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Open data
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Basic information
Entry | Database: PDB / ID: 1g02 | ||||||
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Title | Ribonuclease T1 V16S mutant | ||||||
![]() | GUANYL-SPECIFIC RIBONUCLEASE T1 | ||||||
![]() | ![]() ![]() | ||||||
Function / homology | ![]() hyphal tip / ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | De Vos, S. / Loris, R. / Steyaert, J. | ||||||
![]() | ![]() Title: Hydrophobic core manipulations in ribonuclease T1. Authors: De Vos, S. / Backmann, J. / Prevost, M. / 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 | ![]() | 30.1 KB | Display | ![]() |
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PDB format | ![]() | 22.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1fysC ![]() 1fzuC ![]() 1i2eC ![]() 1i2fC ![]() 1i2gC ![]() 1i3fC ![]() 1i3iC 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
#1: Protein | Mass: 11082.642 Da / Num. of mol.: 1 / Mutation: V16S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-2GP / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.68 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: MPD, calcium chloride, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 46 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 4.2 / Details: Zegers, I., (1998) Nat.Struct.Biol., 5, 280. | ||||||||||||||||||||||||||||||||||||
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: IMAGE PLATE / Date: Jan 27, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.86→20 Å / Num. all: 7945 / Num. obs: 7945 / % possible obs: 94.9 % / Observed criterion σ(F): -6 / Observed criterion σ(I): -3 / Redundancy: 9.3 % / Biso Wilson estimate: 13.8 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 1.86→1.94 Å / Redundancy: 9.8 % / Rmerge(I) obs: 0.603 / Num. unique all: 749 / % possible all: 90.8 |
Reflection | *PLUS Num. obs: 7969 / Num. measured all: 73803 |
Reflection shell | *PLUS % possible obs: 90.8 % |
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Processing
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Refinement | Resolution: 1.86→1.94 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.86→1.94 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.87 Å / Rfactor Rfree![]() ![]() | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |