Residue-by-residue listing for refined_10 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 - - - - - - - - - - - 179.5 - - - 2 SER 2 B - 185.1 - - - - - - - - 179.5 - 34.2 - 3 ASP 3 B 64.8 - - - - - - - - - 182.9 - 33.5 - 4 PRO 4 - - - - - -77.2 - - - - - 180.3 - 38.3 - * * * 5 GLY 5 h - - - - - - - - - - - 180.7 - - - 6 PRO 6 H - - - - - -58.9 -58.9 -35.8 - - - 179.0 - 38.2 - * * 7 GLU 7 H A - - -66.0 189.9 - -75.8 -30.0 - - - 175.8 - 30.2 - * * 8 ALA 8 H A - - - - - -72.6 -31.1 - - - 172.9 - 33.0 - * * 9 ALA 9 H A - - - - - -63.2 -46.7 - - - 177.1 -2.1 34.9 - 10 ARG 10 H A - 178.4 - 178.1 - -61.9 -34.2 - - - 178.6 -2.3 33.5 - 11 LEU 11 H A - 174.8 - - - -63.0 -51.1 - - - 178.3 -1.9 35.5 - * * 12 ARG 12 H A - - -58.9 177.1 - -60.3 -40.7 - - - 181.3 -2.4 35.9 - 13 PHE 13 H A - 169.4 - - - -70.1 -50.5 - - - 183.6 -2.5 34.5 - 14 ARG 14 H A - 178.9 - - - -73.2 -34.0 - - - 178.9 -3.8 32.4 - ** ** 15 CYS 15 h A - - -61.9 - - - - - - - 177.9 -2.5 32.7 - 16 PHE 16 t B - 179.7 - - - - - - - - 180.3 -.8 34.1 - +* +* 17 HIS 17 B 77.3 - - - - - - - - - 175.0 - 34.9 - 18 TYR 18 B - 172.8 - - - - - - - - 182.3 -1.6 31.8 - 19 GLU 19 t B 43.0 - - 183.2 - - - - - - 182.6 -.7 32.5 - * +* +* Residue-by-residue listing for refined_10 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 - - -63.7 181.6 - - - - - - 178.7 -.7 33.5 - +* +* 21 ALA 21 T A - - - - - - - - - - 184.0 - 36.2 - 22 THR 22 T A - - -66.6 - - - - - - - 180.9 -1.4 37.0 - 23 GLY 23 h - - - - - - - - - - - 181.9 -.8 - - +* +* 24 PRO 24 H - - - - - -83.9 -83.9 -31.5 - - - 186.1 - 38.8 - +* +* * * +* 25 GLN 25 H A - 202.7 - 164.1 - -79.2 -30.8 - - - 174.3 - 32.6 - * * * 26 GLU 26 H A - 184.3 - 181.7 - -72.7 -33.7 - - - 174.5 - 33.2 - 27 ALA 27 H A - - - - - -59.0 -46.0 - - - 176.7 -.9 34.1 - +* +* 28 LEU 28 H A - - -64.8 180.8 - -57.8 -43.4 - - - 178.2 -2.3 33.6 - 29 ALA 29 H A - - - - - -57.0 -47.5 - - - 177.5 -2.0 34.1 - 30 GLN 30 H A - - -68.8 167.0 - -62.8 -51.8 - - - 180.6 -2.3 34.7 - * * 31 LEU 31 H A - - -67.4 171.1 - -60.4 -36.0 - - - 181.6 -3.5 34.3 - +* +* 32 ARG 32 H A - 186.4 - 179.3 - -63.7 -48.2 - - - 180.3 -3.0 33.0 - * * 33 GLU 33 H A 70.3 - - 177.2 - -73.8 -35.9 - - - 177.8 -1.7 30.9 - 34 LEU 34 H A - - -64.2 178.3 - -62.1 -43.0 - - - 176.3 -2.7 32.9 - 35 CYS 35 H A - 184.2 - - - -63.1 -35.6 - - - 178.4 -3.2 34.6 - * * 36 ARG 36 H A - 178.1 - - - -72.6 -30.5 - - - 176.7 -1.7 30.8 - 37 GLN 37 H A - - -48.7 - - -68.4 -17.9 - - - 182.3 -2.0 36.6 - * +* +* 38 TRP 38 H a - 163.6 - - - -97.8 -68.1 - - - 182.1 -.6 33.2 - * +** +** +* +** 39 LEU 39 H A - - -60.1 174.6 - -63.4 -38.6 - - - 178.9 -3.3 34.4 - +* +* 40 ARG 40 h l - - -57.2 180.2 - - - - - - 180.9 -1.0 31.2 - * * 41 PRO 41 T - - - - - -67.6 - - - - - 180.4 - 38.9 - * * 42 GLU 42 T A - 188.1 - - - - - - - - 184.7 - 35.0 - 43 VAL 43 T A - - -60.6 - - - - - - - 180.5 -.8 32.4 - +* +* 44 ARG 44 t B - - -62.3 186.3 - - - - - - 181.5 -3.3 31.9 - +* +* 45 SER 45 h B - - -52.8 - - - - - - - 182.5 - 35.2 - 46 LYS 46 H A - - -62.3 167.8 - -65.8 -37.0 - - - 182.2 - 35.8 - 47 GLU 47 H A - - -57.2 - - -58.5 -43.7 - - - 179.8 - 35.6 - 48 GLN 48 H A - - -66.0 - - -61.4 -33.4 - - - 179.4 - 32.7 - 49 MET 49 H A - - -60.0 181.7 - -64.6 -38.8 - - - 172.4 -.9 32.4 - * +* +* 50 LEU 50 H A - - -76.4 - - -57.5 -52.3 - - - 181.8 -1.3 34.7 - * * 51 GLU 51 H A - 179.6 - 175.4 - -55.6 -46.5 - - - 178.8 -2.0 34.9 - 52 LEU 52 H A - - -63.1 176.8 - -65.1 -45.7 - - - 180.8 -2.8 33.8 - 53 LEU 53 H A - 181.1 - - - -69.2 -33.0 - - - 176.0 -2.7 33.6 - 54 VAL 54 H A - 176.5 - - - -63.1 -39.6 - - - 176.7 -3.0 32.4 - * * 55 LEU 55 H A - 181.0 - - - -60.0 -46.4 - - - 178.2 -1.7 35.8 - 56 GLU 56 H A - - -71.2 - - -52.8 -52.0 - - - 183.5 -1.8 35.4 - * * * Residue-by-residue listing for refined_10 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 - 192.0 - - - -73.6 -46.2 - - - 182.4 -2.3 33.3 - 58 PHE 58 H A - 178.6 - - - -53.8 -45.7 - - - 178.7 -3.2 33.5 - * * 59 LEU 59 H A - - -87.9 - - -60.9 -42.6 - - - 180.1 -2.6 29.9 - * * * 60 GLY 60 H - - - - - - -80.8 -15.1 - - - 177.4 -1.4 - - * ** ** 61 ALA 61 H A - - - - - -74.4 -35.0 - - - 175.9 -1.8 34.1 - 62 LEU 62 h b - - -67.3 170.6 - - - - - - 176.7 -1.7 36.9 - 63 PRO 63 h - - - - - -71.9 - - - - - 181.0 - 39.3 - +* +* 64 PRO 64 H - - - - - -42.2 -42.2 -46.6 - - - 180.2 - 38.7 - ** +* * ** 65 GLU 65 H A - 172.6 - - - -60.3 -49.6 - - - 181.8 - 35.5 - 66 ILE 66 H A - - -59.2 186.0 - -73.4 -38.0 - - - 180.1 - 33.5 - 67 GLN 67 H A - 179.6 - 179.1 - -64.7 -43.2 - - - 181.5 -3.5 34.3 - ** ** 68 ALA 68 H A - - - - - -59.4 -31.0 - - - 181.0 -2.9 33.7 - * * 69 ARG 69 H A - - -53.2 - - -71.0 -47.5 - - - 176.6 -.9 33.5 - * * 70 VAL 70 H A - 173.7 - - - -59.4 -50.8 - - - 179.7 -1.6 35.9 - * * 71 GLN 71 H A - - -99.7 - - -55.2 -29.4 - - - 178.8 -2.9 32.9 - ** * ** 72 GLY 72 H - - - - - - -67.2 -40.2 - - - 181.6 -1.1 - - * * 73 GLN 73 H A - - -63.9 - - -95.3 -41.0 - - - 186.9 -1.1 33.6 - +** * * +** 74 ARG 74 h l - - -63.9 - - - - - - - 182.3 -3.5 31.5 - ** ** 75 PRO 75 - - - - - -62.4 - - - - - 181.3 - 39.7 - +* +* 76 GLY 76 S - - - - - - - - - - - 179.3 - - - 77 SER 77 h B - - -57.9 - - - - - - - 180.9 - 34.1 - 78 PRO 78 H - - - - - -57.8 -57.8 -44.1 - - - 182.3 - 37.2 - 79 GLU 79 H A - - -45.4 - - -68.0 -30.4 - - - 177.1 - 33.4 - * * 80 GLU 80 H A - 186.4 - - - -69.3 -47.9 - - - 175.8 - 34.8 - 81 ALA 81 H A - - - - - -56.4 -44.6 - - - 179.0 -2.5 34.3 - 82 ALA 82 H A - - - - - -58.2 -36.7 - - - 178.5 -3.0 34.3 - * * 83 ALA 83 H A - - - - - -74.1 -38.0 - - - 180.1 -1.4 33.6 - 84 LEU 84 H A - - -47.7 186.2 - -62.8 -49.2 - - - 185.1 -2.3 36.6 - * * 85 VAL 85 H A - - -57.4 - - -69.3 -33.0 - - - 180.2 -2.8 32.1 - * * 86 ASP 86 H A - 184.7 - - - -62.8 -35.5 - - - 180.0 -1.5 34.1 - 87 GLY 87 H - - - - - - -66.5 -44.0 - - - 183.2 -1.3 - - 88 LEU 88 H A 56.4 - - - - -91.1 -10.0 - - - 171.4 -1.3 30.3 - ** +** * * * +** 89 ARG 89 h b - 176.2 - 178.9 - - - - - - 183.9 -1.6 36.6 - 90 ARG 90 B - 192.4 - - - - - - - - 177.1 - 34.6 - 91 GLU 91 B 58.7 - - 171.8 - - - - - - 177.7 -.7 34.4 - +* +* 92 PRO 92 S - - - - - -59.4 - - - - - 183.2 - 38.5 - * * Residue-by-residue listing for refined_10 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 - - - - - - - - - - - 179.4 - - - 94 GLY 94 - - - - - - - - - - - - -1.2 - - * * 95 GLY 301 - - - - - - - - - - - 181.4 - - - 96 SER 302 B - 180.9 - - - - - - - - 179.6 - 34.4 - 97 ASP 303 B 63.9 - - - - - - - - - 183.1 - 34.0 - 98 PRO 304 S - - - - - -78.7 - - - - - 182.5 - 38.7 - * * * 99 GLY 305 h - - - - - - - - - - - 180.7 - - - 100 PRO 306 H - - - - - -64.7 -64.7 -25.6 - - - 179.4 - 38.5 - * * * 101 GLU 307 H A - - -58.7 183.2 - -67.5 -47.9 - - - 178.4 - 33.9 - 102 ALA 308 H A - - - - - -71.9 -31.4 - - - 177.8 - 33.8 - 103 ALA 309 H A - - - - - -58.0 -48.3 - - - 179.3 -2.2 34.3 - 104 ARG 310 H A - 186.2 - 182.0 - -64.5 -37.2 - - - 182.0 -2.2 33.4 - 105 LEU 311 H A - 175.2 - - - -63.5 -40.2 - - - 179.4 -1.5 34.9 - 106 ARG 312 H A - - -60.9 177.8 - -73.9 -34.0 - - - 177.8 -2.3 33.0 - 107 PHE 313 H A - 167.4 - - - -74.5 -49.4 - - - 187.9 -2.1 34.8 - * * 108 ARG 314 H A - 186.9 - - - -73.8 -34.2 - - - 180.5 -3.8 34.1 - ** ** 109 CYS 315 h A - - -60.1 - - - - - - - 176.9 -1.6 32.3 - 110 PHE 316 t B - 178.3 - - - - - - - - 178.2 -.7 34.8 - +* +* 111 HIS 317 B 72.0 - - - - - - - - - 173.9 - 34.5 - * * 112 TYR 318 B - 164.9 - - - - - - - - 181.8 -1.7 33.3 - * * 113 GLU 319 t B 51.7 - - 175.3 - - - - - - 179.7 -.7 32.0 - +* +* 114 GLU 320 T A - - -60.3 177.3 - - - - - - 178.1 -.6 34.8 - +* +* 115 ALA 321 T A - - - - - - - - - - 180.7 - 33.5 - 116 THR 322 T A - 198.9 - - - - - - - - 181.1 -1.6 34.5 - 117 GLY 323 h - - - - - - - - - - - 183.1 -1.4 - - 118 PRO 324 H - - - - - -64.3 -64.3 -34.9 - - - 180.6 - 38.0 - * * 119 GLN 325 H A - - -88.5 - - -71.0 -39.1 - - - 178.1 - 33.2 - * * 120 GLU 326 H A - 178.2 - 169.7 - -73.5 -33.5 - - - 173.6 - 32.4 - * * 121 ALA 327 H A - - - - - -61.1 -45.2 - - - 176.6 -2.4 34.2 - 122 LEU 328 H A - - -68.5 178.1 - -56.3 -41.1 - - - 178.7 -2.4 33.3 - 123 ALA 329 H A - - - - - -58.6 -48.2 - - - 178.2 -1.5 34.1 - 124 GLN 330 H A - - -68.4 169.5 - -61.3 -51.0 - - - 179.6 -2.0 34.2 - * * 125 LEU 331 H A - - -68.9 173.5 - -60.0 -43.1 - - - 183.9 -3.2 34.8 - +* +* 126 ARG 332 H A - 185.9 - 175.0 - -58.4 -46.4 - - - 179.8 -3.3 33.2 - +* +* 127 GLU 333 H A 71.3 - - 178.8 - -75.2 -38.3 - - - 179.9 -1.6 31.2 - 128 LEU 334 H A - - -65.9 178.1 - -61.5 -40.3 - - - 176.8 -2.2 32.5 - 129 CYS 335 H A - 182.9 - - - -63.8 -36.8 - - - 179.7 -3.3 34.9 - +* +* 130 ARG 336 H A - 194.0 - 172.5 - -73.1 -29.3 - - - 176.2 -1.3 31.1 - 131 GLN 337 H A - - -47.8 - - -65.5 -16.6 - - - 180.6 -1.9 36.3 - * ** ** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 132 TRP 338 H a - 162.0 - - - -102.4 -49.4 - - - 180.1 -.7 32.3 - * *** +* *** 133 LEU 339 H A - - -62.8 179.2 - -77.1 -43.8 - - - 174.6 -3.2 31.7 - +* +* 134 ARG 340 h l - - -55.2 180.1 - - - - - - 178.3 -1.7 32.6 - 135 PRO 341 T - - - - - -58.4 - - - - - 183.4 - 40.2 - +* +* 136 GLU 342 T A - 191.3 - - - - - - - - 180.8 - 34.0 - 137 VAL 343 T A - - -60.7 - - - - - - - 181.9 -1.3 32.6 - 138 ARG 344 t B - - -67.0 179.8 - - - - - - 178.7 -3.3 33.3 - +* +* 139 SER 345 h B - - -57.7 - - - - - - - 181.6 - 35.2 - 140 LYS 346 H A - - -67.7 170.4 - -65.2 -32.4 - - - 180.6 - 34.1 - 141 GLU 347 H A - - -60.0 - - -54.6 -50.4 - - - 178.8 - 35.4 - 142 GLN 348 H A - - -61.4 - - -56.1 -41.8 - - - 181.3 - 34.0 - 143 MET 349 H A - - -60.1 180.2 - -63.2 -46.3 - - - 173.5 -1.0 33.3 - * * * 144 LEU 350 H A - - -81.9 - - -52.3 -52.7 - - - 182.8 -2.3 34.9 - * * * * 145 GLU 351 H A - 182.5 - 175.8 - -59.7 -46.9 - - - 179.1 -2.4 34.6 - 146 LEU 352 H A - - -61.8 176.8 - -61.7 -43.8 - - - 180.7 -2.9 34.3 - * * 147 LEU 353 H A - 181.9 - - - -72.6 -29.8 - - - 173.2 -2.8 31.2 - * * 148 VAL 354 H A - 175.1 - - - -57.9 -47.9 - - - 177.5 -2.5 33.5 - 149 LEU 355 H A - 173.2 - - - -56.2 -45.8 - - - 183.1 -2.0 35.3 - 150 GLU 356 H A - 189.4 - - - -53.8 -47.2 - - - 178.3 -1.7 34.2 - 151 GLN 357 H A - 190.9 - - - -75.7 -47.1 - - - 184.4 -1.9 33.3 - 152 PHE 358 H A - 170.4 - - - -53.1 -47.8 - - - 186.0 -3.0 35.6 - * * * * 153 LEU 359 H A - 198.1 - - - -66.9 -35.5 - - - 178.3 -3.3 35.2 - +* +* 154 GLY 360 H - - - - - - -81.2 -15.2 - - - 178.7 -.9 - - * ** +* ** 155 ALA 361 H A - - - - - -76.5 -28.1 - - - 176.5 -1.3 34.1 - 156 LEU 362 h b - - -64.4 169.5 - - - - - - 177.0 -1.2 37.0 - * * 157 PRO 363 h - - - - - -71.9 - - - - - 183.2 - 38.8 - * * 158 PRO 364 H - - - - - -47.7 -47.7 -43.8 - - - 180.1 - 37.4 - +* * * +* 159 GLU 365 H A - 170.4 - - - -62.4 -50.3 - - - 184.1 - 35.8 - 160 ILE 366 H A - - -58.0 185.8 - -70.1 -38.6 - - - 179.8 - 33.1 - 161 GLN 367 H A - 180.1 - 177.5 - -68.6 -41.3 - - - 180.7 -3.2 34.2 - +* +* 162 ALA 368 H A - - - - - -63.9 -32.9 - - - 178.4 -2.6 33.3 - 163 ARG 369 H A - - -60.3 - - -61.7 -50.7 - - - 178.2 -1.5 34.0 - * * 164 VAL 370 H A - 173.6 - - - -60.7 -40.4 - - - 185.4 -1.5 36.3 - 165 GLN 371 H A - 231.9 - - - -56.4 -30.0 - - - 179.9 -2.3 34.5 - +** +** 166 GLY 372 h - - - - - - - - - - - 181.6 -1.0 - - * * 167 GLN 373 T a - - -61.0 - - - - - - - 182.7 -2.1 33.3 - 168 ARG 374 t l - - -58.2 - - - - - - - 182.2 -3.2 32.2 - +* +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 169 PRO 375 - - - - - -65.4 - - - - - 178.6 - 39.4 - +* +* 170 GLY 376 S - - - - - - - - - - - 180.4 - - - 171 SER 377 h B - - -57.7 - - - - - - - 185.1 - 34.1 - 172 PRO 378 H - - - - - -61.9 -61.9 -44.5 - - - 182.3 - 37.5 - * * 173 GLU 379 H A - - -62.6 169.1 - -69.3 -30.1 - - - 176.0 - 32.7 - 174 GLU 380 H A - 187.0 - - - -68.2 -48.3 - - - 175.8 - 35.0 - 175 ALA 381 H A - - - - - -57.3 -40.8 - - - 177.3 -2.3 34.0 - 176 ALA 382 H A - - - - - -56.6 -46.5 - - - 179.2 -2.7 34.4 - 177 ALA 383 H A - - - - - -62.4 -45.7 - - - 182.4 -2.1 33.8 - 178 LEU 384 H A - - -44.5 184.3 - -59.3 -48.6 - - - 184.4 -2.5 36.7 - * * 179 VAL 385 H A - - -58.5 - - -74.6 -34.9 - - - 184.2 -2.7 32.3 - 180 ASP 386 H A - 186.1 - - - -58.9 -34.7 - - - 179.6 -2.6 33.8 - 181 GLY 387 H - - - - - - -74.0 -37.6 - - - 181.8 -1.3 - - * * 182 LEU 388 H A 54.7 - - - - -91.8 -11.4 - - - 173.1 -.9 28.9 - ** ** * +* * ** 183 ARG 389 h b - 167.2 - 185.3 - - - - - - 177.8 -2.0 38.0 - * * 184 ARG 390 B - 192.9 - - - - - - - - 175.9 - 33.8 - 185 GLU 391 B 62.6 - - 170.7 - - - - - - 176.5 -1.0 34.2 - * * 186 PRO 392 S - - - - - -66.6 - - - - - 179.1 - 38.4 - * * 187 GLY 393 - - - - - - - - - - - 181.5 -.8 - - +* +* 188 GLY 394 - - - - - - - - - - - - -1.5 - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +** ** ** *** +** * ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 62.2 181.8 -62.8 177.4 -64.5 -65.8 -39.9 - - - 179.8 -2.0 34.4 Standard deviations: 9.8 11.1 9.4 5.7 10.3 9.7 9.3 - - - 2.9 .8 2.0 Numbers of values: 12 57 63 53 18 122 122 0 0 0 186 125 170 0 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_10 Page 7 ---------------------------------------- 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 - 1.235 1.499 - 1.457 - 116.66 120.21 - 110.91 - 123.13 2 SER 2 1.303 1.250 1.520 1.543 1.426 121.73 115.55 121.17 111.15 108.78 110.46 123.25 +* +* +* 3 ASP 3 1.301 1.228 1.525 1.544 1.446 122.52 119.37 119.39 111.27 108.42 111.32 121.24 +* +* * +* 4 PRO 4 1.351 1.220 1.543 1.527 1.467 121.85 118.15 119.84 110.42 114.65 103.23 122.00 * * 5 GLY 5 1.322 1.233 1.523 - 1.454 120.20 118.50 119.96 - 112.31 - 121.55 6 PRO 6 1.350 1.224 1.536 1.530 1.472 122.82 118.19 120.31 110.22 113.43 103.93 121.50 7 GLU 7 1.329 1.221 1.503 1.498 1.442 119.40 116.97 120.13 111.47 112.60 113.73 122.89 * +* * +* +* 8 ALA 8 1.318 1.226 1.515 1.510 1.448 120.51 115.30 121.30 111.46 108.38 111.51 123.38 * * 9 ALA 9 1.328 1.227 1.518 1.510 1.444 122.25 115.67 120.89 110.03 108.64 110.04 123.43 10 ARG 10 1.337 1.208 1.523 1.535 1.453 122.56 116.90 120.38 110.06 111.14 111.60 122.71 * * 11 LEU 11 1.321 1.223 1.531 1.526 1.416 122.91 115.90 120.83 111.46 109.37 107.95 123.21 ** * ** 12 ARG 12 1.327 1.228 1.520 1.520 1.467 122.55 114.88 121.41 108.45 110.02 109.80 123.70 13 PHE 13 1.307 1.202 1.538 1.530 1.439 123.49 117.80 120.09 111.44 113.13 108.01 122.07 +* * * +* Residue-by-residue listing for refined_10 Page 8 ---------------------------------------- ................................................................................................................................... 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 1.316 1.237 1.528 1.547 1.462 121.59 116.58 120.62 112.18 111.66 110.74 122.77 * * 15 CYS 15 1.317 1.238 1.535 1.528 1.454 121.86 116.72 120.29 111.13 111.88 111.21 122.98 16 PHE 16 1.336 1.240 1.528 1.540 1.459 122.02 116.08 120.93 110.67 109.64 110.59 122.96 17 HIS 17 1.309 1.237 1.504 1.568 1.445 121.43 117.97 119.76 109.24 108.30 111.74 122.27 * * +* * +* 18 TYR 18 1.295 1.233 1.508 1.516 1.423 118.20 114.19 121.86 112.04 109.45 112.59 123.95 ** +* +* * * * ** 19 GLU 19 1.284 1.231 1.529 1.561 1.414 123.66 115.89 121.00 114.90 110.63 108.80 123.07 *** +* ** * +** * *** 20 GLU 20 1.349 1.221 1.510 1.528 1.477 122.91 116.40 120.31 108.69 112.01 112.45 123.28 * * * 21 ALA 21 1.316 1.222 1.521 1.512 1.465 123.09 114.24 122.06 108.86 110.21 108.71 123.69 * * * 22 THR 22 1.280 1.234 1.543 1.496 1.413 124.36 116.37 121.06 112.14 112.27 103.93 122.47 +*** +* ** * * **** **** 23 GLY 23 1.314 1.237 1.514 - 1.445 120.86 119.61 119.97 - 110.71 - 120.42 * +* +* +* 24 PRO 24 1.331 1.225 1.510 1.514 1.436 120.70 116.05 121.15 110.54 112.59 103.01 122.79 +* +* 25 GLN 25 1.288 1.227 1.518 1.478 1.389 121.61 117.32 120.39 114.58 111.37 108.00 122.25 +** +** +*** ** * +*** 26 GLU 26 1.344 1.236 1.514 1.520 1.445 119.23 115.26 121.50 110.11 107.78 113.00 123.24 * * * * * 27 ALA 27 1.327 1.212 1.520 1.518 1.442 121.90 116.42 120.15 110.86 108.86 110.54 123.40 28 LEU 28 1.337 1.210 1.514 1.530 1.469 122.37 116.97 119.96 108.90 111.65 112.30 123.07 * * * 29 ALA 29 1.329 1.245 1.525 1.519 1.465 121.85 115.36 121.00 110.40 110.33 110.35 123.63 30 GLN 30 1.325 1.229 1.521 1.508 1.448 122.82 115.48 121.04 110.42 111.13 109.23 123.39 * * 31 LEU 31 1.320 1.207 1.502 1.526 1.455 123.63 116.84 120.12 109.97 112.15 110.24 123.03 * * * * 32 ARG 32 1.309 1.235 1.512 1.521 1.439 121.43 117.49 120.04 110.69 111.08 111.62 122.45 * * 33 GLU 33 1.333 1.199 1.515 1.537 1.437 118.49 117.55 119.46 111.30 110.14 114.45 122.98 +* * +* ** ** 34 LEU 34 1.345 1.226 1.519 1.537 1.474 121.70 116.13 120.60 110.30 110.75 112.12 123.27 * * 35 CYS 35 1.322 1.225 1.531 1.543 1.447 122.37 116.36 121.18 110.98 109.18 109.77 122.44 36 ARG 36 1.331 1.215 1.533 1.547 1.423 122.05 117.34 119.84 114.94 112.13 110.23 122.80 +* +** +** 37 GLN 37 1.338 1.231 1.532 1.540 1.488 122.04 114.62 121.57 105.96 108.06 111.55 123.78 +* ** * ** 38 TRP 38 1.310 1.231 1.548 1.542 1.436 124.62 117.55 119.68 113.22 112.92 108.28 122.77 * * * +* +* * +* 39 LEU 39 1.340 1.230 1.521 1.547 1.475 121.93 114.75 120.99 109.63 109.92 111.12 124.25 40 ARG 40 1.333 1.230 1.529 1.527 1.456 124.88 117.32 120.92 111.23 113.28 112.50 121.76 +* * +* 41 PRO 41 1.345 1.232 1.525 1.533 1.467 123.21 116.30 120.79 109.97 112.66 103.44 122.91 42 GLU 42 1.311 1.229 1.526 1.533 1.443 121.27 116.34 120.88 109.68 109.83 110.24 122.75 * * 43 VAL 43 1.323 1.227 1.525 1.556 1.455 120.80 117.63 120.28 110.11 113.26 112.33 122.09 44 ARG 44 1.319 1.240 1.503 1.535 1.450 119.78 115.10 121.07 110.71 111.41 113.10 123.82 * * +* +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 SER 45 1.300 1.243 1.528 1.521 1.425 122.92 115.24 121.15 110.84 110.38 108.64 123.61 ** +* * ** 46 LYS 46 1.308 1.221 1.528 1.518 1.449 123.73 116.09 120.65 110.08 111.55 108.01 123.24 +* * * +* 47 GLU 47 1.325 1.237 1.530 1.520 1.477 122.86 115.48 121.35 107.96 110.96 110.31 123.17 * * 48 GLN 48 1.315 1.227 1.519 1.550 1.452 123.04 116.65 120.58 109.71 111.84 112.93 122.77 * * * * 49 MET 49 1.321 1.230 1.515 1.507 1.452 121.13 115.82 120.60 112.49 110.71 110.56 123.57 * * * 50 LEU 50 1.336 1.210 1.504 1.558 1.471 122.39 115.74 120.61 108.58 109.63 112.08 123.62 * * * * 51 GLU 51 1.320 1.242 1.538 1.519 1.429 123.73 116.13 120.88 111.57 111.60 107.86 122.98 +* * +* +* 52 LEU 52 1.318 1.232 1.530 1.531 1.435 122.01 116.81 120.41 111.14 111.25 110.04 122.77 * * 53 LEU 53 1.326 1.238 1.547 1.497 1.431 121.82 117.52 120.24 112.60 113.15 107.82 122.24 * +* * * +* +* 54 VAL 54 1.325 1.222 1.531 1.568 1.460 120.98 116.28 120.55 110.77 109.73 113.08 123.14 * * 55 LEU 55 1.333 1.236 1.530 1.530 1.468 122.51 114.96 120.85 109.18 109.51 109.40 124.19 56 GLU 56 1.332 1.241 1.520 1.540 1.479 123.70 116.18 121.10 108.35 112.03 110.18 122.72 * * * 57 GLN 57 1.312 1.231 1.517 1.539 1.437 120.67 116.69 119.65 111.99 110.20 110.42 123.63 * * * 58 PHE 58 1.341 1.237 1.518 1.549 1.466 122.68 116.21 120.67 110.55 111.06 111.21 123.10 59 LEU 59 1.321 1.214 1.509 1.540 1.452 121.15 117.72 119.68 113.25 113.37 112.32 122.54 +* * +* 60 GLY 60 1.320 1.240 1.513 - 1.452 119.57 116.02 120.81 - 112.36 - 123.16 61 ALA 61 1.322 1.240 1.510 1.522 1.445 122.28 115.05 120.64 110.72 109.17 110.66 124.30 62 LEU 62 1.335 1.247 1.528 1.535 1.458 124.08 118.02 120.21 107.93 110.17 109.01 121.76 * * * 63 PRO 63 1.341 1.233 1.521 1.534 1.449 121.79 118.41 119.11 110.10 108.51 103.59 122.47 * * * * 64 PRO 64 1.342 1.223 1.540 1.517 1.477 123.71 116.84 120.23 110.49 113.81 102.55 122.91 65 GLU 65 1.333 1.225 1.526 1.541 1.471 122.51 116.61 120.71 109.96 111.61 108.64 122.63 * * 66 ILE 66 1.310 1.242 1.537 1.541 1.430 121.20 115.82 121.15 111.84 111.18 109.90 122.98 * * * * 67 GLN 67 1.314 1.237 1.526 1.521 1.443 122.57 116.57 120.49 110.40 111.19 110.02 122.92 * * 68 ALA 68 1.326 1.235 1.523 1.519 1.467 121.88 115.89 121.08 110.21 111.43 110.70 123.01 69 ARG 69 1.315 1.222 1.530 1.525 1.446 121.83 116.56 120.64 111.56 110.28 110.16 122.78 * * 70 VAL 70 1.332 1.227 1.513 1.537 1.476 121.89 114.69 121.29 106.92 110.20 111.47 124.02 71 GLN 71 1.317 1.233 1.533 1.536 1.459 123.81 116.39 120.45 111.70 112.45 110.18 123.15 * * 72 GLY 72 1.327 1.227 1.525 - 1.443 121.44 117.39 120.26 - 112.87 - 122.34 73 GLN 73 1.331 1.223 1.503 1.547 1.460 120.33 115.67 120.36 107.77 111.14 113.78 123.95 * * +* +* 74 ARG 74 1.327 1.221 1.539 1.539 1.460 123.84 116.71 120.91 111.53 110.34 113.06 122.29 * +* +* 75 PRO 75 1.352 1.225 1.530 1.532 1.486 123.78 116.16 121.01 108.91 114.27 102.95 122.82 * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 76 GLY 76 1.310 1.231 1.518 - 1.448 121.20 117.33 120.57 - 113.24 - 122.11 * * 77 SER 77 1.316 1.243 1.536 1.521 1.451 121.35 117.35 120.26 110.61 110.81 109.98 122.36 78 PRO 78 1.350 1.228 1.531 1.534 1.468 123.36 117.46 120.04 110.22 114.22 105.22 122.49 ** ** 79 GLU 79 1.323 1.234 1.515 1.535 1.467 121.56 115.42 121.20 110.02 110.16 111.97 123.38 80 GLU 80 1.314 1.215 1.528 1.531 1.419 122.92 116.60 120.38 111.92 107.80 108.99 122.98 * ** * ** 81 ALA 81 1.350 1.223 1.533 1.517 1.455 122.16 116.07 120.56 110.28 110.64 109.99 123.35 * * 82 ALA 82 1.336 1.224 1.529 1.529 1.469 123.31 115.58 121.44 110.28 111.16 109.93 122.98 83 ALA 83 1.290 1.235 1.528 1.522 1.444 122.73 116.84 120.35 110.76 110.79 110.67 122.81 +** +** 84 LEU 84 1.341 1.245 1.512 1.547 1.470 121.39 114.32 121.66 105.58 108.79 112.21 123.97 ** * ** 85 VAL 85 1.320 1.210 1.502 1.551 1.436 122.72 116.95 119.78 111.05 112.11 112.46 123.24 * * * * 86 ASP 86 1.326 1.228 1.517 1.527 1.465 121.59 115.79 120.99 109.35 110.44 111.44 123.21 87 GLY 87 1.318 1.219 1.516 - 1.444 121.05 116.80 120.59 - 112.91 - 122.59 88 LEU 88 1.315 1.241 1.538 1.529 1.459 121.20 114.61 121.39 114.99 113.06 109.93 123.97 * +** +** 89 ARG 89 1.321 1.242 1.524 1.525 1.449 126.03 115.11 121.39 111.12 109.61 106.26 123.46 ** ** ** 90 ARG 90 1.299 1.238 1.524 1.557 1.447 122.68 115.73 120.82 111.86 109.89 108.88 123.42 ** * ** 91 GLU 91 1.313 1.240 1.532 1.534 1.452 123.23 118.89 119.40 109.92 109.19 111.01 121.69 * * * 92 PRO 92 1.357 1.240 1.530 1.534 1.469 122.29 116.04 121.03 110.30 111.26 103.95 122.92 * * 93 GLY 93 1.308 1.234 1.508 - 1.430 120.94 116.36 120.54 - 110.63 - 123.07 * * * 94 GLY 94 1.314 1.243 1.512 - 1.454 120.83 - 120.15 - 112.19 - - * * 95 GLY 301 - 1.232 1.512 - 1.448 - 115.95 120.79 - 111.60 - 123.25 96 SER 302 1.308 1.239 1.528 1.539 1.439 122.07 115.33 121.10 110.60 110.63 110.02 123.57 +* +* 97 ASP 303 1.307 1.244 1.535 1.548 1.441 123.84 119.44 119.46 111.15 107.56 111.00 121.10 +* * +* * * +* 98 PRO 304 1.354 1.233 1.540 1.528 1.473 122.12 117.12 120.35 110.26 114.22 102.87 122.52 99 GLY 305 1.314 1.230 1.521 - 1.441 120.42 118.96 119.88 - 111.22 - 121.16 * * * * 100 PRO 306 1.349 1.234 1.527 1.532 1.479 122.54 115.60 121.23 110.06 111.86 103.91 123.16 101 GLU 307 1.322 1.235 1.522 1.520 1.442 122.11 115.95 120.76 110.85 110.32 110.34 123.26 102 ALA 308 1.328 1.229 1.520 1.521 1.449 121.60 115.67 120.90 110.84 109.74 110.62 123.42 103 ALA 309 1.328 1.235 1.513 1.508 1.451 122.56 116.72 120.37 109.76 110.81 110.60 122.90 104 ARG 310 1.340 1.207 1.516 1.523 1.444 120.27 116.50 120.67 108.64 110.43 113.20 122.81 * +* +* 105 LEU 311 1.317 1.233 1.542 1.524 1.416 122.99 116.51 120.94 112.02 110.95 107.73 122.52 ** * +* ** 106 ARG 312 1.314 1.229 1.527 1.523 1.457 121.57 115.62 121.00 111.81 111.06 110.31 123.37 * * 107 PHE 313 1.312 1.209 1.536 1.541 1.456 123.01 116.39 121.04 110.34 112.55 108.96 122.55 * * * 108 ARG 314 1.300 1.235 1.525 1.524 1.452 122.57 116.75 120.48 111.60 112.60 108.57 122.75 ** * ** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 109 CYS 315 1.310 1.240 1.527 1.520 1.450 121.14 116.15 120.49 111.91 111.69 110.93 123.35 * * 110 PHE 316 1.339 1.243 1.517 1.548 1.455 122.43 116.15 120.91 110.33 109.16 110.14 122.90 111 HIS 317 1.301 1.231 1.495 1.573 1.434 120.45 117.82 119.72 109.79 107.52 112.21 122.44 ** * ** * * * ** 112 TYR 318 1.296 1.229 1.491 1.520 1.420 118.57 115.32 121.08 111.35 107.88 111.80 123.58 ** +* +* +* * ** 113 GLU 319 1.280 1.238 1.507 1.543 1.403 121.46 115.18 121.47 113.34 110.76 110.90 123.35 *** +** +* *** 114 GLU 320 1.315 1.217 1.518 1.518 1.453 122.90 115.73 120.97 109.54 110.38 110.20 123.30 115 ALA 321 1.318 1.231 1.529 1.517 1.438 122.43 117.76 120.14 110.76 111.64 110.48 122.10 * * 116 THR 322 1.332 1.214 1.554 1.588 1.450 119.46 116.61 121.00 110.79 109.34 110.42 122.28 * +* * +* 117 GLY 323 1.335 1.227 1.526 - 1.458 121.04 119.42 119.67 - 111.38 - 120.91 * * * 118 PRO 324 1.349 1.225 1.535 1.516 1.471 122.31 117.71 120.05 110.57 114.47 103.42 122.23 * * 119 GLN 325 1.329 1.238 1.513 1.537 1.466 120.47 115.15 121.48 109.44 110.15 112.95 123.36 * * 120 GLU 326 1.306 1.238 1.534 1.524 1.442 121.94 116.24 121.08 113.21 110.38 110.12 122.68 +* +* +* 121 ALA 327 1.322 1.222 1.519 1.521 1.456 121.81 116.06 120.45 110.36 109.13 110.69 123.47 122 LEU 328 1.337 1.207 1.508 1.528 1.466 122.34 117.15 119.75 109.07 111.90 112.43 123.10 * * * 123 ALA 329 1.329 1.237 1.522 1.521 1.463 121.50 115.33 121.13 110.23 110.05 110.60 123.53 124 GLN 330 1.315 1.235 1.525 1.509 1.442 122.93 115.21 121.18 111.68 111.25 108.67 123.54 * * * * 125 LEU 331 1.314 1.220 1.512 1.524 1.456 123.73 116.22 120.51 109.68 112.51 109.55 123.26 * * * 126 ARG 332 1.307 1.236 1.520 1.521 1.446 122.69 117.55 120.17 111.47 111.92 110.16 122.26 +* +* 127 GLU 333 1.329 1.208 1.523 1.541 1.443 118.20 117.44 119.71 111.17 110.27 114.08 122.82 * +* ** ** 128 LEU 334 1.346 1.227 1.514 1.530 1.475 121.72 115.89 120.79 110.62 111.46 112.10 123.31 * * 129 CYS 335 1.313 1.229 1.524 1.532 1.442 122.20 116.08 121.22 110.30 109.22 109.98 122.70 * * 130 ARG 336 1.323 1.210 1.521 1.516 1.439 121.61 117.16 120.01 112.37 111.79 112.12 122.82 * * * 131 GLN 337 1.333 1.228 1.536 1.534 1.485 122.15 114.87 121.83 106.74 108.32 111.16 123.26 * +* * +* 132 TRP 338 1.302 1.238 1.563 1.545 1.425 124.15 118.50 119.64 114.63 112.60 108.13 121.85 +* +* +* * * ** * ** 133 LEU 339 1.340 1.227 1.536 1.549 1.471 120.37 116.23 120.36 111.67 110.82 112.51 123.41 * * 134 ARG 340 1.344 1.222 1.548 1.533 1.478 124.27 118.17 120.43 110.20 114.49 111.10 121.39 * * * * * * * 135 PRO 341 1.349 1.225 1.523 1.525 1.486 123.70 116.93 120.58 107.79 113.94 103.30 122.48 * * * 136 GLU 342 1.304 1.227 1.534 1.527 1.440 120.72 116.71 120.90 111.38 110.63 109.68 122.39 +* +* 137 VAL 343 1.319 1.233 1.525 1.558 1.456 120.62 116.60 120.69 110.23 112.16 112.45 122.71 138 ARG 344 1.314 1.232 1.501 1.526 1.447 121.34 114.59 121.35 109.91 112.54 111.53 124.06 * * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 139 SER 345 1.306 1.242 1.530 1.526 1.427 123.40 115.07 121.32 110.15 110.05 109.44 123.61 +* +* +* 140 LYS 346 1.303 1.219 1.538 1.514 1.444 124.08 117.00 120.11 112.11 113.33 107.69 122.88 +* * * +* +* 141 GLU 347 1.328 1.244 1.507 1.539 1.490 122.92 113.76 121.66 106.75 110.60 112.12 124.56 +* * +* +* 142 GLN 348 1.304 1.220 1.524 1.560 1.445 124.30 116.17 120.62 109.01 110.84 112.22 123.20 +* * * * +* 143 MET 349 1.324 1.235 1.502 1.502 1.462 122.46 115.71 120.42 111.15 111.23 110.37 123.87 * * * 144 LEU 350 1.334 1.214 1.509 1.557 1.464 122.45 116.14 120.07 108.75 110.14 111.44 123.72 * * 145 GLU 351 1.323 1.246 1.542 1.518 1.431 123.57 116.35 120.79 111.71 111.85 108.00 122.85 * * * * 146 LEU 352 1.324 1.242 1.524 1.533 1.443 122.15 116.31 120.64 110.23 110.93 110.35 123.04 147 LEU 353 1.319 1.237 1.554 1.524 1.419 122.06 117.49 120.23 116.26 112.35 107.90 122.26 * ** *** +* *** 148 VAL 354 1.339 1.226 1.531 1.569 1.474 121.03 116.08 120.55 109.15 109.22 113.17 123.33 * * 149 LEU 355 1.344 1.221 1.514 1.539 1.473 122.20 115.05 120.81 108.08 110.84 111.07 124.14 * * * 150 GLU 356 1.312 1.238 1.539 1.532 1.444 123.44 116.89 121.09 110.75 111.82 109.63 122.01 * * 151 GLN 357 1.315 1.228 1.511 1.532 1.443 119.66 115.75 120.10 111.37 109.98 110.97 124.10 * * * 152 PHE 358 1.334 1.239 1.500 1.543 1.464 123.37 115.17 121.25 108.27 112.14 110.27 123.57 * * 153 LEU 359 1.291 1.221 1.523 1.512 1.404 122.40 115.99 120.73 112.20 109.76 107.52 123.23 +** +** * +* +** 154 GLY 360 1.327 1.233 1.520 - 1.441 121.02 116.48 120.45 - 112.45 - 123.05 155 ALA 361 1.327 1.237 1.514 1.525 1.457 122.49 115.34 120.89 110.44 110.00 110.60 123.76 156 LEU 362 1.329 1.244 1.535 1.531 1.458 123.28 118.18 120.29 107.95 109.62 108.84 121.52 * * 157 PRO 363 1.335 1.243 1.529 1.527 1.446 121.71 118.32 119.44 110.56 109.24 103.68 122.24 * * * 158 PRO 364 1.349 1.221 1.534 1.536 1.469 123.19 117.39 119.84 110.96 113.78 104.27 122.74 * * 159 GLU 365 1.336 1.221 1.524 1.543 1.465 121.15 116.46 120.65 109.01 111.35 109.36 122.74 160 ILE 366 1.314 1.238 1.537 1.547 1.437 121.59 115.96 121.10 112.08 111.52 110.05 122.89 * * * * 161 GLN 367 1.314 1.243 1.533 1.521 1.449 122.17 116.31 120.73 110.59 111.13 109.79 122.94 * * 162 ALA 368 1.330 1.233 1.520 1.514 1.464 121.86 116.18 120.71 110.41 111.24 111.12 123.11 163 ARG 369 1.324 1.218 1.517 1.527 1.459 121.82 115.92 120.76 110.34 110.09 110.74 123.30 164 VAL 370 1.325 1.241 1.518 1.539 1.467 122.84 114.81 121.19 106.89 111.20 110.63 124.00 * * 165 GLN 371 1.314 1.231 1.540 1.526 1.449 123.91 116.40 120.75 111.07 111.73 108.72 122.81 * * * * 166 GLY 372 1.322 1.238 1.531 - 1.449 120.92 117.31 120.40 - 113.26 - 122.29 167 GLN 373 1.328 1.227 1.522 1.548 1.455 120.78 115.59 120.59 109.33 110.79 112.79 123.80 * * 168 ARG 374 1.336 1.229 1.548 1.536 1.474 124.00 117.12 120.91 110.38 111.07 112.72 121.94 * * * * 169 PRO 375 1.343 1.231 1.531 1.527 1.483 123.64 115.89 120.90 109.44 113.86 102.76 123.15 * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 170 GLY 376 1.316 1.231 1.518 - 1.455 121.57 116.87 120.71 - 113.32 - 122.42 171 SER 377 1.316 1.244 1.549 1.526 1.448 121.88 117.80 120.05 111.76 110.39 109.07 122.15 * * 172 PRO 378 1.362 1.224 1.528 1.538 1.477 123.14 117.26 120.11 110.33 114.71 104.64 122.62 * * * * 173 GLU 379 1.313 1.235 1.518 1.508 1.462 121.52 115.82 120.81 112.26 111.54 110.00 123.36 * * * * 174 GLU 380 1.317 1.217 1.536 1.532 1.417 122.46 116.99 120.21 111.43 107.67 109.24 122.75 ** * ** 175 ALA 381 1.364 1.224 1.526 1.519 1.458 121.68 115.98 120.40 110.38 110.35 110.50 123.61 ** ** 176 ALA 382 1.338 1.213 1.512 1.520 1.458 123.16 115.91 120.74 109.97 110.65 110.34 123.33 177 ALA 383 1.304 1.229 1.521 1.521 1.447 122.59 116.28 120.03 110.34 111.16 110.80 123.67 +* +* 178 LEU 384 1.340 1.243 1.525 1.546 1.471 122.48 114.82 121.58 105.98 109.71 111.31 123.59 ** ** 179 VAL 385 1.327 1.212 1.509 1.554 1.447 122.37 116.79 119.80 110.08 113.10 112.64 123.38 180 ASP 386 1.324 1.221 1.523 1.534 1.469 122.61 116.09 120.77 110.89 111.14 110.14 123.09 181 GLY 387 1.322 1.227 1.528 - 1.443 120.96 117.37 120.45 - 113.31 - 122.18 182 LEU 388 1.327 1.240 1.541 1.538 1.473 121.21 114.61 121.32 114.75 113.77 111.58 124.06 ** ** 183 ARG 389 1.315 1.247 1.514 1.527 1.434 126.69 115.31 121.44 109.58 110.90 105.78 123.25 * * +** +** +** 184 ARG 390 1.283 1.233 1.518 1.559 1.432 121.27 115.71 121.13 111.23 108.03 111.44 123.15 *** * * * *** 185 GLU 391 1.294 1.232 1.521 1.540 1.437 122.44 119.49 119.17 110.47 107.17 111.45 121.27 ** * +* * * ** 186 PRO 392 1.340 1.238 1.533 1.542 1.459 121.63 116.46 120.71 110.49 111.07 104.03 122.75 187 GLY 393 1.313 1.237 1.513 - 1.441 121.11 116.53 120.83 - 112.24 - 122.63 * * 188 GLY 394 1.301 - 1.492 - 1.432 120.68 - - - 109.89 - - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +* +* +** +*** +** +* *** * **** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 14 ---------------------------------------- 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 1.364 1.320 .014 +*** ** C-N (Pro) 1.341 .016 18 1.331 1.362 1.347 .007 * C-O C-O 1.231 .020 187 1.199 1.250 1.230 .010 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.491 1.563 1.524 .012 +* +* CH2G*-C (Gly) 1.516 .018 18 1.492 1.531 1.516 .010 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.508 1.529 1.518 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.496 1.588 1.550 .021 +* +* CH1E-CH2E (the rest) 1.530 .020 138 1.478 1.573 1.532 .014 +** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.389 1.490 1.450 .018 +*** +* NH1-CH2G* (Gly) 1.451 .016 18 1.430 1.458 1.446 .008 * N-CH1E (Pro) 1.466 .015 18 1.436 1.486 1.469 .013 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 15 ---------------------------------------- +-----------------+ | 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 2.0 152 113.76 119.49 116.26 1.05 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.95 119.61 117.35 1.13 +* CH1E-C-N (Pro) 116.9 1.5 18 115.60 118.41 117.02 .88 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.42 124.56 122.98 .71 +* O-C-N (Pro) 122.0 1.4 18 121.50 123.16 122.60 .40 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.20 126.69 122.17 1.34 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.57 121.57 120.86 .46 C-N-CH1E (Pro) 122.6 5.0 18 120.70 123.78 122.64 .87 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.11 122.06 120.64 .57 CH2G*-C-O (Gly) 120.8 2.1 17 119.67 120.83 120.37 .34 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 108.86 111.46 110.37 .50 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.89 112.14 110.17 1.69 * * CH2E-CH1E-C (the rest) 110.1 1.9 138 105.58 116.26 110.60 1.75 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.17 114.49 110.72 1.41 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.89 113.32 112.04 1.03 N-CH1E-C (Pro) 111.8 2.5 18 108.51 114.71 112.92 1.80 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 108.71 111.51 110.47 .53 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 103.93 113.17 111.04 2.42 **** N-CH1E-CH2E (Pro) 103.0 1.1 18 102.55 105.22 103.60 .67 ** NH1-CH1E-CH2E (the rest) 110.5 1.7 120 105.78 114.45 110.50 1.69 +** ** ------------------------------------------------------------------------------------------------------------- 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_10 Page 16 ---------------------------------------- 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] 141 92.8% Residues in additional allowed regions [a,b,l,p] 11 7.2% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% 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 92.8 83.8 10.0 .9 Inside b. Omega angle st dev 186 2.9 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 125 .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 12 9.8 18.1 6.5 -1.3 BETTER b. Chi-1 trans st dev 57 11.1 19.0 5.3 -1.5 BETTER c. Chi-1 gauche plus st dev 63 9.4 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 132 10.6 18.2 4.8 -1.6 BETTER e. Chi-2 trans st dev 53 5.7 20.4 5.0 -2.9 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% 92.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_10 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .11 Chi1-chi2 distribution -.13 Chi1 only -.11 Chi3 & chi4 .45 Omega .17 ------ .13 ===== Main-chain covalent forces:- Main-chain bond lengths .24 Main-chain bond angles .39 ------ .33 ===== OVERALL AVERAGE .20 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.