==== 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 PROTEIN BINDING 15-AUG-07 2JU6 . COMPND 2 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN G; . SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G'; . AUTHOR D.H.ZHOU,J.J.SHEA,A.J.NIEUWKOOP,W.FRANKS,B.J.WYLIE,C.MULLEN, . 56 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 4612.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 41 73.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 6 10.7 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 8 14.3 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 1.8 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 1.8 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 . 12 21.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 1.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 12 21.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 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 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 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 PARALLEL BRIDGES PER LADDER . 0 0 0 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 ANTIPARALLEL BRIDGES PER LADDER . 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 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 X M 0 0 168 0, 0.0 19,-1.5 0, 0.0 2,-0.4 0.000 360.0 360.0 360.0 -20.9 -14.8 8.0 16.0 2 2 X Q E +A 19 0A 129 17,-0.2 2,-0.3 19,-0.1 17,-0.2 -0.978 360.0 175.1-125.0 132.1 -15.8 8.9 12.4 3 3 X Y E -A 18 0A 86 15,-1.7 15,-1.2 -2,-0.4 2,-0.4 -0.829 20.2-134.5-129.0 167.9 -16.3 6.4 9.6 4 4 X K E -Ab 17 51A 65 46,-1.1 48,-2.2 -2,-0.3 2,-0.5 -0.973 7.4-160.2-127.3 140.1 -17.5 6.6 5.9 5 5 X L E +Ab 16 52A 34 11,-1.4 2,-0.7 -2,-0.4 11,-0.7 -0.904 10.0 179.2-123.8 105.1 -20.0 4.4 4.1 6 6 X I E +Ab 15 53A 57 46,-2.5 48,-2.2 -2,-0.5 2,-0.6 -0.885 5.3 177.7-107.6 106.7 -19.8 4.4 0.3 7 7 X L E -Ab 14 54A 40 7,-1.3 2,-0.7 -2,-0.7 7,-0.5 -0.925 11.3-163.0-113.6 114.1 -22.4 2.1 -1.2 8 8 X N E -Ab 13 55A 46 46,-3.6 48,-1.8 -2,-0.6 2,-1.0 -0.843 7.1-162.2 -98.4 114.8 -22.6 2.0 -5.0 9 9 X G - 0 0 18 3,-4.6 2,-5.5 -2,-0.7 4,-0.1 -0.254 48.6-106.9 -87.9 47.7 -25.8 0.5 -6.3 10 10 X K S S+ 0 0 146 -2,-1.0 -1,-0.1 1,-0.3 3,-0.1 -0.160 121.6 26.9 60.6 -56.4 -24.3 -0.2 -9.7 11 11 