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- PDB-1g04: SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1g04 | ||||||
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Title | SOLUTION STRUCTURE OF SYNTHETIC 26-MER PEPTIDE CONTAINING 145-169 SHEEP PRION PROTEIN SEGMENT AND C-TERMINAL CYSTEINE | ||||||
![]() | MAJOR PRION PROTEIN | ||||||
![]() | UNKNOWN FUNCTION / prion / beta hairpin | ||||||
Function / homology | ![]() side of membrane / tubulin binding / protein homooligomerization / microtubule binding / copper ion binding / Golgi apparatus / identical protein binding / plasma membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing torsion angle dynamics | ||||||
Model type details | minimized average | ||||||
![]() | Kozin, S.A. / Bertho, G. / Mazur, A.K. / Rabesona, H. / Girault, J.-P. / Haertle, T. / Takahashi, M. / Debey, P. / Hui Bon Hoa, G. | ||||||
![]() | ![]() Title: Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution. Authors: Kozin, S.A. / Bertho, G. / Mazur, A.K. / Rabesona, H. / Girault, J.P. / Haertle, T. / Takahashi, M. / Debey, P. / Hoa, G.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 190.3 KB | Display | ![]() |
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PDB format | ![]() | 157.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 338.4 KB | Display | ![]() |
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Full document | ![]() | 462.5 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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/peptide | Mass: 3431.729 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This peptide was chemically synthesized. Except for the C-terminal Cysteine, this sequence occurs naturally in sheep. References: UniProt: P23907 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
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Sample preparation
Details | Contents: 4.5mM Solvent system: 10mM sodium phosphate buffer, pH 6.5; 90% H2O, 10% D2O |
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Sample conditions | Ionic strength: 15mM / pH: 6.5 / Pressure: 1 atm / Temperature: 278 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
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Processing
NMR software | Name: XwinNMR / Version: 2.1 / Developer: bruker sowttfare / Classification: collection |
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Refinement | Method: simulated annealing torsion angle dynamics / Software ordinal: 1 Details: The structures are based on a total of 169 interresidual NOE-derived distance constraints. |
NMR representative | Selection criteria: minimized average structure |
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 1000 / Conformers submitted total number: 21 |