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Open data
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Basic information
Entry | Database: PDB / ID: 1db2 | ||||||
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Title | CRYSTAL STRUCTURE OF NATIVE PLASMINOGEN ACTIVATOR INHIBITOR-1 | ||||||
![]() | PLASMINOGEN ACTIVATOR INHIBITOR-1![]() | ||||||
![]() | hydrolase inhibitor / NATIVE SERPIN | ||||||
Function / homology | ![]() positive regulation of leukotriene production involved in inflammatory response / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nar, H. / Bauer, M. / Stassen, J.M. / Lang, D. / Gils, A. / Declerck, P. | ||||||
![]() | ![]() Title: Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. Authors: Nar, H. / Bauer, M. / Stassen, J.M. / Lang, D. / Gils, A. / Declerck, P.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.3 KB | Display | ![]() |
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PDB format | ![]() | 122.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 42513.738 Da / Num. of mol.: 2 / Mutation: N150H, K154T, Q301P, Q319L, M354I Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 66.38 % | ||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.6 Details: sodium chloride, sodium/potassium phosphate, pH 6.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 20, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.55→20 Å / Num. all: 706774 / Num. obs: 42076 / % possible obs: 95.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 16.8 % / Biso Wilson estimate: 51 Å2 / Rmerge(I) obs: 0.085 / Net I/σ(I): 5.5 |
Reflection shell | Resolution: 2.55→2.59 Å / Rmerge(I) obs: 0.551 / % possible all: 78.3 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 100 Å / Num. obs: 35572 / % possible obs: 97.8 % / Num. measured all: 603807 / Rmerge(I) obs: 0.078 |
Reflection shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.75 Å / % possible obs: 90.1 % / Rmerge(I) obs: 0.383 |
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Processing
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Refinement | Resolution: 2.7→20 Å / σ(F): 1 / σ(I): 1 / Stereochemistry target values: Engh & Huber Details: THE EXPERIMENTAL DATA SET IS PARTIALLY MEROHEDRALLY TWINNED WITH A TWINNING INDEX OF 0.28. THE STRUCTURE WAS REFINED AGAINST DETWINNED DATA.
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS σ(F): 1 / Num. reflection Rfree: 1954 / Rfactor obs: 0.255 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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