Supplemental Research Data

Files in this Data Supplement:

• Adobe PDF File (1 MB) - Fig. S1. Triangle maps indicating deviations of Calpha-Calpha distances along each PCA axis of 10-residue-segment sub-universe from the mean Csubalpha-Csubalpha distances. Scale bar indicates relative deviation. Red color is anti-phase against blue color. Residue numbers are displayed with horizontal and vertical sides of the triangle maps. (A) v1, (B) v2, and (C) v3 for helical segment sub-universe. (D) v1, (E) v2, and (F) v3 for strand segment sub-universe (PMF <2.84 kcal). (G) v1, (H) v2, and (I) v3 for strand segment sub- universe (2.36 less than or equal to PMF<2.84 kcal).
  
  Figure S2. Se strand motifs existing in protein-protein interfaces. Three tertiary structures, where Se strand motif participates in the complex formation, are shown iwth ribbon model: (A) citrate synthase (5csc), (B) baseplate structural protein gp11 (1e16), and (C) lignin peroxidase (1qpa). Each chain is represented by different color. Positions of Se strand motif in each structure are emphasized by space filling model (5csc;region 415-424, 1e16; region 194-203, and 1qpa: regions 320-329 and 330-339). Two Se segments are sequentially located in the region of 320-339 in 1qpa.