==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=2-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER ANTIMICROBIAL PROTEIN 20-NOV-06 2NY9 . COMPND 2 MOLECULE: DEFENSIN, MUTANT DEF-ABB; . SOURCE 2 ORGANISM_SCIENTIFIC: ANOPHELES GAMBIAE; . AUTHOR C.LANDON,F.BARBAULT,F.VOVELLE . 41 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3128.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 26 63.4 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 . 7 17.1 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 . 1 2.4 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 12.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 2.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 9 22.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 4.9 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 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 . 1 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 X A 0 0 139 0, 0.0 33,-0.1 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 146.7 -2.6 5.8 -9.5 2 2 X T + 0 0 41 31,-0.1 2,-0.4 2,-0.1 14,-0.1 0.900 360.0 53.9 -71.1 -42.7 -1.4 5.2 -6.0 3 3 X a + 0 0 14 30,-0.3 9,-0.2 12,-0.1 2,-0.2 -0.769 64.3 127.9 -99.5 141.4 0.4 8.6 -5.7 4 4 X D - 0 0 96 7,-2.5 29,-0.1 -2,-0.4 -2,-0.1 -0.492 62.8 -93.9-153.0-137.5 -1.3 11.9 -6.5 5 5 X L S >S+ 0 0 127 -2,-0.2 5,-0.7 7,-0.0 2,-0.3 0.595 113.8 56.3-126.6 -45.4 -1.6 15.2 -4.7 6 6 X A T 5 + 0 0 86 1,-0.2 2,-1.8 3,-0.1 5,-0.1 -0.030 69.9 133.5 -82.3 33.5 -4.9 15.0 -2.8 7 7 X S T 5S- 0 0 38 3,-0.3 4,-0.4 -2,-0.3 5,-0.3 -0.347 98.6 -62.3 -81.9 54.9 -3.5 11.9 -1.2 8 8 X G T 5S- 0 0 68 -2,-1.8 -1,-0.2 1,-0.2 -2,-0.1 0.931 103.7 -47.6 65.5 45.6 -4.7 13.0 2.3 9 9 X F T 5S+ 0 0 218 -4,-0.2 -1,-0.2 1,-0.2 2,-0.2 0.938 134.4 63.2 59.3 49.9 -2.4 16.1 2.2 10 10 X G S S+ 0 0 4 -5,-0.3 4,-1.6 -9,-0.2 19,-0.1 0.521 84.4 126.2 142.0 33.3 0.3 8.4 -1.3 13 13 X S H > S+ 0 0 53 -6,-0.2 4,-2.7 2,-0.2 5,-0.2 0.925 78.4 49.2 -78.2 -46.6 2.4 6.8 1.4 14 14 X S H > S+ 0 0 96 -7,-0.2 4,-2.6 2,-0.2 5,-0.3 0.934 116.5 42.7 -58.1 -48.4 -0.4 5.7 3.7 15 15 X L H > S+ 0 0 93 1,-0.2 4,-3.6 2,-0.2 5,-0.4 0.952 112.4 54.1 -62.2 -49.7 -2.3 4.2 0.8 16 16 X b H X S+ 0 0 0 -4,-1.6 4,-1.7 1,-0.2 13,-0.2 0.883 112.6 44.7 -50.8 -44.5 0.8 2.6 -0.6 17 17 X A H X S+ 0 0 24 -4,-2.7 4,-1.7 11,-0.6 10,-0.2 0.981 118.3 40.0 -65.6 -59.1 1.5 