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Open data
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Basic information
Entry | Database: PDB / ID: 5ifg | ||||||
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Title | Crystal structure of HigA-HigB complex from E. Coli | ||||||
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![]() | HYDROLASE/ANTITOXIN / mRNA interferase / HYDROLASE-ANTITOXIN complex | ||||||
Function / homology | ![]() toxin-antitoxin complex / regulation of growth / core promoter sequence-specific DNA binding / regulation of mRNA stability / RNA endonuclease activity / Hydrolases; Acting on ester bonds / negative regulation of translation / regulation of DNA-templated transcription / protein homodimerization activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yang, J.S. / Zhou, K. / Gao, z.Q. / Liu, Q.S. / Dong, Y.H. | ||||||
![]() | ![]() Title: Structural insight into the E. coli HigBA complex Authors: Yang, J. / Zhou, K. / Liu, P. / Dong, Y. / Gao, Z. / Zhang, J. / Liu, Q. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92.6 KB | Display | ![]() |
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PDB format | ![]() | 76.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.6 KB | Display | ![]() |
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Full document | ![]() | 484.1 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 27.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 12266.822 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: higB, ygjN, b3083, JW3054 / Production host: ![]() ![]() References: UniProt: P64578, Hydrolases; Acting on ester bonds #2: Protein | Mass: 15242.830 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: higA, ygjM, b3082, JW3053 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 61.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.3 Details: 0.2M (NH4)2SO4, 0.1M Bis-Tris pH5.3, 20%(w/v) PEG3350, 0.01M KCl |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jun 3, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection twin | Operator: -h,-k,l / Fraction: 0.33 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 35954 / % possible obs: 99.2 % / Redundancy: 17.4 % / Rmerge(I) obs: 0.105 / Net I/σ(I): 65.78 |
Reflection shell | Resolution: 2.7→2.75 Å / Redundancy: 20.9 % / Rmerge(I) obs: 0.519 / Mean I/σ(I) obs: 14.67 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS AND I_PLUS/MINUS COLUMNS
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.702→44.928 Å
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Refine LS restraints |
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LS refinement shell |
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