==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=24-JUL-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER ANTIBIOTIC 25-APR-00 1EWF . COMPND 2 MOLECULE: BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR G.KLEIGER,L.J.BEAMER,R.GROTHE,P.MALLICK,D.EISENBERG . 456 1 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 22209.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 325 71.3 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 . 163 35.7 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 0.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 4 0.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 6 1.3 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 . 36 7.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 25 5.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 83 18.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 8 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 1 2 0 0 0 0 2 1 0 1 0 0 0 0 0 1 0 0 1 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 . 2 2 3 1 4 5 1 0 2 1 1 0 0 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 0 1 0 2 0 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 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 V 0 0 110 0, 0.0 210,-0.0 0, 0.0 209,-0.0 0.000 360.0 360.0 360.0 -52.7 98.7 12.7 13.7 2 2 A N - 0 0 81 241,-0.1 241,-0.1 208,-0.1 2,-0.1 -0.854 360.0-169.0-114.4 93.9 96.0 15.3 14.0 3 3 A P - 0 0 11 0, 0.0 222,-0.2 0, 0.0 223,-0.1 -0.379 29.5-128.7 -76.5 165.0 97.0 18.1 16.3 4 4 A G S S+ 0 0 1 220,-1.1 255,-2.1 221,-0.9 258,-0.4 0.765 98.5 21.7 -76.6 -28.7 94.7 20.9 17.7 5 5 A V E -AB 224 258A 0 219,-1.8 219,-3.0 253,-0.2 2,-0.4 -1.000 69.9-165.8-142.3 135.9 97.2 23.5 16.4 6 6 A V E -AB 223 257A 10 251,-1.9 251,-3.0 -2,-0.4 2,-0.5 -0.977 6.8-161.3-126.0 140.9 99.9 23.3 13.8 7 7 A V E -AB 222 256A 20 215,-2.2 215,-3.3 -2,-0.4 2,-0.5 -0.990 12.8-168.0-119.2 114.9 102.8 25.8 13.1 8 8 A R E -AB 221 255A 29 247,-3.0 247,-2.5 -2,-0.5 2,-0.5 -0.934 6.5-155.0-105.5 121.6 104.3 25.4 9.6 9 9 A I E -AB 220 254A 33 211,-3.4 211,-2.0 -2,-0.5 245,-0.2 -0.870 13.1-150.8 -99.5 126.7 107.6 27.1 8.9 10 10 A S E > -A 219 0A 1 243,-2.1 4,-2.4 -2,-0.5 5,-0.2 -0.358 33.3 -99.7 -87.4 172.9 108.2 27.9 5.2 11 11 A Q H > S+ 0 0 59 207,-0.5 4,-2.6 1,-0.2 5,-0.2 0.886 126.2 58.5 -61.0 -36.0 111.5 28.2 3.4 12 12 A K H > S+ 0 0 60 240,-0.3 4,-1.9 1,-0.2 -1,-0.2 0.925 107.1 45.6 -59.5 -43.2 111.1 32.0 3.8 13 13 A G H > S+ 0 0 7 240,-0.4 4,-2.6 239,-0.4 -1,-0.2 0.896 113.3 48.0 -67.9 -38.9 110.9 31.6 7.6 14 14 A L H X S+ 0 0 10 -4,-2.4 4,-2.3 2,-0.2 -1,-0.2 0.853 107.6 56.9 -70.0 -31.0 113.9 29.2 7.6 15 15 A D H X S+ 0 0 86 -4,-2.6 4,-1.7 -5,-0.2 -2,-0.2 0.901 111.6 43.9 -63.8 -42.1 115.8 31.8 5.4 16 16 A Y H X S+ 0 0 40 -4,-1.9 4,-2.1 -5,-0.2 -2,-0.2 0.918 112.0 50.9 -68.4 -41.9 115.1 34.4 8.1 17 17 A A H X S+ 0 0 41 -4,-2.6 4,-2.7 1,-0.2 5,-0.3 0.911 107.6 55.2 -62.3 -36.3 116.0 32.0 10.9 18 18 A S H X S+ 0 0 4 -4,-2.3 4,-2.4 1,-0.2 -1,-0.2 0.938 106.3 50.6 -60.0 -46.3 119.3 31.2 9.1 19 19 A Q H X S+ 0 0 112 -4,-1.7 4,-1.7 1,-0.2 -1,-0.2 0.878 112.7 46.7 -60.3 -41.4 120.2 35.0 9.0 20 20 A Q H X S+ 0 0 48 -4,-2.1 4,-1.8 2,-0.2 -1,-0.2 0.899 113.1 46.6 -71.0 -41.5 119.6 35.3 12.7 21 21 A G H X S+ 0 0 41 -4,-2.7 4,-2.7 1,-0.2 -2,-0.2 0.850 110.4 54.7 -69.9 -30.8 121.5 32.2 13.7 22 22 A T H X S+ 0 0 12 -4,-2.4 4,-2.5 -5,-0.3 -1,-0.2 0.904 105.2 53.6 -67.8 -38.0 124.4 33.3 11.5 23 23 A A H X S+ 0 0 39 -4,-1.7 4,-1.1 2,-0.2 -2,-0.2 0.932 112.1 44.0 -61.8 -45.5 124.5 36.7 13.2 24 24 A A H >X S+ 0 0 43 -4,-1.8 4,-1.4 1,-0.2 3,-0.6 0.943 114.1 49.7 -64.0 -46.3 124.9 35.0 16.6 25 25 A L H 3X S+ 0 0 11 -4,-2.7 4,-2.6 1,-0.2 5,-0.2 0.853 102.8 62.1 -61.6 -35.3 127.4 32.5 15.3 26 26 A Q H 3X S+ 0 0 59 -4,-2.5 4,-1.7 1,-0.2 -1,-0.2 0.858 102.3 50.1 -59.7 -38.7 129.5 35.3 13.7 27 27 A K H << S+ 0 0 124 -4,-1.1 4,-0.4 -3,-0.6 -1,-0.2 0.893 113.5 46.1 -68.5 -38.5 130.2 36.9 17.1 28 28 A E H >< S+ 0 0 12 -4,-1.4 3,-0.8 1,-0.2 -2,-0.2 0.851 110.6 51.9 -72.2 -35.9 131.3 33.6 18.6 29 29 A L H >< S+ 0 0 0 -4,-2.6 3,-2.0 1,-0.3 -1,-0.2 0.888 101.9 60.8 -66.8 -38.2 133.5 32.6 15.6 30 30 A K T 3< S+ 0 0 81 -4,-1.7 28,-0.4 1,-0.3 -1,-0.3 0.689 98.5 60.0 -62.5 -17.0 135.2 35.9 15.9 31 31 A R T < S+ 0 0 152 -3,-0.8 -1,-0.3 -4,-0.4 -2,-0.2 0.414 72.1 128.8 -91.4 -2.1 136.2 34.9 19.4 32 32 A I < - 0 0 10 -3,-2.0 2,-0.8 -4,-0.1 26,-0.4 -0.314 58.3-135.0 -53.4 134.4 138.2 31.8 18.3 33 33 A K - 0 0 77 24,-0.1 -1,-0.1 140,-0.0 24,-0.1 -0.861 17.0-148.6 -97.9 111.2 141.6 32.0 19.8 34 34 A I - 0 0 16 -2,-0.8 22,-0.4 22,-0.4 21,-0.1 -0.651 16.7-122.4 -83.0 131.6 144.2 31.1 17.1 35 35 A P - 0 0 45 0, 0.0 2,-0.2 0, 0.0 -1,-0.1 -0.286 24.7-107.7 -68.0 155.1 147.4 29.3 18.4 36 36 A D - 0 0 96 18,-0.1 2,-0.4 19,-0.1 18,-0.2 -0.571 31.4-149.0 -77.1 149.5 150.9 30.8 17.8 37 37 A Y E +G 53 0B 37 16,-2.7 16,-2.7 -2,-0.2 2,-0.3 -0.983 19.2 174.2-124.8 122.0 153.0 28.8 15.2 38 38 A S E +G 52 0B 87 -2,-0.4 2,-0.3 14,-0.2 14,-0.2 -0.906 6.7 152.2-125.9 154.8 156.8 28.6 15.4 39 39 A D E -G 51 0B 57 12,-2.1 12,-2.5 -2,-0.3 2,-0.3 -0.947 31.6-112.1-162.7-179.7 159.3 26.6 13.3 40 40 A S E -G 50 0B 42 -2,-0.3 2,-0.3 10,-0.2 10,-0.3 -0.815 24.8-169.7-123.4 165.2 162.9 26.5 12.0 41 41 A F - 0 0 8 8,-2.3 2,-0.2 7,-0.5 3,-0.0 -0.946 31.9-154.7-148.9 171.2 164.6 26.8 8.6 42 42 A K S S+ 0 0 183 -2,-0.3 6,-0.2 2,-0.0 2,-0.2 -0.768 71.1 102.7-144.7 74.3 167.8 26.4 6.6 43 43 A I - 0 0 54 4,-1.9 114,-0.1 -2,-0.2 5,-0.0 -0.606 69.3-104.5-172.3 98.8 166.8 29.0 4.0 44 44 A K S S+ 0 0 52 -2,-0.2 -2,-0.0 1,-0.2 109,-0.0 0.764 73.6 133.1 -20.7 178.4 168.3 32.5 4.0 45 45 A H S S- 0 0 34 108,-0.0 -1,-0.2 109,-0.0 50,-0.1 -0.486 140.2 -22.4 146.6 -9.3 167.9 36.2 4.8 46 46 A L S S- 0 0 105 48,-0.1 3,-0.4 1,-0.0 -3,-0.2 0.035 96.2 -99.0 141.7 106.2 171.0 34.3 5.9 47 47 A G S S+ 0 0 32 1,-0.2 -4,-1.9 -5,-0.1 -1,-0.0 0.324 92.1 63.8 6.4 -74.5 170.8 30.4 6.3 48 48 A K S S+ 0 0 106 -6,-0.2 -7,-0.5 -3,-0.1 47,-0.2 0.811 70.3 82.6 -27.3 -93.5 170.3 29.5 10.0 49 49 A G - 0 0 7 -3,-0.4 -8,-2.3 1,-0.1 2,-0.3 0.936 52.7-106.2 -11.4-166.2 167.2 30.4 12.1 50 50 A H E -GH 40 94B 130 44,-1.3 44,-2.8 -10,-0.3 2,-0.3 -0.910 24.2-170.5-138.8 162.0 163.8 30.2 13.5 51 51 A Y E -GH 39 93B 6 -12,-2.5 -12,-2.1 -2,-0.3 2,-0.3 -0.966 3.1-161.2-154.5 165.0 160.7 32.2 13.0 52 52 A S E -GH 38 92B 6 40,-2.3 40,-1.6 -2,-0.3 2,-0.5 -0.987 16.1-153.0-154.2 146.4 157.2 32.5 14.4 53 53 A F E +GH 37 91B 1 -16,-2.7 -16,-2.7 -2,-0.3 2,-0.3 -0.988 45.8 155.3-115.2 115.4 153.7 33.9 13.5 54 54 A Y E + H 0 90B 57 36,-3.2 36,-2.7 -2,-0.5 -18,-0.1 -0.826 31.3 38.3-143.0 177.5 152.0 34.9 16.8 55 55 A S E S+ 0 0 74 -2,-0.3 2,-0.2 34,-0.2 -1,-0.2 0.903 71.2 179.3 46.3 49.1 149.5 36.9 18.8 56 56 A M E - 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