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- PDB-2vli: Structure of Deinococcus radiodurans tunicamycin resistance protein -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vli | ||||||
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Title | Structure of Deinococcus radiodurans tunicamycin resistance protein | ||||||
![]() | ANTIBIOTIC RESISTANCE PROTEIN | ||||||
![]() | TRANSFERASE / PHOSPHOTRANSFERASE | ||||||
Function / homology | P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / : / Antibiotic resistance protein![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Macedo, S. / Kapp, U. / Leiros, I. / Hall, D.R. / Mitchell, E. | ||||||
![]() | ![]() Title: Structure of Deinococcus Radiodurans Tunicamycin-Resistance Protein (Tmrd), a Phosphotransferase. Authors: Kapp, U. / Macedo, S. / Hall, D.R. / Leiros, I. / Mcsweeney, S.M. / Mitchell, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80 KB | Display | ![]() |
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PDB format | ![]() | 64.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.4 KB | Display | ![]() |
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Full document | ![]() | 438.2 KB | Display | |
Data in XML | ![]() | 16.5 KB | Display | |
Data in CIF | ![]() | 24 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 20420.512 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: R1 / Production host: ![]() ![]() #2: Chemical | ChemComp-CD / | #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | Nonpolymer details | CADMIUM ION (CD): FROM CRYSTALLIS | Sequence details | PROTEIN WAS EXPRESSED USING A CONSTRUCT GIVING A PRODUCT WITH A C-TERMINAL TRUNCATION FROM RESIDUE ...PROTEIN WAS EXPRESSED USING A CONSTRUCT GIVING A PRODUCT WITH A C-TERMINAL TRUNCATION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 48.4 % Description: PHASING DATA WERE COLLECTED FROM A SECOND CRYSTAL. THE INITIAL MODEL WAS THEN TRANSFERRED TO HIGHER RESOLUTION DATA SET FROM ANOTHER CRYSTAL FOR REFINEMENT. |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 20 DEGREESC AFTER 3-6 DAYS USING HANGING DROPS CONTAINING 2 MICROL OF THE PROTEIN, 0.4-0.8 MICROL 0.1 M CDCL2 AND 1.6-1.2 MICROL OF A RESERVOIR SOLUTION CONTAINING 11-13% PEG 4000, 0.8 M ...Details: 20 DEGREESC AFTER 3-6 DAYS USING HANGING DROPS CONTAINING 2 MICROL OF THE PROTEIN, 0.4-0.8 MICROL 0.1 M CDCL2 AND 1.6-1.2 MICROL OF A RESERVOIR SOLUTION CONTAINING 11-13% PEG 4000, 0.8 M SODIUM FORMATE AND 0.1 M SODIUM ACETATE PH 5.0 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 15, 2006 / Details: RH COATED TOROIDAL MIRROR | |||||||||
Radiation | Monochromator: SI DOUBLE CRYSTAL MONOCHROMATOR / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.95→22.93 Å / Num. obs: 28689 / % possible obs: 99.5 % / Observed criterion σ(I): -3.7 / Redundancy: 4.94 % / Biso Wilson estimate: 19.9 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.54 | |||||||||
Reflection shell | Resolution: 1.95→1.97 Å / Redundancy: 5.09 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.95→22.9 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.927 / SU B: 3.354 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.148 / ESU R Free: 0.138 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE N-TERMINAL HIS-TAGS AND RESIDUES TO A4 AND B3 AND FROM A176 AND B176 WERE NOT VISIBLE IN THE DENSITY MAPS. RESIDUES A15-18 AND A126-129 ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE N-TERMINAL HIS-TAGS AND RESIDUES TO A4 AND B3 AND FROM A176 AND B176 WERE NOT VISIBLE IN THE DENSITY MAPS. RESIDUES A15-18 AND A126-129 WERE ALSO NOT VISIBLE. ALL THESE RESIDUES WERE THEREFORE NOT INCLUDED IN THE STRUCTURE MODEL.
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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: 20.9 Å2
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Refinement step | Cycle: LAST / Resolution: 1.95→22.9 Å
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