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Yorodumi- PDB-1ic6: STRUCTURE OF A SERINE PROTEASE PROTEINASE K FROM TRITIRACHIUM ALB... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ic6 | ||||||
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Title | STRUCTURE OF A SERINE PROTEASE PROTEINASE K FROM TRITIRACHIUM ALBUM LIMBER AT 0.98 A RESOLUTION | ||||||
Components | PROTEINASE K | ||||||
Keywords | HYDROLASE / proteinase K / serine proteases | ||||||
Function / homology | Function and homology information peptidase K / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Engyodontium album (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 0.98 Å | ||||||
Authors | Betzel, C. / Gourinath, S. / Kumar, P. / Kaur, P. / Perbandt, M. / Eschenburg, S. / Singh, T.P. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 A resolution. Authors: Betzel, C. / Gourinath, S. / Kumar, P. / Kaur, P. / Perbandt, M. / Eschenburg, S. / Singh, T.P. | ||||||
History |
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Remark 999 | SEQUENCE Amino acid 207 was mutated by persuing electron density at atomic resolution and after ...SEQUENCE Amino acid 207 was mutated by persuing electron density at atomic resolution and after repeation of many refinement cycle. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ic6.cif.gz | 111.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ic6.ent.gz | 92.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ic6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ic/1ic6 ftp://data.pdbj.org/pub/pdb/validation_reports/ic/1ic6 | HTTPS FTP |
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-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: 28958.791 Da / Num. of mol.: 1 / Mutation: S207D / Source method: isolated from a natural source / Source: (natural) Engyodontium album (fungus) / Strain: LIMBER / References: UniProt: P06873, peptidase K | ||||
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#2: Chemical | #3: Chemical | ChemComp-NO3 / #4: 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: 2.08 Å3/Da / Density % sol: 40.93 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion / pH: 6.5 Details: CaCl2 & NaNO3, pH 6.5, VAPOR DIFFUSION, temperature 295K |
Crystal grow | *PLUS Temperature: 22 ℃ / Method: unknown |
Components of the solutions | *PLUS Conc.: 30 mg/ml / Common name: protein |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, Hamburg / Beamline: X11 / Wavelength: 0.91 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 20, 1998 |
Radiation | Monochromator: Graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 0.98→10 Å / Num. all: 1229216 / Num. obs: 1229216 / % possible obs: 98 % / Observed criterion σ(F): 1229216 / Observed criterion σ(I): 136380 / Redundancy: 9.01 % / Biso Wilson estimate: 10.2 Å2 / Rmerge(I) obs: 0.035 / Rsym value: 0.035 / Net I/σ(I): 15 |
Reflection shell | Resolution: 0.98→1 Å / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 8 / % possible all: 95 |
Reflection shell | *PLUS % possible obs: 95 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 0.98→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 12.6 Å2 / Baniso 11: 12.3 Å2 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.98→10 Å
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LS refinement shell | Resolution: 0.98→10 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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