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Yorodumi- PDB-6hn7: Hijacking the Hijackers: Escherichia coli Pathogenicity Islands R... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6hn7 | ||||||
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Title | Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit. | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / Redirecting packaging protein / Hetero-dimer / phage interference / Protein complex | ||||||
Function / homology | Function and homology information viral terminase, small subunit / sequence-specific DNA binding, bending / viral DNA genome packaging / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / host cell cytoplasm / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) Escherichia virus Lambda | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Penades, J.R. / Bacarizo, J. / Marina, A. / Alqasmi, M. / Fillol-Salom, A. / Roszak, A.W. / Ciges-Tomas, J.R. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Mol.Cell / Year: 2019 Title: Hijacking the Hijackers: Escherichia coli Pathogenicity Islands Redirect Helper Phage Packaging for Their Own Benefit. Authors: Fillol-Salom, A. / Bacarizo, J. / Alqasmi, M. / Ciges-Tomas, J.R. / Martinez-Rubio, R. / Roszak, A.W. / Cogdell, R.J. / Chen, J. / Marina, A. / Penades, J.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hn7.cif.gz | 56.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hn7.ent.gz | 38.2 KB | Display | PDB format |
PDBx/mmJSON format | 6hn7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/6hn7 ftp://data.pdbj.org/pub/pdb/validation_reports/hn/6hn7 | HTTPS FTP |
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-Related structure data
Related structure data | 6hlkSC 1j9iS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17828.396 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: CXXR01000010.1 / Variant: EC2733.1 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: A0A5H1ZR32*PLUS |
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#2: Protein | Mass: 11472.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: All alpha proteins, Putative DNA-binding domain, Hetero-dimer complex, Terminase gpNU1 subunit domain, Bacteriophage lambda The first three Ala residues at the beginning of the sequence from ...Details: All alpha proteins, Putative DNA-binding domain, Hetero-dimer complex, Terminase gpNU1 subunit domain, Bacteriophage lambda The first three Ala residues at the beginning of the sequence from coordinates come from the purification tag. Source: (gene. exp.) Escherichia virus Lambda / Gene: Nu1, lambdap01 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: P03707 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.97 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, sitting drop / pH: 5 / Details: 2M Ammonium Sulfate, 0.1M AcONa pH 5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.9762 Å | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Mar 12, 2018 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 3→50.5 Å / Num. obs: 5163 / % possible obs: 97.7 % / Redundancy: 3.5 % / CC1/2: 0.992 / Rmerge(I) obs: 0.064 / Rpim(I) all: 0.041 / Rrim(I) all: 0.076 / Net I/σ(I): 11.1 / Num. measured all: 18007 / Scaling rejects: 3 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6HLK, 1J9I Resolution: 3→50.5 Å / Cor.coef. Fo:Fc: 0.863 / Cor.coef. Fo:Fc free: 0.841 / SU B: 0.01 / SU ML: 0 / SU R Cruickshank DPI: 0.5774 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.577 / ESU R Free: 0.614 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||
Displacement parameters | Biso max: 167.1 Å2 / Biso mean: 67.198 Å2 / Biso min: 20 Å2
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Refinement step | Cycle: final / Resolution: 3→50.5 Å
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LS refinement shell | Resolution: 3→3.078 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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