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- PDB-4aju: Crystal structure of the reactive loop cleaved ZPI in P41 space group -
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Open data
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Basic information
Entry | Database: PDB / ID: 4aju | ||||||
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Title | Crystal structure of the reactive loop cleaved ZPI in P41 space group | ||||||
![]() | (PROTEIN Z-DEPENDENT PROTEASE INHIBITOR) x 2 | ||||||
![]() | BLOOD CLOTTING / SERPIN / PROTEIN Z / ZPI COAGULATION | ||||||
Function / homology | ![]() liver regeneration / Post-translational protein phosphorylation / serine-type endopeptidase inhibitor activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood coagulation / heparin binding / endoplasmic reticulum lumen / extracellular space / extracellular exosome Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zhou, A. / Yan, Y. / Wei, Z. | ||||||
![]() | ![]() Title: Structural Basis for Catalytic Activation of Protein Z-Dependent Protease Inhibitor (Zpi) by Protein Z. Authors: Huang, X. / Yan, Y. / Tu, Y. / Gatti, J. / Broze, G.J.J. / Zhou, A. / Olson, S.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 | ![]() | 169.9 KB | Display | ![]() |
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PDB format | ![]() | 135.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 456.1 KB | Display | ![]() |
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Full document | ![]() | 460.2 KB | Display | |
Data in XML | ![]() | 15.5 KB | Display | |
Data in CIF | ![]() | 20.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4afxC ![]() 4ajtC ![]() 7apiS C: citing same article ( S: Starting model for refinement |
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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: 44357.996 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-408 / Mutation: YES Source method: isolated from a genetically manipulated source Details: REACTIVE LOOP CLEAVED ZPI / Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 4167.010 Da / Num. of mol.: 1 / Fragment: RESIDUES 409-444 / Mutation: YES Source method: isolated from a genetically manipulated source Details: REACTIVE LOOP CLEAVED ZPI / Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-EDO / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 45 % / Description: NONE |
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Crystal grow | pH: 4.5 / Details: 10% 2-PROPANOL, 0.2M LI2SO4, 0.1M NAAC, PH4.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→100.26 Å / Num. obs: 22072 / % possible obs: 95.8 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 2.65→2.79 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.72 / Mean I/σ(I) obs: 1.5 / % possible all: 82.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 7API Resolution: 2.65→100.5 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.923 / SU B: 22.72 / SU ML: 0.21 / Cross valid method: THROUGHOUT / ESU R: 0.362 / ESU R Free: 0.274 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 77.299 Å2
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Refinement step | Cycle: LAST / Resolution: 2.65→100.5 Å
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Refine LS restraints |
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