==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=2-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER IMMUNE SYSTEM, SIGNALING PROTEIN 07-JUN-08 2K4F . COMPND 2 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD3 EPSILON CHAIN; . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR C.XU,M.E.CALL,C.D.SCHWIETERS,J.R.SCHNELL,E.E.GAGNON, . 57 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 5775.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 18 31.6 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 . 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 . 4 7.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 9 15.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 4 7.0 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 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 . 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 1 A C 0 0 131 0, 0.0 2,-0.3 0, 0.0 23,-0.2 0.000 360.0 360.0 360.0 16.2 38.0 -12.4 -3.5 2 2 A S >> - 0 0 12 21,-0.1 3,-1.5 20,-0.1 4,-0.6 -0.870 360.0 -12.3-163.9 127.1 38.9 -16.1 -3.8 3 3 A K T 34 S- 0 0 111 1,-0.3 5,-0.1 -2,-0.3 23,-0.0 0.663 94.6-104.6 55.3 14.9 36.8 -19.3 -3.5 4 4 A N T 34 S+ 0 0 79 1,-0.1 -1,-0.3 3,-0.1 4,-0.1 0.723 98.8 114.4 40.4 21.9 34.1 -16.9 -2.0 5 5 A R T <4 S- 0 0 145 -3,-1.5 -2,-0.1 2,-0.1 -1,-0.1 0.966 92.5 -52.3 -81.8 -66.5 35.3 -18.5 1.3 6 6 A K S < S- 0 0 57 -4,-0.6 2,-4.1 30,-0.1 3,-0.3 -0.250 81.4 -69.0-178.7 79.9 37.0 -15.7 3.2 7 7 A A - 0 0 41 1,-0.2 -3,-0.1 2,-0.1 -2,-0.1 -0.255 59.8-157.4 63.5 -63.6 39.6 -13.5 1.5 8 8 A K + 0 0 74 -2,-4.1 -1,-0.2 1,-0.1 -4,-0.0 0.984 65.2 89.8 53.3 70.0 42.0 -16.5 1.5 9 9 A A + 0 0 66 -3,-0.3 -2,-0.1 -7,-0.0 -1,-0.1 0.232 60.7 80.4-173.7 11.3 45.3 -14.5 1.3 10 10 A K + 0 0 105 32,-0.1 2,-1.2 1,-0.1 3,-0.1 0.784 60.2 100.1 -97.5 -35.8 46.2 -13.8 4.9 11 11 A P > > + 0 0 27 0, 0.0 5,-1.0 0, 0.0 3,-0.6 -0.318 44.0 174.2 -56.7 91.6 47.8 -17.2 5.8 12 12 A V G > 5S+ 0 0 49 -2,-1.2 3,-2.4 1,-0.2 31,-0.1 0.891 77.0 60.0 -67.3 -40.5 51.5 -16.2 5.4 13 13 A T G 3 5S+ 0 0 73 1,-0.3 -1,-0.2 -3,-0.1 30,-0.1 0.712 95.0 65.9 -60.8 -19.6 52.6 -19.6 6.7 14 14 A R G < 5S- 0 0 177 -3,-0.6 3,-0.3 2,-0.1 -1,-0.3 0.372 102.8-133.8 -84.6 6.7 50.7 -21.0 3.8 15 15 A G T < 5 - 0 0 58 -3,-2.4 2,-1.8 1,-0.2 3,-0.2 0.831 23.9-160.1 44.2 35.0 53.2 -19.3 1.4 16 16 A T < + 0 0 66 -5,-1.0 -1,-0.2 1,-0.2 -2,-0.1 -0.176 25.5 162.9 -47.6 79.5 50.1 -18.2 -0.5 17 17 A G - 0 0 65 -2,-1.8 -1,-0.2 -3,-0.3 -2,-0.1 0.998 21.0-167.1 -66.4 -74.2 52.2 -17.6 -3.7 18 18 A A + 0 0 64 -3,-0.2 3,-0.1 3,-0.1 -2,-0.1 0.866 24.1 156.9 85.3 41.7 49.4 -17.5 -6.4 19 19 A G S S+ 0 0 87 1,-0.2 -3,-0.0 2,-0.1 0, 0.0 0.921 82.1 33.8 -64.0 -44.8 51.8 -17.7 -9.3 20 20 A S S S- 0 0 83 1,-0.1 -1,-0.2 2,-0.0 -2,-0.0 0.445 121.0-117.9 -89.2 -1.2 49.1 -19.1 -11.6 21 21 A R - 0 0 151 1,-0.1 -1,-0.1 -3,-0.1 -3,-0.1 0.285 19.4 -94.7 77.6 152.4 46.5 -17.0 -9.8 22 22 A P - 0 0 68 0, 0.0 -1,-0.1 0, 0.0 3,-0.1 0.851 48.6-175.7 -68.4 -35.5 43.5 -18.4 -7.7 23 23 A R + 0 0 133 1,-0.1 2,-0.2 2,-0.1 3,-0.1 0.883 37.0 107.6 33.5 82.3 41.1 -18.0 -10.7 24 24 A G + 0 0 31 -23,-0.2 -1,-0.1 1,-0.2 -22,-0.0 -0.541 23.9 82.2-148.7-144.9 37.8 -19.1 -9.0 25 25 A Q + 0 0 58 -2,-0.2 3,-0.3 1,-0.2 -1,-0.2 0.835 50.5 147.3 29.4 62.3 34.5 -17.7 -7.6 26 26 A N + 0 0 160 1,-0.2 -1,-0.2 -3,-0.1 -3,-0.0 0.047 55.8 68.9-108.9 22.6 33.0 -17.8 -11.1 27 27 A K + 0 0 99 3,-0.0 -1,-0.2 0, 0.0 -2,-0.1 0.316 66.7 171.6-120.0 3.3 29.5 -18.5 -9.9 28 28 A E + 0 0 150 -3,-0.3 -2,-0.0 1,-0.2 -24,-0.0 0.251 28.8 118.0 -19.0 119.6 28.7 -15.2 -8.3 29 29 A R + 0 0 224 3,-0.1 -1,-0.2 1,-0.1 0, 0.0 0.303 49.1 74.6-160.8 -42.2 25.1 -15.2 -7.3 30 30 A P - 0 0 78 0, 0.0 -1,-0.1 0, 0.0 -2,-0.0 -0.680 59.0-164.7 -88.6 87.6 24.6 -15.0 -3.5 31 31 A P + 0 0 116 0, 0.0 -3,-0.0 0, 0.0 -2,-0.0 0.860 59.8 101.9 -37.5 -53.1 25.3 -11.2 -2.7 32 32 A P - 0 0 105 0, 0.0 -3,-0.1 0, 0.0 0, 0.0 0.093 69.2-138.4 -33.4 144.5 25.6 -12.0 1.0 33 33 A V - 0 0 106 1,-0.0 -28,-0.1 -27,-0.0 4,-0.0 -0.949 23.9 -99.5-115.4 131.9 29.2 -12.2 2.2 34 34 A P - 0 0 51 0, 0.0 3,-0.3 0, 0.0 -29,-0.0 -0.110 22.4-153.4 -47.7 140.0 30.5 -14.9 4.7 35 35 A N S > S+ 0 0 133 1,-0.2 3,-2.6 2,-0.1 4,-0.1 0.817 85.3 76.4 -86.1 -35.8 30.8 -13.7 8.3 36 36 A P G > S+ 0 0 78 