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Open data
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Basic information
Entry | Database: PDB / ID: 1jiw | ||||||
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Title | Crystal structure of the APR-APRin complex | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / Pseudomonas aeruginosa alkaline protease inhibitor / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() serralysin / negative regulation of complement activation, lectin pathway / metalloendopeptidase inhibitor activity / negative regulation of complement activation, classical pathway / positive regulation of sodium ion transport / metalloendopeptidase activity / peptidase activity / periplasmic space / calcium ion binding / proteolysis ...serralysin / negative regulation of complement activation, lectin pathway / metalloendopeptidase inhibitor activity / negative regulation of complement activation, classical pathway / positive regulation of sodium ion transport / metalloendopeptidase activity / peptidase activity / periplasmic space / calcium ion binding / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hege, T. / Feltzer, R.E. / Gray, R.D. / Baumann, U. | ||||||
![]() | ![]() Title: Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond Authors: Hege, T. / Feltzer, R.E. / Gray, R.D. / Baumann, U. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.3 KB | Display | ![]() |
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PDB format | ![]() | 103.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.4 KB | Display | ![]() |
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Full document | ![]() | 442.8 KB | Display | |
Data in XML | ![]() | 27.4 KB | Display | |
Data in CIF | ![]() | 41.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1go7C ![]() 1go8C ![]() 1aklS 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: 49531.426 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q03023, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases | ||
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#2: Protein | Mass: 11396.819 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
#3: Chemical | ChemComp-ZN / | ||
#4: Chemical | ChemComp-CA / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.38 Å3/Da / Density % sol: 63.62 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion / pH: 5.6 Details: tri-Na-citrate, isopropanol, PEG 4000, pH 5.6, VAPOR DIFFUSION, temperature 291K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 11, 2000 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 1.74→14.93 Å / Num. all: 84588 / Num. obs: 84597 / % possible obs: 98.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 15.1 Å2 / Limit h max: 43 / Limit h min: 0 / Limit k max: 67 / Limit k min: 0 / Limit l max: 52 / Limit l min: 0 / Observed criterion F max: 2076195.96 / Observed criterion F min: 9.8 |
Reflection shell | Resolution: 1.74→1.77 Å / % possible all: 78.8 |
Reflection | *PLUS Num. measured all: 310401 / Rmerge(I) obs: 0.037 |
Reflection shell | *PLUS % possible obs: 78.8 % / Rmerge(I) obs: 0.212 / Mean I/σ(I) obs: 5.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1AKL Resolution: 1.74→14.93 Å / Rfactor Rfree error: 0.002 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 50.9632 Å2 / ksol: 0.384305 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 108.98 Å2 / Biso mean: 19.54 Å2 / Biso min: 1.13 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.74→14.93 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 8.1 % / Rfactor obs: 0.184 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.216 / % reflection Rfree: 8.1 % / Rfactor Rwork: 0.217 |