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Open data
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Basic information
Entry | Database: PDB / ID: 1hz1 | ||||||
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Title | RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+ | ||||||
![]() | RIBONUCLEASE T1 | ||||||
![]() | HYDROLASE / ribonuclease / metal binding / stability | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | De Swarte, J. / De Vos, S. / Langhorst, U. / Steyaert, J. / Loris, R. | ||||||
![]() | ![]() Title: The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution. Authors: Deswarte, J. / De Vos, S. / Langhorst, U. / Steyaert, J. / Loris, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 30 KB | Display | ![]() |
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PDB format | ![]() | 22.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 814.2 KB | Display | ![]() |
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Full document | ![]() | 814.8 KB | Display | |
Data in XML | ![]() | 7.6 KB | Display | |
Data in CIF | ![]() | 9.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
#1: Protein | Mass: 11066.642 Da / Num. of mol.: 1 / Mutation: V16A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-2GP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.17 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.2 Details: MPD, acetate, calcium chloride, magnesiusm chrloride (soak), pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 16, 2000 / Details: graphite monochromator |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Num. all: 9363 / Num. obs: 9363 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 8.66 % / Biso Wilson estimate: 22.3 Å2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 16.81 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 6.86 % / Rmerge(I) obs: 0.429 / Mean I/σ(I) obs: 3.78 / % possible all: 100 |
Reflection | *PLUS Num. measured all: 81069 |
Reflection shell | *PLUS % possible obs: 100 % / Num. unique obs: 926 / Num. measured obs: 6464 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(F): 0 / Rfactor obs: 0.1964 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |