==== 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 STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-JAN-05 1YLL . COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN; . SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; . AUTHOR MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG) . 768 6 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 33300.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 577 75.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 8 1.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 405 52.7 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 5 0.7 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 . 9 1.2 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 . 3 0.4 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 . 87 11.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 44 5.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 6 0.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 0.1 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 . 4 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 . 5 12 4 15 9 5 7 4 0 0 0 0 0 0 0 1 3 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 0 0 0 4 0 4 0 0 0 0 0 0 0 2 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 2 A S 0 0 123 0, 0.0 2,-0.3 0, 0.0 165,-0.2 0.000 360.0 360.0 360.0 133.0 32.3 78.7 49.1 2 3 A E E -A 165 0A 66 163,-2.4 163,-2.6 2,-0.0 2,-0.4 -0.996 360.0-168.9-150.2 150.4 34.4 75.8 47.9 3 4 A L E +A 164 0A 26 -2,-0.3 2,-0.3 161,-0.2 161,-0.2 -0.968 15.7 162.9-145.6 125.8 35.0 72.1 48.7 4 5 A R E -A 163 0A 53 159,-2.6 159,-3.0 -2,-0.4 2,-0.8 -0.990 34.5-131.5-142.5 148.6 37.7 69.9 47.5 5 6 A I E -A 162 0A 34 -2,-0.3 2,-0.4 157,-0.2 157,-0.2 -0.900 26.6-149.1-102.8 112.1 39.3 66.6 48.4 6 7 A L E -A 161 0A 43 155,-3.1 155,-2.7 -2,-0.8 2,-0.4 -0.676 11.7-139.8 -81.8 134.0 43.0 67.0 48.4 7 8 A R > - 0 0 86 -2,-0.4 3,-2.6 153,-0.2 4,-0.3 -0.810 10.1-138.0-100.4 135.0 44.9 63.8 47.5 8 9 A A G > S+ 0 0 27 -2,-0.4 3,-1.8 1,-0.3 -1,-0.1 0.838 103.7 67.0 -56.1 -33.7 48.1 62.7 49.2 9 10 A V G 3 S+ 0 0 132 1,-0.3 -1,-0.3 -3,-0.0 150,-0.0 0.726 101.7 50.4 -61.5 -17.5 49.5 61.8 45.9 10 11 A D G < S+ 0 0 112 -3,-2.6 -1,-0.3 2,-0.1 -2,-0.2 0.464 79.3 118.9 -99.9 -2.9 49.5 65.6 45.1 11 12 A Y < - 0 0 25 -3,-1.8 11,-0.1 -4,-0.3 2,-0.1 -0.471 57.6-137.1 -71.6 131.0 51.3 66.8 48.3 12 13 A P - 0 0 75 0, 0.0 9,-1.2 0, 0.0 2,-0.4 -0.426 12.0-134.7 -81.4 160.0 54.5 68.7 47.6 13 14 A R E -O 20 0B 185 7,-0.2 7,-0.2 -2,-0.1 5,-0.0 -0.929 17.4-170.0-118.6 141.4 57.6 68.1 49.7 14 15 A X E O 19 0B 51 5,-2.7 5,-2.5 -2,-0.4 0, 0.0 -0.998 360.0 360.0-132.1 138.7 59.8 70.9 51.1 15 16 A P 0 0 141 0, 0.0 3,-0.1 0, 0.0 -2,-0.0 -0.002 360.0 360.0 26.9 360.0 63.3 70.4 52.8 16 ! 