Protein Data Bank File : 1co4 Title : TRANSLATION/REGULATION PROTEIN 04-JUN-99 1CO4 Number of Amino Acid Residues : 42 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET VAL VAL ILE ASN GLY VAL LYS TYR ALA 10 CYS ASP SER CYS ILE LYS SER HIS LYS ALA 20 ALA GLN CYS GLU HIS ASN ASP ARG PRO LEU 30 LYS ILE LEU LYS PRO ARG GLY ARG PRO PRO 40 THR THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 168.6 180.0 73.8 -69.3 -176.2 2 VAL -132.7 150.6 180.0 -178.0 3 VAL -141.0 140.6 180.0 175.7 4 ILE -133.7 124.1 180.0 -49.4 98.3 5 ASN 60.8 -86.9 180.0 165.2 50.7 6 GLY -141.9 25.4 -179.9 7 VAL -118.5 155.4 -180.0 -164.7 8 LYS -122.4 159.9 -180.0 -37.4 -168.7 145.2 -176.7 9 TYR -159.1 174.0 -180.0 -48.5 81.6 10 ALA 173.2 166.2 -180.0 11 CYS -68.0 156.5 180.0 75.7 12 ASP -68.0 -12.7 -180.0 -136.1 65.3 13 SER -99.7 24.5 180.0 -101.3 14 CYS -145.7 -60.8 180.0 -80.9 15 ILE -57.8 -25.3 180.0 -161.5 131.8 16 LYS -94.6 -19.6 -180.0 -121.8 -96.0 -93.0 -57.7 17 SER -96.8 -75.8 -180.0 -119.9 18 HIS 158.9 -25.1 180.0 153.0 -130.4 19 LYS -53.7 -19.2 180.0 -104.7 -73.2 -73.7 -99.8 20 ALA -43.7 -27.2 180.0 21 ALA -37.2 -32.9 -180.0 22 GLN -156.0 39.4 180.0 -174.2 141.7 125.6 23 CYS -52.5 144.2 -180.0 158.1 24 GLU -154.2 23.1 -180.0 -179.3 135.9 -48.0 25 HIS -78.7 164.8 -179.9 -48.2 93.4 26 ASN -108.8 -73.9 179.9 -79.7 -79.6 27 ASP -50.2 178.9 -180.0 -147.5 -70.6 28 ARG 79.7 151.6 180.0 -131.0 123.4 46.0 -169.7 29 PRO -75.0 136.4 180.0 18.7 -14.1 30 LEU -91.0 164.3 -180.0 -149.9 69.9 31 LYS -146.2 169.7 -180.0 -118.9 -152.7 111.7 -105.5 32 ILE -111.4 170.6 -180.0 101.3 -61.7 33 LEU -176.5 166.0 180.0 -149.3 104.4 34 LYS -142.1 173.8 180.0 -112.3 176.0 55.5 146.3 35 PRO -75.0 82.2 180.0 18.7 -14.1 36 ARG 58.9 158.4 -180.0 -99.3 -126.9 -41.5 -84.5 37 GLY -152.2 -73.5 180.0 38 ARG 86.3 150.7 180.0 100.7 -158.1 -45.7 -85.0 39 PRO -75.0 160.4 180.0 18.7 -14.0 40 PRO -74.9 -23.7 -179.9 18.7 -14.0 41 THR -124.4 -80.3 -180.0 -58.2 42 THR -153.9 -16.5 0.0 -40.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET -2.289 6.753 6.026 2 VAL -4.642 7.182 3.092 3 VAL -7.094 4.868 1.372 4 ILE -8.986 5.142 -1.894 5 ASN -11.828 2.873 -2.941 6 GLY -10.131 -0.323 -1.832 7 VAL -6.482 0.681 -1.838 8 LYS -4.219 1.835 0.969 9 TYR -1.227 4.150 1.097 10 ALA 1.123 6.063 3.365 11 CYS 4.488 7.783 3.566 12 ASP 7.608 5.660 3.274 13 SER 8.265 6.790 6.826 14 CYS 5.112 5.076 8.031 15 ILE 4.119 2.219 5.755 16 LYS 7.695 1.081 6.243 17 SER 7.635 1.938 9.930 18 HIS 4.177 1.349 11.351 19 LYS 3.017 4.823 12.306 20 ALA 1.025 4.475 9.106 21 ALA -1.640 3.347 11.545 22 GLN -2.565 7.012 11.370 23 CYS 0.043 8.612 9.141 24 GLU -0.709 12.249 8.416 25 HIS 2.605 13.589 7.173 26 ASN 2.981 15.664 4.030 27 ASP 6.563 15.698 2.806 28 ARG 8.313 12.436 2.019 29 PRO 7.495 9.966 -0.764 30 LEU 4.155 8.207 -0.498 31 LYS 3.491 4.552 -1.225 32 ILE 0.617 2.136 -1.702 33 LEU -0.384 -1.044 0.090 34 LYS -3.238 -3.454 0.698 35 PRO -4.585 -5.827 3.357 36 ARG -2.003 -8.559 2.923 37 GLY -1.433 -10.338 -0.370 38 ARG 1.290 -12.959 -0.570 39 PRO 3.003 -14.426 -3.642 40 PRO 1.288 -16.844 -6.036 41 THR 4.072 -19.347 -5.483 42 THR 6.857 -18.390 -3.105 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C T T T T/S S S S C 10 H H H H H H H H T T 20 T T/S S S S S C S S S 30 S S S S S/S S S S S S/S 40 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E T T E E E E 10 E e T T T T T g G G 20 G G g S S e E 30 E E E S S 40 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 88.0 55.2 63.5 2 VAL 42.1 35.5 60.4 3 VAL 71.7 60.4 50.3 4 ILE 46.4 32.3 67.6 5 ASN 5.6 4.6 75.9 6 GLY 5.5 15.8 74.7 7 VAL 75.3 63.4 62.2 8 LYS 87.3 50.3 55.3 9 TYR 143.0 79.0 40.9 10 ALA 72.4 99.8 32.9 11 CYS 98.6 99.4 47.2 12 ASP 65.7 59.4 56.3 13 SER 43.8 52.4 67.3 14 CYS 99.0 99.8 43.6 15 ILE 130.6 91.0 45.2 16 LYS 35.1 20.2 86.9 17 SER 27.2 32.5 78.3 18 HIS 8.9 5.9 82.3 19 LYS 43.7 25.2 76.1 20 ALA 57.5 79.2 47.7 21 ALA 15.6 21.4 76.3 22 GLN 18.1 12.2 81.5 23 CYS 95.5 96.3 47.5 24 GLU 2.2 1.6 87.0 25 HIS 86.6 57.7 68.1 26 ASN 0.0 0.0 91.0 27 ASP 0.0 0.0 84.4 28 ARG 108.1 51.8 64.9 29 PRO 33.2 26.7 71.0 30 LEU 77.1 52.2 65.7 31 LYS 82.1 47.4 67.3 32 ILE 51.5 35.9 58.8 33 LEU 60.5 40.9 67.7 34 LYS 59.8 34.5 69.7 35 PRO 50.4 40.5 67.0 36 ARG 7.0 3.4 91.6 37 GLY 0.0 0.0 81.8 38 ARG 36.0 17.2 85.5 39 PRO 58.4 46.9 61.1 40 PRO 11.5 9.3 84.1 41 THR 8.8 8.2 81.9 42 THR 4.4 4.1 71.3