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Open data
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Basic information
Entry | Database: PDB / ID: 1box | ||||||
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Title | N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS | ||||||
![]() | GUANYL-SPECIFIC RIBONUCLEASE SA | ||||||
![]() | HYDROLASE / RIBONUCLEASE / MUTANT | ||||||
Function / homology | ![]() ribonuclease T1 activity / ribonuclease T1 / RNA endonuclease activity / lyase activity / RNA binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hebert, E.J. / Giletto, A. / Sevcik, J. / Urbanikova, L. / Wilson, K.S. / Dauter, Z. / Pace, C.N. | ||||||
![]() | ![]() Title: Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1. Authors: Hebert, E.J. / Giletto, A. / Sevcik, J. / Urbanikova, L. / Wilson, K.S. / Dauter, Z. / Pace, C.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 32.2 KB | Display | ![]() |
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PDB format | ![]() | 21.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.4 KB | Display | ![]() |
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Full document | ![]() | 366.3 KB | Display | |
Data in XML | ![]() | 3.8 KB | Display | |
Data in CIF | ![]() | 5.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1rggS S: Starting model for refinement |
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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: 10555.467 Da / Num. of mol.: 1 / Mutation: N39S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48 % | |||||||||||||||||||||||||
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Crystal grow | pH: 8 Details: HANGING DROP VAPOUR EQUILIBRATION DROP: 10 MG/ML OF PROTEIN 0.1 M TRIS-HCL BUFFER AT PH 8.0 12,5 % PEG 6000 RESERVOIR: 25 % PEG 6000 | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
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: Jul 15, 1997 / Details: MSC "LONG" MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→14.9 Å / Num. obs: 12724 / % possible obs: 92.1 % / Redundancy: 4.8 % / Biso Wilson estimate: 25 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 30.1 |
Reflection shell | Resolution: 1.6→1.63 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.471 / Mean I/σ(I) obs: 1.9 / % possible all: 57.1 |
Reflection shell | *PLUS % possible obs: 57.1 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1RGG Resolution: 1.6→14.9 Å / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.084
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Displacement parameters | Biso mean: 26.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→14.9 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 11829 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |