==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=27-NOV-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE/HYDROLASE INHIBITOR 20-OCT-10 3PBD . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA; . AUTHOR H.KOESTER,A.HEINE,G.KLEBE . 330 1 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13029.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 228 69.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 17 5.2 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 103 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 . 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 . 43 13.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 36 10.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 16 4.8 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 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 1 A S 0 0 63 0, 0.0 152,-2.4 0, 0.0 153,-0.3 0.000 360.0 360.0 360.0 167.0 22.6 -13.2 11.3 2 2 A T - 0 0 58 150,-0.2 2,-0.3 96,-0.2 170,-0.2 -0.959 360.0-157.7-142.2 164.8 19.7 -12.7 8.9 3 3 A G E -A 171 0A 2 168,-2.0 168,-2.7 -2,-0.3 2,-0.3 -0.981 3.6-171.2-138.5 159.0 16.0 -13.3 8.8 4 4 A S E +A 170 0A 64 93,-2.0 2,-0.4 -2,-0.3 166,-0.2 -0.911 10.7 173.0-149.8 117.8 13.5 -13.8 6.0 5 5 A A E -A 169 0A 8 164,-2.6 164,-2.8 -2,-0.3 2,-0.3 -0.966 30.1-121.3-128.8 144.7 9.7 -13.8 6.4 6 6 A T E -A 168 0A 76 -2,-0.4 2,-0.4 162,-0.2 162,-0.3 -0.677 23.0-153.2 -80.0 135.1 6.8 -13.9 3.9 7 7 A T E -A 167 0A 0 160,-1.9 160,-2.5 -2,-0.3 12,-0.2 -0.910 11.1-163.0-112.2 139.1 4.4 -11.1 4.0 8 8 A T E -F 18 0B 61 10,-2.8 10,-2.6 -2,-0.4 153,-0.0 -0.954 23.1-113.1-127.1 132.3 0.8 -11.6 2.8 9 9 A P E -F 17 0B 21 0, 0.0 8,-0.3 0, 0.0 3,-0.0 -0.371 21.8-139.6 -61.3 144.2 -2.0 -9.2 1.8 10 10 A I S S+ 0 0 31 6,-2.3 2,-0.3 1,-0.0 7,-0.1 0.630 77.6 3.1 -79.1 -18.2 -4.9 -9.3 4.3 11 11 A D S > S- 0 0 60 5,-0.4 3,-1.4 110,-0.0 5,-0.1 -0.908 89.8 -81.0-157.1-179.0 -7.6 -9.1 1.6 12 12 A S T 3 S+ 0 0 102 1,-0.3 -2,-0.0 -2,-0.3 0, 0.0 0.605 123.0 54.4 -72.6 -8.2 -8.1 -9.0 -2.2 13 13 A L T 3 S- 0 0 53 267,-0.1 -1,-0.3 3,-0.0 268,-0.0 0.351 107.1-119.6-101.8 -1.4 -7.3 -5.2 -2.3 14 14 A D < + 0 0 0 -3,-1.4 -2,-0.1 2,-0.1 3,-0.1 0.921 53.1 162.5 57.4 46.0 -3.9 -5.4 -0.6 15 15 A D - 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0 0 62 -2,-0.2 2,-0.5 -5,-0.1 -3,-0.2 -0.223 31.5-162.9 -56.9 138.3 6.5 -19.4 20.7 28 28 A Q E < -G 23 0C 32 -5,-2.0 -5,-2.9 -4,-0.1 2,-0.6 -0.996 17.3-147.5-113.7 115.7 3.2 -17.7 20.2 29 29 A T E +G 22 0C 65 -2,-0.5 2,-0.4 -7,-0.2 -7,-0.2 -0.797 20.7 176.5 -96.2 121.9 2.8 -16.8 16.5 30 30 A L E -G 21 0C 0 -9,-2.4 -9,-2.3 -2,-0.6 2,-0.8 -0.936 31.5-125.1-121.2 145.7 1.0 -13.6 15.7 31 31 A N E -G 20 0C 59 -2,-0.4 92,-2.6 -11,-0.2 93,-0.4 -0.849 38.7-170.6 -92.4 106.4 0.4 -12.0 12.3 32 32 A L E -G 19 0C 0 -13,-2.6 -13,-2.4 -2,-0.8 2,-0.9 -0.710 28.1-121.9-107.3 152.9 1.7 -8.4 12.6 33 33 A D E -i 125 0C 17 91,-2.5 93,-2.3 -2,-0.3 2,-0.5 -0.823 28.0-142.0 -89.4 103.2 1.6 -5.4 10.3 34 34 A F E -i 126 0C 1 -2,-0.9 2,-0.5 -17,-0.4 93,-0.2 -0.584 24.8-170.9 -69.8 117.2 5.2 -4.4 9.6 35 35 A D E > -i 127 0C 9 91,-2.4 93,-2.9 -2,-0.5 3,-1.4 -0.891 28.5-177.9-127.5 101.5 5.1 -0.6 9.6 36 36 A T T 3 S+ 0 0 0 -2,-0.5 159,-0.5 1,-0.3 94,-0.1 0.415 86.3 67.3 -79.3 5.1 8.0 1.5 8.5 37 37 A G T 3 S+ 0 0 13 92,-0.1 2,-0.3 157,-0.1 -1,-0.3 0.317 105.1 36.5-101.4 2.5 5.8 4.5 9.4 38 38 A S < - 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0 0 52 61,-2.3 3,-2.6 -2,-0.2 4,-0.3 -0.198 37.4-131.0 -37.6 117.3 -10.6 -5.3 26.6 50 50 A A G > S+ 0 0 89 1,-0.3 3,-1.4 2,-0.2 -1,-0.1 0.821 104.7 54.0 -49.1 -46.5 -12.7 -8.4 25.9 51 51 A S G 3 S+ 0 0 100 1,-0.3 -1,-0.3 3,-0.0 -2,-0.1 0.568 103.5 57.8 -66.8 -12.9 -15.2 -6.4 23.8 52 52 A E G < S+ 0 0 50 -3,-2.6 2,-0.5 66,-0.0 -1,-0.3 0.336 89.3 83.0-104.0 4.9 -12.4 -5.0 21.6 53 53 A V < + 0 0 42 -3,-1.4 2,-0.1 -4,-0.3 64,-0.1 -0.947 47.5 165.4-108.9 124.6 -11.1 -8.4 20.4 54 54 A D S S- 0 0 106 -2,-0.5 -3,-0.0 63,-0.2 66,-0.0 -0.543 74.9 -31.0-145.5 73.2 -12.9 -10.0 17.5 55 55 A G S S+ 0 0 63 1,-0.3 63,-0.1 -2,-0.1 -2,-0.0 0.203 94.4 133.6 102.6 -12.2 -11.1 -12.9 15.9 56 56 A Q - 0 0 14 61,-0.1 2,-0.4 66,-0.1 -1,-0.3 -0.318 60.0-115.1 -69.5 154.6 -7.5 -11.7 16.5 57 57 A T - 0 0 68 63,-0.2 2,-0.3 -26,-0.1 -13,-0.3 -0.757 38.2-144.3 -80.4 133.5 -4.8 -14.0 17.9 58 58 A I - 0 0 62 -2,-0.4 2,-0.5 -15,-0.1 -13,-0.3 -0.817 9.1-128.9-111.1 147.6 -3.6 -12.8 21.3 59 59 A Y B -o 45 0D 0 -15,-2.8 -13,-2.4 -2,-0.3 -12,-0.3 -0.803 19.7-164.4 -83.6 127.7 -0.3 -12.8 23.1 60 60 A T > - 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