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- PDB-2bt8: Structure of the C-terminal receptor-binding domain of avian reov... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bt8 | ||||||
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Title | Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, space group P6322. | ||||||
![]() | SIGMA C | ||||||
![]() | VIRAL PROTEIN / ORTHOREOVIRUS / TRIPLE BETA-SPIRAL / BETA-BARREL | ||||||
Function / homology | ![]() Adenovirus Type 5 Fiber Protein (Receptor Binding Domain) - #40 / Reovirus sigma C capsid protein, C-terminal / Reovirus sigma C capsid protein triple beta spiral / Reovirus sigma C capsid protein C-terminal domain / Reovirus sigma C capsid protein triple beta spiral / reovirus attachment protein sigma1; domain 1 / Adenovirus Type 5 Fiber Protein (Receptor Binding Domain) / Laminin / Ribbon / Sandwich / Mainly Beta Similarity search - Domain/homology | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guardado Calvo, P. / Fox, G.C. / Hermo Parrado, X.L. / Llamas-Saiz, A.L. / van Raaij, M.J. | ||||||
![]() | ![]() 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. #1: ![]() Title: Crystal Structure of Reovirus Attachment Protein Sigma1 Reveals Evolutionary Relationship to Adenovirus Fiber Authors: Chappell, J.D. / Prota, A.E. / Dermody, T.S. / Stehle, T. #2: Journal: J.Virol. / Year: 1997 Title: Protein Architecture of Avian Reovirus S1133 and Identification of the Cell Attachment Protein Authors: Martinez-Costas, J. / Grande, A. / Varela, R. / Garcia-Martinez, C. / Benavente, J. #3: Journal: Virology / Year: 2000 Title: Oligomerization and Cell-Binding Properties of the Avian Reovirus Cell-Attachment Protein Sigmac Authors: Grande, A. / Rodriguez, E. / Costas, C. / Everitt, E. / Benavente, J. #4: Journal: Virology / Year: 2001 Title: The Avian Reovirus Genome Segment S1 is a Functionally Tricistronic Gene that Expresses One Structure and Two Nonstructural Proteins in Infected Cells Authors: Bodelon, G. / Labrada, L. / Martinez-Costas, J. / Benavente, J. #5: Journal: J.Gen.Virol. / Year: 2002 Title: Subunit Composition and Conformational Stability of the Oligomeric Form of the Avian Reovirus Cell-Attachment Protein Sigmac Authors: Grande, A. / Costas, C. / Benavente, 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 | ![]() | 45.1 KB | Display | ![]() |
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PDB format | ![]() | 32.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 411.9 KB | Display | ![]() |
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Full document | ![]() | 414.3 KB | Display | |
Data in XML | ![]() | 8.7 KB | Display | |
Data in CIF | ![]() | 11.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Details | THIS IS A COMPLEX OF TWO TRIMERS |
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Components
#1: Protein | Mass: 18324.336 Da / Num. of mol.: 1 Fragment: C-TERMINAL RECEPTOR-BINDING REGION, RESIDUES 157-326 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: PET28CPLUS / Production host: ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.3 Å3/Da / Density % sol: 77 % |
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Crystal grow | pH: 8.5 Details: 100 MM TRIS-HCL PH 8.5, 1.5 M AMMONIUM SULPHATE, 12% GLYCEROL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 27, 2004 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DOUBLE CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97565 Å / Relative weight: 1 |
Reflection | Resolution: 2.71→30 Å / Num. obs: 10910 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 8.8 % / Biso Wilson estimate: 61.56 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 8.2 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 9.2 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 2.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 255-257 WERE MODELED AS WATERS.
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.25 Å2
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Refinement step | Cycle: LAST / Resolution: 3→121.27 Å
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Refine LS restraints |
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