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- PDB-1v1i: Adenovirus fibre shaft sequence N-terminally fused to the bacteri... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1v1i | ||||||
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Title | Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a long linker | ||||||
![]() | FIBRITIN, FIBER PROTEIN | ||||||
![]() | ADENOVIRUS / CHIMERA / FIBER PROTEIN | ||||||
Function / homology | ![]() adhesion receptor-mediated virion attachment to host cell / virion component / viral capsid / cell adhesion / symbiont entry into host cell / host cell nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Papanikolopoulou, K. / Teixeira, S. / Belrhali, H. / Forsyth, V.T. / Mitraki, A. / van Raaij, M.J. | ||||||
![]() | ![]() Title: Adenovirus Fibre Shaft Sequences Fold Into the Native Triple Beta-Spiral Fold When N-Terminally Fused to the Bacteriophage T4 Fibritin Foldon Trimerisation Motif Authors: Papanikolopoulou, K. / Teixeira, S. / Belrhali, H. / Forsyth, V.T. / Mitraki, A. / van Raaij, M.J. #1: Journal: J.Biol.Chem. / Year: 2004 Title: Formation of Highly Stable Chimeric Trimers by Fusion of an Adenovirus Fiber Shaft Fragment with the Foldon Domain of Bacteriophage T4 Fibritin Authors: Papanikolopoulou, K. / Forge, V. / Goeltz, P. / Mitraki, A. #2: ![]() Title: A Triple Beta-Spiral in the Adenovirus Fibre Shaft Reveals a New Structural Motif for a Fibrous Protein Authors: van Raaij, M.J. / Mitraki, A. / Lavigne, G. / Cusack, S. #3: ![]() Title: Structure of Bacteriophage T4 Fibritin M: A Troublesome Packing Arrangement Authors: Strelkov, S. / Tao, Y. / Shneider, M.M. / Mesyanzhinov, V. / Rossmann, M.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.1 KB | Display | ![]() |
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PDB format | ![]() | 57.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.8 KB | Display | ![]() |
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Full document | ![]() | 453.6 KB | Display | |
Data in XML | ![]() | 16.6 KB | Display | |
Data in CIF | ![]() | 23.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1v1hC ![]() 1avyS ![]() 1qiuS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 11509.702 Da / Num. of mol.: 3 Fragment: SHAFT DOMAIN PLUS FOLDON DOMAIN, RESIDUES 319-392 AND 457-483 Source method: isolated from a genetically manipulated source Details: ARTIFICIAL FUSION PROTEIN OF ADENOVIRUS TYPE 2 FIBRE SHAFT RESIDUES 319-398 - BACTERIOPHAGE T4 FIBRITIN FOLDON RESIDUES 457-483 WITH A GLY-SER LINKER IN BETWEEN Source: (gene. exp.) ![]() ![]() Plasmid: PT7.7 / Production host: ![]() ![]() #2: Water | ChemComp-HOH / | Compound details | ADENOVIRUS FIBRE IS RESPONSIBLE FOR ADENOVIRUS RECEPTOR BINDING AND CONTAINS A VIRUS-BINDING N- ...ADENOVIRUS | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.8 % |
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Crystal grow | pH: 7 Details: 10 MM HEPES-NAOH PH 7.0 0.2 M MAGNESIUM ACETATE, 20 % (W/V) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 24, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9202 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 25299 / % possible obs: 99.9 % / Redundancy: 13.8 % / Biso Wilson estimate: 25.453 Å2 / Rmerge(I) obs: 0.068 / Rsym value: 0.068 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 10.5 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.2 / Rsym value: 0.33 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QIU, PDB ENTRY 1AVY Resolution: 1.9→19.9 Å / SU B: 4.5422 / SU ML: 0.1332 / Cross valid method: THROUGHOUT / ESU R: 0.1933 / ESU R Free: 0.1788
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Displacement parameters | Biso mean: 32.746 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→19.9 Å
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