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Yorodumi- PDB-3pmj: Bovine trypsin variant X(tripleIle227) in complex with small mole... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3pmj | ||||||
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Title | Bovine trypsin variant X(tripleIle227) in complex with small molecule inhibitor | ||||||
Components | Cationic trypsin | ||||||
Keywords | Hydrolase/Hydrolase Inhibitor / Trypsin-like serine protease / HYDROLASE / PROTEIN BINDING / DUODENUM / Hydrolase-Hydrolase Inhibitor complex | ||||||
Function / homology | Function and homology information 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 | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å | ||||||
Authors | Tziridis, A. / Neumann, P. / Kolenko, P. / Stubbs, M.T. | ||||||
Citation | Journal: Biol.Chem. / Year: 2014 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3pmj.cif.gz | 109.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3pmj.ent.gz | 82.1 KB | Display | PDB format |
PDBx/mmJSON format | 3pmj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3pmj_validation.pdf.gz | 730.5 KB | Display | wwPDB validaton report |
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Full document | 3pmj_full_validation.pdf.gz | 731.9 KB | Display | |
Data in XML | 3pmj_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | 3pmj_validation.cif.gz | 23 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pm/3pmj ftp://data.pdbj.org/pub/pdb/validation_reports/pm/3pmj | HTTPS FTP |
-Related structure data
Related structure data | 3plbC 3plkC 3plpC 3pm3C 3pwbC 3pwcC 3pyhC 3q00C 3unqC 3unsC 3uopC 3upeC 3uqoC 3uqvC 3uuzC 3uwiC 3uy9C 3v12C 3v13C 1v2kS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 23376.363 Da / Num. of mol.: 1 Mutation: N102E, L104Y, Y175S, P176S, G177F, Q178Y, S195A, V228I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Plasmid: pET3a / Production host: Escherichia coli (E. coli) / References: UniProt: P00760, trypsin |
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-Non-polymers , 6 types, 372 molecules
#2: Chemical | ChemComp-CA / | ||||
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#3: Chemical | ChemComp-PMJ / | ||||
#4: Chemical | ChemComp-GOL / | ||||
#5: Chemical | ChemComp-SO4 / #6: Chemical | ChemComp-CL / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 30% PEG 8000, 0.1M IMIDAZOLE, 0.3M AMMONIUM SULFATE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.91841 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Details: mirrors |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.45→25 Å / Num. all: 32308 / Num. obs: 32308 / % possible obs: 91 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 12.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1V2K Resolution: 1.45→21.8 Å / Cor.coef. Fo:Fc: 0.972 Isotropic thermal model: PROTEIN AND LIGANDS ANISOTROPIC, WATERS 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: 21.521 Å2
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Refinement step | Cycle: LAST / Resolution: 1.45→21.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.45→1.483 Å / Total num. of bins used: 20
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