BMRB Entry 31050

Name: Backbone modifications in the inter-helix loop of designed miniprotein oPPalpha: DPro10Gly11 turn
Published: 2023-03-28

Click here to enlarge.

PDB ID: 8es0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31050
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 modifications in the inter-helix loop of designed miniprotein oPPalpha: DPro10Gly11 turn

Deposition date:

2022-10-13

Original release date:

2023-03-28

Authors:

Harmon, T.; Horne, W.

Citation:

Citation: Harmon, T.; Horne, W.. "Protein Backbone Alteration in Non-Hairpin beta-Turns: Impacts on Tertiary Folded Structure and Folded Stability" Chembiochem 24, e202300113-e202300113 (2023).
PubMed: 36920327

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 3716.324 Da.

Natural source:

Natural source: Common Name: Streptococcus mutans Taxonomy ID: 1309 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus Streptococcus mutans

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XPPKKPKKPGXGATPEKLAA YEKELAAYEKELAAYX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	249

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 36 residues - 3716.324 Da.

1

ACE

PRO

LYS

PRO

LYS

PRO

GLY

2

DPR

GLY

ALA

THR

PRO

GLU

LYS

LEU

ALA

3

TYR

GLU

LYS

GLU

LEU

ALA

TYR

GLU

LYS

4

GLU

LEU

ALA

TYR

NH2

Samples:

sample_1: Designed miniprotein oPPalpha: DPro10Gly11 turn 2.8 mM; DSS 0.3 mM; sodium phosphate 8.2 mM; potassium phosphate 1.8 mM; sodium chloride 137 mM; potassium chloride 2.7 mM

sample_2: Designed miniprotein oPPalpha: DPro10Gly11 turn 3.7 mM; DSS 0.3 mM; sodium phosphate 8.2 mM; potassium phosphate 1.8 mM; sodium chloride 137 mM; potassium chloride 2.7 mM

sample_conditions_1: ionic strength: 163 mM; pH: 7.4 pH*; 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 COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

NMRFAM-SPARKY, Lee, Tonelli, Markley - data analysis

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

NMR spectrometers:

Bruker AVANCE 700 MHz