==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=26-NOV-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER PROTEINASE INHIBITOR (TRYPSIN) 28-AUG-90 1CTI . COMPND 2 MOLECULE: TRYPSIN INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: CUCURBITA MAXIMA; . AUTHOR T.A.HOLAK,D.GONDOL,J.OTLEWSKI,T.WILUSZ . 29 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2755.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 13 44.8 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 . 4 13.8 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 3.4 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 . 4 13.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 13.8 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 . 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 0 0 ANTIPARALLEL BRIDGES PER LADDER . 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 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 0 257 0, 0.0 2,-1.3 0, 0.0 20,-0.1 0.000 360.0 360.0 360.0 10.6 2.5 7.1 -6.6 2 2 A V + 0 0 97 18,-0.1 17,-1.7 1,-0.1 18,-0.2 -0.624 360.0 145.4 -79.6 100.1 6.0 6.9 -5.0 3 3 A a - 0 0 29 -2,-1.3 3,-0.2 16,-0.2 18,-0.1 -0.748 43.7-136.7-137.7 87.5 5.6 3.8 -3.0 4 4 A P - 0 0 81 0, 0.0 2,-1.5 0, 0.0 -2,-0.0 0.026 39.6 -86.8 -45.3 152.2 9.0 1.8 -2.8 5 5 A R S S+ 0 0 229 2,-0.1 2,-0.3 0, 0.0 24,-0.1 -0.444 75.6 139.2 -70.4 90.1 8.6 -2.0 -3.3 6 6 A I - 0 0 101 -2,-1.5 2,-0.7 23,-0.4 0, 0.0 -0.980 45.7-143.2-133.6 148.4 7.9 -3.2 0.3 7 7 A L + 0 0 132 -2,-0.3 2,-0.3 20,-0.1 22,-0.1 -0.826 43.0 137.9-113.1 90.4 5.5 -5.8 1.7 8 8 A M - 0 0 79 -2,-0.7 20,-2.0 20,-0.3 -2,-0.1 -0.945 51.4-105.5-128.7 154.4 4.0 -4.7 5.1 9 9 A E B +A 27 0A 133 -2,-0.3 2,-0.3 18,-0.2 18,-0.2 -0.335 37.9 177.8 -76.9 160.0 0.4 -4.9 6.4 10 10 A b - 0 0 23 16,-1.6 3,-0.1 1,-0.1 4,-0.0 -0.956 30.6-157.4-152.8 168.0 -2.0 -1.9 6.7 11 11 A K S S+ 0 0 181 1,-0.5 2,-0.3 -2,-0.3 -1,-0.1 0.624 85.2 14.4-118.8 -39.7 -5.6 -1.1 7.7 12 12 A K S > S- 0 0 126 1,-0.1 3,-1.6 14,-0.0 -1,-0.5 -0.913 80.5-108.8-132.9 163.6 -6.1 2.2 5.8 13 13 A D G > S+ 0 0 80 -2,-0.3 3,-1.5 1,-0.3 -1,-0.1 0.953 116.2 57.9 -56.8 -51.5 -4.1 3.9 3.0 14 14 A S G 3 S+ 0 0 90 1,-0.3 -1,-0.3 -3,-0.1 7,-0.1 0.461 85.1 90.6 -63.4 5.3 -2.7 6.7 5.1 15 15 A D G < S+ 0 0 58 -3,-1.6 -1,-0.3 2,-0.0 -2,-0.2 0.907 81.2 54.7 -69.1 -41.0 -1.2 3.9 7.3 16 16 A c S < S- 0 0 20 -3,-1.5 6,-0.1 -4,-0.3 -6,-0.0 -0.255 90.1 -99.5 -89.3 178.2 2.1 3.7 5.3 17 17 A L S > S+ 0 0 157 2,-0.1 3,-1.7 -2,-0.0 -1,-0.1 -0.112 83.8 15.6 -82.7-174.9 4.7 6.4 4.5 18 18 A A T 3 S- 0 0 65 1,-0.2 -15,-0.2 -15,-0.1 -2,-0.0 0.004 124.0 -41.4 45.9-150.2 5.2 8.3 1.2 19 19 A E T 3 S+ 0 0 125 -17,-1.7 -1,-0.2 2,-0.0 -16,-0.2 0.011 93.9 141.4 -96.7 27.6 2.2 8.1 -1.2 20 20 A a < - 0 0 18 -3,-1.7 2,-0.3 -18,-0.2 -4,-0.2 -0.344 32.6-162.3 -69.5 153.7 1.6 4.4 -0.6 21 21 A V - 0 0 63 -7,-0.1 8,-1.5 -20,-0.1 2,-0.7 -0.928 28.7 -99.5-132.3 158.7 -2.0 3.1 -0.4 22 22 A b B -B 28 0B 26 -2,-0.3 6,-0.3 6,-0.2 -9,-0.1 -0.690 45.4-158.0 -84.9 112.3 -3.4 -0.2 1.1 23 23 A L > - 0 0 85 4,-3.0 3,-2.3 -2,-0.7 -13,-0.1 -0.041 38.7 -75.6 -81.3-176.4 -4.0 -2.6 -1.8 24 24 A E T 3 S+ 0 0 184 1,-0.3 4,-0.1 2,-0.2 -1,-0.1 0.861 129.3 61.4 -47.5 -43.0 -6.3 -5.7 -2.2 25 25 A H T 3 S- 0 0 141 2,-0.2 -1,-0.3 1,-0.1 3,-0.1 0.380 115.9-116.9 -69.9 8.2 -4.0 -7.8 0.0 26 26 A G S < S+ 0 0 29 -3,-2.3 -16,-1.6 1,-0.3 2,-0.2 0.578 85.5 112.9 66.3 3.2 -4.7 -5.2 2.7 27 27 A Y B S-A 9 0A 108 -18,-0.2 -4,-3.0 1,-0.1 -1,-0.3 -0.674 75.4 -97.6-103.0 162.1 -1.0 -4.5 2.4 28 28 A c B B 22 0B 5 -20,-2.0 -20,-0.3 -6,-0.3 -6,-0.2 -0.414 360.0 360.0 -76.9 152.9 0.8 -1.4 1.1 29 29 A G 0 0 33 -8,-1.5 -23,-0.4 -2,-0.1 -21,-0.2 -0.129 360.0 360.0 -66.0 360.0 2.1 -1.1 -2.4