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- PDB-1npc: THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1npc | ||||||
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Title | THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION | ||||||
![]() | NEUTRAL PROTEASE | ||||||
![]() | HYDROLASE(METALLOPROTEINASE) | ||||||
Function / homology | ![]() bacillolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stark, W. / Pauptit, R.A. / Jansonius, J.N. | ||||||
![]() | ![]() 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. #1: ![]() 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. / Karlsson, R. / Picot, D. / Jenkins, J.A. / Niklaus-Reimer, A. / Jansonius, J.N. #2: ![]() Title: The Primary Structure of Bacillus Cereus Neutral Proteinase and Comparison with Thermolysin and Bacillus Subtilis Proteinase Authors: Sidler, W. / Niederer, E. / Suter, F. / Zuber, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.8 KB | Display | ![]() |
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PDB format | ![]() | 59.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 413 KB | Display | ![]() |
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Full document | ![]() | 419.6 KB | Display | |
Data in XML | ![]() | 16.8 KB | Display | |
Data in CIF | ![]() | 25.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUE 52 IS A CIS PROLINE. | |||||||||||||||
Components on special symmetry positions |
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Components
#1: Protein | Mass: 33816.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||||
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#2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-ZN / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.99 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 0 K / pH: 6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Num. obs: 21168 / % possible obs: 88 % / Num. measured all: 195223 / Rmerge(I) obs: 0.219 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. reflection obs: 21168 / Rfactor obs: 0.175 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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