==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=21-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER ISOMERASE 18-FEB-05 1YWK . COMPND 2 MOLECULE: 4-DEOXY-L-THREO-5-HEXOSULOSE-URONATE KETOL- . SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS; . AUTHOR A.A.FEDOROV,E.V.FEDOROV,S.C.ALMO,S.K.BURLEY,NEW YORK SGX . 1523 12 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 62662.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 1066 70.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 39 2.6 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 531 34.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 6 0.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 6 0.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 4 0.3 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 . 216 14.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 128 8.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 56 3.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 18 1.2 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 3 0 0 0 6 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 3 3 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 . 6 12 12 6 30 21 9 0 0 0 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 6 6 0 0 12 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 1 998 A L 0 0 151 0, 0.0 37,-1.2 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 167.6 -15.8 -10.0 -31.1 2 999 A Q E -a 38 0A 41 35,-0.2 2,-0.3 61,-0.0 37,-0.2 -0.920 360.0-177.1-128.9 155.8 -19.1 -8.2 -31.6 3 1000 A N E -a 39 0A 106 35,-1.6 37,-3.6 -2,-0.3 2,-0.4 -0.942 15.1-169.8-162.1 135.4 -21.8 -7.5 -28.9 4 1001 A M E -a 40 0A 40 -2,-0.3 2,-0.5 35,-0.2 37,-0.3 -0.895 8.2-162.9-132.9 106.2 -25.3 -6.0 -28.6 5 1002 A E E -a 41 0A 101 35,-2.3 37,-1.9 -2,-0.4 2,-0.3 -0.730 15.1-145.3 -87.0 125.2 -26.9 -5.3 -25.2 6 1003 A T E -a 42 0A 69 -2,-0.5 2,-0.4 35,-0.2 37,-0.2 -0.636 11.9-161.8 -90.4 149.4 -30.7 -4.8 -25.3 7 1004 A R E -a 43 0A 20 35,-3.0 37,-2.3 -2,-0.3 38,-0.3 -0.973 10.4-139.0-135.5 122.5 -32.4 -2.3 -23.0 8 1005 A Y - 0 0 158 -2,-0.4 2,-0.2 35,-0.2 37,-0.1 -0.332 22.9-124.3 -72.1 157.7 -36.0 -2.1 -22.1 9 1006 A T - 0 0 56 35,-0.1 2,-0.2 -2,-0.0 -1,-0.1 -0.575 24.9-160.5 -98.4 166.2 -37.7 1.3 -21.9 10 1007 A H - 0 0 39 -2,-0.2 -1,-0.0 16,-0.0 0, 0.0 -0.674 18.0-104.8-133.4-172.9 -39.6 2.6 -18.9 11 1008 A S > - 0 0 40 -2,-0.2 4,-1.9 1,-0.1 3,-0.5 -0.855 36.5-105.9-116.9 155.4 -42.2 5.1 -18.0 12 1009 A P H > S+ 0 0 29 0, 0.0 4,-0.5 0, 0.0 204,-0.1 0.768 124.1 51.6 -50.6 -24.1 -41.6 8.5 -16.2 13 1010 A A H 4 S+ 0 0 48 2,-0.2 3,-0.5 1,-0.2 4,-0.4 0.882 102.4 55.0 -81.3 -40.7 -43.1 6.7 -13.2 14 1011 A D H 4 S+ 0 0 95 -3,-0.5 3,-0.4 1,-0.2 -1,-0.2 0.897 115.4 41.9 -56.6 -38.9 -41.0 3.6 -13.2 15 1012 A I H >< S+ 0 0 6 -4,-1.9 3,-2.6 1,-0.2 -1,-0.2 0.608 84.5 103.3 -83.3 -15.3 -37.9 6.0 -13.1 16 1013 A R T 3< S+ 0 0 75 -4,-0.5 516,-0.3 -3,-0.5 -1,-0.2 0.759 95.4 24.2 -41.5 -41.7 -39.4 8.4 -10.5 17 1014 A H T 3 S+ 0 0 81 -3,-0.4 -1,-0.3 -4,-0.4 -2,-0.1 0.144 89.6 143.9-114.9 20.8 -37.3 7.0 -7.6 18 1015 A Y < - 0 0 31 -3,-2.6 2,-0.1 1,-0.1 -3,-0.1 -0.205 47.6-124.7 -56.7 144.6 -34.5 5.5 -9.6 19 1016 A S > - 0 0 6 1,-0.1 4,-2.9 510,-0.1 5,-0.2 -0.465 27.9-102.9 -87.5 165.7 -31.0 5.8 -8.0 20 1017 A T H > S+ 0 0 20 508,-0.3 4,-2.2 2,-0.2 5,-0.2 0.894 126.8 51.1 -53.8 -37.3 -28.1 7.4 -9.8 21 1018 A E H > S+ 0 0 133 2,-0.2 4,-3.0 1,-0.2 5,-0.2 0.993 108.7 47.9 -63.6 -60.9 -27.0 3.9 -10.4 22 1019 A Q H > S+ 0 0 61 1,-0.2 4,-2.3 2,-0.2 5,-0.3 0.900 110.2 53.3 -45.9 -51.5 -30.2 2.7 -11.8 23 1020 A L H X S+ 0 0 3 -4,-2.9 4,-3.2 1,-0.2 5,-0.5 0.950 111.6 45.2 -49.5 -54.3 -30.4 5.7 -14.1 24 1021 A R H X S+ 0 0 60 -4,-2.2 4,-2.1 1,-0.2 -1,-0.2 0.922 110.3 55.5 -57.0 -45.6 -27.0 5.0 -15.4 25 1022 A D H < S+ 0 0 80 -4,-3.0 -1,-0.2 1,-0.2 -2,-0.2 0.837 118.5 32.2 -57.7 -35.7 -27.8 1.3 -15.8 26 1023 A E H < S+ 0 0 51 -4,-2.3 -2,-0.2 -3,-0.4 -1,-0.2 0.868 132.1 23.4 -93.5 -38.5 -30.8 2.0 -18.0 27 1024 A F H < S+ 0 0 5 -4,-3.2 205,-2.4 -5,-0.3 2,-0.5 0.529 102.9 80.5-109.8 -3.6 -30.0 5.1 -19.9 28 1025 A L E < -G 231 0B 2 -4,-2.1 2,-0.7 -5,-0.5 203,-0.2 -0.882 51.8-162.7-110.5 132.7 -26.2 5.4 -20.1 29 1026 A V E -G 230 0B 11 201,-3.7 201,-2.5 -2,-0.5 3,-0.1 -0.931 9.0-173.9-109.5 106.1 -24.0 3.5 -22.5 30 1027 A E S S+ 0 0 109 -2,-0.7 2,-0.5 199,-0.2 -1,-0.1 0.811 71.0 41.7 -71.5 -35.3 -20.4 3.7 -21.0 31 1028 A K + 0 0 151 1,-0.1 -1,-0.2 198,-0.1 3,-0.2 -0.954 55.8 149.5-120.0 116.2 -18.5 2.0 -23.8 32 1029 A V S S+ 0 0 2 196,-0.9 20,-0.9 -2,-0.5 2,-0.6 0.746 73.0 39.4-108.7 -40.5 -19.4 2.9 -27.4 33 1030 A F + 0 0 16 195,-0.4 -1,-0.2 18,-0.1 20,-0.1 -0.784 62.4 167.6-116.7 86.9 -16.1 2.6 -29.2 34 1031 A I > - 0 0 77 -2,-0.6 3,-1.5 18,-0.4 20,-0.4 -0.887 42.0-116.5-101.4 106.3 -14.2 -0.4 -27.9 35 1032 A P T 3 S+ 0 0 87 0, 0.0 3,-0.1 0, 0.0 21,-0.1 -0.045 92.5 19.9 -44.5 129.3 -11.3 -1.0 -30.5 36 1033 A G T 3 S+ 0 0 27 18,-2.8 2,-0.3 1,-0.2 20,-0.1 0.307 118.9 64.4 91.5 -6.4 -11.2 -4.2 -32.5 37 1034 A A S < S- 0 0 14 -3,-1.5 17,-1.5 17,-0.4 2,-0.5 -0.904 80.2-113.0-142.3 167.7 -14.9 -4.9 -31.9 38 1035 A I E -aB 2 53A 3 -37,-1.2 -35,-1.6 -2,-0.3 2,-0.6 -0.917 26.6-163.0-106.0 127.0 -18.4 -3.6 -32.6 39 1036 A S E +aB 3 52A 24 13,-3.0 13,-2.1 -2,-0.5 2,-0.3 -0.939 19.1 170.9-112.5 111.0 -20.2 -2.4 -29.4 40 1037 A L E -aB 4 51A 4 -37,-3.6 -35,-2.3 -2,-0.6 2,-0.4 -0.863 22.0-160.3-124.1 156.2 -23.9 -2.1 -30.0 41 1038 A T E -aB 5 50A 5 9,-3.1 9,-2.4 -2,-0.3 2,-0.7 -0.998 10.4-149.4-136.9 129.4 -27.0 -1.5 -27.8 42 1039 A Y E -aB 6 49A 25 -37,-1.9 -35,-3.0 -2,-0.4 2,-0.5 -0.888 14.9-162.8-101.0 111.6 -30.6 -2.4 -28.8 43 1040 A T E > -aB 7 48A 3 5,-2.8 5,-0.5 -2,-0.7 4,-0.4 -0.826 20.1-145.5-100.2 131.7 -33.2 -0.0 -27.3 44 1041 A H T 5S+ 0 0 59 -37,-2.3 2,-1.4 -2,-0.5 -36,-0.1 0.561 77.1 105.4 -68.4 -6.7 -36.8 -1.0 -27.2 45 1042 A N T > 5S- 0 0 16 -38,-0.3 3,-1.3 1,-0.3 -2,-0.2 -0.655 118.8 -31.9 -73.8 97.6 -37.5 2.6 -27.8 46 1043 A D T 3 5S- 0 0 65 -2,-1.4 -1,-0.3 1,-0.2 -2,-0.2 0.631 101.9 -87.2 62.3 13.8 -38.5 2.2 -31.4 47 1044 A R T 3 5S+ 0 0 127 -4,-0.4 2,-0.3 1,-0.2 -1,-0.2 0.774 71.8 166.2 60.4 30.2 -36.1 -0.7 -31.8 48 1045 A M E < < -B 43 0A 0 -3,-1.3 -5,-2.8 -5,-0.5 2,-0.5 -0.574 22.2-158.2 -77.4 138.1 -33.1 1.5 -32.7 49 1046 A I E +BC 42 131A 0 82,-2.7 82,-3.4 -2,-0.3 2,-0.3 -0.987 24.2 162.2-118.9 120.1 -29.8 -0.4 -32.5 50 1047 A F E +BC 41 130A 0 -9,-2.4 -9,-3.1 -2,-0.5 2,-0.3 -0.855 9.5 104.7-132.0 169.6 -26.8 2.0 -32.1 51 1048 A G E -BC 40 129A 1 78,-1.6 78,-2.4 -2,-0.3 2,-0.5 -0.965 59.8 -59.7 151.4-166.5 -23.2 1.8 -31.0 52 1049 A G E -BC 39 128A 0 -13,-2.1 -13,-3.0 -20,-0.9 2,-0.7 -0.956 22.0-168.4-126.1 128.7 -19.7 1.9 -32.3 53 1050 A V E +BC 38 127A 0 74,-2.7 74,-1.9 -2,-0.5 -15,-0.2 -0.940 17.5 176.3-108.4 105.4 -17.9 -0.4 -34.7 54 1051 A T - 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