+Open data
-Basic information
Entry | Database: PDB / ID: 1g60 | ||||||
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Title | Crystal Structure of Methyltransferase MboIIa (Moraxella bovis) | ||||||
Components | Adenine-specific Methyltransferase MboIIA | ||||||
Keywords | TRANSFERASE / STRUCTURAL GENOMICS / MORAXELLA BOVIS / DNA METHYLATION / S-ADENOSYLMETHIONINE / PSI / Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG | ||||||
Function / homology | Function and homology information N-methyltransferase activity / site-specific DNA-methyltransferase (adenine-specific) / site-specific DNA-methyltransferase (adenine-specific) activity / DNA restriction-modification system / DNA binding Similarity search - Function | ||||||
Biological species | Moraxella bovis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.74 Å | ||||||
Authors | Osipiuk, J. / Walsh, M.A. / Joachimiak, A. / Midwest Center for Structural Genomics (MCSG) | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2003 Title: Crystal structure of MboIIA methyltransferase. Authors: Osipiuk, J. / Walsh, M.A. / Joachimiak, A. #1: Journal: Nucleic Acids Res. / Year: 1991 Title: Cloning and Characterization of the MboII Restriction-modification System Authors: Bocklage, H. / Heeger, K. / Muller-Hill, B. | ||||||
History |
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Remark 999 | SEQUENCE DNA SEQUENCING OF THE CLONES SHOWED THERE IS A ALANINE CODON FOR RESIDUE 51 AND A ARGININE ...SEQUENCE DNA SEQUENCING OF THE CLONES SHOWED THERE IS A ALANINE CODON FOR RESIDUE 51 AND A ARGININE CODON FOR RESIDUE 111. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g60.cif.gz | 118.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g60.ent.gz | 91.2 KB | Display | PDB format |
PDBx/mmJSON format | 1g60.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g6/1g60 ftp://data.pdbj.org/pub/pdb/validation_reports/g6/1g60 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30192.391 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Moraxella bovis (bacteria) / Plasmid: PET24A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PLYSS References: UniProt: P23192, site-specific DNA-methyltransferase (adenine-specific) #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.29 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.4 Details: 4% PEG monomethyl ether 5000, 50 mM potassium chloride, 50 mM sodium chloride, 1 mM DTT, 50 mM bicine, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1.00599 Å |
Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Aug 29, 1999 |
Radiation | Monochromator: SI 111 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00599 Å / Relative weight: 1 |
Reflection | Resolution: 1.74→28.79 Å / Num. obs: 60668 / % possible obs: 99.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 3.72 % / Biso Wilson estimate: 22 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 1.74→1.77 Å / Redundancy: 3.63 % / Rmerge(I) obs: 0.339 / Mean I/σ(I) obs: 3.4 / Num. unique all: 2974 / % possible all: 99.4 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. obs: 60068 |
Reflection shell | *PLUS % possible obs: 99.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.74→29.75 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 27.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.74→29.75 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.74→1.826 Å
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Refinement | *PLUS Lowest resolution: 30 Å / Rfactor obs: 0.198 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |