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Open data
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Basic information
Entry | Database: PDB / ID: 2bu4 | ||||||
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Title | RIBONUCLEASE T1 COMPLEX WITH 2'GMP | ||||||
![]() | PROTEIN (RIBONUCLEASE T1) | ||||||
![]() | HYDROLASE / ENDORIBONUCLEASE | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Loris, R. / Devos, S. / Langhorst, U. / Decanniere, K. / Bouckaert, J. / Maes, D. / Transue, T.R. / Steyaert, J. | ||||||
![]() | ![]() Title: Conserved water molecules in a large family of microbial ribonucleases. Authors: Loris, R. / Langhorst, U. / De Vos, S. / Decanniere, K. / Bouckaert, J. / Maes, D. / Transue, T.R. / Steyaert, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.7 KB | Display | ![]() |
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PDB format | ![]() | 22.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1bu4C ![]() 3bu4C ![]() 4bu4C ![]() 5bu4C ![]() 1rn1S S: Starting model for refinement 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
#1: Protein | Mass: 11094.694 Da / Num. of mol.: 1 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: 2.26 Å3/Da / Density % sol: 46 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.2 / Details: 20 MM NA-ACETATE PH 4.2 2 MM CACL2 55 % MPD | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Zegers, I., (1998) Nat. Struct. Biol., 5, 280. | ||||||||||||||||||||||||||||||||||||
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: Feb 15, 1998 |
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: 1.95→18 Å / Num. obs: 7393 / % possible obs: 97.3 % / Redundancy: 5.15 % / Rsym value: 0.17 / Net I/σ(I): 10.71 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 5.5 % / Mean I/σ(I) obs: 3 / Rsym value: 0.517 / % possible all: 94.2 |
Reflection | *PLUS Redundancy: 5.1 % / Num. measured all: 38058 / Rmerge(I) obs: 0.17 |
Reflection shell | *PLUS Rmerge(I) obs: 0.517 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1RN1 Resolution: 1.95→18 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.95→18 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→1.99 Å / Total num. of bins used: 8
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 18 Å / σ(F): 0 / % reflection Rfree: 8.5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.291 / % reflection Rfree: 8.5 % |