+Open data
-Basic information
Entry | Database: PDB / ID: 6ity | ||||||
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Title | CTX-M-64 sulbactam complex | ||||||
Components | Beta-lactamase | ||||||
Keywords | HYDROLASE / beta-lactamase inhibitor complex | ||||||
Function / homology | Function and homology information beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.14 Å | ||||||
Authors | Cheng, Q. / Chen, S. | ||||||
Citation | Journal: Acs Infect Dis. / Year: 2020 Title: Structural Insight into the Mechanism of Inhibitor Resistance in CTX-M-199, a CTX-M-64 Variant Carrying the S130T Substitution. Authors: Cheng, Q. / Xu, C. / Chai, J. / Zhang, R. / Wai Chi Chan, E. / Chen, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6ity.cif.gz | 116.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ity.ent.gz | 89.1 KB | Display | PDB format |
PDBx/mmJSON format | 6ity.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6ity_validation.pdf.gz | 459.4 KB | Display | wwPDB validaton report |
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Full document | 6ity_full_validation.pdf.gz | 463.7 KB | Display | |
Data in XML | 6ity_validation.xml.gz | 23.7 KB | Display | |
Data in CIF | 6ity_validation.cif.gz | 34.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/it/6ity ftp://data.pdbj.org/pub/pdb/validation_reports/it/6ity | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 29138.900 Da / Num. of mol.: 2 / Fragment: UNP residues 29-291 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: blaCTX-M-64, BK400_21830, pHNAH46_020 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: C8CP57, beta-lactamase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.84 Å3/Da / Density % sol: 32.98 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop Details: 0.1M HEPES (pH 7.4) and 17.5% polyethylene glycol 10000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.97917 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 30, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97917 Å / Relative weight: 1 |
Reflection | Resolution: 1.78→46.71 Å / Num. obs: 23098 / % possible obs: 94.6 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.196 / Net I/σ(I): 6.6 |
Reflection shell | Resolution: 1.78→1.88 Å / Redundancy: 6.5 % / Rmerge(I) obs: 0.739 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 6117 / % possible all: 96.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.14→46.71 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.914 / SU B: 5.482 / SU ML: 0.144 / Cross valid method: THROUGHOUT / ESU R: 0.292 / ESU R Free: 0.208 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.178 Å2
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Refinement step | Cycle: 1 / Resolution: 2.14→46.71 Å
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Refine LS restraints |
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