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Open data
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Basic information
Entry | Database: PDB / ID: 2l39 | ||||||
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Title | Mouse prion protein fragment 121-231 AT 37 C | ||||||
![]() | Major prion protein | ||||||
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Function / homology | ![]() Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / negative regulation of amyloid precursor protein catabolic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
Model details | fewest violations, model 1 | ||||||
![]() | Christen, B. / Damberger, F.F. / Perez, D.R. / Hornemann, S. / Wuthrich, K. | ||||||
![]() | ![]() Title: Cellular prion protein conformation and function. Authors: Damberger, F.F. / Christen, B. / Perez, D.R. / Hornemann, S. / Wuthrich, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 697.3 KB | Display | ![]() |
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PDB format | ![]() | 587.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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: 13408.877 Da / Num. of mol.: 1 / Fragment: UNP residues 120-231 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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Sequence details | RESIDUES GLY A 119 AND SER A 120 ARE LEFT OVER FROM THE THROMBIN CLEAVAGE OF THE HIS TAG |
-Experimental details
-Experiment
Experiment | Method: ![]() Details: Additional HN/N signals from the beta 2-alpha 2 loop of the mouse prion protein fragment 121-231 are visible at 37C allowing the identification of additional NOE constraints which lead to a ...Details: Additional HN/N signals from the beta 2-alpha 2 loop of the mouse prion protein fragment 121-231 are visible at 37C allowing the identification of additional NOE constraints which lead to a defined conformation for the loop. | ||||||||||||||||
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NMR experiment |
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NMR details | Text: Two 13C-resolved [1H,1H]-NOESY spectra were obtained with the 13C carrier and spectral width optimized for aliphatic and aromatic 13C resonances respectively. |
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Sample preparation
Details | Contents: 1.6 mM [U-99% 13C; U-99% 15N] entity-1, 10 mM [U-2H] sodium acetate-2, 0.02 % sodium azide-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.01 / pH: 4.5 / Pressure: ambient / Temperature: 310.2 K |
-NMR measurement
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: 120 / Conformers submitted total number: 20 / Representative conformer: 1 |