

Entity 1, p53 312 residues - Formula weight is not available

1   METGLUGLUPROGLNSERASPPROSERVAL
2   GLUPROPROLEUSERGLNGLUTHRPHESER
3   ASPLEUTRPLYSLEULEUPROGLUASNASN
4   VALLEUSERPROLEUPROSERGLNALAMET
5   ASPASPLEUMETLEUSERPROASPASPILE
6   GLUGLNTRPPHETHRGLUASPPROGLYPRO
7   ASPGLUALAPROARGMETPROGLUALAALA
8   PROPROVALALAPROALAPROALAALAPRO
9   THRPROALAALAPROALAPROALAPROSER
10   TRPPROLEUSERSERSERVALPROSERGLN
11   LYSTHRTYRGLNGLYSERTYRGLYPHEARG
12   LEUGLYPHELEUHISSERGLYTHRALALYS
13   SERVALTHRCYSTHRTYRSERPROALALEU
14   ASNLYSMETPHECYSGLNLEUALALYSTHR
15   CYSPROVALGLNLEUTRPVALASPSERTHR
16   PROPROPROGLYTHRARGVALARGALAMET
17   ALAILETYRLYSGLNSERGLNHISMETTHR
18   GLUVALVALARGARGCYSPROHISHISGLU
19   ARGCYSSERASPSERASPGLYLEUALAPRO
20   PROGLNHISLEUILEARGVALGLUGLYASN
21   LEUARGVALGLUTYRLEUASPASPARGASN
22   THRPHEARGHISSERVALVALVALPROTYR
23   GLUPROPROGLUVALGLYSERASPCYSTHR
24   THRILEHISTYRASNTYRMETCYSASNSER
25   SERCYSMETGLYGLYMETASNARGARGPRO
26   ILELEUTHRILEILETHRLEUGLUASPSER
27   SERGLYASNLEULEUGLYARGASNSERPHE
28   GLUVALARGVALCYSALACYSPROGLYARG
29   ASPARGARGTHRGLUGLUGLUASNLEUARG
30   LYSLYSGLYGLUPROHISHISGLULEUPRO
31   PROGLYSERTHRLYSARGALALEUPROASN
32   ASNTHR

Samples:

sample_1: p53_fragment, [U-100% 13C; U-100% 15N; U-80% 2H], 290 uM; TRIS 25 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 175 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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