==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=22-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SIGNALING PROTEIN 12-SEP-05 2AZV . COMPND 2 MOLECULE: SH2-SH3 ADAPTER PROTEIN DRK; . SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; . AUTHOR I.BEZSONOVA,A.U.SINGER,W.-Y.CHOY,M.TOLLINGER,J.D.FORMAN-KAY . 59 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4858.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 31 52.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 3.4 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 19 32.2 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 . 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 . 5 8.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 6.8 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+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 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 . 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 PARALLEL BRIDGES PER LADDER . 1 2 1 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 M 0 0 144 0, 0.0 26,-2.3 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0-165.3 -0.6 -9.0 -4.1 2 2 A E E +A 26 0A 88 24,-0.2 2,-0.2 54,-0.1 24,-0.2 -0.919 360.0 173.7-122.6 151.0 -2.5 -7.6 -1.1 3 3 A A E -A 25 0A 2 22,-3.2 22,-0.9 -2,-0.3 2,-0.3 -0.838 20.2-131.3-144.9 179.1 -1.2 -5.6 1.9 4 4 A I E -AB 24 54A 17 50,-1.3 50,-4.0 20,-0.3 2,-0.3 -1.000 27.9-107.1-141.5 140.5 -2.2 -3.7 5.0 5 5 A A E - B 0 53A 0 18,-2.3 17,-2.5 -2,-0.3 18,-0.4 -0.466 26.5-178.3 -67.2 123.1 -1.3 -0.3 6.5 6 6 A K S S+ 0 0 100 46,-1.6 2,-0.2 -2,-0.3 15,-0.2 0.775 71.7 5.9 -90.0 -29.4 1.0 -0.6 9.5 7 7 A H S S- 0 0 108 45,-0.6 2,-0.3 13,-0.1 16,-0.1 -0.786 89.6 -78.7-144.8 178.0 1.1 3.2 10.1 8 8 A D - 0 0 87 -2,-0.2 2,-0.4 12,-0.2 12,-0.2 -0.657 38.8-171.6 -87.2 143.0 -0.4 6.4 8.9 9 9 A F B -F 19 0B 33 10,-2.2 10,-1.0 -2,-0.3 2,-0.5 -0.944 9.0-168.7-140.9 124.2 0.7 8.2 5.7 10 10 A S - 0 0 89 -2,-0.4 8,-0.1 8,-0.2 7,-0.1 -0.935 30.6-116.6-115.9 121.4 -0.2 11.6 4.3 11 11 A A + 0 0 41 -2,-0.5 3,-0.1 5,-0.1 7,-0.1 -0.115 30.7 176.5 -54.9 141.9 0.8 12.4 0.7 12 12 A T + 0 0 131 1,-0.4 2,-0.2 0, 0.0 -1,-0.1 0.692 60.1 16.7-111.4 -76.7 3.3 15.2 -0.1 13 13 A A S S- 0 0 63 2,-0.1 -1,-0.4 0, 0.0 3,-0.3 -0.544 111.7 -12.7 -99.3 167.9 4.1 15.4 -3.9 14 14 A D S S- 0 0 161 1,-0.2 2,-0.6 -2,-0.2 -3,-0.0 -0.110 117.3 -26.3 47.5-131.8 2.4 14.1 -7.0 15 15 A D S S+ 0 0 121 2,-0.0 32,-1.0 -4,-0.0 -1,-0.2 -0.713 77.2 159.3-120.2 86.2 -0.3 11.4 -6.4 16 16 A E B -c 47 0A 58 -2,-0.6 2,-0.4 -3,-0.3 32,-0.2 -0.487 33.7-123.3 -94.3 166.8 0.5 9.6 -3.2 17 17 A L - 0 0 15 30,-2.1 2,-0.2 -2,-0.2 29,-0.1 -0.939 13.7-141.0-120.8 137.1 -2.0 7.7 -1.1 18 18 A S + 0 0 70 -2,-0.4 2,-0.3 -8,-0.1 -8,-0.2 -0.625 28.3 161.9 -91.5 152.2 -3.0 8.2 2.5 19 19 A F B -F 9 0B 3 -10,-1.0 -10,-2.2 -2,-0.2 2,-0.3 -0.989 23.0-141.7-164.8 161.6 -3.7 5.3 5.0 20 20 A R > - 0 0 162 -2,-0.3 3,-2.1 -12,-0.2 -15,-0.3 -0.882 42.4 -71.8-129.7 160.7 -3.9 4.4 8.6 21 21 A K T 3 S+ 0 0 169 -2,-0.3 -15,-0.2 1,-0.3 3,-0.1 -0.213 117.7 23.5 -52.2 133.1 -3.0 1.4 10.8 22 22 A G T 3 S+ 0 0 58 -17,-2.5 -1,-0.3 1,-0.3 -16,-0.1 0.296 92.7 130.1 93.7 -10.0 -5.2 -1.6 10.2 23 23 A Q < - 0 0 80 -3,-2.1 -18,-2.3 -18,-0.4 2,-0.7 -0.378 56.8-124.5 -78.4 156.3 -6.2 -0.6 6.7 24 24 A I E -A 4 0A 99 -20,-0.3 2,-0.4 -3,-0.1 -20,-0.3 -0.879 24.9-172.3-109.5 110.1 -6.0 -2.9 3.6 25 25 A L E -A 3 0A 0 -22,-0.9 -22,-3.2 -2,-0.7 2,-0.5 -0.822 17.5-134.6 -99.5 135.4 -3.9 -1.7 0.7 26 26 A K E -AD 2 40A 77 14,-1.5 14,-1.0 -2,-0.4 2,-0.7 -0.763 7.7-145.8 -92.3 132.6 -3.9 -3.6 -2.7 27 27 A I E + D 0 39A 24 -26,-2.3 12,-0.2 -2,-0.5 -1,-0.0 -0.808 45.9 132.2 -97.7 112.9 -0.6 -4.3 -4.5 28 28 A L + 0 0 114 10,-1.8 11,-0.2 -2,-0.7 -1,-0.1 -0.024 30.8 121.3-150.9 34.2 -1.2 -4.2 -8.3 29 29 A N - 0 0 26 9,-0.5 8,-0.1 1,-0.2 2,-0.1 0.268 62.9 -94.1 -80.5-148.8 1.5 -2.0 -9.7 30 30 A M - 0 0 121 0, 0.0 3,-0.2 0, 0.0 -1,-0.2 0.067 55.1 -67.3-105.7-137.8 4.1 -3.0 -12.3 31 31 A E S S+ 0 0 164 1,-0.2 -2,-0.0 2,-0.1 0, 0.0 -0.202 84.6 120.7-114.5 45.3 7.7 -4.4 -11.9 32 32 A D - 0 0 58 4,-0.1 -1,-0.2 2,-0.0 3,-0.1 0.930 50.2-163.4 -67.9 -48.5 9.4 -1.3 -10.5 33 33 A D + 0 0 117 -3,-0.2 2,-0.2 1,-0.2 4,-0.1 0.979 45.0 93.0 61.2 66.7 10.5 -3.1 -7.3 34 34 A S S S- 0 0 68 2,-0.3 16,-0.2 0, 0.0 -1,-0.2 -0.601 89.1 -54.6-155.5-151.0 11.3 -0.1 -5.1 35 35 A N S S+ 0 0 117 -2,-0.2 15,-1.7 14,-0.1 2,-0.5 0.763 113.0 58.0 -79.3 -26.9 10.2 2.4 -2.4 36 36 A W E + E 0 49A 137 13,-0.2 -2,-0.3 14,-0.1 2,-0.3 -0.911 67.4 169.9-109.3 129.6 7.1 3.7 -4.3 37 37 A Y