==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=26-JAN-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SUGAR BINDING PROTEIN 29-JAN-10 3LLY . COMPND 2 MOLECULE: AGGLUTININ ALPHA CHAIN; . SOURCE 2 ORGANISM_SCIENTIFIC: MACLURA POMIFERA; . AUTHOR J.HUANG,Z.XU,D.WANG,C.OGATO,T.HIRAMA,K.PALCZEWSKI,S.L.HAZEN, . 149 2 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 8151.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 96 64.4 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 . 72 48.3 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 . 17 11.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 2 1.3 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 4 0 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 60 0, 0.0 2,-0.5 0, 0.0 120,-0.3 0.000 360.0 360.0 360.0-161.7 12.5 22.2 19.1 2 2 A V E -A 120 0A 97 118,-2.2 118,-2.0 119,-0.0 2,-0.1 -0.755 360.0-130.9 -90.8 130.2 12.4 18.5 20.0 3 3 A T E -A 119 0A 94 -2,-0.5 2,-0.3 116,-0.2 116,-0.3 -0.407 24.9-173.4 -77.2 154.9 11.4 16.2 17.1 4 4 A F E -A 118 0A 14 114,-2.4 114,-3.0 -2,-0.1 2,-0.2 -0.975 14.5-169.9-145.4 156.5 8.7 13.5 17.5 5 5 A D E -A 117 0A 81 -2,-0.3 112,-0.2 112,-0.3 3,-0.1 -0.758 6.1-174.8-153.9 99.3 7.4 10.7 15.3 6 6 A D - 0 0 13 110,-2.3 111,-0.2 -2,-0.2 2,-0.1 0.723 36.4-148.2 -65.8 -23.5 4.2 8.9 16.3 7 7 A G - 0 0 19 109,-0.4 109,-0.4 2,-0.0 2,-0.3 -0.449 35.3 -38.2 84.5-162.5 4.7 6.4 13.5 8 8 A A + 0 0 47 107,-0.1 107,-0.2 -2,-0.1 2,-0.2 -0.749 55.8 168.2-106.4 149.6 1.7 4.8 11.7 9 9 A Y - 0 0 46 105,-2.3 25,-0.2 -2,-0.3 3,-0.1 -0.599 48.0 -94.2-136.4-163.9 -1.6 3.5 13.0 10 10 A T S S- 0 0 56 23,-2.3 2,-0.3 1,-0.2 24,-0.2 0.429 89.0 -45.8-102.4 2.4 -4.9 2.3 11.7 11 11 A G E -D 33 0B 5 22,-0.7 22,-1.8 103,-0.2 2,-0.4 -0.976 62.3 -78.4 160.9-171.5 -6.7 5.7 11.9 12 12 A I E +D 32 0B 11 20,-0.3 20,-0.3 -2,-0.3 3,-0.1 -0.984 28.3 168.8-130.7 129.6 -7.4 8.8 14.1 13 13 A R E S+ 0 0 58 18,-2.5 45,-1.3 -2,-0.4 2,-0.3 0.761 71.2 1.4-102.9 -36.0 -9.9 9.1 17.0 14 14 A E E -DE 31 57B 47 17,-2.6 17,-3.7 43,-0.3 2,-0.4 -0.992 49.3-161.7-158.0 148.7 -8.8 12.5 18.4 15 15 A I E -DE 30 56B 1 41,-3.1 41,-2.9 -2,-0.3 2,-0.4 -0.974 10.7-176.4-134.6 117.9 -6.4 15.4 18.0 16 16 A N E +DE 29 55B 34 13,-2.8 13,-3.0 -2,-0.4 2,-0.3 -0.932 16.7 155.1-113.5 136.5 -5.7 17.9 20.8 17 17 A F E -DE 28 54B 6 37,-2.0 37,-2.8 -2,-0.4 2,-0.3 -0.992 35.0-116.1-157.5 161.0 -3.4 20.9 20.2 18 18 A E E + E 0 53B 45 9,-2.3 8,-2.9 -2,-0.3 2,-0.3 -0.735 26.9 178.0-102.1 149.3 -2.5 24.4 21.3 19 19 A Y E -DE 25 52B 34 33,-1.9 33,-2.2 -2,-0.3 2,-0.4 -0.992 16.0-156.6-148.6 148.8 -2.9 27.7 19.4 20 20 A N - 0 0 36 4,-0.8 78,-0.3 -2,-0.3 31,-0.1 -0.982 16.8-142.9-130.5 118.3 -2.3 31.4 20.2 21 21 A S S S+ 0 0 91 -2,-0.4 78,-0.1 1,-0.2 -1,-0.1 0.597 102.1 38.5 -56.8 -12.1 -4.1 34.0 18.2 22 22 A E S S+ 0 0 160 2,-0.1 -1,-0.2 76,-0.1 60,-0.0 0.787 128.3 19.3-106.4 -40.1 -1.0 36.2 18.2 23 23 A T S S- 0 0 34 1,-0.2 2,-0.2 52,-0.0 75,-0.2 0.758 98.1 -83.4 -96.7 -98.8 1.9 33.8 17.8 24 24 A A - 0 0 0 98,-0.1 -4,-0.8 73,-0.1 58,-0.3 -0.848 54.5 -41.4-158.2-167.4 1.5 30.3 16.5 25 25 A I E -D 19 0B 1 56,-2.4 99,-2.3 -2,-0.2 -6,-0.3 -0.447 50.8-172.7 -72.0 144.6 0.6 26.6 17.1 26 26 A G E - 0 0 0 -8,-2.9 -1,-0.1 1,-0.3 97,-0.1 0.250 43.1 -4.8-107.4-130.4 1.8 25.0 20.3 27 27 A G E - 0 0 3 95,-0.1 -9,-2.3 -10,-0.1 2,-0.3 -0.110 56.1-157.4 -66.4 163.9 1.7 21.5 21.6 28 28 A L E +DF 17 44B 10 16,-3.1 16,-2.7 -11,-0.2 2,-0.4 -0.997 13.3 178.1-147.0 137.3 0.0 18.5 19.9 29 29 A R E -D 16 0B 101 -13,-3.0 -13,-2.8 -2,-0.3 2,-0.4 -0.952 12.6-161.4-143.3 120.1 -1.3 15.1 21.2 30 30 A V E -D 15 0B 0 12,-0.4 11,-2.6 -2,-0.4 2,-0.7 -0.838 10.5-156.5-108.1 137.7 -3.0 12.6 18.9 31 31 A T E -DG 14 40B 23 -17,-3.7 -17,-2.6 -2,-0.4 -18,-2.5 -0.943 25.6-173.0-110.2 109.1 -5.2 9.7 19.9 32 32 A Y E -DG 12 39B 0 7,-2.5 7,-2.3 -2,-0.7 2,-0.5 -0.302 26.1-113.5 -92.5 176.9 -5.1 7.2 17.1 33 33 A D E -DG 11 38B 5 -22,-1.8 -23,-2.3 5,-0.2 -22,-0.7 -0.966 25.6-165.8-111.8 131.3 -7.0 4.0 16.5 34 34 A L E > S- G 0 37B 51 3,-3.4 3,-2.0 -2,-0.5 -25,-0.0 -0.923 72.2 -39.4-120.2 101.3 -4.9 0.9 16.6 35 35 A N T 3 S- 0 0 132 -2,-0.6 -1,-0.1 1,-0.3 -24,-0.0 0.847 126.0 -38.8 50.3 41.6 -6.8 -2.1 15.2 36 36 A G T 3 S+ 0 0 47 1,-0.3 -1,-0.3 0, 0.0 -3,-0.0 0.288 121.2 98.7 96.7 -10.9 -10.0 -1.0 