Protein Data Bank File : 1efnb Title : COMPLEX (SH3 DOMAIN/VIRAL ENHANCER) 29-JUN-96 1EFN Number of Amino Acid Residues : 104 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG PRO GLN VAL PRO LEU ARG PRO MET THR 10 TYR LYS ALA ALA VAL ASP LEU SER HIS PHE 20 LEU LYS GLU LYS GLY GLY LEU GLU GLY LEU 30 ILE HIS SER GLN ARG ARG GLN ASP ILE LEU 40 ASP LEU TRP ILE TYR HIS THR GLN GLY TYR 50 PHE PRO ASP TRP GLN ASN TYR THR PRO GLY 60 PRO GLY VAL ARG TYR PRO LEU THR PHE GLY 70 TRP CYS TYR LYS LEU VAL PRO VAL ARG GLU 80 VAL LEU GLU TRP ARG PHE ASP SER ARG LEU 90 ALA PHE HIS HIS VAL ALA ARG GLU LEU HIS 100 PRO GLU TYR PHE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 92.9 -179.4 -177.2 -168.5 171.5 119.3 2 PRO -48.5 158.9 176.9 -25.9 41.7 3 GLN -81.3 120.0 179.6 -178.4 -83.6 -30.8 4 VAL -48.5 153.6 179.9 132.3 5 PRO -59.4 148.3 178.3 -29.9 42.0 6 LEU -68.2 153.6 177.4 164.7 153.2 7 ARG -159.4 132.7 -179.4 55.3 175.9 171.3 171.6 8 PRO -56.9 147.1 178.4 32.0 -44.9 9 MET -79.2 146.9 179.4 178.2 54.1 82.2 10 THR -149.1 159.3 179.0 47.3 11 TYR -44.1 -54.1 -179.8 172.7 77.5 12 LYS -55.9 -44.3 -179.5 -173.4 -161.0 165.1 -156.7 13 ALA -66.1 -34.9 179.9 14 ALA -68.5 -45.1 177.6 15 VAL -61.4 -41.1 178.6 177.4 16 ASP -65.7 -42.4 179.5 -71.5 -10.5 17 LEU -62.1 -39.6 -179.7 -83.3 177.5 18 SER -56.6 -51.3 -178.6 -58.1 19 HIS -70.6 -29.5 179.4 -63.8 125.2 20 PHE -65.1 -53.1 -179.9 171.3 76.9 21 LEU -66.8 -23.3 178.1 -67.1 167.7 22 LYS -74.2 -42.3 178.7 -151.2 -170.8 148.8 60.3 23 GLU -55.5 -57.8 178.8 -65.8 159.5 26.2 24 LYS -78.3 55.7 -178.0 0.0 0.0 0.0 0.0 25 GLY -34.1 136.1 -179.9 26 GLY 172.8 -30.9 179.9 27 LEU -77.9 -26.2 -177.1 -74.5 -177.6 28 GLU -52.5 118.4 179.7 -149.3 57.0 51.5 29 GLY 69.5 -14.9 179.4 30 LEU -50.7 133.1 -179.2 177.8 62.2 31 ILE -67.5 124.8 179.9 -55.8 -70.4 32 HIS -67.4 153.6 179.5 -170.8 -117.8 33 SER -164.7 125.8 179.7 164.3 34 GLN -48.4 -39.0 179.6 -169.8 59.3 36.6 35 ARG -65.5 -46.4 -179.8 -125.6 -67.4 -170.0 -57.4 36 ARG -58.7 -40.3 180.0 -78.3 169.4 154.1 -156.3 37 GLN -73.4 -42.6 179.6 -179.2 -168.4 -38.8 38 ASP -58.6 -37.4 178.3 -78.6 -12.3 39 ILE -65.5 -46.9 179.3 -64.3 175.3 40 LEU -57.2 -49.7 -178.6 -152.3 -163.0 41 ASP -63.5 -35.7 179.7 -65.1 -6.1 42 LEU -69.7 -37.0 179.0 -70.5 170.8 43 TRP -60.8 -47.7 179.3 178.1 79.5 44 ILE -64.5 -34.6 178.8 -64.1 158.1 45 TYR -62.7 -51.3 -179.6 175.8 34.7 46 HIS -67.1 -48.4 -178.7 161.4 103.5 47 THR -65.7 -54.4 -178.9 -75.8 48 GLN -109.8 -13.9 175.7 -51.6 -58.9 -18.9 49 GLY 91.6 14.0 179.3 50 TYR -94.5 112.8 179.5 -63.0 -61.1 51 PHE -50.4 125.6 -179.5 -159.9 78.3 52 PRO -64.7 74.5 178.3 31.7 -44.7 53 ASP -152.2 16.7 -177.9 64.3 -18.0 54 TRP -96.9 -47.7 -177.8 57.1 -83.0 55 GLN -70.0 62.4 178.5 -171.9 -176.7 170.6 56 ASN -101.3 137.7 -179.1 -67.4 -43.6 57 TYR -111.6 159.2 179.6 -61.0 -79.6 58 THR -68.6 166.8 179.9 49.8 59 PRO -62.2 171.3 175.9 -29.7 42.9 60 GLY -98.6 -175.3 -0.4 61 PRO -92.9 171.7 179.7 37.6 -41.6 62 GLY 105.8 -147.5 179.6 63 VAL -80.8 137.3 178.7 -179.7 64 ARG -106.8 115.2 -177.1 -76.4 64.6 177.9 -57.3 65 TYR -89.2 143.7 180.0 -62.3 -74.4 66 PRO -67.3 133.4 -179.0 31.8 -44.8 67 LEU -78.2 -29.7 179.6 -61.4 -156.2 68 THR -81.5 116.6 -179.6 -65.0 69 PHE -67.8 128.6 -179.4 -171.5 36.1 70 GLY 120.5 -34.3 -179.9 71 TRP -72.0 112.4 -177.4 177.9 -123.3 72 CYS -91.1 41.8 176.6 -54.6 73 TYR -133.5 145.5 178.3 -82.3 -86.5 74 LYS -137.8 163.0 179.4 53.3 -176.9 175.3 177.8 75 LEU -103.8 120.3 -177.6 -57.7 -176.5 76 VAL -114.8 123.6 179.7 175.3 77 PRO -47.1 134.1 -179.0 -40.7 44.6 78 VAL 70.9 76.7 -40.9 169.0 79 ARG 1.0 -146.5 -179.5 0.0 0.0 0.0 0.0 80 GLU -64.2 124.7 178.5 -141.2 173.1 25.9 81 VAL -86.5 130.4 -177.4 178.3 82 LEU -121.9 163.0 177.8 -55.2 161.6 83 GLU -136.5 159.7 177.2 -64.6 167.3 -56.0 84 TRP -84.5 119.0 179.6 -90.3 -72.2 85 ARG -122.4 121.0 179.3 -79.8 -74.3 140.3 62.5 86 PHE -73.6 121.5 177.6 -174.7 -87.4 87 ASP -128.4 87.0 178.0 -179.2 12.1 88 SER -33.1 -36.1 -177.8 -179.1 89 ARG -76.7 -4.4 178.1 70.8 -171.8 70.7 107.0 90 LEU -69.1 -14.8 178.7 -73.2 168.5 91 ALA -84.3 -9.9 -178.9 92 PHE -116.5 -12.7 -179.2 -56.2 -74.8 93 HIS -135.5 111.4 178.5 -76.1 -84.0 94 HIS -77.7 72.9 -178.6 -154.7 -173.0 95 VAL -53.7 -50.9 -179.4 -174.6 96 ALA -48.5 -40.3 -179.8 97 ARG -75.3 -29.8 -179.9 -166.6 -177.3 -163.5 -140.5 98 GLU -67.2 -54.9 -178.5 -66.6 179.9 13.1 99 LEU -78.2 -23.6 -178.0 -49.4 170.5 100 HIS -140.2 62.5 -179.9 -66.4 -75.8 101 PRO -59.8 -17.3 -179.3 26.9 -43.1 102 GLU -56.6 -28.4 178.7 80.5 -88.8 -8.7 103 TYR -81.3 1.8 179.4 -58.3 -54.9 104 PHE -133.9 95.2 0.0 -42.9 83.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG 34.775 7.285 18.896 2 PRO 32.823 7.992 22.115 3 GLN 34.396 8.707 25.436 4 VAL 34.434 5.244 27.006 5 PRO 32.196 4.638 30.037 6 LEU 33.609 5.875 33.341 7 ARG 35.068 3.170 35.596 8 PRO 36.767 3.430 39.014 9 MET 40.520 3.241 39.484 10 THR 41.703 0.217 41.433 11 TYR 45.097 -1.188 42.402 12 LYS 44.727 -3.573 39.532 13 ALA 43.781 -0.854 37.059 14 ALA 46.746 1.294 38.127 15 VAL 49.091 -1.708 37.790 16 ASP 47.571 -2.555 34.429 17 LEU 47.928 1.014 33.120 18 SER 51.587 1.096 34.187 19 HIS 52.499 -1.951 32.144 20 PHE 50.251 -0.785 29.338 21 LEU 52.002 2.591 29.040 22 LYS 55.321 0.827 29.463 