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Open data
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Basic information
Entry | Database: PDB / ID: 1fni | ||||||
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Title | CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.01% POLYDOCANOL | ||||||
![]() | TRYPSIN | ||||||
![]() | HYDROLASE / SERINE PROTEASE | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Deepthi, S. / Johnson, A. / Pattabhi, V. | ||||||
![]() | ![]() Title: Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol. Authors: Deepthi, S. / Johnson, A. / Pattabhi, V. #1: ![]() Title: Crystal Structure at 1.63 Angstroms Resolution of the Native Form of Porcine Beta Trypsin : Revealing an Acetate Ion Binding Site and Functional Water Network Authors: Johnson, A. / Gautham, N. / Pattabhi, V. #2: ![]() Title: The First Structure at 1.8 Angstroms Resolution of an Active Autolysate Form of Porcine Alpha Trypsin Authors: Johnson, A. / Krishnaswamy, S. / Sundaram, P.V. / Pattabhi, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59.7 KB | Display | ![]() |
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PDB format | ![]() | 42 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387 KB | Display | ![]() |
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Full document | ![]() | 390.4 KB | Display | |
Data in XML | ![]() | 6.6 KB | Display | |
Data in CIF | ![]() | 10 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fmgC ![]() 1fn6C ![]() 1qquS 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: 23491.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() | ||||
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#2: Chemical | ChemComp-SO4 / | ||||
#3: Chemical | ChemComp-CA / | ||||
#4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | Sequence details | THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.64 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.7 / Details: pH 6.70, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 6.7 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 19, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.64→23.42 Å / Num. obs: 22228 / % possible obs: 82.68 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.0652 / Net I/σ(I): 20.08 |
Reflection shell | Resolution: 1.64→1.8 Å / Redundancy: 3 % / Rmerge(I) obs: 0.4153 / Mean I/σ(I) obs: 1.76 / % possible all: 56.8 |
Reflection | *PLUS Num. measured all: 88932 / Rmerge(I) obs: 0.065 |
Reflection shell | *PLUS Num. unique obs: 4475 / Rmerge(I) obs: 0.415 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QQU Resolution: 1.6→8 Å / Cross valid method: FREE R / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.6→8 Å
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Software | *PLUS Name: X-PLOR,REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.64 Å / Rfactor all: 0.185 / Rfactor Rfree: 0.234 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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