BMRB Entry 16706

Name: 1H, 13C, and 15N chemical shift assignments for H2H2, a mini prion protein
Published: 2010-03-31

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16706

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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:

1H, 13C, and 15N chemical shift assignments for H2H2, a mini prion protein

Deposition date:

2010-02-04

Original release date:

2010-03-31

Authors:

Pastore, Annalisa; Pauwels, Kris; Adrover, Miquel; de Chiara, Cesira; Prigent, Stephanie; Rezeai, Human

Citation:

Citation: Adrover, Miquel; Pauwels, Kris; Prigent, Stephanie; de Chiara, Cesira; Xu, Zhou; Chapuis, Celine; Pastore, Annalisa; Rezaei, Human. "Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3." J. Biol. Chem. 285, 21004-21012 (2010).
PubMed: 20375014

Assembly members:

Assembly members:
H2H3, polymer, 89 residues, 10227.3 Da.

Natural source:

Natural source: Common Name: sheep Taxonomy ID: 9940 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ovis aries

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H2H3: MGSSHHHHHHSSGLVPRGSH MRPVDQYSNQNNFVHDCVNI TVKQHTVTTTTKGENFTETD IKAMERVVEQMCITQYQRES QAYYQRGAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	194
15N chemical shifts	72
1H chemical shifts	420

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H2H3	1

Entities:

Entity 1, H2H3 89 residues - 10227.3 Da.

The first 21 residues represents a non-native his-tag. Residues 22-89 represent residues 167-234 of the native ovine PrP.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ARG

PRO

VAL

ASP

GLN

TYR

SER

ASN

GLN

4

ASN

PHE

VAL

HIS

ASP

CYS

VAL

ASN

ILE

5

THR

VAL

LYS

GLN

HIS

THR

VAL

THR

6

THR

LYS

GLY

GLU

ASN

PHE

THR

GLU

THR

ASP

7

ILE

LYS

ALA

MET

GLU

ARG

VAL

GLU

GLN

8

MET

CYS

ILE

THR

GLN

TYR

GLN

ARG

GLU

SER

9

GLN

ALA

TYR

GLN

ARG

GLY

ALA

SER

Samples:

sample_1: H2H3, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 10%; H2O 90%; sodium citrate 5 mM

sample_conditions_1: ionic strength: 0.006 M; pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
CBARO	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

ARIA vv2.2, Linge, O'Donoghue and Nilges - data analysis, geometry optimization, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Varian INOVA 600 MHz

PDB	2KTM
GB	AAQ81754 AIE40054