==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=23-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER PROTEINASE INHIBITOR (TRYPSIN) 17-DEC-90 8PTI . COMPND 2 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; . AUTHOR D.HOUSSET,K.-S.KIM,J.FUCHS,C.WOODWARD,A.WLODAWER . 58 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3795.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 31 53.4 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 15.5 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 1.7 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 . 6 10.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 8.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 7 12.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 3.4 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 1 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 1 A R 0 0 169 0, 0.0 54,-0.1 0, 0.0 53,-0.1 0.000 360.0 360.0 360.0 163.6 16.6 30.3 2.9 2 2 A P > - 0 0 47 0, 0.0 3,-1.8 0, 0.0 4,-0.2 -0.088 360.0-120.7 -51.1 148.6 15.3 26.9 1.7 3 3 A D G > S+ 0 0 134 1,-0.3 3,-1.9 2,-0.2 4,-0.1 0.826 109.9 68.2 -61.4 -35.6 12.2 26.9 -0.5 4 4 A F G > S+ 0 0 48 1,-0.3 3,-1.9 2,-0.2 -1,-0.3 0.669 80.2 78.7 -63.8 -13.1 10.4 24.8 2.1 5 5 A a G < S+ 0 0 1 -3,-1.8 20,-0.3 1,-0.3 -1,-0.3 0.760 92.9 51.1 -62.7 -24.1 10.4 27.8 4.5 6 6 A L G < S+ 0 0 120 -3,-1.9 -1,-0.3 -4,-0.2 -2,-0.2 0.327 97.4 89.8 -93.3 1.9 7.5 29.1 2.4 7 7 A E S < S- 0 0 65 -3,-1.9 18,-0.2 1,-0.2 3,-0.1 -0.428 84.4 -92.6 -96.1 170.1 5.4 26.0 2.7 8 8 A P - 0 0 96 0, 0.0 35,-0.3 0, 0.0 -1,-0.2 -0.316 64.0 -65.4 -71.0 166.3 2.9 24.8 5.2 9 9 A P - 0 0 37 0, 0.0 2,-1.3 0, 0.0 35,-0.2 -0.237 56.0-115.6 -49.4 137.8 3.8 22.7 8.2 10 10 A Y - 0 0 62 33,-2.2 31,-0.2 31,-0.2 2,-0.2 -0.713 45.4-179.6 -85.5 95.0 5.0 19.3 7.0 11 11 A T - 0 0 83 -2,-1.3 25,-0.2 26,-0.0 24,-0.1 -0.465 6.1-179.5 -92.9 165.1 2.4 17.0 8.4 12 12 A G - 0 0 26 23,-2.7 2,-3.1 -2,-0.2 25,-0.1 -0.841 52.4 -64.7-146.7-172.1 2.2 13.2 8.1 13 13 A P S S+ 0 0 84 0, 0.0 2,-0.7 0, 0.0 23,-0.1 -0.267 79.8 150.9 -78.4 58.6 0.0 10.2 9.1 14 14 A b + 0 0 18 -2,-3.1 23,-0.1 21,-0.5 -2,-0.1 -0.826 28.5 171.3-105.5 111.6 1.0 11.0 12.6 15 15 A K + 0 0 187 -2,-0.7 -1,-0.2 21,-0.1 21,-0.1 0.755 50.8 106.4 -87.7 -23.7 -1.4 10.1 15.4 16 16 A A S S- 0 0 46 1,-0.1 19,-0.4 19,-0.1 21,-0.4 -0.238 73.7-131.9 -59.9 141.4 1.1 10.9 18.1 17 17 A R + 0 0 172 17,-0.1 2,-0.3 19,-0.1 -1,-0.1 -0.024 57.0 141.7 -84.6 27.6 0.5 14.2 20.0 18 18 A I - 0 0 94 1,-0.0 17,-0.6 16,-0.0 19,-0.5 -0.599 47.2-132.7 -80.3 130.7 4.1 15.3 19.7 19 19 A I E +A 34 0A 72 -2,-0.3 2,-0.3 15,-0.1 15,-0.2 -0.621 27.2 176.3 -80.7 146.7 4.6 19.0 19.0 20 20 A R E -A 33 0A 36 13,-2.4 13,-2.1 -2,-0.3 2,-0.3 -0.868 24.3-118.7-140.0 165.8 6.9 20.2 16.3 21 21 A