+Open data
-Basic information
Entry | Database: PDB / ID: 1esp | ||||||
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Title | NEUTRAL PROTEASE MUTANT E144S | ||||||
Components | NEUTRAL PROTEASE MUTANT E144S | ||||||
Keywords | HYDROLASE (METALLOPROTEINASE) / INACTIVE MUTANT E144S | ||||||
Function / homology | Function and homology information bacillolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus cereus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Litster, S.A. / Wetmore, D.R. / Roche, R.S. / Codding, P.W. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1996 Title: E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution. Authors: Lister, S.A. / Wetmore, D.R. / Roche, R.S. / Codding, P.W. #1: Journal: Eur.J.Biochem. / Year: 1992 Title: The Structure of Neutral Protease from Bacillus Cereus at 0.2-Nm Resolution Authors: Stark, W. / Pauptit, R.A. / Wilson, K.S. / Jansonius, J.N. #2: Journal: J.Mol.Biol. / Year: 1988 Title: Crystal Structure of Neutral Protease from Bacillus Cereus Refined at 3.0 Angstroms Resolution and Comparison with the Homologous But More Thermostable Enzyme Thermolysin Authors: Pauptit, R.A. / Karlson, R. / Picot, D. / Jenkins, J.A. / Niklaus-Reimer, A. / Jansonius, J.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1esp.cif.gz | 74.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1esp.ent.gz | 55.6 KB | Display | PDB format |
PDBx/mmJSON format | 1esp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1esp_validation.pdf.gz | 409.4 KB | Display | wwPDB validaton report |
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Full document | 1esp_full_validation.pdf.gz | 411.2 KB | Display | |
Data in XML | 1esp_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1esp_validation.cif.gz | 19.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/es/1esp ftp://data.pdbj.org/pub/pdb/validation_reports/es/1esp | 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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Atom site foot note | 1: CIS PROLINE - PRO 52 |
-Components
#1: Protein | Mass: 33774.469 Da / Num. of mol.: 1 / Mutation: E144S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus cereus (bacteria) Description: GERMAN COLLECTION OF MICROORGANISMS (DSM) NUMBER DSM 3101 Gene: CNP (GENBANK ACCESSION #M83910 / Plasmid: PUB18 / Gene (production host): CNP (GENBANK ACCESSION #M83910) / Production host: Bacillus subtilis (bacteria) / References: UniProt: P05806 | ||||
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#2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-ZN / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.36 % | ||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 51 % | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Wavelength: 1.4 |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: May 20, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.4 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→55 Å / Num. obs: 8508 / % possible obs: 89 % / Observed criterion σ(I): 3 / Rmerge(I) obs: 0.077 |
Reflection | *PLUS Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 3 Å / % possible obs: 87.5 % |
-Processing
Software |
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Refinement | Resolution: 2.8→55 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.8→55 Å
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Refine LS restraints |
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