==== 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 2LFK . 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 4 4 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4810.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 22 38.6 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 . 9 15.8 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 . 0 0.0 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 . 5 8.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 7.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 3 5.3 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 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 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 . 1 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 0 128 0, 0.0 2,-0.4 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 172.3 5.1 -8.6 24.3 2 20 A D + 0 0 168 2,-0.0 2,-0.3 0, 0.0 0, 0.0 -0.978 360.0 144.4-135.3 117.9 7.3 -6.0 22.6 3 21 A K - 0 0 208 -2,-0.4 2,-0.2 54,-0.0 54,-0.0 -0.879 35.8-120.9-137.8 171.7 6.5 -3.9 19.4 4 22 A E - 0 0 152 -2,-0.3 2,-0.1 28,-0.1 28,-0.0 -0.723 30.9-100.2-109.9 162.7 7.1 -0.3 18.0 5 23 A E - 0 0 157 -2,-0.2 2,-0.4 1,-0.0 -1,-0.1 -0.333 20.7-136.5 -75.1 164.7 4.6 2.5 17.0 6 24 A a - 0 0 45 26,-0.1 2,-0.6 25,-0.1 25,-0.1 -0.768 18.3-167.3-127.9 81.2 3.6 3.3 13.4 7 25 A T + 0 0 108 -2,-0.4 26,-0.1 1,-0.0 25,-0.0 -0.630 12.9 170.9 -71.1 109.5 3.7 7.2 12.9 8 26 A V - 0 0 69 -2,-0.6 2,-0.1 23,-0.1 -1,-0.0 -0.804 9.4-178.2-125.7 83.7 1.9 8.0 9.6 9 27 A P > - 0 0 79 0, 0.0 3,-1.8 0, 0.0 -2,-0.0 -0.340 44.0-103.0 -75.8 167.0 1.3 11.8 9.2 10 28 A I T 3 S+ 0 0 182 1,-0.3 -2,-0.0 -2,-0.1 0, 0.0 0.787 120.4 62.3 -57.9 -28.1 -0.4 13.6 6.3 11 29 A G T 3 S+ 0 0 72 2,-0.1 -1,-0.3 0, 0.0 3,-0.0 0.355 79.3 118.2 -82.4 2.0 3.1 14.6 5.0 12 30 A W S < S- 0 0 97 -3,-1.8 2,-0.9 1,-0.1 -4,-0.1 -0.280 79.9 -95.9 -65.1 156.4 4.2 10.9 4.4 13 31 A S + 0 0 108 -2,-0.0 -1,-0.1 0, 0.0 -2,-0.1 -0.661 54.9 178.6 -77.1 99.8 5.1 9.6 0.9 14 32 A E - 0 0 123 -2,-0.9 2,-0.1 1,-0.1 16,-0.0 -0.698 27.2-107.6-103.0 155.7 1.8 7.9 -0.4 15 33 A P - 0 