Residue-by-residue listing for refined_13 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.7 - - - 2 SER 2 l - - -54.6 - - - - - - - 180.5 - 32.9 - 3 ASP 3 B - 182.5 - - - - - - - - 183.0 - 34.3 - 4 PRO 4 - - - - - -79.0 - - - - - 182.8 - 38.7 - * * * 5 GLY 5 h - - - - - - - - - - - 180.1 - - - 6 PRO 6 H - - - - - -56.8 -56.8 -32.5 - - - 178.7 - 38.6 - * * 7 GLU 7 H A 56.6 - - 173.5 - -61.4 -41.9 - - - 180.7 - 32.9 - 8 ALA 8 H A - - - - - -75.2 -33.6 - - - 177.5 -.7 33.8 - +* +* 9 ALA 9 H A - - - - - -64.0 -44.4 - - - 175.6 -2.1 33.9 - 10 ARG 10 H A - 170.8 - 167.0 - -66.1 -33.3 - - - 177.0 -2.7 31.1 - 11 LEU 11 H A - 170.4 - - - -60.1 -45.3 - - - 176.2 -1.6 34.3 - 12 ARG 12 H A - - -59.5 177.5 - -60.3 -48.1 - - - 182.1 -2.3 36.5 - 13 PHE 13 H A - 181.7 - - - -59.7 -38.7 - - - 178.4 -2.4 35.0 - 14 ARG 14 H A - - -71.5 - - -89.1 -14.3 - - - 178.0 -2.8 32.5 - +* ** * ** 15 CYS 15 H A - 185.9 - - - -89.3 -7.9 - - - 180.5 -1.4 34.2 - ** +** +** 16 PHE 16 h B - 184.0 - - - - - - - - 175.4 -.8 34.8 - +* +* 17 HIS 17 B 77.3 - - - - - - - - - 174.6 - 33.9 - 18 TYR 18 B - 172.1 - - - - - - - - 180.1 -.9 31.7 - +* +* 19 GLU 19 g B 44.5 - - 183.8 - - - - - - 182.6 -.6 31.7 - * +* +* Residue-by-residue listing for refined_13 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 GLU 20 G A - - -53.3 - - - - - - - 180.7 -.6 34.0 - +* +* 21 ALA 21 G A - - - - - - - - - - 183.5 - 36.7 - 22 THR 22 G A - - -67.9 - - - - - - - 179.5 -1.8 36.5 - 23 GLY 23 h - - - - - - - - - - - 183.3 -1.1 - - * * 24 PRO 24 H - - - - - -84.9 -84.9 -30.7 - - - 184.9 - 39.0 - +* +* * +* 25 GLN 25 H A - 197.2 - 169.1 - -78.2 -27.7 - - - 174.2 - 33.8 - * * * * 26 GLU 26 H A - 186.0 - 179.6 - -74.9 -34.2 - - - 175.4 - 33.9 - 27 ALA 27 H A - - - - - -62.0 -44.2 - - - 176.6 -1.0 34.2 - * * 28 LEU 28 H A - - -63.7 180.9 - -58.2 -45.7 - - - 179.7 -2.4 34.3 - 29 ALA 29 H A - - - - - -56.2 -44.9 - - - 178.3 -1.9 33.8 - 30 GLN 30 H A - - -69.5 169.8 - -67.6 -47.5 - - - 178.4 -2.1 33.8 - 31 LEU 31 H A - - -71.1 171.9 - -61.7 -41.4 - - - 179.4 -3.3 33.7 - +* +* 32 ARG 32 H A - 182.6 - 175.6 - -63.6 -41.1 - - - 176.8 -3.5 34.2 - +* +* 33 GLU 33 H A - 179.8 - 181.9 - -63.8 -50.0 - - - 179.7 -1.8 35.6 - 34 LEU 34 H A - - -61.5 176.6 - -62.6 -43.0 - - - 180.9 -3.0 34.0 - * * 35 CYS 35 H A 70.7 - - - - -68.9 -31.2 - - - 177.5 -3.5 33.2 - +* +* 36 ARG 36 H A - 175.0 - - - -70.9 -30.4 - - - 176.0 -1.8 31.4 - 37 GLN 37 H A - - -64.0 179.7 - -70.9 -19.0 - - - 181.6 -1.6 34.9 - +* +* 38 TRP 38 H a - 165.6 - - - -96.4 -59.5 - - - 180.9 -.7 35.3 - * +** +* +* +** 39 LEU 39 H A - - -63.8 158.4 - -70.7 -44.0 - - - 178.8 -3.8 34.7 - * ** ** 40 ARG 40 h l - - -58.0 181.5 - - - - - - 180.8 -1.1 31.9 - * * 41 PRO 41 T - - - - - -60.7 - - - - - 179.4 - 38.6 - * * 42 GLU 42 T A - 184.3 - - - - - - - - 183.1 - 34.1 - 43 VAL 43 T A - - -60.2 - - - - - - - 180.2 -1.0 32.4 - * * 44 ARG 44 t B - - -68.8 188.1 - - - - - - 181.9 -3.6 29.8 - ** * ** 45 SER 45 h B - - -49.3 - - - - - - - 178.4 - 37.1 - * * 46 LYS 46 H A - - -61.6 167.6 - -51.9 -44.5 - - - 182.9 - 37.0 - * * 47 GLU 47 H A - - -60.7 181.9 - -62.1 -29.9 - - - 180.8 - 34.9 - 48 GLN 48 H A - - -60.0 - - -73.8 -31.4 - - - 179.6 -.9 33.8 - +* +* 49 MET 49 H A - - -61.1 179.4 - -66.3 -34.2 - - - 173.7 -1.1 33.0 - * * * 50 LEU 50 H A - - -77.2 - - -52.2 -52.5 - - - 182.4 -1.1 34.2 - * * * * 51 GLU 51 H A - 178.8 - 174.8 - -58.6 -43.0 - - - 178.5 -1.0 33.3 - * * 52 LEU 52 H A - - -65.6 177.4 - -64.7 -44.5 - - - 178.1 -1.5 33.2 - 53 LEU 53 H A - 174.5 - - - -62.7 -39.9 - - - 180.9 -2.8 34.9 - * * Residue-by-residue listing for refined_13 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 54 VAL 54 H A - 187.1 - - - -58.1 -43.3 - - - 179.4 -2.7 33.7 - 55 LEU 55 H A - 182.6 - - - -56.2 -48.0 - - - 182.5 -1.6 35.4 - 56 GLU 56 H A - - -60.6 - - -54.6 -50.0 - - - 180.9 -1.5 33.5 - 57 GLN 57 H A - 205.8 - - - -74.8 -42.1 - - - 182.6 -1.8 34.5 - * * 58 PHE 58 H A - 177.4 - - - -53.4 -44.2 - - - 179.9 -3.0 33.7 - * * * 59 LEU 59 H A - - -61.1 190.9 - -65.6 -35.0 - - - 181.1 -2.8 31.1 - * * 60 GLY 60 H - - - - - - -80.3 -22.9 - - - 177.9 -1.0 - - * * * * 61 ALA 61 H A - - - - - -67.6 -27.3 - - - 177.4 -2.1 33.7 - * * 62 LEU 62 h B - - -64.0 170.4 - - - - - - 174.5 -.9 37.4 - * * * 63 PRO 63 h - - - - - -69.2 - - - - - 181.6 - 39.5 - +* +* 64 PRO 64 H - - - - - -42.6 -42.6 -43.2 - - - 181.7 - 38.6 - ** +* * ** 65 GLU 65 H A 64.5 - - 191.1 - -65.2 -47.3 - - - 179.3 - 32.7 - 66 ILE 66 H A - - -61.3 180.6 - -71.0 -38.8 - - - 180.3 - 34.8 - 67 GLN 67 H A - 179.7 - 178.2 - -62.6 -42.7 - - - 178.7 -3.4 33.9 - +* +* 68 ALA 68 H A - - - - - -60.2 -36.3 - - - 178.2 -2.7 33.6 - 69 ARG 69 H A - - -59.7 - - -59.8 -48.8 - - - 180.3 -1.2 35.3 - * * 70 VAL 70 H A - 178.6 - - - -68.8 -42.1 - - - 183.9 -1.7 35.5 - 71 GLN 71 H A - 207.7 - - - -54.4 -37.2 - - - 180.4 -3.2 37.2 - * +* +* 72 GLY 72 H - - - - - - -75.2 -40.1 - - - 183.2 -1.7 - - 73 GLN 73 H A - - -48.1 193.7 - -80.8 -41.2 - - - 183.4 -1.3 35.5 - * * * * 74 ARG 74 h l - 199.4 - - - - - - - - 180.7 -3.8 31.3 - ** ** 75 PRO 75 - - - - - -62.2 - - - - - 178.1 - 39.6 - +* +* 76 GLY 76 - - - - - - - - - - - 178.1 - - - 77 SER 77 h B 52.2 - - - - - - - - - 182.6 - 33.3 - 78 PRO 78 H - - - - - -52.0 -52.0 -44.9 - - - 185.1 - 39.4 - * * +* +* 79 GLU 79 H A - - -60.8 172.1 - -71.5 -30.6 - - - 176.3 - 32.4 - 80 GLU 80 H A - 181.8 - - - -71.5 -44.4 - - - 177.0 - 35.1 - 81 ALA 81 H A - - - - - -60.5 -43.0 - - - 178.9 -2.5 34.6 - 82 ALA 82 H A - - - - - -58.8 -37.2 - - - 178.9 -3.0 34.1 - * * 83 ALA 83 H A - - - - - -74.2 -34.3 - - - 179.4 -1.4 33.5 - 84 LEU 84 H A - - -46.1 179.1 - -64.8 -50.0 - - - 183.7 -1.9 37.4 - * * * 85 VAL 85 H A - - -56.5 - - -71.3 -30.8 - - - 175.5 -2.7 30.9 - 86 ASP 86 H A - 182.0 - - - -53.0 -39.1 - - - 175.7 -1.6 34.8 - * * 87 GLY 87 H - - - - - - -84.7 -39.7 - - - 181.6 -1.2 - - +* * +* 88 LEU 88 H A - - -62.0 174.2 - -58.3 -28.0 - - - 181.1 -2.3 33.8 - * * 89 ARG 89 h A 56.7 - - 180.1 - - - - - - 182.8 -2.2 32.9 - 90 ARG 90 t l - - -73.7 - - - - - - - 177.8 -1.4 32.0 - Residue-by-residue listing for refined_13 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 91 GLU 91 B - - -61.9 190.0 - - - - - - 185.4 - 31.8 - 92 PRO 92 S - - - - - -76.0 - - - - - 177.8 - 38.5 - * * 93 GLY 93 - - - - - - - - - - - 179.2 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 181.2 - - - 96 SER 302 l - - -55.8 - - - - - - - 182.5 - 32.4 - 97 ASP 303 B - 187.2 - - - - - - - - 179.7 - 34.6 - 98 PRO 304 - - - - - -62.5 - - - - - 182.3 - 38.7 - * * 99 GLY 305 h - - - - - - - - - - - 181.0 - - - 100 PRO 306 H - - - - - -55.4 -55.4 -34.3 - - - 178.6 - 38.6 - * * 101 GLU 307 H A 52.6 - - 179.2 - -62.9 -46.9 - - - 180.1 - 33.2 - 102 ALA 308 H A - - - - - -73.9 -34.7 - - - 177.5 - 33.8 - 103 ALA 309 H A - - - - - -60.0 -49.7 - - - 177.7 -2.8 34.7 - * * 104 ARG 310 H A - 171.8 - 169.1 - -62.0 -37.0 - - - 180.4 -2.9 33.2 - * * 105 LEU 311 H A - 173.6 - - - -61.3 -51.0 - - - 180.1 -1.8 35.1 - * * 106 ARG 312 H A - - -59.7 175.4 - -66.4 -34.9 - - - 177.3 -2.7 34.7 - 107 PHE 313 H A - 168.9 - - - -63.9 -48.9 - - - 177.1 -2.4 33.7 - 108 ARG 314 H A - - -66.2 186.1 - -71.7 -30.9 - - - 180.8 -3.1 33.5 - * * 109 CYS 315 h A - 183.5 - - - - - - - - 177.3 -2.3 33.9 - 110 PHE 316 t B - 181.5 - - - - - - - - 178.3 -.8 34.5 - +* +* 111 HIS 317 B 72.4 - - - - - - - - - 175.9 - 34.2 - 112 TYR 318 B - 169.2 - - - - - - - - 179.2 -1.1 32.0 - * * 113 GLU 319 t B 48.8 - - 179.3 - - - - - - 180.0 -.6 32.6 - +* +* 114 GLU 320 T A - - -51.9 - - - - - - - 179.8 -.6 34.5 - +* +* 115 ALA 321 T A - - - - - - - - - - 180.7 - 33.5 - 116 THR 322 T A - 202.6 - - - - - - - - 182.4 -1.7 34.6 - * * 117 GLY 323 h - - - - - - - - - - - 182.7 -1.0 - - * * 118 PRO 324 H - - - - - -61.6 -61.6 -31.5 - - - 179.6 - 38.1 - * * 119 GLN 325 H A - - -81.1 - - -72.1 -41.5 - - - 177.5 - 32.7 - 120 GLU 326 H A - 182.2 - 171.9 - -68.5 -33.5 - - - 174.4 - 33.1 - 121 ALA 327 H A - - - - - -62.0 -42.2 - - - 176.7 -2.4 34.0 - 122 LEU 328 H A - - -63.8 180.9 - -59.8 -42.7 - - - 179.6 -2.0 34.1 - 123 ALA 329 H A - - - - - -57.5 -39.9 - - - 177.5 -1.8 34.1 - 124 GLN 330 H A - - -71.8 166.6 - -69.2 -51.6 - - - 178.3 -1.6 34.1 - * * 125 LEU 331 H A - - -73.2 166.4 - -59.6 -38.3 - - - 184.5 -3.0 34.8 - * * 126 ARG 332 H A - 185.1 - 172.1 - -63.9 -45.8 - - - 179.2 -3.3 31.7 - +* +* 127 GLU 333 H A 80.3 - - 176.6 - -69.5 -38.0 - - - 179.1 -1.4 30.5 - * * 128 LEU 334 H A - - -62.7 176.9 - -60.4 -46.4 - - - 178.3 -1.9 33.5 - Residue-by-residue listing for refined_13 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 129 CYS 335 H A 64.5 - - - - -66.4 -30.5 - - - 177.3 -3.3 32.4 - +* +* 130 ARG 336 H A - 176.5 - - - -73.2 -30.6 - - - 175.2 -1.8 30.4 - 131 GLN 337 H A - - -56.0 183.1 - -65.1 -25.6 - - - 182.3 -2.0 37.1 - * * 132 TRP 338 H a - 160.4 - - - -90.9 -60.7 - - - 180.6 -.9 31.7 - * ** +* * ** 133 LEU 339 H A - - -60.5 181.3 - -67.7 -44.3 - - - 180.2 -3.4 33.4 - +* +* 134 ARG 340 h l - - -58.5 188.3 - - - - - - 176.8 -1.2 30.2 - * * * 135 PRO 341 T - - - - - -63.2 - - - - - 175.8 - 38.3 - * * 136 GLU 342 T A - 179.9 - - - - - - - - 184.6 - 35.0 - 137 VAL 343 T A - - -59.2 - - - - - - - 183.5 -1.2 32.2 - * * 138 ARG 344 t B - - -67.5 188.3 - - - - - - 176.9 -3.5 30.3 - ** * ** 139 SER 345 h B - - -53.6 - - - - - - - 179.9 - 36.8 - 140 LYS 346 H A - - -64.7 170.6 - -59.3 -43.8 - - - 183.2 - 35.9 - 141 GLU 347 H A - - -49.3 - - -53.9 -43.0 - - - 179.7 - 36.1 - * * 142 GLN 348 H A - - -55.4 - - -62.6 -35.1 - - - 179.4 - 34.4 - 143 MET 349 H A - - -59.0 180.3 - -68.7 -37.9 - - - 172.7 -1.0 33.0 - * * * 144 LEU 350 H A - - -76.2 - - -55.5 -53.4 - - - 183.5 -1.7 35.6 - * * 145 GLU 351 H A - 185.7 - 181.3 - -57.6 -49.1 - - - 178.9 -2.2 34.9 - 146 LEU 352 H A - - -64.4 176.5 - -59.5 -45.9 - - - 180.9 -2.8 33.7 - * * 147 LEU 353 H A - 177.1 - - - -70.7 -30.0 - - - 173.8 -2.6 30.9 - * * 148 VAL 354 H A - 182.6 - - - -60.4 -45.3 - - - 179.5 -2.5 34.6 - 149 LEU 355 H A - 180.9 - - - -57.4 -45.2 - - - 179.9 -2.0 34.9 - 150 GLU 356 H A - - -56.7 - - -54.2 -48.6 - - - 180.9 -1.7 33.5 - 151 GLN 357 H A - 202.6 - - - -74.3 -45.4 - - - 183.6 -1.8 35.3 - * * 152 PHE 358 H A - 177.6 - - - -53.1 -44.8 - - - 179.9 -3.4 33.4 - * +* +* 153 LEU 359 H A - - -62.1 190.6 - -64.0 -35.9 - - - 179.6 -2.9 30.9 - * * 154 GLY 360 H - - - - - - -81.2 -18.4 - - - 176.3 -1.0 - - * +* * +* 155 ALA 361 H A - - - - - -72.8 -27.5 - - - 175.6 -1.8 33.4 - * * 156 LEU 362 h B - - -63.6 172.5 - - - - - - 175.7 -1.2 37.0 - * * 157 PRO 363 h - - - - - -68.8 - - - - - 179.6 - 39.5 - +* +* 158 PRO 364 H - - - - - -39.9 -39.9 -41.9 - - - 180.0 - 38.9 - ** ** * ** 159 GLU 365 H A 54.4 - - 177.4 - -66.6 -47.4 - - - 178.6 - 31.9 - 160 ILE 366 H A - - -62.2 180.6 - -70.5 -40.3 - - - 179.9 -.5 34.7 - +* +* 161 GLN 367 H A - 179.3 - 177.3 - -61.5 -39.9 - - - 178.7 -3.5 34.5 - +* +* 162 ALA 368 H A - - - - - -61.4 -38.7 - - - 179.3 -2.2 34.0 - Residue-by-residue listing for refined_13 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 163 ARG 369 H A - - -57.4 - - -64.2 -41.2 - - - 176.8 -1.2 34.7 - * * 164 VAL 370 H A - 172.1 - - - -61.2 -47.7 - - - 181.8 -1.8 34.8 - 165 GLN 371 H A - - -100.5 - - -64.2 -29.7 - - - 176.7 -2.6 30.3 - ** * ** 166 GLY 372 H - - - - - - -68.7 -40.4 - - - 180.6 -1.9 - - 167 GLN 373 H A - - -57.9 187.2 - -86.7 -37.3 - - - 180.6 -1.6 34.8 - +* +* 168 ARG 374 h l - 203.2 - - - - - - - - 180.9 -3.6 31.6 - * ** ** 169 PRO 375 - - - - - -66.3 - - - - - 179.4 - 39.2 - +* +* 170 GLY 376 - - - - - - - - - - - 177.7 - - - 171 SER 377 h B 56.1 - - - - - - - - - 181.1 - 34.0 - 172 PRO 378 H - - - - - -51.9 -51.9 -44.9 - - - 185.5 - 39.7 - * * +* +* 173 GLU 379 H A - - -63.8 169.0 - -74.4 -30.0 - - - 175.2 - 31.9 - 174 GLU 380 H A - 184.4 - - - -71.1 -43.7 - - - 176.5 - 34.8 - 175 ALA 381 H A - - - - - -58.2 -42.2 - - - 177.7 -2.7 34.2 - 176 ALA 382 H A - - - - - -55.6 -47.8 - - - 179.9 -2.5 34.4 - 177 ALA 383 H A - - - - - -62.8 -38.3 - - - 181.4 -1.9 33.7 - 178 LEU 384 H A - - -42.1 181.5 - -67.5 -50.0 - - - 186.5 -2.0 37.3 - +* * +* 179 VAL 385 H A - - -58.5 - - -73.1 -31.1 - - - 176.8 -3.0 29.9 - * * * 180 ASP 386 H A - 185.4 - - - -56.7 -37.9 - - - 175.5 -2.6 33.8 - 181 GLY 387 H - - - - - - -73.5 -47.5 - - - 181.1 -1.0 - - * * 182 LEU 388 H A - - -60.2 175.7 - -56.8 -31.0 - - - 183.1 -2.1 34.8 - 183 ARG 389 h A 63.6 - - 181.5 - - - - - - 177.1 -2.5 33.4 - 184 ARG 390 t ~l - - -77.7 - - - - - - - 169.2 -1.9 30.8 - ** +* ** 185 GLU 391 B - - -67.6 196.6 - - - - - - 177.0 - 32.7 - * * 186 PRO 392 S - - - - - -62.5 - - - - - 179.7 - 38.5 - * * 187 GLY 393 - - - - - - - - - - - 180.9 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * ** * ** +** +** +* ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.0 182.1 -62.4 178.4 -62.0 -65.2 -39.7 - - - 179.5 -2.0 34.3 Standard deviations: 10.6 10.2 8.8 7.4 11.6 9.4 8.5 - - - 2.7 .9 2.2 Numbers of values: 15 50 67 63 18 125 125 0 0 0 186 125 170 0 Residue-by-residue listing for refined_13 Page 7 ---------------------------------------- KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_13 Page 8 