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Open data
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Basic information
Entry | Database: PDB / ID: 5yj4 | ||||||
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Title | structure for the protective mutant G127V of Human prion protein | ||||||
![]() | Major prion protein | ||||||
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Function / homology | ![]() positive regulation of glutamate receptor signaling pathway / negative regulation of amyloid precursor protein catabolic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Zheng, Z. / Lin, D. | ||||||
![]() | ![]() Title: Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease. Authors: Zheng, Z. / Zhang, M. / Wang, Y. / Ma, R. / Guo, C. / Feng, L. / Wu, J. / Yao, H. / Lin, D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 863.2 KB | Display | ![]() |
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PDB format | ![]() | 729.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5yj5C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 16285.220 Da / Num. of mol.: 1 / Fragment: UNP residues 91-231 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() References: UniProt: P04156 |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 0.5 mM [U-99% 13C; U-99% 15N] HuPrP(G127V), 90% H2O/10% D2O Label: 13C/15N_sample / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.5 mM / Component: HuPrP(G127V) / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Ionic strength: 20 mM / Label: nmrbuffer / pH: 4.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model![]() |
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Processing
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Refinement | Method: ![]() Details: 2841 are NOE-derived distance constraints, 168 dihedral angle restraints | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 |