Residue-by-residue listing for refined_20 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 - - - - - - - - - - - 180.5 - - - 2 SER 2 B - - -58.8 - - - - - - - 180.5 - 34.4 - 3 ASP 3 B 62.6 - - - - - - - - - 181.8 - 34.6 - 4 PRO 4 S - - - - - -75.6 - - - - - 181.0 - 38.7 - * * 5 GLY 5 h - - - - - - - - - - - 181.6 - - - 6 PRO 6 H - - - - - -61.6 -61.6 -36.0 - - - 180.2 - 38.3 - * * 7 GLU 7 H A 50.8 - - - - -73.3 -28.4 - - - 175.7 - 29.4 - * * 8 ALA 8 H A - - - - - -73.2 -37.7 - - - 174.8 - 33.6 - 9 ALA 9 H A - - - - - -63.2 -42.2 - - - 176.7 -2.3 34.2 - 10 ARG 10 H A - 184.7 - 186.5 - -59.8 -38.2 - - - 181.0 -2.4 35.4 - 11 LEU 11 H A - 173.6 - - - -64.3 -44.6 - - - 177.5 -1.5 34.5 - 12 ARG 12 H A - - -63.5 180.1 - -64.2 -36.9 - - - 176.2 -2.1 33.7 - 13 PHE 13 H A - 171.9 - - - -64.9 -37.8 - - - 178.4 -2.2 34.4 - 14 ARG 14 H A - - -63.5 - - -82.1 -22.3 - - - 179.2 -2.2 33.3 - * +* +* 15 CYS 15 H A - 182.0 - - - -83.8 -9.7 - - - 177.1 -1.8 34.1 - +* +** +** 16 PHE 16 h B - 180.2 - - - - - - - - 179.6 -.5 34.2 - ** ** 17 HIS 17 B 73.5 - - - - - - - - - 174.9 - 34.3 - 18 TYR 18 B - 165.4 - - - - - - - - 179.5 -1.1 32.0 - * * * 19 GLU 19 t B 48.3 - - 176.4 - - - - - - 182.3 -.7 32.3 - * +* +* Residue-by-residue listing for refined_20 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 T A - - -59.4 174.2 - - - - - - 179.3 -.6 35.4 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.0 - 33.9 - 22 THR 22 T A - 196.3 - - - - - - - - 183.2 -1.1 34.6 - * * 23 GLY 23 h - - - - - - - - - - - 184.0 -1.0 - - * * 24 PRO 24 H - - - - - -68.7 -68.7 -33.0 - - - 182.8 - 38.7 - * * 25 GLN 25 H A - - -52.1 - - -69.3 -37.1 - - - 180.8 - 35.6 - 26 GLU 26 H A - 180.0 - 165.7 - -75.3 -38.0 - - - 176.4 - 33.1 - 27 ALA 27 H A - - - - - -56.1 -38.4 - - - 176.3 -2.2 34.3 - 28 LEU 28 H A - - -64.8 181.5 - -59.2 -37.3 - - - 181.0 -1.7 34.0 - 29 ALA 29 H A - - - - - -66.2 -36.8 - - - 176.6 -.8 33.6 - +* +* 30 GLN 30 H A - - -80.2 - - -72.1 -50.4 - - - 179.4 -1.5 33.3 - 31 LEU 31 H A - - -69.3 168.5 - -59.0 -40.9 - - - 181.2 -3.1 34.0 - * * 32 ARG 32 H A - 180.4 - 180.5 - -60.2 -46.1 - - - 180.4 -3.0 32.6 - * * 33 GLU 33 H A 75.0 - - 180.9 - -68.7 -42.8 - - - 180.8 -1.2 30.6 - * * 34 LEU 34 H A - - -63.7 176.8 - -59.0 -45.3 - - - 179.1 -2.2 33.3 - 35 CYS 35 H A 66.9 - - - - -65.0 -37.5 - - - 177.0 -3.1 33.0 - * * 36 ARG 36 H A - 171.5 - - - -66.9 -30.8 - - - 177.6 -1.9 30.9 - 37 GLN 37 H A - - -54.5 185.8 - -67.1 -32.9 - - - 179.0 -1.9 35.6 - 38 TRP 38 H A - 162.4 - - - -81.4 -59.7 - - - 183.1 -1.4 34.1 - * * +* +* 39 LEU 39 H A - - -63.2 159.8 - -67.9 -46.7 - - - 179.5 -3.6 33.6 - ** ** 40 ARG 40 h l - - -66.2 - - - - - - - 179.3 -1.5 32.5 - 41 PRO 41 T - - - - - -66.2 - - - - - 179.2 - 38.8 - * * 42 GLU 42 T A - 184.6 - 178.0 - - - - - - 182.0 - 35.1 - 43 VAL 43 T A - - -61.5 - - - - - - - 184.1 -1.1 33.4 - * * 44 ARG 44 t B - - -77.4 182.6 - - - - - - 181.1 -3.3 29.2 - +* * +* 45 SER 45 h B - - -56.6 - - - - - - - 179.0 - 36.8 - 46 LYS 46 H A - - -65.2 172.6 - -54.6 -40.3 - - - 181.1 - 36.0 - 47 GLU 47 H A 58.0 - - 182.5 - -62.3 -29.5 - - - 177.8 - 33.3 - 48 GLN 48 H A - - -64.3 - - -72.2 -31.4 - - - 179.8 -1.1 35.3 - * * 49 MET 49 H A - - -59.8 177.9 - -70.2 -40.7 - - - 170.6 -1.0 32.5 - +* * +* 50 LEU 50 H A - - -78.5 - - -53.8 -52.9 - - - 181.7 -1.8 33.9 - * * 51 GLU 51 H A - 182.6 - 185.1 - -54.3 -52.6 - - - 179.8 -2.1 36.5 - * * 52 LEU 52 H A - - -63.2 177.4 - -60.9 -41.2 - - - 179.4 -2.8 34.1 - * * 53 LEU 53 H A - 182.6 - - - -70.0 -31.0 - - - 178.1 -2.6 34.7 - 54 VAL 54 H A - 188.1 - - - -64.6 -43.8 - - - 177.4 -2.4 33.5 - 55 LEU 55 H A - 182.6 - - - -59.6 -42.0 - - - 178.5 -1.9 35.4 - 56 GLU 56 H A - 171.8 - - - -51.8 -53.2 - - - 178.7 -1.8 35.1 - * * * Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 GLN 57 H A - 175.7 - - - -75.6 -41.2 - - - 183.3 -2.0 31.1 - 58 PHE 58 H A - 182.5 - - - -53.9 -47.7 - - - 177.9 -3.2 32.8 - +* +* 59 LEU 59 H A - - -96.5 - - -63.0 -40.6 - - - 178.9 -2.7 29.7 - +* * +* 60 GLY 60 H - - - - - - -80.5 -16.0 - - - 177.0 -1.2 - - * ** * ** 61 ALA 61 H A - - - - - -77.6 -25.3 - - - 175.2 -2.1 34.0 - * * * 62 LEU 62 h B - - -68.1 170.7 - - - - - - 176.7 -1.1 36.5 - * * 63 PRO 63 h - - - - - -71.5 - - - - - 181.0 - 38.5 - * * 64 PRO 64 H - - - - - -44.7 -44.7 -42.3 - - - 180.7 - 38.9 - +* +* * +* 65 GLU 65 H A 55.5 - - 188.8 - -63.5 -49.2 - - - 180.5 - 33.3 - 66 ILE 66 H A - - -59.7 181.0 - -73.5 -38.3 - - - 180.4 - 34.0 - 67 GLN 67 H A - 181.6 - 178.3 - -63.2 -37.2 - - - 178.1 -3.3 34.1 - +* +* 68 ALA 68 H A - - - - - -65.5 -30.5 - - - 179.6 -2.1 34.1 - 69 ARG 69 H A - - -56.0 - - -71.6 -47.3 - - - 182.9 -.9 35.5 - +* +* 70 VAL 70 H A - 175.3 - - - -55.8 -49.9 - - - 175.0 -2.3 34.5 - 71 GLN 71 H A - - -90.9 - - -52.1 -25.9 - - - 176.1 -2.0 29.3 - +* * * * +* 72 GLY 72 H - - - - - - -68.9 -40.8 - - - 180.4 -1.6 - - 73 GLN 73 H A 54.9 - - - - -98.2 -31.7 - - - 177.2 -.9 28.6 - +** * +* +** 74 ARG 74 h l - - -64.7 - - - - - - - 176.5 -3.7 31.5 - ** ** 75 PRO 75 - - - - - -68.8 - - - - - 180.3 - 38.9 - * * 76 GLY 76 - - - - - - - - - - - 177.9 - - - 77 SER 77 h B 53.8 - - - - - - - - - 184.6 - 33.4 - 78 PRO 78 H - - - - - -54.7 -54.7 -45.3 - - - 184.8 - 39.0 - * * 79 GLU 79 H A - - -61.7 171.3 - -74.4 -31.0 - - - 176.2 - 32.4 - 80 GLU 80 H A - 183.6 - - - -70.1 -45.0 - - - 175.0 - 34.2 - 81 ALA 81 H A - - - - - -56.3 -47.2 - - - 178.8 -2.8 34.2 - 82 ALA 82 H A - - - - - -55.2 -41.9 - - - 180.2 -2.7 34.0 - 83 ALA 83 H A - - - - - -64.2 -46.2 - - - 179.8 -1.9 33.5 - 84 LEU 84 H A 48.7 - - - - -75.3 -36.0 - - - 178.4 -2.2 28.1 - +* +* 85 VAL 85 H A - - -61.8 - - -65.4 -31.1 - - - 179.4 -3.2 30.6 - +* +* 86 ASP 86 H A - 186.2 - - - -58.7 -35.7 - - - 176.3 -1.6 32.8 - 87 GLY 87 H - - - - - - -77.5 -32.7 - - - 180.9 -.7 - - * +* +* 88 LEU 88 h A - - -61.6 173.9 - - - - - - 180.3 -1.5 35.2 - 89 ARG 89 T A - - -68.0 170.5 - - - - - - 173.1 -.6 32.9 - * +* +* 90 ARG 90 t ~l - - -61.8 173.4 - - - - - - 178.9 -.7 31.9 - ** +* ** 91 GLU 91 S B - - -58.0 185.9 - - - - - - 177.1 - 34.5 - 92 PRO 92 S - - - - - -72.1 - - - - - 181.3 - 38.3 - * * Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 GLY 93 - - - - - - - - - - - 179.5 -.7 - - +* +* 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 178.6 - - - 96 SER 302 B - - -59.3 - - - - - - - 179.1 - 34.9 - 97 ASP 303 B 66.6 - - - - - - - - - 172.8 - 34.1 - * * 98 PRO 304 S - - - - - -94.6 - - - - - 185.7 - 40.2 - +** +* +** 99 GLY 305 h - - - - - - - - - - - 181.1 - - - 100 PRO 306 H - - - - - -60.7 -60.7 -35.2 - - - 177.1 - 38.2 - * * 101 GLU 307 H A 56.2 - - 177.0 - -72.1 -29.4 - - - 177.1 - 33.0 - 102 ALA 308 H A - - - - - -71.9 -40.7 - - - 176.4 - 34.1 - 103 ALA 309 H A - - - - - -61.2 -45.6 - - - 178.0 -2.8 34.3 - * * 104 ARG 310 H A - 185.0 - 183.6 - -61.8 -38.8 - - - 180.7 -2.5 34.7 - 105 LEU 311 H A - 175.0 - - - -63.9 -42.5 - - - 177.6 -1.9 34.7 - 106 ARG 312 H A - - -62.4 180.8 - -65.9 -38.2 - - - 177.2 -2.4 33.9 - 107 PHE 313 H A - 177.3 - - - -61.1 -49.0 - - - 176.6 -2.3 34.3 - 108 ARG 314 H A - - -77.2 - - -71.5 -25.8 - - - 181.4 -2.9 33.0 - * * * 109 CYS 315 H A - 184.9 - - - -81.7 -25.2 - - - 179.9 -1.9 34.3 - * * * 110 PHE 316 h b - 179.6 - - - - - - - - 179.6 -1.8 35.3 - 111 HIS 317 B 75.9 - - - - - - - - - 172.0 - 34.3 - * * 112 TYR 318 B - 167.0 - - - - - - - - 178.6 -1.6 32.4 - 113 GLU 319 t B 47.7 - - 174.6 - - - - - - 180.2 - 33.1 - * * 114 GLU 320 T A - - -54.7 - - - - - - - 180.7 - 34.6 - 115 ALA 321 T A - - - - - - - - - - 181.7 - 34.1 - 116 THR 322 T A - 205.0 - - - - - - - - 181.3 -1.7 34.4 - * * 117 GLY 323 h - - - - - - - - - - - 183.4 -1.0 - - * * 118 PRO 324 H - - - - - -68.8 -68.8 -32.6 - - - 182.1 - 38.2 - * * 119 GLN 325 H A - - -50.4 - - -67.1 -38.2 - - - 180.4 - 35.3 - * * 120 GLU 326 H A - 180.7 - 166.2 - -71.7 -46.3 - - - 178.8 - 33.1 - 121 ALA 327 H A - - - - - -56.5 -32.8 - - - 175.4 -2.5 33.7 - 122 LEU 328 H A - - -67.5 179.7 - -59.0 -37.9 - - - 179.8 -1.8 33.5 - 123 ALA 329 H A - - - - - -62.4 -41.6 - - - 178.1 -1.2 34.2 - * * 124 GLN 330 H A - - -78.2 - - -66.1 -48.1 - - - 177.6 -1.3 33.8 - 125 LEU 331 H A - - -69.6 171.0 - -63.5 -41.9 - - - 178.6 -2.9 33.2 - * * 126 ARG 332 H A - 181.5 - 173.6 - -62.4 -36.3 - - - 176.3 -3.4 34.3 - +* +* 127 GLU 333 H A - 175.0 - 181.0 - -70.0 -51.2 - - - 181.2 -1.8 35.2 - * * 128 LEU 334 H A - - -63.5 174.3 - -59.5 -44.0 - - - 179.2 -3.1 33.6 - * * 129 CYS 335 H A 60.8 - - - - -68.6 -33.0 - - - 175.4 -3.2 32.5 - +* +* 130 ARG 336 H A - 182.6 - - - -69.5 -37.8 - - - 176.7 -1.3 31.7 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 131 GLN 337 H A - - -60.7 184.7 - -63.9 -33.3 - - - 177.1 -2.6 34.6 - 132 TRP 338 H a - 160.0 - - - -79.5 -61.8 - - - 183.4 -1.6 31.3 - * * +* +* 133 LEU 339 H A - - -59.0 182.6 - -66.2 -48.4 - - - 181.0 -3.7 32.4 - ** ** 134 ARG 340 h l - - -62.1 - - - - - - - 183.1 -1.5 33.0 - 135 PRO 341 T - - - - - -65.8 - - - - - 179.4 - 38.9 - * * 136 GLU 342 T A - 176.3 - 176.0 - - - - - - 182.6 - 35.8 - 137 VAL 343 T A - - -60.3 - - - - - - - 179.8 -.9 32.4 - +* +* 138 ARG 344 t B - - -71.3 190.9 - - - - - - 181.8 -3.0 29.6 - * * * 139 SER 345 h B - - -58.6 - - - - - - - 182.5 - 35.3 - 140 LYS 346 H A - - -63.2 172.0 - -51.1 -46.4 - - - 181.3 - 36.0 - * * 141 GLU 347 H A 40.1 - - - - -58.8 -31.8 - - - 174.5 - 29.2 - +* * +* 142 GLN 348 H A - - -79.9 - - -72.2 -31.0 - - - 179.8 -1.1 32.7 - * * 143 MET 349 H A - - -59.7 178.3 - -69.3 -39.3 - - - 173.6 -1.1 33.0 - * * * 144 LEU 350 H A - - -78.9 - - -56.5 -53.6 - - - 183.5 -2.0 35.0 - * * 145 GLU 351 H A - 189.0 - 176.6 - -58.0 -45.0 - - - 178.1 -1.9 34.9 - 146 LEU 352 H A - - -64.5 177.8 - -64.1 -43.6 - - - 183.9 -2.7 35.7 - 147 LEU 353 H A - 189.8 - - - -74.1 -29.1 - - - 171.6 -2.5 31.5 - * * 148 VAL 354 H A - 182.4 - - - -62.0 -46.6 - - - 178.1 -2.5 34.5 - 149 LEU 355 H A - 180.2 - - - -55.6 -43.5 - - - 177.8 -2.0 35.1 - 150 GLU 356 H A - 172.9 - - - -52.3 -52.2 - - - 179.5 -2.0 34.5 - * * * 151 GLN 357 H A - 178.0 - - - -74.5 -39.0 - - - 181.1 -1.8 31.2 - 152 PHE 358 H A - 182.3 - - - -55.6 -50.0 - - - 177.9 -3.3 32.6 - +* +* 153 LEU 359 H A - - -92.1 - - -61.3 -42.0 - - - 180.4 -2.9 29.9 - +* * * +* 154 GLY 360 H - - - - - - -80.3 -13.7 - - - 177.3 -1.5 - - * ** ** 155 ALA 361 H A - - - - - -79.7 -26.6 - - - 175.9 -1.8 33.7 - * * * 156 LEU 362 h B - - -66.1 171.8 - - - - - - 174.1 -1.2 37.4 - * * * 157 PRO 363 h - - - - - -63.0 - - - - - 181.4 - 40.0 - +* +* 158 PRO 364 H - - - - - -45.6 -45.6 -41.4 - - - 178.9 - 38.2 - +* +* * +* 159 GLU 365 H A 57.5 - - 182.4 - -61.3 -47.3 - - - 178.6 - 33.2 - 160 ILE 366 H A - - -61.2 180.2 - -72.3 -40.5 - - - 180.4 -.6 34.9 - +* +* 161 GLN 367 H A - 178.3 - 179.2 - -59.5 -42.5 - - - 178.5 -3.4 34.6 - +* +* 162 ALA 368 H A - - - - - -65.6 -35.5 - - - 176.4 -2.7 33.4 - 163 ARG 369 H A - - -65.6 - - -62.7 -49.4 - - - 177.0 -1.2 34.1 - * * 164 VAL 370 H A - 174.8 - - - -59.5 -46.0 - - - 180.4 -2.6 35.3 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 165 GLN 371 H A - 209.4 - - - -56.9 -29.5 - - - 177.2 -3.0 34.7 - +* * +* 166 GLY 372 H - - - - - - -79.9 -41.0 - - - 182.7 -1.2 - - * * * 167 GLN 373 H A 50.4 - - 184.2 - -82.3 -33.1 - - - 174.0 -2.0 30.5 - * * * 168 ARG 374 h l - - -62.7 - - - - - - - 176.5 -3.7 31.1 - ** ** 169 PRO 375 - - - - - -63.5 - - - - - 179.8 - 39.5 - +* +* 170 GLY 376 S - - - - - - - - - - - 181.2 - - - 171 SER 377 h B 49.6 - - - - - - - - - 185.2 - 34.4 - 172 PRO 378 H - - - - - -59.8 -59.8 -44.4 - - - 182.5 - 37.1 - 173 GLU 379 H A - - -64.7 166.8 - -69.6 -36.5 - - - 176.3 - 33.0 - 174 GLU 380 H A - 183.9 - - - -63.0 -48.2 - - - 176.2 - 34.8 - 175 ALA 381 H A - - - - - -56.0 -49.3 - - - 180.9 -2.5 34.5 - 176 ALA 382 H A - - - - - -55.7 -44.7 - - - 180.0 -3.1 33.5 - * * 177 ALA 383 H A - - - - - -59.5 -48.9 - - - 179.4 -2.5 33.5 - 178 LEU 384 H A 48.5 - - - - -71.8 -34.4 - - - 176.0 -2.2 28.8 - * * 179 VAL 385 H A - 166.8 - - - -61.6 -36.9 - - - 179.3 -3.2 33.8 - +* +* 180 ASP 386 H A - 183.2 - - - -58.7 -31.9 - - - 176.6 -2.2 33.5 - 181 GLY 387 H - - - - - - -86.0 -15.5 - - - 185.3 -.7 - - +* ** +* ** 182 LEU 388 h A - - -65.1 176.3 - - - - - - 183.6 -.8 34.5 - +* +* 183 ARG 389 T A - - -48.3 187.8 - - - - - - 184.8 - 34.6 - * * 184 ARG 390 t l - - -70.7 - - - - - - - 182.0 -.5 31.2 - ** ** 185 GLU 391 B - - -54.6 182.6 - - - - - - 173.5 - 36.6 - * * 186 PRO 392 - - - - - -84.6 - - - - - 183.3 - 37.7 - +* * +* 187 GLY 393 - - - - - - - - - - - 179.9 -1.7 - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* +* +* +** +** +** +* ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.2 180.1 -65.3 177.8 -66.1 -65.5 -39.3 - - - 179.2 -2.0 34.1 Standard deviations: 9.8 9.0 9.4 6.3 12.0 8.9 8.8 - - - 2.8 .8 2.3 Numbers of values: 21 49 62 55 18 124 124 0 0 0 186 124 170 0 Residue-by-residue listing for refined_20 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_20 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 - 1.240 1.498 - 1.456 - 116.54 120.53 - 111.18 - 122.93 * * 2 SER 2 1.308 1.242 1.527 1.520 1.431 121.45 115.61 121.12 110.46 110.91 109.91 123.26 +* * +* 3 ASP 3 1.298 1.232 1.515 1.542 1.446 123.54 118.98 119.26 110.76 107.95 110.42 121.75 ** * * * ** 4 PRO 4 1.348 1.236 1.540 1.531 1.476 122.42 117.00 120.46 110.32 113.75 102.98 122.53 5 GLY 5 1.317 1.240 1.509 - 1.431 120.82 118.51 119.99 - 111.32 - 121.50 * * * 6 PRO 6 1.350 1.223 1.523 1.540 1.459 122.14 116.61 121.05 110.53 111.49 104.13 122.25 * * 7 GLU 7 1.318 1.239 1.526 1.548 1.439 120.73 115.99 120.64 114.16 112.31 112.62 123.37 * ** * ** 8 ALA 8 1.316 1.233 1.523 1.521 1.453 122.40 115.86 121.06 110.93 109.18 110.94 123.08 9 ALA 9 1.330 1.233 1.519 1.522 1.454 121.78 115.44 121.08 110.49 108.96 110.74 123.45 10 ARG 10 1.337 1.217 1.524 1.524 1.456 122.44 115.89 121.10 107.89 110.16 111.08 123.01 * * 11 LEU 11 1.324 1.210 1.521 1.522 1.411 123.06 116.62 120.34 111.63 110.33 108.93 123.02 * ** ** 12 ARG 12 1.323 1.233 1.526 1.523 1.469 121.98 115.17 121.16 110.63 110.73 110.63 123.66 13 PHE 13 1.310 1.218 1.542 1.539 1.454 123.98 116.60 120.78 112.80 110.59 107.69 122.60 * * * +* +* Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 14 ARG 14 1.323 1.228 1.521 1.536 1.466 122.06 116.17 120.82 110.38 111.45 111.25 123.01 15 CYS 15 1.313 1.239 1.524 1.541 1.447 122.50 115.94 121.02 110.94 109.94 110.25 123.04 * * 16 PHE 16 1.324 1.244 1.508 1.539 1.435 121.68 115.98 120.92 110.49 108.64 111.15 123.08 * * 17 HIS 17 1.294 1.236 1.497 1.571 1.423 120.60 117.82 119.86 110.28 107.14 112.13 122.29 ** * ** +* * ** 18 TYR 18 1.294 1.234 1.500 1.531 1.416 118.35 114.63 121.60 112.01 108.97 112.69 123.77 ** * ** +* * * ** 19 GLU 19 1.283 1.232 1.502 1.537 1.406 122.27 115.12 121.36 113.21 109.82 110.97 123.52 *** * +** +* *** 20 GLU 20 1.299 1.228 1.520 1.514 1.445 123.46 115.27 121.05 110.36 110.40 108.62 123.67 ** * ** 21 ALA 21 1.315 1.225 1.531 1.519 1.438 123.37 117.91 120.09 110.51 112.26 110.09 122.00 * * * 22 THR 22 1.339 1.213 1.534 1.595 1.458 119.22 115.96 121.17 110.10 108.63 111.27 122.71 ** * ** 23 GLY 23 1.329 1.239 1.532 - 1.447 120.74 119.26 120.17 - 110.98 - 120.57 * +* +* 24 PRO 24 1.335 1.235 1.530 1.510 1.462 121.91 116.78 120.36 110.34 113.83 102.82 122.84 25 GLN 25 1.328 1.237 1.519 1.532 1.451 121.32 114.94 121.50 108.17 108.30 111.24 123.56 * * * 26 GLU 26 1.324 1.228 1.513 1.516 1.436 122.45 116.58 120.45 112.51 110.88 109.71 122.96 * * * 27 ALA 27 1.327 1.227 1.524 1.522 1.464 122.04 115.62 120.78 110.41 109.67 110.32 123.58 28 LEU 28 1.328 1.218 1.529 1.532 1.460 122.69 117.05 120.25 109.18 111.82 111.42 122.69 29 ALA 29 1.329 1.242 1.523 1.518 1.466 121.79 115.42 120.99 110.60 110.65 110.74 123.59 30 GLN 30 1.317 1.232 1.529 1.550 1.448 122.66 115.75 120.96 111.34 110.52 110.96 123.25 31 LEU 31 1.323 1.227 1.518 1.526 1.463 122.98 116.56 120.29 110.43 112.32 109.89 123.14 32 ARG 32 1.320 1.233 1.519 1.518 1.446 121.78 118.19 119.79 110.69 112.31 111.66 122.01 33 GLU 33 1.329 1.209 1.521 1.550 1.447 117.75 116.72 119.77 111.73 109.74 114.59 123.40 * * ** ** ** 34 LEU 34 1.341 1.232 1.524 1.536 1.466 122.62 116.81 120.47 110.46 112.03 111.08 122.71 35 CYS 35 1.328 1.219 1.536 1.549 1.452 120.74 116.35 121.01 111.57 109.58 111.35 122.61 36 ARG 36 1.335 1.225 1.545 1.559 1.438 122.92 117.35 119.97 114.79 112.51 109.97 122.67 * * ** ** 37 GLN 37 1.331 1.237 1.519 1.510 1.472 122.28 113.79 121.82 108.60 109.54 110.01 124.38 * * 38 TRP 38 1.315 1.217 1.541 1.553 1.446 125.00 116.85 120.59 112.58 112.19 107.98 122.56 * * +* * * +* 39 LEU 39 1.305 1.238 1.532 1.531 1.461 122.85 116.09 120.34 112.47 111.79 108.63 123.53 +* * * +* 40 ARG 40 1.335 1.225 1.548 1.547 1.476 123.64 118.29 120.36 110.94 113.41 111.09 121.35 * * * * * 41 PRO 41 1.359 1.244 1.533 1.535 1.486 123.02 115.42 121.11 110.01 112.69 103.41 123.47 * * * * 42 GLU 42 1.320 1.240 1.530 1.540 1.451 123.27 116.26 121.10 110.82 110.04 108.89 122.63 43 VAL 43 1.324 1.234 1.525 1.555 1.453 121.00 116.97 120.32 109.41 112.58 112.03 122.68 44 ARG 44 1.319 1.232 1.497 1.521 1.441 120.59 113.48 121.89 111.99 115.35 113.37 124.63 * * * +* * +* 45 SER 45 1.304 1.242 1.530 1.530 1.426 125.01 115.20 121.03 109.96 110.96 107.16 123.76 +* +* +* +* +* 46 LYS 46 1.325 1.217 1.522 1.519 1.466 124.61 115.69 121.13 109.74 111.41 107.94 123.14 +* +* +* Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 47 GLU 47 1.312 1.229 1.538 1.522 1.465 122.90 116.26 120.97 111.23 112.13 110.00 122.76 * * 48 GLN 48 1.329 1.217 1.507 1.524 1.457 121.97 115.37 121.27 109.12 109.00 110.48 123.35 49 MET 49 1.312 1.222 1.500 1.504 1.443 122.28 116.35 119.93 112.89 110.54 110.17 123.72 * * * * * 50 LEU 50 1.345 1.202 1.512 1.567 1.471 121.36 116.05 120.12 109.06 109.18 112.85 123.66 * * +* * +* 51 GLU 51 1.334 1.242 1.542 1.520 1.446 124.19 116.13 120.89 109.80 111.24 107.35 122.98 * +* +* 52 LEU 52 1.322 1.240 1.526 1.529 1.442 122.34 116.17 120.82 110.71 111.15 109.99 123.01 53 LEU 53 1.320 1.234 1.547 1.487 1.416 122.24 117.87 120.09 111.55 112.73 107.40 122.04 * ** ** +* ** 54 VAL 54 1.329 1.232 1.533 1.563 1.463 120.34 115.22 121.12 108.75 108.61 113.79 123.64 * * 55 LEU 55 1.333 1.240 1.524 1.555 1.469 123.48 114.57 121.06 111.33 109.16 108.27 124.36 * * * 56 GLU 56 1.323 1.239 1.534 1.551 1.462 124.00 117.00 120.69 110.74 111.56 108.59 122.31 * * * * 57 GLN 57 1.305 1.205 1.495 1.512 1.439 119.83 117.20 119.52 111.90 112.45 112.43 123.27 +* * * * * +* 58 PHE 58 1.320 1.233 1.526 1.527 1.453 121.42 116.49 120.50 111.06 111.56 111.25 122.98 59 LEU 59 1.320 1.220 1.520 1.538 1.455 121.07 117.54 119.88 113.49 113.64 112.08 122.54 +* +* 60 GLY 60 1.317 1.232 1.524 - 1.456 119.74 116.47 120.70 - 112.75 - 122.82 61 ALA 61 1.325 1.238 1.508 1.526 1.457 122.50 115.40 120.84 110.27 109.62 111.09 123.73 62 LEU 62 1.325 1.241 1.521 1.527 1.441 123.32 117.93 120.30 108.68 109.90 108.90 121.77 63 PRO 63 1.336 1.242 1.521 1.533 1.441 121.41 118.28 119.31 110.32 109.13 104.49 122.41 +* * * +* 64 PRO 64 1.352 1.233 1.531 1.524 1.474 123.40 116.06 120.55 110.14 112.95 103.03 123.37 65 GLU 65 1.327 1.223 1.548 1.541 1.457 122.56 117.64 120.04 112.02 112.70 109.19 122.24 * * * 66 ILE 66 1.333 1.229 1.532 1.551 1.451 121.88 116.16 121.08 110.53 110.94 110.65 122.73 67 GLN 67 1.321 1.235 1.533 1.520 1.456 122.06 115.82 121.11 110.93 110.58 109.82 123.05 68 ALA 68 1.332 1.242 1.527 1.525 1.468 122.21 115.55 121.10 110.13 110.64 110.60 123.35 69 ARG 69 1.321 1.219 1.518 1.518 1.447 122.38 115.79 120.44 108.54 109.68 110.42 123.72 70 VAL 70 1.343 1.235 1.499 1.530 1.480 123.15 114.76 121.25 108.61 111.40 111.39 123.99 * * * 71 GLN 71 1.293 1.229 1.536 1.520 1.446 123.62 116.69 120.46 114.64 113.65 111.26 122.81 +** * ** +** 72 GLY 72 1.321 1.229 1.540 - 1.439 120.79 117.97 120.01 - 112.66 - 122.00 * * 73 GLN 73 1.339 1.230 1.534 1.569 1.474 120.19 116.62 120.19 112.20 113.48 115.00 123.18 +* * +** +** 74 ARG 74 1.326 1.237 1.542 1.537 1.481 123.80 117.20 120.86 111.18 114.60 111.60 121.88 * * * * 75 PRO 75 1.349 1.223 1.548 1.536 1.477 122.77 116.11 121.11 110.03 112.75 103.22 122.77 * * 76 GLY 76 1.326 1.229 1.522 - 1.459 121.70 116.63 120.64 - 113.27 - 122.71 77 SER 77 1.305 1.249 1.538 1.525 1.438 121.86 117.61 120.14 112.29 109.73 109.87 122.21 +* * * +* 78 PRO 78 1.357 1.231 1.530 1.531 1.477 123.14 116.78 120.42 109.10 114.25 103.77 122.78 * * 79 GLU 79 1.315 1.239 1.520 1.518 1.458 121.55 116.18 120.68 113.05 111.97 109.57 123.12 +* +* Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 80 GLU 80 1.321 1.232 1.522 1.526 1.446 121.39 116.34 120.58 111.22 108.37 110.18 123.08 * * 81 ALA 81 1.351 1.217 1.521 1.513 1.441 121.75 116.40 120.09 110.53 110.19 110.26 123.48 +* +* 82 ALA 82 1.338 1.225 1.537 1.533 1.463 122.89 115.93 121.20 110.65 111.26 110.07 122.87 83 ALA 83 1.305 1.235 1.525 1.513 1.454 122.67 117.03 120.55 110.59 111.68 110.59 122.41 +* +* 84 LEU 84 1.323 1.233 1.523 1.513 1.438 120.11 117.20 120.22 114.06 114.32 112.98 122.55 * ** * * ** 85 VAL 85 1.337 1.224 1.501 1.545 1.466 121.16 116.35 120.30 109.81 111.92 115.47 123.34 * ** ** 86 ASP 86 1.325 1.223 1.533 1.530 1.452 121.53 116.58 120.87 111.25 110.58 111.36 122.50 87 GLY 87 1.323 1.228 1.519 - 1.458 120.44 115.42 121.14 - 111.03 - 123.36 88 LEU 88 1.328 1.229 1.534 1.531 1.477 124.25 116.36 120.79 109.01 112.06 109.58 122.85 * * * 89 ARG 89 1.321 1.227 1.530 1.526 1.460 123.39 116.75 120.16 111.42 112.89 110.19 123.08 90 ARG 90 1.343 1.231 1.531 1.537 1.485 124.26 117.26 120.45 111.51 114.30 110.88 122.29 * * * * 91 GLU 91 1.306 1.238 1.521 1.528 1.446 121.53 117.85 120.13 109.37 109.95 111.16 122.00 +* +* 92 PRO 92 1.336 1.243 1.529 1.531 1.456 122.26 115.99 121.02 110.79 110.86 103.77 122.96 93 GLY 93 1.311 1.245 1.514 - 1.439 120.73 116.22 120.81 - 112.05 - 122.97 * * 94 GLY 94 1.301 1.240 1.500 - 1.441 120.95 - 120.09 - 111.54 - - ** ** 95 GLY 301 - 1.227 1.512 - 1.451 - 115.76 121.25 - 111.69 - 122.98 96 SER 302 1.306 1.240 1.520 1.527 1.442 122.26 116.97 120.29 110.06 109.55 110.01 122.74 +* +* 97 ASP 303 1.309 1.238 1.522 1.559 1.447 120.87 117.87 120.39 109.73 110.02 111.76 121.66 * * * 98 PRO 304 1.342 1.232 1.522 1.529 1.456 123.06 115.09 121.58 109.50 109.36 102.50 123.32 * * 99 GLY 305 1.310 1.223 1.503 - 1.411 121.70 118.98 119.72 - 109.15 - 121.28 * +** * * * +** 100 PRO 306 1.341 1.229 1.522 1.526 1.466 122.16 116.06 121.12 110.61 111.33 103.92 122.79 101 GLU 307 1.319 1.231 1.529 1.528 1.442 121.33 116.37 120.80 111.34 110.33 111.23 122.83 102 ALA 308 1.329 1.226 1.513 1.528 1.456 121.89 115.21 121.14 110.50 108.41 111.01 123.63 103 ALA 309 1.324 1.231 1.520 1.521 1.445 122.89 116.17 120.71 110.80 109.58 110.09 123.09 104 ARG 310 1.339 1.229 1.530 1.520 1.451 121.55 115.64 121.37 108.10 110.38 111.76 122.99 * * 105 LEU 311 1.327 1.213 1.524 1.525 1.410 123.30 116.71 120.26 111.80 110.30 108.60 123.02 +** * +** 106 ARG 312 1.330 1.220 1.520 1.525 1.465 122.06 115.12 121.12 110.26 110.16 110.88 123.75 107 PHE 313 1.310 1.220 1.544 1.532 1.452 123.96 116.87 120.37 113.09 110.59 107.37 122.72 * * +* +* +* 108 ARG 314 1.327 1.243 1.542 1.544 1.475 122.04 116.69 120.74 109.98 112.60 111.57 122.57 109 CYS 315 1.316 1.238 1.528 1.542 1.458 122.07 115.91 120.51 110.70 110.55 109.97 123.57 110 PHE 316 1.332 1.243 1.517 1.546 1.456 123.57 116.34 120.84 110.03 110.11 109.53 122.81 * * 111 HIS 317 1.310 1.239 1.505 1.573 1.437 120.41 117.17 120.09 109.64 108.32 112.37 122.72 * ** * * * ** 112 TYR 318 1.296 1.228 1.498 1.536 1.425 119.38 115.28 120.95 111.89 108.23 112.54 123.65 ** * +* * * * ** 113 GLU 319 1.276 1.239 1.506 1.537 1.410 122.80 115.31 121.05 112.80 109.06 110.47 123.57 +*** +** * +*** Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 114 GLU 320 1.318 1.219 1.515 1.543 1.454 123.47 115.27 121.01 108.51 110.26 111.91 123.69 115 ALA 321 1.313 1.238 1.540 1.518 1.450 123.49 117.59 120.19 110.20 112.77 109.75 122.21 * * 116 THR 322 1.329 1.237 1.541 1.575 1.450 120.41 115.41 121.45 111.12 108.95 110.25 123.05 * * 117 GLY 323 1.325 1.244 1.518 - 1.439 121.40 118.91 120.04 - 111.04 - 121.04 * * * 118 PRO 324 1.339 1.229 1.516 1.512 1.456 121.87 116.81 120.07 110.47 113.46 103.62 123.10 119 GLN 325 1.330 1.225 1.522 1.531 1.451 121.01 115.37 121.25 108.12 108.10 111.67 123.37 * * * 120 GLU 326 1.333 1.214 1.510 1.530 1.439 122.08 116.74 120.28 111.87 110.51 110.58 122.96 * * 121 ALA 327 1.327 1.233 1.534 1.520 1.469 121.99 116.25 120.65 110.80 110.89 110.25 123.10 122 LEU 328 1.332 1.204 1.510 1.523 1.462 122.14 117.47 119.53 108.57 111.89 112.63 123.00 * * * 123 ALA 329 1.330 1.227 1.513 1.524 1.462 121.56 114.94 121.34 110.35 109.33 110.76 123.67 124 GLN 330 1.308 1.224 1.521 1.541 1.447 123.33 116.39 120.56 111.52 110.77 109.95 123.04 +* +* 125 LEU 331 1.314 1.216 1.513 1.520 1.466 122.21 116.45 120.43 110.68 112.07 110.87 123.12 * * 126 ARG 332 1.313 1.221 1.513 1.520 1.459 123.18 115.23 121.31 111.38 109.85 109.32 123.44 * * 127 GLU 333 1.297 1.216 1.531 1.514 1.427 122.21 116.59 120.30 110.90 110.17 108.39 123.04 ** +* * ** 128 LEU 334 1.329 1.233 1.528 1.534 1.472 122.70 116.71 120.63 110.37 112.02 110.60 122.65 129 CYS 335 1.323 1.219 1.535 1.543 1.448 121.08 116.91 120.60 112.24 110.27 111.12 122.49 * * 130 ARG 336 1.338 1.228 1.523 1.553 1.463 121.79 116.81 120.02 113.17 111.06 111.07 123.17 * +* +* 131 GLN 337 1.327 1.225 1.510 1.510 1.458 122.28 114.91 121.51 109.52 110.05 110.58 123.57 132 TRP 338 1.309 1.230 1.551 1.558 1.433 123.15 118.71 119.38 114.12 112.94 109.97 121.91 * * * * * ** ** 133 LEU 339 1.337 1.243 1.528 1.552 1.469 120.54 116.38 119.90 109.94 111.09 113.21 123.70 * +* +* 134 ARG 340 1.358 1.229 1.543 1.550 1.470 122.88 117.64 120.65 111.36 110.87 111.05 121.71 ** * ** 135 PRO 341 1.364 1.225 1.519 1.536 1.488 123.26 115.33 121.44 110.05 112.72 103.27 123.22 * * * * 136 GLU 342 1.296 1.236 1.523 1.509 1.434 122.79 116.24 120.95 