==== 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 2F2W . 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, . 56 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3822.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 38 67.9 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 39.3 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 . 7 12.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 8.9 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 98 0, 0.0 26,-3.3 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 162.9 2.8 -0.5 5.8 2 8 A L E -A 26 0A 73 24,-0.2 53,-2.7 22,-0.0 54,-0.8 -0.724 360.0-168.4-100.7 148.1 2.8 -2.1 9.2 3 9 A V E -AB 25 54A 0 22,-2.6 22,-2.9 -2,-0.3 2,-0.4 -0.952 17.2-129.9-132.9 153.1 4.3 -0.6 12.4 4 10 A L E -AB 24 53A 51 49,-2.8 49,-2.1 -2,-0.3 2,-0.6 -0.883 20.1-126.6-105.5 132.3 5.0 -2.2 15.8 5 11 A A E - B 0 52A 1 18,-2.6 17,-2.8 -2,-0.4 47,-0.2 -0.680 23.3-174.9 -78.5 117.7 3.8 -0.5 19.0 6 12 A L S S+ 0 0 59 45,-3.1 2,-0.3 -2,-0.6 -1,-0.2 0.694 70.3 15.4 -85.4 -22.0 6.9 -0.2 21.2 7 13 A Y S S- 0 0 141 44,-0.9 2,-0.2 13,-0.1 -1,-0.1 -0.948 86.6 -99.0-145.4 161.6 4.9 1.2 24.2 8 14 A D - 0 0 95 -2,-0.3 2,-0.3 12,-0.1 12,-0.2 -0.523 38.9-166.3 -80.2 154.3 1.3 1.4 25.2 9 15 A Y B -F 19 0B 24 10,-2.6 10,-2.5 -2,-0.2 2,-0.5 -0.958 11.8-153.1-147.2 128.3 -0.4 4.7 24.6 10 16 A Q - 0 0 141 -2,-0.3 8,-0.1 8,-0.2 7,-0.0 -0.889 30.9-113.2-103.4 124.6 -3.6 6.1 25.9 11 17 A E + 0 0 62 -2,-0.5 7,-0.1 1,-0.1 36,-0.1 -0.252 33.0 177.9 -56.5 137.0 -5.4 8.6 23.7 12 18 A K + 0 0 146 5,-0.1 -1,-0.1 1,-0.1 3,-0.0 0.267 62.3 35.1-125.6 7.7 -5.6 12.1 25.3 13 19 A S S > S- 0 0 45 1,-0.0 3,-1.0 0, 0.0 -1,-0.1 -0.962 89.1 -97.2-153.7 165.4 -7.3 14.1 22.6 14 20 A P T 3 S+ 0 0 137 0, 0.0 -3,-0.0 0, 0.0 -1,-0.0 0.814 120.6 49.8 -56.5 -34.8 -10.1 13.6 19.9 15 21 A A T 3 S+ 0 0 57 30,-0.1 31,-2.4 2,-0.0 2,-0.1 0.669 98.3 87.4 -81.2 -16.8 -7.6 12.9 17.1 16 22 A E B < -c 46 0A 25 -3,-1.0 2,-0.3 29,-0.3 31,-0.2 -0.323 58.4-156.9 -84.1 164.4 -5.6 10.3 19.1 17 23 A V - 0 0 0 29,-1.7 2,-0.3 28,-0.1 -5,-0.1 -0.954 19.0-114.8-136.9 155.2 -6.2 6.6 19.4 18 24 A T + 0 0 50 -2,-0.3 2,-0.3 -8,-0.1 -8,-0.2 -0.694 32.7 175.4 -95.1 144.3 -5.1 4.0 22.1 19 25 A M B -F 9 0B 3 -10,-2.5 -10,-2.6 -2,-0.3 2,-0.4 -0.954 21.8-132.7-142.7 161.3 -2.7 1.2 21.5 20 26 A K > - 0 0 129 -2,-0.3 3,-2.4 -12,-0.2 -15,-0.2 -0.913 38.4 -93.2-117.4 143.7 -1.0 -1.6 23.5 21 27 A K T 3 S+ 0 0 142 -2,-0.4 -15,-0.2 1,-0.3 -13,-0.1 -0.251 114.5 27.4 -52.2 135.1 2.7 -2.5 23.4 22 28 A G T 3 S+ 0 0 45 -17,-2.8 -1,-0.3 1,-0.3 -16,-0.1 0.243 87.6 138.6 94.7 -14.5 3.2 -5.3 20.9 23 29 A D < - 0 0 45 -3,-2.4 -18,-2.6 -19,-0.1 2,-0.6 -0.344 50.8-135.9 -64.7 145.3 0.2 -4.3 18.8 24 30 A I E -A 4 0A 94 -20,-0.2 17,-0.4 -3,-0.1 2,-0.3 -0.927 29.6-171.0-104.9 115.3 0.7 -4.4 15.0 25 31 A L E -A 3 0A 1 -22,-2.9 -22,-2.6 -2,-0.6 2,-0.6 -0.743 24.5-122.7-109.5 156.9 -0.8 -1.3 13.5 26 32 A T E -AD 2 39A 53 13,-1.8 13,-2.1 -2,-0.3 2,-0.5 -0.868 29.3-130.7 -97.4 123.7 -1.4 -0.2 9.9 27 33 A L E + D 0 38A 16 -26,-3.3 11,-0.2 -2,-0.6 3,-0.1 -0.638 33.4 168.2 -77.9 123.3 0.4 3.1 9.1 28 34 A L E + 0 0 71 9,-2.7 2,-0.3 -2,-0.5 10,-0.2 0.787 65.6 5.9-103.9 -39.2 -2.0 5.6 7.4 29 35 A N E + D 0 37A 64 8,-1.7 8,-2.6 1,-0.1 -1,-0.3 -0.881 47.3 167.7-154.9 118.0 -0.2 8.9 7.5 30 36 A S + 0 0 46 -2,-0.3 6,-0.1 6,-0.2 -1,-0.1 -0.011 46.1 114.6-117.2 28.3 3.4 9.7 8.5 31 37 A T + 0 0 125 2,-0.0 2,-0.4 6,-0.0 -1,-0.1 0.757 65.7 71.8 -70.6 -23.6 3.6 13.2 7.1 32 38 A N S S- 0 0 74 3,-0.5 5,-0.1 -3,-0.2 -3,-0.0 -0.764 75.3-147.2 -92.8 138.3 3.9 14.7 10.6 33 39 A K S S+ 0 0 168 -2,-0.4 -1,-0.1 1,-0.2 3,-0.1 0.709 95.5 35.5 -79.0 -18.4 7.3 14.0 12.4 34 40 A D S S+ 0 0 82 1,-0.2 15,-2.3 15,-0.1 2,-0.4 0.721 120.0 39.5-104.8 -28.8 5.8 13.8 15.9 35 41 A W E - E 0 48A 88 13,-0.3 -3,-0.5 14,-0.1 2,-0.4 -0.984 62.3-166.8-130.9 127.4 2.4 12.2 15.3 36 42 A W E - E 0 47A 40 11,-2.4 11,-2.0 -2,-0.4 2,-0.4 -0.895 20.5-129.6-112.4 139.0 1.5 9.3 12.9 37 43 A K E +DE 29 46A 70 -8,-2.6 -9,-2.7 -2,-0.4 -8,-1.7 -0.726 38.2 169.9 -86.2 131.9 -2.0 8.3 12.0 38 44 A V E -DE 27 45A 0 7,-3.2 7,-2.3 -2,-0.4 2,-0.6 -0.919 36.1-123.9-139.1 162.9 -2.6 4.5 12.4 39 45 A E E -DE 26 44A 63 -13,-2.1 -13,-1.8 -2,-0.3 2,-0.7 -0.959 23.1-167.3-111.1 117.2 -5.3 2.0 12.4 40 46 A V E > - E 0 43A 15 3,-2.8 3,-3.0 -2,-0.6 2,-0.6 -0.930 64.3 -55.2-107.8 110.3 -5.4 -0.0 15.6 41 47 A N T 3 S- 0 0 146 -2,-0.7 -15,-0.1 -17,-0.4 -2,-0.0 -0.441 125.9 -17.9 58.0-105.7 -7.7 -3.0 15.1 42 48 A D T 3 S+ 0 0 128 -2,-0.6 2,-0.3 -3,-0.0 -1,-0.3 0.260 123.1 84.7-113.0 9.5 -10.8 -1.2 13.9 43 49 A R E < - E 0 40A 108 -3,-3.0 -3,-2.8 -25,-0.1 2,-0.4 -0.825 58.3-154.0-113.7 153.8 -10.0 2.3 15.1 44 50 A Q E + E 0 39A 105 -2,-0.3 2,-0.3 -5,-0.3 -5,-0.2 -0.970 34.7 106.8-127.3 141.9 -8.0 5.1 13.5 45 51 A G E - E 0 38A 4 -7,-2.3 -7,-3.2 -2,-0.4 2,-0.3 -0.980 59.0 -61.3 173.4-177.8 -6.1 8.0 15.0 46 52 A F E +cE 16 37A 58 -31,-2.4 -29,-1.7 -2,-0.3 -9,-0.2 -0.671 38.2 172.5 -96.5 146.1 -2.8 9.5 15.9 47 53 A V E - E 0 36A 0 -11,-2.0 -11,-2.4 -2,-0.3 2,-0.1 -0.924 50.0 -73.7-139.2 160.6 -0.1 8.1 18.2 48 54 A P E > - E 0 35A 15 0, 0.0 3,-1.5 0, 0.0 -13,-0.3 -0.393 36.7-139.8 -61.2 128.9 3.4 9.4 18.9 49 55 A A G > S+ 0 0 11 -15,-2.3 3,-1.4 1,-0.3 -14,-0.1 0.864 102.4 58.7 -56.1 -36.8 5.6 8.6 15.9 50 56 A A G 3 S+ 0 0 81 -16,-0.4 -1,-0.3 1,-0.2 -15,-0.1 0.703 95.4 64.6 -67.9 -18.6 8.4 7.7 18.3 51 57 A Y G < S+ 0 0 90 -3,-1.5 -45,-3.1 -45,-0.1 -44,-0.9 0.432 99.4 58.4 -86.4 0.9 6.3 5.0 20.0 52 58 A V E < -B 5 0A 10 -3,-1.4 2,-0.4 -47,-0.2 -47,-0.2 -0.919 66.7-147.9-129.6 157.2 6.0 2.8 16.9 53 59 A K E -B 4 0A 116 -49,-2.1 -49,-2.8 -2,-0.3 2,-0.1 -0.988 21.8-121.7-128.8 127.6 8.5 1.1 14.6 54 60 A K E -B 3 0A 83 -2,-0.4 -51,-0.2 -51,-0.2 -2,-0.0 -0.424 17.3-169.6 -65.5 135.8 8.1 0.5 10.9 55 61 A L 0 0 81 -53,-2.7 -1,-0.2 -2,-0.1 -52,-0.2 0.571 360.0 360.0 -99.2 -15.2 8.3 -3.2 10.0 56 62 A D 0 0 147 -54,-0.8 -2,-0.0 0, 0.0 0, 0.0 -0.526 360.0 360.0-116.5 360.0 8.5 -2.3 6.3