[English] 日本語
Yorodumi- PDB-2cp5: Solution structure of the 1st CAP-Gly domain in human CLIP-170/restin -
+Open data
-Basic information
Entry | Database: PDB / ID: 2cp5 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the 1st CAP-Gly domain in human CLIP-170/restin | ||||||
Components | Restin | ||||||
Keywords | PROTEIN BINDING / microtubule binding / cytoskeleton associated protein / restin / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information microtubule plus-end / microtubule bundle formation / microtubule plus-end binding / intermediate filament / RHO GTPases activate IQGAPs / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / cytoplasmic microtubule organization / EML4 and NUDC in mitotic spindle formation / positive regulation of microtubule polymerization ...microtubule plus-end / microtubule bundle formation / microtubule plus-end binding / intermediate filament / RHO GTPases activate IQGAPs / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / cytoplasmic microtubule organization / EML4 and NUDC in mitotic spindle formation / positive regulation of microtubule polymerization / ruffle / Resolution of Sister Chromatid Cohesion / tubulin binding / RHO GTPases Activate Formins / cytoplasmic vesicle membrane / kinetochore / Separation of Sister Chromatids / microtubule cytoskeleton / mitotic cell cycle / cell cortex / microtubule binding / microtubule / centrosome / zinc ion binding / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Saito, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the 1st CAP-Gly domain in human CLIP-170/restin Authors: Saito, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2cp5.cif.gz | 815.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2cp5.ent.gz | 684.1 KB | Display | PDB format |
PDBx/mmJSON format | 2cp5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2cp5_validation.pdf.gz | 344.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2cp5_full_validation.pdf.gz | 486.7 KB | Display | |
Data in XML | 2cp5_validation.xml.gz | 40.6 KB | Display | |
Data in CIF | 2cp5_validation.cif.gz | 66.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cp/2cp5 ftp://data.pdbj.org/pub/pdb/validation_reports/cp/2cp5 | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14847.786 Da / Num. of mol.: 1 / Fragment: CAP-Gly domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: FB2383_D01 / Plasmid: P040816-08 / References: UniProt: P30622 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1mM protein, 20mM d-Tris-HCl, pH7.0, 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120 / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |