==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=3-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER IMMUNE SYSTEM/PROTEIN BINDING 20-APR-07 2PLP . COMPND 2 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN G; . SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G'; . AUTHOR G.BOUVIGNIES,S.MEIER,S.GRZESIEK,M.BLACKLEDGE . 54 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 3613.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 39 72.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 5 9.3 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 12 22.2 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 1.9 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 . 1 1.9 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 . 6 11.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 1.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 13 24.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 3.7 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 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 0 1 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 1 0 1 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 1 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 7 A T 0 0 112 0, 0.0 2,-0.3 0, 0.0 17,-0.3 0.000 360.0 360.0 360.0 120.6 -8.4 -22.2 -3.6 2 8 A Y E -A 17 0A 32 15,-2.8 15,-2.3 48,-0.0 2,-0.3 -0.837 360.0-140.8-114.1 154.3 -5.7 -19.5 -3.3 3 9 A K E -Ab 16 50A 46 46,-2.2 48,-3.2 -2,-0.3 2,-0.5 -0.890 6.0-152.4-120.6 150.5 -6.3 -16.5 -1.0 4 10 A L E -Ab 15 51A 35 11,-2.7 11,-1.6 -2,-0.3 2,-0.6 -0.979 3.6-159.2-123.6 126.4 -5.6 -12.8 -1.2 5 11 A I E -Ab 14 52A 50 46,-3.2 48,-2.5 -2,-0.5 2,-0.7 -0.913 10.9-159.2-104.0 124.6 -5.0 -10.6 1.8 6 12 A L E -Ab 13 53A 44 7,-2.3 7,-1.5 -2,-0.6 2,-0.8 -0.916 8.7-174.4-109.4 111.8 -5.6 -7.0 0.9 7 13 A N E +A 12 0A 65 46,-3.0 2,-0.2 -2,-0.7 5,-0.2 -0.749 23.8 145.4-110.3 87.3 -3.9 -4.7 3.4 8 14 A G - 0 0 51 3,-1.3 30,-0.1 -2,-0.8 32,-0.0 -0.555 55.2-114.7-113.7 179.3 -4.8 -1.0 2.6 9 15 A K S S+ 0 0 118 -2,-0.2 3,-0.1 1,-0.1 -1,-0.1 0.765 113.2 18.1 -85.3 -27.3 -5.4 2.2 4.4 10 16 A T S S+ 0 0 111 1,-0.2 2,-0.4 0, 0.0 -1,-0.1 0.548 129.0 49.1-116.1 -19.5 -9.1 2.7 3.6 11 17 A L + 0 0 64 2,-0.0 -3,-1.3 0, 0.0 2,-0.3 -0.957 59.4 167.4-131.9 121.3 -9.9 -0.9 2.6 12 18 A K E +A 7 0A 94 -2,-0.4 2,-0.3 -5,-0.2 -5,-0.2 -0.959 23.5 94.2-129.8 147.6 -9.1 -4.1 4.4 13 19 A G E -A 6 0A 47 -7,-1.5 -7,-2.3 -2,-0.3 2,-0.3 -0.988 50.8 -99.3 164.1-171.5 -10.2 -7.7 3.9 14 20 A E E +A 5 0A 92 -2,-0.3 2,-0.3 -9,-0.2 -9,-0.2 -0.971 25.0 175.8-142.5 156.8 -9.7 -11.1 2.4 15 21 A T E -A 4 0A 66 -11,-1.6 -11,-2.7 -2,-0.3 2,-0.3 -0.953 11.4-149.8-152.7 167.7 -11.0 -13.1 -0.6 16 22 A T E -A 3 0A 79 -2,-0.3 2,-0.3 -13,-0.2 -13,-0.2 -0.939 7.2-171.1-142.6 164.7 -10.3 -16.4 -2.3 17 23 A T E -A 2 0A 43 -15,-2.3 -15,-2.8 -2,-0.3 2,-0.6 -0.993 23.9-126.8-154.6 157.2 -10.4 -18.1 -5.8 18 24 A E + 0 0 93 -2,-0.3 2,-0.3 -17,-0.3 -2,-0.0 -0.938 42.8 158.5-109.6 120.8 -10.2 -21.6 -7.4 19 25 A A - 0 0 49 -2,-0.6 3,-0.1 1,-0.1 -2,-0.1 -0.989 47.3-127.3-143.6 151.8 -7.5 -21.6 -10.1 20 26 A V S S+ 0 0 111 -2,-0.3 2,-0.3 1,-0.1 -1,-0.1 0.743 92.5 10.1 -69.7 -24.6 -5.4 -24.2 -11.9 21 27 A D S > S- 0 0 58 1,-0.1 4,-1.9 0, 0.0 3,-0.2 -0.983 76.8-109.5-151.7 157.7 -2.1 -22.5 -11.3 22 28 A A H > S+ 0 0 88 -2,-0.3 4,-2.5 1,-0.2 5,-0.2 0.851 115.6 58.1 -58.4 -36.1 -0.7 -19.6 -9.2 23 29 A A H > S+ 0 0 79 2,-0.2 4,-1.6 1,-0.2 -1,-0.2 0.927 105.6 49.0 -61.4 -45.1 -0.2 -17.5 -12.4 24 30 A T H > S+ 0 0 54 -3,-0.2 4,-1.7 1,-0.2 -1,-0.2 0.933 110.9 50.7 -60.8 -45.9 -3.9 -17.7 -13.3 25 31 A A H X S+ 0 0 15 -4,-1.9 4,-3.0 1,-0.2 5,-0.3 0.933 104.9 56.8 -58.1 -47.3 -4.9 -16.8 -9.8 26 32 A E H X S+ 0 0 59 -4,-2.5 4,-2.9 1,-0.2 -1,-0.2 0.880 105.3 51.7 -52.5 -40.7 -2.7 -13.7 -9.8 27 33 A K H X S+ 0 0 64 -4,-1.6 4,-2.1 2,-0.2 -1,-0.2 0.906 110.7 47.9 -64.5 -40.8 -4.4 -12.4 -12.9 28 34 A V H X S+ 0 0 52 -4,-1.7 4,-2.2 -3,-0.2 -2,-0.2 0.955 114.6 46.0 -64.6 -49.2 -7.8 -12.8 -11.3 29 35 A F H X S+ 0 0 40 -4,-3.0 4,-3.3 1,-0.2 -2,-0.2 0.897 110.3 52.9 -60.8 -42.0 -6.6 -11.1 -8.1 30 36 A K H X S+ 0 0 58 -4,-2.9 4,-3.0 -5,-0.3 5,-0.2 0.933 108.6 50.3 -60.5 -45.6 -4.9 -8.2 -10.0 31 37 A Q H X S+ 0 0 63 -4,-2.1 4,-2.5 2,-0.2 -1,-0.2 0.943 112.9 47.0 -58.1 -47.4 -8.1 -7.5 -11.9 32 38 A Y H X S+ 0 0 60 -4,-2.2 4,-2.0 2,-0.2 -2,-0.2 0.964 112.1 49.3 -59.0 -53.1 -10.0 -7.4 -8.6 33 39 A A H <>S+ 0 0 35 -4,-3.3 5,-2.5 1,-0.2 3,-0.2 0.923 111.2 49.7 -52.6 -48.0 -7.5 -5.2 -6.9 34 40 A N H ><5S+ 0 0 77 -4,-3.0 3,-1.3 1,-0.2 -1,-0.2 0.928 110.4 51.5 -58.4 -45.1 -7.5 -2.8 -9.9 35 41 A D H 3<5S+ 0 0 90 -4,-2.5 -1,-0.2 1,-0.3 -2,-0.2 0.818 111.1 46.1 -62.7 -32.7 -11.3 -2.7 -9.8 36 42 A N T 3<5S- 0 0 80 -4,-2.0 -1,-0.3 -3,-0.2 -2,-0.2 0.184 115.1-111.1 -97.0 17.5 -11.5 -1.9 -6.1 37 43 A G T < 5S+ 0 0 72 -3,-1.3 2,-0.6 1,-0.2 -3,-0.2 0.776 70.1 140.4 60.4 29.7 -8.8 0.8 -6.2 38 44 A V < + 0 0 49 -5,-2.5 2,-0.4 -6,-0.2 -1,-0.2 -0.908 20.1 168.2-108.0 117.4 -6.2 -1.1 -4.3 39 45 A D + 0 0 103 -2,-0.6 2,-0.3 -3,-0.1 14,-0.0 -0.986 23.7 95.7-128.8 137.9 -2.6 -0.8 -5.5 40 46 A G - 0 0 61 -2,-0.4 2,-0.4 -32,-0.0 -32,-0.1 -0.894 67.4 -26.1-179.9-148.6 0.4 -2.0 -3.6 41 47 A E - 0 0 65 13,-2.7 13,-1.6 -2,-0.3 2,-0.4 -0.812 47.9-148.0-100.8 132.9 3.0 -4.7 -3.1 42 48 A W E +C 53 0A 94 -2,-0.4 2,-0.3 11,-0.2 11,-0.2 -0.813 17.0 176.5-102.5 135.7 2.3 -8.4 -3.8 43 49 A T E -C 52 0A 59 9,-2.1 9,-2.6 -2,-0.4 2,-0.4 -0.971 11.6-156.2-133.9 148.7 3.7 -11.3 -1.9 44 50 A Y E -C 51 0A 95 -2,-0.3 2,-0.6 7,-0.2 7,-0.2 -0.987 5.3-166.1-130.6 135.0 3.1 -15.1 -2.3 45 51 A D E >> -C 50 0A 50 5,-2.1 5,-1.7 -2,-0.4 4,-0.8 -0.961 4.9-164.1-120.7 113.5 3.5 -17.9 0.3 46 52 A D T 45S+ 0 0 103 -2,-0.6 -1,-0.1 1,-0.2 5,-0.0 0.775 84.1 60.6 -67.8 -28.6 3.4 -21.3 -1.3 47 53 A A T 45S+ 0 0 113 1,-0.2 -1,-0.2 3,-0.1 -2,-0.0 0.862 122.7 23.2 -68.4 -35.2 2.9 -23.3 1.9 48 54 A T T 45S- 0 0 73 -3,-0.3 -1,-0.2 2,-0.1 -2,-0.2 0.354 100.9-128.3-111.4 3.1 -0.4 -21.5 2.6 49 55 A K T <5 + 0 0 49 -4,-0.8 -46,-2.2 1,-0.2 2,-0.4 0.922 57.4 149.0 48.9 49.6 -1.2 -20.5 -0.9 50 56 A T E < -bC 3 45A 41 -5,-1.7 -5,-2.1 -48,-0.2 2,-0.4 -0.949 35.1-162.7-120.7 132.9 -1.6 -16.9 0.2 51 57 A F E -bC 4 44A 41 -48,-3.2 -46,-3.2 -2,-0.4 2,-0.4 -0.888 12.1-163.5-109.4 140.6 -1.0 -13.7 -1.8 52 58 A T E -bC 5 43A 45 -9,-2.6 -9,-2.1 -2,-0.4 2,-0.4 -0.984 5.7-166.9-129.0 136.1 -0.7 -10.4 0.1 53 59 A V E bC 6 42A 43 -48,-2.5 -46,-3.0 -2,-0.4 -11,-0.2 -0.980 360.0 360.0-125.3 129.0 -0.9 -6.9 -1.3 54 60 A T 0 0 83 -13,-1.6 -13,-2.7 -2,-0.4 -46,-0.2 -0.977 360.0 360.0-131.6 360.0 0.1 -3.7 0.7