BMRB Entry 27264
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27264
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Title: 1H, 15N, 13C resonance assignments for Human prion protein (91-231): wild type (scilicet HuPrPM129) PubMed: 30181558
Deposition date: 2017-09-25 Original release date: 2017-10-25
Authors: Zheng, Zhen; Lin, Donghai; Feng, Liubin
Citation: Zheng, Zhen; Zhang, Meilan; Wang, Yongheng; Ma, Rongsheng; Guo, Chenyun; Feng, Liubin; Wu, Jihui; Yao, Hongwei; Lin, Donghai. "Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease" Sci. Rep. 8, 13211-13211 (2018).
Assembly members:
HuPrPM129, polymer, 142 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 Vector: pET30a
Entity Sequences (FASTA):
HuPrPM129: MQGGGTHSQWNKPSKPKTNM
KHMAGAAAAGAVVGGLGGYM
LGSAMSRPIIHFGSDYEDRY
YRENMHRYPNQVYYRPMDEY
SNQNNFVHDCVNITIKQHTV
TTTTKGENFTETDVKMMERV
VEQMCITQYERESQAYYQRG
SS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 505 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 882 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HuPrPM129 | 1 |
Entities:
Entity 1, HuPrPM129 142 residues - Formula weight is not available
| 1 | MET | GLN | GLY | GLY | GLY | THR | HIS | SER | GLN | TRP | ||||
| 2 | ASN | LYS | PRO | SER | LYS | PRO | LYS | THR | ASN | MET | ||||
| 3 | LYS | HIS | MET | ALA | GLY | ALA | ALA | ALA | ALA | GLY | ||||
| 4 | ALA | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | MET | ||||
| 5 | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | ILE | ILE | ||||
| 6 | HIS | PHE | GLY | SER | ASP | TYR | GLU | ASP | ARG | TYR | ||||
| 7 | TYR | ARG | GLU | ASN | MET | HIS | ARG | TYR | PRO | ASN | ||||
| 8 | GLN | VAL | TYR | TYR | ARG | PRO | MET | ASP | GLU | TYR | ||||
| 9 | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ASP | CYS | ||||
| 10 | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | THR | VAL | ||||
| 11 | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | THR | ||||
| 12 | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ARG | VAL | ||||
| 13 | VAL | GLU | GLN | MET | CYS | ILE | THR | GLN | TYR | GLU | ||||
| 14 | ARG | GLU | SER | GLN | ALA | TYR | TYR | GLN | ARG | GLY | ||||
| 15 | SER | SER |
Samples:
sample_1: HuPrPM129, [U-100% 13C; U-100% 15N], 0.5 mM; NaOAc 20 mM; NaN3 0.2%
sample_conditions_1: ionic strength: 0.02 M; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts