Protein Data Bank File : 3gcc Title : TRANSCRIPTION FACTOR 13-MAR-98 3GCC Number of Amino Acid Residues : 63 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS HIS TYR ARG GLY VAL ARG GLN ARG PRO 10 TRP GLY LYS PHE ALA ALA GLU ILE ARG ASP 20 PRO ALA LYS ASN GLY ALA ARG VAL TRP LEU 30 GLY THR PHE GLU THR ALA GLU ASP ALA ALA 40 LEU ALA TYR ASP ARG ALA ALA PHE ARG MET 50 ARG GLY SER ARG ALA LEU LEU ASN PHE PRO 60 LEU ARG VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 162.8 -179.9 -102.7 -84.0 -130.8 -131.2 2 HIS -135.0 78.0 180.0 -158.0 139.6 3 TYR -48.4 150.6 179.9 -68.6 -43.3 4 ARG -79.8 82.2 179.9 -83.1 -115.8 97.4 -161.4 5 GLY 137.6 -13.5 -179.9 6 VAL -102.2 120.9 -179.8 -174.1 7 ARG -103.9 89.4 179.8 -111.7 122.7 94.8 125.6 8 GLN -47.0 150.0 -179.8 70.6 -65.6 103.5 9 ARG -113.4 161.8 180.0 -80.2 -84.2 -173.6 -140.4 10 PRO -78.3 6.1 -180.0 22.5 -20.8 11 TRP -114.2 -15.1 179.9 -95.0 -50.0 12 GLY 112.8 31.0 -180.0 13 LYS -120.4 -175.3 179.9 -48.6 -69.1 -65.5 -177.0 14 PHE -157.6 117.7 -179.4 -69.6 88.4 15 ALA -89.9 122.5 179.0 16 ALA -98.5 111.9 -179.2 17 GLU -135.2 150.9 179.8 -39.2 155.1 79.8 18 ILE -127.9 148.3 -179.8 -175.7 -175.1 19 ARG -80.1 133.0 179.9 -175.1 99.4 123.1 169.7 20 ASP -126.6 94.5 -179.8 -171.1 -31.0 21 PRO -77.8 -25.0 -179.8 22.3 -20.8 22 ALA -71.4 -11.9 -179.8 23 LYS -100.1 55.6 179.9 -80.0 -171.7 166.3 150.2 24 ASN 56.3 31.0 179.9 -49.0 -91.5 25 GLY 64.2 68.0 179.9 26 ALA -124.7 -180.0 -179.9 27 ARG -111.3 156.1 179.9 -68.3 151.5 69.9 -126.6 28 VAL -129.1 88.3 -180.0 164.8 29 TRP -79.6 102.2 179.9 -179.7 -60.9 30 LEU -56.8 -55.5 179.9 -67.5 148.2 31 GLY 159.5 153.3 179.9 32 THR -66.0 166.7 -180.0 85.1 33 PHE -141.4 -177.3 179.9 -73.6 84.4 34 GLU -95.8 -30.3 180.0 174.9 155.5 35.8 35 THR -136.7 167.1 179.5 82.2 36 ALA -71.4 -26.3 179.7 37 GLU -71.9 -35.3 179.6 -164.0 -124.9 -84.8 38 ASP -74.1 -43.6 179.6 -31.6 -40.7 39 ALA -71.4 -23.8 179.7 40 ALA -76.6 -42.8 179.4 41 LEU -63.0 -38.8 179.6 -152.9 -58.7 42 ALA -67.8 -38.6 179.7 43 TYR -60.6 -39.2 180.0 175.9 -74.1 44 ASP -57.0 -44.1 -179.5 -83.6 44.6 45 ARG -59.8 -48.8 -179.6 -125.5 -98.2 -147.1 -129.8 46 ALA -72.8 -15.4 179.9 47 ALA -91.5 -17.5 179.5 48 PHE -94.3 -31.3 179.3 -148.1 -82.7 49 ARG -76.3 -46.7 180.0 -97.1 -93.7 121.0 -144.3 50 MET -65.5 -33.5 -179.7 -139.9 174.3 -90.0 51 ARG -100.1 18.2 179.7 -84.5 124.3 139.5 40.6 52 GLY 57.4 -99.4 -179.7 53 SER -126.1 158.1 179.9 -105.6 54 ARG 58.6 91.1 179.9 -137.9 68.4 -150.5 99.1 55 ALA -140.2 174.1 -180.0 56 LEU -102.0 113.6 179.9 -48.3 132.5 57 LEU -125.2 179.5 178.8 2.0 160.3 58 ASN -73.9 -35.2 179.8 -24.2 -61.5 59 PHE -120.0 83.4 -179.6 -44.7 -37.4 60 PRO -77.3 71.8 -179.8 22.3 -21.0 61 LEU 174.5 -73.6 179.8 -116.8 139.4 62 ARG -75.0 102.6 180.0 -62.9 -102.1 -85.8 -61.8 63 VAL -78.8 154.4 0.0 66.