==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=30-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER TRANSCRIPTION/METAL BINDING PROTEIN 01-MAR-07 2EGM . COMPND 2 MOLECULE: TRIPARTITE MOTIF-CONTAINING PROTEIN 41; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR K.INOUE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL . 57 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4856.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 26 45.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 9 15.8 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 3.5 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 . 0 0.0 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 . 6 10.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 2 3.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 7 12.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 1.8 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 1 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 RESIDUES PER ALPHA HELIX . 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 0 0 0 PARALLEL BRIDGES PER LADDER . 1 1 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 0 ANTIPARALLEL BRIDGES PER LADDER . 0 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 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 G 0 0 137 0, 0.0 2,-0.2 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 112.7 -31.2 11.2 32.6 2 2 A S - 0 0 126 2,-0.0 2,-0.3 0, 0.0 0, 0.0 -0.563 360.0-162.8-104.1 169.9 -29.4 8.0 31.5 3 3 A S - 0 0 108 -2,-0.2 2,-2.5 2,-0.0 0, 0.0 -0.984 31.0-117.0-155.0 141.6 -26.6 7.4 29.0 4 4 A G + 0 0 77 -2,-0.3 2,-1.6 1,-0.2 -2,-0.0 -0.334 48.1 157.6 -76.8 60.7 -25.1 4.5 27.2 5 5 A S + 0 0 118 -2,-2.5 2,-0.5 2,-0.0 -1,-0.2 -0.198 34.2 118.1 -80.1 46.7 -21.7 4.9 28.8 6 6 A S + 0 0 120 -2,-1.6 2,-0.3 2,-0.0 -2,-0.0 -0.961 31.2 128.0-119.7 129.7 -21.0 1.2 28.1 7 7 A G - 0 0 75 -2,-0.5 -2,-0.0 0, 0.0 0, 0.0 -0.986 48.2-104.2-167.1 169.4 -18.1 -0.0 25.9 8 8 A T - 0 0 132 -2,-0.3 2,-0.1 1,-0.0 -2,-0.0 -0.854 36.1-112.4-109.5 142.0 -15.1 -2.3 25.6 9 9 A P - 0 0 117 0, 0.0 2,-0.8 0, 0.0 -1,-0.0 -0.381 24.1-131.5 -69.7 145.0 -11.5 -1.2 25.7 10 10 A G - 0 0 82 -2,-0.1 3,-0.2 2,-0.0 2,-0.1 -0.854 27.6-174.9-104.7 105.5 -9.3 -1.5 22.6 11 11 A R + 0 0 232 -2,-0.8 2,-0.2 1,-0.1 3,-0.1 -0.402 43.5 79.9 -91.2 170.4 -6.0 -3.2 23.2 12 12 A G - 0 0 36 1,-0.1 -1,-0.1 -2,-0.1 3,-0.1 -0.567 49.6-159.6 136.3 -73.5 -3.1 -3.6 20.7 13 13 A S + 0 0 142 1,-0.2 2,-0.3 -3,-0.2 -1,-0.1 0.924 58.9 104.8 57.9 47.1 -1.0 -0.5 20.4 14 14 A R S S- 0 0 215 -3,-0.1 -1,-0.2 0, 0.0 2,-0.0 -0.966 73.5-108.4-158.3 139.3 0.4 -1.6 17.1 15 15 A V + 0 0 88 -2,-0.3 3,-0.0 1,-0.1 -3,-0.0 -0.340 26.9 176.9 -67.7 147.7 -0.2 -0.7 13.4 16 16 A T > + 0 0 132 -2,-0.0 3,-0.6 1,-0.0 -1,-0.1 0.403 63.9 85.7-128.8 -7.4 -2.0 -3.2 11.2 17 17 A D T 3 S+ 0 0 83 1,-0.2 22,-0.1 2,-0.1 40,-0.1 0.123 82.5 67.9 -83.5 22.3 -2.1 -1.3 7.9 18 18 A Q T 3 + 0 0 71 20,-0.1 -1,-0.2 11,-0.1 10,-0.2 -0.149 67.8 112.6-132.6 38.2 1.3 -2.6 7.1 19 19 A G S < S- 0 0 41 -3,-0.6 9,-1.2 1,-0.2 2,-0.3 0.877 78.2 -51.0 -74.8-100.9 0.7 -6.3 6.6 20 20 A I B -A 27 0A 80 7,-0.2 -1,-0.2 18,-0.0 7,-0.2 -0.998 47.2-107.8-147.9 142.6 1.1 -7.6 3.1 21 21 A C > - 0 0 4 5,-1.1 4,-2.5 -2,-0.3 18,-0.1 -0.560 19.1-149.3 -73.2 119.8 -0.1 -6.6 -0.4 22 22 A P T 4 S+ 0 0 106 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 0.372 96.3 50.1 -69.7 7.3 -2.7 -9.1 -1.7 23 23 A K T 4 S+ 0 0 143 3,-0.1 -2,-0.0 0, 0.0 0, 0.0 0.781 132.1 6.4-109.5 -53.4 -1.4 -8.3 -5.2 24 24 A H T 4 S- 0 0 73 2,-0.1 -3,-0.0 0, 0.0 0, 0.0 0.531 90.7-131.0-107.9 -13.1 2.4 -8.6 -5.0 25 25 A Q < + 0 0 126 -4,-2.5 2,-0.4 1,-0.2 -5,-0.0 0.952 53.8 148.6 60.5 52.0 2.6 -10.0 -1.5 26 26 A E - 0 0 83 -5,-0.1 -5,-1.1 1,-0.0 -1,-0.2 -0.964 60.5 -88.2-122.4 135.2 5.3 -7.5 -0.4 27 27 A A B -A 20 0A 50 -2,-0.4 2,-0.8 -7,-0.2 14,-0.6 -0.092 47.5-121.8 -39.7 115.9 5.8 -6.1 3.1 28 28 A L + 0 0 21 -9,-1.2 12,-0.2 -10,-0.2 -1,-0.1 -0.538 53.6 148.8 -69.6 106.2 3.6 -3.0 3.1 29 29 A K + 0 0 81 -2,-0.8 2,-0.3 10,-0.4 28,-0.3 0.027 54.8 60.3-126.8 24.4 6.0 -0.1 3.9 30 30 A L E -B 39 0B 29 9,-1.5 9,-3.2 26,-0.3 2,-0.4 -0.992 59.5-152.2-151.1 153.5 4.3 2.7 2.0 31 31 A F E -BC 38 55B 54 24,-2.9 24,-1.9 -2,-0.3 2,-0.5 -0.972 22.7-126.9-134.3 119.7 0.9 4.5 1.9 32 32 A C E >> -BC 37 54B 0 5,-1.9 4,-2.1 -2,-0.4 5,-0.6 -0.492 13.8-163.1 -66.4 114.8 -0.6 6.1 -1.2 33 33 A E T 45S+ 0 0 118 20,-1.5 -1,-0.2 -2,-0.5 21,-0.1 0.344 90.0 51.7 -80.4 7.7 -1.4 9.7 -0.2 34 34 A V T 45S+ 0 0 81 3,-0.1 -1,-0.2 15,-0.0 -2,-0.1 0.687 