Residue-by-residue listing for refined_15 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.7 - - - 2 SER 2 B 56.7 - - - - - - - - - 179.0 - 34.2 - 3 ASP 3 B - 185.5 - - - - - - - - 182.1 - 35.7 - 4 PRO 4 - - - - - -66.8 - - - - - 182.5 - 38.6 - * * 5 GLY 5 h - - - - - - - - - - - 179.1 - - - 6 PRO 6 H - - - - - -61.0 -61.0 -28.8 - - - 178.0 - 38.6 - * * 7 GLU 7 H A 56.4 - - 181.1 - -67.2 -39.9 - - - 177.8 - 33.4 - 8 ALA 8 H A - - - - - -75.2 -31.1 - - - 178.8 - 34.8 - 9 ALA 9 H A - - - - - -61.9 -49.3 - - - 178.8 -2.1 34.0 - 10 ARG 10 H A - 185.1 - 179.5 - -63.4 -37.6 - - - 181.3 -2.4 33.1 - 11 LEU 11 H A - 175.5 - - - -61.1 -47.5 - - - 177.5 -1.5 34.4 - 12 ARG 12 H A - - -64.5 184.8 - -65.3 -40.5 - - - 180.7 -2.7 33.8 - 13 PHE 13 H A - 173.8 - - - -62.2 -42.0 - - - 181.4 -2.5 34.2 - 14 ARG 14 H A - - -52.8 179.3 - -80.1 -25.2 - - - 182.6 -2.8 34.8 - * * * 15 CYS 15 H A - 188.9 - - - -82.8 -7.1 - - - 178.5 -1.5 33.9 - * +** +** 16 PHE 16 h B - 180.3 - - - - - - - - 178.1 -.5 35.2 - +* +* 17 HIS 17 B 70.8 - - - - - - - - - 172.6 - 33.7 - * * 18 TYR 18 B - 167.0 - - - - - - - - 178.0 -1.1 31.8 - * * 19 GLU 19 t B 47.3 - - 173.9 - - - - - - 182.7 -.8 32.1 - * +* +* Residue-by-residue listing for refined_15 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 - - -63.1 165.2 - - - - - - 181.6 -.6 34.8 - +* +* 21 ALA 21 T A - - - - - - - - - - 182.5 - 33.1 - 22 THR 22 T A - 198.7 - - - - - - - - 181.8 -.8 34.5 - +* +* 23 GLY 23 h - - - - - - - - - - - 183.8 -.9 - - +* +* 24 PRO 24 H - - - - - -70.2 -70.2 -31.0 - - - 182.3 - 38.6 - * * 25 GLN 25 H A - - -51.9 - - -69.1 -36.5 - - - 179.7 - 35.6 - 26 GLU 26 H A - 178.7 - 163.2 - -74.7 -40.0 - - - 176.4 - 32.8 - 27 ALA 27 H A - - - - - -56.7 -38.5 - - - 176.2 -2.3 34.2 - 28 LEU 28 H A - - -67.5 176.5 - -58.0 -38.8 - - - 179.9 -1.9 33.8 - 29 ALA 29 H A - - - - - -61.9 -46.9 - - - 177.0 -.9 33.5 - +* +* 30 GLN 30 H A - - -79.8 - - -63.5 -46.1 - - - 178.9 -1.7 33.4 - 31 LEU 31 H A - - -71.9 170.3 - -61.0 -46.5 - - - 180.9 -3.0 32.3 - * * 32 ARG 32 H A 61.2 - - 180.8 - -66.7 -29.8 - - - 175.9 -3.4 30.0 - +* * +* 33 GLU 33 H A - 178.1 - - - -66.5 -50.8 - - - 181.4 -1.6 35.5 - * * 34 LEU 34 H A - - -59.9 173.7 - -65.8 -40.7 - - - 177.6 -2.4 34.0 - 35 CYS 35 H A - 186.1 - - - -65.6 -35.2 - - - 178.6 -3.3 34.6 - +* +* 36 ARG 36 H A - 178.5 - - - -66.2 -42.5 - - - 180.0 -1.8 32.1 - 37 GLN 37 H A - - -59.3 187.7 - -64.7 -16.6 - - - 180.3 -2.2 34.5 - ** ** 38 TRP 38 H a - 166.6 - - - -96.1 -57.8 - - - 183.0 -.6 33.9 - * +** +* +* +** 39 LEU 39 H A - - -57.9 174.8 - -75.9 -44.2 - - - 176.7 -3.5 33.4 - +* +* 40 ARG 40 h l - - -55.9 181.1 - - - - - - 179.8 -1.8 32.1 - 41 PRO 41 T - - - - - -66.2 - - - - - 184.0 - 38.9 - * * 42 GLU 42 T A 65.4 - - - - - - - - - 180.3 - 31.0 - 43 VAL 43 T A - - -61.5 - - - - - - - 178.6 - 32.1 - 44 ARG 44 t B - - -71.5 180.4 - - - - - - 181.3 -2.4 31.3 - 45 SER 45 h B - 175.6 - - - - - - - - 174.5 - 35.9 - 46 LYS 46 H A - - -66.1 171.2 - -54.8 -34.3 - - - 179.9 - 36.4 - 47 GLU 47 H A - 180.9 - 182.8 - -55.3 -48.0 - - - 179.9 - 35.8 - 48 GLN 48 H A - - -75.9 - - -65.2 -34.4 - - - 179.8 -.6 33.0 - +* +* 49 MET 49 H A - - -59.9 179.7 - -63.8 -45.3 - - - 171.8 -1.3 32.7 - * * * 50 LEU 50 H A - - -79.8 - - -53.5 -52.5 - - - 182.6 -2.2 34.4 - * * 51 GLU 51 H A - - -59.3 187.6 - -57.7 -48.3 - - - 181.1 -2.2 33.3 - 52 LEU 52 H A - - -61.2 178.2 - -62.5 -41.1 - - - 180.9 -3.1 34.2 - * * 53 LEU 53 H A - 183.5 - - - -75.2 -30.6 - - - 173.7 -2.4 32.1 - * * 54 VAL 54 H A - 175.8 - - - -64.0 -44.0 - - - 177.2 -2.6 33.2 - 55 LEU 55 H A - 181.8 - - - -54.1 -46.2 - - - 182.5 -2.4 35.9 - 56 GLU 56 H A - 184.9 - - - -55.2 -53.4 - - - 179.9 -1.7 34.1 - * * 57 GLN 57 H A - 175.6 - - - -74.4 -31.8 - - - 178.0 -1.7 31.5 - Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 PHE 58 H A - 178.8 - - - -58.0 -49.6 - - - 177.8 -2.7 32.8 - 59 LEU 59 H A - - -87.8 - - -60.4 -44.1 - - - 180.9 -2.8 30.5 - * * * 60 GLY 60 H - - - - - - -78.6 -7.7 - - - 175.0 -1.8 - - * +** +** 61 ALA 61 H A - - - - - -84.8 -28.9 - - - 176.1 -1.1 33.0 - +* * +* 62 LEU 62 h B - - -68.3 170.9 - - - - - - 176.4 -1.3 37.0 - 63 PRO 63 h - - - - - -68.8 - - - - - 182.0 - 39.3 - +* +* 64 PRO 64 H - - - - - -44.0 -44.0 -44.6 - - - 181.2 - 38.8 - +* +* * +* 65 GLU 65 H A 55.9 - - 185.4 - -62.7 -48.3 - - - 180.0 - 33.0 - 66 ILE 66 H A - - -59.1 181.6 - -72.2 -42.6 - - - 180.8 - 34.7 - 67 GLN 67 H A - 178.4 - 178.6 - -58.0 -43.3 - - - 179.5 -3.4 34.3 - +* +* 68 ALA 68 H A - - - - - -67.6 -32.1 - - - 177.7 -2.6 32.6 - 69 ARG 69 H A - - -59.9 - - -69.5 -34.6 - - - 173.6 -1.2 32.6 - * * * 70 VAL 70 H A - 172.4 - - - -70.0 -47.1 - - - 180.2 -2.0 35.1 - 71 GLN 71 H A - 211.2 - - - -54.7 -36.6 - - - 180.7 -3.2 36.1 - +* +* +* 72 GLY 72 h - - - - - - - - - - - 180.6 -2.1 - - 73 GLN 73 T A - 182.8 - 178.9 - - - - - - 180.1 -1.7 34.4 - 74 ARG 74 t l - - -59.1 - - - - - - - 180.7 -3.7 30.0 - ** * ** 75 PRO 75 - - - - - -70.4 - - - - - 180.1 - 39.2 - +* +* 76 GLY 76 S - - - - - - - - - - - 180.1 - - - 77 SER 77 h B - - -59.5 - - - - - - - 181.7 - 34.5 - 78 PRO 78 H - - - - - -51.7 -51.7 -45.1 - - - 183.3 - 38.7 - * * * * 79 GLU 79 H A - - -54.1 - - -68.8 -37.3 - - - 177.1 - 31.9 - 80 GLU 80 H A - 184.9 - - - -64.9 -45.9 - - - 175.0 - 34.2 - 81 ALA 81 H A - - - - - -55.8 -44.6 - - - 178.3 -2.7 34.7 - 82 ALA 82 H A - - - - - -60.5 -38.0 - - - 178.9 -2.8 33.7 - * * 83 ALA 83 H A - - - - - -68.8 -31.0 - - - 179.7 -2.2 33.4 - 84 LEU 84 H A - - -44.4 186.2 - -70.0 -49.3 - - - 178.0 -1.7 35.0 - * * 85 VAL 85 H A 41.7 - - - - -64.9 -35.5 - - - 175.6 -2.4 30.8 - * * 86 ASP 86 H A - 175.7 - - - -52.2 -40.9 - - - 178.8 -2.4 33.9 - * * 87 GLY 87 H - - - - - - -84.0 -20.7 - - - 179.2 -1.2 - - +* +* * +* 88 LEU 88 H A - - -62.8 175.7 - -78.7 -26.8 - - - 172.8 -1.1 33.4 - * * * * * 89 ARG 89 h b - - -60.7 182.7 - - - - - - 178.7 -2.1 34.8 - 90 ARG 90 S B - - -64.7 170.3 - - - - - - 189.4 -.8 33.1 - +* +* +* 91 GLU 91 S l - - -57.1 - - - - - - - 184.8 -.7 31.1 - +* +* 92 PRO 92 - - - - - -83.7 - - - - - 178.0 - 39.1 - +* * +* 93 GLY 93 - - - - - - - - - - - 180.7 - - - 94 GLY 94 - - - - - - - - - - - - - - - Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 95 GLY 301 - - - - - - - - - - - 179.2 - - - 96 SER 302 b 52.0 - - - - - - - - - 179.8 - 33.1 - 97 ASP 303 S B - - -63.4 - - - - - - - 174.1 -1.3 36.3 - * * * 98 PRO 304 S - - - - - -72.9 - - - - - 175.6 - 37.8 - * * 99 GLY 305 h - - - - - - - - - - - 176.2 - - - 100 PRO 306 H - - - - - -60.6 -60.6 -29.2 - - - 178.4 - 38.7 - * * 101 GLU 307 H A 60.3 - - 182.1 - -58.3 -45.6 - - - 180.1 - 33.7 - 102 ALA 308 H A - - - - - -75.5 -26.4 - - - 177.4 - 33.2 - * * 103 ALA 309 H A - - - - - -68.9 -40.1 - - - 175.3 -1.4 33.0 - 104 ARG 310 H A - 181.1 - 186.6 - -63.5 -34.9 - - - 178.5 -2.6 35.2 - 105 LEU 311 H A - 170.4 - - - -62.2 -48.2 - - - 177.1 -1.3 35.6 - 106 ARG 312 H A - - -62.0 177.2 - -58.4 -42.1 - - - 180.4 -2.4 35.9 - 107 PHE 313 H A - 177.6 - - - -61.1 -42.6 - - - 177.9 -2.2 34.7 - 108 ARG 314 H A - - -71.1 190.9 - -87.8 -16.7 - - - 176.8 -2.3 30.9 - +* ** ** 109 CYS 315 H A - 182.5 - - - -74.5 -29.1 - - - 179.7 -1.9 34.5 - 110 PHE 316 h B - 181.6 - - - - - - - - 177.4 -1.6 35.1 - 111 HIS 317 B 73.1 - - - - - - - - - 172.7 - 34.2 - * * 112 TYR 318 B - 165.6 - - - - - - - - 180.4 -.9 31.0 - * +* +* 113 GLU 319 t B 49.7 - - 175.0 - - - - - - 181.6 -.8 32.7 - +* +* 114 GLU 320 T A - - -62.6 177.1 - - - - - - 181.0 -.6 34.0 - +* +* 115 ALA 321 T A - - - - - - - - - - 181.2 - 33.8 - 116 THR 322 T A - 199.5 - - - - - - - - 181.9 -1.2 33.8 - * * 117 GLY 323 h - - - - - - - - - - - 182.4 -.9 - - +* +* 118 PRO 324 H - - - - - -68.0 -68.0 -34.7 - - - 180.3 - 38.8 - * * 119 GLN 325 H A - - -56.0 - - -61.0 -44.3 - - - 179.9 - 35.7 - 120 GLU 326 H A - 175.1 - 165.7 - -74.0 -40.8 - - - 177.6 - 32.2 - 121 ALA 327 H A - - - - - -56.8 -34.1 - - - 175.1 -2.5 34.1 - 122 LEU 328 H A - - -70.7 176.4 - -55.9 -40.9 - - - 180.1 -1.9 33.9 - 123 ALA 329 H A - - - - - -60.5 -43.5 - - - 177.4 -.9 33.9 - * * 124 GLN 330 H A - - -80.0 - - -65.2 -47.7 - - - 178.8 -1.3 34.4 - 125 LEU 331 H A - - -70.9 170.1 - -62.5 -45.1 - - - 179.9 -3.0 32.5 - * * 126 ARG 332 H A 63.2 - - 186.1 - -67.6 -30.8 - - - 175.6 -3.5 31.4 - +* +* 127 GLU 333 H A - 177.7 - 176.4 - -66.2 -50.4 - - - 179.9 -1.6 34.9 - 128 LEU 334 H A - - -61.7 175.4 - -63.1 -42.0 - - - 178.0 -2.8 33.8 - * * 129 CYS 335 H A - 184.7 - - - -64.5 -42.5 - - - 176.4 -3.2 33.9 - +* +* 130 ARG 336 H A - 175.6 - - - -60.5 -40.1 - - - 178.8 -2.4 31.2 - 131 GLN 337 H A - - -62.1 186.6 - -65.0 -20.3 - - - 179.8 -2.3 34.0 - +* +* 132 TRP 338 H a - 164.1 - - - -92.4 -58.6 - - - 182.4 -.8 33.7 - * ** +* +* ** Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 133 LEU 339 H A - - -57.2 177.6 - -72.4 -42.8 - - - 179.7 -3.5 32.5 - ** ** 134 ARG 340 h l - - -57.8 181.8 - - - - - - 181.4 -1.9 31.8 - 135 PRO 341 T - - - - - -63.1 - - - - - 179.7 - 38.5 - * * 136 GLU 342 T A 60.7 - - 186.2 - - - - - - 180.0 - 33.1 - 137 VAL 343 T A - - -62.8 - - - - - - - 180.1 -1.6 31.7 - 138 ARG 344 t B - - -71.0 183.1 - - - - - - 181.8 -3.3 30.3 - +* * +* 139 SER 345 h B - - -55.4 - - - - - - - 180.3 - 35.8 - 140 LYS 346 H A - - -68.3 169.8 - -55.4 -40.0 - - - 181.7 - 34.9 - 141 GLU 347 H A - 178.7 - 178.9 - -56.4 -42.9 - - - 180.2 - 34.1 - 142 GLN 348 H A - - -75.0 - - -64.6 -31.0 - - - 179.4 -.6 32.7 - +* +* 143 MET 349 H A - - -60.3 180.3 - -67.1 -38.2 - - - 173.0 -1.0 32.5 - * * * 144 LEU 350 H A - - -73.1 - - -60.4 -50.5 - - - 181.9 -1.5 33.6 - 145 GLU 351 H A - - -55.6 184.2 - -58.2 -48.5 - - - 180.1 -2.2 33.9 - 146 LEU 352 H A - - -60.3 179.3 - -61.5 -41.0 - - - 179.5 -3.3 34.5 - +* +* 147 LEU 353 H A - 181.1 - - - -74.1 -30.4 - - - 171.4 -2.1 31.8 - * * 148 VAL 354 H A - 174.3 - - - -61.7 -45.6 - - - 176.7 -2.5 33.4 - 149 LEU 355 H A - 178.4 - - - -56.2 -45.8 - - - 181.3 -2.7 35.4 - 150 GLU 356 H A - 186.1 - - - -55.7 -52.1 - - - 180.4 -2.1 34.9 - * * 151 GLN 357 H A - 181.3 - - - -72.4 -39.5 - - - 180.7 -2.3 33.7 - 152 PHE 358 H A - 181.1 - - - -55.8 -48.8 - - - 178.9 -3.4 33.5 - +* +* 153 LEU 359 H A - - -95.6 - - -59.4 -41.3 - - - 180.1 -2.9 30.2 - +* * * +* 154 GLY 360 H - - - - - - -80.6 -16.2 - - - 176.7 -1.3 - - * ** ** 155 ALA 361 H A - - - - - -76.2 -28.2 - - - 174.9 -1.6 33.3 - 156 LEU 362 h B - - -68.3 171.3 - - - - - - 176.6 -1.4 36.8 - 157 PRO 363 h - - - - - -68.3 - - - - - 182.5 - 39.3 - +* +* 158 PRO 364 H - - - - - -46.0 -46.0 -41.3 - - - 180.2 - 38.2 - +* +* * +* 159 GLU 365 H A 59.8 - - 187.7 - -63.8 -48.0 - - - 179.1 - 32.6 - 160 ILE 366 H A - - -63.5 181.3 - -71.1 -42.1 - - - 179.6 - 35.1 - 161 GLN 367 H A - 177.6 - 177.4 - -56.8 -44.8 - - - 178.7 -3.6 34.2 - ** ** 162 ALA 368 H A - - - - - -64.0 -34.2 - - - 177.4 -2.6 33.0 - 163 ARG 369 H A - - -59.1 - - -63.2 -43.8 - - - 176.7 -1.2 35.1 - * * 164 VAL 370 H A - 170.9 - - - -62.9 -50.8 - - - 178.1 -2.2 35.0 - * * 165 GLN 371 H A - - -96.0 - - -55.1 -29.9 - - - 177.3 -3.2 32.0 - +* +* +* 166 GLY 372 H - - - - - - -71.0 -23.7 - - - 181.3 -1.7 - - * * 167 GLN 373 H A - - -51.6 192.7 - -105.3 -34.1 - - - 182.0 -1.7 34.2 - * *** *** 168 ARG 374 h l - - -71.2 - - - - - - - 178.2 -3.5 29.4 - +* * +* Residue-by-residue listing for refined_15 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 - - - - - -71.8 - - - - - 179.9 - 38.5 - * * 170 GLY 376 - - - - - - - - - - - 180.3 - - - 171 SER 377 h B - - -54.7 - - - - - - - 187.5 - 34.2 - * * 172 PRO 378 H - - - - - -60.0 -60.0 -45.0 - - - 183.4 - 37.4 - 173 GLU 379 H A - - -60.3 - - -72.7 -31.8 - - - 175.1 - 32.3 - 174 GLU 380 H A - 183.5 - - - -60.5 -52.3 - - - 176.9 - 35.9 - * * 175 ALA 381 H A - - - - - -55.8 -44.5 - - - 178.7 -2.4 34.5 - 176 ALA 382 H A - - - - - -60.6 -40.4 - - - 178.7 -2.6 33.5 - 177 ALA 383 H A - - - - - -66.6 -36.0 - - - 180.4 -2.4 33.4 - 178 LEU 384 H A - - -45.2 183.4 - -65.8 -49.9 - - - 184.0 -2.1 36.8 - * * 179 VAL 385 H A 56.1 - - - - -69.3 -32.7 - - - 175.8 -2.7 31.0 - 180 ASP 386 H A - 182.4 - - - -54.1 -40.4 - - - 177.4 -2.2 34.2 - 181 GLY 387 H - - - - - - -84.3 -28.2 - - - 178.4 -1.2 - - +* * +* 182 LEU 388 H A - - -63.0 176.5 - -65.0 -32.4 - - - 173.3 -1.7 33.4 - * * 183 ARG 389 h b - - -61.6 182.8 - - - - - - 181.7 -2.3 35.0 - 184 ARG 390 S b - - -61.9 176.2 - - - - - - 176.8 -.9 29.6 - * * * 185 GLU 391 S b - - -76.5 - - - - - - - 181.5 -2.2 34.4 - 186 PRO 392 - - - - - -60.6 - - - - - 180.1 - 38.0 - * * 187 GLY 393 - - - - - - - - - - - 180.5 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* +* +* *** +** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.1 179.9 -64.3 179.0 -64.1 -65.4 -39.2 - - - 179.2 -2.0 34.1 Standard deviations: 8.1 8.2 9.9 6.3 9.7 9.6 9.4 - - - 2.7 .8 2.1 Numbers of values: 16 50 66 60 18 124 124 0 0 0 186 126 170 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_15 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 1.503 - 1.457 - 116.47 120.63 - 111.22 - 122.89 2 SER 2 1.309 1.241 1.517 1.536 1.431 121.81 115.85 120.93 110.87 109.95 110.30 123.20 * * * 3 ASP 3 1.291 1.227 1.516 1.531 1.441 122.25 119.07 119.40 110.07 107.23 109.45 121.51 +** * * +** 4 PRO 4 1.339 1.232 1.536 1.531 1.472 122.11 116.68 120.56 110.27 113.07 103.41 122.74 5 GLY 5 1.322 1.229 1.517 - 1.431 120.72 118.63 120.11 - 111.42 - 121.26 * * * * 6 PRO 6 1.346 1.234 1.531 1.532 1.481 122.81 115.25 121.49 110.30 111.47 103.60 123.24 * * 7 GLU 7 1.317 1.238 1.542 1.534 1.446 122.81 116.00 121.07 112.01 110.81 109.77 122.90 * * 8 ALA 8 1.329 1.230 1.508 1.513 1.449 122.29 115.19 121.30 109.77 109.39 110.29 123.51 9 ALA 9 1.322 1.231 1.507 1.506 1.440 122.48 116.70 120.22 110.59 110.51 110.29 123.05 10 ARG 10 1.337 1.220 1.524 1.530 1.445 120.24 116.14 120.89 109.23 110.22 113.14 122.94 +* +* 11 LEU 11 1.324 1.229 1.541 1.518 1.413 123.12 116.88 120.18 112.43 110.97 107.94 122.90 ** * +* ** 12 ARG 12 1.335 1.231 1.530 1.535 1.467 121.42 115.20 121.10 109.49 110.58 111.68 123.69 13 PHE 13 1.315 1.222 1.537 1.533 1.459 124.03 117.28 120.51 111.67 112.62 108.27 122.20 * * * 14 ARG 14 1.321 1.227 1.522 1.523 1.466 120.52 116.39 121.00 108.25 110.48 111.40 122.61 Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.321 1.242 1.537 1.543 1.453 121.55 115.50 121.40 111.58 109.99 109.80 123.10 16 PHE 16 1.318 1.241 1.521 1.538 1.444 122.87 116.53 120.76 110.22 109.48 109.52 122.69 17 HIS 17 1.308 1.234 1.499 1.574 1.445 120.15 118.11 119.94 110.02 108.45 112.74 121.93 * * ** * ** 18 TYR 18 1.290 1.235 1.500 1.529 1.414 117.43 114.83 121.41 111.76 108.91 113.33 123.75 +** * ** ** +* +** 19 GLU 19 1.284 1.234 1.505 1.536 1.408 122.39 114.74 121.52 113.05 109.71 111.45 123.72 *** +** +* *** 20 GLU 20 1.302 1.226 1.518 1.524 1.446 123.68 116.13 120.38 111.12 111.13 108.58 123.43 +* * * +* 21 ALA 21 1.322 1.234 1.534 1.516 1.452 122.63 117.96 119.97 110.78 112.93 110.49 122.04 22 THR 22 1.332 1.227 1.538 1.577 1.457 119.79 116.04 121.02 110.06 109.42 111.00 122.84 * * * 23 GLY 23 1.328 1.239 1.522 - 1.448 121.04 119.26 119.91 - 110.87 - 120.83 * * * 24 PRO 24 1.342 1.230 1.520 1.505 1.459 121.47 116.69 120.43 110.11 113.44 103.31 122.86 * * 25 GLN 25 1.326 1.234 1.521 1.523 1.451 121.36 115.07 121.44 108.37 108.24 110.89 123.48 * * 26 GLU 26 1.329 1.225 1.513 1.526 1.434 122.25 116.43 120.41 112.49 110.69 110.25 123.14 * * * 27 ALA 27 1.325 1.227 1.527 1.519 1.462 121.86 115.98 120.70 110.65 109.75 110.09 123.30 28 LEU 28 1.332 1.220 1.520 1.525 1.463 122.58 117.04 119.86 109.14 111.95 111.54 123.09 29 ALA 29 1.331 1.231 1.523 1.523 1.462 121.78 115.44 121.08 110.99 110.11 110.77 123.45 30 GLN 30 1.319 1.232 1.526 1.548 1.450 122.66 115.94 120.92 111.39 110.66 110.69 123.12 31 LEU 31 1.318 1.212 1.517 1.524 1.451 122.43 118.03 119.70 111.23 112.92 111.26 122.25 32 ARG 32 1.325 1.215 1.517 1.543 1.460 120.15 116.95 119.95 112.22 112.15 113.77 123.09 * +* +* 33 GLU 33 1.327 1.236 1.534 1.538 1.460 121.56 115.37 121.39 109.50 109.26 109.67 123.17 34 LEU 34 1.319 1.231 1.527 1.528 1.453 122.57 115.95 120.86 111.49 110.91 109.41 123.18 35 CYS 35 1.323 1.228 1.540 1.542 1.448 122.65 116.47 121.06 111.11 109.62 109.37 122.44 36 ARG 36 1.334 1.213 1.508 1.554 1.456 121.96 117.06 119.90 112.52 111.00 111.33 123.03 * * * 37 GLN 37 1.326 1.236 1.526 1.505 1.469 122.09 114.80 121.78 109.30 111.06 110.40 123.41 * * 38 TRP 38 1.296 1.236 1.552 1.540 1.427 124.20 117.24 120.23 113.19 112.03 107.57 122.52 ** * +* * +* +* ** 39 LEU 39 1.319 1.227 1.530 1.526 1.466 121.75 116.25 120.03 111.02 111.67 110.26 123.71 40 ARG 40 1.345 1.220 1.543 1.530 1.473 124.13 117.95 120.96 111.18 114.06 110.99 121.07 * * * * * 41 PRO 41 1.338 1.224 1.536 1.534 1.476 122.78 116.86 120.93 109.90 113.81 103.18 122.21 42 GLU 42 1.299 1.236 1.531 1.540 1.448 121.10 117.08 120.42 112.05 113.02 112.25 122.50 ** * * ** 43 VAL 43 1.326 1.233 1.526 1.546 1.466 120.44 117.34 120.53 109.87 113.31 112.81 122.12 44 ARG 44 1.306 1.231 1.514 1.532 1.460 120.71 115.05 121.31 111.06 112.74 112.84 123.64 +* * +* 45 SER 45 1.307 1.246 1.524 1.544 1.438 123.56 114.82 120.96 109.97 110.91 108.52 124.22 +* * * * +* 46 LYS 46 1.335 1.221 1.518 1.536 1.461 124.74 114.96 121.26 109.34 109.47 108.50 123.75 +* * +* 47 GLU 47 1.324 1.232 1.539 1.517 1.449 123.85 115.74 121.05 109.87 110.77 108.23 123.20 * * * 48 GLN 48 1.325 1.219 1.508 1.541 1.457 122.26 116.32 120.46 110.37 111.30 112.05 123.22 49 MET 49 1.317 1.232 1.515 1.505 1.451 121.86 116.22 120.23 112.37 110.85 110.12 123.54 * * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 50 LEU 50 1.343 1.214 1.517 1.564 1.474 121.90 116.34 120.46 108.73 109.72 112.27 123.14 * +* * +* 51 GLU 51 1.329 1.237 1.527 1.520 1.464 122.01 116.21 120.65 109.66 112.45 111.47 123.13 52 LEU 52 1.317 1.237 1.523 1.532 1.442 122.21 116.43 120.75 110.67 111.23 109.99 122.81 53 LEU 53 1.316 1.237 1.557 1.519 1.416 121.36 117.43 120.45 115.59 112.09 107.49 122.09 +* ** +** +* +** 54 VAL 54 1.334 1.231 1.533 1.563 1.473 121.24 115.62 120.75 109.92 109.76 112.72 123.62 55 LEU 55 1.333 1.237 1.521 1.563 1.474 123.69 114.88 120.87 110.57 109.77 108.27 124.25 +* * * +* 56 GLU 56 1.318 1.242 1.544 1.542 1.458 123.18 116.99 120.90 110.86 111.92 109.56 122.08 57 GLN 57 1.314 1.215 1.508 1.523 1.452 120.02 117.31 119.80 112.08 111.71 112.01 122.87 * * * 58 PHE 58 1.328 1.238 1.529 1.537 1.447 120.49 116.15 120.69 110.48 110.28 112.45 123.14 * * 59 LEU 59 1.330 1.218 1.507 1.545 1.460 121.26 117.04 120.13 112.65 112.60 112.49 122.74 * * * 60 GLY 60 1.315 1.236 1.522 - 1.451 119.80 117.02 120.43 - 113.58 - 122.54 61 ALA 61 1.317 1.229 1.525 1.534 1.448 121.40 115.58 120.97 111.46 109.02 111.57 123.45 62 LEU 62 1.327 1.241 1.537 1.528 1.453 123.44 118.15 120.15 107.92 110.23 108.70 121.70 * * * 63 PRO 63 1.351 1.238 1.523 1.541 1.458 122.03 118.38 119.07 109.22 108.99 104.45 122.55 * * * * 64 PRO 64 1.354 1.225 1.532 1.527 1.478 123.57 116.21 120.52 110.19 113.28 103.08 123.24 65 GLU 65 1.327 1.223 1.543 1.538 1.459 122.22 117.44 120.33 111.93 112.53 109.74 122.17 66 ILE 66 1.332 1.240 1.521 1.539 1.449 121.17 115.36 121.07 109.36 110.25 110.92 123.55 67 GLN 67 1.318 1.226 1.516 1.519 1.445 122.86 116.40 120.57 110.51 110.88 110.00 123.02 68 ALA 68 1.321 1.221 1.522 1.508 1.451 121.61 117.30 120.25 110.99 111.79 111.36 122.44 69 ARG 69 1.327 1.227 1.515 1.529 1.463 120.64 116.10 120.96 111.02 109.83 112.16 122.93 70 VAL 70 1.319 1.230 1.513 1.541 1.450 121.48 114.66 121.31 108.08 109.16 111.95 124.03 71 GLN 71 1.316 1.221 1.537 1.536 1.453 124.39 115.96 121.10 108.79 110.18 109.28 122.92 * * 72 GLY 72 1.313 1.228 1.521 - 1.439 121.48 117.61 119.88 - 114.25 - 122.50 * * 73 GLN 73 1.322 1.238 1.526 1.524 1.458 120.98 114.78 121.18 109.87 110.62 110.44 124.04 74 ARG 74 1.327 1.228 1.524 1.529 1.462 124.91 115.68 121.66 113.58 112.51 112.10 122.56 +* +* +* 75 PRO 75 1.344 1.222 1.534 1.529 1.465 123.21 116.01 121.13 109.94 113.02 102.89 122.84 76 GLY 76 1.318 1.220 1.518 - 1.452 121.10 116.69 121.00 - 112.64 - 122.31 77 SER 77 1.312 1.246 1.527 1.520 1.447 121.80 117.36 119.87 110.40 110.14 109.96 122.73 * * 78 PRO 78 1.360 1.227 1.531 1.529 1.472 123.63 117.32 120.12 109.30 114.37 104.01 122.55 * * * 79 GLU 79 1.325 1.231 1.513 1.526 1.458 120.75 116.35 120.41 110.11 111.89 113.37 123.24 +* +* 80 GLU 80 1.323 1.211 1.526 1.532 1.433 121.96 116.71 120.33 111.74 108.14 109.95 122.93 * * * * 81 ALA 81 1.351 1.227 1.523 1.508 1.451 121.91 115.95 120.52 109.82 110.45 109.93 123.52 +* +* 82 ALA 82 1.336 1.207 1.520 1.531 1.454 122.83 116.11 121.11 110.63 110.65 110.83 122.78 * * 83 ALA 83 1.292 1.236 1.525 1.523 1.450 122.50 116.84 120.48 110.79 111.01 110.86 122.68 +** +** 84 LEU 84 1.334 1.229 1.523 1.550 1.460 120.76 115.47 121.23 108.42 107.98 111.99 123.22 * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 85 VAL 85 1.333 1.225 1.506 1.564 1.460 122.50 115.28 121.07 112.20 112.08 112.98 123.64 * * 86 ASP 86 1.292 1.224 1.528 1.525 1.471 122.75 116.18 120.51 110.05 111.51 110.63 123.27 +** +** 87 GLY 87 1.324 1.227 1.524 - 1.452 120.83 116.44 120.80 - 112.47 - 122.76 88 LEU 88 1.323 1.240 1.521 1.528 1.464 122.09 115.74 120.91 111.00 110.78 110.74 123.33 89 ARG 89 1.323 1.231 1.510 1.532 1.443 121.95 115.78 120.79 108.51 108.99 111.96 123.39 90 ARG 90 1.300 1.243 1.500 1.519 1.440 122.07 114.33 120.75 113.02 108.89 109.96 124.90 ** * +* * ** 91 GLU 91 1.324 1.240 1.529 1.546 1.452 124.84 116.60 121.23 112.02 108.52 113.95 122.06 +* * ** ** 92 PRO 92 1.340 1.237 1.526 1.528 1.453 122.75 115.61 121.12 110.46 113.31 102.56 123.26 93 GLY 93 1.311 1.237 1.509 - 1.436 121.51 116.74 120.26 - 111.16 - 123.00 * * 94 GLY 94 1.303 1.252 1.510 - 1.450 121.14 - 119.73 - 111.50 - - +* * +* 95 GLY 301 - 1.232 1.508 - 1.447 - 116.05 120.87 - 111.59 - 123.07 96 SER 302 1.309 1.245 1.521 1.527 1.434 121.35 115.18 121.17 111.92 110.76 110.37 123.58 * * * 97 ASP 303 1.310 1.221 1.489 1.546 1.444 123.25 118.49 119.70 106.73 108.11 111.92 121.80 * +* * +* * +* 98 PRO 304 1.334 1.229 1.553 1.530 1.463 122.00 115.89 121.49 111.34 111.53 103.63 122.61 * * 99 GLY 305 1.321 1.246 1.509 - 1.433 121.48 117.65 120.48 - 113.37 - 121.86 * * 100 PRO 306 1.347 1.231 1.527 1.534 1.466 123.13 115.95 120.75 110.54 111.15 103.47 123.27 101 GLU 307 1.336 1.241 1.537 1.549 1.457 122.35 115.98 120.99 111.08 110.24 110.64 123.00 102 ALA 308 1.320 1.221 1.517 1.505 1.440 122.26 116.79 120.83 111.12 111.07 110.66 122.38 103 ALA 309 1.319 1.230 1.523 1.509 1.453 120.61 116.16 120.65 111.30 109.62 111.29 123.17 104 ARG 310 1.338 1.229 1.529 1.520 1.459 121.60 115.19 121.54 108.48 109.16 111.03 123.26 105 LEU 311 1.327 1.214 1.527 1.516 1.416 123.67 116.27 120.55 111.17 110.08 107.71 123.15 ** * +* ** 106 ARG 312 1.329 1.232 1.517 1.522 1.471 122.73 114.11 121.57 108.15 109.85 110.07 124.31 * * * 107 PHE 313 1.306 1.222 1.539 1.531 1.443 125.27 117.29 120.46 113.15 111.65 106.60 122.22 +* +* +* ** ** 108 ARG 314 1.321 1.241 1.522 1.517 1.459 120.51 116.69 120.50 110.69 113.53 113.19 122.80 +* +* 109 CYS 315 1.311 1.237 1.522 1.541 1.449 121.60 114.96 121.03 110.64 108.87 110.26 123.98 * * 110 PHE 316 1.332 1.244 1.517 1.536 1.447 123.59 116.18 120.80 109.71 110.66 109.84 123.00 * * 111 HIS 317 1.309 1.235 1.499 1.587 1.441 120.30 118.45 119.54 109.79 107.36 112.77 121.96 * * +** * * * +** 112 TYR 318 1.294 1.228 1.502 1.536 1.418 117.08 114.56 121.48 111.97 108.80 114.23 123.96 ** * ** +** ** +** 113 GLU 319 1.285 1.236 1.519 1.548 1.411 122.82 115.80 121.05 113.11 110.04 110.38 123.13 *** ** +* *** 114 GLU 320 1.322 1.233 1.520 1.536 1.462 123.04 115.71 120.61 110.19 111.26 110.65 123.66 115 ALA 321 1.322 1.229 1.525 1.519 1.451 123.12 117.66 120.23 110.03 112.43 110.54 122.11 116 THR 322 1.323 1.219 1.530 1.569 1.446 119.45 115.62 121.24 110.54 108.82 111.83 123.12 * * * 117 GLY 323 1.326 1.239 1.511 - 1.442 120.90 119.17 119.97 - 110.78 - 120.85 * * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 118 PRO 324 1.340 1.229 1.518 1.515 1.454 121.54 115.23 121.04 110.53 111.71 103.14 123.71 * * * 119 GLN 325 1.322 1.233 1.529 1.524 1.454 122.77 115.82 121.18 108.47 109.77 110.25 123.00 120 GLU 326 1.324 1.222 1.514 1.528 1.443 122.03 116.96 120.12 112.45 111.68 110.81 122.90 * * 121 ALA 327 1.324 1.227 1.532 1.517 1.470 121.86 116.08 120.66 110.51 110.35 110.07 123.25 122 LEU 328 1.333 1.215 1.512 1.522 1.467 122.68 116.87 119.90 108.84 112.10 111.72 123.23 123 ALA 329 1.330 1.223 1.522 1.523 1.462 121.87 115.00 121.44 110.91 109.72 110.35 123.50 124 GLN 330 1.309 1.225 1.528 1.540 1.451 123.54 116.26 120.65 111.29 110.74 109.17 123.08 * * * 125 LEU 331 1.315 1.220 1.516 1.523 1.464 122.56 117.71 119.92 110.89 112.98 111.26 122.36 126 ARG 332 1.322 1.218 1.515 1.542 1.456 120.49 116.09 120.48 112.30 110.39 112.63 123.41 * * * 127 GLU 333 1.323 1.233 1.529 1.530 1.445 122.31 115.83 120.93 110.59 109.58 109.40 123.20 128 LEU 334 1.323 1.231 1.527 1.532 1.455 122.56 116.07 120.70 111.08 110.85 110.07 123.21 129 CYS 335 1.325 1.224 1.534 1.536 1.446 122.26 116.76 120.68 111.07 110.07 110.31 122.56 130 ARG 336 1.333 1.222 1.524 1.555 1.458 122.11 117.52 119.77 113.39 112.15 111.16 122.70 * +* +* 131 GLN 337 1.332 1.240 1.526 1.512 1.471 121.48 114.70 121.61 109.79 111.19 110.72 123.69 132 TRP 338 1.299 1.230 1.548 1.542 1.433 124.63 117.65 120.05 113.34 112.15 107.79 122.31 ** * * +* +* +* ** 133 LEU 339 1.324 1.230 1.535 1.549 1.463 120.64 116.67 119.90 111.08 111.25 111.84 123.42 134 ARG 340 1.355 1.233 1.543 1.538 1.475 123.64 117.65 120.76 110.56 113.08 112.44 121.59 +* * * +* 135 PRO 341 1.349 1.220 1.527 1.537 1.479 123.51 116.77 120.63 110.05 113.48 103.66 122.59 136 GLU 342 1.305 1.234 1.539 1.527 1.453 121.56 116.89 120.73 111.33 111.69 110.52 122.38 +* +* 137 VAL 343 1.328 1.228 1.516 1.559 1.459 120.60 117.10 120.48 110.26 112.31 113.55 122.42 * * 138 ARG 344 1.315 1.240 1.497 1.524 1.444 120.01 114.56 121.24 112.09 113.19 113.03 124.20 * * * * * 139 SER 345 1.305 1.247 1.524 1.530 1.432 123.40 115.40 120.60 110.39 110.04 108.37 123.99 +* * * +* 140 LYS 346 1.320 1.217 1.519 1.528 1.459 123.88 115.92 120.70 110.45 111.57 108.95 123.34 * * 141 GLU 347 1.318 1.234 1.529 1.525 1.456 123.12 115.98 120.83 110.39 111.61 109.99 123.16 142 GLN 348 1.323 1.210 1.498 1.539 1.460 121.99 116.69 120.34 110.30 111.29 112.53 122.96 * * * * 143 MET 349 1.314 1.230 1.501 1.500 1.446 121.30 116.12 120.26 112.24 110.63 110.66 123.59 * * * * * 144 LEU 350 1.337 1.212 1.507 1.563 1.453 120.99 116.01 120.29 109.16 108.83 113.48 123.64 +* +* +* 145 GLU 351 1.333 1.233 1.534 1.529 1.465 122.99 116.59 120.53 110.03 111.86 110.58 122.87 146 LEU 352 1.326 1.230 1.518 1.529 1.450 122.31 116.21 120.85 109.93 110.91 110.29 122.93 147 LEU 353 1.313 1.236 1.551 1.518 1.423 121.60 117.04 120.60 115.85 111.41 107.90 122.34 * * +* *** +* *** 148 VAL 354 1.334 1.214 1.526 1.567 1.465 121.18 115.86 120.54 109.83 108.77 112.88 123.57 149 LEU 355 1.332 1.240 1.520 1.561 1.470 123.59 115.10 120.82 111.05 109.80 108.42 124.08 +* * * +* 150 GLU 356 1.321 1.243 1.538 1.538 1.443 123.28 116.24 121.14 110.17 110.87 109.55 122.61 151 GLN 357 1.314 1.224 1.524 1.527 1.450 121.26 116.51 120.17 110.66 110.85 110.62 123.31 * * 152 PHE 358 1.334 1.234 1.526 1.550 1.459 122.53 116.38 120.54 110.31 110.86 111.45 123.07 153 LEU 359 1.327 1.219 1.510 1.536 1.464 121.26 117.47 119.81 112.61 113.68 112.33 122.69 * * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 154 GLY 360 1.312 1.236 1.515 - 1.446 119.26 116.60 120.32 - 112.95 - 123.07 * * 155 ALA 