BMRB Entry 27214

Name: RSK1 phosphorylated C-terminal peptide (696-735)
Published: 2017-10-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27214

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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:

RSK1 phosphorylated C-terminal peptide (696-735)

Deposition date:

2017-08-10

Original release date:

2017-10-31

Authors:

Gogl, Gergo; Nyitray, Laszlo

Citation:

Citation: Gogl, Gergo; Biri-Kovacs, Beata; Poti, Adam Levente; Vadaszi, Henrietta; Szeder, Balint; Bodor, Andrea; Schlosser, Gitta; Acs, Andras; Turiak, Lilla; Buday, Laszlo; Alexa, Anita; Nyitray, Laszlo; Remenyi, Attila. "Dynamic control of RSK complexes by phosphoswitch-based regulation" FEBS J. 85, 46-71 (2017).
PubMed: 29083550

Assembly members:

Assembly members:
RSK1_peptide, polymer, 42 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: petara

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RSK1_peptide: GSGAMAATYSALNSSKPTPQ LKPIESSILAQRRVRKLPXT TL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	35
1H chemical shifts	35

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RSK1 peptide	1

Entities:

Entity 1, RSK1 peptide 42 residues - Formula weight is not available

1

GLY

SER

GLY

ALA

MET

ALA

THR

TYR

SER

2

ALA

LEU

ASN

SER

LYS

PRO

THR

PRO

GLN

3

LEU

LYS

PRO

ILE

GLU

SER

ILE

LEU

ALA

4

GLN

ARG

VAL

ARG

LYS

LEU

PRO

SEP

THR

5

THR

LEU

Samples:

sample_1: RSK1 peptide, [U-99% 13C; U-99% 15N], 0.7 mM; sodium chloride 20 mM; HEPES 20 mM; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.75; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

Sparky, Goddard - data analysis

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