BMRB Entry 26762

Title:
Elk1 C-terminus aa309-429
Deposition date:
2016-03-20
Original release date:
2017-08-24
Authors:
Theillet, Francois; Selenko, Philipp; Mylona, Anastasia; Treisman, Richard
Citation:

Citation: Mylona, Anastasia; Theillet, Francois-Xavier; Foster, Charles; Cheng, Tammy; Miralles, Francesc; Bates, Paul; Selenko, Philipp; Treisman, Richard. "Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation"  Science 354, 233-237 (2016).
PubMed: 27738173

Assembly members:

Assembly members:
Elk1, polymer, 122 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-29

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Elk11

Entities:

Entity 1, Elk1 122 residues - Formula weight is not available

There is one supplementary glycine at the N-terminus (for improved TEV cleavage of the initial construct).

1   GLYTHRGLNPROGLNLYSGLYARGLYSPRO
2   ARGASPLEUGLULEUPROLEUSERPROSER
3   LEULEUGLYGLYGLNGLYPROGLUARGTHR
4   PROGLYSERGLYTHRSERSERGLYLEUGLN
5   ALAPROGLYPROALALEUTHRPROSERLEU
6   LEUPROTHRHISTHRLEUTHRPROVALLEU
7   LEUTHRPROSERSERLEUPROPROSERILE
8   HISPHETRPSERTHRLEUSERPROILEALA
9   PROARGSERPROALALYSLEUSERPHEGLN
10   PHEPROSERSERGLYSERALAGLNVALHIS
11   ILEPROSERILESERVALASPGLYLEUSER
12   THRPROVALVALLEUSERPROGLYPROGLN
13   LYSPRO

Samples:

sample_1: Elk1, [U-99% 13C; U-99% 15N], 400 uM; Na phosphate 10 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

CcpNMR_Analysis v2.4, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz

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