==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=6-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE INHIBITOR 29-OCT-01 1K9B . COMPND 2 MOLECULE: BOWMAN-BIRK TYPE PROTEINASE INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX; . AUTHOR R.H.VOSS,U.ERMLER,L.O.ESSEN,G.WENZL,Y.M.KIM,P.FLECKER . 58 1 7 7 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4326.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 32 55.2 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 . 14 24.1 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 . 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 . 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 . 12 20.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 1.7 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 0 2 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 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 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 6 A K 0 0 119 0, 0.0 2,-0.6 0, 0.0 28,-0.4 0.000 360.0 360.0 360.0 129.4 30.7 89.5 19.6 2 7 A P + 0 0 43 0, 0.0 53,-0.4 0, 0.0 2,-0.3 -0.951 360.0 165.6 -93.1 122.4 33.2 88.8 22.3 3 8 A a - 0 0 20 -2,-0.6 2,-0.2 51,-0.2 54,-0.2 -0.768 20.8-157.9-123.0 175.0 36.7 88.5 21.0 4 9 A b - 0 0 3 51,-2.7 3,-0.1 -2,-0.3 16,-0.0 -0.801 13.1-177.8-159.3 117.5 40.2 88.5 22.6 5 10 A D S S+ 0 0 100 -2,-0.2 2,-0.7 1,-0.2 -1,-0.1 0.841 83.3 46.8 -78.4 -50.8 43.6 89.3 21.0 6 11 A Q S S+ 0 0 120 2,-0.0 14,-1.3 50,-0.0 15,-0.7 -0.915 76.1 175.3 -96.4 109.1 45.7 88.6 24.0 7 12 A c E -A 19 0A 52 -2,-0.7 2,-0.4 12,-0.2 12,-0.2 -0.890 11.8-168.2-117.5 149.7 44.8 85.4 25.7 8 13 A A E +A 18 0A 40 10,-2.3 10,-1.7 -2,-0.4 2,-0.3 -0.995 6.9 177.0-136.9 138.8 46.3 83.5 28.6 9 14 A d E -A 17 0A 62 -2,-0.4 8,-0.2 8,-0.3 42,-0.0 -0.958 26.6-124.8-147.8 131.9 45.8 80.0 29.9 10 15 A T - 0 0 62 6,-2.2 2,-1.0 -2,-0.3 6,-0.1 -0.276 36.3-109.1 -69.0 146.7 47.2 77.9 32.7 11 16 A K S S+ 0 0 209 4,-0.1 2,-0.3 2,-0.0 -1,-0.1 -0.645 79.6 97.4 -78.3 101.4 48.6 74.5 31.7 12 17 A S S S- 0 0 52 -2,-1.0 -2,-0.0 -3,-0.0 0, 0.0 -0.887 77.8 -73.7-179.0 152.7 46.0 72.3 33.2 13 18 A N S S+ 0 0 169 -2,-0.3 -2,-0.0 2,-0.1 3,-0.0 -0.906 124.1 15.5-105.4 117.8 42.8 70.3 32.5 14 19 A P S S- 0 0 83 0, 0.0 2,-0.3 0, 0.0 38,-0.1 0.768 101.0-139.3 -81.4 171.4 40.7 72.2 32.2 15 20 A P - 0 0 38 0, 0.0 2,-0.5 0, 0.0 -4,-0.1 -0.663 2.2-137.4 -93.8 148.2 42.6 75.4 31.8 16 21 A Q - 0 0 95 -2,-0.3 -6,-2.2 -6,-0.1 2,-0.4 -0.949 28.3-171.4-100.7 124.9 41.7 78.7 33.3 17 22 A d E -A 9 0A 2 33,-2.2 2,-0.3 -2,-0.5 -8,-0.3 -0.980 10.6-170.2-122.1 135.6 42.1 81.4 30.8 18 23 A R E -A 8 0A 156 -10,-1.7 -10,-2.3 -2,-0.4 2,-0.6 -0.787 21.8-128.0-116.2 157.9 42.0 85.2 31.2 19 24 A b E -AB 7 46A 16 27,-0.7 27,-0.6 29,-0.5 -12,-0.2 -0.902 17.8-171.3-112.5 115.1 41.9 87.8 28.5 20 25 A S E + 0 0 50 -14,-1.3 -13,-0.1 -2,-0.6 -1,-0.1 0.475 44.6 114.6 -81.1 -9.6 44.5 90.6 28.9 21 26 A D E - 0 0 25 -15,-0.7 25,-0.5 25,-0.1 2,-0.5 -0.385 57.1-137.3 -77.4 156.2 43.5 93.0 26.2 22 27 A M E - B 0 45A 69 23,-0.1 23,-0.2 5,-0.1 2,-0.2 -0.943 19.4-175.7-128.2 116.5 42.3 96.4 27.3 23 28 A R E - B 0 44A 84 21,-2.4 21,-3.8 -2,-0.5 2,-0.4 -0.654 28.5-105.7-105.8 167.3 39.3 98.4 26.0 24 29 A L E S- B 0 43A 102 19,-0.2 2,-0.5 -2,-0.2 19,-0.2 -0.786 88.7 -9.0 -97.2 132.5 38.0 101.9 26.8 25 30 A N S S+ 0 0 94 17,-2.3 2,-0.3 -2,-0.4 -1,-0.1 -0.007 125.7 16.4 79.8 -33.6 34.8 102.6 28.9 26 31 A S - 0 0 72 -2,-0.5 18,-0.1 16,-0.2 -2,-0.1 -0.908 69.6-109.1-165.1 157.0 33.7 99.0 29.1 27 32 A e - 0 0 20 -2,-0.3 4,-0.1 18,-0.2 7,-0.1 -0.183 55.0 -76.9 -71.9 166.3 34.4 95.3 28.7 28 33 A H > - 0 0 18 -25,-0.1 3,-1.7 2,-0.1 -1,-0.1 -0.048 52.2 -91.3 -65.3 174.6 33.0 93.1 25.9 29 34 A S T 3 S+ 0 0 110 -28,-0.4 -1,-0.1 1,-0.3 -2,-0.1 0.802 121.2 45.0 -64.4 -31.1 29.4 91.8 25.8 30 35 A A T 3 S+ 0 0 41 -29,-0.0 2,-0.6 2,-0.0 -1,-0.3 -0.113 81.7 120.2-106.2 34.9 30.0 88.5 27.6 31 36 A f < - 0 0 22 -3,-1.7 3,-0.2 1,-0.2 -4,-0.1 -0.902 37.1-175.2-103.5 117.3 32.2 89.8 30.4 32 37 A K S S+ 0 0 192 -2,-0.6 2,-0.6 1,-0.2 -1,-0.2 0.983 77.4 35.4 -66.3 -65.8 30.9 89.2 33.9 33 38 A S S S+ 0 0 64 2,-0.0 14,-1.5 0, 0.0 15,-0.7 -0.855 71.5 179.2-100.3 117.1 33.6 91.0 36.0 34 39 A e E -C 46 0A 54 -2,-0.6 2,-0.5 12,-0.2 12,-0.2 -0.960 8.3-164.8-121.8 124.0 34.9 94.1 34.3 35 40 A I E -C 45 0A 99 10,-2.8 10,-2.1 -2,-0.4 2,-0.3 -0.948 12.6-178.5-124.6 112.6 37.6 96.2 36.1 36 41 A g E -C 44 0A 52 -2,-0.5 8,-0.3 8,-0.2 -12,-0.1 -0.877 33.5-102.6-115.3 149.5 38.3 99.7 34.8 37 42 A A - 0 0 42 6,-2.7 2,-1.9 -2,-0.3 -12,-0.1 -0.278 39.9-118.0 -60.0 131.1 40.6 102.6 35.7 38 43 A L S S+ 0 0 186 4,-0.1 2,-0.2 2,-0.1 -1,-0.1 -0.632 82.0 86.8 -73.1 81.2 38.7 105.2 37.6 39 44 A S S S- 0 0 67 -2,-1.9 4,-0.1 4,-0.0 -2,-0.1 -0.812 83.1 -70.8-174.2 150.5 39.2 108.0 35.0 40 45 A Y S S+ 0 0 221 -2,-0.2 2,-0.1 2,-0.1 -2,-0.1 -0.727 120.9 21.8 -97.4 130.0 37.7 109.4 31.8 41 46 A P S S- 0 0 73 0, 0.0 2,-0.3 0, 0.0 -1,-0.1 0.710 103.5-139.3 -72.8 163.4 38.0 107.6 29.4 42 47 A A - 0 0 16 -2,-0.1 -17,-2.3 -6,-0.0 2,-0.8 -0.613 7.5-133.0-106.8 142.7 38.5 104.4 31.3 43 48 A Q E -B 24 0A 103 -2,-0.3 -6,-2.7 -19,-0.2 2,-0.5 -0.784 31.3-169.3 -93.6 108.1 40.8 101.5 30.8 44 49 A g E +BC 23 36A 0 -21,-3.8 -21,-2.4 -2,-0.8 2,-0.3 -0.930 11.8 179.6-105.5 126.9 38.8 98.4 31.2 45 50 A F E -BC 22 35A 95 -10,-2.1 -10,-2.8 -2,-0.5 2,-0.6 -0.935 27.7-127.8-106.3 160.1 40.1 94.8 31.4 46 51 A f E -BC 19 34A 14 -27,-0.6 -27,-0.7 -25,-0.5 -12,-0.2 -0.867 18.1-170.1-111.0 115.0 37.9 91.8 31.8 47 52 A V + 0 0 69 -14,-1.5 -13,-0.1 -2,-0.6 -1,-0.1 0.509 39.6 130.5 -89.9 1.4 39.1 89.7 34.7 48 53 A D - 0 0 27 -15,-0.7 -29,-0.5 1,-0.1 -2,-0.1 -0.090 48.7-150.0 -50.3 146.3 36.9 86.7 34.0 49 54 A I + 0 0 54 -31,-0.1 -32,-0.4 -33,-0.0 -31,-0.2 -0.254 26.5 172.9-119.6 52.2 38.8 83.4 34.0 50 55 A T - 0 0 51 -34,-0.2 -33,-2.2 1,-0.1 2,-0.3 -0.085 40.7-117.0 -58.3 155.8 36.9 81.2 31.5 51 56 A D S S+ 0 0 90 -35,-0.2 2,-0.3 -42,-0.0 -1,-0.1 0.022 92.2 42.2 -94.9 37.2 38.2 77.8 30.4 52 57 A F S S- 0 0 102 -2,-0.3 2,-0.4 -35,-0.2 -35,-0.1 -0.949 82.4-112.5-166.7 153.3 38.8 78.6 26.7 53 58 A c - 0 0 55 -2,-0.3 -49,-0.1 -46,-0.1 -46,-0.1 -0.748 25.3-129.4 -92.8 138.9 40.1 81.6 24.7 54 59 A Y - 0 0 63 -2,-0.4 -51,-0.2 1,-0.1 -1,-0.1 -0.192 36.1 -98.0 -68.5 172.8 37.9 83.7 22.5 55 60 A E - 0 0 66 -53,-0.4 -51,-2.7 1,-0.2 -1,-0.1 -0.605 43.5 -91.5 -91.5 158.8 39.2 84.3 19.0 56 61 A P - 0 0 97 0, 0.0 -1,-0.2 0, 0.0 2,-0.2 0.288 50.1-115.5 -44.2-172.0 41.0 87.5 17.9 57 62 A a 0 0 49 -54,-0.2 0, 0.0 1,-0.0 0, 0.0 -0.620 360.0 360.0-126.9-177.4 39.1 90.5 16.5 58 63 A K 0 0 177 -2,-0.2 -1,-0.0 0, 0.0 -55,-0.0 -0.233 360.0 360.0 82.1 360.0 38.3 92.9 13.6