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.229 1.494 - 1.459 - 116.08 119.59 - 111.39 - 124.32 * * 2 SER 2 1.334 1.229 1.534 1.542 1.460 124.03 116.65 120.96 111.03 111.58 111.24 122.34 * * 3 ASP 3 1.309 1.229 1.519 1.530 1.453 121.32 117.97 120.25 110.32 109.20 110.70 121.77 * * 4 PRO 4 1.338 1.240 1.534 1.529 1.467 122.58 116.87 120.62 110.43 113.63 102.91 122.50 5 GLY 5 1.314 1.241 1.516 - 1.429 120.72 118.54 119.87 - 111.14 - 121.59 * * * * 6 PRO 6 1.350 1.236 1.527 1.530 1.476 122.68 115.96 120.96 109.93 111.87 103.93 123.07 7 GLU 7 1.327 1.234 1.539 1.536 1.450 121.98 116.36 120.65 110.82 111.66 111.40 122.95 8 ALA 8 1.330 1.228 1.511 1.516 1.455 122.13 115.68 121.12 110.58 109.98 110.83 123.20 9 ALA 9 1.319 1.233 1.523 1.504 1.446 121.86 116.12 121.00 111.01 109.81 110.12 122.86 10 ARG 10 1.330 1.224 1.520 1.525 1.445 121.28 116.89 120.39 111.88 111.65 112.78 122.71 * * 11 LEU 11 1.326 1.213 1.526 1.523 1.413 122.11 116.38 120.29 112.01 109.45 109.14 123.27 ** * ** 12 ARG 12 1.332 1.229 1.525 1.522 1.470 122.39 114.21 121.69 107.28 109.67 110.07 124.09 * * 13 PHE 13 1.314 1.224 1.546 1.533 1.454 125.05 116.75 120.71 112.52 111.80 106.60 122.54 * * +* * ** ** 14 ARG 14 1.319 1.232 1.529 1.537 1.462 122.22 117.14 120.65 110.92 112.60 111.46 122.21 Residue-by-residue listing for refined_13 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.312 1.230 1.523 1.544 1.456 121.29 115.53 121.30 110.71 109.19 110.65 123.16 * * 16 PHE 16 1.316 1.241 1.518 1.536 1.435 122.26 116.42 120.63 110.00 110.25 110.26 122.93 * * 17 HIS 17 1.311 1.237 1.502 1.572 1.445 120.37 117.90 119.76 109.49 107.16 113.41 122.31 * * ** * +* ** 18 TYR 18 1.288 1.224 1.509 1.530 1.419 118.75 114.97 121.20 112.61 108.75 112.62 123.71 +** ** +* * * +** 19 GLU 19 1.291 1.230 1.520 1.549 1.417 122.88 114.87 121.25 114.35 110.61 110.29 123.82 +** ** ** +** 20 GLU 20 1.334 1.212 1.522 1.544 1.473 124.37 115.74 120.56 108.18 112.11 112.32 123.66 * * * * 21 ALA 21 1.320 1.231 1.532 1.516 1.481 124.44 114.52 121.99 108.45 111.71 108.03 123.49 * +* * +* +* 22 THR 22 1.280 1.236 1.532 1.492 1.420 124.93 115.56 121.63 112.81 111.79 103.98 122.75 *** +* ** +* +* **** **** 23 GLY 23 1.300 1.237 1.503 - 1.428 120.73 119.08 120.19 - 110.60 - 120.73 ** * * * ** 24 PRO 24 1.322 1.218 1.509 1.503 1.435 121.11 115.83 121.21 110.36 112.44 102.84 122.95 * * ** ** 25 GLN 25 1.296 1.235 1.524 1.496 1.400 122.36 116.75 120.65 114.09 109.98 107.33 122.57 ** +* *** ** +* *** 26 GLU 26 1.344 1.237 1.516 1.523 1.448 120.04 115.11 121.59 109.89 107.84 112.02 123.30 * * * 27 ALA 27 1.322 1.218 1.519 1.519 1.443 122.29 116.12 120.46 110.82 109.13 110.39 123.41 28 LEU 28 1.336 1.207 1.504 1.526 1.464 122.47 116.86 119.91 108.10 111.24 112.21 123.23 * * * * 29 ALA 29 1.329 1.238 1.523 1.522 1.459 121.83 115.28 120.96 110.67 110.31 110.53 123.72 30 GLN 30 1.321 1.225 1.520 1.500 1.442 123.00 116.45 120.44 111.38 112.08 109.22 123.10 * * 31 LEU 31 1.327 1.209 1.507 1.531 1.467 123.00 116.44 120.35 110.20 111.77 110.89 123.21 * * 32 ARG 32 1.313 1.227 1.512 1.520 1.450 122.64 115.11 121.30 111.11 109.95 109.71 123.57 * * 33 GLU 33 1.297 1.225 1.541 1.521 1.436 123.21 116.35 120.51 111.92 109.28 107.01 123.07 ** * ** ** 34 LEU 34 1.332 1.228 1.526 1.536 1.467 122.69 116.84 120.50 109.71 111.69 110.88 122.65 35 CYS 35 1.329 1.208 1.522 1.545 1.448 120.97 116.83 120.68 110.69 109.86 111.85 122.49 * * 36 ARG 36 1.328 1.210 1.526 1.550 1.425 121.98 116.79 120.32 114.91 110.73 110.06 122.88 * * +* +** +** 37 GLN 37 1.322 1.238 1.537 1.512 1.464 122.31 114.24 121.70 110.10 110.81 109.24 124.05 38 TRP 38 1.314 1.232 1.544 1.546 1.453 125.62 115.92 120.99 112.49 111.91 106.35 123.10 * ** * ** ** 39 LEU 39 1.311 1.226 1.520 1.539 1.458 123.52 115.71 120.38 111.61 110.55 108.56 123.90 * * * * 40 ARG 40 1.337 1.230 1.533 1.541 1.465 124.17 117.84 120.47 110.65 112.88 112.43 121.69 * * * 41 PRO 41 1.353 1.229 1.523 1.537 1.475 123.29 116.24 120.91 110.12 112.63 103.75 122.85 42 GLU 42 1.311 1.232 1.524 1.534 1.443 121.67 116.80 121.02 110.11 110.17 110.94 122.15 * * 43 VAL 43 1.316 1.231 1.523 1.552 1.451 120.14 117.59 120.35 110.40 112.67 112.26 122.02 44 ARG 44 1.314 1.233 1.482 1.523 1.440 119.71 113.71 121.71 111.55 112.79 114.42 124.56 * ** * * ** ** Residue-by-residue listing for refined_13 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 45 SER 45 1.287 1.243 1.532 1.518 1.413 123.90 115.54 120.70 110.08 109.93 106.73 123.75 +** ** * ** +** 46 LYS 46 1.320 1.219 1.530 1.526 1.472 124.32 115.26 121.37 108.55 110.50 107.94 123.32 * +* +* 47 GLU 47 1.321 1.231 1.505 1.502 1.474 123.74 115.02 121.46 109.27 112.63 109.53 123.53 * * * 48 GLN 48 1.287 1.239 1.525 1.533 1.449 122.16 115.81 120.96 110.78 110.70 110.52 123.22 *** *** 49 MET 49 1.325 1.234 1.513 1.511 1.455 122.40 115.94 120.35 111.73 111.30 110.28 123.71 50 LEU 50 1.343 1.211 1.510 1.564 1.472 122.52 116.79 119.97 108.81 110.58 112.30 123.15 * * +* * +* 51 GLU 51 1.333 1.231 1.535 1.528 1.429 122.48 116.75 120.64 111.85 111.73 109.84 122.59 +* +* 52 LEU 52 1.317 1.231 1.522 1.522 1.438 121.19 116.16 120.42 111.58 111.09 110.45 123.40 * * 53 LEU 53 1.324 1.241 1.546 1.498 1.429 122.81 117.61 119.85 110.69 113.23 107.90 122.54 +* +* +* +* 54 VAL 54 1.340 1.230 1.529 1.564 1.472 120.91 115.36 120.77 108.45 109.79 113.50 123.84 * * 55 LEU 55 1.332 1.236 1.521 1.560 1.468 123.58 115.05 120.82 111.04 109.80 108.46 124.12 +* * * +* 56 GLU 56 1.317 1.235 1.540 1.538 1.453 123.32 117.57 120.23 110.89 112.53 110.23 122.20 57 GLN 57 1.330 1.224 1.531 1.534 1.464 119.88 116.19 120.64 109.61 108.72 111.18 123.14 * * 58 PHE 58 1.341 1.235 1.516 1.547 1.465 122.29 116.42 120.55 110.15 111.26 111.22 123.01 59 LEU 59 1.318 1.219 1.512 1.525 1.444 120.49 117.38 120.03 111.61 113.27 112.40 122.54 * * 60 GLY 60 1.317 1.230 1.503 - 1.445 119.28 115.96 120.75 - 111.85 - 123.29 61 ALA 61 1.321 1.230 1.530 1.526 1.448 122.24 115.99 120.73 110.95 110.44 110.45 123.28 62 LEU 62 1.321 1.243 1.540 1.523 1.460 123.64 118.31 120.17 107.78 110.72 108.01 121.52 * * * * * 63 PRO 63 1.354 1.237 1.518 1.541 1.459 121.95 118.52 118.95 109.00 108.46 104.33 122.53 * * * * * 64 PRO 64 1.349 1.220 1.539 1.523 1.476 123.68 116.88 120.34 110.45 114.01 102.78 122.75 65 GLU 65 1.327 1.234 1.547 1.532 1.461 121.62 117.13 120.19 111.77 111.95 110.50 122.66 * * 66 ILE 66 1.341 1.237 1.525 1.554 1.451 121.88 115.39 121.29 109.74 109.82 110.69 123.30 67 GLN 67 1.316 1.227 1.521 1.519 1.444 122.58 116.27 120.37 110.67 110.88 110.31 123.36 68 ALA 68 1.329 1.233 1.520 1.521 1.461 122.62 116.15 120.56 110.40 111.09 110.91 123.27 69 ARG 69 1.332 1.236 1.523 1.528 1.465 122.02 115.20 121.45 108.28 109.46 111.03 123.34 70 VAL 70 1.317 1.218 1.508 1.535 1.449 122.64 114.97 120.94 107.75 110.80 111.25 124.09 71 GLN 71 1.307 1.230 1.538 1.524 1.458 124.89 115.85 121.00 109.11 109.79 107.27 123.13 +* +* +* +* 72 GLY 72 1.328 1.234 1.521 - 1.442 121.20 117.34 119.86 - 113.60 - 122.79 73 GLN 73 1.335 1.232 1.511 1.528 1.465 120.79 113.23 121.81 108.03 109.44 111.15 124.96 * * * * 74 ARG 74 1.315 1.227 1.539 1.523 1.445 127.13 117.26 120.94 111.02 111.46 113.35 121.75 *** +* *** 75 PRO 75 1.341 1.233 1.526 1.536 1.480 123.17 114.83 121.65 109.82 111.94 102.63 123.52 * * * 76 GLY 76 1.310 1.236 1.515 - 1.440 122.17 116.44 120.55 - 113.06 - 122.98 * * 77 SER 77 1.301 1.247 1.533 1.523 1.427 121.95 117.13 120.34 112.42 110.30 109.73 122.48 ** +* * ** 78 PRO 78 1.354 1.213 1.522 1.527 1.473 123.76 116.74 120.42 108.77 114.17 103.61 122.83 Residue-by-residue listing for refined_13 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 79 GLU 79 1.309 1.230 1.527 1.517 1.463 121.99 116.56 120.59 113.18 112.40 109.20 122.82 * +* +* 80 GLU 80 1.322 1.220 1.525 1.535 1.432 122.05 115.83 120.77 111.58 107.11 109.03 123.32 * * * 81 ALA 81 1.350 1.228 1.520 1.508 1.453 122.50 115.71 120.79 109.75 110.63 110.19 123.50 * * 82 ALA 82 1.326 1.205 1.519 1.531 1.452 123.26 116.04 120.97 110.81 110.65 110.12 122.99 * * 83 ALA 83 1.296 1.237 1.533 1.515 1.452 122.80 116.86 120.42 110.82 111.40 110.45 122.72 ** ** 84 LEU 84 1.340 1.228 1.513 1.542 1.468 121.01 114.55 121.89 105.40 107.66 111.29 123.47 ** * ** 85 VAL 85 1.321 1.231 1.510 1.539 1.440 122.53 115.31 120.90 112.27 111.57 112.94 123.79 * * 86 ASP 86 1.324 1.226 1.522 1.530 1.459 123.57 116.02 120.89 110.22 109.91 109.84 123.08 * * 87 GLY 87 1.319 1.228 1.525 - 1.438 120.77 116.52 120.66 - 111.97 - 122.82 88 LEU 88 1.334 1.219 1.525 1.527 1.485 123.21 117.06 120.25 109.14 113.37 110.98 122.69 * * 89 ARG 89 1.313 1.223 1.534 1.531 1.461 121.51 117.03 119.60 110.56 113.02 111.03 123.36 * * 90 ARG 90 1.339 1.240 1.538 1.561 1.488 122.81 116.72 120.81 109.23 112.25 114.01 122.42 +* +* ** ** 91 GLU 91 1.316 1.230 1.530 1.553 1.453 122.01 118.24 120.33 112.07 109.57 112.57 121.43 * * * * * 92 PRO 92 1.344 1.232 1.540 1.525 1.471 123.02 117.49 120.08 110.37 114.75 102.90 122.42 * * 93 GLY 93 1.320 1.240 1.509 - 1.444 120.22 116.28 120.66 - 110.86 - 123.03 94 GLY 94 1.309 1.238 1.515 - 1.452 120.94 - 120.43 - 112.25 - - * * 95 GLY 301 - 1.244 1.508 - 1.448 - 115.16 120.53 - 111.61 - 124.31 96 SER 302 1.328 1.235 1.526 1.539 1.457 124.19 115.85 121.52 111.74 111.00 111.50 122.56 * * 97 ASP 303 1.309 1.241 1.519 1.531 1.444 121.11 118.05 119.92 110.00 109.69 110.53 122.01 * * 98 PRO 304 1.349 1.230 1.527 1.538 1.468 122.75 116.51 120.83 109.77 112.23 104.13 122.63 * * 99 GLY 305 1.312 1.235 1.507 - 1.430 120.68 118.46 119.56 - 110.98 - 121.98 * * * 100 PRO 306 1.351 1.228 1.528 1.531 1.476 123.02 115.58 121.16 110.20 112.12 103.60 123.26 101 GLU 307 1.319 1.236 1.540 1.534 1.446 122.69 116.59 120.60 111.84 111.60 110.03 122.76 102 ALA 308 1.327 1.230 1.510 1.518 1.452 121.68 115.64 120.77 110.51 109.87 110.94 123.58 103 ALA 309 1.324 1.229 1.517 1.510 1.448 122.34 116.10 120.76 110.22 109.78 109.90 123.08 104 ARG 310 1.333 1.232 1.522 1.515 1.446 121.75 116.21 120.75 110.14 111.89 111.48 123.03 105 LEU 311 1.325 1.218 1.525 1.524 1.411 122.80 116.14 120.49 111.33 110.00 108.56 123.31 ** * ** 106 ARG 312 1.320 1.236 1.524 1.514 1.464 122.82 115.12 121.10 110.52 110.67 109.18 123.78 107 PHE 313 1.314 1.227 1.533 1.524 1.447 123.75 117.48 120.23 112.14 111.87 108.76 122.29 * * * * * 108 ARG 314 1.328 1.222 1.520 1.529 1.463 120.36 116.13 120.78 108.40 110.38 113.32 123.08 +* +* 109 CYS 315 1.324 1.235 1.534 1.542 1.459 122.66 116.41 120.99 110.99 111.14 110.07 122.61 110 PHE 316 1.319 1.243 1.522 1.537 1.434 122.08 116.37 120.89 110.68 109.26 110.18 122.73 * * Residue-by-residue listing for refined_13 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 111 HIS 317 1.310 1.231 1.500 1.568 1.442 120.44 117.74 119.82 109.85 107.56 112.44 122.44 * * +* * * +* 112 TYR 318 1.297 1.229 1.503 1.529 1.426 119.20 114.84 121.43 112.21 109.29 112.38 123.66 ** * +* * * * ** 113 GLU 319 1.282 1.238 1.513 1.547 1.416 122.77 115.48 121.23 113.18 109.89 110.52 123.24 *** ** +* *** 114 GLU 320 1.320 1.223 1.520 1.546 1.455 123.27 114.82 121.28 108.83 109.68 111.90 123.86 115 ALA 321 1.321 1.239 1.536 1.520 1.450 123.92 117.87 119.95 110.70 112.93 110.11 122.18 * * 116 THR 322 1.335 1.213 1.545 1.587 1.452 119.89 116.29 121.07 110.42 108.91 110.78 122.53 +* * +* 117 GLY 323 1.326 1.227 1.522 - 1.447 121.24 119.43 119.77 - 110.68 - 120.80 * * * 118 PRO 324 1.344 1.224 1.537 1.508 1.469 122.41 117.72 120.13 110.25 114.34 103.52 122.14 * * * 119 GLN 325 1.332 1.231 1.510 1.550 1.464 120.27 115.07 121.40 109.48 109.08 114.15 123.51 ** ** 120 GLU 326 1.315 1.236 1.538 1.532 1.448 121.96 115.91 121.38 112.44 109.74 110.13 122.71 * * 121 ALA 327 1.324 1.231 1.524 1.522 1.453 122.26 116.15 120.63 110.56 109.89 110.52 123.21 122 LEU 328 1.337 1.205 1.507 1.529 1.462 122.14 116.68 120.00 108.30 110.82 112.47 123.32 * * * 123 ALA 329 1.327 1.240 1.529 1.518 1.468 122.12 115.21 121.22 110.45 110.66 110.14 123.55 124 GLN 330 1.319 1.228 1.527 1.505 1.441 122.91 116.03 120.84 111.66 111.28 108.78 123.09 * * * 125 LEU 331 1.329 1.219 1.511 1.533 1.471 122.96 116.25 120.52 109.04 112.10 110.34 123.22 126 ARG 332 1.310 1.239 1.508 1.516 1.438 122.07 118.18 119.67 111.80 112.91 111.59 122.14 * * * 127 GLU 333 1.328 1.211 1.522 1.547 1.442 117.32 116.43 119.94 111.68 109.31 114.96 123.51 * ** +** +** 128 LEU 334 1.346 1.229 1.527 1.537 1.468 122.60 117.07 120.47 110.14 111.32 111.28 122.46 * * 129 CYS 335 1.333 1.230 1.535 1.547 1.444 120.70 116.69 120.82 111.90 110.48 111.58 122.48 130 ARG 336 1.339 1.213 1.530 1.553 1.425 121.89 117.33 119.54 115.13 111.73 110.68 123.12 * +* +** +** 131 GLN 337 1.340 1.227 1.516 1.505 1.479 122.71 113.66 122.39 106.48 109.30 109.84 123.95 * * * +* +* 132 TRP 338 1.302 1.232 1.556 1.542 1.419 124.31 118.79 119.32 114.96 113.74 108.12 121.89 +* * ** * * +** * +** 133 LEU 339 1.340 1.223 1.526 1.548 1.480 119.94 115.11 120.97 109.21 110.23 112.77 123.92 * * * 134 ARG 340 1.327 1.228 1.529 1.537 1.462 124.78 117.69 120.67 111.41 114.62 113.03 121.63 +* * * +* 135 PRO 341 1.357 1.228 1.533 1.536 1.475 123.09 115.99 120.87 110.34 112.05 103.99 123.13 136 GLU 342 1.319 1.227 1.534 1.541 1.442 122.53 116.94 120.84 110.21 110.08 109.59 122.20 137 VAL 343 1.330 1.223 1.525 1.560 1.457 119.58 118.33 119.76 109.70 114.10 112.69 121.90 * * * * 138 ARG 344 1.321 1.236 1.506 1.536 1.464 119.13 114.49 121.33 110.50 114.05 114.13 124.18 * * ** ** 139 SER 345 1.316 1.242 1.533 1.528 1.440 124.19 115.78 120.70 109.22 109.39 108.01 123.51 * * * 140 LYS 346 1.319 1.210 1.521 1.523 1.463 123.44 115.58 120.79 109.17 111.06 108.85 123.61 * * 141 GLU 347 1.320 1.235 1.499 1.526 1.474 124.49 114.03 121.61 106.60 110.80 111.32 124.35 * +* * +* +* Residue-by-residue listing for refined_13 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 142 GLN 348 1.302 1.224 1.525 1.529 1.452 122.95 116.18 120.88 110.17 110.79 110.24 122.93 +* +* 143 MET 349 1.322 1.232 1.507 1.507 1.453 122.02 116.08 120.26 111.57 110.54 110.67 123.66 * * 144 LEU 350 1.352 1.210 1.508 1.567 1.469 121.69 115.38 120.66 107.27 108.55 112.41 123.83 +* * +* * * +* 145 GLU 351 1.335 1.238 1.538 1.524 1.429 123.83 116.43 120.67 111.19 111.22 108.36 122.89 +* * * +* 146 LEU 352 1.324 1.226 1.528 1.531 1.441 122.03 116.62 120.34 110.88 111.39 110.32 123.01 147 LEU 353 1.321 1.241 1.557 1.533 1.438 122.17 117.68 120.26 115.85 112.81 108.49 122.05 +* * *** * *** 148 VAL 354 1.342 1.228 1.528 1.565 1.475 120.85 115.16 121.11 107.49 108.53 113.50 123.72 * * 149 LEU 355 1.333 1.236 1.519 1.559 1.464 123.68 115.45 120.60 111.60 109.98 108.63 123.95 * * * * 150 GLU 356 1.318 1.239 1.531 1.539 1.463 122.61 116.91 120.46 109.83 111.75 111.51 122.63 151 GLN 357 1.327 1.218 1.526 1.533 1.460 120.61 116.24 120.51 109.03 108.50 110.64 123.21 152 PHE 358 1.342 1.237 1.512 1.546 1.465 122.40 116.58 120.33 109.78 111.64 111.83 123.08 153 LEU 359 1.319 1.218 1.514 1.528 1.441 120.12 117.15 119.99 111.94 112.56 112.64 122.83 * * 154 GLY 360 1.318 1.234 1.513 - 1.444 119.90 116.40 120.64 - 112.38 - 122.95 155 ALA 361 1.325 1.235 1.521 1.530 1.451 121.83 115.34 121.11 111.17 109.46 111.05 123.54 156 LEU 362 1.332 1.245 1.530 1.529 1.447 123.06 118.01 120.16 107.37 109.55 109.49 121.83 * * 157 PRO 363 1.337 1.234 1.521 1.535 1.453 122.00 118.04 119.21 108.93 109.31 104.23 122.74 * * 158 PRO 364 1.352 1.222 1.537 1.513 1.475 124.28 117.20 120.12 110.05 114.27 102.59 122.68 159 GLU 365 1.329 1.230 1.547 1.536 1.463 121.39 117.21 120.50 111.83 112.54 111.31 122.27 * * 160 ILE 366 1.333 1.236 1.531 1.552 1.455 121.72 115.20 121.42 110.13 109.94 110.29 123.37 161 GLN 367 1.312 1.234 1.534 1.523 1.447 123.24 116.13 120.80 110.96 110.99 109.19 123.05 * * 162 ALA 368 1.318 1.230 1.522 1.515 1.462 122.19 116.07 120.97 110.21 110.98 110.52 122.94 163 ARG 369 1.325 1.237 1.522 1.526 1.464 121.56 115.46 121.28 109.18 109.45 111.09 123.26 164 VAL 370 1.328 1.209 1.500 1.538 1.450 122.27 116.21 120.41 108.05 110.50 112.08 123.38 * * * 165 GLN 371 1.304 1.229 1.528 1.537 1.443 121.85 116.70 120.25 113.71 112.86 111.57 123.03 +* +* +* 166 GLY 372 1.323 1.233 1.535 - 1.453 120.88 116.87 120.53 - 112.68 - 122.59 * * 167 GLN 373 1.331 1.223 1.516 1.518 1.470 121.41 113.69 121.80 109.51 110.36 110.23 124.51 * * 168 ARG 374 1.306 1.232 1.549 1.526 1.449 126.99 117.05 120.85 110.82 112.08 112.81 122.07 +* * +** * +** 169 PRO 375 1.350 1.220 1.536 1.534 1.480 123.27 116.01 121.02 109.81 112.98 103.00 122.97 170 GLY 376 1.320 1.234 1.526 - 1.446 121.76 117.07 120.36 - 113.49 - 122.55 171 SER 377 1.306 1.246 1.532 1.530 1.440 121.57 117.74 119.97 111.39 109.71 109.97 122.25 +* +* 172 PRO 378 1.359 1.220 1.519 1.529 1.476 123.31 115.94 120.92 108.53 113.38 103.51 123.11 * * 173 GLU 379 1.303 1.232 1.518 1.502 1.446 122.45 116.85 120.47 113.75 112.99 109.13 122.68 +* * +* +* 174 GLU 380 1.320 1.219 1.521 1.531 1.432 121.03 115.86 120.91 110.85 107.15 110.20 123.18 * * * Residue-by-residue listing for refined_13 Page 14 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 175 ALA 381 1.350 1.224 1.520 1.516 1.450 122.18 115.82 120.42 110.20 110.25 110.46 123.75 * * 176 ALA 382 1.334 1.223 1.515 1.521 1.454 123.22 115.82 120.75 110.10 110.65 110.26 123.40 177 ALA 383 1.309 1.237 1.528 1.523 1.448 122.52 116.83 120.35 110.52 111.47 110.55 122.80 * * 178 LEU 384 1.337 1.234 1.524 1.544 1.463 120.97 114.67 121.88 105.29 108.58 111.43 123.38 +** +** 179 VAL 385 1.322 1.221 1.504 1.541 1.441 122.27 117.07 119.91 111.65 113.47 113.93 123.01 * * * * 180 ASP 386 1.326 1.223 1.519 1.528 1.467 121.56 115.49 121.14 110.04 109.32 111.57 123.33 181 GLY 387 1.319 1.231 1.521 - 1.434 121.00 115.91 120.99 - 110.99 - 123.07 * * 182 LEU 388 1.330 1.221 1.534 1.531 1.482 123.76 116.87 120.64 108.73 113.10 110.18 122.48 * * * 183 ARG 389 1.311 1.226 1.548 1.526 1.462 121.72 116.56 120.02 110.78 112.48 110.20 123.41 * * * 184 ARG 390 1.338 1.234 1.560 1.558 1.500 123.87 116.06 120.80 109.56 116.49 113.21 123.13 +* * ** * +* +* ** 185 GLU 391 1.324 1.234 1.506 1.557 1.475 124.60 118.42 119.45 108.05 108.00 115.87 122.11 * +* * * * *** *** 186 PRO 392 1.343 1.246 1.537 1.538 1.457 122.06 116.23 120.93 110.46 111.10 103.94 122.81 187 GLY 393 1.309 1.240 1.504 - 1.429 121.11 115.99 120.59 - 111.32 - 123.42 * * * 188 GLY 394 1.300 - 1.489 - 1.423 122.02 - - - 109.44 - - ** * +* * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** * ** ** *** *** * * *** +* **** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_13 Page 15 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 168 1.280 1.352 1.322 .013 *** +* C-N (Pro) 1.341 .016 18 1.322 1.359 1.347 .008 * * C-O C-O 1.231 .020 187 1.205 1.247 1.229 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.482 1.560 1.525 .012 ** +* CH2G*-C (Gly) 1.516 .018 18 1.489 1.535 1.513 .011 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.504 1.531 1.519 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.492 1.587 1.548 .022 +* +* CH1E-CH2E (the rest) 1.530 .020 138 1.496 1.572 1.532 .014 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.400 1.500 1.452 .016 *** ** NH1-CH2G* (Gly) 1.451 .016 18 1.423 1.459 1.441 .010 +* N-CH1E (Pro) 1.466 .015 18 1.435 1.480 1.469 .011 ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_13 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 113.23 118.79 116.22 1.05 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.16 119.43 116.97 1.22 * CH1E-C-N (Pro) 116.9 1.5 18 114.83 118.52 116.59 .91 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.73 124.96 123.02 .70 * * O-C-N (Pro) 122.0 1.4 18 122.14 123.52 122.83 .32 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.32 127.13 122.32 1.44 ** *** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.28 122.17 120.91 .71 C-N-CH1E (Pro) 122.6 5.0 18 121.11 124.28 122.86 .74 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.95 122.39 120.69 .57 * CH2G*-C-O (Gly) 120.8 2.1 17 119.56 120.99 120.33 .42 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 108.45 111.17 110.45 .57 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.49 112.81 109.90 1.68 +* CH2E-CH1E-C (the rest) 110.1 1.9 138 105.29 115.85 110.49 1.77 +** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.11 116.49 110.79 1.56 * +* NH1-CH2G*-C (Gly) 112.5 2.9 18 109.44 113.60 111.68 1.06 * N-CH1E-C (Pro) 111.8 2.5 18 108.46 114.75 112.54 1.64 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 108.03 111.05 110.32 .61 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 103.98 113.93 111.49 2.54 **** * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.59 104.33 103.45 .57 * NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.35 115.87 110.67 1.80 ** *** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_13 Page 17 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 142 93.4% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 93.4 83.8 10.0 1.0 Inside b. Omega angle st dev 186 2.7 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 125 .9 .8 .2 .3 Inside f. Overall G-factor 188 .2 -.4 .3 2.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 15 10.6 18.1 6.5 -1.2 BETTER b. Chi-1 trans st dev 50 10.2 19.0 5.3 -1.7 BETTER c. Chi-1 gauche plus st dev 67 8.8 17.5 4.9 -1.8 BETTER d. Chi-1 pooled st dev 132 10.2 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 63 7.4 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 93.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .86 2 Residue-by-residue listing for refined_13 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .13 Chi1-chi2 distribution .01 Chi1 only .08 Chi3 & chi4 .40 Omega .20 ------ .17 ===== Main-chain covalent forces:- Main-chain bond lengths .29 Main-chain bond angles .37 ------ .34 ===== OVERALL AVERAGE .23 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.