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Open data
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Basic information
Entry | Database: PDB / ID: 3cl0 | ||||||
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Title | N1 Neuraminidase H274Y + oseltamivir | ||||||
![]() | Neuraminidase![]() | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Collins, P. / Haire, L.F. / Lin, Y.P. / Liu, J. / Russell, R.J. / Walker, P.A. / Skehel, J.J. / Martin, S.R. / Hay, A.J. / Gamblin, S.J. | ||||||
![]() | ![]() Title: Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Authors: Collins, P.J. / Haire, L.F. / Lin, Y.P. / Liu, J. / Russell, R.J. / Walker, P.A. / Skehel, J.J. / Martin, S.R. / Hay, A.J. / Gamblin, S.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 | ![]() | 87.6 KB | Display | ![]() |
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PDB format | ![]() | 69.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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
#1: Protein | ![]() Mass: 42209.941 Da / Num. of mol.: 1 / Fragment: UNP residues 63-447 / Mutation: H274Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-G39 / (![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.46 % |
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8 Details: 15% PEG 3350, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jan 4, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.2→20 Å / Num. obs: 20040 / % possible obs: 95.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.2→2.3 Å / % possible all: 93.3 |
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Processing
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Refinement | Method to determine structure![]() ![]() Details: RESIDUE (A ASN 306 ) AND RESIDUE (A GLN 308 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.03. RESIDUE (A GLY 333 ) AND RESIDUE (A SER 335 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.11. ...Details: RESIDUE (A ASN 306 ) AND RESIDUE (A GLN 308 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.03. RESIDUE (A GLY 333 ) AND RESIDUE (A SER 335 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.11. RESIDUE (A CYS 336 ) AND RESIDUE (A GLY 339 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.49. RESIDUE (A SER 342 ) AND RESIDUE (A SER 344 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.24. RESIDUE (A VAL 392 ) AND RESIDUE (A LYS 394 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 1.94. RESIDUE (A GLU 433 ) AND RESIDUE (A SER 435 ) ARE NOT LINKED. DISTANCE OF C-N BOND IS 2.14.
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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: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.704 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.256 Å / Total num. of bins used: 20
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