==== 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 1UH1 . 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) . 28196.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 442 74.7 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 . 16 2.7 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 65 0, 0.0 2,-0.6 0, 0.0 120,-0.3 0.000 360.0 360.0 360.0 176.6 10.6 49.8 16.2 2 2 A K E -A 120 0A 145 118,-2.8 118,-1.9 1,-0.0 2,-0.1 -0.756 360.0-134.6 -88.1 122.3 7.9 48.6 18.5 3 3 A A E -A 119 0A 65 -2,-0.6 2,-0.3 116,-0.3 116,-0.3 -0.325 23.2-174.6 -73.3 152.7 6.5 51.4 20.7 4 4 A F E -A 118 0A 19 114,-2.9 114,-2.5 -2,-0.1 2,-0.3 -0.972 14.7-172.2-145.1 157.5 5.9 51.0 24.4 5 5 A D E -A 117 0A 83 -2,-0.3 112,-0.2 112,-0.3 3,-0.1 -0.785 4.6-175.3-154.7 102.4 4.4 53.1 27.2 6 6 A D - 0 0 28 110,-2.2 2,-0.2 -2,-0.3 111,-0.1 0.735 35.2-145.5 -73.2 -21.5 4.6 52.0 30.8 7 7 A G - 0 0 17 109,-0.5 2,-0.3 2,-0.0 109,-0.3 -0.495 34.9 -43.4 87.8-162.0 2.5 54.8 32.1 8 8 A A + 0 0 47 -2,-0.2 107,-0.2 107,-0.1 2,-0.2 -0.813 54.3 170.7-113.2 151.2 3.0 56.4 35.4 9 9 A F - 0 0 35 105,-1.9 25,-0.2 -2,-0.3 3,-0.1 -0.671 48.2 -89.7-137.7-168.5 3.8 55.1 38.9 10 10 A T S S- 0 0 59 23,-2.1 2,-0.3 1,-0.2 24,-0.2 0.727 91.7 -50.2 -82.4 -24.1 4.7 56.1 42.4 11 11 A G E -E 33 0B 5 22,-1.1 22,-2.7 103,-0.2 2,-0.5 -0.987 59.5 -76.4 172.9-174.1 8.5 55.9 41.7 12 12 A I E +E 32 0B 15 -2,-0.3 20,-0.2 20,-0.3 3,-0.1 -0.946 31.7 166.6-119.3 131.7 11.4 53.9 40.4 13 13 A R E + 0 0 59 18,-2.3 45,-2.5 -2,-0.5 2,-0.3 0.795 68.0 2.0-106.3 -44.4 13.0 51.0 42.2 14 14 A E E -EF 31 57B 45 17,-2.1 17,-3.2 43,-0.2 2,-0.4 -0.998 53.6-155.0-149.9 147.5 15.2 49.3 39.6 15 15 A I E -EF 30 56B 0 41,-2.2 41,-3.0 -2,-0.3 2,-0.5 -0.992 6.8-168.8-127.5 130.1 16.2 49.7 35.9 16 16 A N E +EF 29 55B 31 13,-3.4 13,-1.4 -2,-0.4 2,-0.3 -0.939 21.4 152.6-122.3 110.5 17.4 46.9 33.6 17 17 A L E -EF 28 54B 4 37,-2.0 37,-2.6 -2,-0.5 2,-0.3 -0.856 25.9-150.9-131.1 166.5 18.9 47.8 30.3 18 18 A S E + F 0 53B 5 9,-1.7 8,-3.2 -2,-0.3 2,-0.3 -0.937 16.4 173.9-134.7 158.0 21.4 46.4 27.8 19 19 A Y E -EF 25 52B 48 33,-1.5 33,-3.5 -2,-0.3 2,-0.4 -0.927 27.1-131.1-153.6 175.4 23.8 48.0 25.3 20 20 A N > - 0 0 43 4,-1.3 3,-0.7 -2,-0.3 78,-0.3 -0.989 19.4-138.3-136.2 122.6 26.6 47.3 22.9 21 21 A K T 3 S+ 0 0 169 -2,-0.4 78,-0.1 1,-0.2 4,-0.1 0.504 104.1 46.8 -64.9 3.2 29.7 49.5 23.1 22 22 A E T 3 S+ 0 0 159 2,-0.1 -1,-0.2 76,-0.1 60,-0.0 0.685 124.7 15.8-112.1 -29.8 29.6 49.6 19.3 23 23 A T S < S- 0 0 32 -3,-0.7 2,-0.2 1,-0.3 75,-0.2 0.664 98.1 -83.2-108.5 -92.1 26.0 50.4 18.4 24 24 A A - 0 0 0 73,-0.1 -4,-1.3 48,-0.0 -1,-0.3 -0.822 59.9 -33.6-161.3-160.9 23.5 51.7 21.0 25 25 A I E -E 19 0B 0 56,-2.0 99,-1.9 -2,-0.2 -6,-0.3 -0.552 50.2-179.6 -77.6 138.6 21.1 50.9 23.7 26 26 A G E + 0 0 0 -8,-3.2 -7,-0.1 1,-0.3 -1,-0.1 0.769 50.8 17.8-101.2 -93.5 19.2 47.6 23.4 27 27 A D E - 0 0 36 18,-0.1 -9,-1.7 19,-0.1 2,-0.3 -0.438 57.5-167.6 -84.6 159.4 16.7 46.3 25.9 28 28 A F E +EG 17 44B 5 16,-2.5 16,-2.3 -11,-0.2 2,-0.3 -0.974 15.0 156.6-149.3 130.4 14.9 48.4 28.5 29 29 A Q E -E 16 0B 18 -13,-1.4 -13,-3.4 -2,-0.3 2,-0.4 -0.975 17.9-158.9-155.6 138.9 12.8 47.3 31.5 30 30 A V E -E 15 0B 0 12,-0.4 11,-2.2 -2,-0.3 2,-0.8 -0.954 14.9-149.2-129.0 144.0 11.9 49.0 34.7 31 31 A V E -EH 14 40B 19 -17,-3.2 -18,-2.3 -2,-0.4 -17,-2.1 -0.921 32.1-168.2-108.3 104.1 10.7 47.8 38.1 32 32 A Y E -EH 12 39B 0 7,-2.1 7,-3.1 -2,-0.8 2,-0.5 -0.275 22.2-115.1 -87.0 173.1 8.5 50.6 39.4 33 33 A D E -EH 11 38B 3 -22,-2.7 -23,-2.1 5,-0.2 -22,-1.1 -0.952 23.1-165.8-109.0 128.7 7.1 51.3 42.8 34 34 A L E > S- H 0 37B 68 3,-3.7 3,-1.3 -2,-0.5 -25,-0.0 -0.849 72.1 -43.9-118.2 93.4 3.4 51.2 43.1 35 35 A N T 3 S- 0 0 134 -2,-0.6 -1,-0.1 1,-0.3 -2,-0.0 0.935 124.7 -35.9 51.3 54.2 2.3 52.8 46.3 36 36 A G T 3 S+ 0 0 49 1,-0.2 -1,-0.3 0, 0.0 -3,-0.0 0.345 122.1 99.5 85.4 -7.1 5.0 51.0 48.3 37 37 A S E < S-H 34 0B 72 -3,-1.3 -3,-3.7 2,-0.0 -1,-0.2 -0.928 77.5-111.0-117.1 139.8 4.9 47.7 46.4 38 38 A P E -H 33 0B 85 0, 0.0 2,-0.5 0, 0.0 -5,-0.2 -0.404 30.3-164.6 -64.1 137.6 7.4 46.7 43.7 39 39 A Y E -H 32 0B 113 -7,-3.1 -7,-2.1 -2,-0.1 2,-0.8 -0.962 13.0-140.8-129.7 113.0 5.7 46.6 40.2 40 40 A V E -H 31 0B 105 -2,-0.5 -9,-0.2 -9,-0.2 3,-0.1 -0.617 20.4-144.7 -76.5 110.4 7.6 44.7 37.5 41 41 A G - 0 0 6 -11,-2.2 2,-0.1 -2,-0.8 -1,-0.0 -0.240 30.1 -85.4 -71.7 162.3 7.3 46.6 34.3 42 42 A Q - 0 0 129 1,-0.1 2,-0.7 -13,-0.1 -12,-0.4 -0.462 44.2-117.8 -67.4 138.5 7.0 44.8 30.9 43 43 A N - 0 0 79 -2,-0.1 2,-0.7 -14,-0.1 -14,-0.2 -0.688 24.1-155.7 -83.9 115.8 10.4 44.0 29.4 44 44 A H B -G 28 0B 15 -16,-2.3 -16,-2.5 -2,-0.7 2,-0.3 -0.821 19.9-164.6 -93.1 112.3 10.8 45.8 26.1 45 45 A K - 0 0 135 -2,-0.7 -18,-0.1 -18,-0.2 75,-0.1 -0.703 19.3-111.5-107.8 153.5 13.3 43.9 24.0 46 46 A S - 0 0 13 -2,-0.3 76,-0.2 2,-0.2 77,-0.1 -0.323 27.4-121.1 -70.7 155.1 15.4 44.6 20.9 47 47 A F S S+ 0 0 130 74,-2.7 2,-0.2 -21,-0.1 75,-0.2 0.737 98.9 40.6 -69.6 -21.0 14.6 42.8 17.7 48 48 A I S S- 0 0 55 73,-0.3 -2,-0.2 74,-0.3 2,-0.2 -0.593 76.9-136.4-117.8-179.5 18.2 41.4 17.9 49 49 A T + 0 0 130 -2,-0.2 -2,-0.0 1,-0.1 -1,-0.0 -0.556 58.7 95.3-124.8-170.5 20.5 40.1 20.5 50 50 A G + 0 0 59 1,-0.3 2,-0.2 -2,-0.2 -1,-0.1 0.615 56.6 136.9 98.3 14.5 24.2 40.5 21.5 51 51 A F - 0 0 30 -3,-0.1 -1,-0.3 -31,-0.1 -31,-0.2 -0.511 55.6-119.3 -92.9 161.6 23.8 43.2 24.1 52 52 A T E -F 19 0B 65 -33,-3.5 -33,-1.5 -2,-0.2 -26,-0.2 -0.892 31.0-133.8-101.6 119.8 25.4 43.5 27.6 53 53 A P E -F 18 0B 108 0, 0.0 2,-0.3 0, 0.0 -35,-0.3 -0.410 21.8-172.2 -73.4 148.8 22.9 43.5 30.4 54 54 A V E -F 17 0B 24 -37,-2.6 -37,-2.0 -2,-0.1 2,-0.5 -0.991 8.7-156.8-142.9 131.7 23.1 46.1 33.2 55 55 A K E -F 16 0B 120 -2,-0.3 2,-0.6 -39,-0.2 -39,-0.2 -0.947 2.6-166.8-113.3 129.7 21.0 46.2 36.4 56 56 A I E -F 15 0B 2 -41,-3.0 -41,-2.2 -2,-0.5 2,-0.6 -0.879 7.9-171.4-117.2 96.2 20.6 49.5 38.2 57 57 A S E -F 14 0B 65 -2,-0.6 2,-0.3 -43,-0.2 -43,-0.2 -0.799 10.2-154.1 -91.3 119.9 19.2 48.9 41.7 58 58 A L - 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