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Open data
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Basic information
| Entry | Database: PDB / ID: 9okd | ||||||||||||||||||||||||||||||
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| Title | Structure of the monomeric Bombyx mori CCAN bound to linear DNA | ||||||||||||||||||||||||||||||
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Keywords | DNA BINDING PROTEIN/DNA / CCAN / complex / protein-DNA / segregation / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationCENP-A containing chromatin assembly / inner kinetochore / mitotic sister chromatid segregation / chromosome, centromeric region / nucleus Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() synthetic construct (others) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.83 Å | ||||||||||||||||||||||||||||||
Authors | Yatskevich, S. / Ciferri, C. | ||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Architecture and Function of Holocentric CENP-A-Independent Inner Kinetochores Authors: Yatskevich, S. / Ciferri, C. | ||||||||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9okd.cif.gz | 923.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9okd.ent.gz | 742.7 KB | Display | PDB format |
| PDBx/mmJSON format | 9okd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ok/9okd ftp://data.pdbj.org/pub/pdb/validation_reports/ok/9okd | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70560MC ![]() 9okbC ![]() 9oklC ![]() 77479 ![]() 77480 M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 9 types, 9 molecules HKNPTACDB
| #1: Protein | Mass: 27719.170 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2AFF4 |
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| #2: Protein | Mass: 24760.084 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2AP23 |
| #6: Protein | Mass: 36883.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R1WGT7 |
| #8: Protein | Mass: 71100.820 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R1WGN9 |
| #9: Protein | Mass: 116758.258 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2HRP3 |
| #10: Protein | Mass: 10754.051 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) |
| #11: Protein | Mass: 8577.579 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2AV77 |
| #12: Protein | Mass: 9175.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) |
| #13: Protein | Mass: 9122.198 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) |
-Centromere protein ... , 4 types, 4 molecules IMLO
| #3: Protein | Mass: 75965.023 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2LUB8 |
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| #4: Protein | Mass: 20135.387 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2ARQ0 |
| #5: Protein | Mass: 34229.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: H9IXB1 |
| #7: Protein | Mass: 37681.129 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper) / References: UniProt: A0A8R2AFZ4 |
-DNA chain , 2 types, 2 molecules GJ
| #14: DNA chain | Mass: 11095.101 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #15: DNA chain | Mass: 11064.092 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Details
| Has protein modification | N |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Bombyx mori CCAN monomer bound to DNA / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 241975 / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Atomic model building | Protocol: AB INITIO MODEL | ||||||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN