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- PDB-2c7o: HhaI DNA methyltransferase complex with 13mer oligonucleotide con... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2c7o | ||||||
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Title | HhaI DNA methyltransferase complex with 13mer oligonucleotide containing 2-aminopurine adjacent to the target base (PCGC:GMGC) and SAH | ||||||
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![]() | TRANSFERASE/DNA / TRANSFERASE-DNA COMPLEX / BASE FLIPPING / TRANSFERASE RESTRICTION SYSTEM | ||||||
Function / homology | ![]() DNA (cytosine-5-)-methyltransferase / DNA (cytosine-5-)-methyltransferase activity / DNA restriction-modification system / methylation / DNA binding Similarity search - Function | ||||||
Biological species | ![]() SYNTHETIC CONSTRUCT (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Daujotyte, D. / Grazulis, S. | ||||||
![]() | ![]() Title: Time-Resolved Fluorescence of 2-Aminopurine as a Probe of Base Flipping in M.HhaI-DNA Complexes. Authors: Neely, R.K. / Daujotyte, D. / Grazulis, S. / Magennis, S.W. / Dryden, D.T.F. / Klimasauskas, S. / Jones, A.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 106.3 KB | Display | ![]() |
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PDB format | ![]() | 77.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
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Full document | ![]() | 441.9 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 12.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2c7pC ![]() 2c7qC ![]() 2c7rC ![]() 3mhtS S: Starting model for refinement C: citing same article ( |
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Similar 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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Components on special symmetry positions |
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Details | THE OLIGOMERIC STATE OF HHAI METHYLTRANSFERASE IS MONOMERIC, BUT SINCE IN THIS ENTRY, THE PROTEIN IS IN COMPLEX WITH DNA, THE QUATERNARY STRUCTURE FOR THIS ENTRY IS MARKED AS TRIMERIC. |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 37042.207 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P05102, DNA (cytosine-5-)-methyltransferase |
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-DNA chain , 2 types, 2 molecules CD
#2: DNA chain | Mass: 4021.636 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
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#3: DNA chain | Mass: 3911.562 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
-Non-polymers , 3 types, 346 molecules ![](data/chem/img/SAH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-SAH / | ||
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#5: Chemical | ChemComp-SO4 / #6: Water | ChemComp-HOH / | |
-Details
Compound details | RECOGNIZES THE DOUBLE-STRANDED SEQUENCE GCGC, CAUSES SPECIFIC METHYLATION AND PROTECTS THE DNA FROM ...RECOGNIZES |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 54.79 % |
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Crystal grow | pH: 5.6 Details: 50 MM NA CITRATE PH 5.6, 1.6 M AMMONIUM SULFATE, 5 % GLUCOSE. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 18, 2004 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.812 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→23.2 Å / Num. obs: 43361 / % possible obs: 99.6 % / Observed criterion σ(I): 3.9 / Redundancy: 21.6 % / Biso Wilson estimate: 10.9 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 20.8 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 3.9 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3MHT Resolution: 1.9→23.08 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 34200167.59 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: RESOLUTION-DEPENDENT WEIGHTING SCHEME USED. BULK SOLVENT MODEL USED
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 51.1244 Å2 / ksol: 0.385184 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→23.08 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.008 / Total num. of bins used: 6
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Xplor file |
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