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Yorodumi- PDB-4rtm: Complex of Escherichia coli DNA Adenine Methyltransferase (DAM) w... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4rtm | ||||||
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Title | Complex of Escherichia coli DNA Adenine Methyltransferase (DAM) with AdoMet and with DNA Containing Distal Pap Regulon Sequence | ||||||
Components |
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Keywords | Transferase/DNA / DAM METHYLATION / GATC RECOGNITION / BASE FLIPPING / BACTERIAL VIRULENCE / methylation-independent transcriptional repressor / Transferase-DNA complex | ||||||
Function / homology | Function and homology information bacterial-type DNA replication initiation / site-specific DNA-methyltransferase (adenine-specific) / site-specific DNA-methyltransferase (adenine-specific) activity / S-adenosyl-L-methionine binding / DNA restriction-modification system / mismatch repair / response to UV / DNA-templated DNA replication / sequence-specific DNA binding / methylation Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Horton, J.R. / Cheng, X. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2015 Title: Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression. Authors: Horton, J.R. / Zhang, X. / Blumenthal, R.M. / Cheng, X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rtm.cif.gz | 81.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rtm.ent.gz | 56.4 KB | Display | PDB format |
PDBx/mmJSON format | 4rtm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4rtm_validation.pdf.gz | 925 KB | Display | wwPDB validaton report |
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Full document | 4rtm_full_validation.pdf.gz | 916.1 KB | Display | |
Data in XML | 4rtm_validation.xml.gz | 12.5 KB | Display | |
Data in CIF | 4rtm_validation.cif.gz | 16.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rt/4rtm ftp://data.pdbj.org/pub/pdb/validation_reports/rt/4rtm | HTTPS FTP |
-Related structure data
Related structure data | 4rtjC 4rtkC 4rtlC 4rtnC 4rtoC 4rtpC 4rtqC 4rtrC 4rtsC 2g1pS 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: Protein | Mass: 34330.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 substr. MDS42 / Gene: dam, ECMDS42_2833 / Production host: Escherichia coli (E. coli) / Strain (production host): HMS174(DE3) / References: UniProt: H0Q7C9, UniProt: P0AEE8*PLUS |
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#2: DNA chain | Mass: 3357.223 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#3: DNA chain | Mass: 3348.209 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#4: Chemical | ChemComp-SAM / |
#5: Water | ChemComp-HOH / |
Sequence details | AUTHOR STATES THAT RESIDUES 175 WERE MODELED AS SER INSTEAD OF ALA BECAUSE OF EXTRA DENSITY. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.55 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 21% PEG200, 100mM KCl, 10mM MgSO4, 100mM MES buffer, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Dec 15, 2006 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→32.431 Å / Num. all: 12050 / Num. obs: 12050 / % possible obs: 100 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 12 % / Biso Wilson estimate: 41.8 Å2 / Rmerge(I) obs: 0.113 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 2.5→2.58 Å / Redundancy: 12.9 % / Rmerge(I) obs: 0.439 / Mean I/σ(I) obs: 8.3 / Num. unique all: 1194 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2G1P Resolution: 2.5→32.431 Å / SU ML: 0.29 / σ(F): 1.35 / Phase error: 23.33 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→32.431 Å
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Refine LS restraints |
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LS refinement shell |
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