BMRB Entry 31089

Name: Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype
Published: 2023-09-23

Click here to enlarge.

PDB ID: 8t0g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31089
MolProbity Validation Chart

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:

Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype

Deposition date:

2023-06-01

Original release date:

2023-09-23

Authors:

Heath, S.; Horne, W.; Lengyel, G.

Citation:

Citation: Heath, S.; Horne, W.; Lengyel, G.. "Effects of chirality and side chain length in C alpha, alpha-dialkylated residues on beta-hairpin peptide folded structure and stability" Org. Biomol. Chem. 21, 6320-6324 (2023).
PubMed: 37503895

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, 1826.960 Da.

Natural source:

Natural source: Common Name: Streptococcus sp. group G Taxonomy ID: 1320 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus Streptococcus sp. group G

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEWAYNPATGKFAWTEX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 17 residues - 1826.960 Da.

1

GLY

GLU

TRP

ALA

TYR

ASN

PRO

ALA

THR

GLY

2

LYS

PHE

ALA

TRP

THR

GLU

NH2

Samples:

sample_1: GB1 C-terminal Hairpin Mutant: Ala13 variant 2 mM; sodium phosphate 50 mM; DSS 0.2 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.3 pH*; pressure: 1 atm; temperature: 298 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-1H COSY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE 700 MHz