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Open data
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Basic information
Entry | Database: PDB / ID: 6bsq | ||||||
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Title | Enterococcus faecalis Penicillin Binding Protein 4 (PBP4) | ||||||
![]() | PBP4 protein | ||||||
![]() | HYDROLASE / Penicillin binding protein / transpeptidase / beta-lactam / antibiotic | ||||||
Function / homology | ![]() peptidoglycan L,D-transpeptidase activity / penicillin binding / cell wall organization / response to antibiotic / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Moon, T.M. / D'Andrea, E.D. / Peti, W. / Page, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: The structures of penicillin-binding protein 4 (PBP4) and PBP5 fromEnterococciprovide structural insights into beta-lactam resistance. Authors: Moon, T.M. / D'Andrea, E.D. / Lee, C.W. / Soares, A. / Jakoncic, J. / Desbonnet, C. / Garcia-Solache, M. / Rice, L.B. / Page, R. / Peti, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126.1 KB | Display | ![]() |
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PDB format | ![]() | 91.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.6 KB | Display | ![]() |
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Full document | ![]() | 441.3 KB | Display | |
Data in XML | ![]() | 24.8 KB | Display | |
Data in CIF | ![]() | 39 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6bsrC ![]() 6mkaC ![]() 6mkfC ![]() 6mkgC ![]() 6mkhC ![]() 6mkiC ![]() 6mkjC 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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Unit cell |
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Components
#1: Protein | Mass: 70709.102 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 58.96 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 40 mM potassium phosphate monobasic, 18% PEG800, 22% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: LIQUID ANODE / Type: BRUKER METALJET / Wavelength: 1.34 Å |
Detector | Type: Bruker PHOTON II / Detector: CMOS / Date: Jul 27, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.34 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→17.512 Å / Num. obs: 76417 / % possible obs: 98.9 % / Redundancy: 6.7 % / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 1.8→1.83 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PBP5 Resolution: 1.8→17.512 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.14
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→17.512 Å
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Refine LS restraints |
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LS refinement shell |
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