==== 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 TRANSFERASE 29-JUN-11 3SO4 . COMPND 2 MOLECULE: METHIONINE-ADENOSYLTRANSFERASE; . SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA; . AUTHOR E.A.MERRITT,MEDICAL STRUCTURAL GENOMICS OF PATHOGENIC PROTOZ . 1516 8 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 49426.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 1034 68.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 60 4.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 237 15.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 3 0.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 8 0.5 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 . 142 9.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 151 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 359 23.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 33 2.2 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 4 0 0 0 4 0 0 8 4 0 0 0 0 0 4 8 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 0 4 0 0 0 0 4 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 . 7 7 0 0 0 4 0 11 1 0 0 3 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 3 4 4 0 0 0 0 0 2 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 4 A R 0 0 96 0, 0.0 2,-0.3 0, 0.0 162,-0.2 0.000 360.0 360.0 360.0 141.4 14.8 16.9 -1.1 2 5 A F E -A 162 0A 47 160,-1.2 160,-3.9 684,-0.0 2,-0.3 -0.948 360.0-108.6-156.2 172.6 13.2 13.9 -2.9 3 6 A F E -A 161 0A 77 682,-0.4 2,-0.3 -2,-0.3 158,-0.2 -0.846 25.8-176.4-111.8 155.2 12.7 10.1 -2.9 4 7 A F E -A 160 0A 13 156,-2.7 156,-2.6 -2,-0.3 2,-0.4 -0.979 9.5-150.6-145.2 153.7 14.1 7.5 -5.3 5 8 A T E +A 159 0A 0 -2,-0.3 2,-0.3 154,-0.3 154,-0.2 -0.988 14.4 171.2-130.6 137.8 13.8 3.7 -5.7 6 9 A S E -A 158 0A 0 152,-1.3 152,-1.9 -2,-0.4 2,-0.3 -0.925 11.8-156.5-135.2 166.5 16.1 0.9 -7.0 7 10 A E E -A 157 0A 12 -2,-0.3 2,-0.3 150,-0.2 150,-0.2 -0.876 8.4-173.2-137.8 165.1 15.9 -2.9 -7.1 8 11 A S E -A 156 0A 3 148,-1.9 148,-2.9 -2,-0.3 2,-0.3 -0.975 10.2-147.6-152.8 163.6 18.0 -6.0 -7.3 9 12 A V E -A 155 0A 2 -2,-0.3 342,-0.4 146,-0.2 146,-0.2 -0.946 21.8-110.6-134.5 154.8 17.6 -9.8 -7.7 10 13 A S > - 0 0 3 144,-2.5 3,-1.5 -2,-0.3 6,-0.3 -0.298 32.6-106.1 -80.1 167.4 19.5 -12.9 -6.5 11 14 A G T 3 S+ 0 0 2 1,-0.3 142,-0.1 124,-0.1 9,-0.1 0.544 117.5 67.1 -70.6 -9.0 21.5 -15.3 -8.5 12 15 A G T 3 S+ 0 0 0 140,-0.7 141,-0.3 142,-0.1 -1,-0.3 0.672 73.6 107.8 -82.0 -22.1 18.7 -17.8 -8.1 13 16 A H S X> S- 0 0 8 -3,-1.5 4,-3.0 139,-0.3 3,-0.6 -0.406 76.6-131.8 -56.1 125.3 16.4 -15.6 -10.2 14 17 A P H 3> S+ 0 0 0 0, 0.0 4,-1.9 0, 0.0 220,-0.2 0.867 106.5 53.2 -52.1 -45.4 15.9 -17.4 -13.5 15 18 A D H 3> S+ 0 0 10 1,-0.2 4,-1.6 218,-0.2 223,-0.3 0.898 117.1 39.2 -53.4 -43.6 16.7 -14.3 -15.6 16 19 A K H <> S+ 0 0 2 -3,-0.6 4,-2.6 -6,-0.3 -1,-0.2 0.778 107.1 63.5 -79.6 -31.2 19.9 -13.9 -13.6 17 20 A M H X S+ 0 0 0 -4,-3.0 4,-2.3 2,-0.2 -2,-0.2 0.860 106.1 47.2 -58.5 -38.1 20.6 -17.7 -13.6 18 21 A C H X S+ 0 0 0 -4,-1.9 4,-3.2 -5,-0.2 5,-0.3 0.964 107.7 53.5 -65.4 -56.1 20.8 -17.4 -17.4 19 22 A D H X S+ 0 0 0 -4,-1.6 4,-1.9 216,-0.3 239,-0.2 0.908 113.4 45.6 -43.5 -50.6 23.1 -14.3 -17.2 20 23 A Q H X S+ 0 0 20 -4,-2.6 4,-1.8 329,-0.2 -1,-0.2 0.948 112.4 48.4 -58.9 -55.6 25.4 -16.4 -14.9 21 24 A I H X S+ 0 0 0 -4,-2.3 4,-1.8 1,-0.2 -2,-0.2 0.895 110.9 52.0 -53.7 -46.4 25.3 -19.6 -17.1 22 25 A S H X S+ 0 0 0 -4,-3.2 4,-1.8 1,-0.2 -1,-0.2 0.906 112.1 44.3 -58.6 -46.1 26.1 -17.6 -20.2 23 26 A D H X S+ 0 0 0 -4,-1.9 4,-2.4 -5,-0.3 323,-0.3 0.714 106.0 63.2 -75.1 -21.7 29.1 -15.9 -18.7 24 27 A A H X S+ 0 0 3 -4,-1.8 4,-2.3 2,-0.2 -1,-0.2 0.900 104.8 46.5 -64.2 -42.5 30.1 -19.3 -17.3 25 28 A I H X S+ 0 0 2 -4,-1.8 4,-1.8 2,-0.2 -2,-0.2 0.938 111.0 52.2 -62.7 -50.1 30.5 -20.6 -20.9 26 29 A L H X S+ 0 0 0 -4,-1.8 4,-2.7 2,-0.2 3,-0.5 0.934 110.9 46.4 -51.1 -54.7 32.4 -17.4 -21.8 27 30 A D H X S+ 0 0 21 -4,-2.4 4,-2.3 1,-0.2 -1,-0.2 0.937 108.3 56.7 -52.8 -52.8 34.9 -17.9 -18.9 28 31 A A H X S+ 0 0 21 -4,-2.3 4,-0.6 1,-0.2 -1,-0.2 0.826 112.4 43.6 -46.0 -38.8 35.3 -21.6 -19.8 29 32 A C H >X S+ 0 0 0 -4,-1.8 4,-2.8 -3,-0.5 3,-1.3 0.964 110.4 49.9 -75.8 -56.8 36.3 -20.4 -23.3 30 33 A L H 3< S+ 0 0 6 -4,-2.7 -2,-0.2 1,-0.3 -1,-0.2 0.771 99.8 71.8 -54.9 -28.4 38.7 -17.6 -22.5 31 34 A A H 3< S+ 0 0 68 -4,-2.3 -1,-0.3 -5,-0.3 -2,-0.2 0.898 115.3 19.6 -53.7 -46.9 40.4 -20.0 -20.1 32 35 A Q H << S+ 0 0 112 -3,-1.3 -2,-0.2 -4,-0.6 -1,-0.2 0.833 140.1 27.9 -91.9 -40.8 41.9 -22.0 -22.9 33 36 A D >< - 0 0 16 -4,-2.8 3,-1.7 1,-0.1 -1,-0.2 -0.877 57.8-176.4-131.1 96.6 41.6 -19.4 -25.7 34 37 A P T 3 S+ 0 0 64 0, 0.0 -1,-0.1 0, 0.0 -4,-0.1 0.804 87.0 61.3 -64.1 -30.1 41.7 -15.7 -24.7 35 38 A K T 3 S+ 0 0 89 -5,-0.1 -5,-0.1 2,-0.1 306,-0.0 0.236 82.5 136.7 -79.6 14.2 41.2 -14.6 -28.3 36 39 A S < - 0 0 5 -3,-1.7 2,-0.5 305,-0.1 21,-0.2 -0.227 48.0-144.6 -62.9 150.6 37.8 -16.5 -28.2 37 40 A H E +D 56 0B 82 19,-3.1 19,-2.4 223,-0.1 2,-0.5 -0.975 22.7 175.1-121.4 115.5 34.7 -15.0 -29.6 38 41 A V E +D 55 0B 0 -2,-0.5 222,-2.0 17,-0.2 2,-0.3 -0.954 18.0 161.7-130.6 112.5 31.5 -15.8 -27.7 39 42 A A E +DE 54 259B 22 15,-2.8 15,-1.7 -2,-0.5 2,-0.3 -0.650 35.8 140.7-123.9 72.4 28.1 -14.4 -28.5 40 43 A C E -D 53 0B 3 218,-2.0 2,-0.3 -2,-0.3 13,-0.3 -0.882 30.6-164.0-127.2 150.7 25.8 -16.8 -26.7 41 44 A E E -D 52 0B 14 11,-3.2 11,-3.0 -2,-0.3 2,-0.4 -0.932 9.6-139.7-134.9 151.9 22.6 -16.7 -24.6 42 45 A T E -D 51 0B 1 -2,-0.3 194,-1.4 9,-0.2 2,-0.4 -0.888 10.8-172.5-115.1 143.3 20.7 -18.9 -22.2 43 46 A A E -DF 50 235B 1 7,-2.6 7,-3.8 -2,-0.4 2,-0.4 -0.996 9.8-173.8-131.7 138.0 17.0 -19.5 -21.8 44 47 A T E +DF 49 234B 0 190,-2.5 190,-2.1 -2,-0.4 5,-0.2 -0.990 12.5 152.4-134.4 142.7 15.3 -21.5 -19.0 45 48 A K - 0 0 2 3,-1.9 187,-0.2 -2,-0.4 -1,-0.1 0.332 59.8 -29.5-132.4-102.6 11.9 -22.8 -18.1 46 49 A T S S- 0 0 3 184,-0.2 805,-0.1 185,-0.1 186,-0.1 0.897 128.1 -11.5 -99.2 -45.8 10.3 -25.5 -16.2 47 50 A G S S+ 0 0 6 182,-0.1 42,-2.5 36,-0.1 804,-0.4 0.110 119.8 85.0-136.2 20.2 12.6 -28.5 -16.3 48 51 A L E - g 0 89B 7 40,-0.2 -3,-1.9 802,-0.1 2,-0.4 -0.931 49.3-164.0-141.1 144.3 14.9 -27.2 -19.0 49 52 A I E -Dg 44 90B 0 40,-2.4 42,-2.5 -2,-0.3 2,-0.6 -0.996 16.7-168.2-124.9 122.5 17.9 -25.1 -19.8 50 53 A L E -Dg 43 91B 4 -7,-3.8 -7,-2.6 -2,-0.4 2,-0.6 -0.946 1.9-165.5-114.1 112.0 18.4 -24.1 -23.5 51 54 A V E +Dg 42 92B 1 40,-2.5 42,-3.4 -2,-0.6 2,-0.4 -0.868 17.0 169.5 -95.7 123.3 21.7 -22.7 -24.5 52 55 A L E +Dg 41 93B 2 -11,-3.0 -11,-3.2 -2,-0.6 2,-0.3 -0.993 22.7 76.4-136.3 142.9 21.7 -21.0 -27.9 53 56 A G E -Dg 40 94B 0 40,-0.8 42,-1.9 -2,-0.4 2,-0.4 -0.978 65.8 -74.2 153.3-166.0 24.2 -18.8 -29.6 54 57 A E E -Dg 39 95B 35 -15,-1.7 -15,-2.8 -2,-0.3 2,-0.4 -0.989 30.7-176.6-135.0 139.0 27.5 -18.8 -31.5 55 58 A I E -Dg 38 96B 2 40,-1.7 42,-2.1 -2,-0.4 2,-0.7 -0.945 12.3-162.8-140.7 118.3 31.1 -19.2 -30.4 56 59 A T E +Dg 37 97B 49 -19,-2.4 -19,-3.1 -2,-0.4 2,-0.3 -0.888 43.5 127.5 -92.7 114.8 34.3 -19.0 -32.5 57 60 A T - 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