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- PDB-1qnj: THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RES... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qnj | ||||||
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Title | THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RESOLUTION (1.1 A) | ||||||
![]() | ELASTASE | ||||||
![]() | HYDROLASE (SERINE PROTEASE) / HYDROLASE(SERINE PROTEASE) / ATOMIC RESOLUTION | ||||||
Function / homology | ![]() pancreatic elastase / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wurtele, M. / Hahn, M. / Hilpert, K. / Hohne, W. | ||||||
![]() | ![]() Title: Atomic Resolution Structure of Native Porcine Pancreatic Elastase at 1.1 A Authors: Wurtele, M. / Hahn, M. / Hilpert, K. / Hohne, W. #1: ![]() Title: Inhibition of Elastase by N-Sulfonylaryl Beta-Lactams: Anatomy of a Stable Acyl-Enzyme Complex Authors: Wilmouth, R.C. / Westwood, N.J. / Anderson, K. / Brownlee, W. / Claridge, T.D.W. / Clifton, I.J. / Pritchard, G.J. / Aplin, R.T. / Schofield, C.J. #2: ![]() Title: Structure of Native Porcine Pancreatic Elastase at 1.65 Angstroms Resolution Authors: Meyer, E. / Cole, G. / Radhakrishnan, R. / Epp, O. #3: ![]() Title: The Atomic Structure of Crystalline Porcine Pancreatic Elastase at 2.5 Angstroms Resolution. Comparisons with the Structure of Alpha- Chymotrypsin Authors: Sawyer, L. / Shotton, D.M. / Campbell, J.W. / Wendell, P.L. / Muirhead, H. / Watson, H.C. / Diamond, R. / Ladner, R.C. #4: Journal: Nature / Year: 1970 Title: Three-Dimensional Fourier Synthesis of Tosyl-Elastase at 3.5 Angstroms Resolution Authors: Watson, H.C. / Shotton, D.M. / Cox, J.M. / Muirhead, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 183.7 KB | Display | ![]() |
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PDB format | ![]() | 140.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425 KB | Display | ![]() |
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Full document | ![]() | 426.8 KB | Display | |
Data in XML | ![]() | 15 KB | Display | |
Data in CIF | ![]() | 23.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1btuS 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: 25929.016 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PORCINE PANCREATIC ELASTASE / Source: (natural) ![]() ![]() | ||||
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#2: Chemical | ChemComp-NA / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Compound details | RESIDUE NUMBERING FOLLOWS THE NUMBERING OF BOVINE CHYMOTRYPSINOGEN A. THE RESIDUE ASN-77 OF ...RESIDUE NUMBERING FOLLOWS THE NUMBERING OF BOVINE CHYMOTRYPS | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 32.6 % | ||||||||||||||||||
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Crystal grow | Temperature: 291 K / pH: 8 / Details: 0.25 M NA2SO4 18 DEGREES CELSIUS, pH 8.00 | ||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 8 / PH range high: 7 | ||||||||||||||||||
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: Mar 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9116 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→45.6 Å / Num. obs: 81820 / % possible obs: 92.7 % / Redundancy: 13.1 % / Rmerge(I) obs: 0.045 / Net I/σ(I): 14.9 |
Reflection shell | Resolution: 1.1→1.14 Å / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.02 / % possible all: 60.4 |
Reflection | *PLUS Num. measured all: 1071726 |
Reflection shell | *PLUS % possible obs: 60.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1BTU Resolution: 1.1→45.6 Å / Num. parameters: 19897 / Num. restraintsaints: 24006 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC SCALING APPLIED BY THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28 (1995)53-56
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Solvent computation | Solvent model: MOEWS & KRETSINGER | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 23 / Occupancy sum hydrogen: 1762 / Occupancy sum non hydrogen: 2177 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→45.6 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.1267 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_plane_restr / Dev ideal: 0.0289 |