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 27764

Title: FoxM1 Transactivation Domain, Phosphorylated form   PubMed: 31134895

Deposition date: 2019-01-22 Original release date: 2019-06-13

Authors: Marceau, Aimee; Brison, Caileen; Nerli, Santrupti; Arsenault, Heather; McShane, Andrew; Chen, Eefei; Lee, Hsiau-Wei; Benanti, Jennifer; Sgourakis, Nikolaos; Rubin, Seth

Citation: Marceau, Aimee; Brison, Caileen; Nerli, Santrupti; Arsenault, Heather; McShane, Andrew; Chen, Eefei; Lee, Hsiau-Wei; Benanti, Jennifer; Sgourakis, Nikolaos; Rubin, Seth. "An order-to-disorder structural switch activates the FoxM1 transcription factor."  Elife 8, e46131-e46131 (2019).

Assembly members:
Phosphorylated_FoxM1_TAD, polymer, 55 residues, Formula weight is not available

Natural source:   Common Name: zebrafish   Taxonomy ID: 7955   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Danio rerio

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEV

Entity Sequences (FASTA):
Phosphorylated_FoxM1_TAD: GEFGAANRXLTEGFVLDTMN DXLSKILVDIXFSGLEDEDL GMGNISWXQFIPELK

Data typeCount
13C chemical shifts153
15N chemical shifts54
1H chemical shifts55

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Phosphorylated FoxM1 TAD1

Entities:

Entity 1, Phosphorylated FoxM1 TAD 55 residues - Formula weight is not available

1   GLYGLUPHEGLYALAALAASNARGSEPLEU
2   THRGLUGLYPHEVALLEUASPTHRMETASN
3   ASPSEPLEUSERLYSILELEUVALASPILE
4   SEPPHESERGLYLEUGLUASPGLUASPLEU
5   GLYMETGLYASNILESERTRPSEPGLNPHE
6   ILEPROGLULEULYS

Samples:

sample_1: Phosphorylated FoxM1 TAD, [U-100% 13C; U-100% 15N], 450 mM; sodium chloride 100 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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