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- PDB-3uns: Bovine trypsin variant X(triplePhe227) in complex with small mole... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3uns | ||||||
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Title | Bovine trypsin variant X(triplePhe227) in complex with small molecule inhibitor | ||||||
![]() | Cationic trypsin | ||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / Trypsin-like serine protease / HYDROLASE / PROTEIN BINDING / DUODENUM / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Tziridis, A. / Neumann, P. / Kolenko, P. / Stubbs, M.T. | ||||||
![]() | ![]() Title: Correlating structure and ligand affinity in drug discovery: a cautionary tale involving second shell residues. Authors: Tziridis, A. / Rauh, D. / Neumann, P. / Kolenko, P. / Menzel, A. / Brauer, U. / Ursel, C. / Steinmetzer, P. / Sturzebecher, J. / Schweinitz, A. / Steinmetzer, T. / Stubbs, M.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66 KB | Display | ![]() |
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PDB format | ![]() | 45.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 742.6 KB | Display | ![]() |
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Full document | ![]() | 743.1 KB | Display | |
Data in XML | ![]() | 13.8 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3plbC ![]() 3plkC ![]() 3plpC ![]() 3pm3C ![]() 3pmjC ![]() 3pwbC ![]() 3pwcC ![]() 3pyhC ![]() 3q00C ![]() 3unqC ![]() 3uopC ![]() 3upeC ![]() 3uqoC ![]() 3uqvC ![]() 3uuzC ![]() 3uwiC ![]() 3uy9C ![]() 3v12C ![]() 3v13C ![]() 1v2kS 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 23410.379 Da / Num. of mol.: 1 Mutation: N102E, L104Y, Y175S, P176S, G177F, Q178Y, S195A, V228F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 297 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/ANH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ANH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CA / | ||||
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#3: Chemical | ChemComp-ANH / | ||||
#4: Chemical | #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.51 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 20% PEG8000, 0.1M AMMONIUM SULPHATE, 0.1M IMIDAZOLE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944+ / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.542 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→43.48 Å / Num. all: 19879 / Num. obs: 19879 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3.7 / Redundancy: 5.7 % / Rmerge(I) obs: 0.083 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.414 / Mean I/σ(I) obs: 3.4 / Num. unique all: 1951 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1V2K Resolution: 1.8→43.48 Å / Cor.coef. Fo:Fc: 0.963 / SU B: 2.305 / SU ML: 0.069 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / 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: 23.768 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→43.48 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.847 Å / Total num. of bins used: 20
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