==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=20-JUL-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SUGAR BINDING PROTEIN 23-JUN-03 1UH0 . COMPND 2 MOLECULE: AGGLUTININ ALPHA CHAIN; . SOURCE 2 ORGANISM_SCIENTIFIC: ARTOCARPUS INTEGER; . AUTHOR A.A.JEYAPRAKASH,S.KATIYAR,C.P.SWAMINATHAN,K.SEKAR,A.SUROLIA, . 592 8 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 28243.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 441 74.5 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 . 308 52.0 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 . 4 0.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 12 2.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 4 0.7 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 . 91 15.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 14 2.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 4 0.7 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 . 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 . 4 4 0 12 4 8 4 4 0 4 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 4 8 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 G 0 0 70 0, 0.0 2,-0.6 0, 0.0 120,-0.3 0.000 360.0 360.0 360.0 174.8 10.6 50.1 16.1 2 2 A K E -A 120 0A 134 118,-2.9 118,-2.0 119,-0.0 2,-0.1 -0.799 360.0-134.9 -93.2 118.9 7.9 48.8 18.5 3 3 A A E -A 119 0A 66 -2,-0.6 2,-0.3 116,-0.3 116,-0.3 -0.357 23.6-175.6 -72.5 150.6 6.5 51.6 20.7 4 4 A F E -A 118 0A 18 114,-2.9 114,-2.7 -2,-0.1 2,-0.2 -0.966 13.7-173.9-142.8 158.2 6.0 51.2 24.4 5 5 A D E -A 117 0A 81 -2,-0.3 112,-0.2 112,-0.3 -2,-0.0 -0.765 5.1-174.8-157.8 100.9 4.5 53.4 27.2 6 6 A D - 0 0 30 110,-2.4 111,-0.2 -2,-0.2 2,-0.1 0.788 34.7-145.7 -70.8 -28.2 4.6 52.2 30.8 7 7 A G - 0 0 15 109,-0.6 109,-0.3 2,-0.0 2,-0.3 -0.475 34.6 -40.0 91.8-167.7 2.6 55.1 32.1 8 8 A A + 0 0 48 107,-0.1 107,-0.2 -2,-0.1 2,-0.2 -0.739 55.4 169.3-104.8 148.9 3.0 56.8 35.5 9 9 A F - 0 0 35 105,-2.0 25,-0.2 -2,-0.3 3,-0.1 -0.675 48.1 -90.8-136.8-169.4 3.8 55.3 38.9 10 10 A T S S- 0 0 59 23,-2.1 2,-0.3 1,-0.2 24,-0.2 0.739 91.2 -49.4 -81.7 -25.5 4.8 56.3 42.5 11 11 A G E -E 33 0B 6 22,-1.0 22,-2.1 103,-0.2 2,-0.4 -0.977 59.7 -79.4 175.9-170.5 8.5 56.1 41.8 12 12 A I E +E 32 0B 15 -2,-0.3 20,-0.2 20,-0.3 3,-0.1 -0.976 31.3 168.0-124.8 131.3 11.4 54.1 40.5 13 13 A R E + 0 0 60 18,-2.4 45,-2.3 -2,-0.4 2,-0.3 0.778 68.0 2.5-106.9 -42.3 13.1 51.2 42.2 14 14 A E E -EF 31 57B 44 17,-1.9 17,-3.5 43,-0.2 2,-0.4 -0.994 53.6-155.2-153.2 141.9 15.3 49.5 39.6 15 15 A I E -EF 30 56B 0 41,-2.3 41,-3.1 -2,-0.3 2,-0.6 -0.980 7.2-168.7-121.7 128.1 16.3 49.9 36.0 16 16 A N E +EF 29 55B 32 13,-3.4 13,-1.7 -2,-0.4 2,-0.3 -0.947 20.9 154.3-118.6 113.0 17.4 47.1 33.7 17 17 A L E -EF 28 54B 4 37,-1.9 37,-2.4 -2,-0.6 2,-0.3 -0.881 25.9-150.1-132.8 165.2 18.9 48.0 30.4 18 18 A S E + F 0 53B 6 9,-1.7 8,-3.4 -2,-0.3 2,-0.3 -0.953 17.1 175.0-133.9 154.2 21.4 46.5 27.9 19 19 A Y E -EF 25 52B 50 33,-1.4 33,-3.3 -2,-0.3 2,-0.4 -0.918 26.3-132.6-149.7 174.5 23.8 48.2 25.4 20 20 A N > - 0 0 42 4,-1.2 3,-0.8 -2,-0.3 78,-0.2 -0.985 18.3-139.2-135.2 120.0 26.6 47.5 22.9 21 21 A K T 3 S+ 0 0 166 -2,-0.4 78,-0.1 1,-0.2 4,-0.1 0.508 103.6 44.9 -61.0 -4.7 29.7 49.6 23.0 22 22 A E T 3 S+ 0 0 162 2,-0.1 -1,-0.2 76,-0.1 60,-0.0 0.602 126.3 16.8-103.3 -24.2 29.7 49.8 19.2 23 23 A T S < S- 0 0 30 -3,-0.8 2,-0.2 1,-0.2 75,-0.2 0.702 97.5 -79.0-112.9 -90.5 26.2 50.5 18.5 24 24 A A - 0 0 0 73,-0.1 -4,-1.2 48,-0.0 -1,-0.2 -0.886 58.1 -41.0-163.0-166.3 23.5 51.8 21.0 25 25 A I E +E 19 0B 0 56,-2.0 99,-1.9 -2,-0.2 -6,-0.3 -0.516 50.2 179.6 -74.3 139.1 21.1 51.0 23.8 26 26 A G E + 0 0 0 -8,-3.4 2,-0.2 1,-0.3 -7,-0.1 0.794 50.3 21.2-104.4 -86.9 19.2 47.8 23.4 27 27 A D E - 0 0 35 18,-0.1 -9,-1.7 19,-0.1 2,-0.3 -0.550 58.0-166.9 -89.8 155.3 16.7 46.5 25.9 28 28 A F E +EG 17 44B 6 16,-2.7 16,-2.3 -11,-0.2 2,-0.3 -0.985 14.9 157.5-144.7 129.7 14.9 48.6 28.5 29 29 A Q E -E 16 0B 17 -13,-1.7 -13,-3.4 -2,-0.3 2,-0.4 -0.982 17.0-160.1-153.3 138.0 12.9 47.5 31.6 30 30 A V E -E 15 0B 0 12,-0.4 11,-2.2 -2,-0.3 2,-0.7 -0.945 14.7-150.1-127.4 144.7 11.9 49.2 34.8 31 31 A V E -EH 14 40B 20 -17,-3.5 -18,-2.4 -2,-0.4 -17,-1.9 -0.930 32.1-168.8-109.6 103.7 10.8 48.0 38.2 32 32 A Y E -EH 12 39B 0 7,-2.2 7,-3.2 -2,-0.7 2,-0.5 -0.278 22.3-115.0 -87.5 174.2 8.6 50.8 39.5 33 33 A D E -EH 11 38B 3 -22,-2.1 -23,-2.1 5,-0.2 -22,-1.0 -0.953 23.0-166.0-110.1 128.3 7.1 51.5 42.9 34 34 A L E > S- H 0 37B 67 3,-4.1 3,-1.5 -2,-0.5 -25,-0.0 -0.872 72.0 -43.5-118.4 97.0 3.3 51.4 43.1 35 35 A N T 3 S- 0 0 138 -2,-0.6 -1,-0.1 1,-0.3 -2,-0.0 0.902 125.3 -35.4 50.0 50.6 2.2 52.9 46.4 36 36 A G T 3 S+ 0 0 52 1,-0.2 -1,-0.3 0, 0.0 -3,-0.0 0.350 122.6 99.1 90.2 -7.3 4.9 51.2 48.4 37 37 A S E < S-H 34 0B 74 -3,-1.5 -3,-4.1 2,-0.0 -1,-0.2 -0.905 77.5-111.0-116.6 143.1 4.9 48.0 46.4 38 38 A P E -H 33 0B 81 0, 0.0 2,-0.5 0, 0.0 -5,-0.2 -0.485 29.7-163.5 -69.6 136.4 7.4 46.9 43.7 39 39 A Y E -H 32 0B 112 -7,-3.2 -7,-2.2 -2,-0.2 2,-0.9 -0.966 12.4-141.5-125.5 114.0 5.7 46.8 40.3 40 40 A V E -H 31 0B 105 -2,-0.5 -9,-0.2 -9,-0.2 3,-0.1 -0.644 20.4-147.9 -79.0 107.0 7.6 44.9 37.6 41 41 A G - 0 0 5 -11,-2.2 2,-0.1 -2,-0.9 -35,-0.0 -0.239 30.3 -83.2 -70.6 161.3 7.2 46.8 34.3 42 42 A Q - 0 0 128 1,-0.1 2,-0.8 -13,-0.1 -12,-0.4 -0.388 42.5-118.0 -66.3 139.4 7.1 45.0 31.0 43 43 A N - 0 0 81 -14,-0.1 2,-0.8 -2,-0.1 -14,-0.2 -0.708 24.6-155.7 -84.2 111.3 10.5 44.2 29.5 44 44 A H B -G 28 0B 14 -16,-2.3 -16,-2.7 -2,-0.8 2,-0.3 -0.795 20.5-164.5 -89.3 113.3 10.8 46.0 26.2 45 45 A K - 0 0 135 -2,-0.8 -18,-0.1 -18,-0.2 75,-0.1 -0.716 19.6-110.7-109.7 153.7 13.3 44.1 24.1 46 46 A S - 0 0 13 -2,-0.3 76,-0.2 2,-0.2 -19,-0.1 -0.374 27.2-122.4 -71.3 150.4 15.4 44.7 20.9 47 47 A F S S+ 0 0 129 74,-3.0 2,-0.2 -21,-0.1 75,-0.2 0.737 98.9 43.8 -65.4 -20.9 14.6 42.9 17.8 48 48 A I S S- 0 0 55 73,-0.3 -2,-0.2 74,-0.2 2,-0.2 -0.624 76.5-137.2-117.8 178.3 18.1 41.6 17.9 49 49 A T + 0 0 133 -2,-0.2 -2,-0.0 1,-0.1 -1,-0.0 -0.539 58.7 92.0-122.7-171.6 20.5 40.2 20.6 50 50 A G + 0 0 59 1,-0.3 2,-0.2 -2,-0.2 -1,-0.1 0.684 56.9 135.4 95.2 20.7 24.1 40.6 21.6 51 51 A F - 0 0 30 -3,-0.1 -1,-0.3 -31,-0.1 -31,-0.2 -0.547 56.1-117.5 -97.9 165.4 23.8 43.4 24.2 52 52 A T E -F 19 0B 65 -33,-3.3 -33,-1.4 -2,-0.2 -26,-0.1 -0.910 31.1-134.1-105.7 115.9 25.4 43.7 27.6 53 53 A P E -F 18 0B 106 0, 0.0 2,-0.3 0, 0.0 -35,-0.3 -0.327 21.1-172.1 -69.9 150.4 22.9 43.8 30.4 54 54 A V E -F 17 0B 25 -37,-2.4 -37,-1.9 -2,-0.0 2,-0.5 -0.993 9.6-155.4-143.6 132.4 23.1 46.3 33.3 55 55 A K E -F 16 0B 121 -2,-0.3 2,-0.7 -39,-0.2 -39,-0.2 -0.955 3.1-166.6-114.0 126.1 21.1 46.4 36.5 56 56 A I E -F 15 0B 2 -41,-3.1 -41,-2.3 -2,-0.5 2,-0.7 -0.872 8.5-171.9-112.9 95.6 20.7 49.7 38.3 57 57 A S E -F 14 0B 63 -2,-0.7 2,-0.3 -43,-0.2 -43,-0.2 -0.811 9.4-155.1 -92.3 116.0 19.2 49.1 41.8 58 58 A L - 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