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Open data
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Basic information
| Entry | Database: PDB / ID: 9tic | |||||||||||||||||||||||||||
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| Title | Phage 812 baseplate in the pre-contraction state (C3) | |||||||||||||||||||||||||||
Components |
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Keywords | VIRUS / phage / baseplate | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationsymbiont-mediated cytolysis of host cell / hydrolase activity, acting on glycosyl bonds / phosphoric diester hydrolase activity / cysteine-type peptidase activity / lipid metabolic process / proteolysis Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Staphylococcus phage 812K1/420 (virus) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.9 Å | |||||||||||||||||||||||||||
Authors | Binovsky, J. / Plevka, P. | |||||||||||||||||||||||||||
| Funding support | European Union, Czech Republic, 2items
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Citation | Journal: To Be PublishedTitle: Conformational changes of baseplate regulating tail contraction of Staphylococcus phage 812 Authors: Binovsky, J. / Plevka, P. | |||||||||||||||||||||||||||
| 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 | 9tic.cif.gz | 5.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9tic.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9tic.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/9tic ftp://data.pdbj.org/pub/pdb/validation_reports/ti/9tic | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 55951MC ![]() 9tidC ![]() 9tieC ![]() 9tifC ![]() 9tigC ![]() 9tihC ![]() 9tiiC ![]() 9tijC ![]() 9tikC ![]() 9tilC ![]() 9timC ![]() 9tinC ![]() 9tioC ![]() 9tipC ![]() 9tisC ![]() 9titC ![]() 9tiwC 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 , 15 types, 76 molecules 089wxy1PQRSTUVWXYZefghijklmnop...
| #1: Protein | Mass: 50474.078 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7P9#2: Protein | Mass: 19259.613 Da / Num. of mol.: 24 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q3#3: Protein | Mass: 129262.961 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q2#4: Protein | | Mass: 96199.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q9#5: Protein | Mass: 72654.742 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: A0A0U1UXW5#6: Protein | Mass: 15942.970 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7R7#7: Protein | Mass: 64559.008 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7R8#8: Protein | | Mass: 34645.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7R0#9: Protein | | Mass: 91364.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7R1#10: Protein | Mass: 19998.748 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q7#11: Protein | Mass: 29381.604 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q8#12: Protein | Mass: 26611.752 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q6#13: Protein | Mass: 39248.859 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q5#14: Protein | Mass: 116389.945 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q4#15: Protein | | Mass: 14627.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus phage 812K1/420 (virus) / References: UniProt: Q6Y7Q0 |
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-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: Staphylococcus phage 812K1/420 / Type: VIRUS Details: Propagated in S. aureus SA 812 (CCM 4028) planktonic culture and purified on a CsCl gradient. Entity ID: all / Source: NATURAL | ||||||||||||||||||||
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| Source (natural) | Organism: Staphylococcus phage 812K1/420 (virus) | ||||||||||||||||||||
| Details of virus | Empty: NO / Enveloped: NO / Isolate: STRAIN / Type: VIRION | ||||||||||||||||||||
| Buffer solution | pH: 8 | ||||||||||||||||||||
| Buffer component |
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: 10e9 PFU/ml | ||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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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 magnification: 105000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 2 sec. / Electron dose: 40.8 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 26731 |
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Processing
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 64874 | ||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C3 (3 fold cyclic) | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 5.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 3586 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| Atomic model building | B value: 287 / Protocol: RIGID BODY FIT / Space: REAL Details: Fitting of previously refined sub-models (e.g. lower arm, upper arm, core, baseplate-proximal tail) in ChimeraX as rigid bodies, then relaxing the model using ISOLDE before rigid body ...Details: Fitting of previously refined sub-models (e.g. lower arm, upper arm, core, baseplate-proximal tail) in ChimeraX as rigid bodies, then relaxing the model using ISOLDE before rigid body refinement in Phenix (all chains as a single rigid body). |
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About Yorodumi




Staphylococcus phage 812K1/420 (virus)
Czech Republic, 2items
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FIELD EMISSION GUN