==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=25-DEC-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE INHIBITOR 06-JUL-11 2LFL . COMPND 2 MOLECULE: TRYPTASE INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: RHIPICEPHALUS APPENDICULATUS; . AUTHOR S.BRONSOMS,D.PANTOJA-UCEDA,D.GABRIJELCIC-GEIGER,L.SANGLAS,F. . 57 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 5043.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 19 33.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 5 8.8 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 1 1.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . 1 1.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . 4 7.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 5.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 4 7.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . 0 0 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA 1 19 A G 0 0 129 0, 0.0 2,-0.2 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 100.2 6.0 -3.3 24.7 2 20 A D - 0 0 174 1,-0.1 0, 0.0 2,-0.0 0, 0.0 -0.479 360.0-176.0 -67.3 134.5 3.8 -5.0 22.0 3 21 A K + 0 0 194 -2,-0.2 -1,-0.1 2,-0.0 2,-0.1 0.445 47.1 103.7-114.1 -6.7 5.8 -7.0 19.4 4 22 A E + 0 0 186 1,-0.0 2,-0.2 2,-0.0 -2,-0.0 -0.363 44.4 178.5 -72.0 158.0 2.9 -8.1 17.0 5 23 A E - 0 0 159 -2,-0.1 2,-0.4 2,-0.0 -2,-0.0 -0.875 28.1-104.8-145.3 178.4 2.2 -6.5 13.5 6 24 A a + 0 0 55 -2,-0.2 2,-0.3 26,-0.0 28,-0.0 -0.953 37.8 169.0-115.9 135.4 -0.1 -6.8 10.5 7 25 A T - 0 0 89 -2,-0.4 26,-0.1 28,-0.0 25,-0.1 -0.906 47.1 -67.9-140.0 159.0 1.0 -8.3 7.1 8 26 A V - 0 0 30 -2,-0.3 6,-0.1 1,-0.1 3,-0.1 -0.317 55.7-142.2 -51.6 118.5 -0.6 -9.4 3.7 9 27 A P > - 0 0 62 0, 0.0 3,-0.8 0, 0.0 -1,-0.1 -0.218 38.4 -58.1 -78.1 175.4 -2.8 -12.6 4.4 10 28 A I T 3 S+ 0 0 177 1,-0.2 3,-0.1 3,-0.0 2,-0.1 -0.283 116.9 45.1 -58.1 133.9 -3.2 -15.7 2.2 11 29 A G T 3 S+ 0 0 72 1,-0.5 -1,-0.2 -3,-0.1 2,-0.1 -0.534 102.3 62.3 128.2 -60.8 -4.6 -14.9 -1.3 12 30 A W < - 0 0 132 -3,-0.8 -1,-0.5 -2,-0.1 2,-0.3 -0.273 68.2-140.5 -85.2 175.7 -2.5 -11.8 -2.4 13 31 A S - 0 0 96 -3,-0.1 3,-0.0 -2,-0.1 -3,-0.0 -0.984 14.3-130.9-143.2 