X T S S+ 0 0 126 -2,-5.5 2,-0.4 1,-0.1 -1,-0.3 0.312 121.5 67.0-111.9 2.8 -26.4 2.7 -10.9 12 12 X L + 0 0 111 2,-0.0 -3,-4.6 0, 0.0 2,-0.4 -0.991 56.5 179.7-131.2 132.4 -26.6 4.5 -7.5 13 13 X K E +A 8 0A 152 -2,-0.4 2,-0.3 -5,-0.3 -5,-0.2 -0.989 8.7 159.5-132.0 139.5 -23.8 6.1 -5.6 14 14 X G E -A 7 0A 26 -7,-0.5 -7,-1.3 -2,-0.4 2,-0.4 -0.967 18.0-160.2-159.9 141.8 -24.0 7.9 -2.2 15 15 X E E +A 6 0A 138 -2,-0.3 2,-0.3 -9,-0.2 -9,-0.2 -0.975 14.9 170.7-127.6 139.7 -21.6 8.9 0.6 16 16 X T E -A 5 0A 68 -11,-0.7 -11,-1.4 -2,-0.4 2,-0.4 -0.953 20.0-140.3-143.2 161.2 -22.4 9.8 4.2 17 17 X T E +A 4 0A 91 -2,-0.3 2,-0.3 -13,-0.2 -13,-0.2 -0.977 18.7 174.7-128.3 139.9 -20.6 10.5 7.5 18 18 X T E -A 3 0A 65 -15,-1.2 -15,-1.7 -2,-0.4 2,-0.7 -0.998 23.8-138.5-144.1 144.6 -21.4 9.4 11.0 19 19 X E E +A 2 0A 141 -2,-0.3 2,-0.3 -17,-0.2 -17,-0.2 -0.894 39.6 148.1-108.2 110.1 -19.7 9.7 14.4 20 20 X A - 0 0 25 -19,-1.5 3,-0.2 -2,-0.7 -2,-0.0 -0.800 46.7-141.4-132.2 174.2 -20.0 6.6 16.6 21 21 X V S S+ 0 0 124 -2,-0.3 2,-0.2 1,-0.2 3,-0.1 0.339 94.9 54.3-117.1 1.2 -17.9 4.8 19.2 22 22 X D > + 0 0 81 1,-0.1 4,-2.8 -21,-0.1 3,-0.3 -0.602 51.9 161.4-137.7 75.0 -18.8 1.3 18.0 23 23 X A H > S+ 0 0 14 1,-0.2 4,-3.6 2,-0.2 5,-0.3 0.843 77.6 61.8 -62.3 -33.9 -18.0 0.8 14.3 24 24 X A H > S+ 0 0 74 2,-0.2 4,-1.2 1,-0.2 -1,-0.2 0.917 112.3 35.6 -58.9 -45.1 -18.1 -3.0 14.8 25 25 X T H > S+ 0 0 70 -3,-0.3 4,-2.5 2,-0.2 -2,-0.2 0.916 120.7 47.3 -75.1 -45.3 -21.7 -2.8 15.9 26 26 X A H X S+ 0 0 35 -4,-2.8 4,-3.0 1,-0.2 5,-0.3 0.911 109.9 53.5 -62.7 -44.0 -22.7 -0.0 13.5 27 27 X E H X S+ 0 0 34 -4,-3.6 4,-1.8 -5,-0.2 -1,-0.2 0.896 112.1 45.0 -58.5 -41.9 -21.0 -1.7 10.5 28 28 X K H X S+ 0 0 122 -4,-1.2 4,-2.1 -5,-0.3 5,-0.2 0.923 114.7 47.0 -68.8 -45.6 -22.9 -4.9 11.1 29 29 X V H X S+ 0 0 89 -4,-2.5 4,-2.0 1,-0.2 -2,-0.2 0.900 113.4 48.9 -63.2 -41.7 -26.2 -3.2 11.6 30 30 X F H X S+ 0 0 93 -4,-3.0 4,-3.5 2,-0.2 5,-0.3 0.863 108.5 54.5 -66.6 -36.5 -25.7 -1.0 8.5 31 31 X K H X S+ 0 0 72 -4,-1.8 4,-2.7 -5,-0.3 5,-0.2 0.952 112.3 41.4 -62.6 -50.8 -24.7 -4.0 6.4 32 32 X Q H X S+ 0 0 126 -4,-2.1 4,-1.7 1,-0.2 -1,-0.2 0.850 118.4 48.5 -65.8 -33.9 -27.9 -6.0 7.3 33 33 X Y H X S+ 0 0 154 -4,-2.0 4,-1.4 -5,-0.2 -2,-0.2 0.921 112.6 46.5 -72.5 -44.3 -29.9 -2.8 