110.54 110.61 107.77 122.75 ** * * +* ** 137 VAL 343 1.313 1.233 1.515 1.557 1.443 120.47 117.12 120.31 110.36 111.96 112.71 122.57 * * 138 ARG 344 1.320 1.225 1.497 1.516 1.444 120.37 113.92 121.52 111.52 114.86 113.63 124.56 * * * +* +* 139 SER 345 1.307 1.246 1.540 1.521 1.428 124.67 114.82 121.10 111.38 111.70 107.38 124.08 +* +* +* +* +* 140 LYS 346 1.330 1.217 1.523 1.515 1.475 125.49 116.40 120.71 109.04 112.81 108.25 122.88 ** * ** 141 GLU 347 1.309 1.230 1.531 1.551 1.458 122.92 116.95 120.61 113.14 113.38 113.28 122.41 * * +* +* +* 142 GLN 348 1.320 1.220 1.507 1.525 1.456 120.78 116.02 120.88 110.94 110.83 111.88 123.08 143 MET 349 1.312 1.222 1.497 1.502 1.445 121.75 116.37 119.99 111.81 110.61 110.42 123.62 * * * * 144 LEU 350 1.344 1.208 1.511 1.568 1.466 121.29 115.41 120.67 108.62 108.67 111.93 123.72 * * +* +* Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 145 GLU 351 1.322 1.244 1.554 1.518 1.432 124.30 116.74 120.57 112.02 111.93 107.16 122.68 * * * * +* +* 146 LEU 352 1.331 1.235 1.511 1.527 1.456 122.48 115.47 121.37 108.22 111.02 110.26 123.16 147 LEU 353 1.300 1.241 1.554 1.518 1.408 122.29 117.15 120.38 116.70 111.71 107.37 122.46 ** * +** *** +* *** 148 VAL 354 1.343 1.227 1.536 1.570 1.474 121.28 115.47 121.00 107.80 108.26 113.38 123.53 * * * * * 149 LEU 355 1.345 1.237 1.525 1.560 1.478 123.88 114.89 120.95 111.58 109.50 108.40 124.15 * * * * * * 150 GLU 356 1.322 1.236 1.539 1.547 1.458 123.89 117.16 120.63 111.61 111.01 108.61 122.19 * * * 151 GLN 357 1.318 1.206 1.498 1.525 1.450 119.89 117.30 119.46 111.79 112.04 112.55 123.22 * * * * * 152 PHE 358 1.318 1.233 1.526 1.533 1.451 121.14 116.45 120.51 111.00 111.02 111.88 123.00 153 LEU 359 1.325 1.217 1.515 1.541 1.457 121.29 117.50 119.90 113.45 113.29 112.13 122.52 +* +* 154 GLY 360 1.319 1.230 1.523 - 1.457 119.62 116.97 120.69 - 113.33 - 122.32 155 ALA 361 1.316 1.235 1.511 1.522 1.452 121.75 115.17 120.95 110.73 109.45 111.10 123.88 156 LEU 362 1.323 1.241 1.516 1.526 1.442 123.65 117.86 120.13 107.49 110.21 108.81 122.01 * * * 157 PRO 363 1.341 1.236 1.516 1.540 1.456 121.99 118.78 118.85 109.17 107.81 103.54 122.36 * * +* +* 158 PRO 364 1.345 1.222 1.539 1.525 1.479 123.03 116.07 120.77 111.28 112.76 102.74 123.10 159 GLU 365 1.323 1.232 1.556 1.529 1.461 122.92 117.42 120.25 111.55 112.70 109.69 122.33 * * 160 ILE 366 1.340 1.236 1.523 1.555 1.462 122.03 114.97 121.53 109.52 109.65 110.75 123.48 161 GLN 367 1.316 1.225 1.520 1.517 1.443 123.31 116.33 120.54 110.66 110.88 109.36 123.13 162 ALA 368 1.323 1.240 1.527 1.515 1.459 122.36 116.53 120.54 110.69 111.12 110.74 122.92 163 ARG 369 1.336 1.238 1.511 1.526 1.466 121.37 115.41 120.84 109.11 109.24 112.05 123.75 164 VAL 370 1.325 1.222 1.506 1.537 1.452 122.47 115.18 121.04 107.76 110.14 111.69 123.77 165 GLN 371 1.308 1.217 1.543 1.521 1.441 123.42 116.70 120.56 109.78 110.80 110.10 122.72 +* +* 166 GLY 372 1.324 1.226 1.526 - 1.444 120.53 116.96 120.41 - 112.97 - 122.59 167 GLN 373 1.331 1.234 1.518 1.522 1.466 121.29 115.66 120.66 112.82 113.28 111.84 123.68 * * 168 ARG 374 1.316 1.231 1.534 1.519 1.463 124.29 116.42 121.15 113.05 114.89 109.97 122.30 * +* * +* 169 PRO 375 1.348 1.233 1.538 1.536 1.477 123.49 115.97 120.90 109.30 113.05 103.09 123.11 170 GLY 376 1.334 1.241 1.525 - 1.458 121.69 115.94 120.87 - 112.73 - 123.18 171 SER 377 1.314 1.245 1.548 1.523 1.441 122.90 117.94 120.09 112.30 110.08 108.16 121.95 * * * * * 172 PRO 378 1.363 1.225 1.536 1.539 1.475 123.03 117.62 119.97 110.74 115.14 104.58 122.41 * * * * 173 GLU 379 1.320 1.238 1.516 1.515 1.469 121.10 115.89 120.58 111.69 111.42 110.29 123.52 174 GLU 380 1.327 1.235 1.525 1.533 1.439 122.29 116.03 120.55 110.79 108.14 109.87 123.40 * * 175 ALA 381 1.354 1.208 1.514 1.516 1.441 122.03 116.46 120.26 110.05 110.48 110.23 123.24 +* * +* 176 ALA 382 1.325 1.233 1.533 1.532 1.457 122.54 115.98 120.84 111.15 111.31 110.30 123.16 177 ALA 383 1.318 1.242 1.527 1.520 1.459 122.57 116.59 120.62 110.71 111.18 110.58 122.77 178 LEU 384 1.324 1.231 1.523 1.506 1.437 120.92 116.21 120.50 114.43 113.69 112.13 123.25 * * ** ** 179 VAL 385 1.334 1.232 1.519 1.560 1.470 123.32 115.95 120.86 109.82 111.21 111.57 123.18 180 ASP 386 1.318 1.222 1.533 1.536 1.459 122.43 115.89 120.80 111.42 110.46 110.28 123.30 Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 181 GLY 387 1.328 1.233 1.541 - 1.455 122.28 116.76 120.73 - 113.47 - 122.51 * * 182 LEU 388 1.324 1.235 1.526 1.532 1.474 122.83 117.88 119.97 108.64 113.94 110.41 122.16 183 ARG 389 1.318 1.234 1.522 1.529 1.466 120.03 115.91 120.38 108.34 110.84 111.64 123.70 184 ARG 390 1.341 1.234 1.526 1.567 1.483 124.54 115.83 121.03 110.49 110.82 114.53 123.07 +* * +* ** ** 185 GLU 391 1.316 1.239 1.514 1.518 1.439 122.18 118.31 120.20 107.03 110.16 110.33 121.49 * * +* +* 186 PRO 392 1.322 1.242 1.536 1.529 1.432 121.64 115.53 121.43 111.88 109.82 103.93 122.96 * ** ** 187 GLY 393 1.324 1.232 1.497 - 1.445 121.02 115.72 120.87 - 111.90 - 123.41 * * 188 GLY 394 1.295 - 1.483 - 1.421 121.96 - - - 109.76 - - ** +* +* ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * +* ** +** ** * * *** +* +** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 1.276 1.358 1.322 .013 +*** ** C-N (Pro) 1.341 .016 18 1.322 1.364 1.346 .011 * * C-O C-O 1.231 .020 187 1.202 1.249 1.230 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.495 1.556 1.525 .013 * * CH2G*-C (Gly) 1.516 .018 18 1.483 1.541 1.516 .015 +* * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.513 1.533 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.530 1.595 1.558 .017 ** CH1E-CH2E (the rest) 1.530 .020 138 1.487 1.573 1.532 .015 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.406 1.485 1.452 .016 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.411 1.459 1.445 .013 +** N-CH1E (Pro) 1.466 .015 18 1.432 1.488 1.466 .015 ** * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 2.0 152 113.48 118.98 116.31 .97 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.42 119.26 117.06 1.22 * CH1E-C-N (Pro) 116.9 1.5 18 115.09 118.78 116.46 .97 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.57 124.63 122.96 .67 +* * O-C-N (Pro) 122.0 1.4 18 122.25 123.47 122.87 .36 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.75 125.49 122.23 1.29 ** ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.62 122.28 121.01 .73 C-N-CH1E (Pro) 122.6 5.0 18 121.41 123.49 122.56 .63 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.85 121.89 120.64 .53 * CH2G*-C-O (Gly) 120.8 2.1 17 119.72 121.25 120.51 .43 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 110.05 111.15 110.56 .27 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.76 111.12 109.46 1.01 CH2E-CH1E-C (the rest) 110.1 1.9 138 107.03 116.70 110.92 1.62 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.14 115.35 110.91 1.59 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.15 113.47 111.82 1.18 * N-CH1E-C (Pro) 111.8 2.5 18 107.81 115.14 112.06 1.93 +* * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.75 111.10 110.51 .37 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.25 115.47 112.08 1.45 ** N-CH1E-CH2E (Pro) 103.0 1.1 18 102.50 104.58 103.49 .57 * NH1-CH1E-CH2E (the rest) 110.5 1.7 120 107.16 115.00 110.51 1.67 +* +** ------------------------------------------------------------------------------------------------------------- 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_20 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] 144 94.7% Residues in additional allowed regions [a,b,l,p] 7 4.6% 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 94.7 83.8 10.0 1.1 BETTER b. Omega angle st dev 186 2.8 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 2.3 3.1 1.6 -.5 Inside e. H-bond energy st dev 124 .8 .8 .2 .1 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 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 21 9.8 18.1 6.5 -1.3 BETTER b. Chi-1 trans st dev 49 9.0 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 62 9.4 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 132 10.0 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 55 6.3 20.4 5.0 -2.8 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% 94.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_20 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .17 Chi1-chi2 distribution -.11 Chi1 only .00 Chi3 & chi4 .26 Omega .14 ------ .12 ===== Main-chain covalent forces:- Main-chain bond lengths .28 Main-chain bond angles .41 ------ .36 ===== OVERALL AVERAGE .20 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.