+Open data
-Basic information
Entry | Database: PDB / ID: 1cy2 | ||||||
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Title | COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3' | ||||||
Components | DNA TOPOISOMERASE I | ||||||
Keywords | ISOMERASE / DNA TOPOISOMERASE / RELAXING ENZYME | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Feinberg, H. / Changela, A. / Mondragon, A. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cy2.cif.gz | 125.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cy2.ent.gz | 97 KB | Display | PDB format |
PDBx/mmJSON format | 1cy2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cy/1cy2 ftp://data.pdbj.org/pub/pdb/validation_reports/cy/1cy2 | HTTPS FTP |
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-Related structure data
Related structure data | 1cy0C 1cy1C 1cy4C 1cy6C 1cy7C 1cy8C 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: 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.) Escherichia coli (E. coli) / Strain: K12 / Plasmid: PGEX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: P06612, DNA topoisomerase | ||
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#2: Chemical | ChemComp-PO4 / | ||
#3: Chemical | #4: 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: 2.52 Å3/Da / Density % sol: 51.19 % | ||||||||||||||||||||
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Crystal grow | Temperature: 287 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 2.3M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / 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: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.9 |
Detector | Type: PRINCETON 2K / Detector: CCD / Date: Apr 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. all: 545417 / Num. obs: 31167 / % possible obs: 96.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 28.8 Å2 / Rmerge(I) obs: 0.085 |
Reflection shell | Resolution: 2.3→2.38 Å / Rmerge(I) obs: 0.174 / % possible all: 98.3 |
Reflection | *PLUS Num. measured all: 545417 |
Reflection shell | *PLUS % possible obs: 98.3 % |
-Processing
Software |
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Refinement | Resolution: 2.3→19.99 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 2100537.59 / 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: 33.93 Å2 / ksol: 0.428 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→19.99 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.02 / 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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