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- PDB-6t71: 3C-like protease from Southampton virus complexed with XST00000375b. -
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Open data
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Basic information
Entry | Database: PDB / ID: 6t71 | ||||||
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Title | 3C-like protease from Southampton virus complexed with XST00000375b. | ||||||
![]() | (Genome polyprotein) x 2 | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | Southampton virus | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Guo, J. / Cooper, J.B. | ||||||
![]() | ![]() Title: In crystallo-screening for discovery of human norovirus 3C-like protease inhibitors. Authors: Guo, J. / Douangamath, A. / Song, W. / Coker, A.R. / Chan, A.W.E. / Wood, S.P. / Cooper, J.B. / Resnick, E. / London, N. / Delft, F.V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164.4 KB | Display | ![]() |
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PDB format | ![]() | 129 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6t1qSC ![]() 6t2iC ![]() 6t2xC ![]() 6t3gC ![]() 6t49C ![]() 6t4eC ![]() 6t4sC ![]() 6t5dC ![]() 6t5rC ![]() 6t6wC ![]() 6t82C ![]() 6t8rC ![]() 6t8tC ![]() 6talC ![]() 6tawC ![]() 6tboC ![]() 6tbpC ![]() 6tc1C ![]() 6tcfC ![]() 6tglC 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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Components on special symmetry positions |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 18387.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() ![]() References: UniProt: Q04544, nucleoside-triphosphate phosphatase, ![]() ![]() |
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#2: Protein | Mass: 18290.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() ![]() References: UniProt: Q04544, nucleoside-triphosphate phosphatase, ![]() ![]() |
-Non-polymers , 4 types, 356 molecules ![](data/chem/img/MQB.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | ChemComp-DMS / | ![]() #5: Chemical | ChemComp-PO4 / | ![]() #6: Water | ChemComp-HOH / | ![]() |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.54 % |
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Crystal grow![]() | Temperature: 294 K / Method: vapor diffusion, sitting drop / pH: 5.1 Details: Protein concentration 4 mg/ml. 0.2 M ammonium citrate and 12% (v/v) PEG3350. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 4, 2016 | |||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||
Radiation wavelength | Wavelength![]() | |||||||||||||||||||||||||||
Reflection | Resolution: 1.52→60.95 Å / Num. obs: 51832 / % possible obs: 99.8 % / Redundancy: 3.1 % / CC1/2: 0.998 / Rmerge(I) obs: 0.047 / Rpim(I) all: 0.031 / Rrim(I) all: 0.056 / Net I/σ(I): 9.6 / Num. measured all: 162852 / Scaling rejects: 10 | |||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 6t1q Resolution: 1.52→60.93 Å / Cor.coef. Fo:Fc: 0.983 / Cor.coef. Fo:Fc free: 0.965 / SU B: 4.791 / SU ML: 0.071 / SU R Cruickshank DPI: 0.0799 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.08 / ESU R Free: 0.077 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS ANISOTROPIC U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 127.96 Å2 / Biso mean: 27.703 Å2 / Biso min: 9.7 Å2
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Refinement step | Cycle: final / Resolution: 1.52→60.93 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.52→1.559 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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