16.8 37 37 A M E < S-G 34 0B 123 -3,-2.0 -3,-3.4 1,-0.0 -1,-0.3 -0.834 78.3-104.8-113.0 150.3 -8.6 0.2 20.1 38 38 A P E -G 33 0B 91 0, 0.0 2,-0.3 0, 0.0 -5,-0.2 -0.435 33.8-173.4 -68.7 141.3 -7.8 3.8 21.2 39 39 A F E -G 32 0B 86 -7,-2.3 -7,-2.5 -2,-0.1 2,-0.7 -0.806 10.0-157.1-141.6 97.9 -4.1 4.5 21.3 40 40 A V E -G 31 0B 75 -2,-0.3 -9,-0.2 -9,-0.3 3,-0.1 -0.654 15.8-147.8 -79.0 111.5 -3.1 7.8 22.8 41 41 A A - 0 0 6 -11,-2.6 3,-0.0 -2,-0.7 -35,-0.0 -0.186 37.1 -71.3 -70.1 170.8 0.3 8.8 21.5 42 42 A E - 0 0 127 1,-0.1 2,-0.5 -13,-0.1 -12,-0.4 -0.305 51.9-106.0 -67.6 147.9 2.7 10.8 23.6 43 43 A D - 0 0 69 -14,-0.1 2,-1.0 -3,-0.1 -14,-0.2 -0.631 25.7-154.4 -77.1 121.1 2.0 14.4 24.3 44 44 A H B -F 28 0B 13 -16,-2.7 -16,-3.1 -2,-0.5 2,-0.2 -0.840 25.5-164.4 -99.2 99.0 4.3 16.7 22.2 45 45 A K - 0 0 141 -2,-1.0 75,-0.1 -18,-0.3 2,-0.1 -0.502 19.7-114.4 -92.5 155.3 4.4 19.8 24.3 46 46 A S - 0 0 16 2,-0.2 76,-0.2 -2,-0.2 77,-0.1 -0.396 24.6-125.1 -75.1 157.9 5.5 23.4 23.7 47 47 A F S S+ 0 0 118 74,-2.3 2,-0.2 -2,-0.1 75,-0.2 0.716 94.2 40.0 -75.9 -20.5 8.4 24.7 25.7 48 48 A I S S- 0 0 76 74,-0.4 -2,-0.2 73,-0.3 2,-0.2 -0.635 73.8-135.2-121.9 177.8 6.2 27.5 26.9 49 49 A T + 0 0 123 -2,-0.2 -2,-0.1 1,-0.1 -1,-0.0 -0.507 58.6 97.0-120.9-170.8 2.6 28.2 28.0 50 50 A G + 0 0 51 1,-0.3 2,-0.2 -2,-0.2 -1,-0.1 0.642 61.5 126.9 98.7 19.4 -0.0 30.8 27.3 51 51 A F - 0 0 23 -3,-0.1 -1,-0.3 -31,-0.1 -31,-0.2 -0.471 58.4-123.0-103.4 175.3 -2.0 28.8 24.6 52 52 A K E -E 19 0B 121 -33,-2.2 -33,-1.9 -2,-0.2 2,-0.4 -0.970 28.3-138.2-116.6 127.6 -5.6 27.8 24.1 53 53 A P E -E 18 0B 97 0, 0.0 2,-0.4 0, 0.0 -35,-0.2 -0.755 14.1-165.2 -94.0 138.9 -6.2 24.1 23.7 54 54 A V E -E 17 0B 16 -37,-2.8 -37,-2.0 -2,-0.4 2,-0.6 -0.965 4.7-157.3-118.7 134.9 -8.6 22.7 21.1 55 55 A K E -E 16 0B 155 -2,-0.4 2,-0.8 -39,-0.2 -39,-0.2 -0.929 6.3-172.1-118.3 110.0 -9.8 19.1 21.3 56 56 A I E -E 15 0B 4 -41,-2.9 -41,-3.1 -2,-0.6 2,-0.8 -0.881 3.6-175.4-101.8 107.5 -11.1 17.5 18.2 57 57 A S E -E 14 0B 80 -2,-0.8 -43,-0.3 -43,-0.2 -44,-0.1 -0.872 17.9-146.8-105.9 101.4 -12.6 14.1 18.9 58 58 A L - 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