==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=10-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER INHIBITOR 08-APR-99 1QFD . COMPND 2 MOLECULE: PROTEIN (ALPHA-AMYLASE INHIBITOR); . SOURCE 2 ORGANISM_SCIENTIFIC: AMARANTHUS HYPOCHONDRIACUS; . AUTHOR S.LU,P.DENG,X.LIU,J.LUO,R.HAN,X.GU,S.LIANG,X.WANG,L.FENG, . 32 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2567.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 14 43.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 6.2 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 4 12.5 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 . 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 . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 2 6.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 2 6.2 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 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 RESIDUES PER ALPHA HELIX . 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 PARALLEL BRIDGES PER LADDER . 2 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 a 0 0 96 0, 0.0 16,-0.2 0, 0.0 14,-0.0 0.000 360.0 360.0 360.0 178.3 2.4 4.1 6.6 2 2 A I B -a 17 0A 22 14,-0.9 16,-1.8 4,-0.1 2,-0.1 -0.825 360.0-114.3-102.3 140.1 0.4 5.1 3.4 3 3 A P > - 0 0 78 0, 0.0 3,-0.7 0, 0.0 28,-0.2 -0.436 45.5 -91.4 -69.8 138.8 -2.8 7.1 3.5 4 4 A K T 3 S+ 0 0 75 1,-0.2 28,-0.2 -2,-0.1 3,-0.1 -0.031 111.4 27.4 -46.7 153.2 -5.9 5.1 2.3 5 5 A W T 3 S+ 0 0 188 26,-1.8 2,-0.3 1,-0.2 -1,-0.2 0.764 103.2 107.5 62.6 26.7 -6.7 5.4 -1.5 6 6 A N S < S- 0 0 75 -3,-0.7 25,-0.5 -4,-0.1 -1,-0.2 -0.802 81.6 -77.6-127.2 170.6 -3.0 6.1 -2.3 7 7 A R - 0 0 173 -2,-0.3 2,-0.4 23,-0.2 23,-0.2 -0.443 49.7-168.7 -68.7 137.1 -0.2 4.1 -4.0 8 8 A b + 0 0 5 17,-0.2 21,-0.5 -2,-0.1 17,-0.2 -0.973 20.7 165.4-130.4 144.3 1.4 1.5 -1.7 9 9 A G B >> +B 15 0B 4 6,-0.8 4,-2.4 -2,-0.4 6,-0.6 -0.487 6.4 162.7-158.2 80.3 4.5 -0.7 -2.1 10 10 A P H >5S+ 0 0 30 0, 0.0 4,-0.7 0, 0.0 17,-0.1 0.778 81.4 54.9 -72.3 -27.7 5.8 -2.4 1.1 11 11 A K H 45S+ 0 0 147 15,-0.7 16,-0.1 2,-0.1 15,-0.1 0.753 118.9 33.0 -78.4 -22.0 8.0 -4.9 -0.9 12 12 A M H 45S+ 0 0 120 14,-0.7 -1,-0.1 -3,-0.2 15,-0.1 0.737 136.7 21.4-103.7 -29.3 9.8 -2.0 -2.7 13 13 A D H <5S- 0 0 111 -4,-2.4 -2,-0.1 2,-0.1 14,-0.0 0.597 95.8-123.8-112.8 -17.3 9.8 0.7 0.1 14 14 A G S < - 0 0 36 -16,-1.8 3,-2.3 4,-0.1 -1,-0.1 -0.101 52.2-100.3 -55.8 159.5 -1.6 1.9 7.6 19 19 A E T 3 S+ 0 0 175 1,-0.3 -1,-0.1 -3,-0.1 -2,-0.1 0.904 124.5 53.4 -50.0 -48.3 -2.7 -0.9 9.9 20 20 A P T 3 S+ 0 0 94 0, 0.0 -1,-0.3 0, 0.0 2,-0.3 0.501 114.6 51.5 -68.5 -0.0 -6.4 -0.1 9.4 21 21 A Y S < S- 0 0 83 -3,-2.3 2,-0.3 -4,-0.1 -19,-0.0 -0.814 71.7-145.8-129.9 172.0 -5.8 -0.4 5.6 22 22 A T - 0 0 94 -2,-0.3 10,-1.0 10,-0.1 2,-0.4 -0.973 14.7-123.5-138.9 154.4 -4.2 -2.9 3.2 23 23 A b B -C 31 0C 33 -2,-0.3 8,-0.2 8,-0.2 3,-0.1 -0.776 9.5-158.7 -98.6 140.8 -2.2 -2.7 -0.0 24 24 A T S S+ 0 0 94 6,-1.7 2,-0.5 -2,-0.4 -1,-0.1 0.938 81.3 30.1 -82.8 -50.5 -3.4 -4.5 -3.2 25 25 A S - 0 0 47 5,-0.3 -1,-0.3 -17,-0.2 4,-0.2 -0.932 64.1-152.3-114.2 126.9 -0.0 -4.8 -5.1 26 26 A D S S+ 0 0 73 -2,-0.5 -15,-0.7 -17,-0.1 -14,-0.7 0.792 100.6 39.0 -65.1 -25.0 3.3 -5.0 -3.3 27 27 A Y S S- 0 0 169 1,-0.2 2,-0.3 -16,-0.1 -1,-0.1 0.930 136.8 -20.7 -89.3 -59.6 5.0 -3.4 -6.3 28 28 A Y S S+ 0 0 150 -21,-0.0 -1,-0.2 2,-0.0 2,-0.2 -0.882 88.2 99.5-155.8 120.0 2.5 -0.7 -7.4 29 29 A G - 0 0 17 -21,-0.5 2,-0.3 -2,-0.3 -21,-0.1 -0.646 58.7 -82.4-163.9-137.2 -1.3 -0.5 -6.7 30 30 A N - 0 0 87 -23,-0.2 -6,-1.7 -2,-0.2 2,-0.4 -0.907 27.4-118.6-145.3 173.0 -3.7 1.4 -4.3 31 31 A c B C 23 0C 1 -25,-0.5 -26,-1.8 -2,-0.3 -8,-0.2 -0.942 360.0 360.0-121.1 141.0 -5.1 1.1 -0.7 32 32 A S 0 0 90 -10,-1.0 -10,-0.1 -2,-0.4 -2,-0.1 -0.879 360.0 360.0-174.1 360.0 -8.7 0.7 0.3