BMRB Entry 17558

Name: Structure of the CHR of the Prion protein in DPC Micelles
Published: 2011-12-05

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PDB ID: 2lbg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17558
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of the CHR of the Prion protein in DPC Micelles PubMed: 22128151

Deposition date: 2011-03-31 Original release date: 2011-12-05

Authors: Sauve, Simon; Aubin, Yves

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).

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

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
PrP_Conserved_Hydrophobic_Domain: KHMAGAAAAGAVVGGLGGYM LGSAMSR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	90
15N chemical shifts	25
1H chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	peptide	1
2	micelle	2

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

LYS

HIS

MET

ALA

GLY

ALA

GLY

2

ALA

VAL

GLY

LEU

GLY

TYR

MET

3

LEU

GLY

SER

ALA

MET

SER

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_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

BMRB	16743 17034 17714 17756 17757 17780 18426 18550 19268 4307 4402 4434 4641
PDB	1B10 1FKC 1FO7 1I4M 1QLX 1QLZ 1QM0 1QM1 1XYJ 1XYK 1XYQ 1XYU 1XYW 1XYX 1Y15 1Y16 2KUN 2LBG 2LEJ 2LFT 2LSB 2LV1 2M8T 2W9E 3HEQ 3HES 4DGI 4H88 4HLS 4HMM 4HMR 4KML 4N9O 4YXK 4YXL
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

Biological Magnetic Resonance Data Bank