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 9.565 -5.614 -8.910 2 HIS 7.003 -2.789 -8.609 3 TYR 4.209 -3.706 -6.166 4 ARG 0.973 -1.804 -6.886 5 GLY 1.247 0.772 -4.073 6 VAL 4.881 0.407 -2.950 7 ARG 7.233 3.162 -4.152 8 GLN 10.776 1.817 -3.680 9 ARG 13.180 4.610 -2.674 10 PRO 16.709 5.461 -3.836 11 TRP 17.918 4.989 -0.239 12 GLY 16.603 1.454 0.381 13 LYS 13.067 2.143 1.661 14 PHE 9.527 1.481 0.378 15 ALA 6.410 3.639 0.856 16 ALA 3.184 1.626 1.158 17 GLU 0.196 3.785 0.149 18 ILE -3.304 2.974 -1.161 19 ARG -5.740 5.101 -3.203 20 ASP -8.907 6.076 -1.297 21 PRO -11.593 7.567 -3.555 22 ALA -14.300 7.157 -0.887 23 LYS -12.460 9.818 1.154 24 ASN -13.325 12.800 -1.080 25 GLY -10.555 11.582 -3.416 26 ALA -7.631 11.612 -0.956 27 ARG -4.452 9.545 -0.461 28 VAL -3.675 7.038 2.318 29 TRP 0.075 6.760 3.005 30 LEU 0.358 3.733 5.327 31 GLY 4.023 4.432 6.118 32 THR 7.536 3.957 4.707 33 PHE 9.153 0.516 5.073 34 GLU 12.580 -1.142 4.862 35 THR 11.829 -3.398 1.865 36 ALA 9.179 -3.608 -0.869 37 GLU 7.954 -6.879 0.681 38 ASP 7.330 -5.166 4.036 39 ALA 5.624 -2.134 2.460 40 ALA 3.706 -4.543 0.201 41 LEU 2.388 -6.638 3.109 42 ALA 1.268 -3.434 4.850 43 TYR -0.452 -2.244 1.656 44 ASP -2.478 -5.479 1.612 45 ARG -3.895 -4.657 5.063 46 ALA -5.011 -1.158 4.004 47 ALA -6.239 -2.648 0.707 48 PHE -8.368 -5.286 2.460 49 ARG -9.848 -2.924 5.066 50 MET -10.626 -0.155 2.566 51 ARG -12.063 -2.729 0.138 52 GLY -13.775 -4.711 2.924 53 SER -13.309 -8.233 1.513 54 ARG -11.975 -9.547 -1.819 55 ALA -9.521 -6.875 -3.018 56 LEU -6.432 -6.602 -5.254 57 LEU -3.162 -6.583 -3.275 58 ASN 0.484 -7.454 -3.989 59 PHE 0.083 -10.683 -2.007 60 PRO -3.438 -11.967 -2.697 61 LEU -3.286 -14.932 -0.290 62 ARG -0.974 -14.621 2.729 63 VAL -2.659 -11.890 4.806 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S S/T T 10 T T/S S S S S S S S S/T 20 T T T S S S S S S S/S 30 S S S S H H H H H H 40 H H H H H H H H H H 50 H H S S S S C C T T 60 T T/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T e E E E e T 10 T t e E E E E E E E 20 T T T T t E E E E E 30 E E E S h H H H H H 40 H H H H H H H H H h 50 T t S S S S S 60 S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 15.9 9.1 86.7 2 HIS 44.3 29.5 86.2 3 TYR 141.3 78.1 46.0 4 ARG 2.2 1.1 93.5 5 GLY 18.8 54.1 65.8 6 VAL 117.9 99.2 46.4 7 ARG 73.2 35.0 88.2 8 GLN 81.2 54.6 63.5 9 ARG 103.8 49.7 64.5 10 PRO 28.8 23.2 71.5 11 TRP 10.5 5.1 80.0 12 GLY 1.9 5.6 75.1 13 LYS 87.4 50.4 63.3 14 PHE 131.4 78.8 50.0 15 ALA 71.8 98.9 48.0 16 ALA 72.6 100.0 39.8 17 GLU 122.4 88.3 55.8 18 ILE 140.4 97.8 44.2 19 ARG 26.6 12.7 81.0 20 ASP 107.7 97.5 35.2 21 PRO 42.3 34.0 75.1 22 ALA 1.1 1.5 82.4 23 LYS 63.8 36.8 75.0 24 ASN 0.0 0.0 88.8 25 GLY 5.1 14.8 76.7 26 ALA 30.7 42.3 76.0 27 ARG 61.4 29.4 80.7 28 VAL 89.9 75.7 57.1 29 TRP 127.7 62.3 68.0 30 LEU 109.9 74.4 52.1 31 GLY 13.2 38.0 70.0 32 THR 41.0 38.3 65.6 33 PHE 120.1 72.0 61.4 34 GLU 23.1 16.7 79.4 35 THR 53.3 49.8 63.4 36 ALA 54.0 74.4 41.6 37 GLU 36.6 26.4 75.0 38 ASP 63.8 57.7 61.1 39 ALA 72.6 100.0 40.2 40 ALA 72.6 100.0 39.1 41 LEU 89.4 60.5 70.3 42 ALA 50.6 69.7 48.7 43 TYR 158.6 87.6 54.4 44 ASP 109.7 99.3 48.2 45 ARG 47.8 22.9 78.1 46 ALA 61.0 84.0 43.9 47 ALA 72.6 100.0 46.3 48 PHE 91.8 55.1 69.6 49 ARG 44.3 21.2 85.0 50 MET 120.5 75.6 59.1 51 ARG 108.8 52.1 66.2 52 GLY 5.4 15.4 84.9 53 SER 15.9 19.0 69.9 54 ARG 20.9 10.0 83.9 55 ALA 68.2 93.9 50.4 56 LEU 8.1 5.5 84.5 57 LEU 137.6 93.1 52.1 58 ASN 111.3 92.0 40.9 59 PHE 127.8 76.6 53.6 60 PRO 52.5 42.1 75.4 61 LEU 5.1 3.5 84.9 62 ARG 13.8 6.6 86.3 63 VAL 17.9 15.1 79.7