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Open data
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Basic information
Entry | Database: PDB / ID: 2jjl | ||||||
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Title | Structure of avian reovirus sigmaC117-326, P321 crystal form | ||||||
![]() | SIGMA-C CAPSID PROTEIN | ||||||
![]() | VIRAL PROTEIN / ALPHA-HELICAL COILED COIL / RECEPTOR-BINDING / TRIPLE BETA-SPIRAL / VIRION / COILED COIL / BETA-BARREL | ||||||
Function / homology | ![]() viral capsid / symbiont entry into host cell / virion attachment to host cell / apoptotic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guardado-Calvo, P. / Fox, G.C. / Llamas-Saiz, A.L. / Benavente, J. / van Raaij, M.J. | ||||||
![]() | ![]() Title: Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre. Authors: Guardado-Calvo, P. / Fox, G.C. / Llamas-Saiz, A.L. / van Raaij, M.J. #1: Journal: Acta Crystallogr., Sect.F / Year: 2005 Title: Crystallization of the C-Terminal Globular Domain of Avian Reovirus Fibre. Authors: van Raaij, M.J. / Hermo-Parrado, X.L. / Guardado-Calvo, P. / Fox, G.C. / Llamas-Saiz, A.L. / Costas, C. / Martinez-Costas, J. / Benavente, J. #2: ![]() Title: Structure of the Carboxy-Terminal Receptor-Binding Domain of Avian Reovirus Fibre Sigmac. Authors: Guardado-Calvo, P. / Fox, G.C. / Hermo-Parrado, X.L. / Llamas-Saiz, A.L. / Costas, C. / Martinez-Costas, J. / Benavente, J. / van Raaij, M.J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.1 KB | Display | ![]() |
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PDB format | ![]() | 41.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2vrsSC 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 22587.023 Da / Num. of mol.: 1 / Fragment: RESIDUES 117-326 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: THE AVIAN REOVIRUS STRAIN S1133 WAS ORIGINALLY PROVIDED BY DR. PHILIP I.MARCUS WHEN DR. J.BENAVENTE WAS A ROCHE VISITING SCIENTIST IN THE LABORATORY OF DR. A.SHATKIN Plasmid: PET28C-PLUS / Production host: ![]() ![]() | ||||||||
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#2: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | THE FIRST RESIDUE, ILE-116, IS A REMNANT OF THE EXPRESSION | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.7 Å3/Da / Density % sol: 73.7 % / Description: NONE |
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Crystal grow | pH: 8.4 Details: 0.6-0.75 M AMMONIUM SULPHATE, 0.1 M TRIS-HCL PH 8.4, 25% GLYCEROL, 50 MM ZINC SULPHATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 3, 2007 / Details: RD COATED FLAT AND TOROIDAL MIRRORS |
Radiation | Monochromator: SI111 DOUBLE-CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.984 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 19318 / % possible obs: 99 % / Redundancy: 20 % / Biso Wilson estimate: 44.1 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 52.6 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 20.3 % / Rmerge(I) obs: 0.43 / Mean I/σ(I) obs: 10.4 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: CHAIN C OF PDB ENTRY 2VRS Resolution: 2.3→25 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.94 / SU B: 3.7 / SU ML: 0.093 / Cross valid method: THROUGHOUT / ESU R: 0.175 / ESU R Free: 0.165 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.49 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→25 Å
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