BMRB Entry 16706
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16706
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Title: 1H, 13C, and 15N chemical shift assignments for H2H2, a mini prion protein PubMed: 20375014
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: 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).
Assembly members:
H2H3, polymer, 89 residues, 10227.3 Da.
Natural source: Common Name: sheep Taxonomy ID: 9940 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ovis aries
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
H2H3: MGSSHHHHHHSSGLVPRGSH
MRPVDQYSNQNNFVHDCVNI
TVKQHTVTTTTKGENFTETD
IKAMERVVEQMCITQYQRES
QAYYQRGAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 194 |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 420 |
Additional metadata:
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 | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ARG | PRO | VAL | ASP | GLN | TYR | SER | ASN | GLN | ||||
| 4 | ASN | ASN | PHE | VAL | HIS | ASP | CYS | VAL | ASN | ILE | ||||
| 5 | THR | VAL | LYS | GLN | HIS | THR | VAL | THR | THR | THR | ||||
| 6 | THR | LYS | GLY | GLU | ASN | PHE | THR | GLU | THR | ASP | ||||
| 7 | ILE | LYS | ALA | MET | GLU | ARG | VAL | VAL | GLU | GLN | ||||
| 8 | MET | CYS | ILE | THR | GLN | TYR | GLN | ARG | GLU | SER | ||||
| 9 | GLN | ALA | TYR | 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, . - data analysis, geometry optimization, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts