+Open data
-Basic information
Entry | Database: PDB / ID: 1t0f | ||||||
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Title | Crystal Structure of the TnsA/TnsC(504-555) complex | ||||||
Components | (Transposon Tn7 transposition protein ...) x 2 | ||||||
Keywords | DNA BINDING PROTEIN / protein-protein complex / mixed alpha-beta | ||||||
Function / homology | Function and homology information transposition / transposase activity / DNA transposition / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / chromosome / endonuclease activity / DNA recombination / ATP hydrolysis activity / DNA binding / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Ronning, D.R. / Li, Y. / Perez, Z.N. / Ross, P.D. / Hickman, A.B. / Craig, N.L. / Dyda, F. | ||||||
Citation | Journal: Embo J. / Year: 2004 Title: The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA. Authors: Ronning, D.R. / Li, Y. / Perez, Z.N. / Ross, P.D. / Hickman, A.B. / Craig, N.L. / Dyda, F. #1: Journal: Mol.Cell / Year: 2000 Title: Unexpected structural diversity in DNA recombination: the restriction endonuclease connection. Authors: Hickman, A.B. / Li, Y. / Mathew, S.V. / May, E.W. / Craig, N.L. / Dyda, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t0f.cif.gz | 147.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t0f.ent.gz | 114.9 KB | Display | PDB format |
PDBx/mmJSON format | 1t0f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t0/1t0f ftp://data.pdbj.org/pub/pdb/validation_reports/t0/1t0f | HTTPS FTP |
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-Related structure data
Related structure data | 1f1zS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
-Transposon Tn7 transposition protein ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 31511.906 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: TNSA / Plasmid: pET30 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P13988 #2: Protein | Mass: 6102.005 Da / Num. of mol.: 2 / Fragment: Residues 504-555 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: TNSC / Plasmid: pET32 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P05846 |
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-Non-polymers , 4 types, 365 molecules
#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-MPD / ( #6: 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: 2.72 Å3/Da / Density % sol: 54.7 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9 Details: malonate, lithium sulfate, 2,4 methylpentanediol, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 11, 2003 / Details: mirrors |
Radiation | Monochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→50 Å / Num. all: 66363 / Num. obs: 66363 / % possible obs: 97.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 20.4 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 1.85→1.91 Å / Rmerge(I) obs: 0.386 / Mean I/σ(I) obs: 2.37 / Rsym value: 0.386 / % possible all: 99.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1F1Z Resolution: 1.85→42.41 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 494976.55 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 43.9947 Å2 / ksol: 0.363691 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.85→42.41 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.97 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Xplor file |
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