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Open data
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Basic information
Entry | Database: PDB / ID: 2g4v | ||||||
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Title | anomalous substructure of proteinase K | ||||||
![]() | Proteinase K | ||||||
![]() | HYDROLASE / anomalous substructure of proteinase K | ||||||
Function / homology | ![]() peptidase K / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mueller-Dieckmann, C. / Weiss, M.S. | ||||||
![]() | ![]() Title: On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths. Authors: Mueller-Dieckmann, C. / Panjikar, S. / Schmidt, A. / Mueller, S. / Kuper, J. / Geerlof, A. / Wilmanns, M. / Singh, R.K. / Tucker, P.A. / Weiss, M.S. | ||||||
History |
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Remark 999 | SEQUENCE AUTHOR STATES THAT AMINO ACID 207 WAS MUTATED BY PERSUING ELECTRON DENSITY AT ATOMIC ...SEQUENCE AUTHOR STATES THAT AMINO ACID 207 WAS MUTATED BY PERSUING ELECTRON DENSITY AT ATOMIC RESOLUTION AND AFTER REPEATION OF MANY REFINEMENT CYCLE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 62 KB | Display | ![]() |
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PDB format | ![]() | 49.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 410.6 KB | Display | ![]() |
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Full document | ![]() | 413.6 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 18.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2g4hC ![]() 2g4iC ![]() 2g4jC ![]() 2g4kC ![]() 2g4lC ![]() 2g4mC ![]() 2g4nC ![]() 2g4oC ![]() 2g4pC ![]() 2g4qC ![]() 2g4rC ![]() 2g4sC ![]() 2g4tC ![]() 2g4uC ![]() 2g4wC ![]() 2g4xC ![]() 2g4yC ![]() 2g4zC ![]() 2g51C ![]() 2g52C ![]() 2g55C ![]() 2illC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 28958.791 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||
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#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.1 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jan 1, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 2 Å / Relative weight: 1 |
Reflection | Resolution: 2.14→30 Å / Num. obs: 13684 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 6.808 Å2
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Refinement step | Cycle: LAST / Resolution: 2.14→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.14→2.195 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 16.1659 Å / Origin y: 12.972 Å / Origin z: 25.2282 Å
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