==== 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 12-NOV-90 2ER7 . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR B.VEERAPANDIAN,J.B.COOPER,M.SZELKE,T.L.BLUNDELL . 337 2 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13086.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 233 69.1 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 . 109 32.3 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 . 3 0.9 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 . 40 11.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 34 10.1 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 . 4 3 5 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 59 0, 0.0 152,-1.9 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 154.5 27.8 33.0 -2.6 2 -1 E T - 0 0 58 150,-0.2 2,-0.3 96,-0.1 170,-0.2 -0.947 360.0-160.0-135.0 169.6 25.8 30.4 -0.8 3 0 E G E -A 171 0A 3 168,-2.1 168,-2.9 -2,-0.3 2,-0.3 -0.990 2.6-168.2-143.7 161.8 25.3 29.3 2.8 4 1 E S E +A 170 0A 61 93,-1.8 2,-0.3 -2,-0.3 166,-0.2 -0.942 10.9 179.0-148.5 126.4 24.1 26.1 4.5 5 2 E A E -A 169 0A 9 164,-2.2 164,-2.7 -2,-0.3 2,-0.4 -0.983 27.9-121.4-134.0 140.9 23.1 25.8 8.2 6 3 E T E -A 168 0A 81 -2,-0.3 2,-0.4 162,-0.2 162,-0.3 -0.638 24.5-159.1 -75.8 127.1 21.8 22.9 10.4 7 4 E T E -A 167 0A 0 160,-1.8 160,-3.1 -2,-0.4 155,-0.3 -0.963 9.4-167.1-110.1 137.6 18.5 23.6 12.0 8 5 E T E -F 18 0B 63 10,-2.5 10,-2.6 -2,-0.4 153,-0.0 -0.932 25.2-108.9-125.6 139.0 17.6 21.5 15.1 9 6 E P E -F 17 0B 22 0, 0.0 8,-0.3 0, 0.0 154,-0.0 -0.414 22.1-138.3 -64.4 148.4 14.3 21.0 17.0 10 7 E I S S+ 0 0 30 6,-2.4 2,-0.2 2,-0.0 7,-0.1 0.660 80.7 5.4 -81.0 -18.7 14.3 22.7 20.4 11 8 E D S > S- 0 0 54 5,-0.4 3,-1.1 0, 0.0 5,-0.1 -0.826 89.3 -85.7-155.8-176.5 12.6 19.8 22.1 12 9 E S T 3 S+ 0 0 102 1,-0.2 -2,-0.0 -2,-0.2 0, 0.0 0.520 120.7 59.5 -85.1 3.0 11.3 16.2 21.4 13 10 E L T 3 S- 0 0 33 3,-0.1 -1,-0.2 319,-0.0 151,-0.0 0.490 104.8-123.4 -98.0 -3.8 8.0 17.5 20.0 14 11 E D < + 0 0 0 -3,-1.1 3,-0.1 2,-0.1 -2,-0.1 0.904 53.7 158.5 56.1 42.7 9.5 19.6 17.1 15 12 E D - 0 0 0 1,-0.2 319,-0.6 318,-0.1 2,-0.3 0.877 68.2 -19.9 -63.3 -33.6 7.7 22.7 18.6 16 13 E A - 0 0 2 317,-0.1 -6,-2.4 -5,-0.1 -5,-0.4 -0.953 65.5-122.7-164.0 169.8 10.2 24.9 16.8 17 14 E Y E -F 9 0B 4 -2,-0.3 17,-0.4 -8,-0.3 2,-0.3 -0.957 15.7-154.6-126.8 139.3 13.7 24.8 15.2 18 15 E I E -F 8 0B 23 -10,-2.6 -10,-2.5 -2,-0.4 15,-0.2 -0.896 4.8-167.6-115.6 150.8 16.7 26.8 16.0 19 16 E T E -G 32 0C 0 13,-2.3 13,-2.2 -2,-0.3 -12,-0.2 -0.996 27.3-116.5-134.1 123.8 19.6 27.7 13.6 20 17 E P E -G 31 0C 50 0, 0.0 2,-0.4 0, 0.0 77,-0.4 -0.421 32.7-174.1 -64.6 137.2 22.9 29.2 14.8 21 18 E V E -G 30 0C 0 9,-3.0 9,-2.9 75,-0.1 2,-0.6 -0.999 17.9-138.0-133.9 136.2 23.7 32.6 13.4 22 19 E Q E -GH 29 95C 55 73,-2.3 73,-2.9 -2,-0.4 2,-0.5 -0.818 22.8-173.0 -94.6 123.3 26.9 34.6 13.9 23 20 E I E > -GH 28 94C 0 5,-3.0 5,-2.1 -2,-0.6 71,-0.2 -0.955 41.2 -9.5-124.7 131.1 26.5 38.2 14.6 24 21 E G T 5S- 0 0 7 69,-2.9 40,-0.1 -2,-0.5 71,-0.1 -0.171 90.3 -38.6 85.4-176.4 29.1 40.9 14.8 25 22 E T T 5S+ 0 0 54 2,-0.1 40,-2.6 1,-0.1 41,-0.3 -0.984 132.6 26.0-136.3 117.4 32.9 40.9 14.9 26 23 E P T 5S- 0 0 98 0, 0.0 -1,-0.1 0, 0.0 2,-0.1 0.699 120.9-103.1 -62.5 168.5 34.3 38.8 16.4 27 24 E A T 5 - 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0 0 56 61,-2.4 3,-2.2 -2,-0.2 63,-0.1 -0.291 35.9-127.0 -55.2 128.0 15.8 44.3 31.0 50 47 E A G > S+ 0 0 85 1,-0.3 3,-1.8 2,-0.2 -1,-0.1 0.785 103.7 57.1 -48.4 -46.4 17.6 41.9 33.2 51 48 E S G 3 S+ 0 0 108 1,-0.3 -1,-0.3 3,-0.0 -2,-0.1 0.559 103.1 58.9 -70.1 -2.4 14.6 40.3 34.9 52 49 E E G < S+ 0 0 54 -3,-2.2 2,-0.5 -4,-0.1 -1,-0.3 0.244 85.6 87.8-110.0 10.8 13.3 39.3 31.4 53 50 E V < + 0 0 48 -3,-1.8 2,-0.2 -5,-0.1 64,-0.1 -0.979 48.0 168.5-116.2 116.0 16.4 37.3 30.5 54 51 E D S S- 0 0 82 -2,-0.5 -3,-0.0 63,-0.4 -4,-0.0 -0.691 73.8 -35.9-136.9 71.6 16.1 33.4 31.7 55 52 E G S S+ 0 0 69 1,-0.3 65,-0.1 -2,-0.2 63,-0.1 0.051 96.4 130.4 105.1 -20.2 19.0 31.3 30.1 56 53 E Q - 0 0 16 61,-0.2 2,-0.5 66,-0.1 -1,-0.3 -0.189 60.6-114.6 -67.7 157.2 19.3 32.9 26.6 57 54 E T - 0 0 71 63,-0.1 2,-0.3 -26,-0.1 -13,-0.3 -0.807 36.0-147.9 -90.2 126.6 22.6 34.0 24.9 58 55 E I - 0 0 62 -2,-0.5 2,-0.4 -15,-0.1 -13,-0.3 -0.728 8.2-128.3-102.4 146.9 22.6 37.8 24.5 59 56 E Y B -o 45 0D 0 -15,-2.3 -13,-2.1 -2,-0.3 -12,-0.3 -0.800 18.6-159.1 -86.5 135.0 24.2 39.9 21.8 60 57 E T > - 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