==== 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 22-JUN-03 1UGX . 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, . 148 2 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 7959.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 103 69.6 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 . 73 49.3 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 . 1 0.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 3 2.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 1 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 . 20 13.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 2.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 1 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 . 1 0 0 3 1 2 1 1 0 1 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 2 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 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 73 0, 0.0 2,-0.7 0, 0.0 120,-0.3 0.000 360.0 360.0 360.0-179.3 35.2 32.1 21.9 2 2 A K E -A 120 0A 145 118,-2.9 118,-1.8 1,-0.0 2,-0.1 -0.806 360.0-135.2 -92.7 118.1 34.7 30.8 18.4 3 3 A A E -A 119 0A 66 -2,-0.7 2,-0.3 116,-0.2 116,-0.3 -0.360 23.9-175.0 -72.0 149.9 33.7 33.6 16.0 4 4 A F E -A 118 0A 19 114,-2.8 114,-2.6 -2,-0.1 2,-0.3 -0.961 14.3-171.5-141.0 157.7 31.0 33.1 13.4 5 5 A D E -A 117 0A 84 -2,-0.3 112,-0.2 112,-0.2 -2,-0.0 -0.778 5.7-177.8-153.9 101.9 29.5 35.1 10.6 6 6 A D - 0 0 28 110,-2.2 2,-0.2 -2,-0.3 111,-0.2 0.812 36.3-147.5 -72.1 -29.8 26.4 34.0 8.9 7 7 A G - 0 0 18 109,-0.7 109,-0.4 2,-0.0 2,-0.3 -0.490 32.4 -40.0 93.3-167.6 26.4 36.9 6.4 8 8 A A + 0 0 47 -2,-0.2 107,-0.2 107,-0.2 2,-0.2 -0.795 56.2 166.1-105.7 143.3 23.4 38.6 4.9 9 9 A F - 0 0 40 105,-2.4 25,-0.2 -2,-0.3 3,-0.1 -0.498 48.8 -89.0-131.2-161.2 20.2 37.1 3.6 10 10 A T S S- 0 0 58 23,-2.3 2,-0.3 1,-0.3 24,-0.2 0.620 89.8 -45.2 -94.5 -18.0 16.7 38.2 2.5 11 11 A G E -D 33 0B 6 22,-1.0 22,-2.0 103,-0.2 2,-0.4 -0.975 61.3 -82.6 172.9-172.3 15.0 38.0 5.9 12 12 A I E +D 32 0B 12 -2,-0.3 20,-0.2 20,-0.3 3,-0.1 -0.982 30.4 168.8-125.7 132.2 14.5 35.9 9.0 13 13 A R E + 0 0 64 18,-2.6 45,-2.4 -2,-0.4 2,-0.3 0.764 68.1 1.9-107.6 -38.1 12.1 33.0 9.4 14 14 A E E -DE 31 57B 41 17,-2.1 17,-3.1 