==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=19-APR-2013 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SIGNALING PROTEIN 06-DEC-11 2LMK . COMPND 2 MOLECULE: EXOCRINE GLAND-SECRETING PEPTIDE 1; . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR S.YOSHINAGA,T.SATO,M.HIRAKANE,K.ESAKI,T.HAMAGUCHI,S.HAGA-YAM . 57 1 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4987.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 28 49.1 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 . 0 0.0 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 . 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 . 3 5.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 12 21.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 13 22.8 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 1 0 1 0 1 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 . 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 46 A G 0 0 135 0, 0.0 2,-0.3 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -82.7 2.1 0.0 -1.2 2 47 A S - 0 0 117 0, 0.0 0, 0.0 0, 0.0 0, 0.0 -0.935 360.0 -97.8-165.8 140.3 3.1 3.6 -2.0 3 48 A N - 0 0 67 -2,-0.3 27,-0.1 30,-0.1 31,-0.0 -0.051 48.3-100.5 -55.3 160.6 1.7 7.1 -1.7 4 49 A P - 0 0 32 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 0.150 39.8 -95.8 -69.7-168.1 -0.0 8.7 -4.8 5 50 A D >> - 0 0 73 1,-0.0 4,-2.6 32,-0.0 3,-0.5 -0.762 22.5-114.5-115.1 161.5 1.5 11.3 -7.1 6 51 A P T 34 S+ 0 0 54 0, 0.0 4,-0.3 0, 0.0 33,-0.2 0.531 114.7 60.3 -69.7 -5.2 1.3 15.1 -7.3 7 52 A Q T 3> S+ 0 0 156 3,-0.1 4,-0.7 2,-0.1 30,-0.0 0.812 114.0 30.3 -90.7 -36.2 -0.6 14.7 -10.6 8 53 A E H <> S+ 0 0 103 -3,-0.5 4,-0.5 2,-0.1 5,-0.1 0.819 123.8 47.2 -90.6 -37.1 -3.5 12.7 -9.2 9 54 A V H >X S+ 0 0 0 -4,-2.6 4,-1.7 2,-0.2 3,-0.8 0.921 107.3 56.3 -70.4 -45.7 -3.5 14.2 -5.7 10 55 A Q H >> S+ 0 0 64 -5,-0.3 4,-1.0 -4,-0.3 3,-0.6 0.925 109.3 45.8 -51.7 -50.3 -3.2 17.8 -6.9 11 56 A R H 3< S+ 0 0 176 -4,-0.7 -1,-0.3 1,-0.2 -2,-0.2 0.693 112.3 54.1 -67.5 -18.1 -6.4 17.5 -9.0 12 57 A A H << S+ 0 0 14 -3,-0.8 4,-0.3 -4,-0.5 -1,-0.2 0.713 94.7 68.8 -87.2 -23.7 -8.0 15.8 -6.0 13 58 A L H X< S+ 0 0 5 -4,-1.7 3,-1.3 -3,-0.6 -2,-0.2 0.954 105.3 39.0 -59.4 -52.9 -7.2 18.7 -3.7 14 59 A A T >< S+ 0 0 38 -4,-1.0 3,-0.7 1,-0.3 -1,-0.2 0.559 105.1 72.1 -74.5 -7.7 -9.6 21.1 -5.4 15 60 A R T >> + 0 0 146 -3,-0.2 4,-3.2 1,-0.2 3,-0.7 0.516 69.9 90.0 -84.1 -5.8 -12.0 18.2 -5.7 16 61 A I H <> S+ 0 0 32 -3,-1.3 4,-0.9 -4,-0.3 -1,-0.2 0.742 87.5 50.8 -61.6 -22.6 -12.6 18.3 -2.0 17 62 A L H <4 S+ 0 0 45 -3,-0.7 -1,-0.3 2,-0.1 -2,-0.2 0.724 114.7 41.8 -86.5 -24.4 -15.5 20.7 -2.8 18 63 A a H <4 S+ 0 0 45 -3,-0.7 -2,-0.2 -4,-0.2 -1,-0.1 0.803 120.3 41.8 -90.3 -34.9 -17.0 18.4 -5.4 19 64 A A H < S- 0 0 36 -4,-3.2 -3,-0.2 -7,-0.2 -2,-0.1 0.983 76.2-176.5 -75.3 -64.4 -16.5 15.1 -3.4 20 65 A L S < S+ 0 0 85 -4,-0.9 -3,-0.1 -5,-0.3 -4,-0.1 0.994 78.6 14.0 61.2 79.6 -17.5 16.2 0.1 21 66 A G S S+ 0 0 40 -5,-0.2 -1,-0.1 0, 0.0 -5,-0.1 0.149 122.1 64.6 113.4 -17.9 -16.9 13.1 2.2 22 67 A E S > S+ 0 0 131 -6,-0.1 3,-1.6 2,-0.1 4,-0.3 0.812 96.5 50.4-101.8 -45.5 -14.8 11.2 -0.4 23 68 A L T >> S+ 0 0 18 1,-0.3 4,-2.5 -8,-0.2 3,-1.7 0.749 93.7 77.9 -65.6 -23.4 -11.7 13.4 -0.8 24 69 A D H 3> S+ 0 0 80 1,-0.3 4,-0.9 2,-0.2 -1,-0.3 0.740 86.8 61.0 -57.9 -22.4 -11.5 13.4 3.0 25 70 A K H <> S+ 0 0 156 -3,-1.6 4,-0.9 2,-0.2 -1,-0.3 0.764 110.2 39.2 -76.0 -26.1 -10.0 9.9 2.6 26 71 A L H <4 S+ 0 0 38 -3,-1.7 4,-0.4 -4,-0.3 5,-0.3 0.900 109.3 56.4 -88.2 -49.7 -7.1 11.3 0.6 27 72 A V H X S+ 0 0 28 -4,-2.5 4,-2.0 1,-0.2 3,-0.2 0.787 111.6 48.3 -53.2 -28.1 -6.4 14.5 2.5 28 73 A K H X S+ 0 0 126 -4,-0.9 4,-0.6 -5,-0.3 -1,-0.2 0.892 115.8 40.2 -79.9 -43.1 -6.0 12.3 5.5 29 74 A D H < S+ 0 0 102 -4,-0.9 -2,-0.2 3,-0.1 -1,-0.2 0.194 126.0 40.0 -90.3 15.9 -3.6 9.8 3.9 30 75 A Q H > S+ 0 0 2 -4,-0.4 4,-0.7 -3,-0.2 7,-0.2 0.624 118.1 38.4-126.7 -49.1 -1.9 12.6 2.1 31 76 A A H < S+ 0 0 22 -4,-2.0 4,-0.2 -5,-0.3 -3,-0.2 0.561 133.5 29.6 -83.3 -9.4 -1.5 15.5 4.5 32 77 A N T < S+ 0 0 119 -4,-0.6 -1,-0.2 -5,-0.2 -3,-0.1 0.259 125.4 44.9-129.8 6.0 -0.8 13.1 7.4 33 78 A A T 4 S- 0 0 50 -6,-0.1 -2,-0.2 0, 0.0 -30,-0.1 0.286 135.7 -37.6-130.9 3.4 0.8 10.3 5.4 34 79 A G >< - 0 0 28 -4,-0.7 3,-0.7 -31,-0.0 -2,-0.1 0.390 48.0-177.8 132.9 87.2 3.2 12.3 3.2 35 80 A Q T 3 + 0 0 67 1,-0.2 -4,-0.1 -4,-0.2 -5,-0.1 0.283 64.5 101.3 -88.8 10.3 2.3 15.6 1.7 36 81 A Q T 3 + 0 0 186 1,-0.2 -1,-0.2 -6,-0.1 -5,-0.1 0.625 64.4 80.7 -68.6 -12.2 5.7 15.7 -0.1 37 82 A E S < S+ 0 0 49 -3,-0.7 -1,-0.2 -7,-0.2 -2,-0.1 0.987 99.0 19.0 -56.2 -80.0 3.8 14.6 -3.2 38 83 A F - 0 0 12 -33,-0.2 -31,-0.1 2,-0.1 0, 0.0 -0.101 64.9-141.5 -82.6-174.7 2.4 17.9 -4.5 39 84 A K + 0 0 207 -33,-0.2 -1,-0.1 2,-0.1 -3,-0.1 0.246 64.3 108.4-132.3 6.9 3.5 21.5 -3.6 40 85 A L - 0 0 54 1,-0.1 -2,-0.1 2,-0.0 -27,-0.0 -0.651 68.7-114.0 -91.2 145.6 0.1 23.2 -3.4 41 86 A P - 0 0 76 0, 0.0 4,-0.1 0, 0.0 -1,-0.1 -0.135 13.6-126.8 -69.7 169.4 -1.4 24.3 -0.1 42 87 A K S > S+ 0 0 100 1,-0.2 3,-0.9 2,-0.1 -2,-0.0 0.692 106.1 62.4 -90.6 -22.4 -4.6 22.9 1.4 43 88 A D G > S+ 0 0 150 1,-0.2 3,-0.6 2,-0.1 -1,-0.2 0.760 85.1 75.8 -73.3 -25.4 -6.3 26.3 1.8 44 89 A F G > S+ 0 0 127 1,-0.3 3,-0.6 2,-0.1 2,-0.6 0.740 83.3 70.0 -57.7 -22.3 -6.2 26.8 -2.0 45 90 A T G < + 0 0 19 -3,-0.9 -1,-0.3 1,-0.2 3,-0.1 -0.230 64.8 108.6 -91.0 45.0 -9.1 24.3 -2.1 46 91 A G G < S+ 0 0 58 -3,-0.6 2,-0.3 -2,-0.6 -1,-0.2 0.674 82.7 24.5 -92.7 -20.0 -11.5 26.8 -0.5 47 92 A R < + 0 0 216 -3,-0.6 -1,-0.3 4,-0.0 2,-0.2 -0.995 66.2 164.0-148.3 139.4 -13.5 27.4 -3.7 48 93 A S - 0 0 39 -2,-0.3 3,-0.1 -3,-0.1 -33,-0.1 -0.817 46.9-108.0-142.2-179.0 -14.2 25.4 -6.8 49 94 A K S S+ 0 0 211 -2,-0.2 2,-1.3 1,-0.2 -1,-0.0 0.712 102.5 75.2 -87.1 -23.4 -16.5 25.2 -9.8 50 95 A a S S- 0 0 33 2,-0.0 -1,-0.2 3,-0.0 -2,-0.0 -0.687 79.2-154.6 -93.3 85.1 -18.3 22.1 -8.5 51 96 A R - 0 0 176 -2,-1.3 -2,-0.1 1,-0.1 -4,-0.0 -0.014 34.1 -97.1 -52.7 162.5 -20.5 23.5 -5.8 52 97 A S - 0 0 60 1,-0.1 -1,-0.1 3,-0.0 4,-0.1 0.811 43.5-158.7 -53.0 -31.2 -21.5 21.2 -2.9 53 98 A L + 0 0 114 1,-0.1 -1,-0.1 2,-0.1 3,-0.1 0.786 66.9 95.1 54.4 27.9 -24.8 20.7 -4.8 54 99 A G S S+ 0 0 58 1,-0.1 2,-0.8 3,-0.0 -1,-0.1 0.775 73.8 48.2-111.6 -49.5 -26.3 19.6 -1.5 55 100 A R S S+ 0 0 230 1,-0.2 2,-0.4 2,-0.0 -2,-0.1 -0.277 70.7 129.9 -90.2 48.6 -28.0 22.7 0.0 56 101 A I 0 0 133 -2,-0.8 -1,-0.2 -3,-0.1 0, 0.0 -0.264 360.0 360.0 -96.4 46.1 -29.8 23.5 -3.2 57 102 A K 0 0 249 -2,-0.4 -3,-0.0 0, 0.0 -2,-0.0 -0.881 360.0 360.0-147.5 360.0 -33.2 23.9 -1.6