122.6 1.3 -11.3 -2.9 14 32 A E - 0 0 97 -2,-0.3 2,-0.4 -6,-0.1 23,-0.1 -0.375 36.5 -93.4 -69.5 152.9 3.4 -8.3 -1.9 15 33 A P - 0 0 47 0, 0.0 -1,-0.1 0, 0.0 23,-0.0 -0.559 24.9-159.7 -69.8 121.9 5.9 -6.6 -4.4 16 34 A V S S+ 0 0 149 -2,-0.4 -2,-0.0 -3,-0.0 2,-0.0 0.772 72.9 78.7 -70.1 -27.1 9.5 -8.1 -4.1 17 35 A K - 0 0 132 21,-0.0 2,-0.3 2,-0.0 21,-0.1 -0.189 61.1-169.7 -70.9 168.7 10.8 -4.8 -5.9 18 36 A G - 0 0 62 19,-0.1 2,-0.1 20,-0.0 19,-0.0 -0.953 14.6-176.2-161.9 148.8 11.3 -1.4 -4.3 19 37 A L > + 0 0 93 -2,-0.3 3,-1.1 1,-0.1 -2,-0.0 -0.590 9.8 169.1-150.9 79.6 12.1 2.2 -5.6 20 38 A C T 3 + 0 0 128 1,-0.2 -1,-0.1 -2,-0.1 0, 0.0 0.481 64.6 90.5 -68.7 -3.9 12.6 4.9 -2.9 21 39 A K T 3 + 0 0 175 2,-0.0 -1,-0.2 0, 0.0 -2,-0.0 0.644 64.7 100.1 -68.8 -21.1 13.9 7.2 -5.7 22 40 A A S < S- 0 0 35 -3,-1.1 -3,-0.0 2,-0.1 16,-0.0 -0.248 75.4-132.4 -66.7 158.3 10.4 8.7 -6.3 23 41 A R S S+ 0 0 250 2,-0.0 2,-0.3 -2,-0.0 -1,-0.1 0.273 92.0 40.7 -93.0 6.6 9.2 12.1 -4.9 24 42 A F S S- 0 0 130 2,-0.0 2,-0.3 0, 0.0 -2,-0.1 -0.900 70.2-148.6-144.1 167.2 5.9 10.4 -3.7 25 43 A T - 0 0 55 -2,-0.3 2,-0.3 21,-0.2 13,-0.1 -0.967 9.9-142.9-142.2 152.8 4.9 7.1 -2.0 26 44 A R E -A 37 0A 42 11,-1.0 11,-2.0 -2,-0.3 2,-0.4 -0.929 7.8-164.5-128.0 146.1 1.7 4.9 -2.3 27 45 A Y E -A 36 0A 54 18,-0.8 18,-0.4 -2,-0.3 2,-0.4 -0.996 6.5-174.5-138.3 125.7 -0.2 2.9 0.3 28 46 A Y E -A 35 0A 19 7,-1.5 7,-0.7 -2,-0.4 2,-0.4 -0.983 24.8-123.3-131.9 128.6 -2.9 0.2 -0.3 29 47 A b E +A 34 0A 31 -2,-0.4 5,-0.3 5,-0.2 23,-0.1 -0.571 28.1 175.1 -70.8 123.6 -5.1 -1.8 2.1 30 48 A M S S- 0 0 32 3,-2.1 -1,-0.1 -2,-0.4 4,-0.1 0.821 73.8 -29.0 -85.0 -90.7 -4.8 -5.7 1.8 31 49 A G S S- 0 0 37 2,-0.2 3,-0.1 -24,-0.1 -2,-0.1 0.892 129.1 -27.7 -94.3 -55.2 -6.9 -7.4 4.6 32 50 A N S S+ 0 0 68 1,-0.2 25,-1.6 23,-0.1 2,-0.2 0.586 125.1 49.3-131.4 -49.2 -6.9 -4.8 7.4 33 51 A a S S- 0 0 28 24,-0.2 -3,-2.1 23,-0.1 2,-0.5 -0.493 72.9-126.0 -93.5 167.8 -3.7 -2.7 7.3 34 52 A c E -A 29 0A 19 -5,-0.3 -5,-0.2 -2,-0.2 18,-0.1 -0.913 23.9-164.1-121.7 103.0 -2.1 -0.8 4.3 35 53 A K E -A 28 0A 69 -7,-0.7 -7,-1.5 -2,-0.5 2,-0.4 -0.236 31.0 -92.6 -70.4 167.3 1.6 -1.6 3.5 36 54 A V E +A 27 0A 82 -9,-0.2 2,-0.3 -2,-0.0 -9,-0.2 -0.768 48.1 172.1 -89.7 126.4 3.9 0.5 1.3 37 55 A Y E -A 26 0A 11 -11,-2.0 -11,-1.0 -2,-0.4 2,-0.4 -0.882 29.7-135.0-133.4 161.0 4.2 -0.3 -2.4 38 56 A E + 0 0 40 -2,-0.3 2,-0.2 -21,-0.1 -21,-0.0 -0.746 68.2 53.3-127.8 81.0 5.8 1.2 -5.5 39 57 A G S S- 0 0 41 -2,-0.4 2,-1.6 4,-0.1 -2,-0.1 -0.879 90.3 -81.3 171.1 167.2 3.5 1.2 -8.5 40 58 A C - 0 0 103 -2,-0.2 2,-1.7 2,-0.1 4,-0.1 -0.563 46.8-176.5 -85.1 72.0 -0.0 2.2 -9.9 41 59 A Y S S- 0 0 134 -2,-1.6 -1,-0.1 1,-0.2 -2,-0.0 -0.525 75.4 -49.5 -74.1 79.4 -1.9 -0.8 -8.4 42 60 A T S S- 0 0 138 -2,-1.7 2,-2.0 1,-0.2 -1,-0.2 0.788 92.6 -84.4 55.0 31.3 -5.4 0.0 -9.9 43 61 A G S S+ 0 0 38 2,-0.1 -1,-0.2 3,-0.0 -2,-0.2 -0.410 75.8 160.3 79.1 -63.3 -5.1 3.6 -8.5 44 62 A G - 0 0 52 -2,-2.0 2,-0.3 -4,-0.1 -16,-0.1 -0.250 52.1 -19.5 51.8-118.3 -6.3 2.9 -4.9 45 63 A Y - 0 0 86 -18,-0.4 -18,-0.8 -2,-0.1 -2,-0.1 -0.910 37.8-161.2-125.9 153.2 -5.3 5.6 -2.4 46 64 A S S S+ 0 0 85 -2,-0.3 2,-0.3 -20,-0.2 -21,-0.2 0.279 75.7 60.0-118.2 5.7 -2.6 8.3 -2.2 47 65 A R S > S- 0 0 189 -20,-0.2 4,-2.0 1,-0.1 5,-0.2 -0.998 71.5-137.0-134.0 140.8 -2.5 9.0 1.6 48 66 A M H > S+ 0 0 102 -2,-0.3 4,-1.2 1,-0.2 5,-0.1 0.836 109.0 57.9 -63.3 -31.0 -1.7 6.6 4.5 49 67 A G H > S+ 0 0 46 2,-0.2 4,-2.8 1,-0.2 -1,-0.2 0.909 106.6 47.5 -63.4 -43.3 -4.7 8.2 6.3 50 68 A E H > S+ 0 0 71 2,-0.2 4,-1.9 1,-0.2 -2,-0.2 0.932 110.2 49.6 -65.6 -48.0 -7.1 7.2 3.5 51 69 A c H < S+ 0 0 0 -4,-2.0 -1,-0.2 2,-0.2 -2,-0.2 0.763 117.9 43.5 -67.6 -21.5 -5.9 3.6 3.2 52 70 A A H >< S+ 0 0 32 -4,-1.2 3,-2.2 -5,-0.2 -2,-0.2 0.949 113.5 46.2 -78.4 -61.9 -6.3 3.3 7.0 53 71 A R H 3< S+ 0 0 182 -4,-2.8 -2,-0.2 1,-0.3 -3,-0.2 0.742 110.5 53.8 -61.5 -27.9 -9.7 5.1 7.6 54 72 A N T 3< S+ 0 0 87 -4,-1.9 -1,-0.3 -5,-0.2 -2,-0.1 0.450 111.3 56.2 -81.6 -2.8 -11.4 3.1 4.7 55 73 A b S < S- 0 0 38 -3,-2.2 -23,-0.1 -5,-0.1 -22,-0.1 -0.765 90.1-111.5-126.8 167.4 -10.3 -0.2 6.3 56 74 A P 0 0 111 0, 0.0 -23,-0.1 0, 0.0 -24,-0.1 0.568 360.0 360.0 -79.4 -8.7 -10.7 -2.0 9.7 57 75 A G 0 0 68 -25,-1.6 -24,-0.2 -5,-0.2 -5,-0.1 0.709 360.0 360.0 -98.9 360.0 -6.9 -1.6 10.6