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- PDB-1oqp: STRUCTURE OF THE CA2+/C-TERMINAL DOMAIN OF CALTRACTIN IN COMPLEX ... -
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Open data
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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 | ||||||
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![]() | PROTEIN BINDING / protein-peptide complex / caltractin / KAR1P / calcium-binding | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Hu, H.T. / Chazin, W.J. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 616.5 KB | Display | ![]() |
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PDB format | ![]() | 516.4 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 363.4 KB | Display | ![]() |
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Full document | ![]() | 546.3 KB | Display | |
Data in XML | ![]() | 26.7 KB | Display | |
Data in CIF | ![]() | 47.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() ![]() |
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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: 7.0 / 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 |