BMRB Entry 26925
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26925
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Title: 13C and 15N Chemical Shift Assignments for human Y145Stop Prion Protein Amyloid Fibrils PubMed: 28004358
Deposition date: 2016-10-26 Original release date: 2017-02-15
Authors: Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher
Citation: Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher. "13C and 15N Chemical Shift Assignments of Mammalian Y145Stop Prion Protein Amyloid Fibrils" Biomol. NMR Assign. 11, 75-80 (2017).
Assembly members:
huPrP23-144, polymer, 126 residues, Formula weight is not available
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):
huPrP23-144: GSDPKKRPKPGGWNTGGSRY
PGQGSPGGNRYPPQGGGGWG
QPHGGGWGQPHGGGWGQPHG
GGWGQPHGGGWGQGGGTHSQ
WNKPSKPKTNMKHMAGAAAA
GAVVGGLGGYMLGSAMSRPI
IHFGSD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 92 |
15N chemical shifts | 28 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | huPrP23-144 | 1 |
Entities:
Entity 1, huPrP23-144 126 residues - Formula weight is not available
The four N-terminal residues (GSDP) correspond to non-native thrombin cleavage sites used for protein purification.
1 | GLY | SER | ASP | PRO | LYS | LYS | ARG | PRO | LYS | PRO | ||||
2 | GLY | GLY | TRP | ASN | THR | GLY | GLY | SER | ARG | TYR | ||||
3 | PRO | GLY | GLN | GLY | SER | PRO | GLY | GLY | ASN | ARG | ||||
4 | TYR | PRO | PRO | GLN | GLY | GLY | GLY | GLY | TRP | GLY | ||||
5 | GLN | PRO | HIS | GLY | GLY | GLY | TRP | GLY | GLN | PRO | ||||
6 | HIS | GLY | GLY | GLY | TRP | GLY | GLN | PRO | HIS | GLY | ||||
7 | GLY | GLY | TRP | GLY | GLN | PRO | HIS | GLY | GLY | GLY | ||||
8 | TRP | GLY | GLN | GLY | GLY | GLY | THR | HIS | SER | GLN | ||||
9 | TRP | ASN | LYS | PRO | SER | LYS | PRO | LYS | THR | ASN | ||||
10 | MET | LYS | HIS | MET | ALA | GLY | ALA | ALA | ALA | ALA | ||||
11 | GLY | ALA | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | ||||
12 | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | ILE | ||||
13 | ILE | HIS | PHE | GLY | SER | ASP |
Samples:
sample_1: huPrP23-144, [U-100% 13C; U-100% 15N], 20 mg
sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 277 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NCA | sample_1 | solid | sample_conditions_1 |
2D NCACX | sample_1 | solid | sample_conditions_1 |
3D NCACX | sample_1 | solid | sample_conditions_1 |
3D NCOCX | sample_1 | solid | sample_conditions_1 |
3D CONCA | sample_1 | solid | sample_conditions_1 |
2D DARR | sample_1 | solid | sample_conditions_1 |
Software:
VNMR, Varian - collection
SPARKY, Goddard - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS-N, Shen and Bax - secondary structure analysis
nmrglue, Helmus, Jaroniec - processing
NMR spectrometers:
- Varian VNMRS 500 MHz