==== 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 HYDROLASE 04-DEC-07 3BJK . COMPND 2 MOLECULE: ACYL-COA THIOESTER HYDROLASE HI0827; . SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE RD KW20; . AUTHOR M.A.WILLIS,O.HERZBERG,STRUCTURE 2 FUNCTION PROJECT (S2F) . 840 8 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 35305.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 607 72.3 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 . 316 37.6 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 . 11 1.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 6 0.7 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 . 33 3.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 58 6.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 164 19.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 6 0.7 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 2 1 3 0 0 0 0 0 0 0 6 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 . 14 0 0 0 3 6 0 3 3 6 6 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 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 1 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 13 A S 0 0 65 0, 0.0 2,-0.5 0, 0.0 4,-0.1 0.000 360.0 360.0 360.0 100.3 2.1 11.4 55.6 2 14 A K + 0 0 95 68,-0.1 2,-0.2 2,-0.1 84,-0.2 -0.800 360.0 1.4-109.7 129.7 -0.4 8.7 56.8 3 15 A G S S- 0 0 28 -2,-0.5 2,-0.3 67,-0.1 69,-0.2 -0.636 101.8 -31.0 101.0-162.8 0.0 5.0 56.7 4 16 A V E -A 71 0A 71 67,-2.3 67,-2.7 -2,-0.2 2,-0.3 -0.654 65.0-102.2 -94.3 147.8 3.0 3.0 55.7 5 17 A L E +A 70 0A 41 -2,-0.3 65,-0.2 65,-0.2 3,-0.1 -0.504 41.9 168.5 -70.3 121.5 5.5 4.0 53.0 6 18 A L E + 0 0 0 63,-3.5 2,-0.3 1,-0.4 64,-0.2 0.820 61.4 4.9 -99.9 -44.2 4.8 2.1 49.8 7 19 A L E -A 69 0A 0 62,-1.6 62,-2.5 2,-0.0 -1,-0.4 -0.978 52.9-173.1-149.5 148.5 7.0 3.8 47.2 8 20 A R E +AB 68 433A 21 425,-1.7 425,-2.0 -2,-0.3 2,-0.3 -0.965 23.0 137.5-148.8 128.6 9.6 6.6 47.0 9 21 A T E -A 67 0A 14 58,-2.5 58,-3.4 -2,-0.3 2,-0.4 -0.932 47.1 -96.7-154.9 178.8 11.1 8.1 43.9 10 22 A L E -A 66 0A 14 -2,-0.3 2,-0.4 56,-0.2 56,-0.2 -0.874 36.4-118.5-108.0 134.9 12.2 11.4 42.2 11 23 A A - 0 0 1 54,-2.5 53,-3.0 -2,-0.4 292,-0.1 -0.651 37.6-160.7 -73.7 126.6 10.0 13.2 39.7 12 24 A M > - 0 0 23 -2,-0.4 3,-1.7 51,-0.2 290,-0.1 -0.779 29.0-115.7-119.1 153.1 11.8 13.4 36.3 13 25 A P G > S+ 0 0 23 0, 0.0 3,-1.8 0, 0.0 289,-0.1 0.794 109.5 65.2 -52.0 -38.3 11.4 15.5 33.2 14 26 A S G 3 S+ 0 0 36 287,-0.4 566,-0.4 285,-0.4 285,-0.1 0.716 99.3 54.9 -65.5 -18.9 10.4 12.6 31.0 15 27 A D G < S+ 0 0 51 -3,-1.7 8,-2.8 564,-0.1 -1,-0.3 0.151 85.5 116.1-100.3 22.9 7.2 12.2 33.0 16 28 A T B < -E 22 0B 15 -3,-1.8 564,-0.4 6,-0.3 6,-0.3 -0.430 54.7-137.9 -86.5 157.9 6.0 15.8 32.5 17 29 A N > - 0 0 33 4,-2.9 3,-1.9 -2,-0.1 -1,-0.1 -0.432 43.9 -80.8 -99.2-176.5 2.8 17.0 30.8 18 30 A A T 3 S+ 0 0 57 1,-0.3 611,-0.1 -2,-0.2 -2,-0.0 0.825 129.9 56.6 -61.2 -30.2 2.5 20.0 28.4 19 31 A N T 3 S- 0 0 78 2,-0.1 -1,-0.3 1,-0.1 3,-0.1 0.606 117.5-112.7 -75.5 -11.3 2.3 22.4 31.4 20 32 A G S < S+ 0 0 41 -3,-1.9 43,-0.5 1,-0.4 -2,-0.1 0.361 81.8 114.3 94.4 -4.0 5.6 21.2 32.7 21 33 A D S S- 0 0 54 1,-0.1 -4,-2.9 41,-0.1 -1,-0.4 -0.374 83.9 -74.1 -87.8 173.0 4.2 19.5 35.8 22 34 A I B -E 16 0B 7 39,-2.7 39,-0.3 -6,-0.3 -6,-0.3 -0.526 56.8-106.4 -76.2 135.3 4.2 15.8 36.3 23 35 A F >> - 0 0 37 -8,-2.8 4,-1.3 -2,-0.3 3,-0.8 -0.309 20.0-129.5 -63.5 135.1 1.7 14.0 34.1 24 36 A G H 3> S+ 0 0 20 1,-0.2 4,-2.3 2,-0.2 5,-0.2 0.815 105.5 62.0 -53.8 -38.2 -1.4 12.7 36.0 25 37 A G H 3> S+ 0 0 0 2,-0.2 4,-2.4 1,-0.2 -1,-0.2 0.856 100.9 51.3 -57.7 -39.6 -1.0 9.2 34.4 26 38 A W H <> S+ 0 0 36 -3,-0.8 4,-2.6 -11,-0.2 -1,-0.2 0.929 110.1 49.5 -64.5 -44.9 2.4 8.7 36.0 27 39 A I H X S+ 0 0 6 -4,-1.3 4,-2.5 2,-0.2 -2,-0.2 0.914 111.2 49.3 -64.8 -44.6 1.0 9.6 39.5 28 40 A M H X S+ 0 0 0 -4,-2.3 4,-2.2 1,-0.2 -1,-0.2 0.904 111.1 51.2 -57.4 -42.4 -1.9 7.2 39.0 29 41 A S H X S+ 0 0 15 -4,-2.4 4,-2.3 139,-0.2 -2,-0.2 0.893 108.5 49.6 -65.2 -44.4 0.6 4.5 38.0 30 42 A Q H X S+ 0 0 18 -4,-2.6 4,-2.7 2,-0.2 5,-0.2 0.955 112.3 49.9 -57.0 -49.1 2.8 5.1 41.1 31 43 A M H X S+ 0 0 0 -4,-2.5 4,-2.5 1,-0.2 -2,-0.2 0.884 111.4 47.0 -55.1 -42.5 -0.3 4.8 43.3 32 44 A A H X S+ 0 0 7 -4,-2.2 4,-2.4 1,-0.2 -1,-0.2 0.908 113.8 47.6 -71.6 -43.1 -1.4 1.6 41.7 33 45 A M H X S+ 0 0 16 -4,-2.3 4,-1.7 2,-0.2 -2,-0.2 0.891 116.3 43.4 -61.3 -44.4 2.0 0.0 41.9 34 46 A G H X S+ 0 0 0 -4,-2.7 4,-1.8 2,-0.2 -2,-0.2 0.939 114.3 50.3 -68.4 -46.5 2.5 1.1 45.6 35 47 A G H X S+ 0 0 0 -4,-2.5 4,-2.3 -5,-0.2 -2,-0.2 0.905 109.8 51.2 -57.7 -44.7 -1.1 0.1 46.5 36 48 A A H X S+ 0 0 8 -4,-2.4 4,-2.9 2,-0.2 -1,-0.2 0.848 103.7 57.7 -65.0 -34.3 -0.5 -3.3 44.9 37 49 A I H X S+ 0 0 0 -4,-1.7 4,-2.4 2,-0.2 -1,-0.2 0.968 110.6 43.4 -57.9 -47.3 2.7 -4.0 46.8 38 50 A L H X S+ 0 0 11 -4,-1.8 4,-2.5 1,-0.2 5,-0.2 0.894 112.3 52.6 -68.0 -38.4 0.9 -3.6 50.1 39 51 A A H X S+ 0 0 0 -4,-2.3 4,-2.7 1,-0.2 -1,-0.2 0.931 110.4 48.5 -62.0 -43.3 -2.0 -5.6 48.9 40 52 A K H X>S+ 0 0 31 -4,-2.9 5,-1.8 2,-0.2 4,-0.7 0.858 112.0 49.7 -62.0 -39.4 0.5 -8.4 47.9 41 53 A E H ><5S+ 0 0 24 -4,-2.4 3,-0.6 -5,-0.2 88,-0.2 0.934 113.7 44.2 -59.4 -52.5 2.1 -8.2 51.3 42 54 A I H 3<5S+ 0 0 0 -4,-2.5 88,-0.3 1,-0.2 -2,-0.2 0.888 117.0 46.7 -60.0 -44.2 -1.2 -8.4 53.1 43 55 A A H 3<5S- 0 0 0 -4,-2.7 -1,-0.2 2,-0.2 -2,-0.2 0.546 103.0-130.6 -78.8 -8.4 -2.4 -11.3 50.8 44 56 A H T <<5S+ 0 0 53 -4,-0.7 2,-0.3 -3,-0.6 -3,-0.2 0.824 78.5 3.7 55.8 38.4 0.9 -13.2 51.1 45 57 A G S - 0 0 48 -2,-0.4 3,-2.1 -41,-0.2 -51,-0.2 -0.809 27.1 -92.3-105.6 147.5 7.1 19.4 40.1 63 75 A V T 3 S+ 0 0 43 -43,-0.5 -51,-0.2 -2,-0.3 3,-0.1 -0.303 114.6 26.5 -51.3 131.5 10.3 18.0 38.4 64 76 A G T 3 S+ 0 0 9 -53,-3.0 28,-0.4 1,-0.3 29,-0.3 0.263 88.7 131.7 92.5 -12.2 12.9 17.2 41.1 65 77 A D < - 0 0 0 -3,-2.1 -54,-2.5 26,-0.1 2,-0.5 -0.455 63.6-118.7 -63.5 143.2 10.3 16.7 43.9 66 78 A V E -AE 10 90A 0 24,-2.6 24,-1.9 -56,-0.2 2,-0.5 -0.779 32.7-152.3 -80.1 128.8 10.7 13.6 46.0 67 79 A V E -AE 9 89A 0 -58,-3.4 -58,-2.5 -2,-0.5 2,-0.3 -0.954 16.3-179.6-112.6 123.6 7.5 11.6 45.5 68 80 A C E -AE 8 88A 8 20,-2.8 20,-2.9 -2,-0.5 2,-0.5 -0.936 14.9-155.4-120.6 136.6 6.3 9.2 48.2 69 81 A C E -AE 7 87A 1 -62,-2.5 -63,-3.5 -2,-0.3 -62,-1.6 -0.984 13.8-167.8-112.4 131.0 3.2 7.0 48.2 70 82 A Y E -AE 5 86A 39 16,-2.7 16,-2.2 -2,-0.5 2,-0.4 -0.898 7.2-147.5-114.8 144.9 1.7 6.0 51.6 71 83 A G E -AE 4 85A 0 -67,-2.7 -67,-2.3 -2,-0.3 2,-0.5 -0.936 14.6-176.3-124.7 131.3 -0.9 3.3 52.2 72 84 A Q E - E 0 84A 18 12,-2.3 12,-3.2 -2,-0.4 2,-0.2 -0.987 25.0-138.9-120.1 112.4 -3.7 3.1 54.8 73 85 A C E + E 0 83A 0 -2,-0.5 10,-0.3 10,-0.3 3,-0.1 -0.560 22.1 179.8 -71.6 137.1 -5.6 -0.2 54.6 74 86 A L E + 0 0 68 8,-3.0 2,-0.3 1,-0.4 9,-0.2 0.625 61.8 3.8-109.4 -20.0 -9.4 0.5 55.1 75 87 A K E - 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