BMRB Entry 25022

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

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Title:
Polyglutamine binding peptide 1 (QBP1)
Deposition date:
2014-06-16
Original release date:
2014-09-18
Authors:
Laurents, Douglas
Citation:

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).
PubMed: 25009140

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Polyglutamine_binding_peptide_1: XWKWWPGIFX

Data sets:
Data typeCount
1H chemical shifts73
13C chemical shifts44
15N chemical shifts11

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Polyglutamine binding peptide 1 (QBP1)1

Entities:

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

1   ACETRPLYSTRPTRPPROGLYILEPHEAMD

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:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aromaticsample_2isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks