BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27894

Title: Backbone assignment of human FOXO1   PubMed: 31913281

Deposition date: 2019-05-08 Original release date: 2020-02-26

Authors: Hennig, Janosch; Hollmann, Nele Merret

Citation: Ibarra, Ignacio; Hollmann, Nele Merret; Klaus, Bernd; Augsten, Sandra; Velten, Britta; Hennig, Janosch; Zaugg, Judith. "Mechanistic insights into transcription factor cooperativity and its impact on protein-phenotype interactions"  Nat. Commun. 11, 124-124 (2020).

Assembly members:
FOXO1, polymer, 130 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: pETM-22

Entity Sequences (FASTA):
FOXO1: GPGPLAGQPRKSSSSRRNAW GNLSYADLITKAIESSAEKR LTLSQIYEWMVKSVPYFKDK GDSNSSAGWKNSIRHNLSLH SKFIRVQNEGTGKSSWWMLN PEGGKSGKSPRRRAASMDNN SKFAKSRSRA

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts106
1H chemical shifts106

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1FOXO11

Entities:

Entity 1, FOXO1 130 residues - Formula weight is not available

1   GLYPROGLYPROLEUALAGLYGLNPROARG
2   LYSSERSERSERSERARGARGASNALATRP
3   GLYASNLEUSERTYRALAASPLEUILETHR
4   LYSALAILEGLUSERSERALAGLULYSARG
5   LEUTHRLEUSERGLNILETYRGLUTRPMET
6   VALLYSSERVALPROTYRPHELYSASPLYS
7   GLYASPSERASNSERSERALAGLYTRPLYS
8   ASNSERILEARGHISASNLEUSERLEUHIS
9   SERLYSPHEILEARGVALGLNASNGLUGLY
10   THRGLYLYSSERSERTRPTRPMETLEUASN
11   PROGLUGLYGLYLYSSERGLYLYSSERPRO
12   ARGARGARGALAALASERMETASPASNASN
13   SERLYSPHEALALYSSERARGSERARGALA

Samples:

sample_1: FOXO1, [U-99% 13C; U-99% 15N], 0.25 mM; D2O, [U-99% 2H], 10%; bis-TRIS 50 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CARA, Fred Damberger - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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