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Kinetic, Thermodynamic and Structural Analysis of Tamiphosphor Binding to
Neuraminidase of H1N1 (2009) Pandemic Influenza
Carlos Berenguer Albiñana1, Aleš Machara1, Pavlína Řezáčová2,3, Petr Pachl2, Jan Konvalinka2,4*,
Milan Kožíšek2*
1Department of Organic Chemistry, Faculty of Science, Charles University, Hlavova 8, 128 00 Prague 2,
Czech Republic; 2Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech
Republic, Gilead Sciences and IOCB Research Center, Flemingovo n. 2, 166 10 Prague 6, Czech
Republic; 3Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Vídeňská 1083,
140 00 Prague 4, Czech Republic; 4Department of Biochemistry, Faculty of Science, Charles University,
Hlavova 8, 128 00 Prague 2, Czech Republic
*Corresponding authors:
Milan Kožíšek or Jan Konvalinka, Institute of Organic Chemistry and Biochemistry, Academy of
Sciences of the Czech Republic, Gilead Sciences and IOCB Research Center, Flemingovo n. 2,
166 10 Prague 6, Czech Republic
Fax : +420 220 183 578; Tel : +420 220 183 218; e-mails : [email protected],
Table of Contents1
Figure S1 S03
Table S1 S04
Copies of 1H-NMR and 13CNMR spectra S05
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Figure S1: A) Neuraminidase molecules in two crystal lattice domains are shown as ribbons. Ligand
bound to the active site is highlighted as spheres. High-occupancy and low-occupancy dimers are shown
in green and yellow, respectively. B) Electron density map (2Fo – Fc) for tamiphosphor bound to the active
site in the high occupancy model contoured at 1.0 . C) Electron density map (2Fo – Fc) for tamiphosphor
bound to the active site in the low occupancy model contoured at 0.6 .
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Table S1: Hydrogen bond distance analysis.
Oseltamivir carboxylate Tamiphosphor
Inhibitor atom Protein residue/atom Distance[Å]
Inhibitor atom Protein residue/atom Distance[Å]
G39 O1A Arg 118 A NH1 2.84 G40 O1A Arg 118 A NH1 2.89
G39 O1A Arg 118 A NH2 3.5 G40 O1A Arg 118 A NH2 3.45
G39 N4 Glu 119 A OE1 2.8 G40 N4 Glu 119 A OE2 2.73
G39 N4 Asp 151 A OD1 3.19 G40 N4 Asp 151 A OD1 3.06
G39 O10 Asp 151 A OD2 4.03 G40 O10 Asp 151 A OD2 3.95
G39 O10 Arg 152 A NH1 2.81 G40 O10 Arg 152 A NH1 2.91
G39 O1B Arg 292 A NH2 3.1 G40 O1B Arg 293 A NH2 2.82
G39 O1B Arg 292 A NH1 3.29 G40 O1B Arg 293 A NH1 3.28
G39 O1B Arg 371 A NH2 2.64 G40 O1A Arg 368 A NH1 2.75
G39 O1A Arg 371 A NH1 2.83 G40 O1B Arg 368 A NH2 2.78
G39 O1A Arg 371 A NH2 3.44 G40 O1A Arg 368 A NH2 3.45
G39 O1B Arg 371 A NH1 3.65 G40 O1B Arg 368 A NH1 3.81
G39 O1A Tyr 406 A OH 3.47 G40 O1A Tyr 402 A OH 3.32
G39 O1B Tyr 406 A OH 3.61 G40 O1B Tyr 402 A OH 3.69
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