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- PDB-1law: STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY-FILLI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1law | ||||||
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Title | STABILIZATION OF ESCHERICHIA COLI RIBONUCLEASE HI BY CAVITY-FILLING MUTATIONS WITHIN A HYDROPHOBIC CORE | ||||||
![]() | RIBONUCLEASE H | ||||||
![]() | HYDROLASE | ||||||
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 | ![]() | ||||||
![]() | Ishikawa, K. / Nakamura, H. / Morikawa, K. / Kanaya, S. | ||||||
![]() | ![]() Title: Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. Authors: Ishikawa, K. / Nakamura, H. / Morikawa, K. / Kanaya, S. #1: ![]() Title: Structural Study of Mutants of Escherichia Coli Ribonuclease Hi with Enhanced Thermostability Authors: Ishikawa, K. / Kimura, S. / Kanaya, S. / Morikawa, K. / Nakamura, H. #2: ![]() Title: Structural Details of Ribonuclease H from Escherichia Coli as Refined at an Atomic Resolution Authors: Katayanagi, K. / Miyagawa, M. / Matsushima, M. / Ishikawa, M. / Kanaya, S. / Nakamura, H. / Ikehara, M. / Matsuzaki, T. / Morikawa, K. #3: ![]() Title: Three-Dimensional Structure of Ribonuclease H from E. Coli Authors: Katayanagi, K. / Miyagawa, M. / Matsushima, M. / Ishikawa, M. / Kanaya, S. / Ikehara, M. / Matsuzaki, T. / Morikawa, K. | ||||||
History |
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Remark 700 | SHEET THE STRANDS IN THE SHEET RECORD BELOW ARE DEFINED AS FOLLOWS IN THE PAPER (KATAYANAGI ET AL. ...SHEET THE STRANDS IN THE SHEET RECORD BELOW ARE DEFINED AS FOLLOWS IN THE PAPER (KATAYANAGI ET AL. NATURE (1990) VOL. 347, PP. 306-309). STRAND 1 (RIGHT ARROW) BETA C STRAND 2 (RIGHT ARROW) BETA B STRAND 3 (RIGHT ARROW) BETA A STRAND 4 (RIGHT ARROW) BETA D STRAND 5 (RIGHT ARROW) BETA E |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.7 KB | Display | ![]() |
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PDB format | ![]() | 31.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.2 KB | Display | ![]() |
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Full document | ![]() | 366.7 KB | Display | |
Data in XML | ![]() | 5.3 KB | Display | |
Data in CIF | ![]() | 7.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: CIS PROLINE - PRO 17 |
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Components
#1: Protein | Mass: 17637.025 Da / Num. of mol.: 1 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: 1.93 Å3/Da / Density % sol: 36.19 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 9 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→6 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 6 Å / Num. reflection obs: 9916 / σ(F): 1 / Rfactor obs: 0.188 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |