==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=26-NOV-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SIGNALING PROTEIN 31-AUG-99 1CXX . COMPND 2 MOLECULE: CYSTEINE AND GLYCINE-RICH PROTEIN CRP2; . SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX JAPONICA; . AUTHOR K.KLOIBER,R.WEISKIRCHEN,B.KRAEUTLER,K.BISTER,R.KONRAT . 59 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4021.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 23 39.0 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 . 10 16.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 3.4 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 . 2 3.4 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 . 1 1.7 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 . 5 8.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 2 3.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 6 10.2 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+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 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 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 . 2 2 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 . 2 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 1 117 A A 0 0 108 0, 0.0 2,-1.5 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -54.8 4.5 8.9 4.7 2 118 A E + 0 0 109 20,-0.1 9,-0.6 9,-0.1 2,-0.3 -0.624 360.0 118.8 -87.5 81.3 1.1 8.9 2.9 3 119 A K B -A 10 0A 103 -2,-1.5 2,-0.7 7,-0.3 7,-0.2 -0.982 60.2-133.8-154.3 137.8 1.9 6.6 0.1 4 120 A C > - 0 0 1 5,-2.1 4,-1.0 -2,-0.3 20,-0.2 -0.802 14.0-167.7 -90.8 115.1 0.8 3.3 -1.3 5 121 A S T 4 S+ 0 0 76 -2,-0.7 -1,-0.1 18,-0.4 19,-0.1 0.325 78.8 68.7 -83.1 4.8 3.9 1.3 -2.1 6 122 A A T 4 S+ 0 0 47 3,-0.2 -1,-0.2 1,-0.0 18,-0.1 0.935 117.2 15.2 -87.2 -57.9 1.8 -1.2 -4.1 7 123 A C T 4 S- 0 0 55 2,-0.2 -2,-0.2 0, 0.0 3,-0.1 0.573 103.1-122.5 -90.6 -13.6 0.7 0.9 -7.1 8 124 A G S < S+ 0 0 65 -4,-1.0 2,-0.2 1,-0.4 -3,-0.1 0.332 74.2 121.2 87.2 -5.2 3.3 3.5 -6.4 9 125 A D - 0 0 102 1,-0.1 -5,-2.1 -6,-0.1 -1,-0.4 -0.524 67.7-106.6 -88.7 158.0 0.7 6.2 -6.1 10 126 A S B -A 3 0A 83 -7,-0.2 -7,-0.3 -2,-0.2 2,-0.1 -0.494 34.6-113.6 -82.6 157.3 0.1 8.3 -3.0 11 127 A V - 0 0 10 -9,-0.6 -1,-0.1 -2,-0.1 -9,-0.1 -0.381 13.4-133.8 -86.1 165.6 -2.8 7.8 -0.8 12 128 A Y - 0 0 158 -2,-0.1 -1,-0.1 