BMRB Entry 51081

Title:
FOXO4 (aa 14-217)
Deposition date:
2021-09-08
Original release date:
2022-05-06
Authors:
Kohoutova, Klara
Citation:

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).
PubMed: 35481640

Assembly members:

Assembly members:
entity_1, polymer, 204 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

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts143
1H chemical shifts144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FOXO41

Entities:

Entity 1, FOXO4 204 residues - Formula weight is not available

1   GLYILEILEASPLEUASPPROASPPHEGLU
2   PROGLNSERARGPROARGSERCYSTHRTRP
3   PROLEUPROARGPROGLUILEALAASNGLN
4   PROSERGLUPROPROGLUVALGLUPROASP
5   LEUGLYGLULYSVALHISTHRGLUGLYARG
6   SERGLUPROILELEULEUPROSERARGLEU
7   PROGLUPROALAGLYGLYPROGLNPROGLY
8   ILELEUGLYALAVALTHRGLYPROARGLYS
9   GLYGLYSERARGARGASNALATRPGLYASN
10   GLNSERTYRALAGLULEUILESERGLNALA
11   ILEGLUSERALAPROGLULYSARGLEUTHR
12   LEUALAGLNILETYRGLUTRPMETVALARG
13   THRVALPROTYRPHELYSASPLYSGLYASP
14   SERASNSERSERALAGLYTRPLYSASNSER
15   ILEARGHISASNLEUSERLEUHISSERLYS
16   PHEILELYSVALHISASNGLUALATHRGLY
17   LYSSERSERTRPTRPMETLEUASNPROGLU
18   GLYGLYLYSSERGLYLYSALAPROARGARG
19   ARGALAALASERMETASPSERSERSERLYS
20   LEULEUARGGLYARGSERLYSALAPROLYS
21   LYSLYSPROSER

Samples:

sample_1: FOXO4, [U-13C; U-15N], 250 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 HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

TOPSPIN - 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 peaks
SPARKY: Backbone or all simulated peaks