[English] 日本語
Yorodumi- PDB-1wyo: Solution structure of the CH domain of human microtubule-associat... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wyo | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3 | ||||||
Components | Microtubule-associated protein RP/EB family member 3 | ||||||
Keywords | STRUCTURAL PROTEIN / RP/EB family / CH domain / microtubule-binding / structural genomics / NPPSFA / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information mitotic spindle astral microtubule end / protein localization to microtubule / microtubule plus-end / microtubule plus-end binding / microtubule organizing center / regulation of microtubule polymerization / positive regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of protein kinase activity / regulation of microtubule polymerization or depolymerization / spindle assembly ...mitotic spindle astral microtubule end / protein localization to microtubule / microtubule plus-end / microtubule plus-end binding / microtubule organizing center / regulation of microtubule polymerization / positive regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of protein kinase activity / regulation of microtubule polymerization or depolymerization / spindle assembly / spindle midzone / protein localization / microtubule cytoskeleton / midbody / microtubule binding / cell division / protein kinase binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
Authors | Tomizawa, T. / Kigawa, T. / Koshiba, S. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3 Authors: Tomizawa, T. / Kigawa, T. / Koshiba, S. / Inoue, M. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1wyo.cif.gz | 961.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1wyo.ent.gz | 806.1 KB | Display | PDB format |
PDBx/mmJSON format | 1wyo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wyo_validation.pdf.gz | 345.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1wyo_full_validation.pdf.gz | 510 KB | Display | |
Data in XML | 1wyo_validation.xml.gz | 67.7 KB | Display | |
Data in CIF | 1wyo_validation.cif.gz | 83.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wy/1wyo ftp://data.pdbj.org/pub/pdb/validation_reports/wy/1wyo | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 17912.385 Da / Num. of mol.: 1 / Fragment: CH domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: MAPRE3 / Plasmid: P040621-06 / References: UniProt: Q9UPY8 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.28mM CH domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics, restrained molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function,structures with the lowest energy,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |