==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=18-JAN-2013 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE/HYDROLASE INHIBITOR 16-AUG-10 3OFW . COMPND 2 MOLECULE: KUNITZ-TYPE PROTEINASE INHIBITOR SHPI-1; . SOURCE 2 ORGANISM_SCIENTIFIC: STICHODACTYLA HELIANTHUS; . AUTHOR R.GARCIA-FERNANDEZ,L.REDECKE,T.PONS,M.PERBANDT,A.TALAVERA,D. . 56 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3973.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 27 48.2 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 . 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 E 0 0 234 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -47.6 -10.0 14.4 12.8 2 2 A A > + 0 0 54 53,-0.0 3,-0.6 0, 0.0 4,-0.1 0.335 360.0 100.9 160.0 8.7 -8.1 16.1 9.9 3 3 A S G > + 0 0 81 1,-0.2 3,-1.1 2,-0.1 4,-0.4 0.451 69.7 87.0 -66.6 -10.5 -6.5 19.2 11.3 4 4 A I G > S+ 0 0 46 1,-0.2 3,-0.9 2,-0.2 -1,-0.2 0.822 77.0 62.1 -58.8 -31.5 -3.6 16.7 11.2 5 5 A a G < S+ 0 0 15 -3,-0.6 -1,-0.2 1,-0.2 -2,-0.1 0.730 102.6 49.5 -67.3 -24.2 -3.0 17.9 7.6 6 6 A S G < S+ 0 0 84 -3,-1.1 -1,-0.2 -4,-0.1 -2,-0.2 0.485 85.8 107.4 -97.4 -1.3 -2.3 21.3 8.9 7 7 A E S < S- 0 0 62 -3,-0.9 16,-0.2 -4,-0.4 3,-0.1 -0.410 78.3-101.6 -70.3 147.2 0.2 20.2 11.6 8 8 A P - 0 0 93 0, 0.0 35,-0.3 0, 0.0 33,-0.2 -0.371 37.3 -89.7 -76.9 156.9 3.8 21.0 10.7 9 9 A K - 0 0 107 14,-0.1 2,-0.4 31,-0.1 35,-0.1 -0.413 47.7-170.0 -51.3 125.5 6.4 18.6 9.4 10 10 A K + 0 0 99 33,-0.4 31,-0.2 -2,-0.1 26,-0.1 -0.923 21.9 176.0-134.3 106.4 8.1 17.2 12.5 11 11 A V - 0 0 63 -2,-0.4 25,-2.4 24,-0.1 27,-0.4 0.827 37.7-147.3 -71.6 -35.6 11.3 15.1 12.1 12 12 A G - 0 0 28 27,-0.2 27,-0.2 1,-0.2 -1,-0.1 -0.156 27.1 -81.1 85.1 174.0 11.8 14.7 15.9 13 13 A R S S+ 0 0 227 25,-0.2 -1,-0.2 -2,-0.1 2,-0.1 0.505 95.7 102.7 -91.3 -6.0 15.0 14.4 17.9 14 14 A b - 0 0 51 24,-0.5 23,-0.1 -3,-0.2 24,-0.1 -0.394 64.7-143.3 -81.2 158.5 15.5 10.7 17.2 15 15 A K + 0 0 198 -2,-0.1 22,-0.1 22,-0.1 -1,-0.1 0.074 55.3 122.5-113.2 20.4 18.0 9.4 14.6 16 16 A G - 0 0 32 20,-2.2 2,-0.5 1,-0.1 21,-0.1 -0.132 63.7-114.0 -75.3 178.0 16.1 6.5 13.1 17 17 A Y + 0 0 169 19,-0.1 19,-0.2 20,-0.1 -2,-0.1 -0.867 47.3 148.3-122.0 97.8 15.2 5.9 9.5 18 18 A F E -A 35 0A 91 17,-1.7 17,-2.7 -2,-0.5 2,-0.3 -0.873 34.3-148.3-130.0 93.9 11.5 6.0 8.7 19 19 A P E +A 34 0A 71 0, 0.0 2,-0.2 0, 0.0 15,-0.2 -0.507 34.7 157.7 -63.1 125.8 10.4 7.3 5.3 20 20 A R E -A 33 0A 51 13,-2.9 13,-2.0 -2,-0.3 2,-0.4 -0.786 35.8-115.2-138.1 176.3 7.1 9.0 5.6 21 21 A F E -AB 32 45A 45 24,-2.3 24,-2.7 -2,-0.2 2,-0.3 -0.969 21.1-175.9-121.2 139.0 4.8 11.5 4.0 22 22 A Y E -A 31 0A 29 9,-2.3 9,-3.3 -2,-0.4 2,-0.6 -0.931 31.3-116.0-122.3 153.1 3.6 14.9 5.2 23 23 A F E -A 30 0A 34 -2,-0.3 2,-0.6 7,-0.2 7,-0.2 -0.819 29.0-141.2 -87.4 122.6 1.1 17.2 3.5 24 24 A D E >> -A 29 0A 32 5,-1.8 4,-2.4 -2,-0.6 5,-0.5 -0.797 9.0-160.5 -91.7 117.1 2.8 20.4 2.6 25 25 A S T 45S+ 0 0 91 -2,-0.6 -1,-0.1 2,-0.2 -19,-0.0 0.880 90.1 51.0 -55.9 -48.4 0.7 23.6 3.1 26 26 A E T 45S+ 0 0 173 1,-0.2 -1,-0.2 3,-0.1 -2,-0.0 0.939 123.1 27.2 -56.8 -54.5 2.8 25.8 0.8 27 27 A T T 45S- 0 0 87 2,-0.2 -2,-0.2 1,-0.0 -1,-0.2 0.681 93.5-132.3 -87.2 -22.6 2.9 23.4 -2.2 28 28 A G T <5 + 0 0 16 -4,-2.4 2,-0.4 1,-0.2 -3,-0.2 0.670 68.3 119.4 76.5 15.6 -0.4 21.5 -1.7 29 29 A K E S- 0 0 68 1,-0.1 4,-1.9 -26,-0.1 5,-0.1 -0.892 71.9-121.0-133.1 159.0 2.1 5.9 2.3 48 48 A L H > S+ 0 0 59 -2,-0.3 4,-2.0 2,-0.2 5,-0.2 0.863 116.5 53.3 -60.3 -40.8 1.6 8.5 -0.5 49 49 A H H > S+ 0 0 145 2,-0.2 4,-3.2 1,-0.2 5,-0.2 0.926 106.4 51.1 -64.2 -44.2 -1.8 7.1 -1.0 50 50 A Q H > S+ 0 0 66 1,-0.2 4,-2.7 2,-0.2 5,-0.3 0.928 110.4 49.5 -57.4 -48.9 -2.8 7.5 2.7 51 51 A c H X S+ 0 0 0 -4,-1.9 4,-2.7 2,-0.2 5,-0.3 0.899 114.9 43.4 -57.8 -43.6 -1.6 11.1 2.6 52 52 A R H X S+ 0 0 133 -4,-2.0 4,-2.0 2,-0.2 -2,-0.2 0.942 112.5 52.5 -72.8 -44.8 -3.6 12.0 -0.5 53 53 A A H < S+ 0 0 63 -4,-3.2 -2,-0.2 1,-0.2 -3,-0.2 0.944 121.1 32.5 -53.3 -51.2 -6.7 10.1 0.7 54 54 A I H < S+ 0 0 86 -4,-2.7 -2,-0.2 -5,-0.2 -1,-0.2 0.909 129.7 30.8 -73.2 -43.8 -6.7 12.0 4.0 55 55 A a H < 0 0 22 -4,-2.7 -3,-0.2 -5,-0.3 -2,-0.2 0.617 360.0 360.0 -99.9 -10.7 -5.4 15.4 3.0 56 56 A R < 0 0 181 -4,-2.0 -27,-0.1 -5,-0.3 -4,-0.0 -0.226 360.0 360.0-126.2 360.0 -6.3 16.1 -0.6