==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=4-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SERINE PROTEASE INHIBITOR 27-MAR-92 1HPT . COMPND 2 MOLECULE: PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR H.J.HECHT,M.SZARDENINGS,J.COLLINS,D.SCHOMBURG . 56 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4141.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 28 50.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 3.6 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 10 17.9 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 1.8 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-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 . 3 5.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 5.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 9 16.1 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+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 1 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 . 1 1 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 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 1 A D 0 0 200 0, 0.0 2,-0.3 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0-137.8 19.8 20.8 27.7 2 2 A S - 0 0 81 1,-0.0 3,-0.1 47,-0.0 0, 0.0 -0.942 360.0-152.4-124.8 150.4 16.7 19.0 26.2 3 3 A L S S- 0 0 140 -2,-0.3 2,-0.3 2,-0.0 46,-0.0 -0.088 79.0 -18.3-106.6 29.4 13.0 20.0 26.5 4 4 A G S S- 0 0 32 22,-0.0 2,-0.3 21,-0.0 47,-0.2 -0.984 84.1 -62.8 164.3-161.9 11.7 16.5 26.2 5 5 A R B -A 50 0A 109 45,-2.1 45,-2.8 -2,-0.3 2,-0.1 -0.773 48.0 -89.4-121.3 159.1 12.7 12.9 25.1 6 6 A E - 0 0 127 -2,-0.3 2,-0.5 43,-0.2 43,-0.1 -0.410 39.4-122.6 -68.3 135.5 13.7 11.1 21.9 7 7 A A - 0 0 3 41,-0.4 2,-0.2 -2,-0.1 -1,-0.1 -0.703 28.5-146.5 -82.7 127.2 10.9 9.7 19.8 8 8 A K - 0 0 92 -2,-0.5 30,-0.4 1,-0.1 31,-0.2 -0.603 15.8-148.3 -97.1 148.5 11.3 5.9 19.3 9 9 A a > - 0 0 8 -2,-0.2 3,-2.3 29,-0.1 -1,-0.1 0.294 33.1-133.5 -98.0 4.3 10.4 3.9 16.3 10 10 A Y T 3 - 0 0 142 1,-0.3 3,-0.1 6,-0.0 25,-0.0 0.739 64.0 -62.1 51.9 34.2 9.6 0.7 18.4 11 11 A N T 3 S+ 0 0 166 1,-0.2 2,-0.5 2,-0.1 -1,-0.3 0.644 87.1 163.0 63.2 22.1 11.6 -1.6 16.0 12 12 A E < - 0 0 71 -3,-2.3 -1,-0.2 1,-0.2 4,-0.1 -0.560 23.9-162.8 -73.6 120.2 9.2 -0.7 13.2 13 13 A L S S- 0 0 141 -2,-0.5 -1,-0.2 2,-0.1 3,-0.1 0.989 75.7 -1.0 -67.0 -65.8 10.9 -1.7 9.9 14 14 A N S S- 0 0 152 1,-0.3 2,-0.3 0, 0.0 -2,-0.1 0.805 123.1 -19.8-103.5 -30.9 9.0 0.1 7.3 15 15 A G - 0 0 32 -6,-0.1 -1,-0.3 0, 0.0 2,-0.2 -0.968 63.4 -89.8-166.3 178.0 6.2 2.1 8.9 16 16 A b - 0 0 30 -2,-0.3 2,-0.1 1,-0.1 -6,-0.0 -0.509 34.8-110.9 -99.0 162.2 4.1 2.6 11.8 17 17 A T - 0 0 76 -2,-0.2 -1,-0.1 1,-0.1 19,-0.1 -0.335 31.5-112.9 -80.0 172.8 0.7 1.3 12.7 18 18 A Y + 0 0 232 -2,-0.1 2,-0.4 2,-0.1 -1,-0.1 -0.145 63.8 146.6 -99.9 38.8 -2.3 3.6 12.8 19 19 A E - 0 0 93 2,-0.1 2,-0.9 1,-0.1 -2,-0.0 -0.653 47.4-136.5 -73.3 130.7 -2.5 3.3 16.5 20 20 A Y + 0 0 164 -2,-0.4 13,-0.2 13,-0.1 -2,-0.1 -0.799 51.4 136.8 -94.0 105.5 -3.8 6.6 17.8 21 21 A R B -d 33 0B 165 11,-2.4 13,-0.5 -2,-0.9 -2,-0.1 -0.695 46.4-145.0-147.7 81.8 -1.7 7.5 20.9 22 22 A P - 0 0 22 0, 0.0 32,-2.7 0, 0.0 2,-0.4 -0.173 16.9-170.0 -65.7 140.4 -0.9 11.2 20.5 23 23 A V E -BC 31 53A 5 8,-2.6 8,-2.9 30,-0.2 2,-0.6 -0.939 21.5-129.2-126.4 150.7 2.3 12.9 21.5 24 24 A c E -BC 30 52A 2 28,-2.5 27,-2.6 -2,-0.4 28,-1.0 -0.884 26.7-146.1 -94.3 120.7 3.1 16.6 21.6 25 25 A G E > - C 0 50A 0 4,-2.8 3,-2.4 -2,-0.6 25,-0.2 -0.503 24.4-112.8 -83.3 161.3 6.3 17.4 19.8 26 26 A T T 3 S+ 0 0 50 23,-2.2 24,-0.1 1,-0.3 -1,-0.1 0.560 117.5 67.4 -71.1 -5.1 8.8 20.2 20.9 27 27 A D T 3 S- 0 0 61 22,-0.3 -1,-0.3 2,-0.2 3,-0.1 0.452 120.2-110.6 -85.6 -4.4 7.8 21.9 17.6 28 28 A G S < S+ 0 0 43 -3,-2.4 2,-0.4 1,-0.3 -2,-0.1 0.523 79.6 124.0 87.3 1.8 4.2 22.4 19.2 29 29 A D - 0 0 94 27,-0.1 -4,-2.8 26,-0.1 2,-0.4 -0.795 60.3-126.6 -99.0 139.8 2.6 19.9 16.7 30 30 A T E -B 24 0A 59 -2,-0.4 -6,-0.2 -6,-0.2 3,-0.0 -0.657 18.2-158.9 -81.6 134.3 0.7 16.8 17.7 31 31 A Y E -B 23 0A 24 -8,-2.9 -8,-2.6 -2,-0.4 3,-0.1 -0.957 22.3-129.0-113.0 133.8 1.8 13.6 16.2 32 32 A P S S- 0 0 64 0, 0.0 -11,-2.4 0, 0.0 2,-0.3 0.695 89.7 -6.5 -58.7 -25.1 -0.9 10.8 16.1 33 33 A N B >> S-d 21 0B 9 -13,-0.2 4,-0.9 -11,-0.1 3,-0.6 -0.938 77.4-104.9-164.4 153.9 1.6 8.4 17.7 34 34 A E H 3> S+ 0 0 16 -13,-0.5 4,-2.3 -2,-0.3 3,-0.3 0.825 112.0 61.8 -50.7 -40.6 5.3 8.5 