BMRB Entry 26786

Name: Elk1 C-terminus aa309-429 - 8 phosphorylated sites (pS337-pT354-pT364-pT369-pS384-pS390-pT418-pS423)
Published: 2017-08-24

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26786

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2016-04-25

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:
pElk1, 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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	318
15N chemical shifts	94
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pElk1	1

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

GLY

THR

GLN

PRO

GLN

LYS

GLY

ARG

LYS

PRO

2

ARG

ASP

LEU

GLU

LEU

PRO

LEU

SER

PRO

SER

3

LEU

GLY

GLN

GLY

PRO

GLU

ARG

SEP

4

PRO

GLY

SER

GLY

THR

SER

GLY

LEU

GLN

5

ALA

PRO

GLY

PRO

ALA

LEU

TPO

PRO

SER

LEU

6

LEU

PRO

THR

HIS

THR

LEU

TPO

PRO

VAL

LEU

7

LEU

TPO

PRO

SER

LEU

PRO

SER

ILE

8

HIS

PHE

TRP

SER

THR

LEU

SEP

PRO

ILE

ALA

9

PRO

ARG

SEP

PRO

ALA

LYS

LEU

SER

PHE

GLN

10

PHE

PRO

SER

GLY

SER

ALA

GLN

VAL

HIS

11

ILE

PRO

SER

ILE

SER

VAL

ASP

GLY

LEU

SER

12

TPO

PRO

VAL

LEU

SEP

PRO

GLY

PRO

GLN

13

LYS

PRO

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_pElk1	isotropic	sample_conditions_1
3D HNCO	sample_pElk1	isotropic	sample_conditions_1
3D HNCACB	sample_pElk1	isotropic	sample_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