Supplemental Data

Files in this Data Supplement:

• Supplemental Figure 2 - The unexplained Fo-Fc electron density of a ligand at 4.0 σ and residues near the binding pocket in the STR1-Highres. The 2.3 Å resolution data were collected from STR1-tryptamine complex crystal.
• Supplemental Figure 1 - Sequence alignment of STR1 from different plant species with other STR1-related gene family members. The grey shading showed the conserved residues in STR1_Rs and all the other enzymes. The conserved disulfide bond is highlighted with star on top of the two cysteins. The catalytic residue of STR1 is highlighted with black shadow and white letters. STR1-related sequences were picked up to show the diversity of the species and cover the sequence identity from 27 to 38%. STR1_Rs, STR1 from Rauvolfia serpentina and from Rauvolfia mannii; STR1_Cr, STR1 from Catharanthus roseus (sequence identity 79%); STR1_Op, STR1 from Ophiorrhiza pumila (sequence identity 58%); STR1_At, putative STR1 from Arabidopsis thaliana (sequence identity 38%); STR3_At, putative STR1 from Arabidopsis thaliana (sequence identity 37%); Hm_Dm, hemomucin from Drosophila melanogaster (fruit fly) (sequence identity 31%); BSCv_Hm, BSCv protein from human (sequence identity 27%)