==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=2-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER PROTEINASE INHIBITOR(TRYPSIN) 04-JAN-94 2LET . COMPND 2 MOLECULE: TRYPSIN INHIBITOR II; . SOURCE 2 ORGANISM_SCIENTIFIC: ECBALLIUM ELATERIUM; . AUTHOR K.J.NIELSEN,D.ALEWOOD,J.ANDREWS,S.B.H.KENT,D.J.CRAIK . 28 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2592.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 14 50.0 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 . 2 7.1 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 . 2 7.1 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 . 4 14.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 14.3 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 . 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 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 G 0 0 106 0, 0.0 18,-0.2 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 165.8 11.0 0.7 5.6 2 2 A a - 0 0 59 16,-0.2 16,-0.1 13,-0.0 15,-0.0 -0.923 360.0-165.8-126.6 104.2 7.3 1.1 5.1 3 3 A P - 0 0 83 0, 0.0 2,-0.3 0, 0.0 13,-0.1 0.104 13.2-135.2 -67.0-168.3 6.0 4.4 3.4 4 4 A R + 0 0 233 15,-0.0 2,-0.3 2,-0.0 24,-0.1 -0.954 38.4 119.2-159.5 137.2 2.3 5.5 3.4 5 5 A L S S- 0 0 129 -2,-0.3 2,-2.0 22,-0.1 22,-0.2 -0.938 73.7 -54.9 178.6 171.1 -0.1 6.9 0.9 6 6 A L S S+ 0 0 135 -2,-0.3 2,-0.5 20,-0.1 -2,-0.0 -0.436 73.1 147.8 -67.3 83.2 -3.5 6.1 -0.8 7 7 A M - 0 0 119 -2,-2.0 20,-2.3 20,-0.1 -2,-0.1 -0.935 43.1-135.7-125.0 104.0 -2.5 2.7 -2.1 8 8 A R B -A 26 0A 201 -2,-0.5 2,-0.3 18,-0.2 18,-0.3 -0.311 25.6-165.1 -60.8 138.1 -5.4 0.2 -2.3 9 9 A b + 0 0 21 16,-2.6 3,-0.1 13,-0.2 -1,-0.0 -0.837 32.9 173.9-126.5 163.8 -4.6 -3.3 -1.0 10 10 A K S S+ 0 0 188 1,-0.5 2,-0.3 -2,-0.3 -1,-0.1 0.359 80.2 24.0-138.7 -21.0 -6.1 -6.8 -1.2 11 11 A Q S > S- 0 0 131 1,-0.1 3,-0.9 9,-0.0 -1,-0.5 -0.937 81.7-108.2-145.3 163.2 -3.3 -8.7 0.5 12 12 A D G > S+ 0 0 93 -2,-0.3 3,-1.4 1,-0.2 -1,-0.1 0.972 118.6 53.7 -57.3 -57.7 -0.4 -7.9 3.0 13 13 A S G 3 S+ 0 0 92 1,-0.3 -1,-0.2 -3,-0.1 4,-0.1 0.570 83.1 94.4 -54.6 -13.1 2.3 -8.3 0.3 14 14 A D G < S+ 0 0 72 -3,-0.9 -1,-0.3 2,-0.1 -2,-0.2 0.873 87.9 43.1 -47.1 -45.7 0.3 -5.7 -1.8 15 15 A c S < S- 0 0 26 -3,-1.4 2,-0.1 -4,-0.3 3,-0.1 -0.078 112.8 -57.4 -89.6-169.7 2.5 -2.9 -0.4 16 16 A L S > S- 0 0 115 1,-0.1 3,-2.5 4,-0.1 -1,-0.2 -0.475 72.0 -80.2 -75.8 145.0 6.3 -2.7 0.3 17 17 A A T 3 S+ 0 0 100 1,-0.2 -1,-0.1 -2,-0.1 3,-0.1 -0.221 122.5 40.5 -48.0 106.9 7.9 -5.3 2.5 18 18 A G T 3 S+ 0 0 66 1,-0.6 -1,-0.2 -2,-0.2 -16,-0.2 -0.115 98.2 85.8 141.8 -35.3 7.1 -4.1 6.1 19 19 A a < - 0 0 7 -3,-2.5 -1,-0.6 -18,-0.2 2,-0.3 -0.340 57.9-152.2 -89.0 172.1 3.5 -2.9 5.6 20 20 A V - 0 0 66 8,-2.5 8,-2.6 -2,-0.1 2,-1.3 -0.848 42.7 -76.4-135.6 167.2 0.2 -4.8 5.8 21 21 A b - 0 0 43 -2,-0.3 6,-0.2 6,-0.2 -9,-0.1 -0.580 53.7-128.3 -75.0 98.1 -3.2 -4.3 4.2 22 22 A G > - 0 0 2 -2,-1.3 3,-2.1 1,-0.2 2,-1.5 -0.275 23.4-116.0 -49.2 112.1 -4.5 -1.3 6.3 23 23 A P T 3 S+ 0 0 129 0, 0.0 -1,-0.2 0, 0.0 4,-0.1 -0.317 104.5 55.7 -62.2 86.0 -8.0 -2.5 7.5 24 24 A N T 3 S- 0 0 126 -2,-1.5 3,-0.1 2,-0.1 -2,-0.1 0.082 126.4 -72.7-179.8 -35.6 -10.0 0.2 5.6 25 25 A G S < S+ 0 0 33 -3,-2.1 -16,-2.6 1,-0.6 2,-0.2 -0.218 107.6 63.9 157.1 -53.5 -9.0 -0.2 2.0 26 26 A F B S-A 8 0A 104 -18,-0.3 -1,-0.6 1,-0.2 -18,-0.2 -0.569 93.6 -75.1 -97.0 162.2 -5.5 1.1 1.6 27 27 A c 0 0 34 -20,-2.3 -6,-0.2 -6,-0.2 -1,-0.2 0.039 360.0 360.0 -51.3 159.2 -2.2 -0.1 3.1 28 28 A G 0 0 79 -8,-2.6 -8,-2.5 -24,-0.1 -6,-0.1 -0.942 360.0 360.0-150.9 360.0 -1.3 0.5 6.8