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 50398

Title: Backbone/side_chain assignment of human FOXO4 86_207   PubMed: 34320339

Deposition date: 2020-07-21 Original release date: 2021-08-11

Authors: Bourgeois, Benjamin; Madl, Tobias

Citation: Bourgeois, Benjamin; Gui, Tianshu; Hoogeboom, Diana; Hocking, Henry; Richter, Gesa; Spreitzer, Emil; Viertler, Martin; Richter, Klaus; Madl, Tobias; Burgering, Boudewijn. "Multiple regulatory intrinsically disordered motifs control FOXO4 transcription factor binding and function"  Cell Rep. 36, 109446-109446 (2021).

Assembly members:
entity_1, polymer, 125 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: pETZ2_1a

Entity Sequences (FASTA):
entity_1: GAMGAVTGPRKGGSRRNAWG NQSYAELISQAIESAPEKRL TLAQIYEWMVRTVPYFKDKG DSNSSAGWKNSIRHNLSLHS KFIKVHNEATGKSSWWMLNP EGGKSGKAPRRRAASMDSSS KLLRG

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts123
1H chemical shifts657

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human FOXO4 86_2071

Entities:

Entity 1, human FOXO4 86_207 125 residues - Formula weight is not available

1   GLYALAMETGLYALAVALTHRGLYPROARG
2   LYSGLYGLYSERARGARGASNALATRPGLY
3   ASNGLNSERTYRALAGLULEUILESERGLN
4   ALAILEGLUSERALAPROGLULYSARGLEU
5   THRLEUALAGLNILETYRGLUTRPMETVAL
6   ARGTHRVALPROTYRPHELYSASPLYSGLY
7   ASPSERASNSERSERALAGLYTRPLYSASN
8   SERILEARGHISASNLEUSERLEUHISSER
9   LYSPHEILELYSVALHISASNGLUALATHR
10   GLYLYSSERSERTRPTRPMETLEUASNPRO
11   GLUGLYGLYLYSSERGLYLYSALAPROARG
12   ARGARGALAALASERMETASPSERSERSER
13   LYSLEULEUARGGLY

Samples:

sample_1: human FOXO4, [U-99% 13C; U-99% 15N], 500 uM; TRIS 50 mM; sodium chloride 150 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCACONHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

TOPSPIN - processing

NMR spectrometers:

  • Bruker AVANCE III 900 MHz

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