6.9 34 34 X A H <>S+ 0 0 14 -4,-3.5 5,-3.4 2,-0.2 4,-0.4 0.931 112.1 51.0 -63.1 -45.6 -28.4 -1.8 3.5 35 35 X N H ><5S+ 0 0 84 -4,-2.7 3,-1.3 1,-0.3 -1,-0.2 0.905 109.5 50.5 -58.0 -42.3 -28.8 -5.4 2.2 36 36 X D H 3<5S+ 0 0 130 -4,-1.7 -1,-0.3 1,-0.3 -2,-0.2 0.792 108.0 53.5 -66.4 -27.4 -32.5 -5.2 3.3 37 37 X N T 3<5S- 0 0 125 -4,-1.4 -1,-0.3 -3,-0.3 -2,-0.2 0.469 131.5 -96.1 -85.8 -1.3 -32.7 -1.9 1.4 38 38 X G T < 5S+ 0 0 55 -3,-1.3 2,-0.8 -4,-0.4 -3,-0.2 0.690 77.1 145.5 94.5 23.3 -31.3 -3.6 -1.7 39 39 X V < + 0 0 31 -5,-3.4 2,-0.3 -6,-0.2 -1,-0.2 -0.833 18.4 156.5 -99.0 109.0 -27.7 -2.5 -1.1 40 40 X D + 0 0 67 -2,-0.8 2,-0.3 -32,-0.1 -30,-0.2 -0.816 13.2 89.2-126.4 167.4 -25.3 -5.2 -2.3 41 41 X G S S- 0 0 5 -2,-0.3 2,-0.6 15,-0.2 15,-0.2 -0.996 77.6 -30.2 148.0-150.0 -21.7 -5.4 -3.5 42 42 X E - 0 0 127 -2,-0.3 2,-0.3 13,-0.1 13,-0.2 -0.923 54.4-169.8-111.4 116.4 -18.3 -5.9 -2.0 43 43 X W + 0 0 120 -2,-0.6 2,-0.3 11,-0.2 11,-0.1 -0.764 11.5 162.7-104.8 150.0 -17.7 -4.7 1.5 44 44 X T - 0 0 67 9,-0.3 2,-0.7 -2,-0.3 9,-0.3 -0.958 38.0-110.7-155.3 169.1 -14.4 -4.4 3.4 45 45 X Y - 0 0 188 -2,-0.3 2,-0.6 7,-0.1 7,-0.1 -0.893 28.0-167.2-114.0 105.0 -12.7 -2.7 6.4 46 46 X D + 0 0 60 5,-0.8 -2,-0.0 -2,-0.7 5,-0.0 -0.798 12.3 176.2 -93.7 122.4 -10.2 -0.0 5.5 47 47 X D S S+ 0 0 142 -2,-0.6 -1,-0.2 2,-0.2 0, 0.0 0.780 81.5 52.3 -92.5 -32.3 -8.0 1.1 8.4 48 48 X A S S+ 0 0 91 1,-0.2 -1,-0.1 3,-0.1 -2,-0.1 0.783 127.8 23.6 -74.0 -27.5 -5.8 3.5 6.4 49 49 X T S S- 0 0 75 2,-0.2 -1,-0.2 -45,-0.0 -2,-0.2 0.269 88.3-145.5-119.3 7.2 -8.8 5.2 5.0 50 50 X K + 0 0 104 1,-0.1 -46,-1.1 -47,-0.1 2,-0.3 0.759 62.5 126.6 30.8 31.2 -11.3 4.3 7.8 51 51 X T E -b 4 0A 23 -48,-0.2 -5,-0.8 -46,-0.0 2,-0.3 -0.899 52.6-145.8-118.6 147.5 -13.7 4.3 4.8 52 52 X F E -b 5 0A 5 -48,-2.2 -46,-2.5 -2,-0.3 2,-0.4 -0.860 13.0-168.9-112.1 146.0 -16.1 1.6 3.6 53 53 X T E -b 6 0A 51 -2,-0.3 2,-0.4 -9,-0.3 -9,-0.3 -0.995 6.6-171.9-136.9 141.6 -17.0 0.8 -0.0 54 54 X V E -b 7 0A 7 -48,-2.2 -46,-3.6 -2,-0.4 2,-0.5 -0.988 2.1-173.4-135.5 124.8 -19.6 -1.4 -1.6 55 55 X T E b 8 0A 84 -2,-0.4 -46,-0.1 -13,-0.2 -13,-0.1 -0.950 360.0 360.0-124.1 115.5 -19.9 -2.3 -5.3 56 56 X E 0 0 137 -48,-1.8 -15,-0.2 -2,-0.5 -46,-0.0 -0.424 360.0 360.0 -63.9 360.0 -22.9 -4.2 -6.7