+Open data
-Basic information
Entry | Database: PDB / ID: 2trt | |||||||||
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Title | TETRACYCLINE REPRESSOR CLASS D | |||||||||
Components | TETRACYCLINE REPRESSOR 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 / Resolution: 2.5 Å | |||||||||
Authors | Hinrichs, W. / Kisker, C. / Saenger, W. | |||||||||
Citation | 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. #1: Journal: Mol.Gen.Genet. / Year: 1988 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. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2trt.cif.gz | 54.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2trt.ent.gz | 39.7 KB | Display | PDB format |
PDBx/mmJSON format | 2trt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2trt_validation.pdf.gz | 462.8 KB | Display | wwPDB validaton report |
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Full document | 2trt_full_validation.pdf.gz | 466 KB | Display | |
Data in XML | 2trt_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 2trt_validation.cif.gz | 9.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tr/2trt ftp://data.pdbj.org/pub/pdb/validation_reports/tr/2trt | HTTPS FTP |
-Related structure data
-Links
-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. |
-Components
#1: Protein | Mass: 24317.613 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PWH904 / Production host: Escherichia coli (E. coli) / Strain (production host): K12 DELTA H1 DELTA TRP / References: UniProt: P0ACT4 |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-TAC / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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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 |
-Processing
Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 |