1.0 2.8 18 18 X A H X S+ 0 0 51 -4,-2.6 4,-1.2 1,-0.2 -2,-0.2 0.915 116.0 51.7 -56.2 -48.2 -2.1 -0.3 3.5 19 19 X H H X S+ 0 0 73 -4,-3.6 4,-0.8 -5,-0.3 3,-0.3 0.872 112.5 45.5 -58.4 -40.5 -2.5 -1.3 -0.1 20 20 X c H X>S+ 0 0 4 -4,-1.7 4,-2.7 -5,-0.4 5,-2.3 0.749 100.3 68.3 -77.9 -21.7 0.7 -3.3 -0.1 21 21 X L H <5S+ 0 0 75 -4,-1.7 -1,-0.2 1,-0.2 -2,-0.2 0.866 97.1 56.0 -62.0 -34.3 -0.2 -4.8 3.3 22 22 X V H <5S+ 0 0 129 -4,-1.2 -1,-0.2 -3,-0.3 -2,-0.2 0.899 109.2 44.5 -62.3 -45.3 -2.9 -6.7 1.4 23 23 X K H <5S- 0 0 139 -4,-0.8 -2,-0.2 1,-0.0 -1,-0.2 0.942 132.4 -82.7 -67.3 -50.0 -0.4 -8.2 -1.0 24 24 X G T <5S+ 0 0 1 -4,-2.7 17,-2.0 1,-0.1 2,-0.3 0.458 82.6 128.6 148.6 32.0 2.2 -9.1 1.6 25 25 X Y B < -A 40 0A 65 -5,-2.3 15,-0.2 15,-0.2 14,-0.2 -0.749 48.8-147.9-108.7 156.5 4.3 -6.2 2.5 26 26 X R S S+ 0 0 142 13,-1.7 2,-0.3 12,-1.3 13,-0.2 0.049 81.4 11.5-107.9 22.2 5.1 -4.8 5.9 27 27 X G - 0 0 7 11,-0.4 11,-2.4 -10,-0.2 2,-0.3 -0.899 55.9-164.6 174.1 158.2 5.4 -1.2 4.7 28 28 X G E +B 37 0B 11 9,-0.3 -11,-0.6 -2,-0.3 2,-0.3 -0.934 9.3 172.7-161.8 133.5 4.8 1.2 1.8 29 29 X Y E -B 36 0B 108 7,-2.8 7,-2.9 -2,-0.3 2,-0.6 -0.997 28.9-126.3-146.4 139.0 5.9 4.7 0.9 30 30 X a E +B 35 0B 18 -2,-0.3 2,-0.4 5,-0.3 5,-0.3 -0.763 34.2 169.3 -90.1 121.7 5.6 6.9 -2.1 31 31 X K E > +B 34 0B 126 3,-2.7 3,-0.8 -2,-0.6 -2,-0.1 -0.998 66.7 5.5-134.1 134.1 8.8 8.2 -3.5 32 32 X N T 3 S- 0 0 128 -2,-0.4 -1,-0.1 1,-0.3 3,-0.1 0.841 132.1 -60.9 62.4 34.9 9.4 10.0 -6.8 33 33 X K T 3 S+ 0 0 119 1,-0.2 2,-0.4 -3,-0.1 -30,-0.3 0.775 118.1 110.9 63.0 29.7 5.6 9.9 -7.2 34 34 X I E < S-B 31 0B 92 -3,-0.8 -3,-2.7 -32,-0.1 2,-0.7 -0.997 74.1-118.2-138.1 132.4 5.7 6.1 -7.2 35 35 X b E -B 30 0B 27 -2,-0.4 2,-0.6 -5,-0.3 -5,-0.3 -0.554 33.6-173.8 -70.3 109.9 4.4 3.7 -4.5 36 36 X H E -B 29 0B 65 -7,-2.9 -7,-2.8 -2,-0.7 2,-0.2 -0.930 6.9-158.2-111.8 113.6 7.4 1.8 -3.2 37 37 X c E -B 28 0B 36 -2,-0.6 2,-0.3 -9,-0.3 -9,-0.3 -0.504 4.1-155.2 -89.1 158.7 6.6 -1.0 -0.9 38 38 X R + 0 0 144 -11,-2.4 -12,-1.3 1,-0.2 -11,-0.4 -0.980 56.9 27.5-137.6 149.9 9.0 -2.5 1.7 39 39 X D - 0 0 113 -2,-0.3 -13,-1.7 -14,-0.2 2,-0.7 0.996 59.9-165.4 66.2 83.8 9.4 -5.9 3.5 40 40 X K B A 25 0A 119 -15,-0.2 -15,-0.2 1,-0.1 -1,-0.2 -0.871 360.0 360.0-100.8 113.4 7.8 -8.6 1.3 41 41 X F 0 0 163 -17,-2.0 -1,-0.1 -2,-0.7 -16,-0.1 0.641 360.0 360.0 -90.1 360.0 7.3 -11.8 3.3