==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=29-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER METAL BINDING PROTEIN 08-DEC-05 2D8S . COMPND 2 MOLECULE: CELLULAR MODULATOR OF IMMUNE RECOGNITION; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR K.MIYAMOTO,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA, . 80 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 6686.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 29 36.2 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 . 5 6.2 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 2.5 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 . 1 1.2 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 . 10 12.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 3 3.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 8 10.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 1.2 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 0 0 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 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 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 0 124 0, 0.0 2,-1.1 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 85.3 -34.5 3.3 15.3 2 2 A S + 0 0 144 2,-0.0 2,-0.4 0, 0.0 0, 0.0 -0.154 360.0 90.8 -81.3 42.9 -32.1 6.2 14.6 3 3 A S - 0 0 108 -2,-1.1 2,-0.1 0, 0.0 0, 0.0 -0.992 61.5-151.5-142.9 131.5 -29.2 3.7 14.5 4 4 A G - 0 0 71 -2,-0.4 2,-0.4 1,-0.1 -2,-0.0 -0.365 26.9 -98.4 -94.4 176.5 -27.7 1.7 11.7 5 5 A S + 0 0 132 -2,-0.1 2,-0.3 2,-0.0 -1,-0.1 -0.824 55.3 134.4-100.5 133.4 -25.9 -1.6 11.6 6 6 A S + 0 0 126 -2,-0.4 2,-0.2 2,-0.0 -2,-0.0 -0.881 12.3 149.0-174.4 140.8 -22.1 -1.8 11.5 7 7 A G - 0 0 66 -2,-0.3 2,-0.7 2,-0.0 -2,-0.0 -0.665 52.9 -45.7-150.8-154.1 -19.3 -3.7 13.2 8 8 A T + 0 0 144 -2,-0.2 2,-0.3 2,-0.0 -2,-0.0 -0.837 69.8 133.6 -98.0 114.2 -15.8 -5.0 12.8 9 9 A S - 0 0 114 -2,-0.7 2,-0.3 2,-0.0 -2,-0.0 -0.965 36.2-148.4-152.4 165.3 -15.3 -6.9 9.6 10 10 A I - 0 0 157 -2,-0.3 -2,-0.0 0, 0.0 0, 0.0 -0.994 29.4-106.7-144.4 134.4 -12.9 -7.3 6.6 11 11 A T - 0 0 87 -2,-0.3 -2,-0.0 1,-0.1 0, 0.0 -0.335 40.7-126.0 -60.3 131.5 -13.4 -8.2 3.0 12 12 A P > - 0 0 89 0, 0.0 2,-1.0 0, 0.0 3,-0.6 -0.032 31.2 -90.2 -69.7 177.8 -12.2 -11.7 2.1 13 13 A S T 3 S+ 0 0 112 1,-0.2 3,-0.1 3,-0.1 -2,-0.0 -0.236 91.0 113.8 -86.6 46.9 -9.8 -12.6 -0.6 14 14 A S T 3 S+ 0 0 94 -2,-1.0 2,-0.3 1,-0.3 -1,-0.2 0.877 82.6 12.5 -83.3 -42.1 -12.6 -13.1 -3.1 15 15 A Q S < S- 0 0 104 -3,-0.6 2,-0.7 2,-0.0 -1,-0.3 -1.000 75.0-121.7-140.5 140.2 -11.6 -10.2 -5.4 16 16 A D + 0 0 85 -2,-0.3 9,-0.3 -3,-0.1 2,-0.3 -0.709 48.4 149.7 -84.1 116.0 -8.5 -8.0 -5.7 17 17 A I - 0 0 19 -2,-0.7 26,-0.3 1,-0.2 7,-0.2 -0.954 51.7 -61.7-143.4 161.3 -9.4 -4.3 -5.2 18 18 A C - 0 0 1 5,-1.6 26,-0.2 -2,-0.3 -1,-0.2 0.081 34.9-153.1 -38.0 151.7 -7.8 -1.1 -3.9 19 19 A R S S+ 0 0 109 24,-0.1 -1,-0.1 3,-0.1 25,-0.1 0.510 90.2 44.9-108.5 -11.4 -6.8 -1.2 -0.2 20 20 A I S S+ 0 0 49 3,-0.1 24,-0.1 0, 0.0 -2,-0.0 0.858 133.4 13.3 -97.3 -50.2 -7.1 2.5 0.4 21 21 A C S S- 0 0 51 2,-0.1 -2,-0.1 0, 0.0 -3,-0.0 0.676 91.9-137.2 -99.1 -24.0 -10.4 3.4 -1.3 22 22 A H + 0 0 121 1,-0.2 2,-0.3 -5,-0.0 -3,-0.1 0.967 54.4 134.2 64.6 55.0 -11.6 -0.2 -1.8 23 23 A C - 0 0 67 1,-0.0 -5,-1.6 3,-0.0 -1,-0.2 -0.873 62.0 -80.4-131.6 164.2 -12.9 0.3 -5.3 24 24 A E - 0 0 146 -2,-0.3 2,-0.3 -7,-0.2 -7,-0.1 -0.317 55.4 -98.8 -63.7 144.2 -12.7 -1.5 -8.6 25 25 A G - 0 0 40 -9,-0.3 2,-0.2 6,-0.1 -1,-0.1 -0.500 41.7-154.2 -69.2 123.7 -9.4 -1.1 -10.6 26 26 A D - 0 0 84 3,-1.2 -1,-0.0 -2,-0.3 -3,-0.0 -0.534 28.6-108.2 -95.6 163.9 -9.8 1.5 -13.3 27 27 A D S S+ 0 0 133 1,-0.2 -1,-0.1 2,-0.2 -2,-0.0 0.867 124.8 31.2 -56.8 -38.2 -7.9 1.8 -16.6 28 28 A E S S+ 0 0 159 1,-0.2 -1,-0.2 17,-0.0 19,-0.1 0.781 131.5 36.3 -89.9 -32.0 -6.1 4.9 -15.2 29 29 A S S S+ 0 0 21 17,-0.1 -3,-1.2 16,-0.1 -2,-0.2 -0.350 84.7 163.0-117.5 50.3 -6.2 3.8 -11.6 30 30 A P - 0 0 48 0, 0.0 2,-0.8 0, 0.0 16,-0.7 -0.343 52.5 -91.3 -69.8 149.3 -5.7 -0.0 -12.1 31 31 A L E +A 45 0A 53 14,-0.1 2,-0.3 -15,-0.1 14,-0.2 -0.478 59.3 172.4 -65.0 104.4 -4.6 -2.2 -9.1 32 32 A I E -A 44 0A 55 12,-1.7 12,-0.9 -2,-0.8 3,-0.0 -0.874 37.5-110.7-118.0 150.6 -0.8 -2.2 -9.4 33 33 A T - 0 0 78 -2,-0.3 10,-0.1 10,-0.2 5,-0.1 -0.689 20.0-165.1 -83.1 112.8 1.8 -3.5 -7.0 34 34 A P S S- 0 0 3 0, 0.0 2,-0.3 0, 0.0 -1,-0.2 0.646 74.7 -2.7 -69.8 -14.9 3.7 -0.6 -5.3 35 35 A C S S- 0 0 7 2,-0.4 33,-0.0 7,-0.3 7,-0.0 -0.904 91.1 -76.5-159.1-175.5 6.4 -3.1 -4.3 36 36 A H S S+ 0 0 143 -2,-0.3 -1,-0.1 2,-0.1 -3,-0.0 0.921 90.3 109.2 -60.1 -46.0 7.4 -6.8 -4.2 37 37 A C + 0 0 20 1,-0.1 -2,-0.4 -3,-0.0 2,-0.3 0.011 49.4 170.2 -34.8 127.1 5.0 -7.6 -1.4 38 38 A T + 0 0 112 -5,-0.1 2,-1.1 5,-0.0 3,-0.1 -0.861 36.4 46.4-139.2 173.0 2.2 -9.7 -3.0 39 39 A G S S+ 0 0 51 -2,-0.3 4,-0.1 1,-0.2 -2,-0.0 -0.677 91.9 71.3 97.6 -82.7 -0.8 -11.8 -1.9 40 40 A S S S- 0 0 91 -2,-1.1 2,-2.3 1,-0.2 -1,-0.2 0.206 114.6 -66.9 -55.8-173.7 -2.6 -9.6 0.6 41 41 A L S S+ 0 0 74 1,-0.2 -1,-0.2 -3,-0.1 -22,-0.0 -0.194 86.8 133.2 -75.4 48.8 -4.5 -6.5 -0.3 42 42 A H + 0 0 33 -2,-2.3 2,-0.8 1,-0.1 -7,-0.3 0.064 37.5 106.9 -87.6 25.5 -1.2 -4.8 -1.3 43 43 A F + 0 0 17 -26,-0.3 2,-0.2 -10,-0.1 -10,-0.2 -0.836 46.2 169.7-109.8 95.5 -2.8 -3.6 -4.5 44 44 A V E -A 32 0A 7 -12,-0.9 -12,-1.7 -2,-0.8 2,-0.2 -0.649 39.5 -94.3-102.9 161.0 -3.4 0.1 -4.4 45 45 A H E > -A 31 0A 7 -2,-0.2 4,-3.1 -14,-0.2 5,-0.2 -0.514 31.0-121.1 -75.1 138.5 -4.4 2.5 -7.1 46 46 A Q T 4 S+ 0 0 35 -16,-0.7 4,-0.5 -2,-0.2 -1,-0.1 0.872 115.4 36.9 -43.3 -45.6 -1.6 4.4 -8.9 47 47 A A T >> S+ 0 0 47 2,-0.2 3,-2.7 1,-0.1 4,-0.7 0.983 112.5 54.5 -72.7 -61.4 -3.3 7.6 -7.8 48 48 A C H 3> S+ 0 0 28 1,-0.3 4,-1.9 2,-0.2 5,-0.3 0.866 94.3 72.4 -39.0 -48.6 -4.5 6.6 -4.4 49 49 A L H 3X S+ 0 0 4 -4,-3.1 4,-2.2 1,-0.2 -1,-0.3 0.831 96.3 53.1 -36.7 -43.3 -0.9 5.6 -3.5 50 50 A Q H X> S+ 0 0 75 -3,-2.7 4,-2.2 -4,-0.5 3,-0.7 0.994 102.2 52.6 -58.4 -69.8 -0.1 9.3 -3.4 51 51 A Q H 3X S+ 0 0 121 -4,-0.7 4,-2.2 1,-0.3 -1,-0.2 0.827 113.1 48.6 -34.2 -45.5 -2.8 10.4 -1.0 52 52 A W H 3X>S+ 0 0 55 -4,-1.9 4,-2.4 1,-0.2 5,-0.6 0.929 107.0 53.9 -64.5 -46.8 -1.5 7.7 1.3 53 53 A I H