==== 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 SERINE PROTEASE INHIBITOR 13-FEB-95 1AML . COMPND 2 MOLECULE: AMYLOID A4; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR P.ROESCH,H.STICHT . 40 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4057.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 20 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 . 0 0.0 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 . 1 2.5 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 . 1 2.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 12.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 11 27.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 5.0 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 1 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 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 . 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 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 D 0 0 201 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 135.4 10.4 5.0 -7.6 2 2 A A - 0 0 61 1,-0.1 3,-0.0 2,-0.0 0, 0.0 -0.213 360.0-167.2 -75.0 172.8 11.3 1.4 -6.7 3 3 A E + 0 0 115 4,-0.0 -1,-0.1 1,-0.0 4,-0.0 0.069 33.0 142.5-150.5 27.6 12.5 0.4 -3.2 4 4 A F S S- 0 0 171 2,-0.1 2,-0.1 0, 0.0 3,-0.1 0.887 85.1 -12.7 -40.7 -45.0 14.0 -3.1 -3.6 5 5 A R S S+ 0 0 186 1,-0.1 3,-0.1 3,-0.0 0, 0.0 -0.344 86.1 103.6-133.5-144.1 16.6 -2.0 -1.1 6 6 A H + 0 0 145 1,-0.2 2,-0.6 -2,-0.1 -1,-0.1 0.780 62.7 121.9 67.7 22.1 17.8 1.2 0.5 7 7 A D + 0 0 106 -3,-0.1 2,-0.2 -4,-0.0 -1,-0.2 -0.907 33.3 96.5-121.4 106.9 16.0 0.2 3.7 8 8 A S S S- 0 0 105 -2,-0.6 -3,-0.0 1,-0.1 0, 0.0 -0.637 71.4-100.6-156.0-144.7 18.0 -0.1 6.9 9 9 A G S S+ 0 0 61 -2,-0.2 -1,-0.1 0, 0.0 0, 0.0 0.646 101.6 39.4-123.7 -57.7 18.9 2.0 9.9 10 10 A Y + 0 0 131 1,-0.1 -2,-0.1 2,-0.1 0, 0.0 0.841 55.7 144.1 -62.3-105.1 22.4 3.5 9.5 11 11 A E + 0 0 72 -4,-0.1 -1,-0.1 1,-0.1 5,-0.1 0.601 46.3 102.5 77.9 7.5 22.8 4.7 5.9 12 12 A V S S- 0 0 98 3,-0.1 -2,-0.1 4,-0.0 -1,-0.1 0.663 104.6 -6.8 -96.1 -17.8 24.8 7.7 7.1 13 13 A H S > S+ 0 0 115 2,-0.0 4,-1.3 3,-0.0 3,-0.4 0.483 121.8 70.1-141.5 -49.2 28.2 6.2 6.1 14 14 A H H > S+ 0 0 117 1,-0.2 4,-2.3 2,-0.2 3,-0.2 0.839 99.8 58.9 -47.3 -30.8 27.9 2.6 5.0 15 15 A Q H >>S+ 0 0 45 1,-0.2 4,-1.5 2,-0.2 5,-0.5 0.973 96.8 55.9 -66.2 -52.1 26.2 4.1 1.9 16 16 A K H >5S+ 0 0 128 -3,-0.4 4,-0.7 1,-0.2 -1,-0.2 0.809 110.8 50.3 -51.7 -23.6 29.2 6.3 0.9 17 17 A L H X5S+ 0 0 49 -4,-1.3 4,-2.5 -3,-0.2 -2,-0.2 0.973 115.1 38.3 -78.1 -59.7 31.0 2.9 0.9 18 18 A V H X5S+ 0 0 61 -4,-2.3 4,-2.3 1,-0.2 5,-0.3 0.974 112.5 55.3 -50.3 -75.9 28.6 1.0 -1.2 19 19 A F H X5S+ 0 0 129 -4,-1.5 4,-2.1 1,-0.3 -1,-0.2 0.798 110.0 51.3 -26.9 -42.2 27.8 3.8 -3.6 20 20 A F H >XX S+ 0 0 62 -4,-2.5 3,-1.3 1,-0.3 4,-1.2 0.897 110.3 55.1 -43.1 -47.5 31.8 0.1 -4.8 22 22 A E H 3< S+ 0 0 131 -4,-2.3 -1,-0.3 1,-0.3 -2,-0.2 0.935 118.0 32.9 -56.5 -46.9 28.9 0.6 -7.2 23 23 A D H << S+ 0 0 143 -4,-2.1 -1,-0.3 -3,-0.6 -2,-0.2 0.253 113.8 70.6 -94.3 14.6 30.8 3.3 -9.1 24 24 A V H << S- 0 0 39 -3,-1.3 -2,-0.2 -4,-0.7 -3,-0.2 0.879 72.0-160.5 -92.5 -78.5 34.0 1.5 -8.4 25 25 A G S < S- 0 0 60 -4,-1.2 -1,-0.1 2,-0.1 -4,-0.1 -0.261 72.4 -29.4 123.3 -47.3 34.2 -1.7 -10.5 26 26 A S S S+ 0 0 113 2,-0.1 2,-0.1 0, 0.0 -5,-0.0 0.219 105.1 96.4 164.8 51.3 36.9 -3.7 -8.5 27 27 A N S S- 0 0 133 1,-0.2 2,-0.2 -6,-0.1 -2,-0.1 -0.171 77.9 -50.4-126.1-138.7 39.5 -1.5 -6.8 28 28 A K + 0 0 151 1,-0.1 -1,-0.2 -2,-0.1 -2,-0.1 -0.681 43.5 175.9-103.7 160.8 39.8 -0.1 -3.3 29 29 A G - 0 0 36 -2,-0.2 -1,-0.1 1,-0.1 -11,-0.0 0.437 51.3 -65.2-125.4 -91.1 37.2 1.7 -1.2 30 30 A A S S+ 0 0 58 0, 0.0 4,-0.4 0, 0.0 -1,-0.1 0.352 113.7 4.1-133.5 -87.8 37.8 2.8 2.4 31 31 A I S >> S+ 0 0 96 1,-0.2 4,-1.8 2,-0.2 3,-0.9 0.800 123.8 66.0 -78.6 -27.5 38.3 0.2 5.2 32 32 A I H 3> S+ 0 0 78 1,-0.3 4,-2.1 2,-0.2 -1,-0.2 0.951 92.6 59.8 -59.4 -46.9 38.2 -2.7 2.7 33 33 A G H 34 S+ 0 0 12 2,-0.2 -1,-0.3 1,-0.2 -2,-0.2 0.802 108.7 48.7 -52.8 -25.1 41.4 -1.5 1.1 34 34 A L H X4 S+ 0 0 126 -3,-0.9 3,-1.6 -4,-0.4 -2,-0.2 0.972 110.5 42.9 -79.5 -68.0 43.0 -2.0 4.5 35 35 A M H ><>S+ 0 0 110 -4,-1.8 5,-0.9 1,-0.3 3,-0.6 0.764 107.4 68.1 -50.4 -21.1 41.8 -5.5 5.5 36 36 A V T 3<5S+ 0 0 82 -4,-2.1 -1,-0.3 -5,-0.3 -2,-0.1 0.055 98.7 51.1 -88.4 28.6 42.7 -6.4 1.9 37 37 A G T < 5S+ 0 0 66 -3,-1.6 -1,-0.2 -5,-0.1 -2,-0.1 -0.096 108.8 37.6-156.0 46.0 46.4 -5.9 2.7 38 38 A G T < 5S- 0 0 73 -3,-0.6 -2,-0.1 2,-0.6 -3,-0.1 0.145 128.0 -5.3-157.2 -73.2 47.3 -7.9 5.8 39 39 A V T 5 0 0 140 -4,-0.4 -3,-0.1 1,-0.3 -4,-0.1 0.723 360.0 360.0-108.1 -32.0 45.7 -11.3 6.3 40 40 A V < 0 0 137 -5,-0.9 -2,-0.6 0, 0.0 -1,-0.3 -0.987 360.0 360.0-128.3 360.0 43.2 -11.5 3.4