0, 0.0 3,-0.9 0, 0.0 -1,-0.2 0.627 80.1 77.1 -52.7 -9.3 33.6 -16.2 9.3 37 37 A D G 3 + 0 0 60 -3,-0.3 -2,-0.1 1,-0.2 -31,-0.1 0.419 68.9 87.0 -81.3 2.3 35.8 -13.8 7.4 38 38 A Y G < S+ 0 0 205 -3,-2.6 -1,-0.2 1,-0.2 -3,-0.1 0.451 81.3 63.5 -80.1 0.1 35.6 -11.5 10.4 39 39 A E X + 0 0 91 -3,-0.9 3,-1.0 -4,-0.1 -1,-0.2 -0.589 50.8 155.2-125.3 71.7 38.6 -13.3 11.9 40 40 A P T 3 + 0 0 71 0, 0.0 -1,-0.1 0, 0.0 -3,-0.1 0.229 49.4 103.1 -80.1 16.5 41.7 -12.9 9.6 41 41 A I T 3 + 0 0 126 1,-0.1 2,-1.7 -30,-0.0 -2,-0.0 0.693 46.3 109.8 -70.7 -19.3 43.9 -13.5 12.7 42 42 A R < + 0 0 156 -3,-1.0 2,-0.2 -31,-0.0 -32,-0.1 -0.403 48.6 101.6 -62.4 87.8 44.5 -17.0 11.3 43 43 A K - 0 0 97 -2,-1.7 -1,-0.0 -32,-0.1 0, 0.0 -0.585 52.1-162.5-173.3 103.3 48.1 -16.5 10.3 44 44 A G - 0 0 53 -2,-0.2 -1,-0.1 1,-0.0 -2,-0.0 0.931 21.4-174.2 -56.6 -46.4 51.1 -17.8 12.2 45 45 A Q + 0 0 103 1,-0.1 -2,-0.0 2,-0.0 -1,-0.0 0.961 48.4 104.0 46.4 71.5 53.5 -15.4 10.4 46 46 A R > + 0 0 198 3,-0.0 4,-0.7 0, 0.0 3,-0.5 0.367 61.9 66.7-150.4 -16.5 56.7 -16.7 11.9 47 47 A D H > S+ 0 0 92 1,-0.2 4,-2.3 2,-0.2 5,-0.1 0.473 81.2 81.8 -90.3 -3.3 58.3 -18.8 9.1 48 48 A L H 4 S+ 0 0 95 2,-0.2 -1,-0.2 1,-0.2 -3,-0.0 0.776 96.6 42.6 -70.8 -26.5 58.8 -15.7 7.0 49 49 A Y H >4 S+ 0 0 199 -3,-0.5 3,-0.5 2,-0.2 -1,-0.2 0.858 116.4 45.4 -86.5 -40.2 62.0 -14.9 9.0 50 50 A S H >< S+ 0 0 71 -4,-0.7 3,-1.2 1,-0.2 -2,-0.2 0.872 112.4 51.3 -70.4 -37.6 63.3 -18.5 9.1 51 51 A G G >< S+ 0 0 56 -4,-2.3 3,-0.5 1,-0.2 -1,-0.2 0.539 98.2 69.4 -76.6 -5.8 62.6 -19.1 5.4 52 52 A L G < + 0 0 113 -3,-0.5 -1,-0.2 1,-0.2 -2,-0.2 0.499 63.3 105.5 -88.7 -4.6 64.5 -15.8 4.6 53 53 A N G <> - 0 0 100 -3,-1.2 4,-0.6 1,-0.2 -1,-0.2 0.831 52.4-176.7 -42.4 -37.1 67.8 -17.5 5.6 54 54 A Q T <4 - 0 0 142 -3,-0.5 -1,-0.2 -4,-0.1 -2,-0.1 0.655 59.9 -87.1 45.3 11.4 68.5 -17.5 1.9 55 55 A R T 4 S- 0 0 197 1,-0.1 -1,-0.1 2,-0.0 -2,-0.0 0.836 102.0 -6.2 55.8 112.1 71.6 -19.3 3.2 56 56 A A T 4 0 0 79 1,-0.2 -2,-0.1 0, 0.0 -1,-0.1 0.898 360.0 360.0 37.0 65.0 74.4 -16.9 4.1 57 57 A V < 0 0 160 -4,-0.6 -1,-0.2 -5,-0.1 -3,-0.1 0.711 360.0 360.0 -61.3 360.0 72.5 -13.9 2.7