==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=20-JUL-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE/HYDROLASE INHIBITOR 05-JAN-91 3ER5 . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR D.BAILEY,B.VEERAPANDIAN,J.COOPER,M.SZELKE,T.L.BLUNDELL . 340 2 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13312.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 237 69.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 17 5.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 106 31.2 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 1 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 2 0.6 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 . 47 13.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 34 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 18 5.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 0.6 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 3 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 RESIDUES PER ALPHA HELIX . 1 1 3 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 . 3 4 4 3 3 2 1 0 0 0 1 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 1 0 1 0 1 1 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 -2 E S 0 0 62 0, 0.0 152,-1.8 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 159.7 27.9 32.9 -2.7 2 -1 E T - 0 0 56 150,-0.2 2,-0.3 96,-0.2 170,-0.2 -0.949 360.0-151.6-143.0 171.2 25.9 30.4 -0.8 3 0 E G E -A 171 0A 2 168,-2.1 168,-3.0 -2,-0.3 2,-0.3 -0.989 3.8-167.4-142.7 153.2 25.3 29.3 2.9 4 1 E S E +A 170 0A 63 93,-1.7 2,-0.4 -2,-0.3 166,-0.2 -0.972 12.6 173.4-141.0 123.0 24.3 26.0 4.5 5 2 E A E -A 169 0A 10 164,-2.1 164,-2.6 -2,-0.3 2,-0.3 -0.987 28.7-123.4-132.3 147.9 23.3 25.6 8.2 6 3 E T E -A 168 0A 80 -2,-0.4 2,-0.4 162,-0.2 162,-0.3 -0.690 22.2-157.0 -83.9 135.1 21.9 22.8 10.3 7 4 E T E -A 167 0A 0 160,-1.3 160,-2.9 -2,-0.3 155,-0.2 -0.951 8.1-167.9-115.4 134.7 18.6 23.4 12.0 8 5 E T E -F 18 0B 68 10,-2.4 10,-2.7 -2,-0.4 153,-0.0 -0.928 25.8-112.4-121.3 138.4 17.7 21.4 15.1 9 6 E P E -F 17 0B 21 0, 0.0 8,-0.3 0, 0.0 154,-0.0 -0.465 22.7-132.5 -68.0 155.1 14.2 21.1 16.9 10 7 E I S S+ 0 0 29 6,-2.8 2,-0.3 -2,-0.0 7,-0.1 0.617 80.3 4.8 -81.9 -15.1 14.2 22.7 20.3 11 8 E D S > S- 0 0 60 5,-0.4 3,-1.1 0, 0.0 5,-0.1 -0.868 89.1 -81.5-159.3-176.7 12.5 19.7 21.9 12 9 E S T 3 S+ 0 0 101 -2,-0.3 -2,-0.0 1,-0.2 0, 0.0 0.559 121.7 56.0 -76.8 -6.3 11.2 16.1 21.4 13 10 E L T 3 S- 0 0 28 3,-0.1 -1,-0.2 268,-0.0 151,-0.0 0.514 105.0-121.7 -96.5 -9.1 8.0 17.4 19.9 14 11 E D < + 0 0 0 -3,-1.1 3,-0.1 2,-0.1 -2,-0.1 0.906 53.9 158.8 57.8 45.6 9.5 19.6 17.1 15 12 E D - 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0 0 61 -2,-0.2 2,-0.5 -5,-0.1 -3,-0.2 -0.290 32.1-162.7 -57.3 132.1 31.4 36.5 15.8 28 25 E Q E < -G 23 0C 34 -5,-2.4 -5,-3.5 -2,-0.1 2,-0.6 -0.948 17.5-143.6-109.0 126.8 28.9 36.0 18.6 29 26 E T E +G 22 0C 72 -2,-0.5 2,-0.4 -7,-0.3 -7,-0.2 -0.801 23.7 173.6 -95.4 118.7 26.8 32.8 17.9 30 27 E L E -G 21 0C 1 -9,-2.8 -9,-2.7 -2,-0.6 2,-0.8 -0.955 33.0-122.4-117.8 151.5 23.2 32.9 18.9 31 28 E N E -G 20 0C 59 -2,-0.4 92,-2.7 -11,-0.2 93,-0.4 -0.844 36.8-169.5 -97.7 109.5 20.6 30.2 18.1 32 29 E L E -G 19 0C 0 -13,-2.4 -13,-2.7 -2,-0.8 2,-0.8 -0.760 25.4-125.7-105.1 148.0 17.8 31.8 16.1 33 30 E D E -i 125 0C 2 91,-2.3 93,-2.2 -2,-0.3 2,-0.5 -0.791 27.4-137.7 -85.8 111.1 14.3 30.6 15.1 34 31 E F E -i 126 0C 1 -2,-0.8 2,-0.6 -17,-0.5 93,-0.2 -0.638 25.4-169.8 -77.5 113.4 14.1 31.0 11.3 35 32 E D E > -i 127 0C 0 91,-2.6 93,-2.5 -2,-0.5 3,-1.3 -0.886 23.8-177.7-119.3 91.3 10.5 32.4 10.8 36 33 E T T 3 S+ 0 0 0 -2,-0.6 159,-0.5 1,-0.3 94,-0.2 0.541 84.8 66.3 -71.8 3.8 9.1 32.6 7.2 37 34 E G T 3 S+ 0 0 0 92,-0.1 301,-2.7 157,-0.1 2,-0.3 0.187 104.6 37.9-111.7 32.9 6.0 34.2 8.8 38 35 E S < - 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0 0 61 61,-2.1 3,-2.1 -2,-0.2 -1,-0.1 -0.188 36.6-131.6 -44.8 120.4 15.7 44.0 30.9 50 47 E A G > S+ 0 0 88 1,-0.3 3,-2.0 2,-0.2 -1,-0.1 0.862 102.8 56.5 -46.4 -52.0 17.7 41.7 33.1 51 48 E S G 3 S+ 0 0 107 1,-0.3 -1,-0.3 3,-0.0 -2,-0.1 0.651 102.5 59.5 -61.5 -12.7 14.6 40.1 34.9 52 49 E E G < S+ 0 0 55 -3,-2.1 2,-0.5 1,-0.1 -1,-0.3 0.185 85.1 89.7-103.1 17.5 13.3 39.1 31.4 53 50 E V < + 0 0 49 -3,-2.0 2,-0.5 -5,-0.1 64,-0.1 -0.906 47.4 173.7-121.1 105.9 16.4 36.9 30.5 54 51 E D S S- 0 0 79 -2,-0.5 -3,-0.0 63,-0.4 -4,-0.0 -0.783 73.5 -39.4-121.2 86.7 16.2 33.0 31.5 55 52 E G S S+ 0 0 71 -2,-0.5 -1,-0.1 1,-0.3 63,-0.1 0.209 96.1 135.2 88.2 -7.6 19.2 31.0 30.1 56 53 E Q - 0 0 16 61,-0.2 2,-0.4 1,-0.1 -1,-0.3 -0.327 57.7-117.3 -73.6 153.9 19.4 32.7 26.6 57 54 E T - 0 0 71 63,-0.2 2,-0.3 -26,-0.1 -13,-0.3 -0.742 35.6-147.0 -85.9 134.4 22.7 33.8 24.9 58 55 E I - 0 0 61 -2,-0.4 2,-0.5 -15,-0.1 -13,-0.3 -0.749 10.0-126.0-111.7 156.5 22.7 37.5 24.4 59 56 E Y B -o 45 0D 0 -15,-2.0 -13,-2.1 -2,-0.3 -12,-0.3 -0.837 18.5-161.8 -94.5 122.5 24.2 39.8 21.7 60 57 E T > - 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