BMRB Entry 50709

Name: RGG Mini
Published: 2021-11-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50709

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

RGG Mini

Deposition date:

2021-01-15

Original release date:

2021-11-14

Authors:

Mompean, Miguel; Laurents, Douglas

Citation:

Citation: Mompean, Miguel; Oroz, Javier; Laurents, Douglas. "Do polyproline II helix associations modulate biomolecular condensates?" FEBS Open Bio 11, 2390-2399 (2021).
PubMed: 33934561

Assembly members:

Assembly members:
entity_1, polymer, 18 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XRGGYGGRGGWGGRGGYX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	82
15N chemical shifts	1
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RGG mini	1

Entities:

Entity 1, RGG mini 18 residues - Formula weight is not available

The peptide is N-acetylated and C-amidated.

1

ACE

ARG

GLY

TYR

GLY

ARG

GLY

2

TRP

GLY

ARG

GLY

TYR

NH2

Samples:

sample_1: RGG mini 6.1 ± 0.2 mM; DSS 0.05 ± 0.005 mM

sample_conditions_1: ionic strength: 10 mM; pH: 2.7; pressure: 0.92 atm; temperature: 278.2 K

sample_conditions_2: ionic strength: 10 mM; pH: 9.95; pressure: 0.92 atm; temperature: 278.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
1D 1H	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_2
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2

Software:

TOPSPIN v4.0.8 - collection, processing

NMRFAM-SPARKY v3.13 - chemical shift assignment, peak picking

CYANA - structure solution

NMR spectrometers:

Bruker AVANCE NEO 600 MHz
Bruker AVANCE NEO 800 MHz