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- PDB-1ywi: Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ywi | ||||||
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Title | Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP | ||||||
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![]() | STRUCTURAL PROTEIN / WW domain / Class II / Proline-rich peptides / protein-protein interactions | ||||||
Function / homology | ![]() mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape ...mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape / nuclear speck / cell cycle / cell division / RNA binding / nucleoplasm / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / Automated assignment of NOEs, simulated anneling with torsion angle dinamics | ||||||
![]() | Pires, J.R. / Parthier, C. / Aido-Machado, R. / Wiedemann, U. / Otte, L. / Boehm, G. / Rudolph, R. / Oschkinat, H. | ||||||
![]() | ![]() Title: Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain. Authors: Pires, J.R. / Parthier, C. / Aido-Machado, R. / Wiedemann, U. / Otte, L. / Bohm, G. / Rudolph, R. / Oschkinat, 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 | ![]() | 167 KB | Display | ![]() |
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PDB format | ![]() | 136.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 349 KB | Display | ![]() |
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Full document | ![]() | 477.1 KB | Display | |
Data in XML | ![]() | 8.9 KB | Display | |
Data in CIF | ![]() | 14.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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/peptide | Mass: 4747.092 Da / Num. of mol.: 1 / Fragment: WW1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 983.158 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: automated solid phase synthesis on chlortrityl resin using FMOC strategy |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 100mM NaCl / pH: 6.0 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: Automated assignment of NOEs, simulated anneling with torsion angle dinamics Software ordinal: 1 Details: The structure was also refined with ARIA ver.1.2, authors: Linge, J.P., O'Dongue, S.I., Nilges, M. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 15 |