Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18426
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Biljan, Ivana; Giachin, Gabriele; Ilc, Gregor; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe. "Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism." Biochem. J. 446, 243-251 (2012).
PubMed: 22676969
Assembly members:
entity, polymer, 142 residues, 16169.103 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 Vector: pProExHTa
Data type | Count |
13C chemical shifts | 461 |
15N chemical shifts | 150 |
1H chemical shifts | 930 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | human prion protein | 1 |
Entity 1, human prion protein 142 residues - 16169.103 Da.
1 | GLY | 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 |
sample_1: huPrP, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 90%; D2O 10%
sample_2: huPrP, [U-100% 13C; U-100% 15N], 1.5 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1 M; pD: 5.9; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_2 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
YASARA, (YASARA) - refinement
BMRB | 15676 16743 16757 17714 17756 17757 17780 18550 19268 4379 4402 4434 4620 4641 4736 |
PDB | |
DBJ | BAA00011 BAF62360 BAG32276 BAG32277 BAG32278 |
EMBL | CAA58442 CAG46836 CAG46869 CAH92912 |
GB | AAA19664 AAA60182 AAA68632 AAA68633 AAB59442 |
REF | NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592 |
SP | P04156 P40252 P40256 P61766 P61767 |
TPE | CAJ43808 |
AlphaFold | P04156 P40252 P40256 P61766 P61767 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks