+Open data
-Basic information
Entry | Database: PDB / ID: 1gns | ||||||
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Title | SUBTILISIN BPN' | ||||||
Components | SUBTILISIN BPN' | ||||||
Keywords | 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 region / metal ion binding Similarity search - Function | ||||||
Biological species | BACILLUS AMYLOLIQUEFACIENS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Almog, O. / Gallagher, D.T. / Ladner, J.E. / Strausberg, S. / Alexander, P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Structural Basis of Thermostability. Analysis of Stabilizing Mutations in Subtilisin Bpn'. Authors: Almog, O. / Gallagher, D.T. / Ladner, J.E. / Strausberg, S. / Alexander, P. / Bryan, P. / Gilliland, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gns.cif.gz | 65.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gns.ent.gz | 45.9 KB | Display | PDB format |
PDBx/mmJSON format | 1gns.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gn/1gns ftp://data.pdbj.org/pub/pdb/validation_reports/gn/1gns | HTTPS FTP |
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-Related structure data
Related structure data | 1gnvC 1sucS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26400.324 Da / Num. of mol.: 1 / Fragment: RESIDUES 111-181,191-382 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS AMYLOLIQUEFACIENS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P00782, subtilisin |
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#2: Chemical | ChemComp-ACN / |
#3: Water | ChemComp-HOH / |
Compound details | DELETION, RESIDUES 176-185. OTHER MUTATIONS: D142A, M151F, A174L, Q307W, Y318K, N319S, S322C, Q372E |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.44 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: 55% ACETONE, 0.05M GLYCINE PH 9.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 9 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jul 15, 1994 |
Radiation | Monochromator: NI/FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→8 Å / Num. obs: 15590 / % possible obs: 77 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.055 |
Reflection | *PLUS Num. all: 20181 / Num. measured all: 64819 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1SUC Resolution: 1.8→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Refinement | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_bond_d / Dev ideal: 0.02 |