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Yorodumi- PDB-1v6e: Solution Structure of a N-terminal Ubiquitin-like Domain in Mouse... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v6e | ||||||
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Title | Solution Structure of a N-terminal Ubiquitin-like Domain in Mouse Tubulin-specific Chaperone B | ||||||
Components | cytoskeleton-associated protein 1 | ||||||
Keywords | STRUCTURAL PROTEIN / Tubulin-specific Chaperone B / Tubulin folding cofactor B / Cytoskeleton-associated protein CKAP1 / Cytoskeleton / Microtubule / Ubiquitin-like fold / Structural genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information post-chaperonin tubulin folding pathway / cell tip / tubulin complex assembly / microtubule plus-end / microtubule plus-end binding / microtubule associated complex / establishment of mitotic spindle orientation / alpha-tubulin binding / cytoplasmic microtubule organization / kinetochore ...post-chaperonin tubulin folding pathway / cell tip / tubulin complex assembly / microtubule plus-end / microtubule plus-end binding / microtubule associated complex / establishment of mitotic spindle orientation / alpha-tubulin binding / cytoplasmic microtubule organization / kinetochore / spindle pole / nervous system development / cell cortex / cell differentiation / axon / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Zhao, C. / Kigawa, T. / Saito, K. / Koshiba, S. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of a N-terminal Ubiquitin-like Domain in Mouse Tubulin-specific Chaperone B Authors: Zhao, C. / Kigawa, T. / Saito, K. / Koshiba, S. / Inoue, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v6e.cif.gz | 538.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v6e.ent.gz | 452 KB | Display | PDB format |
PDBx/mmJSON format | 1v6e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1v6e_validation.pdf.gz | 345 KB | Display | wwPDB validaton report |
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Full document | 1v6e_full_validation.pdf.gz | 502.1 KB | Display | |
Data in XML | 1v6e_validation.xml.gz | 35.1 KB | Display | |
Data in CIF | 1v6e_validation.cif.gz | 53.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v6/1v6e ftp://data.pdbj.org/pub/pdb/validation_reports/v6/1v6e | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10172.311 Da / Num. of mol.: 1 / Fragment: Ubiquitin-like domain / Mutation: S81R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 2410007D12 / Plasmid: P030414-64 / References: UniProt: Q9D1E6 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.15mM Protein U-15N, 13C; 20mM Phosphate Na (pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298.0 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |