==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=1-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER TRANSFERASE 15-SEP-06 2IDK . COMPND 2 MOLECULE: GLYCINE N-METHYLTRANSFERASE; . SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; . AUTHOR Z.LUKA,S.PAKHOMOVA,L.V.LOUKACHEVITCH,M.EGLI,M.E.NEWCOMER, . 1132 11 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 45368.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 824 72.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 84 7.4 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 174 15.4 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 2 0.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 10 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 . 155 13.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 123 10.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 247 21.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 12 1.1 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 8 0 0 4 4 2 5 2 7 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 4 8 4 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 . 10 2 2 0 2 0 9 0 3 2 0 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 0 0 2 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 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 A D 0 0 78 0, 0.0 585,-0.0 0, 0.0 586,-0.0 0.000 360.0 360.0 360.0 16.2 22.5 -21.1 27.6 2 3 A S - 0 0 69 571,-0.0 572,-0.9 1,-0.0 2,-0.4 -0.241 360.0-134.9 -69.4 163.5 20.9 -18.3 25.5 3 4 A V E -A 573 0A 61 570,-0.2 2,-0.5 571,-0.1 570,-0.2 -0.911 15.8-140.1-117.4 150.4 17.2 -18.2 25.2 4 5 A Y E -A 572 0A 51 568,-2.0 568,-2.2 -2,-0.4 2,-0.3 -0.941 8.7-155.3-120.5 134.6 15.6 -17.5 21.9 5 6 A R E -A 571 0A 53 -2,-0.5 566,-0.1 566,-0.2 3,-0.1 -0.804 18.9-142.0-104.8 145.7 12.6 -15.3 21.1 6 7 A T S S+ 0 0 26 564,-0.7 2,-0.3 -2,-0.3 -1,-0.1 0.877 94.2 11.2 -69.4 -37.3 10.2 -15.6 18.1 7 8 A R S S- 0 0 9 507,-0.2 -1,-0.3 561,-0.1 507,-0.2 -0.995 90.4 -96.8-141.9 149.9 10.1 -11.8 18.1 8 9 A S > - 0 0 18 505,-1.7 3,-0.9 -2,-0.3 2,-0.4 0.018 48.9 -91.2 -55.8 164.2 12.1 -9.0 19.7 9 10 A L T 3 S+ 0 0 54 1,-0.2 298,-0.4 291,-0.0 297,-0.1 -0.687 113.9 22.1 -81.1 129.8 10.8 -7.3 22.9 10 11 A G T 3 S+ 0 0 4 -2,-0.4 -1,-0.2 1,-0.4 2,-0.2 0.196 95.9 120.8 101.3 -15.8 8.7 -4.3 21.9 11 12 A V < - 0 0 1 -3,-0.9 8,-0.4 502,-0.1 -1,-0.4 -0.513 41.4-166.9 -84.2 148.8 7.9 -5.5 18.4 12 13 A A - 0 0 1 -2,-0.2 2,-0.3 6,-0.1 -4,-0.1 -0.779 3.8-155.0-126.6 172.7 4.3 -6.1 17.2 13 14 A A > - 0 0 4 3,-0.5 3,-1.8 -2,-0.3 353,-0.1 -0.982 30.4 -96.9-153.9 140.5 2.8 -7.8 14.2 14 15 A E T 3 S+ 0 0 50 -2,-0.3 408,-0.2 1,-0.2 351,-0.1 -0.295 107.1 20.2 -56.0 129.8 -0.4 -7.5 12.3 15 16 A G T 3 S+ 0 0 2 1,-0.2 382,-0.4 380,-0.1 -1,-0.2 0.245 105.9 83.7 99.3 -16.5 -2.9 -10.1 13.5 16 17 A I S < S- 0 0 22 -3,-1.8 -3,-0.5 380,-0.1 -1,-0.2 -0.948 81.1-104.3-126.5 147.6 -1.6 -11.0 16.9 17 18 A P - 0 0 32 0, 0.0 350,-0.2 0, 0.0 3,-0.2 -0.359 47.4-102.7 -63.8 143.1 -2.0 -9.4 20.3 18 19 A D > - 0 0 20 348,-0.5 3,-1.8 1,-0.2 4,-0.3 -0.131 57.5 -64.1 -62.7 163.8 1.0 -7.5 21.5 19 20 A Q T 3 S- 0 0 19 -8,-0.4 -1,-0.2 1,-0.3 272,-0.1 -0.275 118.5 -8.3 -55.3 121.9 3.3 -9.0 24.1 20 21 A Y T > S+ 0 0 59 -3,-0.2 3,-1.3 1,-0.1 -1,-0.3 0.415 90.4 137.7 72.0 -1.0 1.6 -9.6 27.4 21 22 A A T < S+ 0 0 26 -3,-1.8 -2,-0.1 1,-0.3 -1,-0.1 0.731 76.8 25.7 -47.5 -30.7 -1.4 -7.6 26.2 22 23 A D T 3 S+ 0 0 91 -4,-0.3 -1,-0.3 -5,-0.1 2,-0.1 -0.252 80.6 135.8-137.9 55.7 -3.8 -10.1 27.8 23 24 A G S <> S- 0 0 32 -3,-1.3 4,-1.9 267,-0.2 5,-0.2 -0.394 72.2 -98.2 -87.9 173.9 -2.3 -11.9 30.7 24 25 A E H > S+ 0 0 48 1,-0.2 4,-1.3 2,-0.2 5,-0.1 0.791 124.7 52.5 -65.4 -24.5 -4.3 -12.4 33.9 25 26 A A H > S+ 0 0 23 2,-0.2 4,-1.7 1,-0.2 -1,-0.2 0.877 108.7 45.6 -78.9 -39.8 -2.5 -9.4 35.3 26 27 A A H > S+ 0 0 2 -6,-0.2 4,-1.6 264,-0.2 -2,-0.2 0.859 110.8 56.3 -70.6 -34.1 -3.2 -7.0 32.5 27 28 A R H X S+ 0 0 143 -4,-1.9 4,-1.3 2,-0.2 -1,-0.2 0.894 109.9 43.1 -63.7 -43.6 -6.8 -8.1 32.5 28 29 A V H X S+ 0 0 16 -4,-1.3 4,-1.4 1,-0.2 -1,-0.2 0.876 112.4 55.0 -69.9 -37.0 -7.4 -7.3 36.1 29 30 A W H X S+ 0 0 2 -4,-1.7 4,-1.7 1,-0.2 -2,-0.2 0.791 100.3 59.5 -65.8 -30.0 -5.5 -4.1 35.6 30 31 A Q H < S+ 0 0 61 -4,-1.6 4,-0.4 1,-0.2 3,-0.3 0.943 106.4 47.6 -63.3 -46.3 -7.9 -3.1 32.8 31 32 A L H >X S+ 0 0 112 -4,-1.3 4,-3.8 1,-0.2 3,-0.5 0.813 107.0 58.5 -63.9 -32.1 -10.7 -3.3 35.3 32 33 A Y H 3< S+ 0 0 62 -4,-1.4 -1,-0.2 1,-0.2 -2,-0.2 0.876 108.8 42.5 -67.1 -38.2 -8.7 -1.3 37.8 33 34 A I T 3< S+ 0 0 16 -4,-1.7 -1,-0.2 -3,-0.3 -2,-0.2 0.447 123.2 41.2 -87.6 1.1 -8.4 1.7 35.4 34 35 A G T X4 S+ 0 0 48 -3,-0.5 3,-1.4 -4,-0.4 -2,-0.2 0.730 107.7 55.5-110.9 -42.2 -12.0 1.2 34.4 35 36 A D T 3< S+ 0 0 56 -4,-3.8 159,-0.2 1,-0.3 -2,-0.1 -0.048 115.9 43.0 -83.3 32.9 -13.7 0.6 37.7 36 37 A T T 3 S+ 0 0 31 -2,-0.1 -1,-0.3 159,-0.1 159,-0.1 0.118 73.8 109.2-161.7 20.8 -12.2 3.8 39.0 37 38 A R < + 0 0 48 -3,-1.4 2,-0.3 157,-0.1 -2,-0.1 0.081 60.4 102.4 -91.2 23.9 -12.7 6.2 36.0 38 39 A S - 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