==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=8-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SERINE PROTEASE INHIBITOR 18-AUG-92 1NAG . COMPND 2 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR; . SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; . AUTHOR A.T.DANISHEFSKY,A.WLODAWER,K.-S.KIM,F.TAO,C.WOODWARD . 56 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4013.0 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 . 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 . 5 8.9 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 . 2 3.6 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 0 163 0, 0.0 54,-0.1 0, 0.0 5,-0.1 0.000 360.0 360.0 360.0 116.3 12.3 -5.4 10.1 2 2 A P > - 0 0 50 0, 0.0 3,-1.9 0, 0.0 4,-0.3 -0.285 360.0-117.8 -64.0 148.6 9.2 -6.2 8.0 3 3 A D G > S+ 0 0 146 1,-0.3 3,-2.1 2,-0.2 4,-0.2 0.796 109.6 71.9 -57.4 -29.4 9.8 -6.9 4.3 4 4 A F G > S+ 0 0 46 1,-0.3 3,-1.1 2,-0.2 -1,-0.3 0.701 82.6 73.0 -61.8 -20.5 7.7 -3.9 3.4 5 5 A a G < S+ 0 0 3 -3,-1.9 18,-0.3 1,-0.2 -1,-0.3 0.774 96.3 48.6 -62.3 -31.2 10.5 -1.7 4.7 6 6 A L G < S+ 0 0 108 -3,-2.1 -1,-0.2 -4,-0.3 -2,-0.2 0.383 85.4 105.1 -92.2 1.6 12.6 -2.6 1.6 7 7 A E S < S- 0 0 111 -3,-1.1 16,-0.2 -4,-0.2 3,-0.1 -0.505 82.7-101.6 -79.2 146.3 9.9 -1.9 -1.0 8 8 A P - 0 0 108 0, 0.0 35,-0.1 0, 0.0 -1,-0.1 -0.386 46.0 -92.1 -66.3 152.1 10.5 1.3 -3.0 9 9 A P - 0 0 49 0, 0.0 2,-0.5 0, 0.0 35,-0.1 -0.249 38.4-140.7 -63.3 153.7 8.4 4.3 -1.9 10 10 A Y - 0 0 88 33,-0.2 31,-0.3 1,-0.1 26,-0.1 -0.968 18.9-173.9-126.8 117.5 5.1 4.8 -3.8 11 11 A T - 0 0 70 -2,-0.5 25,-2.7 24,-0.2 27,-0.4 0.891 32.0-161.0 -73.5 -42.3 3.8 8.1 -4.9 12 12 A G - 0 0 22 1,-0.2 27,-0.1 23,-0.1 -1,-0.1 -0.166 33.6 -68.9 85.3 179.0 0.4 6.9 -6.1 13 13 A P S S+ 0 0 87 0, 0.0 -1,-0.2 0, 0.0 26,-0.1 0.451 93.4 102.2 -90.1 -4.2 -2.0 8.5 -8.5 14 14 A b - 0 0 55 24,-0.3 23,-0.2 -3,-0.3 24,-0.1 -0.287 68.9-129.0 -79.5 166.5 -3.4 11.4 -6.4 15 15 A K + 0 0 195 22,-0.1 22,-0.2 -2,-0.1 21,-0.1 0.216 65.3 107.7-103.9 9.1 -2.1 15.0 -6.9 16 16 A A - 0 0 47 20,-2.7 2,-0.3 1,-0.0 22,-0.1 -0.259 61.9-135.7 -77.9 173.8 -1.1 16.3 -3.5 17 17 A R + 0 0 201 19,-0.1 2,-0.5 20,-0.1 19,-0.2 -0.730 36.2 166.4-130.6 76.6 2.6 16.8 -2.6 18 18 A I E -A 35 0A 62 17,-2.7 17,-3.6 -2,-0.3 2,-0.6 -0.866 34.4-130.4 -98.5 127.6 2.8 15.4 0.9 19 19 A I E +A 34 0A 96 -2,-0.5 2,-0.3 15,-0.2 15,-0.2 -0.736 38.0 167.7 -81.1 122.4 6.2 14.8 2.3 20 20 A R E -A 33 0A 34 13,-2.4 13,-2.1 -2,-0.6 2,-0.3 -0.759 28.7-115.7-126.0 170.2 6.4 11.3 3.8 21 21 A Y E +AB 32 45A 65 24,-2.6 24,-2.4 -2,-0.3 2,-0.3 -0.826 25.3 177.9-114.4 148.0 9.3 9.0 5.0 22 22 A F E -A 31 0A 34 9,-2.5 9,-2.6 -2,-0.3 2,-0.6 -0.957 35.1-105.9-141.0 157.1 10.5 5.7 3.7 23 23 A Y E -A 30 0A 21 -2,-0.3 2,-0.9 -18,-0.3 7,-0.2 -0.790 23.2-156.8 -90.6 121.6 13.4 3.5 4.8 24 24 A N E >> -A 29 0A 39 5,-2.3 4,-2.5 -2,-0.6 5,-0.9 -0.856 4.9-166.4 -97.3 103.0 16.4 3.5 2.4 25 25 A A T 45S+ 0 0 50 -2,-0.9 -1,-0.2 1,-0.2 -19,-0.1 0.772 85.8 55.8 -61.8 -31.9 18.2 0.2 3.2 26 26 A K T 45S+ 0 0 198 1,-0.2 -1,-0.2 -3,-0.1 -2,-0.0 0.937 116.1 35.5 -65.3 -51.6 21.3 1.3 1.3 27 27 A A T 45S- 0 0 55 2,-0.2 -2,-0.2 1,-0.0 -1,-0.2 0.744 100.8-135.5 -73.1 -27.4 21.7 4.5 3.4 28 28 A G T <5S+ 0 0 29 -4,-2.5 2,-0.3 1,-0.3 -3,-0.2 0.657 72.9 85.9 80.5 12.7 20.4 2.8 6.6 29 29 A L E S- 0 0 25 -26,-0.1 4,-1.9 1,-0.1 -26,-0.1 -0.952 74.6-117.8-150.8 160.2 7.7 11.0 10.6 48 48 A A H > S+ 0 0 30 -2,-0.3 4,-3.3 1,-0.2 5,-0.2 0.859 116.0 57.1 -65.8 -35.6 11.4 9.9 10.5 49 49 A E H > S+ 0 0 102 2,-0.2 4,-2.6 1,-0.2 -1,-0.2 0.909 105.7 45.7 -63.0 -47.1 10.8 8.5 14.0 50 50 A D H > S+ 0 0 73 1,-0.2 4,-1.6 2,-0.2 5,-0.2 0.902 116.0 49.5 -61.4 -42.6 7.9 6.2 13.1 51 51 A c H X>S+ 0 0 0 -4,-1.9 4,-3.0 2,-0.2 5,-0.5 0.954 113.1 43.9 -61.0 -50.9 9.9 5.1 10.1 52 52 A M H X5S+ 0 0 67 -4,-3.3 4,-1.7 1,-0.2 -2,-0.2 0.863 112.0 54.1 -65.2 -35.7 13.1 4.4 12.1 53 53 A R H <5S+ 0 0 187 -4,-2.6 -1,-0.2 -5,-0.2 -2,-0.2 0.821 119.0 33.6 -69.1 -33.0 11.2 2.6 14.9 54 54 A T H <5S+ 0 0 59 -4,-1.6 -2,-0.2 -3,-0.3 -1,-0.2 0.862 136.8 18.8 -88.1 -45.9 9.5 0.3 12.4 55 55 A a H <5 0 0 1 -4,-3.0 -3,-0.2 -5,-0.2 -2,-0.2 0.604 360.0 360.0-103.8 -17.0 12.2 -0.2 9.8 56 56 A G << 0 0 56 -4,-1.7 -1,-0.2 -5,-0.5 -3,-0.2 0.597 360.0 360.0 -75.7 360.0 15.4 0.8 11.6