==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=20-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE INHIBITOR 18-NOV-04 1Y1B . COMPND 2 MOLECULE: ELASTASE INHIBITOR; . SOURCE 2 SYNTHETIC: YES; . AUTHOR H.HEMMI,T.KUMAZAKI,K.YOSHIZAWA-KUMAGAYE,Y.NISHIUCHI, . 48 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3707.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 30 62.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 4.2 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 9 18.8 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 . 1 2.1 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-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 2.1 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 . 6 12.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 8.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 9 18.8 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 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 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 PARALLEL BRIDGES PER LADDER . 0 0 2 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 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 K 0 0 173 0, 0.0 40,-0.1 0, 0.0 33,-0.0 0.000 360.0 360.0 360.0 142.9 2.2 11.8 4.6 2 2 A P - 0 0 46 0, 0.0 2,-0.2 0, 0.0 39,-0.0 0.364 360.0-118.0 -52.2-164.5 4.1 8.6 5.5 3 3 A D - 0 0 107 32,-0.0 31,-0.3 1,-0.0 30,-0.2 -0.537 25.0 -84.8-128.5-166.3 7.5 7.7 4.1 4 4 A a - 0 0 64 -2,-0.2 27,-0.2 29,-0.1 24,-0.1 -0.735 32.8-137.6-108.0 157.6 9.2 5.0 1.9 5 5 A P - 0 0 42 0, 0.0 -1,-0.1 0, 0.0 3,-0.0 -0.089 21.7-110.2 -95.9-163.2 10.6 1.6 2.9 6 6 A L S S- 0 0 167 1,-0.1 21,-0.0 -2,-0.1 -2,-0.0 -0.441 76.7 -59.0-132.1 58.5 13.7 -0.3 1.9 7 7 A I - 0 0 164 20,-0.1 -1,-0.1 2,-0.0 21,-0.0 0.896 59.7-170.5 65.1 102.6 12.5 -3.2 -0.2 8 8 A b - 0 0 74 1,-0.2 2,-0.3 17,-0.1 17,-0.0 0.924 36.4 -77.3 -86.4 -84.3 10.1 -5.4 1.6 9 9 A T - 0 0 74 1,-0.0 -1,-0.2 2,-0.0 4,-0.1 -0.978 17.4-111.9-169.5 179.0 9.2 -8.6 -0.2 10 10 A M S S+ 0 0 169 -2,-0.3 2,-2.9 2,-0.1 -1,-0.0 0.203 70.5 123.1-110.6 11.7 7.3 -10.4 -2.9 11 11 A Q S S- 0 0 129 1,-0.1 -1,-0.1 2,-0.1 -2,-0.0 -0.413 76.0-123.6 -74.7 67.6 5.1 -12.3 -0.5 12 12 A Y + 0 0 184 -2,-2.9 13,-0.2 1,-0.2 -1,-0.1 0.250 46.2 166.1 -18.1 96.3 2.0 -10.8 -2.1 13 13 A D B -a 25 0A 85 11,-2.0 13,-0.6 -4,-0.1 -1,-0.2 -0.522 21.4-161.3-120.8 58.9 0.3 -9.2 0.9 14 14 A P - 0 0 30 0, 0.0 2,-0.4 0, 0.0 10,-0.2 -0.205 11.5-176.2 -48.8 115.5 -2.2 -7.0 -1.0 15 15 A V E -B 23 0B 6 8,-2.2 8,-2.4 30,-0.2 2,-0.6 -0.966 26.0-125.7-122.0 133.6 -3.4 -4.3 1.3 16 16 A c E -BC 22 44B 4 28,-2.3 27,-2.6 -2,-0.4 28,-1.7 -0.648 30.3-156.7 -79.0 119.4 -6.0 -1.7 0.5 17 17 A G E >> -BC 21 42B 2 4,-2.8 3,-2.3 -2,-0.6 4,-1.4 -0.840 31.3 -95.0-106.1 139.6 -4.7 1.7 1.1 18 18 A S E 34 S+ C 0 41B 64 23,-0.8 23,-0.8 -2,-0.4 -1,-0.1 -0.250 113.7 61.2 -49.7 94.8 -6.7 4.9 1.8 19 19 A D T 34 S- 0 0 92 -2,-0.7 -1,-0.3 21,-0.2 23,-0.1 0.018 121.2 -86.9 170.5 -29.4 -6.9 6.1 -1.8 20 20 A G T <4 S+ 0 0 63 -3,-2.3 2,-0.4 1,-0.3 -2,-0.1 0.723 87.8 116.6 108.0 33.6 -8.7 3.3 -3.4 21 21 A I E < -B 17 0B 86 -4,-1.4 -4,-2.8 -6,-0.0 2,-0.9 -0.995 57.9-139.2-139.0 141.6 -5.9 0.9 -4.4 22 22 A T E -B 16 0B 73 -2,-0.4 2,-0.3 -6,-0.2 -6,-0.3 -0.815 30.2-157.2 -96.9 99.0 -4.9 -2.6 -3.5 23 23 A Y E -B 15 0B 28 -8,-2.4 -8,-2.2 -2,-0.9 3,-0.1 -0.587 28.1-116.8 -82.3 138.9 -1.1 -2.5 -3.1 24 24 A G S S- 0 0 14 -2,-0.3 -11,-2.0 -10,-0.2 2,-0.3 0.765 98.3 -12.8 -40.7 -29.3 1.0 -5.6 -3.5 25 25 A N B >> -a 13 0A 13 -13,-0.2 4,-1.1 -10,-0.2 3,-0.8 -0.918 68.3-107.0-173.9 147.0 1.9 -4.9 0.1 26 26 A A H 3> S+ 0 0 40 -13,-0.6 4,-1.5 1,-0.3 -2,-0.1 0.769 122.3 56.9 -49.6 -26.2 1.6 -2.2 2.7 27 27 A b H 3> S+ 0 0 28 1,-0.2 4,-1.4 2,-0.2 -1,-0.3 0.917 98.9 55.4 -72.7 -43.4 5.4 -1.8 2.1 28 28 A M H <> S+ 0 0 117 -3,-0.8 4,-0.9 1,-0.2 -1,-0.2 0.719 105.3 58.9 -61.5 -17.6 4.9 -1.1 -1.5 29 29 A L H >X>S+ 0 0 4 -4,-1.1 4,-2.9 2,-0.2 3,-0.7 0.942 94.5 57.7 -76.6 -50.5 2.6 1.6 -0.3 30 30 A L H 3X5S+ 0 0 58 -4,-1.5 4,-1.1 1,-0.3 -2,-0.2 0.867 108.8 50.2 -48.6 -34.7 5.2 3.5 1.7 31 31 A G H 3X5S+ 0 0 20 -4,-1.4 4,-0.9 2,-0.2 -1,-0.3 0.863 114.1 45.2 -70.6 -34.0 7.0 3.7 -1.5 32 32 A A H XX5S+ 0 0 17 -4,-0.9 3,-1.9 -3,-0.7 4,-0.5 0.984 110.2 49.1 -71.3 -61.7 3.9 4.9 -3.1 33 33 A S H 3<5S+ 0 0 5 -4,-2.9 3,-0.3 1,-0.3 -1,-0.2 0.800 110.5 57.1 -48.8 -28.5 2.8 7.5 -0.5 34 34 A a H 3<