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- PDB-1eai: COMPLEX OF ASCARIS CHYMOTRPSIN/ELASTASE INHIBITOR WITH PORCINE EL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1eai | ||||||
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Title | COMPLEX OF ASCARIS CHYMOTRPSIN/ELASTASE INHIBITOR WITH PORCINE ELASTASE | ||||||
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![]() | SERINE PROTEINASE / ELASTASE / ASCARIS SUMM / PROTEIN INHIBITOR | ||||||
Function / homology | ![]() pancreatic elastase / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Huang, K. / Strynadka, N.C.J. / Bernard, V.D. / Peanasky, R.J. / James, M.N.G. | ||||||
![]() | ![]() Title: The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Authors: Huang, K. / Strynadka, N.C. / Bernard, V.D. / Peanasky, R.J. / James, M.N. #1: ![]() Title: Structure of Native Porcine Pancreatic Elastase at 1.65 Resolution Authors: Meyer, E. / Cole, G. / Radharkrishnan, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 128.4 KB | Display | ![]() |
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PDB format | ![]() | 100.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 388.3 KB | Display | ![]() |
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Full document | ![]() | 416 KB | Display | |
Data in XML | ![]() | 16 KB | Display | |
Data in CIF | ![]() | 24.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1incS 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.9963, 0.0813, -0.0277), Vector: |
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Components
#1: Protein | Mass: 25929.016 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 6602.523 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.84 % | ||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 29261 / % possible obs: 99 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.07 / Rsym value: 0.07 |
Reflection shell | Highest resolution: 2.4 Å / Rsym value: 0.07 |
Reflection | *PLUS Num. measured all: 192689 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.5 Å / % possible obs: 71 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1INC Resolution: 2.4→20 Å / Isotropic thermal model: TNT BCOOREL / σ(F): 0 / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.191 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_plane_restr / Dev ideal: 0.026 |