[English] 日本語
Yorodumi- PDB-9f4a: Interface between baseplate cup and extended tail tube/sheath of ... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9f4a | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Interface between baseplate cup and extended tail tube/sheath of Klebsiella phage KP1 variant vB_Kpn_Lilla1 | |||||||||||||||||||||||||||
Components |
| |||||||||||||||||||||||||||
Keywords | VIRUS / Baseplate cup / baseplate wedge / fibers | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationvirus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / symbiont entry into host cell via disruption of host cell wall peptidoglycan / virus tail, baseplate / symbiont entry into host cell via disruption of host cell envelope / viral tail assembly / viral release from host cell / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme ...virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / symbiont entry into host cell via disruption of host cell wall peptidoglycan / virus tail, baseplate / symbiont entry into host cell via disruption of host cell envelope / viral tail assembly / viral release from host cell / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to bacterium / structural molecule activity / membrane Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Klebsiella phage KP1 (virus) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.95 Å | |||||||||||||||||||||||||||
Authors | Orlova, E.V. / Isupov, M.N. | |||||||||||||||||||||||||||
| Funding support | 1items
| |||||||||||||||||||||||||||
Citation | Journal: To Be PublishedTitle: Baseplate cup of Klebsiella phage KP1 variant vB_Kpn_Lilla1 Authors: Orlova, E.V. / Isupov, M.N. | |||||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9f4a.cif.gz | 14.4 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9f4a.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9f4a.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9f4a_validation.pdf.gz | 3.8 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 9f4a_full_validation.pdf.gz | 4 MB | Display | |
| Data in XML | 9f4a_validation.xml.gz | 1.6 MB | Display | |
| Data in CIF | 9f4a_validation.cif.gz | 2.6 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/9f4a ftp://data.pdbj.org/pub/pdb/validation_reports/f4/9f4a | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 50186MC ![]() 9ev2C ![]() 9f4bC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-Protein , 8 types, 120 molecules LeLfLgLhLiLjLSLTLULVLWLXLYLZLaLbLcLdBMBKBOBPBLBNBQBVBSBRBTBU...
| #1: Protein | Mass: 138688.438 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A5B9NKG2#2: Protein | Mass: 38263.664 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V618#3: Protein | Mass: 33716.129 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A7I8V4E3#9: Protein | Mass: 71695.094 Da / Num. of mol.: 42 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5S7#10: Protein | Mass: 18633.738 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5T6#11: Protein | Mass: 15382.360 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A0K1Y5J2#12: Protein | Mass: 43526.016 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A7T3TJP2#14: Protein | Mass: 63317.457 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A976LXP5, lysozyme |
|---|
-Baseplate wedge ... , 6 types, 72 molecules AXAWATASAVAUARAQANAMAPAOAYAZA0A1A2A3A4A9A6A5A8A7AdAcAfAeAbAa...
| #4: Protein | Mass: 73689.242 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5R4#5: Protein | Mass: 119645.719 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5T9#6: Protein | Mass: 38704.387 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2Z4QAY9#7: Protein | Mass: 32380.195 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5S1#8: Protein | Mass: 66712.070 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5S8#13: Protein | Mass: 24693.420 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Klebsiella phage KP1 (virus) / References: UniProt: A0A2K9V5R5 |
|---|
-Non-polymers , 1 types, 1 molecules 
| #15: Chemical | ChemComp-CL / |
|---|
-Details
| Has ligand of interest | N |
|---|---|
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: vB_Kpn_Lilla1 / Type: VIRUS / Entity ID: #3-#10, #12, #2, #1 / Source: NATURAL |
|---|---|
| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: vB_Kpn_Lilla1 (virus) |
| Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION |
| Natural host | Organism: Klebsiella |
| Buffer solution | pH: 7.5 / Details: 100mM NaCl, 8mM MgSO4, 50mM Tris-HCl |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Klebsiella phage KP1 variant vB_Kpn_Lilla1 |
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: EMS Lacey Carbon |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 92 % / Chamber temperature: 281 K |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| Microscopy | Model: TFS KRIOS Details: Alignment procedure: EPU Autocoma and Autosrigmate Residual tilt (if alignment procedure is coma free, mrad): 68 Software used to collect images EPU 2.4, Tomo 5.13 Film/CCD/Direct electron ...Details: Alignment procedure: EPU Autocoma and Autosrigmate Residual tilt (if alignment procedure is coma free, mrad): 68 Software used to collect images EPU 2.4, Tomo 5.13 Film/CCD/Direct electron detector model*: post GIF K3 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Calibrated magnification: 83505 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm / Alignment procedure: OTHER |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature (max): 93.6 K / Temperature (min): 78.7 K / Residual tilt: 68 mradians |
| Image recording | Average exposure time: 2 sec. / Electron dose: 40 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 4 |
| Image scans | Sampling size: 5 µm / Width: 4092 / Height: 5760 |
-
Processing
| EM software | Name: REFMAC / Version: 5.8.0258 / Category: model refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 34529 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C6 (6 fold cyclic) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.95 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2415 / Algorithm: FOURIER SPACE / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | Resolution: 3.95→546.304 Å / Cor.coef. Fo:Fc: 0.862 / WRfactor Rwork: 0.45 / SU B: 91.285 / SU ML: 1.147 / Average fsc overall: 0.5353 / Average fsc work: 0.5353 / ESU R: 0.783 Details: Hydrogens have been added in their riding positions
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | Solvent model: BABINET MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 161.415 Å2
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LS refinement shell | Refine-ID: ELECTRON MICROSCOPY / Num. reflection Rfree: _ / Total num. of bins used: 20 / % reflection obs: 100 %
|
Movie
Controller
About Yorodumi



Klebsiella phage KP1 (virus)
Citation




PDBj






FIELD EMISSION GUN