==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=19-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER DNA BINDING PROTEIN 28-MAY-04 1WJ0 . COMPND 2 MOLECULE: SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE 12; . SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; . AUTHOR K.YAMASAKI,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL . 58 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4501.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 27 46.6 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 15.5 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 1.7 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 . 1 1.7 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 . 4 6.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 7 12.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 3 5.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 1.7 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 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 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 . 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 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 1 124 A A 0 0 100 0, 0.0 2,-0.2 0, 0.0 13,-0.2 0.000 360.0 360.0 360.0 104.9 1.5 14.8 -4.4 2 125 A I E -A 13 0A 61 11,-0.9 11,-3.6 23,-0.0 2,-0.3 -0.669 360.0-134.8-100.9 156.7 0.2 11.3 -5.1 3 126 A C E -A 12 0A 83 -2,-0.2 9,-0.2 9,-0.2 7,-0.1 -0.728 31.9 -87.5-109.2 159.5 -2.7 9.5 -3.5 4 127 A C - 0 0 10 7,-1.5 21,-0.2 -2,-0.3 5,-0.2 -0.369 25.0-146.0 -65.1 139.5 -3.0 5.9 -2.1 5 128 A Q S S+ 0 0 61 19,-0.7 33,-0.3 18,-0.1 -1,-0.1 0.800 71.9 99.2 -76.0 -30.0 -4.1 3.3 -4.7 6 129 A V S > S- 0 0 4 18,-0.2 3,-0.8 31,-0.1 31,-0.3 -0.270 81.4-111.4 -59.2 142.0 -6.0 1.4 -2.1 7 130 A D T 3 S+ 0 0 69 29,-3.4 29,-0.3 1,-0.2 -1,-0.1 -0.345 97.9 25.6 -73.9 156.3 -9.7 2.0 -2.0 8 131 A N T 3 S+ 0 0 174 1,-0.1 2,-0.4 -2,-0.1 -1,-0.2 0.767 100.1 109.1 61.7 25.7 -11.4 3.8 0.9 9 132 A C < + 0 0 31 -3,-0.8 -5,-0.2 -5,-0.2 -1,-0.1 -0.880 39.4 174.7-137.7 104.1 -8.0 5.5 1.6 10 133 A G + 0 0 81 -2,-0.4 2,-0.1 -7,-0.1 -3,-0.1 -0.022 28.6 152.3 -96.6 30.8 -7.6 9.2 0.8 11 134 A A - 0 0 32 1,-0.1 -7,-1.5 2,-0.0 2,-0.6 -0.398 42.7-131.7 -64.3 132.3 -4.1 9.3 2.3 12 135 A D E > -A 3 0A 103 -9,-0.2 2,-1.3 -2,-0.1 3,-0.7 -0.776 6.9-153.8 -91.2 120.5 -1.9 12.0 0.7 13 136 A L E 3 S+A 2 0A 2 -11,-3.6 -11,-0.9 -2,-0.6 -10,-0.1 -0.339 70.0 99.4 -88.0 54.3 1.5 10.8 -0.4 14 137 A S T 3 S+ 0 0 65 -2,-1.3 -1,-0.2 -13,-0.2 -11,-0.1 0.701 73.8 54.8-107.3 -31.8 3.1 14.2 -0.0 15 138 A K S < S+ 0 0 195 -3,-0.7 -2,-0.1 2,-0.0 -1,-0.0 0.832 94.2 86.4 -71.9 -33.1 4.7 13.9 3.4 16 139 A V - 0 0 30 -4,-0.2 3,-0.1 1,-0.1 10,-0.0 -0.037 67.5-148.9 -61.6 170.1 6.6 10.8 2.3 17 140 A K - 0 0 189 1,-0.4 2,-0.3 0, 0.0 -1,-0.1 0.719 62.0 -45.6-111.2 -37.9 10.0 11.0 0.5 18 141 A D S S+ 0 0 112 3,-0.0 2,-3.2 5,-0.0 -1,-0.4 -0.966 106.4 53.5-175.9-174.8 10.0 8.0 -1.8 19 142 A Y S > S+ 0 0 120 -2,-0.3 4,-1.9 1,-0.3 5,-0.1 -0.341 111.1 54.4 68.5 -67.5 9.2 4.2 -2.0 20 143 A H T 4>S+ 0 0 26 -2,-3.2 5,-2.0 1,-0.2 -1,-0.3 0.811 114.4 41.6 -64.9 -30.3 5.7 4.7 -0.7 21 144 A R T >45S+ 0 0 77 3,-0.2 3,-0.6 2,-0.2 -1,-0.2 0.745 108.0 61.2 -87.5 -27.1 5.1 7.3 -3.4 22 145 A R T 345S+ 0 0 195 1,-0.2 -2,-0.2 3,-0.1 -1,-0.1 0.920 114.3 33.3 -65.8 -45.2 6.8 5.3 -6.1 23 146 A H T 3<5S- 0 0 37 -4,-1.9 -1,-0.2 2,-0.1 -2,-0.2 0.197 117.1-113.5 -95.9 15.2 4.5 2.3 -5.8 24 147 A K T < 5S+ 0 0 115 -3,-0.6 -19,-0.7 1,-0.2 2,-0.2 0.959 71.6 117.6 50.2 87.0 1.5 4.6 -5.0 25 148 A V < - 0 0 0 -5,-2.0 -1,-0.2 -21,-0.2 -2,-0.1 -0.817 56.0-123.1-178.6 136.7 0.7 3.6 -1.4 26 149 A C > - 0 0 9 -2,-0.2 4,-0.6 1,-0.1 -13,-0.1 0.057 38.7 -99.2 -72.2-171.9 0.6 5.2 2.1 27 150 A E H > S+ 0 0 118 2,-0.1 4,-1.3 3,-0.1 -1,-0.1 0.769 115.4 60.3 -82.6 -27.9 2.6 4.0 5.1 28 151 A I H >4 S+ 0 0 124 2,-0.2 3,-1.0 1,-0.2 -1,-0.1 0.998 112.4 32.5 -62.3 -70.0 -0.5 2.2 6.6 29 152 A H H >4 S+ 0 0 32 1,-0.2 3,-1.3 2,-0.2 15,-0.6 0.763 109.5 72.8 -59.9 -25.0 -1.2 -0.3 3.8 30 153 A S H 3< S+ 0 0 8 -4,-0.6 -1,-0.2 1,-0.3 -2,-0.2 0.910 115.9 19.0 -56.2 -44.9 2.5 -0.4 3.1 31 154 A K T << S+ 0 0 134 -4,-1.3 -1,-0.3 -3,-1.0 -2,-0.2 -0.162 107.6 113.3-118.8 36.8 3.1 -2.4 6.3 32 155 A A < - 0 0 22 -3,-1.3 3,-0.1 1,-0.1 12,-0.1 -0.390 63.8-133.6-100.1-179.9 -0.5 -3.7 6.8 33 156 A T S S+ 0 0 102 1,-0.3 2,-0.4 -2,-0.1 -1,-0.1 0.831 86.9 29.1-100.7 -48.2 -2.0 -7.1 6.6 34 157 A T + 0 0 75 9,-0.1 2,-0.3 7,-0.1 -1,-0.3 -0.943 65.5 174.9-120.3 139.3 -5.1 -6.6 4.5 35 158 A A E -B 42 0B 2 7,-1.7 7,-2.2 -2,-0.4 2,-0.7 -0.992 25.5-135.1-142.6 148.4 -5.7 -4.0 1.8 36 159 A L E +B 41 0B 43 -2,-0.3 -29,-3.4 -29,-0.3 2,-0.5 -0.897 30.6 163.2-108.6 109.2 -8.4 -3.2 -0.7 37 160 A V E > S-B 40 0B 30 3,-1.1 3,-0.7 -2,-0.7 2,-0.4 -0.876 74.9 -26.6-129.3 100.1 -7.2 -2.5 -4.2 38 161 A G T 3 S- 0 0 70 -2,-0.5 3,-0.1 -33,-0.3 -2,-0.1 -0.228 122.1 -52.3 93.8 -45.4 -9.8 -2.7 -7.0 39 162 A G T 3 S+ 0 0 55 1,-0.4 2,-0.4 -2,-0.4 -1,-0.2 0.131 115.0 87.0 165.4 -30.2 -12.0 -5.1 -5.2 40 163 A I E < S-B 37 0B 117 -3,-0.7 -3,-1.1 1,-0.0 -1,-0.4 -0.805 77.6-114.5 -99.1 135.2 -9.9 -8.1 -4.1 41 164 A M E +B 36 0B 88 -2,-0.4 13,-1.1 -5,-0.2 2,-0.3 -0.319 45.2 161.2 -65.1 146.3 -8.1 -8.1 -0.8 42 165 A Q E -BC 35 53B 22 -7,-2.2 -7,-1.7 11,-0.3 2,-0.4 -0.924 32.6-122.2-155.0 177.1 -4.3 -8.1 -0.9 43 166 A R - 0 0 49 9,-2.8 9,-0.5 -2,-0.3 2,-0.4 -0.993 22.0-127.4-135.9 128.6 -1.1 -7.5 1.1 44 167 A F - 0 0 2 -15,-0.6 7,-0.2 -2,-0.4 2,-0.2 -0.580 26.5-140.0 -75.8 128.2 1.7 -5.1 0.2 45 168 A C - 0 0 24 5,-1.8 5,-0.4 -2,-0.4 -1,-0.0 -0.522 10.5-158.7 -87.1 155.4 5.2 -6.8 0.3 46 169 A Q S S+ 0 0 93 -2,-0.2 -1,-0.1 3,-0.2 -15,-0.0 0.835 90.1 42.3 -98.6 -46.3 8.3 -5.1 1.7 47 170 A Q S S+ 0 0 183 1,-0.2 -2,-0.0 3,-0.1 0, 0.0 0.970 128.3 30.0 -65.7 -55.8 11.0 -7.1 -0.0 48 171 A C S S- 0 0 94 2,-0.1 -1,-0.2 0, 0.0 -2,-0.1 0.807 98.7-144.7 -74.0 -30.6 9.4 -7.3 -3.5 49 172 A S + 0 0 25 1,-0.2 2,-0.3 -19,-0.1 -3,-0.2 0.998 55.8 102.3 62.1 69.6 7.7 -3.9 -2.9 50 173 A R S S- 0 0 139 -5,-0.4 -5,-1.8 -7,-0.1 -1,-0.2 -0.918 72.8 -96.3-175.1 149.2 4.4 -4.6 -4.7 51 174 A F + 0 0 10 -2,-0.3 2,-0.3 -7,-0.2 -7,-0.2 -0.425 43.4 169.5 -73.6 147.3 0.8 -5.4 -4.1 52 175 A H - 0 0 88 -9,-0.5 -9,-2.8 -2,-0.1 5,-0.1 -0.948 39.4 -92.7-161.1 137.8 -0.4 -9.0 -4.3 53 176 A V B > -C 42 0B 74 -2,-0.3 3,-0.5 -11,-0.3 4,-0.4 -0.084 30.0-131.5 -48.8 146.9 -3.5 -11.0 -3.4 54 177 A L T 3 S+ 0 0 61 -13,-1.1 -1,-0.1 1,-0.2 -12,-0.1 -0.146 77.6 109.2 -96.0 38.6 -3.5 -12.5 0.0 55 178 A E T 3 S+ 0 0 173 1,-0.1 -1,-0.2 -14,-0.1 -2,-0.1 0.791 94.7 21.3 -81.7 -30.2 -4.6 -16.0 -1.2 56 179 A E S < S+ 0 0 176 -3,-0.5 -2,-0.1 0, 0.0 -1,-0.1 0.603 100.7 111.2-109.4 -20.8 -1.2 -17.5 -0.5 57 180 A F 0 0 69 -4,-0.4 -3,-0.0 1,-0.1 -4,-0.0 -0.026 360.0 360.0 -51.7 159.3 0.1 -15.0 2.1 58 181 A D 0 0 218 0, 0.0 -1,-0.1 0, 0.0 -4,-0.0 0.930 360.0 360.0 -91.2 360.0 0.4 -16.1 5.7