122.0 24.6-111.5 -32.7 -3.7 9.8 -3.3 35 35 A D T 45S- 0 0 73 2,-0.2 -2,-0.2 -3,-0.1 3,-0.1 0.570 96.0-131.2-107.3 -16.7 -5.8 6.7 -2.8 36 36 A E T <5 + 0 0 159 -4,-2.1 2,-0.3 1,-0.2 -3,-0.2 0.927 65.2 121.8 64.7 46.4 -5.4 6.5 1.0 37 37 A E E < -B 32 0B 80 -5,-0.6 -5,-1.9 0, 0.0 -1,-0.2 -0.996 67.5-107.8-143.7 134.8 -4.5 2.8 1.0 38 38 A A E +B 31 0B 19 -2,-0.3 2,-0.3 -7,-0.2 -7,-0.3 -0.299 44.6 176.2 -59.9 139.2 -1.5 0.9 2.2 39 39 A I E -B 30 0B 3 -9,-3.2 -9,-1.5 -22,-0.1 -10,-0.4 -0.848 22.5-119.3-138.7 174.2 0.8 -0.4 -0.5 40 40 A C > - 0 0 0 -2,-0.3 4,-2.3 -12,-0.2 5,-0.2 -0.610 39.1 -93.5-112.0 173.5 4.1 -2.2 -1.0 41 41 A V H > S+ 0 0 48 -14,-0.6 4,-2.1 1,-0.2 5,-0.2 0.893 126.3 51.3 -51.9 -43.9 7.3 -1.3 -2.8 42 42 A V H > S+ 0 0 52 1,-0.2 4,-1.9 2,-0.2 -1,-0.2 0.931 107.5 51.9 -60.5 -47.8 6.1 -3.0 -5.9 43 43 A C H 4 S+ 0 0 4 1,-0.2 6,-1.1 2,-0.2 -2,-0.2 0.930 108.5 51.1 -54.9 -49.5 2.8 -1.1 -5.9 44 44 A R H < S+ 0 0 113 -4,-2.3 -1,-0.2 1,-0.3 -2,-0.2 0.928 111.8 46.3 -54.7 -49.2 4.7 2.2 -5.6 45 45 A E H < S+ 0 0 128 -4,-2.1 2,-0.3 -5,-0.2 -1,-0.3 0.792 96.0 94.6 -64.7 -27.9 6.9 1.4 -8.6 46 46 A S S >X S- 0 0 38 -4,-1.9 3,-1.9 -5,-0.2 4,-1.1 -0.497 89.6-122.3 -70.0 128.2 3.8 0.3 -10.5 47 47 A R H 3> S+ 0 0 212 1,-0.3 4,-0.8 -2,-0.3 5,-0.2 0.748 108.4 76.9 -39.9 -26.1 2.4 3.0 -12.7 48 48 A S H 34 S+ 0 0 69 1,-0.2 -1,-0.3 2,-0.1 -4,-0.1 0.945 119.6 5.9 -52.1 -55.0 -0.7 2.4 -10.6 49 49 A H H <4 S+ 0 0 17 -3,-1.9 -1,-0.2 -6,-1.1 5,-0.2 0.070 109.4 97.0-117.7 21.2 0.7 4.3 -7.6 50 50 A K H < S+ 0 0 94 -4,-1.1 4,-0.2 1,-0.2 -3,-0.2 0.929 89.0 40.1 -75.1 -47.9 3.8 5.6 -9.3 51 51 A Q S < S+ 0 0 177 -4,-0.8 2,-0.2 -5,-0.1 -1,-0.2 0.717 102.0 92.0 -73.4 -21.2 2.5 9.0 -10.2 52 52 A H S S- 0 0 50 -5,-0.2 2,-1.4 -8,-0.1 -3,-0.0 -0.531 92.0-109.3 -77.3 140.0 0.8 9.2 -6.8 53 53 A S - 0 0 85 -2,-0.2 -20,-1.5 -21,-0.1 2,-0.3 -0.530 45.1-171.8 -71.8 92.5 2.7 10.7 -3.9 54 54 A V E -C 32 0B 30 -2,-1.4 -22,-0.2 -5,-0.2 -24,-0.0 -0.652 4.2-159.9 -89.4 143.5 3.4 7.7 -1.8 55 55 A V E -C 31 0B 44 -24,-1.9 -24,-2.9 -2,-0.3 2,-0.7 -0.904 29.2 -97.2-124.2 152.2 5.0 8.0 1.7 56 56 A P 0 0 107 0, 0.0 -26,-0.3 0, 0.0 -27,-0.0 -0.535 360.0 360.0 -69.8 108.5 6.8 5.5 3.9 57 57 A L 0 0 73 -2,-0.7 -39,-0.0 -28,-0.3 -3,-0.0 -0.154 360.0 360.0 -45.1 360.0 4.3 4.0 6.3