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Yorodumi- PDB-2dyf: Solution structure of the first WW domain of FBP11 / HYPA (FBP11 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2dyf | ||||||
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Title | Solution structure of the first WW domain of FBP11 / HYPA (FBP11 WW1) complexed with a PL (PPLP) motif peptide ligand | ||||||
Components |
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Keywords | PROTEIN BINDING / WW DOMAIN / COMPLEX / FBP11 / HYPA / PL MOTIF / PPLP MOTIF / SOLUTION STRUCTURE / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses | ||||||
Function / homology | Function and homology information myosin I tail binding / myosin I binding / negative regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch / mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis ...myosin I tail binding / myosin I binding / negative regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch / 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 / actin cytoskeleton organization / cell cycle / nuclear speck / cell division / nucleolus / RNA binding / nucleoplasm / membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model type details | minimized average | ||||||
Authors | Kato, Y. / Miyakawa, T. / Kurita, J. / Tanokura, M. | ||||||
Citation | Journal: To be Published Title: Complex structure of fbp11 ww1 and a pl ligand reveals the mechanism of proline-rich ligand recognition by group-II/III ww domains Authors: Kato, Y. / Miyakawa, T. / Kurita, J. / Tanokura, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2dyf.cif.gz | 274.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dyf.ent.gz | 232.8 KB | Display | PDB format |
PDBx/mmJSON format | 2dyf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2dyf_validation.pdf.gz | 355.2 KB | Display | wwPDB validaton report |
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Full document | 2dyf_full_validation.pdf.gz | 489.3 KB | Display | |
Data in XML | 2dyf_validation.xml.gz | 10.4 KB | Display | |
Data in CIF | 2dyf_validation.cif.gz | 18.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dy/2dyf ftp://data.pdbj.org/pub/pdb/validation_reports/dy/2dyf | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar 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: 3612.758 Da / Num. of mol.: 1 / Fragment: THE FIRST WW DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX-4T-1 / Production host: Escherichia coli (E. coli) / References: UniProt: O75400 |
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#2: Protein/peptide | Mass: 896.022 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: PGEX-4T-1 / Production host: Escherichia coli (E. coli) / References: UniProt: P47068 |
-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 and 13C half filtered noesy-hsqc. |
-Sample preparation
Details | Contents: 1.5MM FBP11 WW1 U-15N, 13C 5.3MM NATURAL ABUNDANCE PL MOTIF PEPTIDE; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 90% H2O, 10% D2O; 1.5MM FBP11 WW1 U- 15N, 13C; 5.3MM NATURAL ABUNDANCE PL MOTIF ...Contents: 1.5MM FBP11 WW1 U-15N, 13C 5.3MM NATURAL ABUNDANCE PL MOTIF PEPTIDE; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 90% H2O, 10% D2O; 1.5MM FBP11 WW1 U- 15N, 13C; 5.3MM NATURAL ABUNDANCE PL MOTIF PEPTIDE; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 100% D2O; 1.6MM FBP11 WW1 NATURAL ABUNDANCE; 4.4MM PL MOTIF PEPTIDE U-15N, 13C; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 90% H2O, 10% D2O; 1.6MM FBP11 WW1 NATURAL ABUNDANCE; 4.4MM PL MOTIF PEPTIDE U-15N, 13C; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 100% D2O; 1.5MM FBP11 WW1 U-15N; 5.3MM NATURAL ABUNDANCE PL MOTIF PEPTIDE; 50MM PHOSPHATE BUFFER NA; 50MM NACL; 90% H2O, 10% D2O |
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Sample conditions | Ionic strength: 0.3 / pH: 5.0 / Pressure: 1 atm / Temperature: 283 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: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |