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Open data
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Basic information
Entry | Database: PDB / ID: 1a2q | ||||||
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Title | SUBTILISIN BPN' MUTANT 7186 | ||||||
![]() | SUBTILISIN BPN' | ||||||
![]() | HYDROLASE / SERINE PROTEASE / SPORULATION | ||||||
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 | ![]() | ||||||
![]() | Gilliland, G.L. / Whitlow, M. / Howard, A.J. | ||||||
![]() | ![]() Title: Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Authors: Pantoliano, M.W. / Whitlow, M. / Wood, J.F. / Dodd, S.W. / Hardman, K.D. / Rollence, M.L. / Bryan, P.N. #1: ![]() Title: Protein Engineering of Subtilisin Bpn': Enhanced Stabilization Through the Introduction of Two Cysteines to Form a Disulfide Bond Authors: Pantoliano, M.W. / Ladner, R.C. / Bryan, P.N. / Rollence, M.L. / Wood, J.F. / Poulos, T.L. #2: ![]() Title: Proteases of Enhanced Stability: Characterization of a Thermostable Variant of Subtilisin Authors: Bryan, P.N. / Rollence, M.L. / Pantoliano, M.W. / Wood, J. / Finzel, B.C. / Gilliland, G.L. / Howard, A.J. / Poulos, T.L. #3: ![]() Title: Atomic Coordinates for Subtilisin Bpn' (or Novo) Authors: Alden, R.A. / Birktoft, J.J. / Kraut, J. / Robertus, J.D. / Wright, C.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 | ![]() | 63.4 KB | Display | ![]() |
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PDB format | ![]() | 49.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.5 KB | Display | ![]() |
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Full document | ![]() | 384.6 KB | Display | |
Data in XML | ![]() | 7.3 KB | Display | |
Data in CIF | ![]() | 11.8 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: 27679.691 Da / Num. of mol.: 1 / Mutation: T22C, S87C, G169A, N218S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.25 % Description: THE DIFFRACTION DATA STATISTICS HAVE BEEN LOST. | ||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 6.5 Details: CRYSTAL WERE GROWN BY VAPOR DIFFUSION OF 10 MG/ML PROTEIN IN 50 MM MES PH 6.5, 25 MM CACL2 AGAINST 55% ACETONE., vapor diffusion | ||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Bryan, P.N., (1986) Proteins: Struct.,Funct., Genet., 1, 326. pH: 9 | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jan 31, 1987 / Details: COLLIMATOR |
Radiation | Monochromator: HUBER MONOCHROMATOR / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.75 Å / Num. obs: 14470 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE MAP / Resolution: 1.8→10 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.145 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |