==== 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 14-OCT-90 4ER1 . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR J.W.QUAIL,J.B.COOPER,M.SZELKE,T.L.BLUNDELL . 331 2 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13127.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 225 68.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 17 5.1 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 103 31.1 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 . 40 12.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 35 10.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 18 5.4 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 . 2 4 4 3 4 1 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 61 0, 0.0 152,-1.8 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 158.2 27.9 33.0 -2.8 2 -1 E T - 0 0 57 150,-0.2 2,-0.3 96,-0.1 170,-0.2 -0.939 360.0-158.2-136.1 173.9 26.0 30.4 -0.8 3 0 E G E -A 171 0A 2 168,-2.2 168,-3.3 -2,-0.3 2,-0.3 -0.997 3.2-169.7-149.3 161.8 25.4 29.3 2.7 4 1 E S E +A 170 0A 62 93,-1.6 2,-0.3 -2,-0.3 166,-0.2 -0.947 10.0 173.8-150.3 133.4 24.2 26.2 4.5 5 2 E A E -A 169 0A 9 164,-2.2 164,-2.4 -2,-0.3 2,-0.4 -0.952 29.5-119.1-145.0 143.6 23.3 25.7 8.3 6 3 E T E -A 168 0A 80 -2,-0.3 2,-0.4 162,-0.2 162,-0.3 -0.770 23.9-157.0 -85.5 139.4 21.8 22.9 10.3 7 4 E T E -A 167 0A 0 160,-1.7 160,-3.0 -2,-0.4 155,-0.2 -0.936 7.8-164.2-119.2 135.3 18.6 23.5 12.1 8 5 E T E -F 18 0B 65 10,-2.4 10,-3.1 -2,-0.4 2,-0.0 -0.942 25.3-111.4-123.3 142.2 17.5 21.5 15.2 9 6 E P E -F 17 0B 21 0, 0.0 8,-0.3 0, 0.0 3,-0.0 -0.347 25.4-132.5 -73.2 145.5 14.2 21.1 16.9 10 7 E I S S+ 0 0 25 6,-2.8 2,-0.2 -2,-0.0 7,-0.1 0.704 81.5 4.8 -73.6 -15.4 14.3 22.8 20.3 11 8 E D S > S- 0 0 62 5,-0.4 3,-1.3 0, 0.0 5,-0.1 -0.864 91.3 -82.5-157.0-174.5 12.6 19.7 22.1 12 9 E S T 3 S+ 0 0 102 1,-0.3 -2,-0.0 -2,-0.2 0, 0.0 0.567 122.1 58.0 -88.6 -3.6 11.5 16.2 21.5 13 10 E L T 3 S- 0 0 53 268,-0.0 -1,-0.3 3,-0.0 -3,-0.0 0.477 104.4-123.0 -90.6 -3.5 8.1 17.5 20.0 14 11 E D < + 0 0 0 -3,-1.3 -2,-0.1 2,-0.1 3,-0.1 0.876 52.4 159.5 63.2 44.3 9.6 19.6 17.3 15 12 E D S S- 0 0 29 1,-0.2 2,-0.3 292,-0.0 292,-0.1 0.730 70.2 -19.9 -70.9 -24.0 7.7 22.7 18.7 16 13 E A - 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0 0 61 -2,-0.1 2,-0.5 -5,-0.1 -3,-0.2 -0.176 30.3-165.8 -51.7 127.9 31.4 36.6 16.0 28 25 E Q E < -G 23 0C 30 -5,-1.8 -5,-2.7 -4,-0.1 2,-0.4 -0.974 16.9-145.2-107.2 130.5 28.8 36.0 18.6 29 26 E T E +G 22 0C 69 -2,-0.5 2,-0.3 -7,-0.2 -7,-0.2 -0.694 21.8 175.1-101.5 128.1 26.7 32.9 17.9 30 27 E L E -G 21 0C 0 -9,-2.4 -9,-2.9 -2,-0.4 2,-0.8 -0.967 32.8-123.0-126.2 150.0 23.1 33.0 18.9 31 28 E N E -G 20 0C 63 -2,-0.3 92,-2.5 -11,-0.2 93,-0.4 -0.848 37.5-170.0-102.6 110.9 20.5 30.3 18.1 32 29 E L E -G 19 0C 0 -13,-2.4 -13,-2.3 -2,-0.8 2,-0.7 -0.655 26.0-128.0-100.5 146.4 17.7 31.9 16.1 33 30 E D E -i 125 0C 10 91,-2.1 93,-2.1 -2,-0.2 2,-0.4 -0.871 26.7-141.5 -84.1 114.0 14.2 30.7 15.1 34 31 E F E -i 126 0C 1 -2,-0.7 2,-0.6 -17,-0.4 93,-0.2 -0.645 22.0-167.2 -79.5 124.6 14.0 31.3 11.3 35 32 E D E > -i 127 0C 10 91,-2.7 93,-2.5 -2,-0.4 3,-1.3 -0.940 22.2-171.4-126.0 104.9 10.4 32.5 10.8 36 33 E T T 3 S+ 0 0 1 -2,-0.6 159,-0.5 1,-0.2 94,-0.1 0.635 84.6 69.2 -80.4 3.7 9.0 32.7 7.3 37 34 E G T 3 S+ 0 0 13 92,-0.1 2,-0.3 157,-0.1 -1,-0.2 0.356 103.8 30.5 -98.6 11.2 5.9 34.4 8.8 38 35 E S < - 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0 0 62 61,-1.9 3,-2.2 1,-0.1 -1,-0.1 -0.267 36.2-133.7 -49.6 121.4 15.7 44.1 31.0 50 47 E A G > S+ 0 0 86 1,-0.3 3,-1.5 2,-0.2 -1,-0.1 0.821 102.5 58.0 -48.5 -45.5 17.7 41.7 33.2 51 48 E S G 3 S+ 0 0 106 1,-0.3 -1,-0.3 3,-0.0 -2,-0.1 0.470 101.4 59.8 -70.9 0.5 14.6 40.3 35.0 52 49 E E G < S+ 0 0 54 -3,-2.2 2,-0.5 1,-0.1 -1,-0.3 0.116 85.0 89.5-114.8 19.5 13.3 39.2 31.6 53 50 E V < + 0 0 48 -3,-1.5 2,-0.8 -5,-0.1 64,-0.1 -0.893 47.3 179.2-125.2 99.4 16.2 37.0 30.6 54 51 E D S S- 0 0 68 63,-0.5 -3,-0.0 -2,-0.5 -4,-0.0 -0.789 75.8 -49.3-102.9 86.7 16.1 33.0 31.6 55 52 E G S S+ 0 0 69 -2,-0.8 -1,-0.1 1,-0.2 63,-0.0 0.423 92.6 142.1 73.1 6.3 19.4 31.5 30.3 56 53 E Q - 0 0 14 61,-0.1 2,-0.5 1,-0.1 -1,-0.2 -0.342 56.6-108.7 -72.8 160.8 19.3 32.8 26.7 57 54 E T - 0 0 69 63,-0.2 2,-0.3 -26,-0.1 -13,-0.3 -0.803 38.6-149.3 -90.5 128.6 22.5 33.9 24.9 58 55 E I - 0 0 65 -2,-0.5 2,-0.4 -15,-0.1 -13,-0.3 -0.760 9.4-128.6-102.5 149.6 22.6 37.7 24.5 59 56 E Y B -o 45 0D 0 -15,-3.1 -13,-2.5 -2,-0.3 -12,-0.3 -0.790 16.5-160.5 -91.7 134.7 24.2 40.0 21.9 60 57 E T > - 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