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 26786

Title: Elk1 C-terminus aa309-429 - 8 phosphorylated sites (pS337-pT354-pT364-pT369-pS384-pS390-pT418-pS423)   PubMed: 27738173

Authors: Theillet, Francois; Selenko, Philipp; Mylona, Anastasia; Treisman, Richard

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).

Assembly members:
pElk1, polymer, 122 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
pElk1: GTQPQKGRKPRDLELPLSPS LLGGQGPERXPGSGTSSGLQ APGPALXPSLLPTHTLXPVL LXPSSLPPSIHFWSTLXPIA PRXPAKLSFQFPSSGSAQVH IPSISVDGLSXPVVLXPGPQ KP

Data sets:
Data typeCount
13C chemical shifts318
15N chemical shifts94
1H chemical shifts94

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1pElk11

Entities:

Entity 1, pElk1 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   LEULEUGLYGLYGLNGLYPROGLUARGSEP
4   PROGLYSERGLYTHRSERSERGLYLEUGLN
5   ALAPROGLYPROALALEUTPOPROSERLEU
6   LEUPROTHRHISTHRLEUTPOPROVALLEU
7   LEUTPOPROSERSERLEUPROPROSERILE
8   HISPHETRPSERTHRLEUSEPPROILEALA
9   PROARGSEPPROALALYSLEUSERPHEGLN
10   PHEPROSERSERGLYSERALAGLNVALHIS
11   ILEPROSERILESERVALASPGLYLEUSER
12   TPOPROVALVALLEUSEPPROGLYPROGLN
13   LYSPRO

Samples:

sample_pElk1: pElk1, [U-99% 13C; U-99% 15N], 300 uM; sodium phosphate 10 mM; sodium chloride 50 mM; ATP 5 mM; DSS 0.5 mM; magnesium chloride 5 mM; Erk2 kinase 0.05 ug; DTT 2 mM; glycerol 1 % v/v

sample_conditions_1: ionic strength: 60 mM; pH: 6.9; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_pElk1isotropicsample_conditions_1
3D HNCOsample_pElk1isotropicsample_conditions_1
3D HNCACBsample_pElk1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

CcpNMR_Analysis v2.4, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links: