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- PDB-6v54: Crystal Structure of Metallo Beta Lactamase from Hirschia baltica -
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Open data
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Basic information
Entry | Database: PDB / ID: 6v54 | ||||||
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Title | Crystal Structure of Metallo Beta Lactamase from Hirschia baltica | ||||||
![]() | Beta-lactamase | ||||||
![]() | HYDROLASE / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID | ||||||
Function / homology | ![]() antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Maltseva, N. / Kim, Y. / Clancy, S. / Endres, M. / Mulligan, R. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystal Structure of Metallo Beta Lactamase from Hirschia baltica. Authors: Maltseva, N. / Kim, Y. / Clancy, S. / Endres, M. / Mulligan, R. / Joachimiak, 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 | ![]() | 129.6 KB | Display | ![]() |
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PDB format | ![]() | 88.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 455.1 KB | Display | ![]() |
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Full document | ![]() | 456.1 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 18.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 25852.098 Da / Num. of mol.: 1 / Mutation: A257T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 49814 / DSM 5838 / IFAM 1418 / Gene: Hbal_3075 / Plasmid: pMCSG68 Production host: ![]() ![]() Strain (production host): BL21(DE3) / Variant (production host): Gold / References: UniProt: C6XID6, beta-lactamase |
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-Non-polymers , 7 types, 196 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / | ||||||||||
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#3: Chemical | #4: Chemical | ChemComp-EDO / | #5: Chemical | ChemComp-CL / | #6: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 10% PEG 8000, 0.1M TRIS pH 7.0, 0.2M magnesium chloride |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 30, 2015 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 1.45→29.37 Å / Num. obs: 49632 / % possible obs: 99.1 % / Redundancy: 4.1 % / Biso Wilson estimate: 16.03 Å2 / Rsym value: 0.09 / Net I/σ(I): 18.4 |
Reflection shell | Resolution: 1.45→1.48 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 1.7 / Num. unique obs: 2422 / CC1/2: 0.505 / % possible all: 98.4 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.02 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.45→29.37 Å
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Refine LS restraints |
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LS refinement shell |
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