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- PDB-3p95: Human mesotrypsin complexed with bovine pancreatic trypsin inhibi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3p95 | ||||||
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Title | Human mesotrypsin complexed with bovine pancreatic trypsin inhibitor variant (BPTI-K15R/R17D) | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / Human mesotrypsin-canonical inhibitor complex / Mesotrypsin / Trypsin IV / Bovine Pancreatic Trypsin Inhibitor / canonical inhibitor / BPTI-K15R/R17D / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() Uptake of dietary cobalamins into enterocytes / trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / antimicrobial humoral response / Alpha-defensins / zymogen activation ...Uptake of dietary cobalamins into enterocytes / trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / antimicrobial humoral response / Alpha-defensins / zymogen activation / Antimicrobial peptides / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / endothelial cell migration / trypsin / serine protease inhibitor complex / digestion / serine-type peptidase activity / serine-type endopeptidase inhibitor activity / tertiary granule lumen / protease binding / serine-type endopeptidase activity / calcium ion binding / Neutrophil degranulation / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Salameh, M.A. / Soares, A.S. / Radisky, E.S. | ||||||
![]() | ![]() Title: The P2' residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activity. Authors: Salameh, M.A. / Soares, A.S. / Hockla, A. / Radisky, D.C. / Radisky, E.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 181.8 KB | Display | ![]() |
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PDB format | ![]() | 145.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.7 KB | Display | ![]() |
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Full document | ![]() | 436.7 KB | Display | |
Data in XML | ![]() | 16.3 KB | Display | |
Data in CIF | ![]() | 24.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3p92C ![]() 2r9pS 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
#1: Protein | Mass: 24257.457 Da / Num. of mol.: 1 / Mutation: S195A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 6513.476 Da / Num. of mol.: 1 / Fragment: UNP Residues 36-93 / Mutation: K15R, R17D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 34.58 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 25% PEG4000, 0.2M Na acetate and 100mM Tris pH 8.0, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Detector | Type: ADSC QUANTUM 4 / Detector: CCD | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.299→50 Å / Num. obs: 53441 / % possible obs: 94.4 % / Redundancy: 6.3 % / Rmerge(I) obs: 0.068 / Χ2: 1.21 / Net I/σ(I): 17.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2R9P Resolution: 1.2991→33.817 Å / Occupancy max: 1 / Occupancy min: 0 / FOM work R set: 0.9487 / SU ML: 0.07 / σ(F): 0.06 / Phase error: 10.34 / Stereochemistry target values: MLHL
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 62.547 Å2 / ksol: 0.485 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 119.66 Å2 / Biso mean: 19.2292 Å2 / Biso min: 6.32 Å2
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Refinement step | Cycle: LAST / Resolution: 1.2991→33.817 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14
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