0 27 0, 0.0 2,-0.4 0, 0.0 -1,-0.1 -0.336 33.6-113.3 -75.8 165.5 1.0 6.2 -3.7 16 34 A V - 0 0 124 25,-0.1 2,-0.1 -2,-0.1 0, 0.0 -0.815 21.8-120.1-105.2 138.0 -1.3 7.7 -6.5 17 35 A K - 0 0 113 -2,-0.4 23,-0.2 1,-0.1 24,-0.1 -0.454 10.8-143.7 -68.6 146.4 -4.8 6.4 -7.6 18 36 A G - 0 0 44 21,-1.3 22,-0.2 -2,-0.1 -1,-0.1 0.559 20.0-144.3 -87.4 -11.1 -5.2 5.4 -11.3 19 37 A L + 0 0 149 20,-0.4 2,-0.1 1,-0.2 21,-0.1 0.747 51.2 140.3 47.3 34.3 -8.8 6.7 -11.6 20 38 A b S S- 0 0 63 2,-0.3 -1,-0.2 19,-0.1 -2,-0.1 -0.341 70.8 -96.2 -97.4 178.7 -9.7 3.7 -13.9 21 39 A K S S+ 0 0 217 -2,-0.1 2,-0.3 19,-0.0 -1,-0.0 0.371 100.0 70.9 -75.8 1.7 -12.7 1.4 -14.4 22 40 A A - 0 0 41 2,-0.0 2,-0.3 18,-0.0 -2,-0.3 -0.840 63.1-150.9-123.8 158.4 -11.1 -1.4 -12.2 23 41 A R + 0 0 217 -2,-0.3 2,-0.0 16,-0.2 -2,-0.0 -0.759 22.5 176.9-134.7 83.7 -10.3 -1.9 -8.4 24 42 A F - 0 0 99 -2,-0.3 15,-0.8 1,-0.0 2,-0.5 -0.246 29.0-118.9 -73.0 171.8 -7.3 -4.1 -7.8 25 43 A T E +A 38 0A 66 13,-0.2 2,-0.3 21,-0.1 13,-0.2 -0.971 38.9 164.9-122.1 112.8 -5.8 -4.9 -4.3 26 44 A R E -A 37 0A 62 11,-2.8 11,-2.9 -2,-0.5 2,-0.4 -0.791 23.9-139.3-119.8 167.4 -2.2 -3.8 -3.5 27 45 A Y E +AB 36 45A 49 18,-2.5 18,-2.1 16,-0.3 2,-0.3 -0.984 19.0 176.3-133.4 140.1 -0.1 -3.5 -0.3 28 46 A Y E -A 35 0A 40 7,-2.5 7,-2.9 -2,-0.4 2,-0.4 -0.865 26.7-117.2-133.4 165.9 2.4 -0.7 0.7 29 47 A c E -A 34 0A 32 -2,-0.3 2,-0.5 5,-0.2 5,-0.2 -0.923 15.1-165.0-112.7 138.8 4.6 0.1 3.8 30 48 A M E > -A 33 0A 20 3,-2.9 2,-1.8 -2,-0.4 3,-1.3 -0.858 65.9 -62.2-125.7 86.2 4.2 3.3 5.9 31 49 A G T 3 S- 0 0 27 -2,-0.5 -25,-0.1 1,-0.2 -23,-0.1 -0.498 125.0 -8.6 73.4 -77.3 7.2 3.7 8.1 32 50 A N T 3 S+ 0 0 55 -2,-1.8 2,-0.4 23,-0.1 -1,-0.2 0.396 124.0 68.5-131.6 -4.4 6.9 0.5 10.3 33 51 A a E < S-A 30 0A 52 -3,-1.3 -3,-2.9 23,-0.1 2,-0.2 -0.960 71.3-128.2-123.8 139.4 3.4 -0.9 9.3 34 52 A d E -A 29 0A 22 23,-0.7 2,-0.3 -2,-0.4 -5,-0.2 -0.582 27.8-169.4 -79.1 147.5 2.1 -2.5 6.1 35 53 A K E -A 28 0A 107 -7,-2.9 -7,-2.5 -2,-0.2 2,-0.2 -0.996 17.8-125.8-147.0 127.0 -1.2 -1.0 4.7 36 54 A V E -A 27 0A 49 -2,-0.3 2,-0.3 -9,-0.2 -9,-0.3 -0.504 