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- PDB-1cy0: COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-5'-ADENOSINE DIPHOSPHATE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cy0 | ||||||
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Title | COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-5'-ADENOSINE DIPHOSPHATE | ||||||
![]() | DNA TOPOISOMERASE I | ||||||
![]() | ISOMERASE / DNA TOPOISOMERASE / RELAXING ENZYME | ||||||
Function / homology | ![]() DNA topoisomerase activity / DNA topoisomerase / DNA topoisomerase type I (single strand cut, ATP-independent) activity / DNA topological change / chromosome / DNA binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Feinberg, H. / Changela, A. / Mondragon, A. | ||||||
![]() | ![]() Title: Protein-nucleotide interactions in E. coli DNA topoisomerase I. Authors: Feinberg, H. / Changela, A. / Mondragon, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.2 KB | Display | ![]() |
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PDB format | ![]() | 92.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 457.3 KB | Display | ![]() |
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Full document | ![]() | 467.3 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 19.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cy1C ![]() 1cy2C ![]() 1cy4C ![]() 1cy6C ![]() 1cy7C ![]() 1cy8C 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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Unit cell |
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Components
#1: Protein | Mass: 67542.500 Da / Num. of mol.: 1 Fragment: 67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-A3P / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.5 % | ||||||||||||||||||||
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Crystal grow | Temperature: 287 K / Method: microdialysis / pH: 5 Details: 2.14M ammonium sulfate, pH 5.0, MICRODIALYSIS, temperature 287K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: and 14 degrees centigrade | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→999 Å / Num. all: 246384 / Num. obs: 24161 / % possible obs: 96.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 37 Å2 / Rmerge(I) obs: 0.069 |
Reflection shell | Resolution: 2.45→2.52 Å / Rmerge(I) obs: 0.238 / % possible all: 66.8 |
Reflection | *PLUS Num. measured all: 246384 |
Reflection shell | *PLUS % possible obs: 66.8 % |
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Processing
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Refinement | Resolution: 2.45→19.98 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 15292774.3 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 Stereochemistry target values: R. A. Engh and R. Huber, Acta Cryst. Sect. A., 1991 Details: Refinement done with REFMAC. The solvent correction was calculated with XPLOR and applied in REFMAC. Final parameters obtained with CNS 0.9
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 30.38 Å2 / ksol: 0.373 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.45→19.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.45→2.6 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: 'X-PLOR,REFMAC,CNS 0.9' / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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