+Open data
-Basic information
Entry | Database: PDB / ID: 1xyq | ||||||
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Title | NMR structure of the pig prion protein | ||||||
Components | Major prion protein | ||||||
Keywords | UNKNOWN FUNCTION / prion / prp / scprp / tse | ||||||
Function / homology | Function and homology information Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / type 5 metabotropic glutamate receptor binding / cuprous ion binding / side of membrane / inclusion body / cellular response to copper ion / tubulin binding / molecular condensate scaffold activity / protein destabilization / protein homooligomerization ...Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / type 5 metabotropic glutamate receptor binding / cuprous ion binding / side of membrane / inclusion body / cellular response to copper ion / tubulin binding / molecular condensate scaffold activity / protein destabilization / protein homooligomerization / positive regulation of neuron apoptotic process / positive regulation of peptidyl-tyrosine phosphorylation / cellular response to amyloid-beta / amyloid-beta binding / microtubule binding / nuclear membrane / membrane raft / copper ion binding / dendrite / protein-containing complex binding / Golgi apparatus / cell surface / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Lysek, D.A. / Schorn, C. / Herrmann, T. / Wuthrich, K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2005 Title: Prion protein NMR structures of cats, dogs, pigs, and sheep Authors: Lysek, D.A. / Schorn, C. / Nivon, L.G. / Esteve-Moya, V. / Christen, B. / Calzolai, L. / von Schroetter, C. / Fiorito, F. / Herrmann, T. / Guntert, P. / Wuthrich, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xyq.cif.gz | 678.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xyq.ent.gz | 590.2 KB | Display | PDB format |
PDBx/mmJSON format | 1xyq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xyq_validation.pdf.gz | 357.1 KB | Display | wwPDB validaton report |
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Full document | 1xyq_full_validation.pdf.gz | 461.3 KB | Display | |
Data in XML | 1xyq_validation.xml.gz | 31.2 KB | Display | |
Data in CIF | 1xyq_validation.cif.gz | 55.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xy/1xyq ftp://data.pdbj.org/pub/pdb/validation_reports/xy/1xyq | HTTPS FTP |
-Related structure data
Related structure data | 1xyjC 1xykC 1xyuC 1y2sC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12976.418 Da / Num. of mol.: 1 / Fragment: residues 121-231 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: Prnp / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P49927 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 3D heteronuclear techniques |
-Sample preparation
Details | Contents: 1mM pig prion protein, U-15N, 13C; 10mM acetate / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 10 / pH: 4.5 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |