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- PDB-1try: STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 AN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1try | ||||||
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Title | STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS | ||||||
![]() | TRYPSIN | ||||||
![]() | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | ![]() trypsin / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Rypniewski, W.R. / Dambmann, C. / Von Der Osten, C. / Dauter, M. / Wilson, K.S. | ||||||
![]() | ![]() Title: Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A. Authors: Rypniewski, W.R. / Dambmann, C. / von der Osten, C. / Dauter, M. / Wilson, K.S. #1: ![]() Title: Evolutionary Divergence and Conservation of Trypsin Authors: Rypniewski, W.R. / Perrakis, A. / Vorgias, C.E. / Wilson, K.S. #2: ![]() Title: The Sequence and X-Ray Structure of the Trypsin from Fusarium Oxysporum Authors: Rypniewski, W.R. / Hastrup, S. / Betzel, Ch. / Dauter, M. / Dauter, Z. / Papendorf, G. / Branner, S. / Wilson, K.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 57.8 KB | Display | ![]() |
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PDB format | ![]() | 45 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.4 KB | Display | ![]() |
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Full document | ![]() | 433.7 KB | Display | |
Data in XML | ![]() | 15.7 KB | Display | |
Data in CIF | ![]() | 24.4 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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Unit cell |
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Components
#1: Protein | Mass: 22200.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-ISP / |
#3: Chemical | ChemComp-IPA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.37 % | ||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 36 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 5.5 / PH range high: 5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.55 Å / Lowest resolution: 10 Å / Num. obs: 23178 / % possible obs: 94.7 % / Num. measured all: 55012 / Rmerge(I) obs: 0.051 / Biso Wilson estimate: 22.4 Å2 |
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Reflection shell | *PLUS % possible obs: 69 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.55→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.55→10 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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