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- PDB-5uud: Tetragonal thermolysin cryocooled to 100 K with 50% dmf as cryopr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5uud | ||||||
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Title | Tetragonal thermolysin cryocooled to 100 K with 50% dmf as cryoprotectant | ||||||
![]() | Thermolysin | ||||||
![]() | HYDROLASE / zinc protease / alpha/beta | ||||||
Function / homology | ![]() thermolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Juers, D.H. | ||||||
![]() | ![]() Title: The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order. Authors: Juers, D.H. / Farley, C.A. / Saxby, C.P. / Cotter, R.A. / Cahn, J.K.B. / Holton-Burke, R.C. / Harrison, K. / Wu, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 176.6 KB | Display | ![]() |
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PDB format | ![]() | 115.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.3 KB | Display | ![]() |
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Full document | ![]() | 441.2 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 28.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5un3C ![]() 5uu7C ![]() 5uu8C ![]() 5uu9C ![]() 5uuaC ![]() 5uubC ![]() 5uucC ![]() 5uueC ![]() 6avlC ![]() 6b6nC ![]() 6b6oC ![]() 6b6pC ![]() 6b6qC ![]() 6b6rC ![]() 6b6sC ![]() 6b6tC ![]() 6d5nC ![]() 6d5oC ![]() 6d5pC ![]() 6d5qC ![]() 6d5rC ![]() 6d5sC ![]() 6d5tC ![]() 6d5uC ![]() 6d6eC ![]() 6d6fC ![]() 6d6gC ![]() 6d6hC ![]() 6dzfC 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: 34360.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: npr / Production host: ![]() ![]() |
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-Non-polymers , 5 types, 429 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/DMF.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/DMF.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-DMF / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.57 Å3/Da / Density % sol: 65.55 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop Details: Well: ~2 M AmSO4 Drop: 50 mg/mL protein in 45% DMSO, 0.5 M ZnCl2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SEALED TUBE / Type: OXFORD DIFFRACTION ENHANCE ULTRA / Wavelength: 1.54 Å |
Detector | Type: OXFORD ONYX CCD / Detector: CCD / Date: Aug 27, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20.88 Å / Num. obs: 125444 / % possible obs: 100 % / Redundancy: 9.6 % / Biso Wilson estimate: 18.7237838701 Å2 / CC1/2: 0.999 / Net I/σ(I): 20.1 |
Reflection shell | Highest resolution: 1.6 Å / Redundancy: 6.1 % / CC1/2: 0.606 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.4484097384 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.60000346607→19.8870760838 Å
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Refine LS restraints |
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LS refinement shell |
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