==== 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 2JPM . 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) . 3979.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 20 57.1 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 . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 11.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 14 40.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 2.9 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 1 0 0 1 0 1 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 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 0 237 0, 0.0 2,-0.5 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 48.2 2.1 -0.0 -1.2 2 2 A K > - 0 0 177 1,-0.2 4,-0.5 2,-0.1 3,-0.1 -0.541 360.0-179.6 -70.1 116.3 3.5 -3.5 -0.9 3 3 A W H > S+ 0 0 184 -2,-0.5 4,-2.4 2,-0.2 3,-0.3 0.767 72.8 73.7 -86.5 -29.2 5.7 -4.2 -3.9 4 4 A G H 4 S+ 0 0 47 1,-0.3 4,-0.5 2,-0.2 -1,-0.2 0.823 100.0 46.5 -53.6 -33.1 6.7 -7.7 -2.8 5 5 A W H 4 S+ 0 0 181 2,-0.2 3,-0.3 1,-0.2 -1,-0.3 0.819 108.7 54.8 -78.9 -32.9 3.2 -8.8 -3.7 6 6 A L H >X S+ 0 0 95 -4,-0.5 3,-2.0 -3,-0.3 4,-0.6 0.884 102.1 56.8 -67.5 -39.5 3.3 -7.1 -7.1 7 7 A A T 3< S+ 0 0 45 -4,-2.4 3,-0.3 1,-0.3 -1,-0.2 0.759 102.3 57.2 -63.3 -24.5 6.5 -8.8 -8.1 8 8 A W T 34 S+ 0 0 206 -4,-0.5 -1,-0.3 -3,-0.3 -2,-0.2 0.306 91.2 75.9 -88.8 8.6 4.6 -12.1 -7.5 9 9 A V T <4 S- 0 0 97 -3,-2.0 -1,-0.2 1,-0.1 -2,-0.2 0.872 124.4 -26.6 -85.1 -42.1 2.0 -11.0 -10.0 10 10 A D X + 0 0 76 -4,-0.6 4,-1.2 -3,-0.3 5,-0.2 -0.241 65.6 160.5-175.8 73.5 4.0 -11.7 -13.2 11 11 A P H > S+ 0 0 73 0, 0.0 4,-1.9 0, 0.0 5,-0.1 0.821 79.2 59.5 -69.8 -32.4 7.8 -11.5 -12.9 12 12 A A H > S+ 0 0 56 2,-0.2 4,-2.2 1,-0.2 5,-0.2 0.912 100.1 56.4 -63.2 -44.1 8.3 -13.4 -16.1 13 13 A Y H >> S+ 0 0 144 1,-0.2 4,-1.6 2,-0.2 3,-0.8 0.969 113.7 36.8 -51.6 -64.1 6.4 -10.9 -18.2 14 14 A E H 3X S+ 0 0 114 -4,-1.2 4,-2.1 1,-0.3 -1,-0.2 0.829 113.6 60.6 -59.4 -32.6 8.6 -7.9 -17.2 15 15 A F H 3< S+ 0 0 132 -4,-1.9 4,-0.4 1,-0.2 -1,-0.3 0.851 104.2 49.0 -63.9 -35.1 11.6 -10.3 -17.2 16 16 A I H X< S+ 0 0 110 -4,-2.2 3,-0.7 -3,-0.8 -1,-0.2 0.877 114.1 44.3 -72.2 -39.0 11.0 -11.0 -20.9 17 17 A K H 3< S+ 0 0 125 -4,-1.6 6,-0.2 1,-0.2 -2,-0.2 0.765 95.4 78.3 -76.2 -26.3 10.7 -7.3 -21.8 18 18 A G T 3< S- 0 0 48 -4,-2.1 2,-0.3 -5,-0.2 -1,-0.2 0.776 116.8 -20.6 -53.2 -26.9 13.7 -6.4 -19.7 19 19 A F S < S+ 0 0 100 -3,-0.7 -1,-0.2 -4,-0.4 0, 0.0 -0.953 96.3 82.0-175.7 158.8 15.8 -7.8 -22.6 20 20 A G S S+ 0 0 55 -2,-0.3 -1,-0.1 -3,-0.1 -2,-0.1 0.843 92.1 50.5 101.3 49.2 15.7 -10.0 -25.7 21 21 A K S S- 0 0 147 -3,-0.1 -4,-0.1 -4,-0.1 -3,-0.0 0.175 130.0 -38.9-176.9 -35.5 14.2 -7.9 -28.4 22 22 A G S > S+ 0 0 22 3,-0.0 4,-3.1 0, 0.0 5,-0.2 0.229 116.4 80.2-176.7 -33.5 16.1 -4.5 -28.5 23 23 A A T 4 S+ 0 0 48 -6,-0.2 4,-0.3 1,-0.2 -4,-0.1 0.977 112.5 22.9 -54.8 -63.6 16.9 -3.3 -25.0 24 24 A I T > S+ 0 0 91 2,-0.2 4,-2.7 1,-0.2 5,-0.3 0.805 122.1 60.9 -74.6 -30.5 19.9 -5.5 -24.5 25 25 A K H > S+ 0 0 113 1,-0.2 4,-2.0 2,-0.2 5,-0.2 0.951 108.8 40.3 -61.2 -51.5 20.5 -5.9 -28.3 26 26 A E H < S+ 0 0 106 -4,-3.1 -1,-0.2 1,-0.2 -2,-0.2 0.542 116.4 56.2 -75.1 -6.2 20.9 -2.1 -28.8 27 27 A G H 4 S+ 0 0 30 -4,-0.3 4,-0.3 -3,-0.2 -2,-0.2 0.863 112.2 35.0 -91.8 -43.1 23.0 -2.1 -25.6 28 28 A N H >X S+ 0 0 83 -4,-2.7 3,-0.7 1,-0.2 4,-0.7 0.838 122.0 46.9 -79.6 -35.4 25.6 -4.7 -26.4 29 29 A K H 3X S+ 0 0 120 -4,-2.0 4,-1.1 -5,-0.3 5,-0.2 0.736 94.6 76.9 -77.3 -23.6 25.8 -3.8 -30.0 30 30 A D H 3>>S+ 0 0 88 1,-0.2 4,-0.7 -5,-0.2 5,-0.5 0.775 97.4 47.6 -57.0 -26.3 26.0 -0.1 -29.2 31 31 A K H <45S+ 0 0 153 -3,-0.7 -1,-0.2 -4,-0.3 -2,-0.2 0.826 96.1 69.9 -83.8 -35.0 29.6 -0.7 -28.2 32 32 A W H <5S+ 0 0 222 -4,-0.7 -2,-0.2 1,-0.3 -1,-0.2 0.821 107.7 39.9 -51.6 -32.7 30.5 -2.7 -31.4 33 33 A K H <5S- 0 0 140 -4,-1.1 -1,-0.3 2,-0.0 -2,-0.2 0.770 88.9-157.4 -87.5 -29.6 30.2 0.7 -33.2 34 34 A N T <5 0 0 134 -4,-0.7 -3,-0.1 -5,-0.2 -2,-0.1 0.765 360.0 360.0 56.2 25.3 31.9 2.7 -30.5 35 35 A I < 0 0 180 -5,-0.5 -1,-0.2 0, 0.0 -2,-0.0 0.118 360.0 360.0-148.3 360.0 30.1 5.7 -31.9