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Open data
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Basic information
Entry | Database: PDB / ID: 1jl1 | ||||||
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Title | D10A E. coli ribonuclease HI | ||||||
![]() | RIBONUCLEASE HI | ||||||
![]() | HYDROLASE / RNase HI / Protein stability / thermostability / hydrogen exchange / cooperativity | ||||||
Function / homology | ![]() DNA replication, removal of RNA primer / ribonuclease H / RNA-DNA hybrid ribonuclease activity / endonuclease activity / nucleic acid binding / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Goedken, E.R. / Marqusee, S. | ||||||
![]() | ![]() Title: Native-state energetics of a thermostabilized variant of ribonuclease HI. Authors: Goedken, E.R. / Marqusee, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 47.3 KB | Display | ![]() |
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PDB format | ![]() | 32.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.4 KB | Display | ![]() |
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Full document | ![]() | 368.1 KB | Display | |
Data in XML | ![]() | 4.6 KB | Display | |
Data in CIF | ![]() | 7.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1f21S 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: 17482.795 Da / Num. of mol.: 1 / Mutation: Asp10Ala, Cys13Ala, Cys63Ala, Cys133Ala 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: 1.85 Å3/Da / Density % sol: 33.34 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG-3350, Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||
Crystal grow | *PLUS Details: used microseeding | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 28, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→20 Å / Num. all: 28223 / Num. obs: 28054 / % possible obs: 99.4 % / Rmerge(I) obs: 0.088 |
Reflection shell | Resolution: 1.3→1.36 Å / % possible all: 97.2 |
Reflection | *PLUS Lowest resolution: 20 Å |
Reflection shell | *PLUS % possible obs: 97.2 % / Rmerge(I) obs: 0.188 / Mean I/σ(I) obs: 3.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1F21 Resolution: 1.3→20 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 1.3→20 Å
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LS refinement shell | Resolution: 1.3→1.36 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.3 Å / Lowest resolution: 20 Å / % reflection Rfree: 10 % / Rfactor obs: 0.223 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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