E - E 0 48A 38 11,-2.5 11,-2.6 -2,-0.5 2,-0.4 -0.902 32.2-112.4-133.8 162.8 4.4 1.3 -5.4 38 38 A R E + E 0 47A 105 -2,-0.3 -10,-1.8 9,-0.2 -9,-0.5 -0.822 37.9 174.1-102.0 132.5 0.9 1.4 -6.9 39 39 A A E -DE 27 46A 2 7,-2.6 7,-1.2 -2,-0.4 2,-0.4 -0.848 22.4-138.5-132.1 169.0 -2.1 0.3 -4.9 40 40 A E E +DE 26 45A 60 -14,-1.0 -14,-1.5 -2,-0.3 2,-0.3 -0.996 20.5 169.4-132.9 134.8 -5.9 0.2 -5.0 41 41 A L E > S- E 0 44A 27 3,-3.3 3,-2.2 -2,-0.4 -16,-0.1 -0.992 71.6 -9.5-148.3 131.6 -8.4 0.9 -2.2 42 42 A D T 3 S- 0 0 178 -2,-0.3 3,-0.1 1,-0.3 -1,-0.0 0.791 132.9 -50.5 49.6 34.4 -12.2 1.4 -2.3 43 43 A G T 3 S+ 0 0 61 1,-0.3 2,-0.4 0, 0.0 -1,-0.3 0.639 118.0 114.6 83.3 12.5 -11.9 1.4 -6.1 44 44 A K E < - E 0 41A 146 -3,-2.2 -3,-3.3 2,-0.0 -1,-0.3 -0.955 49.8-154.2-118.9 140.1 -9.2 4.0 -6.1 45 45 A E E + E 0 40A 113 -2,-0.4 2,-0.3 -5,-0.3 -5,-0.2 -0.480 27.0 130.8-107.5 171.2 -5.5 3.6 -7.2 46 46 A G E - E 0 39A 7 -7,-1.2 -7,-2.6 -2,-0.2 2,-0.4 -0.986 50.4 -71.0 169.5-175.2 -2.4 5.5 -6.2 47 47 A L E +cE 16 38A 31 -32,-1.0 -30,-2.1 -2,-0.3 -9,-0.2 -0.923 44.3 168.6-112.5 138.8 1.2 5.3 -5.0 48 48 A I E - E 0 37A 2 -11,-2.6 -11,-2.5 -2,-0.4 2,-0.5 -0.907 39.6 -88.9-141.8 168.3 2.3 4.2 -1.5 49 49 A P E > - E 0 36A 21 0, 0.0 3,-2.0 0, 0.0 4,-0.3 -0.714 25.4-142.7 -87.6 125.5 5.5 3.3 0.4 50 50 A S G > S+ 0 0 51 -15,-1.7 3,-1.1 -2,-0.5 -15,-0.1 0.830 103.0 53.5 -53.5 -34.6 6.5 -0.3 0.3 51 51 A N G 3 S+ 0 0 124 1,-0.2 -1,-0.3 -16,-0.2 -45,-0.1 0.621 101.6 62.3 -75.9 -13.2 7.8 -0.3 3.9 52 52 A Y G < S+ 0 0 87 -3,-2.0 -46,-1.6 1,-0.1 2,-0.6 0.461 90.5 78.0 -93.4 0.2 4.3 1.1 4.9 53 53 A I E < -B 5 0A 27 -3,-1.1 -48,-0.2 -4,-0.3 -1,-0.1 -0.933 61.3-175.3-115.9 117.2 2.5 -2.0 3.8 54 54 A E E -B 4 0A 113 -50,-4.0 -50,-1.3 -2,-0.6 2,-0.3 -0.084 24.0-105.1 -90.8-166.7 2.5 -5.1 6.0 55 55 A M + 0 0 122 -52,-0.2 2,-0.3 -2,-0.0 -52,-0.1 -0.951 37.9 160.4-127.7 147.5 1.0 -8.5 5.4 56 56 A K + 0 0 108 -2,-0.3 3,-0.2 -54,-0.2 -54,-0.1 -0.906 39.6 33.1-152.9 177.1 -2.0 -10.3 6.7 57 57 A N S S+ 0 0 125 -2,-0.3 2,-0.4 1,-0.2 -2,-0.0 -0.116 89.2 62.8 63.8-165.7 -4.5 -13.2 6.1 58 58 A H 0 0 166 1,-0.2 -1,-0.2 -3,-0.0 -3,-0.0 -0.364 360.0 360.0 57.2-108.4 -3.2 -16.4 4.4 59 59 A D 0 0 222 -2,-0.4 -1,-0.2 -3,-0.2 -2,-0.0 -0.279 360.0 360.0 64.4 360.0 -0.6 -17.8 6.9