BMRB Entry 17558

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17558
MolProbity Validation Chart

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Title:
Structure of the CHR of the Prion protein in DPC Micelles
Deposition date:
2011-03-31
Original release date:
2011-12-05
Authors:
Sauve, Simon; Aubin, Yves
Citation:

Citation: Sauve, Simon; Buijs, Daniel; Gingras, Genevieve; Aubin, Yves. "Interactions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine Micelles."  J. Biol. Chem. 287, 1915-1922 (2012).
PubMed: 22128151

Assembly members:

Assembly members:
PrP_Conserved_Hydrophobic_Domain, polymer, 27 residues, Formula weight is not available
DPV, non-polymer, 351.462 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET19b-GST

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PrP_Conserved_Hydrophobic_Domain: KHMAGAAAAGAVVGGLGGYM LGSAMSR

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts25
1H chemical shifts141

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1peptide1
2micelle2

Entities:

Entity 1, peptide 27 residues - Formula weight is not available

Residues 1-27 represents the sequence 110-136 in the mature polypeptide sequence of the human PrP protein

1   LYSHISMETALAGLYALAALAALAALAGLY
2   ALAVALVALGLYGLYLEUGLYGLYTYRMET
3   LEUGLYSERALAMETSERARG

Entity 2, micelle - C17 H38 N O4 P - 351.462 Da.

1   DPV

Samples:

sample_1: PrP Conserved Hydrophobic Domain, [U-99% 13C; U-99% 15N], 1.5 mg; Dodecylphosphocholine (DPC) Micelle 14 mg; sodium phosphate 10 mM; DSS 1 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7.6; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

TALOS v+, Cornilescu, Delaglio and Bax - chemical shift calculation

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance III 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16743 17034 17714 17756 17757 17780 18426 18550 19268 4307 4402 4434 4641
PDB
DBJ BAD51981 BAE91721 BAF62360 BAG32276 BAG32278
EMBL CAA58442 CAH92912
GB AAA37014 AAA37090 AAA37091 AAA37092 AAA37093
PIR B34759
REF NP_000302 NP_001009093 NP_001040617 NP_001073590 NP_001073591
SP O18754 P04156 P04273 P40245 P40246
TPE CAJ43807 CAJ43808
AlphaFold O18754 P04156 P04273 P40245 P40246

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