==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=2-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER ANTIMICROBIAL PROTEIN 15-MAY-07 2JPK . COMPND 2 MOLECULE: BACTERIOCIN LACTOCOCCIN-G SUBUNIT BETA; . SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS; . AUTHOR P.ROGNE,G.FIMLAND,J.NISSEN-MEYER,P.E.KRISTIANSEN . 35 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3994.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 21 60.0 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 . 0 0.0 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 . 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 . 2 5.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 8 22.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 11 31.4 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 1 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 . 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 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 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 K 0 0 204 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 139.7 2.1 -0.0 -1.2 2 2 A K - 0 0 210 1,-0.0 0, 0.0 2,-0.0 0, 0.0 0.961 360.0-175.7 -64.1 -53.5 2.0 -2.7 -3.9 3 3 A W + 0 0 172 1,-0.1 4,-0.5 3,-0.0 3,-0.2 0.933 20.3 155.2 54.2 50.6 5.8 -3.2 -4.0 4 4 A G > + 0 0 31 1,-0.2 4,-0.5 2,-0.1 -1,-0.1 0.173 48.6 86.2 -92.5 18.1 5.5 -5.7 -6.8 5 5 A W H >> S+ 0 0 208 2,-0.2 4,-1.8 3,-0.1 3,-0.9 0.961 92.1 37.6 -80.0 -59.1 9.1 -5.0 -7.9 6 6 A L H 3> S+ 0 0 110 1,-0.3 4,-2.2 2,-0.2 -2,-0.1 0.790 111.9 62.8 -63.6 -27.6 11.1 -7.4 -5.7 7 7 A A H 34 S+ 0 0 51 -4,-0.5 -1,-0.3 1,-0.2 -2,-0.2 0.807 109.4 39.3 -67.3 -29.9 8.3 -9.9 -6.2 8 8 A W H << S+ 0 0 209 -3,-0.9 4,-0.5 -4,-0.5 -2,-0.2 0.739 117.7 48.3 -90.1 -27.1 9.0 -10.0 -9.9 9 9 A V H X S+ 0 0 80 -4,-1.8 4,-2.8 2,-0.2 5,-0.4 0.741 98.2 71.2 -83.5 -25.4 12.8 -9.9 -9.5 10 10 A D H X S+ 0 0 82 -4,-2.2 4,-1.6 1,-0.2 -2,-0.1 0.969 107.0 33.8 -53.4 -60.5 12.8 -12.6 -6.9 11 11 A P H > S+ 0 0 69 0, 0.0 4,-0.6 0, 0.0 -1,-0.2 0.702 118.3 58.9 -69.8 -20.0 12.0 -15.4 -9.4 12 12 A A H >> S+ 0 0 45 -4,-0.5 4,-1.4 2,-0.2 3,-1.2 0.986 107.0 40.3 -73.0 -63.2 13.9 -13.6 -12.1 13 13 A Y H 3X S+ 0 0 118 -4,-2.8 4,-1.2 1,-0.3 3,-0.2 0.882 113.4 