18.6 35 35 A b H 3> S+ 0 0 10 1,-0.2 4,-2.6 2,-0.2 5,-0.3 0.876 97.6 55.1 -66.9 -34.3 6.5 6.4 15.8 36 36 A V H <> S+ 0 0 47 -3,-0.6 4,-1.4 1,-0.2 -1,-0.2 0.847 109.3 50.5 -69.6 -26.7 5.3 8.7 13.0 37 37 A L H X S+ 0 0 0 -4,-0.9 4,-2.8 -3,-0.3 -2,-0.2 0.944 109.4 50.8 -69.5 -46.5 7.4 11.4 14.7 38 38 A a H X S+ 0 0 12 -4,-2.3 4,-2.4 -30,-0.4 -2,-0.2 0.960 113.9 42.9 -58.0 -49.5 10.4 9.1 14.8 39 39 A F H X S+ 0 0 20 -4,-2.6 4,-2.3 2,-0.2 -1,-0.2 0.825 111.6 56.2 -63.7 -29.9 10.1 8.3 11.1 40 40 A E H X S+ 0 0 67 -4,-1.4 4,-1.9 -5,-0.3 5,-0.2 0.947 107.8 47.9 -66.9 -41.8 9.5 12.0 10.4 41 41 A N H X>S+ 0 0 22 -4,-2.8 4,-2.1 1,-0.2 5,-0.9 0.925 112.1 50.8 -66.9 -38.3 12.7 12.8 12.1 42 42 A R H <5S+ 0 0 135 -4,-2.4 -1,-0.2 1,-0.2 -2,-0.2 0.902 112.2 45.2 -64.6 -39.9 14.4 10.0 10.0 43 43 A K H <5S+ 0 0 153 -4,-2.3 -1,-0.2 1,-0.2 -2,-0.2 0.785 126.6 28.4 -77.5 -27.9 13.1 11.3 6.7 44 44 A R H <5S- 0 0 122 -4,-1.9 -2,-0.2 -5,-0.2 -1,-0.2 0.542 98.7-125.2-107.9 -9.9 13.9 15.0 7.3 45 45 A Q T <5 + 0 0 160 -4,-2.1 2,-0.2 -5,-0.2 -3,-0.2 0.909 62.6 140.0 59.3 48.3 16.9 14.7 9.7 46 46 A T < - 0 0 46 -5,-0.9 -1,-0.2 -6,-0.2 -2,-0.1 -0.472 51.1-141.0-106.4 176.5 15.2 16.9 12.3 47 47 A S + 0 0 103 -2,-0.2 2,-0.3 -3,-0.1 -9,-0.1 -0.326 31.9 162.6-142.5 53.9 15.3 16.3 16.0 48 48 A I - 0 0 25 -11,-0.2 -41,-0.4 -10,-0.1 2,-0.2 -0.617 23.7-159.7 -69.8 129.6 11.8 17.1 17.2 49 49 A L - 0 0 35 -2,-0.3 -23,-2.2 -43,-0.1 2,-0.6 -0.521 24.2 -96.4-103.9 179.8 11.5 15.6 20.7 50 50 A I E -AC 5 25A 4 -45,-2.8 -45,-2.1 -25,-0.2 -25,-0.2 -0.902 28.8-171.6 -98.9 122.3 8.4 14.7 22.7 51 51 A Q E - 0 0 100 -27,-2.6 2,-0.3 -2,-0.6 -1,-0.2 0.848 68.4 -41.7 -72.1 -45.6 7.5 17.4 25.2 52 52 A K E - C 0 24A 101 -28,-1.0 -28,-2.5 2,-0.2 -1,-0.4 -0.956 68.6 -81.2-171.1 172.7 4.8 15.3 26.8 53 53 A S E S+ C 0 23A 89 -2,-0.3 -30,-0.2 -30,-0.2 -28,-0.0 -0.578 85.8 49.2 -89.2 161.7 2.1 12.8 25.9 54 54 A G S S- 0 0 24 -32,-2.7 -2,-0.2 -2,-0.2 -33,-0.0 -0.230 101.2 -52.6 97.0 163.1 -1.3 13.8 24.8 55 55 A P 0 0 68 0, 0.0 -31,-0.2 0, 0.0 -26,-0.1 -0.235 360.0 360.0 -56.5 162.5 -2.1 16.3 22.1 56 56 A c 0 0 93 -33,-0.2 -32,-0.1 -28,-0.1 -27,-0.1 0.926 360.0 360.0 -82.3 360.0 -0.6 19.7 22.3