Fig. 2

Spectrometry analysis and alignment. a Mass spectrum of Lmr-MP. Molecular mass of Lmr-MP was obtained by MALDI-TOF (positive linear mode) using sinapinic acid (SA) matrix. b HCD MS/MS of the (M + 2H) ^+ 2 ion of the tryptic peptide SNQDLINVQSAAADTLK acquired on an Orbitrap Elite™ Mass Spectrometer with 15,000 resolution (at 400 m/z). N-terminal ions (a and b) are shown in red and indicated by ˩ whereas C-terminal ions (y) are shown in blue and indicated by Г. Internal ions are shown in green. Mass accuracy for all fragment ions is better than 20 ppm. The mass spectrometer used cannot differentiate between leucine and isoleucine residues, and the assignment is made here solely with homology matching. c Sequence alignments of sv-MP hemorrhagic factor-2 (LHF-II) from L. m. muta (UniProt ID P22796) and Lmr-MP from L. m. rhombeata. The highly conserved residues are highlighted in black. Cys residues are shaded gray. Asn-aaX-Ser/Thr residue (star symbol) represents the N-glycosylation site. X = Leu/Ile. Alignment and figure were generated by MultAlin and ESPript servers, respectively