+Open data
-Basic information
Entry | Database: PDB / ID: 1a6i | ||||||
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Title | TET REPRESSOR, CLASS D VARIANT | ||||||
Components | TETRACYCLINE REPRESSOR PROTEIN CLASS D | ||||||
Keywords | TRANSCRIPTION REGULATION / REPRESSOR / DNA-BINDING | ||||||
Function / homology | Function and homology information transcription cis-regulatory region binding / DNA-binding transcription factor activity / response to antibiotic / negative regulation of DNA-templated transcription / metal ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Orth, P. / Cordes, F. / Schnappinger, D. / Hillen, W. / Saenger, W. / Hinrichs, W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: Conformational changes of the Tet repressor induced by tetracycline trapping. Authors: Orth, P. / Cordes, F. / Schnappinger, D. / Hillen, W. / Saenger, W. / Hinrichs, W. #1: Journal: J.Mol.Biol. / Year: 1995 Title: The Complex Formed between Tet Repressor and Tetracycline-Mg2+ Reveals Mechanism of Antibiotic Resistance Authors: Kisker, C. / Hinrichs, W. / Tovar, K. / Hillen, W. / Saenger, W. #2: Journal: Science / Year: 1994 Title: Structure of the Tet Repressor-Tetracycline Complex and Regulation of Antibiotic Resistance Authors: Hinrichs, W. / Kisker, C. / Duvel, M. / Muller, A. / Tovar, K. / Hillen, W. / Saenger, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a6i.cif.gz | 50.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a6i.ent.gz | 36.6 KB | Display | PDB format |
PDBx/mmJSON format | 1a6i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a6i_validation.pdf.gz | 409.7 KB | Display | wwPDB validaton report |
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Full document | 1a6i_full_validation.pdf.gz | 413.2 KB | Display | |
Data in XML | 1a6i_validation.xml.gz | 9.4 KB | Display | |
Data in CIF | 1a6i_validation.cif.gz | 11.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a6/1a6i ftp://data.pdbj.org/pub/pdb/validation_reports/a6/1a6i | HTTPS FTP |
-Related structure data
Related structure data | 2tctS 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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Unit cell |
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-Components
#1: Protein | Mass: 24319.691 Da / Num. of mol.: 1 Mutation: A2S, N5D, R6K, E7S, S8K, D11N, A12S, T20V, D23E, I36V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 DELTA H1 DELTA TRP / Cellular location: CYTOPLASM / Plasmid: PWH610 (B/D)51-208 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ACT4 |
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#2: 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: 2.4 Å3/Da / Density % sol: 49 % Description: DATA WERE COLLECTED USING THE OSCILLATION METHOD | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, hanging dropDetails: 0.01ml protein solution was mixed with 0.005ml reservoir | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→18.5 Å / Num. obs: 9076 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Biso Wilson estimate: 42.4 Å2 / Rsym value: 0.073 / Net I/σ(I): 6.13 |
Reflection shell | Resolution: 2.4→2.47 Å / Redundancy: 4.9 % / Mean I/σ(I) obs: 2.9 / Rsym value: 0.248 / % possible all: 98.6 |
Reflection | *PLUS Rmerge(I) obs: 0.073 |
Reflection shell | *PLUS % possible obs: 98.6 % / Rmerge(I) obs: 0.248 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2TCT Resolution: 2.4→18.5 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 47.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å / Luzzati d res low obs: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→18.5 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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