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Open data
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Basic information
Entry | Database: PDB / ID: 6mjc | ||||||
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Title | Structure of Candida glabrata Csm1:Dsn1(43-67DD) complex | ||||||
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![]() | CELL CYCLE / monopolin / kinetochore | ||||||
Function / homology | ![]() microtubule site clamp / MIS12/MIND type complex / chromosome, centromeric core domain / monopolin complex / meiotic sister chromatid segregation / spindle attachment to meiosis I kinetochore / protein localization to nucleolar rDNA repeats / meiotic sister chromatid cohesion, centromeric / rDNA chromatin condensation / attachment of mitotic spindle microtubules to kinetochore ...microtubule site clamp / MIS12/MIND type complex / chromosome, centromeric core domain / monopolin complex / meiotic sister chromatid segregation / spindle attachment to meiosis I kinetochore / protein localization to nucleolar rDNA repeats / meiotic sister chromatid cohesion, centromeric / rDNA chromatin condensation / attachment of mitotic spindle microtubules to kinetochore / chromosome segregation / mitotic spindle / spindle pole / nuclear envelope / cell division / nucleolus / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Singh, N. / Corbett, K.D. | ||||||
Funding support | ![]()
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![]() | ![]() Title: The molecular basis of monopolin recruitment to the kinetochore. Authors: Plowman, R. / Singh, N. / Tromer, E.C. / Payan, A. / Duro, E. / Spanos, C. / Rappsilber, J. / Snel, B. / Kops, G.J.P.L. / Corbett, K.D. / Marston, A.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.1 KB | Display | ![]() |
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PDB format | ![]() | 74 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.6 KB | Display | ![]() |
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Full document | ![]() | 433.9 KB | Display | |
Data in XML | ![]() | 8 KB | Display | |
Data in CIF | ![]() | 10.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6mj8C ![]() 6mjbC ![]() 6mjeC ![]() 3n4rS S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Experimental dataset #1 | Data reference: ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 13513.335 Da / Num. of mol.: 1 / Fragment: UNP residues 69-181 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 3231.515 Da / Num. of mol.: 1 / Fragment: UNP residues 43-67 / Mutation: S66D, S67D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.97 Å3/Da / Density % sol: 69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 0.1 M sodium acetate, pH 4.5, 3 M sodium chloride, cryoprotectant: 0.5 M sodium chloride, 0.5 M sodium malonate, pH 4.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 22, 2018 |
Radiation | Monochromator: Cryo-Cooled double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 1.79→75 Å / Num. obs: 25112 / % possible obs: 99.7 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.03 / Rpim(I) all: 0.016 / Rrim(I) all: 0.034 / Net I/σ(I): 20 |
Reflection shell | Resolution: 1.79→1.83 Å / Rmerge(I) obs: 1.44 / Num. unique obs: 1462 / Rpim(I) all: 0.753 / Rrim(I) all: 1.025 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 3N4R Resolution: 1.79→52.529 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.01
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.79→52.529 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -13.1902 Å / Origin y: 48.7233 Å / Origin z: 6.238 Å
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Refinement TLS group | Selection details: all |