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. Author manuscript; available in PMC: 2014 Aug 1.
Published in final edited form as: FEBS J. 2013 Jun 24;280(15):3709–3720. doi: 10.1111/febs.12363

Table 2.

Structural alignment of eukaryotic HPt proteins with the present MtHPt1 structure from M. truncatula.

PDBa RMSD of Cα atoms (Å) Number of aligned residues Sequence identity (%) Number of secondary structure elements Q-scoreb
1oxk 1.28 108 19 5 0.43
1yvi 1.28 136 48 6 0.78
1wn0 1.29 136 50 6 0.77
a

The PDB accession codes correspond to the following HPt structures: 1oxk, Saccharomyces cerevisiae; 1yvi, Oryza sativa; 1wn0, Zea mays

b

Q-score represents the quality function of Cα alignment. It reduces the effect of RMSD - Nalgn (number of aligned residues) balance on the estimation of alignments (Nres1 and Nres2 stand for the number of residues in the aligned proteins, and the empirical parameter R0 is set to 3 Å): Q = (Nalgn·Nalgn)/[(1+(RMSD/R0)2)·Nres1·Nres2]