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Yorodumi- PDB-1oqp: STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1oqp | ||||||
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Title | STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX WITH THE CDC31P-BINDING DOMAIN FROM KAR1P | ||||||
Components |
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Keywords | PROTEIN BINDING / protein-peptide complex / caltractin / KAR1P / calcium-binding | ||||||
Function / homology | Function and homology information half bridge of spindle pole body / inner dynein arm / spindle pole body duplication / karyogamy involved in conjugation with cellular fusion / dynein heavy chain binding / centriole / mitotic cell cycle / microtubule / cell division / calcium ion binding / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | Chlamydomonas reinhardtii (plant) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Hu, H.T. / Chazin, W.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Unique Features in the C-terminal Domain Provide Caltractin with Target Specificity Authors: Hu, H.T. / Chazin, W.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oqp.cif.gz | 616.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oqp.ent.gz | 516.4 KB | Display | PDB format |
PDBx/mmJSON format | 1oqp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1oqp_validation.pdf.gz | 363.4 KB | Display | wwPDB validaton report |
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Full document | 1oqp_full_validation.pdf.gz | 546.3 KB | Display | |
Data in XML | 1oqp_validation.xml.gz | 26.7 KB | Display | |
Data in CIF | 1oqp_validation.cif.gz | 47.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oq/1oqp ftp://data.pdbj.org/pub/pdb/validation_reports/oq/1oqp | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8977.838 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chlamydomonas reinhardtii (plant) / Plasmid: PET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PlysS / References: UniProt: P05434 |
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#2: Protein/peptide | Mass: 2501.003 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide consists of the cdc31p-binding domain from Kar1p, residues 239-257, and has been chemically synthesized using solid phase F-Moc chemistry. The sequence is naturally found in ...Details: The peptide consists of the cdc31p-binding domain from Kar1p, residues 239-257, and has been chemically synthesized using solid phase F-Moc chemistry. The sequence is naturally found in Saccharomyces cerevisiae (baker's yeast). References: UniProt: P11927 |
-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: 50mM KCl, 5mM CaCl2 / pH: 7 / Pressure: ambient / Temperature: 298 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: the structures are based on a total of 1827 constraints, 1641 are NOE-derived distance constraints, 134 dihedral angle constraints, 52 distance constraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 20 |