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Open data
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Basic information
Entry | Database: PDB / ID: 2trt | |||||||||
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Title | TETRACYCLINE REPRESSOR CLASS D | |||||||||
![]() | TETRACYCLINE REPRESSOR CLASS D | |||||||||
![]() | TRANSCRIPTION REGULATION / REPRESSOR / DNA-BINDING | |||||||||
Function / homology | ![]() 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 | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Hinrichs, W. / Kisker, C. / Saenger, W. | |||||||||
![]() | ![]() 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. #1: ![]() Title: Identification and Nucleotide Sequence of the Class E Tet Regulatory Elements and Operator and Inducer Binding of the Encoded Purified Tet Repressor Authors: Tovar, K. / Ernst, A. / Hillen, W. | |||||||||
History |
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Remark 650 | HELIX THE PEPTIDE IS FOLDED INTO 10 ALPHA-HELICES WITH CONNECTING TURNS AND LOOPS, WITHOUT ANY BETA-STRANDS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.7 KB | Display | ![]() |
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PDB format | ![]() | 39.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 462.8 KB | Display | ![]() |
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Full document | ![]() | 466 KB | Display | |
Data in XML | ![]() | 6.4 KB | Display | |
Data in CIF | ![]() | 9.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 ASYMMETRIC UNIT CONTAINS RESIDUES ALA 2 - VAL 208, REPRESENTING THE MONOMER OF THE HOMODIMERIC PROTEIN. |
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Components
#1: Protein | Mass: 24317.613 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-TAC / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.38 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: vapor diffusion / Details: H. E. Parge, (1984) J. Mol. Biol., 180, 1189. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / Num. obs: 8505 / % possible obs: 94 % / Rmerge(I) obs: 0.065 |
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Processing
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Refinement | Resolution: 2.5→10 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.19 / Rfactor Rwork: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |