BMRB Entry 25873

Name: Free RSK1 683-735 peptide
Published: 2016-01-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25873

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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:

Free RSK1 683-735 peptide

Deposition date:

2015-10-30

Original release date:

2016-01-06

Authors:

Gogl, Gergo; Nyitray, Laszlo

Citation:

Citation: Gogl, Gergo; Alexa, Anita; Kiss, Bence; Katona, Gergely; Kovacs, Mihaly; Bodor, Andrea; Remenyi, Attila; Nyitray, Laszlo. "Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY" J. Biol. Chem. 291, 11-27 (2016).
PubMed: 26527685

Assembly members:

Assembly members:
RSK1, polymer, 55 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RSK1: GSQSQLSHQDLQLVKGAMAA TYSALNSSKPTPQLKPIESS ILAQRRVRKLPSTTL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	44
1H chemical shifts	44

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 55 residues - Formula weight is not available

1

GLY

SER

GLN

SER

GLN

LEU

SER

HIS

GLN

ASP

2

LEU

GLN

LEU

VAL

LYS

GLY

ALA

MET

ALA

3

THR

TYR

SER

ALA

LEU

ASN

SER

LYS

PRO

4

THR

PRO

GLN

LEU

LYS

PRO

ILE

GLU

SER

5

ILE

LEU

ALA

GLN

ARG

VAL

ARG

LYS

LEU

6

PRO

SER

THR

LEU

Samples:

sample_1: RSK1, [U-99% 15N], 0.9 ± 0.1 mM; NaCl 20 mM; MES buffer 20 mM; CaCl2 5 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 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