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Yorodumi- PDB-3gq8: Crystal Structure of the Bacteriophage phi29 gene product 12 N-te... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3gq8 | ||||||
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Title | Crystal Structure of the Bacteriophage phi29 gene product 12 N-terminal fragment in complex with 2-(N-cyclohexylamino)ethane sulfonic acid (CHES) | ||||||
Components | Preneck appendage protein | ||||||
Keywords | VIRAL PROTEIN / beta helix | ||||||
Function / homology | Function and homology information virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / adhesion receptor-mediated virion attachment to host cell / virion attachment to host cell / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus phage phi29 (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Xiang, Y. / Rossmann, M.G. | ||||||
Citation | Journal: Mol.Cell / Year: 2009 Title: Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Authors: Xiang, Y. / Leiman, P.G. / Li, L. / Grimes, S. / Anderson, D.L. / Rossmann, M.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3gq8.cif.gz | 135.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3gq8.ent.gz | 102.2 KB | Display | PDB format |
PDBx/mmJSON format | 3gq8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3gq8_validation.pdf.gz | 454.4 KB | Display | wwPDB validaton report |
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Full document | 3gq8_full_validation.pdf.gz | 459.8 KB | Display | |
Data in XML | 3gq8_validation.xml.gz | 25.6 KB | Display | |
Data in CIF | 3gq8_validation.cif.gz | 37.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gq/3gq8 ftp://data.pdbj.org/pub/pdb/validation_reports/gq/3gq8 | HTTPS FTP |
-Related structure data
Related structure data | 3gq7SC 3gq9C 3gqaC 3gqhC 3gqkC 3sucC 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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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 64410.914 Da / Num. of mol.: 1 / Fragment: D1*D2D3, residues 89-691 Source method: isolated from a genetically manipulated source Details: RESIDUES 89-854 EXPRESSED WITH A N-TERMIINAL HIS6 TAG Source: (gene. exp.) Bacillus phage phi29 (virus) / Gene: 12, gene product 12 / Plasmid: PET28B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: B3VMP8, UniProt: P20345*PLUS |
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-Non-polymers , 5 types, 308 molecules
#2: Chemical | ChemComp-CA / | ||
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#3: Chemical | ChemComp-MG / | ||
#4: Chemical | ChemComp-NHE / | ||
#5: Chemical | #6: Water | ChemComp-HOH / | |
-Details
Sequence details | THESE MUTATIONS MIGHT BE AN ACCUMULATE |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 66 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 10 Details: 100mM CHES at ~pH 10.0 and 8% PEG3K, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 21, 2008 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: SI(111) double-crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.03 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→44.24 Å / Num. obs: 62712 / % possible obs: 98.3 % / Redundancy: 10.6 % / Rmerge(I) obs: 0.103 / Χ2: 1.394 / Net I/σ(I): 25.233 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3GQ7 Resolution: 2→44.24 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.947 / Occupancy max: 1 / Occupancy min: 0.33 / SU B: 2.61 / SU ML: 0.073 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.12 / ESU R Free: 0.114 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 60.22 Å2 / Biso mean: 23.901 Å2 / Biso min: 11.16 Å2
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Refinement step | Cycle: LAST / Resolution: 2→44.24 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.054 Å / Total num. of bins used: 20
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