Amino acid sequence alignment of human NR2E3 (PNR) and NR2B1 (RXRα) DNA-binding domains (DBDs). The NR2E3 DBD (residues 47–123 of SwissProt Acc. No. Q9Y5X4) exhibits a sequence identity of 57.1% (44 residues) and a sequence similarity of 80.5% (62 residues) with the RXRαDBD (residues 135–210 of SwissProt Acc. No. P19793). The main regions of the DBD, i.e. the two Cys4 Zn-fingers and the so-called T/A box, are indicated above the sequence alignment. Disease-causing mutations are indicated above the NR2E3 sequence. Given the high sequence homology, the structural data obtained for RXRα were also indicated on the NR2E3 sequence [27], [28]. Residues directly interacting with DNA are highlighted in yellow. Residues directly involved in protein-protein interactions in the RXR homodimer are highlighted in blue. Residues involved in both DNA-binding and RXR dimerization are highlighted in grey. The α-helical regions are underlined. The α-helical region extending from the C-terminus of the first Cys4 Zn-finger is called recognition helix and contains the P-box responsible for DNA-binding specificity. The residues of the P-box are shown in italics. In the N-terminus of the second Cys4 Zn-finger, the residues of the D-box involved in dimerization are also shown in italics. A second α-helical region extends from the C-terminus of the second Cys4 Zn-finger. The third α-helix is a part of the so-called T/A box that extends beyond the region for which crystallographic data are available. Sequences were aligned with the CLUSTAL W 2.0 algorithm. Polar residues are shown in green, non-polar residues in red, basic residues in magenta, and acidic residues in blue. Below the sequence alignment, (*) denotes sequence identity, (:) denotes conserved substitutions, and, (.) denotes semi-conserved substitutions.
http://plosone.org/article/info:doi/10.1371/journal.pone.0007379#article1.body1.sec5.supplementary-material7.caption1.p1

Some of the symbols in legend s7 do not appear. The correct legend should read: Amino acid sequence alignment of human NR2E3 (PNR) and NR2B1 (RXRα) DNA-binding domains (DBDs). The NR2E3 DBD (residues 47-123 of SwissProt Acc. No. Q9Y5X4) exhibits a sequence identity of 57.1% (44 residues) and a sequence similarity of 80.5% (62 residues) with the RXRα DBD (residues 135-210 of SwissProt Acc. No. P19793). The main regions of the DBD, i.e. the two Cys4 Zn-fingers and the so-called T/A box, are indicated above the sequence alignment. Disease-causing mutations are indicated above the NR2E3 sequence. Given the high sequence homology, the structural data obtained for RXRα were also indicated on the NR2E3 sequence [27, 28]. Residues directly interacting with DNA are highlighted in yellow. Residues directly involved in protein-protein interactions in the RXR homodimer are highlighted in blue. Residues involved in both DNA-binding and RXR dimerization are highlighted in grey. The α-helical regions are underlined. The α-helical region extending from the C-terminus of the first Cys4 Zn-finger is called recognition helix and contains the P-box responsible for DNA-binding specificity. The residues of the P-box are shown in italics. In the N-terminus of the second Cys4 Zn-finger, the residues of the D-box involved in dimerization are also shown in italics. A second α-helical region extends from the C-terminus of the second Cys4 Zn-finger. The third α-helix is a part of the so-called T/A box that extends beyond the region for which crystallographic data are available. Sequences were aligned with the CLUSTAL W 2.0 algorithm. Polar residues are shown in green, non-polar residues in red, basic residues in magenta, and acidic residues in blue. Below the sequence alignment, (*) denotes sequence identity, (:) denotes conserved substitutions, and, (.) denotes semi-conserved substitutions.