+Open data
-Basic information
Entry | Database: PDB / ID: 1aqn | ||||||
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Title | SUBTILISIN MUTANT 8324 | ||||||
Components | SUBTILISIN 8324 | ||||||
Keywords | SERINE PROTEASE / HYDROLASE / SERINE PROTEINASE | ||||||
Function / homology | Function and homology information 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 | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE MAP / Resolution: 1.8 Å | ||||||
Authors | Whitlow, M. / Howard, A.J. / Wood, J.F. | ||||||
Citation | Journal: To be published Title: Large increases in general stabilityfor subtilisin BPN' through incremental changes in the free energy of unfolding Authors: Muralikrishna, P. / Wickstrom, E. #1: Journal: Biochemistry / Year: 1988 Title: The Engineering of Binding Affinity at Metal Ion Binding Sites for the Stabilization of Proteins: Subtilisin as a Test Case Authors: Pantoliano, M.W. / Whitlow, M. / Wood, J.F. / Rollence, M.L. / Finzel, B.C. / Gilliland, G.L. / Poulos, T.L. / Bryan, P.N. #2: Journal: Biochemistry / Year: 1987 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. #3: Journal: Proteins / Year: 1986 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. #4: Journal: Biochem.Biophys.Res.Commun. / Year: 1971 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1aqn.cif.gz | 64.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1aqn.ent.gz | 49.5 KB | Display | PDB format |
PDBx/mmJSON format | 1aqn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1aqn_validation.pdf.gz | 383.3 KB | Display | wwPDB validaton report |
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Full document | 1aqn_full_validation.pdf.gz | 383.4 KB | Display | |
Data in XML | 1aqn_validation.xml.gz | 7 KB | Display | |
Data in CIF | 1aqn_validation.cif.gz | 11.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aq/1aqn ftp://data.pdbj.org/pub/pdb/validation_reports/aq/1aqn | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 27514.631 Da / Num. of mol.: 1 / Mutation: T22C, M50F, S87C, G169A, Q206C, Y217K, N218S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Strain: GX8324 / Cellular location: SECRETED / Plasmid: PGX8324 / Production host: Bacillus subtilis (bacteria) / Strain (production host): GX8324 / References: UniProt: P00782, subtilisin | ||||||
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#2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.61 % |
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Crystal grow | Method: vapor diffusion / pH: 8.7 Details: CRYSTAL WERE GROWN BY VAPOR DIFFUSION OF 10 MG/ML PROTEIN IN 100 MM TRIS-HCL PH 8.7, 40 MM CACL2 AGAINST 20% 2-PROPANOL., vapor diffusion |
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Bryan, P.N., (1986) Proteins: Struct.,Funct., Genet., 1, 326. |
Components of the solutions | *PLUS Conc.: 55 % / Common name: acetone |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: May 20, 1987 / Details: HUBER MONOCHROMATOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.73→99 Å / Num. obs: 18552 / % possible obs: 79.8 % / Observed criterion σ(I): 2 / Redundancy: 2.7 % / Rsym value: 0.0634 / Net I/σ(I): 17.3 |
Reflection shell | Resolution: 1.73→1.84 Å / Redundancy: 2.33 % / Mean I/σ(I) obs: 2.9 / Rsym value: 0.3174 / % possible all: 41.4 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE MAP / Resolution: 1.8→10 Å / Num. reflection all: 16735 / Num. reflection obs: 16735 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 0.139 / Rfactor Rwork: 0.139 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |