==== 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 27-JUL-94 1EPM . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR M.CRAWFORD,J.B.COOPER,P.STROP,T.L.BLUNDELL . 338 2 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13161.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 237 70.1 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 32.2 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 . 44 13.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 35 10.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 19 5.6 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 2 2 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,-2.1 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 165.1 27.9 32.8 -2.7 2 -1 E T - 0 0 59 150,-0.2 2,-0.3 96,-0.1 170,-0.2 -0.886 360.0-154.5-144.3 167.5 26.0 30.1 -0.8 3 0 E G E -A 171 0A 3 168,-2.0 168,-2.9 -2,-0.3 2,-0.3 -0.993 6.0-174.1-143.6 149.6 25.3 29.2 2.8 4 1 E S E +A 170 0A 64 93,-1.5 2,-0.4 -2,-0.3 166,-0.2 -0.963 11.0 171.8-147.2 123.6 24.3 25.8 4.5 5 2 E A E -A 169 0A 10 164,-2.4 164,-2.4 -2,-0.3 2,-0.4 -0.991 31.0-119.9-134.6 148.5 23.4 25.4 8.2 6 3 E T E -A 168 0A 83 -2,-0.4 2,-0.4 162,-0.2 162,-0.3 -0.647 24.9-158.2 -87.5 132.8 22.0 22.6 10.3 7 4 E T E -A 167 0A 0 160,-2.0 160,-3.1 -2,-0.4 155,-0.2 -0.934 9.6-168.0-110.4 134.1 18.7 23.3 12.0 8 5 E T E -F 18 0B 52 10,-2.3 10,-2.8 -2,-0.4 153,-0.0 -0.966 25.6-108.0-129.8 142.6 17.7 21.3 15.1 9 6 E P E -F 17 0B 30 0, 0.0 8,-0.3 0, 0.0 3,-0.0 -0.296 22.0-138.0 -67.9 146.2 14.4 20.9 17.0 10 7 E I S S+ 0 0 27 6,-2.7 2,-0.3 3,-0.0 7,-0.1 0.664 79.7 4.5 -80.9 -8.9 14.3 22.6 20.3 11 8 E D S > S- 0 0 57 5,-0.4 3,-1.0 110,-0.0 5,-0.1 -0.885 89.2 -82.2-154.9-172.0 12.6 19.6 22.1 12 9 E S T 3 S+ 0 0 100 -2,-0.3 -2,-0.0 1,-0.3 0, 0.0 0.609 120.8 53.8 -81.0 -10.6 11.3 16.1 21.6 13 10 E L T 3 S- 0 0 43 319,-0.0 -1,-0.3 268,-0.0 151,-0.0 0.260 108.4-116.1-100.3 -2.7 8.0 17.2 20.0 14 11 E D < + 0 0 0 -3,-1.0 -2,-0.1 2,-0.1 3,-0.1 0.903 54.5 161.7 69.9 38.7 9.5 19.5 17.2 15 12 E D - 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0 0 63 -2,-0.2 2,-0.5 -5,-0.1 -3,-0.2 -0.200 30.3-162.3 -65.5 137.1 31.4 36.5 16.0 28 25 E Q E < -G 23 0C 35 -5,-1.9 -5,-2.6 -4,-0.1 2,-0.6 -0.962 20.4-141.8-111.3 120.5 28.9 35.9 18.8 29 26 E T E +G 22 0C 71 -2,-0.5 2,-0.3 -7,-0.2 -7,-0.2 -0.731 24.4 175.2 -94.6 127.7 26.9 32.7 18.0 30 27 E L E -G 21 0C 0 -9,-2.6 -9,-2.9 -2,-0.6 2,-0.7 -0.939 31.1-126.3-127.6 144.5 23.2 32.8 18.9 31 28 E N E -G 20 0C 62 -2,-0.3 92,-2.9 -11,-0.2 93,-0.4 -0.919 36.9-173.6 -96.9 112.3 20.5 30.1 18.1 32 29 E L E -G 19 0C 0 -13,-2.4 -13,-2.3 -2,-0.7 2,-0.8 -0.760 28.8-122.0-111.1 155.0 17.7 31.8 16.2 33 30 E D E -i 125 0C 3 91,-2.2 93,-2.1 -2,-0.3 2,-0.5 -0.816 27.5-139.1 -92.9 109.9 14.3 30.5 15.1 34 31 E F E -i 126 0C 1 -2,-0.8 2,-0.6 -17,-0.4 93,-0.2 -0.624 25.8-169.2 -71.8 110.0 14.1 31.0 11.3 35 32 E D E > -i 127 0C 0 91,-3.0 93,-3.1 -2,-0.5 3,-1.3 -0.918 27.2-175.1-118.5 104.9 10.5 32.2 10.7 36 33 E T T 3 S+ 0 0 0 -2,-0.6 159,-0.5 1,-0.2 94,-0.2 0.451 84.5 71.1 -72.1 2.1 9.1 32.5 7.2 37 34 E G T 3 S+ 0 0 0 92,-0.1 300,-2.6 157,-0.1 2,-0.3 0.215 103.8 26.1-103.9 9.0 6.0 34.1 8.9 38 35 E S < - 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0 0 63 61,-2.3 3,-2.3 1,-0.1 4,-0.3 -0.242 37.1-125.4 -49.5 129.2 15.9 44.1 31.1 50 47 E A G > S+ 0 0 83 1,-0.3 3,-1.4 2,-0.2 -1,-0.1 0.817 103.9 54.8 -50.4 -47.0 17.7 41.7 33.4 51 48 E S G 3 S+ 0 0 106 1,-0.2 -1,-0.3 3,-0.1 -2,-0.1 0.567 104.7 56.3 -70.1 -9.0 14.7 40.0 35.0 52 49 E E G < S+ 0 0 54 -3,-2.3 2,-0.5 2,-0.0 -1,-0.2 0.224 89.0 90.5 -98.7 1.4 13.3 39.1 31.6 53 50 E V < + 0 0 47 -3,-1.4 64,-0.1 -4,-0.3 65,-0.1 -0.942 50.3 165.9 -99.1 125.3 16.6 37.2 30.6 54 51 E D - 0 0 75 -2,-0.5 -1,-0.1 63,-0.2 3,-0.1 -0.595 67.0 -37.1-153.9 76.9 16.6 33.5 31.5 55 52 E G S S+ 0 0 67 1,-0.2 -2,-0.1 66,-0.0 63,-0.1 0.566 96.6 121.8 101.1 -16.0 19.1 31.1 30.2 56 53 E Q - 0 0 15 61,-0.2 2,-0.3 66,-0.1 -1,-0.2 -0.334 65.3-112.6 -75.4 160.3 19.4 32.5 26.6 57 54 E T - 0 0 70 63,-0.2 2,-0.4 -26,-0.1 -13,-0.3 -0.730 36.9-147.7 -91.8 136.7 22.7 33.7 25.0 58 55 E I - 0 0 60 -2,-0.3 2,-0.5 -15,-0.1 -13,-0.3 -0.792 9.6-125.3-113.8 160.2 22.7 37.4 24.4 59 56 E Y B -o 45 0D 0 -15,-2.4 -13,-1.9 -2,-0.4 -12,-0.3 -0.705 19.8-159.8 -92.9 127.8 24.2 39.6 21.8 60 57 E T > - 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