Y E -AB 32 45A 69 24,-3.1 24,-2.7 -2,-0.3 2,-0.3 -0.777 23.4-175.8-109.0 154.8 7.8 23.7 15.0 22 22 A F E -A 31 0A 28 9,-2.3 9,-2.9 -2,-0.3 2,-0.6 -0.959 30.3-114.6-141.2 152.1 7.2 25.3 11.5 23 23 A Y E -A 30 0A 4 -2,-0.3 2,-0.9 7,-0.3 7,-0.3 -0.795 22.4-152.6 -90.7 125.2 8.2 28.7 10.1 24 24 A N E >>> -A 29 0A 40 5,-3.0 4,-2.1 -2,-0.6 5,-1.1 -0.881 7.3-167.4 -95.7 100.3 5.1 30.7 9.3 25 25 A A T 345S+ 0 0 35 -2,-0.9 -1,-0.2 -20,-0.3 -19,-0.1 0.775 83.4 60.1 -62.8 -29.2 6.4 33.0 6.4 26 26 A K T 345S+ 0 0 208 1,-0.2 -1,-0.2 -3,-0.1 -20,-0.0 0.864 117.6 28.6 -67.9 -36.5 3.3 35.1 6.7 27 27 A A T <45S- 0 0 56 -3,-0.6 -2,-0.2 2,-0.2 -1,-0.2 0.603 101.8-127.6 -97.4 -17.7 3.9 36.1 10.3 28 28 A G T <5S+ 0 0 29 -4,-2.1 2,-0.3 1,-0.3 29,-0.2 0.681 73.4 101.8 77.0 24.9 7.8 35.8 10.2 29 29 A L E + 0 0 0 -18,-0.5 3,-1.9 -25,-0.2 -17,-0.1 0.394 53.2 107.6-120.4 11.3 4.1 16.2 12.3 37 37 A G T 3 S+ 0 0 24 -19,-0.5 -1,-0.1 -21,-0.4 -20,-0.1 0.704 81.2 53.2 -59.2 -29.3 5.8 14.0 14.9 38 38 A b T 3 S+ 0 0 53 -22,-0.1 2,-0.3 -3,-0.1 -1,-0.3 0.115 104.9 64.8 -93.7 13.2 6.2 11.1 12.6 39 39 A R < - 0 0 94 -3,-1.9 -27,-0.1 -29,-0.1 -29,-0.0 -0.966 52.4-175.9-133.7 153.5 8.0 13.2 9.9 40 40 A A + 0 0 81 -2,-0.3 2,-0.3 6,-0.0 -3,-0.1 -0.251 52.3 77.8-147.8 54.3 11.3 15.0 10.0 41 41 A K S S+ 0 0 116 -31,-0.2 -31,-0.2 4,-0.0 -2,-0.0 -0.918 76.6 12.4-153.7 170.1 11.9 17.0 6.8 42 42 A R S S- 0 0 100 -2,-0.3 2,-2.3 1,-0.2 -37,-0.1 -0.184 126.1 -0.6 58.8-140.6 10.8 20.2 5.0 43 43 A N S S+ 0 0 0 -35,-0.3 -33,-2.2 -39,-0.2 2,-0.3 -0.456 107.2 101.6 -82.0 79.5 9.0 22.7 7.3 44 44 A N + 0 0 6 -2,-2.3 2,-0.3 -35,-0.2 -22,-0.2 -0.842 46.3 177.2-162.2 112.5 9.1 20.6 10.5 45 45 A F B -B 21 0A 20 -24,-2.7 -24,-3.1 -2,-0.3 3,-0.1 -0.895 35.6-135.4-129.1 153.5 11.6 21.3 13.3 46 46 A K S S+ 0 0 154 -2,-0.3 2,-0.3 -26,-0.2 -1,-0.1 0.854 90.0 15.2 -76.1 -29.0 12.4 19.9 16.7 47 47 A S S > S- 0 0 39 1,-0.1 4,-1.7 -26,-0.1 -26,-0.1 -0.896 71.8-117.2-142.3 167.6 12.8 23.3 18.3 48 48 A A H > S+ 0 0 39 -2,-0.3 4,-3.1 1,-0.2 5,-0.2 0.831 115.3 59.8 -72.1 -31.3 12.1 27.0 17.6 49 49 A E H > S+ 0 0 98 2,-0.2 4,-2.1 1,-0.2 -1,-0.2 0.927 107.2 43.6 -62.3 -48.8 15.8 27.6 17.7 50 50 A D H > S+ 0 0 77 2,-0.2 4,-1.8 1,-0.2 -1,-0.2 0.874 114.0 52.3 -58.2 -48.0 16.4 25.1 14.8 51 51 A c H X>S+ 0 0 0 -4,-1.7 4,-2.6 2,-0.2 5,-0.6 0.939 111.2 45.5 -57.9 -45.8 13.4 26.6 12.9 52 52 A M H X5S+ 0 0 83 -4,-3.1 4,-1.1 1,-0.2 -2,-0.2 0.842 111.6 51.5 -73.9 -34.0 14.6 30.2 13.2 53 53 A R H <5S+ 0 0 181 -4,-2.1 -1,-0.2 -5,-0.2 -2,-0.2 0.875 118.7 37.9 -66.9 -37.2 18.2 29.4 12.2 54 54 A T H <5S+ 0 0 44 -4,-1.8 -2,-0.2 -5,-0.2 -1,-0.2 0.879 137.2 10.0 -79.7 -46.6 17.1 27.6 9.1 55 55 A a H ><5S+ 0 0 0 -4,-2.6 3,-2.7 -5,-0.2 -3,-0.2 0.459 83.9 131.2-111.8 -15.5 14.1 29.7 7.9 56 56 A G T 3<