43,-0.2 2,-0.4 -0.997 51.4-154.9-155.5 146.9 13.2 31.4 12.7 15 15 A I E -DE 30 56B 1 41,-2.3 41,-3.0 -2,-0.3 2,-0.5 -0.991 8.0-170.4-126.5 130.8 15.6 31.7 15.6 16 16 A N E +DE 29 55B 35 13,-3.2 13,-2.0 -2,-0.4 2,-0.3 -0.976 22.4 151.3-121.8 115.5 16.8 28.9 17.8 17 17 A L E -DE 28 54B 4 37,-1.7 37,-2.0 -2,-0.5 2,-0.3 -0.899 29.4-143.3-138.5 167.7 18.8 29.8 20.8 18 18 A S E - E 0 53B 3 9,-1.8 8,-3.2 -2,-0.3 2,-0.3 -0.956 17.0-179.9-133.2 153.7 19.4 28.4 24.3 19 19 A Y E -DE 25 52B 54 33,-2.2 33,-3.6 -2,-0.3 2,-0.4 -0.938 22.6-139.7-146.7 166.7 19.9 30.1 27.6 20 20 A N > - 0 0 36 4,-1.3 3,-1.2 -2,-0.3 78,-0.2 -0.994 16.3-142.5-132.7 121.5 20.6 29.4 31.3 21 21 A K T 3 S+ 0 0 163 -2,-0.4 4,-0.1 1,-0.3 30,-0.0 0.495 101.9 48.7 -64.1 -2.9 18.7 31.5 33.9 22 22 A E T 3 S+ 0 0 155 2,-0.1 -1,-0.3 76,-0.1 76,-0.0 0.587 127.4 9.3-109.7 -16.9 21.8 31.5 36.1 23 23 A T S < S- 0 0 31 -3,-1.2 2,-0.2 1,-0.2 75,-0.2 0.488 97.3 -74.2-125.1 -91.6 24.4 32.5 33.5 24 24 A A - 0 0 0 73,-0.1 -4,-1.3 98,-0.1 58,-0.2 -0.851 57.4 -42.5-160.1-167.4 23.9 33.7 29.9 25 25 A I E +D 19 0B 0 56,-2.0 99,-2.1 -2,-0.2 -6,-0.3 -0.524 49.6 174.3 -74.4 140.9 22.9 32.9 26.3 26 26 A G E + 0 0 0 -8,-3.2 -1,-0.1 1,-0.3 -7,-0.1 0.597 48.9 27.0-110.3 -97.6 24.4 29.7 24.9 27 27 A D E - 0 0 40 18,-0.1 -9,-1.8 19,-0.1 2,-0.3 -0.346 58.3-170.5 -74.3 152.1 23.6 28.3 21.4 28 28 A F E +DF 17 44B 6 16,-2.5 16,-2.4 -11,-0.2 2,-0.3 -0.970 13.1 157.8-148.1 127.3 22.5 30.4 18.5 29 29 A Q E -D 16 0B 15 -13,-2.0 -13,-3.2 -2,-0.3 2,-0.4 -0.994 17.2-159.4-149.8 141.5 21.1 29.3 15.1 30 30 A V E -D 15 0B 0 12,-0.4 11,-2.3 -2,-0.3 2,-0.7 -0.972 14.0-149.8-130.0 139.9 19.0 31.1 12.5 31 31 A V E -DG 14 40B 20 -17,-3.1 -18,-2.6 -2,-0.4 -17,-2.1 -0.940 32.4-166.6-103.5 111.8 16.8 29.9 9.7 32 32 A Y E -DG 12 39B 0 7,-2.7 7,-2.8 -2,-0.7 2,-0.4 -0.429 22.0-116.3 -93.9 170.2 16.9 32.7 7.1 33 33 A D E -DG 11 38B 3 -22,-2.0 -23,-2.3 5,-0.2 -22,-1.0 -0.898 24.9-167.8-102.9 138.4 14.9 33.4 4.1 34 34 A L E > S- G 0 37B 73 3,-3.1 3,-1.3 -2,-0.4 -25,-0.0 -0.859 71.0 -42.4-129.7 94.4 16.9 33.3 0.9 35 35 A N T 3 S- 0 0 131 -2,-0.4 -2,-0.0 1,-0.3 -26,-0.0 0.877 125.2 -35.5 52.8 45.6 14.9 34.8 -1.9 36 36 A G T 3 S+ 0 0 49 1,-0.2 -1,-0.3 