+Open data
-Basic information
Entry | Database: PDB / ID: 1ywj | ||||||
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Title | Structure of the FBP11WW1 domain | ||||||
Components | Formin-binding protein 3 | ||||||
Keywords | STRUCTURAL PROTEIN / WW domain / Class II / Proline-rich peptides / protein-protein interactions | ||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Automated assignment of NOEs, simulated anneling with torsion angle dinamics | ||||||
Authors | Pires, J.R. / Parthier, C. / Aido-Machado, R. / Wiedemann, U. / Otte, L. / Boehm, G. / Rudolph, R. / Oschkinat, H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ywj.cif.gz | 141.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ywj.ent.gz | 114.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ywj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yw/1ywj ftp://data.pdbj.org/pub/pdb/validation_reports/yw/1ywj | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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.) Homo sapiens (human) / Plasmid: pGEX-2TK / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: O75400 |
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-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 |