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Open data
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Basic information
Entry | Database: PDB / ID: 1avu | ||||||
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Title | TRYPSIN INHIBITOR FROM SOYBEAN (STI) | ||||||
![]() | TRYPSIN INHIBITOR | ||||||
![]() | SERINE PROTEASE INHIBITOR / TRYPSIN INHIBITOR / KUNITZ-TYPE / BETA-TREFOIL FOLD | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Song, H.K. / Suh, S.W. | ||||||
![]() | ![]() Title: Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina ...Title: Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. Authors: Song, H.K. / Suh, S.W. #1: ![]() Title: Crystal Structure Analyses of Human A1-Antitrypsin, Soybean Kunitz-Type Trypsin Inhibitor, and Barley Chitinase Authors: Song, H.K. #2: ![]() Title: Crystallization of Kunitz-Type Soybean Trypsin Inhibitor Authors: Lee, J.K. / Song, H.K. / Hwang, K.Y. / Kim, K.K. / Suh, S.W. #3: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Study of Kunitz-Type Soybean Trypsin Inhibitor Authors: Lee, J.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 42.4 KB | Display | ![]() |
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PDB format | ![]() | 32.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 416.4 KB | Display | ![]() |
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Full document | ![]() | 420.6 KB | Display | |
Data in XML | ![]() | 9.3 KB | Display | |
Data in CIF | ![]() | 11.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1avwC ![]() 1avxC ![]() 1tieS 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: 20115.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55 % |
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Crystal grow | pH: 7.5 / Details: pH 7.5 |
Crystal grow | *PLUS Method: other / Details: Lee, J., (1993) Mol. Cells, 3, 335. |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Mar 1, 1993 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→99 Å / Num. obs: 10234 / % possible obs: 76 % / Observed criterion σ(I): 0.5 / Redundancy: 2.7 % / Rmerge(I) obs: 0.045 |
Reflection shell | Resolution: 2.1→2.3 Å / % possible all: 26.7 |
Reflection | *PLUS Lowest resolution: 33 Å / Num. measured all: 27868 |
Reflection shell | *PLUS % possible obs: 26.7 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1TIE Resolution: 2.3→8 Å / Data cutoff high absF: 0 / Data cutoff low absF: 0 / σ(F): 2
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Displacement parameters | Biso mean: 38.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 0 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Xplor file |
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