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- PDB-2xgc: Crystal structure of a designed heterodimeric variant T-A(I)B of ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xgc | ||||||
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Title | Crystal structure of a designed heterodimeric variant T-A(I)B of the tetracycline repressor | ||||||
![]() | (TETRACYCLINE REPRESSOR PROTEIN CLASS B FROM TRANSPOSON TN10, TETRACYCLINE REPRESSOR PROTEIN CLASS D) x 2 | ||||||
![]() | TRANSCRIPTION / CHIMERA / TRANSCRIPTION REGULATION / ANTIBIOTIC RESISTANCE | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Stiebritz, M.T. / Wengrzik, S. / Richter, J.P. / Muller, Y.A. | ||||||
![]() | ![]() Title: Computational Design of a Chain-Specific Tetracycline Repressor Heterodimer. Authors: Stiebritz, M.T. / Wengrzik, S. / Klein, D.L. / Richter, J.P. / Srebrzynski, A. / Weiler, S. / Muller, Y.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 169.4 KB | Display | ![]() |
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PDB format | ![]() | 136.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.3 KB | Display | ![]() |
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Full document | ![]() | 442.3 KB | Display | |
Data in XML | ![]() | 16.3 KB | Display | |
Data in CIF | ![]() | 18.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xgdC ![]() 2xgeC ![]() 1a6iS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 23486.723 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-50,51-208 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 23710.916 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-50,51-208 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
Compound details | ENGINEERED RESIDUE IN CHAIN A, ALA 136 TO TRP ENGINEERED RESIDUE IN CHAIN B, PHE 140 TO ALA ...ENGINEERED |
Sequence details | ENGINEERED VARIANT, NAMELY CHIMERA OF P04483 AND P0ACT4 ( UNIPROT ACCESSION NUMBERS) AUTHOR HAS ...ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→40 Å / Num. obs: 12563 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 14.2 % / Biso Wilson estimate: 48.5 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 29.1 |
Reflection shell | Resolution: 2.15→2.28 Å / Redundancy: 12 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 4.6 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1A6I Resolution: 2.15→34.59 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.925 / SU B: 14.642 / SU ML: 0.19 / Cross valid method: THROUGHOUT / ESU R: 0.276 / ESU R Free: 0.226 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. THE CRYSTAL STRUCTURE ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. THE CRYSTAL STRUCTURE CORRESPONDS TO A HETERODIMER WITH CHAINS A AND B. BOTH CHAINS DIFFER AT ONLY 5 POSITIONS. THE DATA HAS BEEN EXPLAINED A BIMODAL DISORDER MODEL IN WHICH BOTH CHAINS ARE PRESENT WITH 0.5 OCCUPANCY IN THE ASYMMETRIC UNIT AT THE SAME TIME.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.349 Å2
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Refinement step | Cycle: LAST / Resolution: 2.15→34.59 Å
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Refine LS restraints |
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