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Open data
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Basic information
Entry | Database: PDB / ID: 1wyk | ||||||
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Title | SINDBIS VIRUS CAPSID PROTEIN (114-264) | ||||||
![]() | SINDBIS VIRUS CAPSID PROTEIN | ||||||
![]() | Viral protein / hydrolase / COAT PROTEIN / SINDBIS / VIRUS / PROTEINASE / ALPHAVIRUS / CAPSID / DIOXANE | ||||||
Function / homology | ![]() togavirin / T=4 icosahedral viral capsid / host cell cytoplasm / membrane => GO:0016020 / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / host cell nucleus / virion attachment to host cell / host cell plasma membrane / structural molecule activity ...togavirin / T=4 icosahedral viral capsid / host cell cytoplasm / membrane => GO:0016020 / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / host cell nucleus / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / RNA binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lee, S. / Kuhn, R.J. / Rossmann, M.G. | ||||||
![]() | ![]() Title: Probing the potential glycoprotein binding site of sindbis virus capsid protein with dioxane and model building. Authors: Lee, S. / Kuhn, R.J. / Rossmann, M.G. #1: ![]() Title: Identification of a Protein Binding Site on the Surface of the Alphavirus Nucleocapsid and its Implication in Virus Assembly Authors: Lee, S. / Owen, K.E. / Choi, H.K. / Lee, H. / Lu, G. / Wengler, G. / Brown, D.T. / Rossmann, M.G. / Kuhn, R.J. #2: ![]() Title: Structure of Sindbis Virus Core Protein Reveals a Chymotrypsin-Like Serine Proteinase and the Organization of the Virion Authors: Choi, H.K. / Tong, L. / Minor, W. / Dumas, P. / Boege, U. / Rossmann, M.G. / Wengler, 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 | ![]() | 176.4 KB | Display | ![]() |
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PDB format | ![]() | 140.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 476.7 KB | Display | ![]() |
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Full document | ![]() | 483.7 KB | Display | |
Data in XML | ![]() | 29.4 KB | Display | |
Data in CIF | ![]() | 42.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 16676.828 Da / Num. of mol.: 4 / Fragment: C-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P27285, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Chemical | ChemComp-FOR / #3: Chemical | ChemComp-DIO / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: 20-26%(W/V) PEG 8000, 100 MM SODIUM CACODYLATE, PH6.5, 150MM SODIUM ACETATE, 6%(V/V) DIOXANE | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.6 / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Oct 26, 1995 / Details: BENT FOCUSING MIRROR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 28851 / % possible obs: 78.3 % / Observed criterion σ(I): 1 / Redundancy: 1.9 % / Biso Wilson estimate: 15.2 Å2 / Rsym value: 0.028 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 1.6 % / Mean I/σ(I) obs: 6 / Rsym value: 0.089 / % possible all: 28.8 |
Reflection | *PLUS Num. measured all: 53873 / Rmerge(I) obs: 0.028 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: SINDBIS VIRUS CAPSID PROTEIN MUTANT (S215A, 106-266) IN TRICLINIC CRYSTAL Resolution: 2→8 Å / Rfactor Rfree error: 0.0072 / Data cutoff high absF: 304 / Data cutoff low absF: 9.7 / σ(F): 1
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Displacement parameters | Biso mean: 15.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 30 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: MOL1 AND MOL4, MOL2 AND MOL3 WERE RESTRAINED IN A PAIRWISE MANNER DURING REFINEMENT. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2→2.03 Å / Rfactor Rfree error: 0.074 / Total num. of bins used: 20
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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