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- PDB-1yjb: SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yjb | ||||||
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Title | SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 35% DIMETHYLFORMAMIDE | ||||||
![]() | SUBTILISIN 8397+1 | ||||||
![]() | HYDROLASE (SERINE PROTEASE) / HYDROLASE / SPORULATION / SERINE PROTEASE / ZYMOGEN | ||||||
Function / homology | ![]() subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kidd, R.D. / Farber, G.K. | ||||||
![]() | ![]() Title: Breaking the low barrier hydrogen bond in a serine protease. Authors: Kidd, R.D. / Sears, P. / Huang, D.H. / Witte, K. / Wong, C.H. / Farber, G.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 | ![]() | 58.1 KB | Display | ![]() |
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PDB format | ![]() | 44.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 413.9 KB | Display | ![]() |
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Full document | ![]() | 415.6 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 18 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 27581.498 Da / Num. of mol.: 1 / Mutation: M50F, N76D, G169A, Q206C, N218S, K256Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.8 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU AFC-6R / Detector: DIFFRACTOMETER / Date: Jul 15, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→17 Å / Num. obs: 21228 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 1 % / Rmerge(I) obs: 0.073 |
Reflection | *PLUS Num. obs: 10660 / Num. measured all: 21228 |
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Processing
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Refinement | Resolution: 1.8→17 Å / σ(F): 2
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Displacement parameters | Biso mean: 2.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→17 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 2.93 Å2 |