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Open data
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Basic information
Entry | Database: PDB / ID: 1fjo | ||||||
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Title | THERMOLYSIN (60% ACETONE SOAKED CRYSTALS) | ||||||
![]() | THERMOLYSIN | ||||||
![]() | HYDROLASE / METALLOPROTEINASE / ORGANIC SOLVENT | ||||||
Function / homology | ![]() thermolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | English, A.C. / Groom, C.R. / Hubbard, R.E. | ||||||
![]() | ![]() Title: Experimental and computational mapping of the binding surface of a crystalline protein. Authors: English, A.C. / Groom, C.R. / Hubbard, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79 KB | Display | ![]() |
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PDB format | ![]() | 59.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 391.5 KB | Display | ![]() |
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Full document | ![]() | 396.9 KB | Display | |
Data in XML | ![]() | 8.4 KB | Display | |
Data in CIF | ![]() | 12.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fj3C ![]() 1fjqC ![]() 1fjtC ![]() 1fjuC ![]() 1fjvC ![]() 1fjwC 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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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 34362.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 5 types, 145 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/ACN.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/ACN.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ZN / | ||||||
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#3: Chemical | ChemComp-CA / #4: Chemical | ChemComp-DMS / | #5: Chemical | ChemComp-ACN / #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.57 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 4.6MM THERMOLYSIN, 45% DMSO, 50MM TRIS-HCL, 2.5M CSCL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknownDetails: English, A.C., (1999) Proteins Struct.Funct.Genet., 37, 628. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Feb 12, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. all: 133453 / Num. obs: 22715 / % possible obs: 96 % / Observed criterion σ(I): 2 / Redundancy: 5.9 % / Biso Wilson estimate: 20 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 6.1 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 6 % / Rmerge(I) obs: 0.164 / Num. unique all: 3154 / % possible all: 94 |
Reflection shell | *PLUS % possible obs: 94 % / Mean I/σ(I) obs: 4.2 |
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Processing
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Refinement | Method to determine structure: isomorphous replacement / Resolution: 2→15 Å / Stereochemistry target values: Engh & Huber / Details: Used maximum likelihood procedure
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Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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