0, 0.0 -3,-0.0 0.323 123.5 89.6 96.3 -9.3 11.6 33.1 -0.9 37 37 A S E < S-G 34 0B 72 -3,-1.3 -3,-3.1 2,-0.0 -1,-0.2 -0.911 80.8-103.5-122.3 149.8 13.0 29.8 0.4 38 38 A P E -G 33 0B 85 0, 0.0 2,-0.4 0, 0.0 -5,-0.2 -0.419 30.1-165.5 -69.9 144.1 14.2 28.8 3.8 39 39 A Y E -G 32 0B 114 -7,-2.8 -7,-2.7 -2,-0.1 2,-0.7 -0.952 14.4-140.5-132.8 112.8 18.0 28.6 4.3 40 40 A V E -G 31 0B 103 -2,-0.4 -9,-0.2 -9,-0.2 3,-0.1 -0.617 18.9-146.6 -77.8 111.7 19.2 26.9 7.5 41 41 A G - 0 0 7 -11,-2.3 -35,-0.0 -2,-0.7 -1,-0.0 -0.306 31.4 -83.4 -73.6 161.6 22.1 28.7 9.0 42 42 A Q - 0 0 123 1,-0.1 2,-0.6 -13,-0.1 -12,-0.4 -0.303 43.9-114.2 -63.3 145.1 24.9 26.9 10.8 43 43 A N - 0 0 91 -14,-0.1 2,-0.8 -3,-0.1 -14,-0.2 -0.743 25.4-154.9 -85.2 121.4 24.3 26.0 14.4 44 44 A H B -F 28 0B 13 -16,-2.4 -16,-2.5 -2,-0.6 2,-0.3 -0.861 20.9-165.3 -99.7 107.0 26.7 28.0 16.6 45 45 A V - 0 0 75 -2,-0.8 75,-0.1 -18,-0.2 -18,-0.1 -0.688 20.2-114.8-104.6 150.2 27.1 26.0 19.8 46 46 A S - 0 0 10 -2,-0.3 76,-0.2 2,-0.2 77,-0.1 -0.284 27.2-121.8 -67.3 156.6 28.5 26.7 23.2 47 47 A F S S+ 0 0 123 74,-2.4 2,-0.2 76,-0.1 75,-0.2 0.673 96.7 44.1 -73.9 -17.8 31.6 24.8 24.3 48 48 A I S S- 0 0 59 73,-0.3 -2,-0.2 74,-0.3 2,-0.2 -0.612 76.3-133.0-119.5-179.9 29.5 23.5 27.2 49 49 A T + 0 0 130 -2,-0.2 -2,-0.1 1,-0.1 -1,-0.0 -0.530 60.1 92.1-121.5-171.5 26.0 22.1 27.9 50 50 A G + 0 0 56 1,-0.3 2,-0.2 -2,-0.2 -1,-0.1 0.637 57.6 137.8 96.6 17.2 23.2 22.6 30.4 51 51 A F - 0 0 28 -3,-0.1 -1,-0.3 -31,-0.1 -31,-0.2 -0.621 52.7-126.3 -97.2 156.1 21.2 25.2 28.4 52 52 A T E -E 19 0B 69 -33,-3.6 -33,-2.2 -2,-0.2 -26,-0.1 -0.888 29.0-142.3-100.7 120.4 17.4 25.5 27.9 53 53 A P E -E 18 0B 102 0, 0.0 2,-0.3 0, 0.0 -35,-0.2 -0.399 18.5-176.9 -82.0 159.7 16.5 25.7 24.2 54 54 A V E -E 17 0B 33 -37,-2.0 -37,-1.7 -2,-0.1 2,-0.5 -0.978 15.4-144.6-153.0 143.9 13.7 27.8 22.7 55 55 A K E -E 16 0B 115 -2,-0.3 2,-0.7 -39,-0.2 -39,-0.2 -0.955 5.7-163.4-115.5 130.9 12.4 28.2 19.2 56 56 A I E -E 15 0B 2 -41,-3.0 -41,-2.3 -2,-0.5 2,-0.7 -0.905 10.3-171.8-115.5 99.5 11.1 31.5 17.8 57 57 A S E -E 14 0B 65 -2,-0.7 2,-0.3 -43,-0.2 -43,-0.2 -0.841 8.5-156.1 -96.7 115.6 9.1 30.9 14.7 58 58 A L - 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