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- PDB-1pi2: REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pi2 | ||||||
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Title | REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS | ||||||
![]() | BOWMAN-BIRK INHIBITOR (PI-II) | ||||||
![]() | SERINE PROTEINASE INHIBITOR | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Chen, P. / Rose, J. / Wang, B.C. | ||||||
![]() | ![]() Title: Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors. Authors: Chen, P. / Rose, J. / Love, R. / Wei, C.H. / Wang, B.C. #1: ![]() Title: Crystallization of Two Cubic Forms of Soybean Trypsin Inhibitor E-I, a Member of the Bowman-Birk Inhibitor Family Authors: Wei, C.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 | ![]() | 20.4 KB | Display | ![]() |
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PDB format | ![]() | 13.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 363.6 KB | Display | ![]() |
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Full document | ![]() | 365.1 KB | Display | |
Data in XML | ![]() | 3.1 KB | Display | |
Data in CIF | ![]() | 3.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES 18 AND 44 ARE CIS-PROLINES. |
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Components
#1: Protein | Mass: 7213.337 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.2 Å3/Da / Density % sol: 70.73 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 4.6 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 9999 Å / Num. all: 5488 / % possible obs: 95.1 % / Num. measured all: 75913 / Rmerge(I) obs: 0.0777 |
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Processing
Software | Name: GPRLSA / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.236 / Highest resolution: 2.5 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Rfactor obs: 0.236 / Lowest resolution: 8 Å / Num. reflection obs: 3287 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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