==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=25-NOV-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER PROTEINASE INHIBITOR (TRYPSIN) 11-DEC-91 1BPT . COMPND 2 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; . AUTHOR D.HOUSSET,A.WLODAWER,F.TAO,J.FUCHS,C.WOODWARD . 56 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3907.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 29 51.8 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 . 10 17.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, 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 . 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 10.7 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 . 7 12.5 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 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 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 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 0 138 0, 0.0 54,-0.1 0, 0.0 5,-0.1 0.000 360.0 360.0 360.0 92.0 29.1 12.0 -11.9 2 2 A P > - 0 0 45 0, 0.0 3,-1.4 0, 0.0 4,-0.3 -0.124 360.0-115.3 -53.0 149.3 32.0 11.5 -9.6 3 3 A D G > S+ 0 0 149 1,-0.3 3,-1.1 2,-0.2 4,-0.1 0.764 112.0 64.9 -63.6 -28.7 33.4 8.0 -9.4 4 4 A F G > S+ 0 0 42 1,-0.3 3,-1.4 2,-0.2 -1,-0.3 0.657 85.6 75.1 -72.8 -14.5 32.4 7.5 -5.8 5 5 A a G < S+ 0 0 0 -3,-1.4 20,-0.5 1,-0.3 -1,-0.3 0.717 92.4 53.7 -66.9 -22.4 28.8 7.8 -6.9 6 6 A L G < S+ 0 0 118 -3,-1.1 -1,-0.3 -4,-0.3 -2,-0.2 0.508 87.2 112.5 -89.5 -6.1 29.1 4.2 -8.3 7 7 A E S < S- 0 0 32 -3,-1.4 18,-0.2 -4,-0.1 16,-0.2 -0.470 72.5-116.5 -70.2 146.6 30.3 2.8 -4.9 8 8 A P - 0 0 101 0, 0.0 35,-0.2 0, 0.0 -1,-0.1 -0.355 44.0 -89.9 -74.7 155.2 28.2 0.4 -2.9 9 9 A P - 0 0 50 0, 0.0 2,-0.5 0, 0.0 35,-0.1 -0.328 39.1-144.5 -65.3 147.7 27.0 1.7 0.5 10 10 A Y - 0 0 93 33,-0.4 31,-0.3 1,-0.2 26,-0.1 -0.918 21.3-180.0-124.8 112.8 29.4 1.0 3.4 11 11 A T - 0 0 69 -2,-0.5 25,-2.2 24,-0.2 27,-0.5 0.897 34.5-160.7 -71.3 -49.0 27.9 0.2 6.8 12 12 A G - 0 0 19 1,-0.2 27,-0.1 23,-0.1 -1,-0.1 -0.233 33.1 -62.7 89.1 177.8 31.4 -0.2 8.3 13 13 A P S S+ 0 0 56 0, 0.0 -1,-0.2 0, 0.0 2,-0.1 0.472 96.1 97.5 -83.4 -10.3 32.4 -2.0 11.5 14 14 A b - 0 0 52 24,-0.5 23,-0.1 -3,-0.3 24,-0.1 -0.357 67.5-132.2 -82.9 163.7 30.6 0.0 14.2 15 15 A K + 0 0 198 -2,-0.1 2,-0.2 22,-0.1 22,-0.1 -0.041 61.6 111.6-107.9 27.1 27.3 -0.9 15.8 16 16 A A - 0 0 51 20,-2.1 2,-0.6 2,-0.0 22,-0.1 -0.531 64.2-127.5 -92.4 169.0 25.1 2.2 15.8 17 17 A R + 0 0 214 -2,-0.2 2,-0.5 19,-0.1 19,-0.2 -0.921 41.2 162.8-118.6 94.2 22.0 2.5 13.6 18 18 A I E -A 35 0A 57 17,-1.9 17,-3.8 -2,-0.6 2,-0.6 -0.980 31.7-138.1-116.3 124.7 22.4 5.8 11.7 19 19 A I E +A 34 0A 99 -2,-0.5 2,-0.2 15,-0.2 15,-0.2 -0.802 34.7 159.1 -91.8 123.8 20.3 6.5 8.6 20 20 A R E -A 33 0A 29 13,-2.1 13,-2.3 -2,-0.6 2,-0.4 -0.759 35.7-107.8-126.6 175.9 22.2 8.1 5.8 21 21 A Y E -AB 32 45A 71 24,-3.2 24,-3.9 -2,-0.2 2,-0.3 -0.878 25.9-176.0-115.0 143.8 21.8 8.4 2.0 22 22 A F E -A 31 0A 19 9,-2.8 9,-2.7 -2,-0.4 2,-0.5 -0.924 30.6-114.7-131.7 149.9 23.8 6.7 -0.8 23 23 A A E -A 30 0A 4 -2,-0.3 2,-0.7 7,-0.2 7,-0.2 -0.826 20.6-150.6 -90.8 128.0 23.4 7.2 -4.5 24 24 A N E >>> -A 29 0A 38 5,-3.0 4,-1.8 -2,-0.5 5,-1.0 -0.893 8.9-170.3-106.2 84.9 22.1 4.1 -6.3 25 25 A A T 345S+ 0 0 48 -2,-0.7 -1,-0.1 -20,-0.5 -19,-0.1 0.632 85.5 54.3 -49.5 -27.4 23.7 4.4 -9.8 26 26 A K T 345S+ 0 0 203 1,-0.1 -1,-0.2 3,-0.1 -20,-0.0 0.853 115.9 33.8 -79.1 -45.8 21.5 1.5 -10.9 27 27 A A T <45S- 0 0 51 -3,-0.5 -2,-0.2 2,-0.2 -1,-0.1 0.474 100.9-127.5 -94.0 -5.9 18.1 3.0 -9.8 28 28 A G T <5S+ 0 0 56 -4,-1.8 2,-0.3 1,-0.2 -3,-0.2 0.657 75.2 106.7 66.2 19.0 19.1 6.5 -10.6 29 29 A L E S- 0 0 45 -26,-0.1 4,-1.6 1,-0.1 -1,-0.2 -0.971 75.6-119.9-142.9 159.9 20.2 14.2 3.2 48 48 A A H > S+ 0 0 36 -2,-0.3 4,-3.0 1,-0.2 5,-0.2 0.739 112.5 58.6 -64.0 -34.7 18.8 13.2 -0.1 49 49 A E H > S+ 0 0 126 2,-0.2 4,-2.4 1,-0.2 -1,-0.2 0.882 105.3 47.6 -64.1 -46.2 19.4 16.8 -1.5 50 50 A D H > S+ 0 0 67 2,-0.2 4,-2.2 1,-0.2 5,-0.2 0.917 114.7 49.0 -59.9 -47.0 23.2 16.6 -0.7 51 51 A c H X S+ 0 0 0 -4,-1.6 4,-3.3 1,-0.2 5,-0.5 0.929 112.9 45.5 -62.1 -48.9 23.1 13.2 -2.5 52 52 A M H X S+ 0 0 97 -4,-3.0 4,-1.4 3,-0.2 -1,-0.2 0.858 112.4 50.8 -65.1 -39.7 21.2 14.4 -5.5 53 53 A R H < S+ 0 0 169 -4,-2.4 -2,-0.2 -5,-0.2 -1,-0.2 0.962 119.3 37.4 -65.2 -46.5 23.4 17.6 -5.9 54 54 A T H < S+ 0 0 51 -4,-2.2 -2,-0.2 -5,-0.2 -3,-0.2 0.895 138.5 9.2 -69.4 -48.9 26.6 15.5 -5.7 55 55 A a H < 0 0 4 -4,-3.3 -3,-0.2 -5,-0.2 -2,-0.2 0.574 360.0 360.0-114.1 -10.2 25.5 12.4 -7.7 56 56 A G < 0 0 85 -4,-1.4 -27,-0.0 -5,-0.5 -4,-0.0 -0.629 360.0 360.0 -74.1 360.0 22.1 12.8 -9.4