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- PDB-2v1z: Structure of a TEM-1 beta-lactamase insertant allosterically regu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2v1z | ||||||
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Title | Structure of a TEM-1 beta-lactamase insertant allosterically regulated by kanamycin and anions. | ||||||
![]() | BETA-LACTAMASE TEM | ||||||
![]() | HYDROLASE / INSERTION MUTANT / ANTIBIOTIC RESISTANCE / ALLOSTERIC REGULATION | ||||||
Function / homology | ![]() beta-lactam antibiotic catabolic process / beta-lactamase activity / beta-lactamase / response to antibiotic Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Evrard, C. / Barrios, H. / Mathonet, P. / Soumillion, P. / Fastrez, J. / Declercq, J.P. | ||||||
![]() | ![]() Title: Engineering an Allosteric Binding Site for Aminoglycosides Into Tem1-Beta-Lactamase. Authors: Volkov, A.N. / Barrios, H. / Mathonet, P. / Evrard, C. / Ubbink, M. / Declercq, J.P. / Soumillion, P. / Fastrez, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.4 KB | Display | ![]() |
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PDB format | ![]() | 55 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 410.9 KB | Display | ![]() |
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Full document | ![]() | 411.7 KB | Display | |
Data in XML | ![]() | 14.9 KB | Display | |
Data in CIF | ![]() | 23.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2v20C ![]() 1btlS S: Starting model for refinement 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: 32447.049 Da / Num. of mol.: 1 / Fragment: RESIDUES 25-38,41-286 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
Compound details | ENGINEERED RESIDUE IN CHAIN A, VAL 82 TO ILE ENGINEERED RESIDUE IN CHAIN A, GLU 102 TO LYS ...ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.9 % / Description: NONE |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.2 Details: RESERVOIR: BIS-TRIS 0.1M PH6.2, PEG6000 25%(W/V), NACL 0.3M, NAN3 0.02%(W/V). HANGING DROP: 1UL PROTEIN AND 1 UL RESERVOIR |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 11, 2005 / Details: TWO MIRRORS ARE USED FOR VERTICAL FOCUSSING. |
Radiation | Monochromator: FIRST CRYSTAL FLAT AND N2 COOLED. SECOND ONE SAGITALLY BENT. SI(111) OR SI(311) Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97976 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→40 Å / Num. obs: 34091 / % possible obs: 96.7 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 23.9 |
Reflection shell | Resolution: 1.6→1.65 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 8.2 / % possible all: 93.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1BTL Resolution: 1.6→52.41 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.933 / SU B: 1.462 / SU ML: 0.053 / Cross valid method: THROUGHOUT / ESU R: 0.092 / ESU R Free: 0.093 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.04 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→52.41 Å
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Refine LS restraints |
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