23 GLU 54.450 -1.420 26.480 24 LYS 53.605 1.710 24.455 25 GLY 56.962 3.044 25.661 26 GLY 57.210 6.809 25.906 27 LEU 56.952 8.075 29.488 28 GLU 60.327 6.691 30.435 29 GLY 62.634 9.530 31.192 30 LEU 60.134 11.811 29.418 31 ILE 60.466 15.225 31.057 32 HIS 57.488 15.827 33.286 33 SER 55.248 18.824 32.715 34 GLN 51.849 19.312 34.349 35 ARG 50.551 19.951 30.846 36 ARG 52.176 16.812 29.466 37 GLN 50.592 14.860 32.294 38 ASP 47.171 16.583 32.090 39 ILE 47.181 15.605 28.442 40 LEU 48.099 12.018 29.380 41 ASP 45.329 11.808 31.956 42 LEU 42.678 13.178 29.646 43 TRP 43.703 10.637 27.022 44 ILE 43.258 7.763 29.527 45 TYR 39.946 9.259 30.670 46 HIS 38.466 9.273 27.131 47 THR 40.230 6.063 26.118 48 GLN 39.872 3.879 29.206 49 GLY 37.373 5.682 31.457 50 TYR 39.432 6.520 34.511 51 PHE 38.425 9.936 35.821 52 PRO 41.592 12.095 35.661 53 ASP 42.255 12.509 39.381 54 TRP 44.409 9.511 40.154 55 GLN 47.929 10.347 38.956 56 ASN 48.790 12.685 41.850 57 TYR 52.343 12.797 43.168 58 THR 53.824 13.648 46.564 59 PRO 55.397 17.085 47.170 60 GLY 58.926 18.006 46.233 61 PRO 61.754 18.336 46.332 62 GLY 63.339 15.095 45.182 63 VAL 61.540 12.039 43.866 64 ARG 57.769 12.513 43.755 65 TYR 55.959 9.293 44.567 66 PRO 52.554 8.311 43.115 67 LEU 49.678 8.560 45.570 68 THR 47.568 5.862 43.859 69 PHE 48.914 2.479 44.962 70 GLY 49.511 0.446 41.843 71 TRP 50.765 3.296 39.669 72 CYS 54.350 2.313 38.959 73 TYR 55.709 5.715 37.981 74 LYS 57.418 8.379 40.008 75 LEU 58.920 11.712 39.088 76 VAL 62.704 11.768 39.369 77 PRO 64.817 15.010 39.302 78 VAL 66.768 15.879 36.170 79 ARG 62.650 24.722 39.862 80 GLU 63.443 20.982 39.921 81 VAL 63.117 19.395 36.451 82 LEU 61.482 15.959 36.652 83 GLU 60.967 12.840 34.540 84 TRP 58.654 9.856 34.561 85 ARG 60.538 6.827 35.953 86 PHE 58.975 3.386 36.067 87 ASP 59.651 1.832 39.448 88 SER 58.153 -1.648 39.513 89 ARG 58.262 -1.905 43.320 90 LEU 55.746 0.869 43.723 91 ALA 53.143 -1.880 43.166 92 PHE 54.384 -3.603 46.311 93 HIS 55.212 -0.540 48.406 94 HIS 52.927 2.412 48.960 95 VAL 55.836 4.826 49.445 96 ALA 53.654 7.943 49.117 97 ARG 51.525 6.797 52.025 98 GLU 54.596 5.928 54.068 99 LEU 56.201 9.327 53.607 100 HIS 53.040 11.452 53.295 101 PRO 50.144 9.939 55.193 102 GLU 48.564 13.400 55.268 103 TYR 47.084 12.733 51.813 104 PHE 45.405 9.647 53.329 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C S S S S S C H 10 H H H H H H H H H H 20 H H H H H C C C C S 30 S S S/H H H H H H H H 40 H H H H H H H H/S S S 50 S C C C S S S S S SPT 60 T T T/S S S S S/S S S S 70 C S S S S S S S/X X/S S 80 S S S S S S C C T T 90 T T C H H H H H H H 100 C S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h 10 H H H H H H H H H H 20 H H H h t t B T t 30 B h H H H H H H H 40 H H H H H H H H h 50 S B S 60 S S B B S t T T 70 t e E E E E E e 80 e E E E E E e G G G 90 G g t h H H H H H h 100 G G G g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 36.7 17.6 85.5 2 PRO 12.7 10.2 84.6 3 GLN 92.2 62.0 65.4 4 VAL 68.3 57.5 71.2 5 PRO 16.6 13.3 80.5 6 LEU 58.7 39.7 69.2 7 ARG 98.8 47.3 69.5 8 PRO 27.6 22.1 73.2 9 MET 136.0 85.3 37.0 10 THR 35.6 33.3 70.0 11 TYR 93.3 51.6 57.8 12 LYS 26.7 15.4 82.8 13 ALA 63.1 86.9 63.8 14 ALA 72.6 100.0 47.1 15 VAL 94.1 79.2 52.7 16 ASP 45.1 40.8 68.9 17 LEU 139.8 94.6 29.9 18 SER 83.6 100.0 44.1 19 HIS 67.4 44.9 63.7 20 PHE 93.1 55.8 62.7 21 LEU 133.6 90.4 34.3 22 LYS 83.4 48.1 68.4 23 GLU 25.6 18.5 78.5 24 LYS 115.7 66.7 75.3 25 GLY 8.8 25.4 82.4 26 GLY 0.0 0.0 86.0 27 LEU 136.3 92.2 33.4 28 GLU 74.0 53.4 73.7 29 GLY 25.5 73.3 74.0 30 LEU 87.1 58.9 68.9 31 ILE 68.0 47.4 76.4 32 HIS 131.2 87.3 45.6 33 SER 43.5 52.1 66.6 34 GLN 45.2 30.4 84.4 35 ARG 42.0 20.1 81.0 36 ARG 110.0 52.6 58.3 37 GLN 138.0 92.9 60.8 38 ASP 56.2 50.9 70.7 39 ILE 44.0 30.7 70.3 40 LEU 126.7 85.7 41.9 41 ASP 100.1 90.6 56.6 42 LEU 45.6 30.9 69.4 43 TRP 88.7 43.3 61.5 44 ILE 143.5 100.0 33.2 45 TYR 120.9 66.8 58.0 46 HIS 84.1 56.0 71.7 47 THR 98.8 92.4 53.0 48 GLN 99.9 67.2 52.5 49 GLY 34.8 100.0 57.5 50 TYR 164.5 90.9 48.4 51 PHE 66.8 40.0 65.6 52 PRO 103.9 83.5 44.8 53 ASP 29.7 26.9 72.0 54 TRP 196.2 95.7 39.6 55 GLN 147.9 99.5 45.0 56 ASN 46.0 38.1 70.6 57 TYR 170.4 94.1 51.3 58 THR 105.5 98.7 41.4 59 PRO 73.2 58.8 72.6 60 GLY 31.4 90.1 67.7 61 PRO 22.1 17.8 85.8 62 GLY 10.5 30.3 69.6 63 VAL 83.5 70.3 50.9 64 ARG 165.9 79.4 54.8 65 TYR 138.1 76.3 42.2 66 PRO 121.0 97.2 46.9 67 LEU 120.7 81.6 50.8 68 THR 79.2 74.1 54.7 69 PHE 104.1 62.4 66.0 70 GLY 34.8 100.0 44.1 71 TRP 204.8 99.9 35.6 72 CYS 98.4 99.2 44.1 73 TYR 179.4 99.1 42.7 74 LYS 137.6 79.4 44.7 75 LEU 143.9 97.4 38.0 76 VAL 86.0 72.4 52.1 77 PRO 100.0 80.3 53.5 78 VAL 0.0 0.0 82.1 79 ARG 126.5 60.6 92.6 80 GLU 91.7 66.1 57.9 81 VAL 41.2 34.7 70.8 82 LEU 137.5 93.0 57.6 83 GLU 117.3 84.6 62.5 84 TRP 204.0 99.5 38.0 85 ARG 129.1 61.8 64.7 86 PHE 153.3 91.9 50.8 87 ASP 95.0 86.0 58.3 88 SER 23.3 27.9 67.0 89 ARG 53.3 25.5 79.1 90 LEU 144.7 97.9 49.0 91 ALA 67.0 92.3 44.2 92 PHE 40.7 24.4 76.9 93 HIS 52.5 34.9 71.5 94 HIS 119.1 79.3 52.6 95 VAL 91.7 77.2 43.7 96 ALA 72.6 100.0 42.5 97 ARG 69.4 33.2 69.2 98 GLU 50.9 36.7 74.4 99 LEU 64.1 43.4 64.2 100 HIS 106.6 71.0 55.8 101 PRO 48.8 39.2 78.1 102 GLU 49.9 36.0 70.2 103 TYR 108.1 59.7 54.2 104 PHE 120.4 72.2 60.7