==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=30-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SIGNALING PROTEIN 18-NOV-05 2F2X . COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, BRAIN; . SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; . AUTHOR A.CAMARA-ARTIGAS,F.CONEJERO-LARA,S.CASARES,O.LOPEZ-MAYORGA, . 55 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3817.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 39 70.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 3.6 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 22 40.0 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 . 1 1.8 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-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 . 9 16.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 9.1 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 0 3 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 7 A E 0 0 140 0, 0.0 26,-3.0 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 154.3 2.8 -0.2 6.4 2 8 A L E -A 26 0A 84 24,-0.2 53,-2.4 36,-0.0 2,-0.3 -0.761 360.0-164.6-109.4 154.4 2.8 -1.5 10.0 3 9 A V E -AB 25 54A 0 22,-2.5 22,-2.8 -2,-0.3 2,-0.4 -0.952 17.3-128.8-134.1 153.1 4.2 -0.2 13.2 4 10 A L E -AB 24 53A 50 49,-2.7 49,-1.9 -2,-0.3 2,-0.6 -0.881 22.2-124.2-104.1 132.2 4.9 -1.9 16.6 5 11 A A E - B 0 52A 1 18,-2.7 17,-2.8 -2,-0.4 47,-0.2 -0.656 23.1-172.4 -75.9 118.3 3.6 -0.3 19.8 6 12 A L + 0 0 57 45,-2.9 2,-0.3 -2,-0.6 -1,-0.2 0.719 69.1 15.5 -82.6 -23.7 6.6 0.1 22.0 7 13 A Y S S- 0 0 135 44,-0.9 2,-0.1 13,-0.1 -1,-0.1 -0.949 86.6 -95.0-145.0 162.3 4.6 1.1 25.1 8 14 A D - 0 0 105 -2,-0.3 2,-0.3 12,-0.2 12,-0.2 -0.519 43.8-171.1 -73.6 150.0 1.0 1.1 26.3 9 15 A Y B -F 19 0B 26 10,-2.6 10,-2.3 -2,-0.1 2,-0.5 -0.906 13.3-156.1-149.6 120.3 -0.7 4.4 25.5 10 16 A Q - 0 0 151 -2,-0.3 8,-0.1 8,-0.2 7,-0.1 -0.843 33.7-107.7 -98.3 128.3 -4.1 5.6 26.7 11 17 A E + 0 0 63 -2,-0.5 7,-0.1 1,-0.1 36,-0.1 -0.250 35.2 179.7 -53.9 134.3 -5.8 8.2 24.6 12 18 A K + 0 0 166 5,-0.1 -1,-0.1 1,-0.1 6,-0.0 0.349 62.9 40.7-119.9 0.5 -5.8 11.6 26.3 13 19 A S S > S- 0 0 48 1,-0.0 3,-1.8 4,-0.0 -1,-0.1 -0.965 90.2-100.9-145.6 158.1 -7.6 13.7 23.7 14 20 A P T 3 S+ 0 0 144 0, 0.0 -3,-0.0 0, 0.0 -1,-0.0 0.807 119.9 46.9 -49.8 -36.4 -10.6 13.2 21.4 15 21 A G T 3 S+ 0 0 42 30,-0.1 31,-2.3 2,-0.0 2,-0.1 0.488 96.0 93.1 -89.1 -1.4 -8.5 12.5 18.3 16 22 A E B < -c 46 0A 21 -3,-1.8 2,-0.3 29,-0.3 31,-0.2 -0.397 59.9-147.4 -88.5 166.4 -6.1 10.0 20.0 17 23 A V - 0 0 0 29,-1.7 2,-0.3 -2,-0.1 -5,-0.1 -0.929 15.1-118.6-131.4 155.3 -6.4 6.2 20.1 18 24 A T + 0 0 33 -2,-0.3 2,-0.3 -8,-0.1 -8,-0.2 -0.744 31.5 176.0 -97.0 143.6 -5.4 3.7 22.7 19 25 A M B -F 9 0B 2 -10,-2.3 -10,-2.6 -2,-0.3 2,-0.4 -0.958 22.2-133.7-142.5 159.1 -2.8 0.9 22.2 20 26 A K > - 0 0 117 -2,-0.3 3,-2.4 -12,-0.2 -15,-0.2 -0.897 39.9 -92.9-114.0 144.3 -1.2 -1.8 24.2 21 27 A K T 3 S+ 0 0 145 -2,-0.4 -15,-0.2 1,-0.3 -13,-0.1 -0.278 115.2 28.2 -53.2 134.4 2.6 -2.6 24.1 22 28 A G T 3 S+ 0 0 46 -17,-2.8 -1,-0.3 1,-0.3 -16,-0.1 0.208 87.2 138.5 97.2 -16.9 3.2 -5.3 21.5 23 29 A D < - 0 0 54 -3,-2.4 -18,-2.7 -19,-0.1 2,-0.7 -0.301 50.6-136.5 -62.4 145.7 0.2 -4.3 19.3 24 30 A I E -A 4 0A 93 -20,-0.2 17,-0.4 -3,-0.1 2,-0.3 -0.932 29.2-170.9-107.1 111.4 0.8 -4.2 15.5 25 31 A L E -A 3 0A 1 -22,-2.8 -22,-2.5 -2,-0.7 2,-0.6 -0.730 24.9-120.9-106.1 153.9 -0.9 -1.1 14.2 26 32 A T E -AD 2 39A 50 13,-2.1 13,-2.2 -2,-0.3 2,-0.6 -0.827 28.9-132.6 -92.5 124.4 -1.5 0.0 10.6 27 33 A L E + D 0 38A 12 -26,-3.0 11,-0.2 -2,-0.6 3,-0.1 -0.687 31.5 170.5 -81.2 117.4 0.3 3.3 9.9 28 34 A L E + 0 0 68 9,-2.6 2,-0.3 -2,-0.6 10,-0.2 0.840 66.4 4.0 -94.8 -41.3 -2.1 5.7 8.2 29 35 A N E + D 0 37A 69 8,-1.8 8,-2.7 1,-0.1 -1,-0.3 -0.905 48.7 167.3-153.6 120.2 -0.3 9.0 8.3 30 36 A S + 0 0 39 -2,-0.3 6,-0.1 6,-0.2 -1,-0.1 -0.013 45.8 114.8-120.0 27.6 3.2 9.8 9.5 31 37 A T + 0 0 126 2,-0.0 2,-0.4 6,-0.0 -1,-0.1 0.729 65.4 72.2 -70.9 -21.8 3.6 13.3 8.0 32 38 A N S S- 0 0 76 3,-0.4 5,-0.1 -3,-0.2 -3,-0.0 -0.784 75.6-146.9 -94.1 137.6 3.8 14.9 11.5 33 39 A K S S+ 0 0 166 -2,-0.4 -1,-0.1 1,-0.2 3,-0.1 0.708 94.6 36.9 -78.5 -17.2 7.0 14.2 13.3 34 40 A D S S+ 0 0 84 1,-0.3 15,-2.6 15,-0.1 16,-0.4 0.772 119.2 36.2-103.7 -32.8 5.4 14.1 16.8 35 41 A W E - E 0 48A 91 13,-0.3 -3,-0.4 14,-0.1 2,-0.4 -0.987 63.7-164.3-129.4 127.0 2.0 12.4 16.2 36 42 A W E - E 0 47A 38 11,-2.4 11,-1.9 -2,-0.4 2,-0.5 -0.891 19.6-129.4-111.0 138.6 1.2 9.6 13.8 37 43 A K E +DE 29 46A 74 -8,-2.7 -9,-2.6 -2,-0.4 -8,-1.8 -0.748 39.0 171.0 -87.3 126.3 -2.2 8.5 12.8 38 44 A V E -DE 27 45A 0 7,-3.1 7,-2.1 -2,-0.5 2,-0.6 -0.850 35.1-126.9-132.2 166.3 -2.7 4.8 13.2 39 45 A E E -DE 26 44A 64 -13,-2.2 -13,-2.1 -2,-0.3 2,-0.8 -0.976 19.5-167.2-117.9 116.6 -5.4 2.1 13.0 40 46 A V E > - E 0 43A 17 3,-2.7 3,-2.1 -2,-0.6 2,-0.7 -0.915 64.3 -60.7-106.5 103.6 -5.5 -0.0 16.2 41 47 A N T 3 S- 0 0 141 -2,-0.8 -15,-0.1 -17,-0.4 -2,-0.0 -0.433 125.0 -10.6 59.8-102.8 -7.7 -3.0 15.3 42 48 A D T 3 S+ 0 0 127 -2,-0.7 2,-0.3 -3,-0.0 -1,-0.3 0.149 123.2 79.1-112.5 16.1 -11.0 -1.2 14.4 43 49 A R E < - E 0 40A 103 -3,-2.1 -3,-2.7 -25,-0.1 2,-0.3 -0.930 58.4-155.6-125.4 150.9 -10.2 2.3 15.6 44 50 A Q E + E 0 39A 104 -2,-0.3 2,-0.3 -5,-0.2 -5,-0.2 -0.931 34.4 103.7-125.0 149.9 -8.2 5.1 14.1 45 51 A G E - E 0 38A 3 -7,-2.1 -7,-3.1 -2,-0.3 2,-0.3 -0.972 59.5 -54.4 165.9-176.9 -6.5 8.1 15.7 46 52 A F E +cE 16 37A 77 -31,-2.3 -29,-1.7 -2,-0.3 -9,-0.2 -0.652 37.6 171.9 -95.8 145.9 -3.2 9.6 16.8 47 53 A V E - E 0 36A 0 -11,-1.9 -11,-2.4 -2,-0.3 2,-0.2 -0.932 49.7 -78.4-138.6 159.0 -0.5 8.3 19.1 48 54 A P E > - E 0 35A 14 0, 0.0 3,-1.7 0, 0.0 -13,-0.3 -0.435 35.2-138.1 -62.8 129.2 3.0 9.7 19.9 49 55 A A G > S+ 0 0 10 -15,-2.6 3,-1.4 1,-0.3 -14,-0.1 0.863 102.5 60.0 -55.1 -36.2 5.3 8.9 17.0 50 56 A A G 3 S+ 0 0 76 -16,-0.4 -1,-0.3 1,-0.3 -15,-0.1 0.696 95.5 62.5 -67.4 -18.6 8.0 8.1 19.5 51 57 A Y G < S+ 0 0 90 -3,-1.7 -45,-2.9 -45,-0.1 -44,-0.9 0.406 101.0 57.3 -89.6 3.1 5.9 5.3 21.0 52 58 A V E < -B 5 0A 10 -3,-1.4 2,-0.4 -47,-0.2 -47,-0.2 -0.928 67.1-148.1-131.7 157.6 5.8 3.2 17.9 53 59 A K E -B 4 0A 128 -49,-1.9 -49,-2.7 -2,-0.3 2,-0.1 -0.988 22.5-119.2-130.5 126.7 8.4 1.6 15.6 54 60 A K E B 3 0A 108 -2,-0.4 -51,-0.2 -51,-0.2 -2,-0.0 -0.385 360.0 360.0 -61.5 134.9 8.1 1.1 11.8 55 61 A L 0 0 128 -53,-2.4 -1,-0.2 -2,-0.1 -52,-0.1 0.845 360.0 360.0 -97.5 360.0 8.4 -2.6 11.0