1,-0.0 -10,-0.0 0.894 32.2-114.2 -79.1 -96.1 -5.7 10.2 -0.1 13 129 A A S S+ 0 0 56 0, 0.0 2,-0.5 0, 0.0 -1,-0.0 0.028 100.3 40.7-171.9 -56.6 -6.5 10.5 3.6 14 130 A A S S+ 0 0 83 1,-0.1 3,-0.1 3,-0.0 0, 0.0 -0.662 115.6 44.5-114.6 69.8 -10.0 9.0 4.2 15 131 A E S S+ 0 0 93 -2,-0.5 -1,-0.1 1,-0.4 -4,-0.0 0.056 83.6 89.9-164.9 -62.6 -9.9 6.0 2.0 16 132 A K - 0 0 36 9,-0.1 -1,-0.4 1,-0.1 2,-0.4 -0.256 69.5-130.7 -60.8 136.5 -6.7 4.1 2.4 17 133 A V E -B 24 0B 31 7,-1.5 7,-2.2 -3,-0.1 2,-0.4 -0.751 21.8-138.1 -89.2 131.5 -6.5 1.4 5.0 18 134 A I E -B 23 0B 94 -2,-0.4 2,-0.2 5,-0.2 4,-0.1 -0.804 13.6-162.5 -99.7 135.9 -3.4 1.6 7.2 19 135 A G S S- 0 0 2 3,-2.4 3,-0.5 -2,-0.4 -1,-0.1 -0.467 76.9 -60.2-109.9 52.8 -1.4 -1.4 8.2 20 136 A A S S- 0 0 88 1,-0.3 2,-1.3 -2,-0.2 -1,-0.1 0.994 116.7 -22.2 63.2 83.1 0.4 0.4 11.1 21 137 A G S S+ 0 0 54 1,-0.1 -1,-0.3 -19,-0.0 0, 0.0 -0.678 119.2 91.1 95.3 -79.0 2.2 3.3 9.4 22 138 A K - 0 0 76 -2,-1.3 -3,-2.4 -3,-0.5 2,-0.4 -0.326 67.8-155.5 -54.1 107.2 2.4 1.8 5.9 23 139 A P E +B 18 0B 3 0, 0.0 -18,-0.4 0, 0.0 2,-0.3 -0.785 15.1 178.2 -98.9 135.2 -0.8 3.0 4.0 24 140 A W E -B 17 0B 25 -7,-2.2 -7,-1.5 -2,-0.4 5,-0.1 -0.948 32.4-100.2-132.2 151.6 -2.3 1.2 1.1 25 141 A H > - 0 0 24 -2,-0.3 4,-0.8 -9,-0.2 -9,-0.1 -0.234 32.5-114.7 -68.1 159.1 -5.4 1.8 -1.1 26 142 A K T 4 S+ 0 0 89 1,-0.2 12,-0.3 2,-0.2 3,-0.2 0.859 120.3 39.9 -60.2 -38.2 -8.6 -0.2 -0.4 27 143 A N T 4 S+ 0 0 141 1,-0.2 -1,-0.2 10,-0.1 11,-0.1 0.796 110.5 57.9 -80.9 -34.0 -8.2 -1.9 -3.8 28 144 A C T 4 S+ 0 0 16 1,-0.1 2,-1.3 9,-0.0 -2,-0.2 0.560 77.6 107.4 -75.1 -8.8 -4.4 -2.3 -3.5 29 145 A F < + 0 0 2 -4,-0.8 9,-1.0 -3,-0.2 2,-0.4 -0.611 46.6 156.2 -78.2 97.4 -4.8 -4.3 -0.3 30 146 A R B -C 37 0C 131 -2,-1.3 20,-0.3 7,-0.2 7,-0.2 -0.976 41.7-111.1-127.9 136.5 -3.9 -7.7 -1.7 31 147 A C - 0 0 13 5,-1.9 20,-0.3 -2,-0.4 14,-0.0 -0.105 9.9-151.8 -64.1 162.0 -2.7 -10.7 0.4 32 148 A A S S+ 0 0 36 3,-0.1 19,-0.2 20,-0.1 -1,-0.1 0.354 91.8 48.6-115.8 -1.3 0.9 -12.0 0.1 33 149 A K S S+ 0 0 104 17,-0.1 18,-0.1 3,-0.1 -2,-0.0 0.844 136.7 0.1 -98.1 -64.6 0.0 -15.7 1.1 34 150 A C S S- 0 0 65 2,-0.1 17,-0.0 18,-0.1 -2,-0.0 0.850 93.8-128.8 -92.1 -46.5 -3.0 -16.5 -1.1 35 151 A G + 0 0 51 1,-0.2 2,-0.2 2,-0.0 -3,-0.1 0.914 55.8 126.0 91.4 61.1 -3.3 -13.2 -2.9 36 152 A K - 0 0 91 1,-0.1 -5,-1.9 0, 0.0 -1,-0.2 -0.718 63.9 -59.7-132.2-177.5 -7.0 -12.1 -2.6 37 153 A S B +C 30 0C 99 -2,-0.2 2,-0.3 -7,-0.2 -7,-0.2 -0.337 54.9 177.8 -65.5 143.5 -9.1 -9.2 -1.5 38 154 A L + 0 0 13 -9,-1.0 -9,-0.1 -12,-0.3 2,-0.1 -0.959 25.3 146.8-159.6 136.1 -8.7 -8.1 2.1 39 155 A E + 0 0 102 -2,-0.3 2,-0.1 -9,-0.0 13,-0.1 -0.534 32.6 170.4-170.7 88.3 -10.0 -5.3 4.4 40 156 A S - 0 0 24 -2,-0.1 -2,-0.0 1,-0.1 12,-0.0 -0.255 44.7-116.9-100.0-177.5 -10.4 -6.5 7.9 41 157 A T S S+ 0 0 142 -2,-0.1 -1,-0.1 0, 0.0 0, 0.0 0.900 116.2 13.4 -82.6 -57.2 -11.0 -5.3 11.4 42 158 A T S S- 0 0 111 -3,-0.0 -2,-0.0 2,-0.0 0, 0.0 0.915 98.4-161.9 -82.8 -56.9 -7.7 -6.2 12.9 43 159 A L - 0 0 11 1,-0.1 2,-0.4 -24,-0.0 9,-0.1 0.689 14.0-116.7 67.6 132.0 -5.9 -6.9 9.6 44 160 A T + 0 0 25 7,-0.5 7,-1.2 2,-0.0 2,-0.3 -0.806 40.2 157.4-100.1 131.7 -2.7 -8.8 9.3 45 161 A E E -D 50 0D 60 -2,-0.4 5,-0.2 5,-0.2 2,-0.2 -0.933 14.2-171.9-157.6 128.5 0.4 -7.2 8.1 46 162 A K E > -D 49 0D 113 3,-2.0 3,-1.1 -2,-0.3 -27,-0.0 -0.589 42.7-102.0-115.0 178.0 4.0 -8.4 8.7 47 163 A E T 3 S+ 0 0 210 1,-0.2 3,-0.1 -2,-0.2 -2,-0.0 -0.101 121.6 59.2 -92.0 33.3 7.4 -6.9 8.1 48 164 A G T 3 S- 0 0 40 1,-0.6 2,-0.2 0, 0.0 -1,-0.2 0.228 124.7 -61.5-141.0 6.1 7.5 -9.3 5.1 49 165 A E E < -D 46 0D 126 -3,-1.1 -3,-2.0 2,-0.0 -1,-0.6 -0.857 64.4 -64.0 140.1-166.1 4.4 -8.0 3.2 50 166 A I E -D 45 0D 17 -20,-0.3 2,-0.2 -2,-0.2 -5,-0.2 -0.984 48.7-175.3-124.2 129.4 0.6 -7.6 3.8 51 167 A Y - 0 0 29 -7,-1.2 -7,-0.5 -2,-0.4 2,-0.3 -0.691 27.9-104.5-120.7 170.6 -1.8 -10.5 4.2 52 168 A C >> - 0 0 0 -2,-0.2 3,-0.9 -9,-0.1 4,-0.6 -0.699 24.8-131.9 -92.8 144.7 -5.5 -11.3 4.5 53 169 A K H 3> S+ 0 0 98 -2,-0.3 4,-1.1 1,-0.2 3,-0.4 0.738 105.4 69.0 -69.0 -22.2 -6.8 -12.2 8.0 54 170 A G H 3> S+ 0 0 17 1,-0.2 4,-1.8 2,-0.2 -1,-0.2 0.768 90.0 61.8 -64.6 -29.9 -8.5 -15.2 6.4 55 171 A C H <> S+ 0 0 7 -3,-0.9 4,-1.8 1,-0.2 -1,-0.2 0.857 108.2 41.8 -65.5 -37.5 -5.1 -16.7 5.8 56 172 A Y H < S+ 0 0 72 -4,-0.6 -1,-0.2 -3,-0.4 -2,-0.2 0.687 108.9 60.3 -82.5 -21.0 -4.4 -16.9 9.5 57 173 A A H < S+ 0 0 86 -4,-1.1 -2,-0.2 2,-0.2 -1,-0.2 0.888 111.7 39.3 -70.3 -39.8 -8.0 -18.0 10.2 58 174 A K H < 0 0 151 -4,-1.8 -2,-0.2 -5,-0.1 -1,-0.2 0.894 360.0 360.0 -71.9 -45.4 -7.3 -21.1 8.0 59 175 A N < 0 0 147 -4,-1.8 -3,-0.2 -5,-0.2 -2,-0.2 0.956 360.0 360.0 -84.4 360.0 -3.8 -21.5 9.4