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- PDB-2bjc: NMR structure of a protein-DNA complex of an altered specificity ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bjc | ||||||
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Title | NMR structure of a protein-DNA complex of an altered specificity mutant of the lac repressor headpiece that mimics the gal repressor | ||||||
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![]() | TRANSCRIPTION REGULATOR / SYMMETRIC DNA-BINDING / DNA-BINDING / HTH / LAC OPERON / LAC REPRESSOR / ALTERED SPECIFICITY / MUTANT / REPRESSOR / TRANSCRIPTION REGULATION / TRANSCRIPTION REGULATOR/DNA / GAL REPRESSOR / GAL OPERON / LAC HEADPIECE / SYMMETRIC DIMER | ||||||
Function / homology | ![]() DNA-binding transcription repressor activity / cis-regulatory region sequence-specific DNA binding / transcription cis-regulatory region binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / HADDOCK | ||||||
![]() | Salinas, R.K. / Folkers, G.E. / Bonvin, A.M.J.J. / Das, D. / Boelens, R. / Kaptein, R. | ||||||
![]() | ![]() Title: Altered Specificity in DNA Binding by the Lac Repressor: A Mutant Lac Headpiece that Mimics the Gal Repressor Authors: Salinas, R.K. / Folkers, G.E. / Bonvin, A.M.J.J. / Das, D. / Boelens, R. / Kaptein, R. #1: ![]() Title: Plasticity in Protein-DNA Recognition: Lac Repressor Interacts with its Natural Operator O1 Through Alternative Conformations of its DNA Binding Domain Authors: Kalodimos, C.G. / Bonvin, A.M.J.J. / Salinas, R.K. / Wechselberger, R. / Boelens, R. / Kaptein, R. #2: Journal: Embo J. / Year: 1987 Title: The Interaction of the Recognition Helix of Lac Repressor with Lac Operator Authors: Lehming, N. / Sartorius, J. / Niemoler, M. / Genenger, G. / Wilcken-Bergmann, B. / Muller-Hill, B. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1022.4 KB | Display | ![]() |
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PDB format | ![]() | 894.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 451.8 KB | Display | ![]() |
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Full document | ![]() | 750.1 KB | Display | |
Data in XML | ![]() | 54.8 KB | Display | |
Data in CIF | ![]() | 85.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6701.661 Da / Num. of mol.: 2 / Fragment: DNA BINDING DOMAIN, LAC HEADPIECE RESIDUES 1-62 / Mutation: YES Source method: isolated from a genetically manipulated source Details: THE PROTEIN IS A DIMER. DISULFIDE BOND BETWEEN CYS52 IN TWO MONOMERS FORMS A COVALENT DIMER Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: DNA chain | Mass: 6750.390 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: ALTERED LAC SYML OPERATOR Compound details | ENGINEERED | Sequence details | RESIDUES 1-62 OF LAC REPRESSOR (P03023) WITH THE SUBSTITUTIONS Y17V Q18A AND V52C ALTERED ...RESIDUES 1-62 OF LAC REPRESSOR (P03023) WITH THE SUBSTITUTI | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 3D 15N NOESY-![]() ![]() ![]() ![]() ![]() |
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR SPECTROSCOPY ON A 13C, 15N LABELED PROTEIN AND UNLABELED DNA. |
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Sample preparation
Details | Contents: 95% WATER/5% D2O |
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Sample conditions | Ionic strength: 20 mM / pH: 6.0 / Pressure: 1.0 atm / Temperature: 315.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 900 MHz |
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Processing
NMR software |
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Refinement | Method: HADDOCK / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE | |||||||||
NMR ensemble | Conformer selection criteria: RMSD TO AVERAGE STRUCTURE AND LOWEST ENERGY Conformers calculated total number: 50 / Conformers submitted total number: 16 |