BMRB Entry 34884

Name: Structure of peptide CpRE12 bound to DPC micelle
Published: 2024-12-02

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PDB ID: 8r89
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34884
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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:

Structure of peptide CpRE12 bound to DPC micelle

Deposition date:

2023-11-28

Original release date:

2024-12-02

Authors:

Kornilov, F.; Taldaev, A.; Bashkirov, P.; Bocharov, E.

Citation:

Citation: Serebrennikova, M.; Latsis, I.; Maltsev, D.; Grafskaia, E.; Kornilov, F.; Taldaev, A.; Bashkirov, P.; Bocharov, E.; Lazarev, V.. "In silico prediction and analysis of novel cell-penetrating peptide" .

Assembly members:

Assembly members:
entity_1, polymer, 18 residues, 2137.310 Da.

Natural source:

Natural source: Common Name: jellyfishes Taxonomy ID: 499914 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rhopilema esculentum

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SYQWQIFYRSLDGSGAKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	54
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 18 residues - 2137.310 Da.

1

SER

TYR

GLN

TRP

GLN

ILE

PHE

TYR

ARG

SER

2

LEU

ASP

GLY

SER

GLY

ALA

LYS

GLU

Samples:

sample_1: CpRE12 peptide 1.5 mM; DPC, [U-98% 2H], 300 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.2; pressure: 1 atm; temperature: 303 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-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - processing

MOLMOL, Koradi, Billeter and Wuthrich - data analysis

PyMOL, schrodinger - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz