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Yorodumi- PDB-1bsu: STRUCTURAL AND ENERGETIC ORIGINS OF INDIRECT READOUT IN SITE-SPEC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bsu | ||||||
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Title | STRUCTURAL AND ENERGETIC ORIGINS OF INDIRECT READOUT IN SITE-SPECIFIC DNA CLEAVAGE BY A RESTRICTION ENDONUCLEASE | ||||||
Components |
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Keywords | HYDROLASE/DNA / COMPLEX ENDONUCLEASE ECORV (3.1.21.4)-DNA / HYDROLASE-DNA COMPLEX | ||||||
Function / homology | Function and homology information type II site-specific deoxyribonuclease / type II site-specific deoxyribonuclease activity / DNA restriction-modification system / DNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 2 Å | ||||||
Authors | Perona, J.J. / Martin, A.M. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1999 Title: Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease. Authors: Martin, A.M. / Sam, M.D. / Reich, N.O. / Perona, J.J. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Metal Ion Mediated Substrate-Assisted Catalysis in Type II Restriction Endonucleases Authors: Horton, N.C. / Perona, J.J. #2: Journal: J.Mol.Biol. / Year: 1997 Title: Conformational Transitions and Structural Deformability of EcoRV Endonuclease Revealed by Crystallographic Analysis Authors: Perona, J.J. / Martin, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bsu.cif.gz | 117.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bsu.ent.gz | 90.2 KB | Display | PDB format |
PDBx/mmJSON format | 1bsu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/1bsu ftp://data.pdbj.org/pub/pdb/validation_reports/bs/1bsu | HTTPS FTP |
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-Related structure data
Related structure data | 1buaC 1az0S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: DNA chain | Mass: 3043.030 Da / Num. of mol.: 1 / Source method: obtained synthetically | ||||
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#2: DNA chain | Mass: 3356.236 Da / Num. of mol.: 1 / Source method: obtained synthetically | ||||
#3: Protein | Mass: 28559.158 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: P04390, type II site-specific deoxyribonuclease #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.7 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 7.5 / Details: pH 7.5, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||||||
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: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Aug 15, 1995 / Details: MIRRORS |
Radiation | Monochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 28884 / % possible obs: 73 % / Observed criterion σ(I): 1 / Redundancy: 2 % / Rmerge(I) obs: 0.092 |
Reflection | *PLUS Num. measured all: 56330 |
Reflection shell | *PLUS % possible obs: 53.3 % |
-Processing
Software |
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Refinement | Method to determine structure: OTHER Starting model: PDB 1AZ0 Resolution: 2→6 Å / Cross valid method: THROUGHOUT / σ(F): 1 Details: THE AMIMO ACID SIDE CHAINS LISTED IN REMARK 470 APPEAR TO BE PARTIALLY OR COMPLETELY DISORDERED.
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Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 23.2 Å2 |