Table 3.

Average displacement of amino acids following S-nitrosylation

	Basic residues (r.m.s.d.)	Acidic residues (r.m.s.d.)	Polar residues (r.m.s.d.)	Apolar residues (r.m.s.d.)	All residues (r.m.s.d.)
Myoglobin	2.1 Å	1.2 Å	1.3 Å	1.1 Å	1.4 Å
Trx1	1.3 Å	1.1 Å	0.8 Å	0.5 Å	0.8 Å
Hemoglobin	1.9 Å	1.7 Å	1.3 Å	1 Å	1.3 Å
PTP1b	1.1 Å	1.5 Å	0.8 Å	0.5 Å	0.9 Å

The structures of human Trx1, with NO-Cys (1ERU) and without this modification (2HXK), Blackfin tuna myoglobin (2NRM and 1MYT), human hemoglobin (1BUW and 1A3N) and human PTP1B (3EU0 and 2F6F) were superimposed with DeepView 4.0. The root mean square deviation (rmsd) was calculated for all atoms of proteins, and separately, for all atoms belonging to each different set of amino acids grouped on the basis of their chemical similarities as defined by DeepView (i.e. basic, acidic, polar not charged and apolar residues). Values reported refer to the rmsd expressed in Å, and reflects different extent of displacement for each group of amino acids following S-nitrosylation event.