==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=19-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE INHIBITOR 12-AUG-04 1WO9 . COMPND 2 MOLECULE: TRYPSIN INHIBITOR; . SOURCE 2 SYNTHETIC: YES; . AUTHOR C.KELLENBERGER,G.FERRAT,P.LEONE,H.DARBON,A.ROUSSEL . 35 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3092.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 19 54.3 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 . 8 22.9 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 . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 1 2.9 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 . 9 25.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 8.6 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+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 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 . 0 1 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 . 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 1 A A 0 0 167 0, 0.0 2,-0.2 0, 0.0 4,-0.0 0.000 360.0 360.0 360.0 -28.3 15.0 -11.2 7.0 2 2 A G - 0 0 57 1,-0.1 21,-0.1 2,-0.1 3,-0.0 -0.774 360.0 -95.3-135.6-179.4 13.5 -8.1 5.5 3 3 A E S S+ 0 0 171 -2,-0.2 2,-0.3 19,-0.2 21,-0.1 0.905 103.4 4.9 -65.2 -43.4 11.6 -5.0 6.4 4 4 A a - 0 0 15 16,-0.2 -1,-0.1 -3,-0.0 -2,-0.1 -0.850 69.9-117.0-137.5 173.8 8.2 -6.6 5.6 5 5 A T > - 0 0 87 -2,-0.3 2,-3.2 18,-0.1 3,-1.4 -0.950 32.7-115.3-116.1 130.5 6.5 -9.8 4.6 6 6 A P T 3 S+ 0 0 74 0, 0.0 14,-0.1 0, 0.0 3,-0.1 -0.316 105.1 62.1 -66.5 71.9 4.7 -10.2 1.2 7 7 A G T 3 S+ 0 0 60 -2,-3.2 2,-0.5 1,-0.2 13,-0.1 0.291 74.8 97.8-171.9 2.4 1.4 -10.8 2.9 8 8 A Q < - 0 0 93 -3,-1.4 11,-2.7 12,-0.0 2,-0.4 -0.929 48.6-163.4-113.7 126.8 0.5 -7.6 4.8 9 9 A T E -A 18 0A 99 -2,-0.5 2,-0.3 9,-0.3 9,-0.3 -0.826 6.7-159.1-104.4 142.3 -1.8 -4.9 3.5 10 10 A K E -A 17 0A 70 7,-2.3 7,-2.3 -2,-0.4 2,-0.8 -0.922 15.9-130.1-122.8 148.3 -1.9 -1.4 5.0 11 11 A K E +A 16 0A 161 -2,-0.3 2,-0.6 5,-0.2 5,-0.2 -0.835 28.2 177.0-101.1 104.7 -4.6 1.3 4.8 12 12 A Q E > -A 15 0A 105 3,-0.9 3,-1.1 -2,-0.8 2,-0.8 -0.928 65.2 -42.2-110.5 113.9 -3.1 4.6 3.8 13 13 A D T 3 S- 0 0 117 -2,-0.6 16,-0.1 1,-0.3 -2,-0.0 -0.576 119.5 -36.0 71.4-106.2 -5.6 7.4 3.4 14 14 A b T 3 S+ 0 0 73 -2,-0.8 -1,-0.3 15,-0.2 18,-0.1 0.567 123.4 79.2-120.4 -23.7 -8.5 5.7 1.6 15 15 A N E < S-A 12 0A 15 -3,-1.1 -3,-0.9 13,-0.2 2,-0.3 -0.203 75.0-119.1 -80.6 175.0 -6.5 3.3 -0.7 16 16 A T E -A 11 0A 89 -5,-0.2 12,-0.5 -2,-0.0 2,-0.3 -0.876 21.8-168.0-119.0 149.7 -4.9 0.0 0.2 17 17 A c E -A 10 0A 2 -7,-2.3 -7,-2.3 -2,-0.3 2,-0.3 -0.938 6.4-151.1-132.3 155.5 -1.2 -1.0 -0.0 18 18 A T E -AB 9 26A 80 8,-0.8 8,-1.2 -2,-0.3 -9,-0.3 -0.962 23.7-111.2-128.0 151.4 0.5 -4.4 0.2 19 19 A a E - B 0 25A 7 -11,-2.7 6,-0.2 -2,-0.3 -11,-0.0 -0.509 37.3-130.9 -72.6 146.3 3.9 -5.4 1.4 20 20 A T > - 0 0 41 4,-1.4 2,-2.3 -2,-0.1 3,-1.7 -0.703 18.2-113.2 -98.1 153.0 6.1 -6.6 -1.5 21 21 A P T 3 S+ 0 0 102 0, 0.0 -1,-0.1 0, 0.0 -16,-0.1 -0.173 112.0 59.7 -75.2 47.7 8.1 -9.9 -1.4 22 22 A T T 3 S- 0 0 118 -2,-2.3 -19,-0.2 2,-0.1 3,-0.1 0.395 120.0 -93.7-146.8 -16.3 11.3 -7.8 -1.5 23 23 A G S < S+ 0 0 15 -3,-1.7 2,-0.6 1,-0.3 -20,-0.1 0.478 85.5 120.0 107.9 6.1 11.1 -5.7 1.6 24 24 A I - 0 0 94 -4,-0.2 -4,-1.4 -21,-0.1 2,-0.7 -0.913 51.5-150.2-112.0 119.7 9.5 -2.6 0.2 25 25 A W E +B 19 0A 81 -2,-0.6 2,-0.3 -6,-0.2 -6,-0.2 -0.782 28.6 177.4 -87.4 113.9 6.2 -1.4 1.6 26 26 A G E -B 18 0A 35 -8,-1.2 -8,-0.8 -2,-0.7 2,-0.2 -0.841 14.5-176.5-124.3 161.6 4.3 0.3 -1.2 27 27 A c - 0 0 62 -2,-0.3 -10,-0.2 -10,-0.2 2,-0.2 -0.861 19.8-119.8-142.6 175.6 0.9 2.0 -1.9 28 28 A T - 0 0 83 -12,-0.5 -13,-0.2 -2,-0.2 3,-0.1 -0.487 8.7-155.2-111.4-178.9 -1.2 3.7 -4.6 29 29 A R + 0 0 198 -2,-0.2 -15,-0.2 1,-0.1 -14,-0.1 0.683 62.5 72.4-124.7 -53.8 -2.7 7.2 -4.8 30 30 A K S S+ 0 0 165 2,-0.1 2,-0.3 -15,-0.0 -1,-0.1 -0.368 71.0 58.0 -73.4 152.2 -5.8 7.5 -7.0 31 31 A A S S+ 0 0 48 4,-0.2 4,-0.3 2,-0.2 -16,-0.1 -0.852 73.6 53.6 128.9-161.6 -9.3 6.1 -6.1 32 32 A b S S+ 0 0 71 -2,-0.3 -2,-0.1 -18,-0.1 -1,-0.0 -0.085 83.6 81.4 38.8-106.0 -11.8 6.6 -3.3 33 33 A R S S- 0 0 136 1,-0.2 2,-3.1 -3,-0.0 -2,-0.2 0.181 117.3 -23.6 -28.2 140.1 -12.4 10.4 -3.1 34 34 A T 0 0 149 0, 0.0 -1,-0.2 0, 0.0 -2,-0.1 -0.176 360.0 360.0 49.9 -67.5 -14.9 11.8 -5.7 35 35 A T 0 0 152 -2,-3.1 -4,-0.2 -4,-0.3 0, 0.0 -0.639 360.0 360.0-172.3 360.0 -14.3 8.8 -8.1