20.8-162.0 -74.4 145.2 -3.6 -2.2 1.9 37 55 A Y E -A 26 0A 41 -11,-2.9 -11,-2.8 -2,-0.2 2,-0.4 -0.993 6.0-173.7-131.7 137.1 -4.6 0.1 -1.1 38 56 A E E +A 25 0A 126 -2,-0.3 -13,-0.2 -13,-0.2 -15,-0.1 -0.986 46.9 76.8-138.5 117.5 -7.6 -0.4 -3.4 39 57 A G S S- 0 0 14 -15,-0.8 -21,-1.3 -2,-0.4 -20,-0.4 0.433 110.4 -52.8 139.6 65.7 -8.4 1.7 -6.6 40 58 A b S S+ 0 0 20 -23,-0.2 -17,-0.1 -22,-0.2 -15,-0.1 0.760 89.3 135.2 56.9 28.7 -6.4 1.1 -9.8 41 59 A Y + 0 0 43 -17,-0.2 2,-1.1 1,-0.1 -25,-0.1 0.910 24.7 173.1 -72.4 -46.4 -3.0 1.5 -7.9 42 60 A T + 0 0 87 1,-0.1 -1,-0.1 4,-0.0 -25,-0.1 0.118 49.0 93.9 50.8 -10.3 -1.1 -1.6 -9.5 43 61 A G + 0 0 30 -2,-1.1 -16,-0.3 -17,-0.0 -1,-0.1 -0.058 61.7 40.8 -86.6-171.4 2.2 -0.6 -7.7 44 62 A G S S- 0 0 41 -18,-0.1 -16,-0.2 -3,-0.1 2,-0.1 -0.043 104.7 -19.4 64.1-168.8 3.7 -1.7 -4.4 45 63 A Y B -B 27 0A 76 -18,-2.1 -18,-2.5 1,-0.1 3,-0.1 -0.382 52.8-136.4 -67.3 146.8 3.7 -5.3 -3.0 46 64 A S S S+ 0 0 62 -20,-0.2 2,-0.3 1,-0.1 -1,-0.1 0.823 84.2 14.6 -75.4 -32.8 1.1 -7.9 -4.5 47 65 A R S >> S- 0 0 176 -20,-0.1 4,-1.5 1,-0.1 3,-1.1 -0.935 77.7-109.0-136.8 163.1 0.2 -9.3 -1.0 48 66 A M H 3> S+ 0 0 85 -2,-0.3 4,-3.0 1,-0.2 5,-0.2 0.880 119.4 58.9 -56.5 -38.5 0.5 -8.5 2.7 49 67 A G H 34 S+ 0 0 41 1,-0.2 4,-0.4 2,-0.2 -1,-0.2 0.657 103.0 51.5 -71.1 -17.4 3.1 -11.4 3.0 50 68 A E H <4 S+ 0 0 74 -3,-1.1 4,-0.3 2,-0.1 -1,-0.2 0.804 115.2 42.6 -82.9 -33.6 5.3 -9.7 0.3 51 69 A d H >X S+ 0 0 0 -4,-1.5 4,-2.6 1,-0.2 3,-1.7 0.960 111.9 52.5 -69.3 -53.4 5.2 -6.4 2.4 52 70 A A T 3< S+ 0 0 41 -4,-3.0 -3,-0.2 1,-0.3 -1,-0.2 0.631 101.8 59.7 -67.3 -17.9 5.7 -8.0 5.9 53 71 A R T 34 S+ 0 0 174 -4,-0.4 -1,-0.3 -5,-0.2 -2,-0.1 0.662 118.1 30.8 -78.9 -18.4 8.8 -10.0 4.8 54 72 A N T <4 S+ 0 0 114 -3,-1.7 -2,-0.2 -4,-0.3 -3,-0.1 0.806 113.5 60.9-106.9 -51.7 10.7 -6.7 4.0 55 73 A c S < S- 0 0 27 -4,-2.6 -23,-0.1 2,-0.1 -21,-0.1 -0.404 89.5-116.6 -73.8 159.0 9.2 -4.1 6.4 56 74 A P 0 0 91 0, 0.0 -23,-0.1 0, 0.0 -1,-0.1 0.610 360.0 360.0 -78.4 -12.9 9.6 -4.7 10.2 57 75 A G 0 0 76 -25,-0.2 -23,-0.7 -6,-0.1 -2,-0.1 -0.889 360.0 360.0-108.5 360.0 5.8 -5.1 11.0