==== 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 TRANSFERASE/TRANSFERASE INHIBITOR 17-AUG-05 2AQ9 . COMPND 2 MOLECULE: ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAM . SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; . AUTHOR A.H.WILLIAMS,R.M.IMMORMINO,D.T.GEWIRTH,C.R.RAETZ . 274 2 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 12310.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 216 78.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 87 31.8 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 9 3.3 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 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 . 0 0.0 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 . 30 10.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 29 10.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 36 13.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 5 1.8 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 1 0 0 1 0 0 1 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 4 20 2 2 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 . 0 0 2 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 ANTIPARALLEL BRIDGES PER LADDER . 1 0 0 0 0 0 0 0 2 1 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 M 0 0 89 0, 0.0 19,-1.9 0, 0.0 2,-0.6 0.000 360.0 360.0 360.0 160.8 62.9 88.0 27.1 2 2 A I B -a 20 0A 82 17,-0.2 19,-0.1 12,-0.1 17,-0.1 -0.861 360.0-121.9-101.7 118.0 59.9 90.2 26.4 3 3 A D > - 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0 0 84 -4,-2.1 3,-1.9 1,-0.1 4,-0.3 -0.887 66.2-167.2-116.3 98.4 28.6 54.3 38.1 244 244 A P G > S+ 0 0 89 0, 0.0 3,-2.3 0, 0.0 4,-0.4 0.800 82.4 70.7 -52.9 -36.3 32.1 55.7 37.2 245 245 A E G > S+ 0 0 60 1,-0.3 3,-1.0 2,-0.2 4,-0.2 0.758 90.4 63.9 -55.4 -23.7 31.5 59.0 38.9 246 246 A V G X> S+ 0 0 0 -3,-1.9 3,-1.5 1,-0.2 4,-0.8 0.667 80.7 77.4 -76.2 -16.8 31.6 57.1 42.2 247 247 A K H <> S+ 0 0 117 -3,-2.3 4,-2.8 1,-0.3 5,-0.3 0.743 75.9 79.1 -64.6 -20.2 35.3 56.2 41.6 248 248 A A H <> S+ 0 0 28 -3,-1.0 4,-1.9 -4,-0.4 -1,-0.3 0.864 91.8 51.4 -54.4 -36.2 36.0 59.8 42.7 249 249 A F H <> S+ 0 0 1 -3,-1.5 4,-2.6 2,-0.2 -1,-0.2 0.939 108.6 50.3 -65.7 -47.2 35.5 58.5 46.3 250 250 A T H X S+ 0 0 47 -4,-0.8 4,-1.5 1,-0.2 -2,-0.2 0.918 111.9 45.8 -56.9 -49.5 38.0 55.6 45.7 251 251 A D H X S+ 0 0 77 -4,-2.8 4,-0.6 1,-0.2 -1,-0.2 0.875 112.7 53.1 -63.5 -36.0 40.7 57.9 44.3 252 252 A F H >X S+ 0 0 3 -4,-1.9 4,-1.7 -5,-0.3 3,-1.3 0.915 104.4 53.3 -65.1 -46.1 40.0 60.3 47.2 253 253 A F H 3< S+ 0 0 17 -4,-2.6 -1,-0.2 1,-0.3 -2,-0.2 0.857 102.8 59.2 -58.8 -35.9 40.4 57.7 49.9 254 254 A A H 3< S+ 0 0 91 -4,-1.5 -1,-0.3 1,-0.2 -2,-0.2 0.728 112.1 39.7 -65.6 -22.9 43.8 56.7 48.5 255 255 A R H << S+ 0 0 100 -3,-1.3 -1,-0.2 -4,-0.6 -2,-0.2 0.692 90.3 108.7 -98.7 -23.9 45.1 60.3 49.0 256 256 A S < + 0 0 30 -4,-1.7 4,-0.1 1,-0.1 -93,-0.1 -0.274 24.8 154.8 -60.5 134.7 43.4 61.0 52.4 257 257 A T + 0 0 113 -95,-0.3 -1,-0.1 2,-0.2 -94,-0.1 0.414 68.7 58.7-136.3 -9.2 45.8 61.2 55.4 258 258 A R S S- 0 0 54 1,-0.2 -95,-0.1 -96,-0.2 -2,-0.1 0.410 105.1-116.5-103.1 -1.8 43.8 63.4 57.9 259 259 A G - 0 0 31 -80,-0.1 -79,-2.8 -6,-0.1 2,-0.2 -0.012 40.9 -64.8 82.5 164.2 40.8 61.2 58.1 260 260 A L B -c 180 0D 9 -81,-0.2 -79,-0.2 -4,-0.1 2,-0.1 -0.598 47.4-110.5 -89.3 147.1 37.3 62.3 56.9 261 261 A I 0 0 1 -81,-2.3 -68,-0.1 -2,-0.2 -1,-0.1 -0.450 360.0 360.0 -69.1 149.1 35.2 65.1 58.4 262 262 A R 0 0 157 -70,-0.4 -39,-0.0 -2,-0.1 -83,-0.0 -0.927 360.0 360.0-146.4 360.0 32.2 63.7 60.3 263 !* 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 0.0 264 4 X W 0 0 198 0, 0.0 2,-0.3 0, 0.0 11,-0.2 0.000 360.0 360.0 360.0 140.7 54.8 67.3 65.5 265 5 X M E -D 274 0E 30 9,-1.9 9,-4.0 2,-0.0 2,-0.5 -0.958 360.0-140.7-149.4 125.6 53.7 70.1 63.2 266 6 X L E -D 273 0E 73 -2,-0.3 7,-0.2 7,-0.2 9,-0.0 -0.767 13.0-169.9 -89.5 128.2 52.8 73.7 64.1 267 7 X D E >> +D 272 0E 3 5,-2.7 4,-2.5 -2,-0.5 5,-1.8 -0.856 5.5 180.0-117.8 90.8 49.8 75.1 62.2 268 8 X P T 45S+ 0 0 90 0, 0.0 -1,-0.2 0, 0.0 5,-0.0 0.899 82.0 52.0 -59.1 -43.4 49.7 78.9 62.9 269 9 X I T 45S+ 0 0 69 1,-0.2 -109,-0.1 2,-0.1 -2,-0.0 0.900 117.1 39.2 -61.2 -40.4 46.7 79.5 60.8 270 10 X A T 45S- 0 0 27 2,-0.2 -1,-0.2 -111,-0.1 3,-0.1 0.802 106.4-135.4 -77.2 -28.7 44.8 76.7 62.5 271 11 X G T <5 + 0 0 64 -4,-2.5 2,-0.3 1,-0.3 -2,-0.1 0.847 64.8 104.0 76.3 37.2 46.4 77.8 65.8 272 12 X K E