BMRB Entry 25022

Name: Polyglutamine binding peptide 1 (QBP1)
Published: 2014-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25022

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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: Polyglutamine binding peptide 1 (QBP1) PubMed: 25009140

Deposition date: 2014-06-16 Original release date: 2014-09-18

Authors: Laurents, Douglas

Citation: Ramos-Martin, Francisco; Hervas, Ruben; Carrion-Vazquez, Mariano; Laurents, Douglas. "NMR spectroscopy reveals a preferred conformation with a defined hydrophobic cluster for polyglutamine binding peptide 1." Arch. Biochem. Biophys. 558, 104-110 (2014).

Assembly members:
Polyglutamine_binding_peptide_1, polymer, 10 residues, Formula weight is not available

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

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
Polyglutamine_binding_peptide_1: XWKWWPGIFX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	73
13C chemical shifts	44
15N chemical shifts	11

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Polyglutamine binding peptide 1 (QBP1)	1

Entities:

Entity 1, Polyglutamine binding peptide 1 (QBP1) 10 residues - Formula weight is not available

1

ACE

TRP

LYS

TRP

PRO

GLY

ILE

PHE

AMD

Samples:

sample_1: Polyglutamine binding peptide 1 0.75 mM; DSS 0.05 mM; potassium dihydrogen phosphate 10 mM; H2O 90%; D2O 10%

sample_2: Polyglutamine binding peptide 1 0.75 mM; DSS 0.05 mM; potassium dihydrogen phosphate 10 mM; D2O 100%

sample_conditions_1: temperature: 278 K; pH: 6.9; pressure: 1 atm; ionic strength: 0.02 M

sample_conditions_2: temperature: 278 K; pH: 6.9; pressure: 1 atm; ionic strength: 0.02 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_2

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

Bruker AMX 600 MHz
Bruker Avance 800 MHz

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