56.9 -53.6 -41.2 17.4 -13.4 -10.5 14 14 A E H 3< S+ 0 0 123 -4,-1.6 4,-0.5 -5,-0.4 -1,-0.3 0.790 101.4 59.0 -61.8 -27.7 16.9 -17.0 -9.1 15 15 A F H XX S+ 0 0 128 -3,-1.2 4,-3.3 -4,-0.6 3,-1.3 0.923 103.0 49.3 -67.8 -45.5 16.3 -18.0 -12.8 16 16 A I H 3X S+ 0 0 75 -4,-1.4 4,-1.4 1,-0.3 -1,-0.2 0.773 97.9 71.1 -64.9 -26.0 19.8 -16.8 -13.9 17 17 A K H 3< S+ 0 0 116 -4,-1.2 -1,-0.3 1,-0.2 -2,-0.2 0.777 117.9 19.1 -61.4 -26.3 21.3 -18.7 -11.0 18 18 A G H X4 S+ 0 0 47 -3,-1.3 3,-0.5 -4,-0.5 -2,-0.2 0.752 130.6 44.1-111.4 -41.6 20.5 -21.9 -12.8 19 19 A F H 3< S+ 0 0 172 -4,-3.3 -3,-0.2 1,-0.2 -2,-0.2 0.854 133.7 20.4 -73.7 -36.1 19.9 -20.9 -16.4 20 20 A G T >< S+ 0 0 15 -4,-1.4 3,-1.2 -5,-0.4 -1,-0.2 -0.266 73.0 140.7-129.1 48.1 23.0 -18.7 -16.4 21 21 A K T < S+ 0 0 170 -3,-0.5 -1,-0.1 1,-0.3 3,-0.1 0.703 86.8 33.4 -62.0 -18.5 25.1 -19.9 -13.5 22 22 A G T 3 S+ 0 0 72 1,-0.1 -1,-0.3 -3,-0.1 -5,-0.1 -0.316 104.0 74.4-134.9 53.4 28.1 -19.3 -15.8 23 23 A A <> + 0 0 26 -3,-1.2 4,-0.7 -7,-0.1 5,-0.2 -0.370 34.2 148.5-163.7 73.6 27.3 -16.3 -17.9 24 24 A I T 4 S+ 0 0 74 1,-0.2 7,-0.1 2,-0.2 -3,-0.0 0.737 76.2 62.1 -81.1 -24.5 27.4 -12.9 -16.2 25 25 A K T 4 S+ 0 0 164 1,-0.2 -1,-0.2 2,-0.1 4,-0.1 0.814 99.2 55.6 -70.1 -30.9 28.4 -11.2 -19.4 26 26 A E T 4 S+ 0 0 156 2,-0.1 -1,-0.2 -6,-0.1 -2,-0.2 0.839 131.7 5.0 -70.4 -33.8 25.2 -12.2 -21.1 27 27 A G S < S+ 0 0 48 -4,-0.7 2,-2.2 1,-0.2 3,-0.3 0.691 129.8 42.7-112.5 -82.8 23.1 -10.6 -18.4 28 28 A N + 0 0 65 -5,-0.2 3,-0.5 1,-0.2 -1,-0.2 -0.477 68.0 148.9 -72.8 80.1 24.9 -8.6 -15.7 29 29 A K S > S+ 0 0 139 -2,-2.2 2,-1.0 1,-0.2 3,-0.6 0.983 73.3 30.3 -76.5 -68.0 27.4 -6.8 -18.0 30 30 A D T 3 S+ 0 0 111 -3,-0.3 -1,-0.2 1,-0.2 4,-0.2 -0.279 85.1 117.9 -88.5 49.3 28.0 -3.5 -16.3 31 31 A K T > + 0 0 96 -2,-1.0 3,-1.2 -3,-0.5 -1,-0.2 0.712 61.3 69.1 -86.1 -23.1 27.4 -5.0 -12.8 32 32 A W G X S+ 0 0 151 -3,-0.6 3,-1.6 1,-0.3 -1,-0.2 0.764 87.7 67.3 -65.8 -25.0 30.9 -4.2 -11.7 33 33 A K G 3 S+ 0 0 136 1,-0.3 -1,-0.3 -3,-0.1 -2,-0.2 0.762 97.5 53.0 -66.6 -24.8 29.9 -0.5 -11.7 34 34 A N G < 0 0 144 -3,-1.2 -1,-0.3 -4,-0.2 -2,-0.2 0.249 360.0 360.0 -93.7 11.7 27.6 -1.2 -8.8 35 35 A I < 0 0 177 -3,-1.6 -3,-0.1 0, 0.0 -2,-0.1 0.037 360.0 360.0-141.6 360.0 30.4 -2.8 -6.8