BMRB Entry 30487

Name: Solution structure of Rbfox2 RRM mimetic peptide CPfox4
Published: 2019-05-07

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PDB ID: 6dza
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30487
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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:

Solution structure of Rbfox2 RRM mimetic peptide CPfox4

Deposition date:

2018-07-03

Original release date:

2019-05-07

Authors:

Sun, Y.-T.; Shortridge, M.; Varani, G.

Citation:

Citation: Sun, Yi-Ting; Shortridge, Matthew; Varani, Gabriele. "A Small Cyclic beta-Hairpin Peptide Mimics the Rbfox2 RNA Recognition Motif and Binds to the Precursor miRNA 20b." Chembiochem 20, 931-939 (2019).
PubMed: 30537200

Assembly members:

Assembly members:
entity_1, polymer, 16 residues, 1997.303 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 36630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSKRFRFXPEIIFNER

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	11
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 16 residues - 1997.303 Da.

1

GLY

SER

LYS

ARG

PHE

ARG

PHE

DPR

PRO

GLU

2

ILE

PHE

ASN

GLU

ARG

Samples:

sample_1: CPfox4 3.0 mg/mL; potassium phosphate 10 mM; potassium chloride 10 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 278 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 500 MHz

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