BMRB Entry 27939

Title:
NMR backbone assignment of full-length human phosphorylated 4E-BP1 T70E mutant
Deposition date:
2019-06-06
Original release date:
2021-04-21
Authors:
Boehm, Raphael; Hiller, Sebastian
Citation:

Citation: Boehm, Raphael; Imseng, Stefan; Jakob, Roman; Hall, Michael; Maier, Timm; Hiller, Sebastian. "The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1"  Mol. Cell 81, 2403-2416 (2021).
PubMed: 33852892

Assembly members:

Assembly members:
phosphorylated_4E-BP1, polymer, 119 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 shifts213
15N chemical shifts98
1H chemical shifts98

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
14E-BP11

Entities:

Entity 1, 4E-BP1 119 residues - Formula weight is not available

1   GLYMETSERGLYGLYSERSERCYSSERGLN
2   THRPROSERARGALAILEPROALATHRARG
3   ARGVALVALLEUGLYASPGLYVALGLNLEU
4   PROPROGLYASPTYRSERTHRTHRPROGLY
5   GLYTHRLEUPHESERTHRTHRPROGLYGLY
6   THRARGILEILETYRASPARGLYSPHELEU
7   METGLUCYSARGASNSERPROVALTHRLYS
8   GLUPROPROARGASPLEUPROTHRILEPRO
9   GLYVALTHRSERPROSERSERASPGLUPRO
10   PROMETGLUALASERGLNSERHISLEUARG
11   ASNSERPROGLUASPLYSARGALAGLYGLY
12   GLUGLUSERGLNPHEGLUMETASPILE

Samples:

sample_1: phosphorylated 4E-BP1, [U-99% 13C; U-99% 15N], 250 uM; sodium phosphate 30 mM; sodium chloride 160 mM; EDTA 1 mM; DTT 10 mM

sample_conditions_1: ionic strength: 0.19 M; pH: 6; pressure: 1 atm; temperature: 293.15 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 700 MHz

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