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Open data
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Basic information
Entry | Database: PDB / ID: 4yg7 | ||||||
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Title | Structure of FL autorepression promoter complex | ||||||
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![]() | TRANSCRIPTION / TRANSFERASE/DNA / persistence / multidrug tolerance / autorepression / promoter / TRANSFERASE-DNA complex | ||||||
Function / homology | ![]() dormancy process / toxin-antitoxin complex / single-species biofilm formation / regulation of growth / DNA-binding transcription repressor activity / core promoter sequence-specific DNA binding / protein-DNA complex / sequence-specific DNA binding / non-specific serine/threonine protein kinase / transcription cis-regulatory region binding ...dormancy process / toxin-antitoxin complex / single-species biofilm formation / regulation of growth / DNA-binding transcription repressor activity / core promoter sequence-specific DNA binding / protein-DNA complex / sequence-specific DNA binding / non-specific serine/threonine protein kinase / transcription cis-regulatory region binding / phosphorylation / response to antibiotic / protein serine kinase activity / protein serine/threonine kinase activity / negative regulation of DNA-templated transcription / DNA-templated transcription / regulation of DNA-templated transcription / magnesium ion binding / protein homodimerization activity / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schumacher, M.A. | ||||||
![]() | ![]() Title: HipBA-promoter structures reveal the basis of heritable multidrug tolerance. Authors: Schumacher, M.A. / Balani, P. / Min, J. / Chinnam, N.B. / Hansen, S. / Vulic, M. / Lewis, K. / Brennan, R.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 282.6 KB | Display | ![]() |
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PDB format | ![]() | 223.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 498.3 KB | Display | ![]() |
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Full document | ![]() | 642.8 KB | Display | |
Data in XML | ![]() | 62 KB | Display | |
Data in CIF | ![]() | 84.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4yg1C ![]() 4yg4C ![]() 5k98C ![]() 3dnvS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 8060.239 Da / Num. of mol.: 4 / Fragment: UNP residues 4-74 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: hipB, b1508, JW1501 / Production host: ![]() ![]() #2: Protein | Mass: 48946.203 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: hipA, b1507, JW1500 / Production host: ![]() ![]() References: UniProt: P23874, non-specific serine/threonine protein kinase #3: DNA chain | | Mass: 15398.923 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #4: DNA chain | | Mass: 15414.922 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.29 Å3/Da / Density % sol: 76.75 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: sodium formate / PH range: 5-7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 23, 2013 |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.77→161.4 Å / Num. obs: 34997 / % possible obs: 63.6 % / Redundancy: 4 % / Net I/σ(I): 4 |
Reflection shell | Mean I/σ(I) obs: 1.4 / Rsym value: 0.762 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 3DNV Resolution: 3.77→161.4 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: AUTHOR STATES ONLY MINIMAL REFINEMENT WAS PERFORMED.
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Solvent computation | Bsol: 72.4475 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 267.11 Å2 / Biso mean: 180.4669 Å2 / Biso min: 1 Å2
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Refinement step | Cycle: final / Resolution: 3.77→161.4 Å
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Refine LS restraints |
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LS refinement shell | Highest resolution: 3.77 Å / Rfactor Rfree: 0.46 | ||||||||||||||||||||||||||||
Xplor file |
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