Significant mapped SLE risk residues.

The most-risk (highest OR; in 19/20 cases, also the most significant) side-chain at each protein position is evaluated according to a simple model (Supplementary Note, S10a Table). Side-chains predicted risk include: W, I, F, L, E, Y, D. R, S, N, K, T are predicted to be protective. Residues written as: position, amino acid, position in binding pocket (p1-p9 or peptide-binding 2nd shell), P-value for the discovery cohort, odds ratio. *: DRB1-13R is in complete LD with DRB1-11P. Residues are formatted according to their consistency with the statistical SLE risk-prediction model: risk (bold); protective (italics); and neither (unformatted). Amino acid properties: Negatively charged (Asp, D; Glu, E); Positively charged (Arg, R; Lys, K); Potentially positively charged (His, H); Large, hydrophobic (Trp, W; Ile, I; Phe, F; Leu, L; Tyr, Y; Met, M); Medium, hydrophobic (Pro, P; Val, V); Small, hydrophobic (Ala, A; Gly, G; Cys, C); Neutral hydrophilic (Gln, Q; Asn, N; Ser, S; Thr, T).