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 17 22 A G 0 0 92 0, 0.0 2,-0.3 0, 0.0 25,-0.1 0.000 360.0 360.0 360.0 158.2 63.8 66.7 57.9 18 23 A S E - P 0 41B 24 23,-0.9 23,-2.5 -3,-0.1 2,-0.4 -0.913 360.0-152.6-133.1 159.4 61.1 67.2 55.3 19 24 A T E -OP 14 40B 34 -5,-2.5 -5,-2.7 -2,-0.3 2,-0.6 -0.995 6.8-151.2-136.8 143.1 57.5 68.3 55.3 20 25 A E E -OP 13 39B 43 19,-3.1 19,-2.4 -2,-0.4 2,-0.5 -0.953 21.9-142.3-111.0 113.9 54.6 67.6 53.0 21 26 A E E - P 0 38B 26 -9,-1.2 17,-0.3 -2,-0.6 3,-0.1 -0.664 18.9-177.2 -83.7 126.4 52.2 70.5 52.9 22 27 A I E - 0 0 13 15,-2.3 2,-0.3 -2,-0.5 16,-0.2 0.908 63.6 -35.5 -83.7 -47.2 48.5 69.5 52.7 23 28 A A E - P 0 37B 13 14,-1.6 14,-2.6 -17,-0.0 -1,-0.3 -0.988 46.5-164.2-168.7 163.7 47.1 73.0 52.5 24 29 A R E - P 0 36B 50 -2,-0.3 12,-0.2 12,-0.2 3,-0.1 -0.945 34.8-118.9-149.4 159.0 47.3 76.6 53.6 25 30 A D S S- 0 0 61 10,-1.6 2,-0.3 1,-0.3 11,-0.1 0.895 76.4 -83.7 -69.1 -33.6 44.9 79.5 53.5 26 31 A G S S+ 0 0 30 9,-0.4 -1,-0.3 -3,-0.1 8,-0.3 -0.961 76.4 101.3 156.1-175.0 47.3 81.3 51.3 27 32 A G - 0 0 44 -2,-0.3 2,-0.3 6,-0.1 6,-0.2 -0.096 64.0 -70.7 91.1 165.6 50.4 83.5 51.2 28 33 A D S >> S- 0 0 145 4,-0.2 4,-0.6 3,-0.1 3,-0.5 -0.766 79.3 -9.9-106.3 143.2 54.0 82.8 50.5 29 34 A G G >4 S- 0 0 48 -2,-0.3 3,-0.7 1,-0.2 4,-0.3 0.000 96.1 -60.2 69.4-176.3 56.7 81.0 52.4 30 35 A L G 34 S+ 0 0 85 1,-0.2 -1,-0.2 2,-0.1 6,-0.0 0.341 135.7 52.0 -89.3 13.2 56.6 79.7 56.0 31 36 A D G <4 S+ 0 0 141 -3,-0.5 -1,-0.2 20,-0.0 -2,-0.2 0.410 99.0 61.9-122.4 -9.1 56.1 83.2 57.2 32 37 A G S << S+ 0 0 34 -3,-0.7 -4,-0.2 -4,-0.6 2,-0.2 0.404 77.5 93.8-109.9 6.3 53.1 84.3 55.0 33 38 A F - 0 0 0 -4,-0.3 3,-0.1 -6,-0.2 -6,-0.1 -0.565 56.9-149.4 -97.8 160.8 50.2 82.1 55.8 34 39 A G S S- 0 0 1 1,-0.4 75,-2.6 -8,-0.3 2,-0.3 0.739 90.3 -1.2 -89.0 -38.9 47.3 82.4 58.3 35 40 A W E - Q 0 108B 2 73,-0.2 -10,-1.6 -9,-0.2 -9,-0.4 -0.994 64.1-173.7-150.4 152.1 47.1 78.6 58.7 36 41 A R E -PQ 24 107B 7 71,-2.4 71,-2.5 -2,-0.3 2,-0.4 -0.984 7.3-161.1-147.5 139.1 49.0 75.6 57.3 37 42 A L E +PQ 23 106B 0 -14,-2.6 -15,-2.3 -2,-0.3 -14,-1.6 -0.976 26.7 156.1-121.9 135.9 48.4 71.8 57.7 38 43 A S E -PQ 21 105B 2 67,-2.2 67,-3.0 -2,-0.4 2,-0.5 -0.940 40.4-127.2-154.3 170.1 51.3 69.4 56.9 39 44 A I E -PQ 20 104B 0 -19,-2.4 -19,-3.1 -2,-0.3 2,-0.3 -0.996 32.0-165.7-123.6 122.0 52.8 66.0 57.5 40 45 A A E -PQ 19 103B 11 63,-1.5 63,-2.7 -2,-0.5 2,-0.5 -0.819 16.2-140.9-114.2 153.8 56.4 66.0 58.6 41 46 A D E -PQ 18 102B 56 -23,-2.5 -23,-0.9 -2,-0.3 2,-0.6 -0.961 16.2-170.6-109.0 125.1 59.0 63.3 58.7 42 47 A V E + Q 0 101B 18 59,-2.5 59,-2.4 -2,-0.5 3,-0.0 -0.952 15.5 163.3-118.3 109.9 61.3 63.5 61.8 43 48 A G + 0 0 57 -2,-0.6 2,-0.3 57,-0.2 57,-0.2 0.594 62.3 33.1-103.7 -10.5 64.2 61.1 61.5 44 49 A E S S- 0 0 145 55,-0.1 2,-0.2 57,-0.1 57,-0.1 -0.921 85.0-102.8-139.7 159.3 66.6 62.4 64.2 45 50 A S + 0 0 59 -2,-0.3 2,-0.3 51,-0.1 50,-0.2 -0.592 67.2 113.0 -77.6 151.1 66.3 64.1 67.5 46 51 A G E -U 94 0C 23 48,-2.0 48,-3.3 -2,-0.2 2,-0.1 -0.971 62.7 -49.4 166.0-178.4 66.9 67.8 67.2 47 52 A G E -U 93 0C 61 -2,-0.3 2,-0.4 46,-0.3 46,-0.2 -0.433 43.1-126.9 -83.2 156.5 65.4 71.3 67.4 48 53 A F E -U 92 0C 40 44,-2.2 44,-0.5 -2,-0.1 -1,-0.0 -0.836 29.4-115.3 -98.1 137.5 62.3 72.5 65.7 49 54 A S - 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