==== 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 02-JAN-91 3ER3 . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR S.AL-KARADAGHI,J.B.COOPER,B.VEERAPANDIAN,D.HOOVER,T.L.BLUNDE . 331 2 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13178.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 239 72.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 18 5.4 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 105 31.7 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 . 1 0.3 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 . 49 14.8 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 . 19 5.7 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 2 1 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 3 4 5 3 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 2 0 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 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 56 0, 0.0 152,-1.7 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 148.3 27.7 33.1 -2.7 2 -1 E T - 0 0 61 150,-0.2 2,-0.3 96,-0.1 170,-0.2 -0.956 360.0-165.8-138.1 161.5 26.0 30.4 -0.8 3 0 E G E -A 171 0A 4 168,-2.1 168,-3.0 -2,-0.3 2,-0.3 -0.969 2.3-174.3-141.5 159.9 25.2 29.4 2.8 4 1 E S E +A 170 0A 62 93,-2.1 2,-0.4 -2,-0.3 166,-0.2 -0.895 9.0 176.7-159.8 119.1 24.1 26.1 4.5 5 2 E A E -A 169 0A 7 164,-2.6 164,-2.7 -2,-0.3 2,-0.3 -0.985 29.3-121.6-134.6 135.1 23.2 25.7 8.2 6 3 E T E -A 168 0A 84 -2,-0.4 2,-0.4 162,-0.2 162,-0.3 -0.613 25.9-159.1 -71.6 130.9 21.8 22.8 10.2 7 4 E T E -A 167 0A 0 160,-2.5 160,-3.3 -2,-0.3 155,-0.2 -0.959 9.5-166.1-115.8 142.0 18.5 23.6 12.0 8 5 E T E -F 18 0B 61 10,-2.4 10,-2.9 -2,-0.4 2,-0.2 -0.952 25.2-107.4-134.4 138.2 17.5 21.5 15.0 9 6 E P E -F 17 0B 23 0, 0.0 8,-0.2 0, 0.0 154,-0.0 -0.505 22.2-139.4 -70.7 137.2 14.2 21.0 17.0 10 7 E I S S+ 0 0 32 6,-1.8 2,-0.3 -2,-0.2 7,-0.1 0.531 81.6 9.5 -73.2 -12.4 14.3 22.7 20.4 11 8 E D S > S- 0 0 56 5,-0.3 3,-1.6 0, 0.0 5,-0.1 -0.936 88.9 -88.5-161.5 174.0 12.5 19.7 22.0 12 9 E S T 3 S+ 0 0 98 1,-0.3 -2,-0.0 -2,-0.3 0, 0.0 0.575 119.6 59.9 -71.3 -8.0 11.4 16.1 21.4 13 10 E L T 3 S- 0 0 56 3,-0.0 -1,-0.3 268,-0.0 -3,-0.0 0.496 105.5-121.6 -98.3 -8.0 8.1 17.4 20.0 14 11 E D < + 0 0 0 -3,-1.6 -2,-0.1 2,-0.1 3,-0.1 0.867 54.1 158.3 62.3 37.6 9.5 19.5 17.1 15 12 E D - 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0 0 59 61,-2.8 3,-1.7 -2,-0.2 4,-0.4 -0.202 36.4-128.0 -44.2 129.1 15.9 44.3 31.0 50 47 E A G > S+ 0 0 84 1,-0.3 3,-1.8 2,-0.2 -1,-0.1 0.830 103.5 55.5 -50.7 -49.6 17.7 41.8 33.2 51 48 E S G 3 S+ 0 0 114 1,-0.3 -1,-0.3 3,-0.0 -2,-0.1 0.512 106.5 57.0 -71.4 0.5 14.8 40.2 35.1 52 49 E E G < S+ 0 0 53 -3,-1.7 2,-0.4 -4,-0.1 -1,-0.3 0.508 88.0 86.3-106.3 -12.6 13.4 39.4 31.6 53 50 E V < + 0 0 46 -3,-1.8 64,-0.1 -4,-0.4 67,-0.1 -0.819 53.2 178.5 -97.2 139.4 16.5 37.4 30.3 54 51 E D - 0 0 78 -2,-0.4 3,-0.1 62,-0.1 -1,-0.1 -0.491 65.0 -44.3-144.1 59.7 16.4 33.7 31.2 55 52 E G S S+ 0 0 72 1,-0.4 -2,-0.1 66,-0.0 63,-0.1 0.203 97.3 131.1 97.6 -17.2 19.2 31.3 30.1 56 53 E Q - 0 0 13 61,-0.1 -1,-0.4 66,-0.1 2,-0.3 -0.296 61.3-118.2 -66.1 151.2 19.2 32.9 26.6 57 54 E T - 0 0 73 63,-0.2 2,-0.3 -3,-0.1 -13,-0.3 -0.688 33.4-144.2 -90.8 139.7 22.5 33.9 25.0 58 55 E I - 0 0 60 -2,-0.3 2,-0.4 -15,-0.1 -13,-0.3 -0.862 10.8-128.5-115.5 154.4 22.7 37.7 24.2 59 56 E Y B -o 45 0D 0 -15,-2.0 -13,-2.2 -2,-0.3 -12,-0.3 -0.734 20.8-159.2 -96.5 109.1 24.2 39.8 21.5 60 57 E T > - 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