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Open data
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Basic information
Entry | Database: PDB / ID: 1fev | ||||||
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Title | CRYSTAL STRUCTURE OF THE ALA4AIB MUTATION IN RNASE S | ||||||
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![]() | HYDROLASE / alpha aminoisobutyric acid / AIB | ||||||
Function / homology | ![]() pancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / lyase activity / defense response to Gram-positive bacterium / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ratnaparkhi, G.S. / Varadarajan, R. | ||||||
![]() | ![]() Title: Structural and thermodynamic consequences of introducing alpha-aminoisobutyric acid in the S peptide of ribonuclease S. Authors: Ratnaparkhi, G.S. / Awasthi, S.K. / Rani, P. / Balaram, P. / Varadarajan, R. #1: ![]() Title: Thermodynamic and Structural Studies of Cavity Formation in Proteins Suggest that Loss of Packing Interactions Rather than the Hydrophobic Effect Dominates the Observed Energetics Authors: Ratnaparkhi, G.S. / Varadarajan, R. #2: ![]() Title: X-ray Crystallographic Studies of the Denaturation of Ribonuclease S Authors: Ratnaparkhi, G.S. / Varadarajan, 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 | ![]() | 33.1 KB | Display | ![]() |
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PDB format | ![]() | 24.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.9 KB | Display | ![]() |
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Full document | ![]() | 436.4 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Data in CIF | ![]() | 9.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein/peptide | Mass: 1748.933 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: S peptide is a 16 residue synthetic peptide with Ala4Aib replacement References: UniProt: P61823 |
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#2: Protein | Mass: 11294.749 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Chemical | ChemComp-SO4 / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.78 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.75 Details: 3M CsCl, 35% Ammonium Sulphate, 50 mM Sodium Acetate, pH=5.75 , VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
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: Aug 26, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→25 Å / Num. obs: 52509 / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 8.26 % / Biso Wilson estimate: 24.2 Å2 / Rmerge(I) obs: 0.095 / Net I/σ(I): 23.3 |
Reflection shell | Resolution: 2.15→2.25 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.38 / Num. unique all: 739 / % possible all: 83.9 |
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Processing
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Refinement | Resolution: 2.25→10 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters | Biso mean: 17.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.25→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.37 Å / Rfactor Rfree error: 0.043 / Total num. of bins used: 7
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Xplor file |
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Software | *PLUS Name: X-PLOR(ONLINE) / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 1 / % reflection Rfree: 10.2 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.326 / % reflection Rfree: 10.4 % / Rfactor Rwork: 0.305 |