361 1.327 1.240 1.525 1.531 1.454 121.89 115.46 120.85 111.27 109.54 111.09 123.68 156 LEU 362 1.335 1.237 1.529 1.536 1.457 123.35 118.57 119.90 107.87 109.79 109.28 121.53 * * * 157 PRO 363 1.350 1.232 1.518 1.538 1.461 121.90 118.66 118.91 109.22 108.89 104.39 122.43 * * * * * 158 PRO 364 1.349 1.235 1.538 1.522 1.477 123.36 116.80 120.26 110.44 113.73 103.39 122.92 159 GLU 365 1.331 1.233 1.541 1.537 1.460 121.75 117.01 120.33 111.93 111.80 110.51 122.60 160 ILE 366 1.336 1.238 1.520 1.538 1.448 122.13 115.25 121.15 109.27 110.36 110.34 123.59 161 GLN 367 1.313 1.221 1.528 1.526 1.440 123.12 116.55 120.65 111.67 110.48 109.18 122.75 * * 162 ALA 368 1.320 1.230 1.532 1.506 1.456 121.83 116.86 120.32 110.90 111.71 110.78 122.81 163 ARG 369 1.338 1.239 1.520 1.530 1.474 121.49 114.94 121.39 108.31 108.72 111.48 123.67 164 VAL 370 1.329 1.225 1.508 1.538 1.450 122.80 115.65 120.79 108.35 110.22 111.53 123.55 165 GLN 371 1.320 1.226 1.533 1.546 1.457 122.57 116.52 120.42 111.87 111.93 111.55 123.04 166 GLY 372 1.321 1.234 1.532 - 1.444 121.31 117.72 120.09 - 113.29 - 122.19 167 GLN 373 1.336 1.223 1.522 1.526 1.467 120.68 115.35 120.76 108.75 110.92 111.66 123.89 168 ARG 374 1.331 1.233 1.536 1.532 1.465 124.20 116.56 121.41 111.85 114.01 113.83 121.98 * * +* +* 169 PRO 375 1.344 1.221 1.541 1.532 1.461 122.58 116.39 120.82 110.65 112.68 103.32 122.80 170 GLY 376 1.328 1.227 1.517 - 1.454 121.84 116.15 120.51 - 112.45 - 123.28 171 SER 377 1.319 1.249 1.546 1.527 1.442 122.37 117.85 119.95 111.78 108.70 109.39 122.19 * * 172 PRO 378 1.355 1.233 1.532 1.532 1.479 123.23 117.55 120.06 110.10 115.43 104.68 122.36 * +* +* 173 GLU 379 1.315 1.232 1.501 1.532 1.464 120.99 115.47 120.65 110.31 110.78 113.12 123.88 * +* +* 174 GLU 380 1.323 1.217 1.531 1.534 1.439 122.67 116.00 120.78 110.22 107.21 109.08 123.16 * * * 175 ALA 381 1.347 1.230 1.519 1.503 1.455 122.74 116.33 120.43 109.96 111.51 109.69 123.24 * * 176 ALA 382 1.328 1.219 1.526 1.521 1.451 122.13 116.09 121.21 110.94 110.70 110.56 122.70 177 ALA 383 1.299 1.240 1.525 1.523 1.451 122.24 116.42 120.33 110.80 110.79 110.92 123.23 ** ** 178 LEU 384 1.339 1.234 1.516 1.544 1.462 121.41 115.16 121.23 105.74 108.65 111.78 123.55 ** ** 179 VAL 385 1.335 1.231 1.501 1.550 1.457 122.71 115.65 120.77 111.78 112.75 112.75 123.58 * * * 180 ASP 386 1.305 1.227 1.534 1.531 1.463 122.16 115.62 120.67 110.28 109.77 110.53 123.66 +* +* 181 GLY 387 1.335 1.232 1.528 - 1.452 121.58 116.47 120.53 - 112.28 - 123.01 182 LEU 388 1.343 1.235 1.513 1.535 1.478 122.51 116.02 120.55 109.77 110.97 111.87 123.39 * * 183 ARG 389 1.331 1.237 1.509 1.530 1.448 121.74 116.81 120.70 108.22 108.52 112.03 122.46 184 ARG 390 1.298 1.224 1.511 1.525 1.434 120.80 112.32 122.02 114.40 112.08 112.09 125.42 ** * +* ** +* ** 185 GLU 391 1.318 1.228 1.516 1.553 1.456 128.93 118.14 119.89 108.48 106.32 113.47 121.79 * **** +* +* **** 186 PRO 392 1.334 1.237 1.528 1.535 1.464 122.42 115.82 121.28 110.98 112.25 103.80 122.88 187 GLY 393 1.306 1.248 1.501 - 1.425 121.01 115.97 120.68 - 111.31 - 123.35 +* +* +* 188 GLY 394 1.297 - 1.499 - 1.425 121.73 - - - 110.45 - - ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** * +* +** +** **** +* * *** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 1.284 1.355 1.321 .013 *** +* C-N (Pro) 1.341 .016 18 1.334 1.360 1.345 .007 * C-O C-O 1.231 .020 187 1.207 1.252 1.230 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 170 1.489 1.557 1.524 .012 +* +* CH2G*-C (Gly) 1.516 .018 18 1.499 1.532 1.515 .009 CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.503 1.534 1.517 .009 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.538 1.577 1.554 .013 * CH1E-CH2E (the rest) 1.530 .020 138 1.500 1.587 1.533 .013 * +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.408 1.478 1.452 .013 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.425 1.457 1.443 .010 +* N-CH1E (Pro) 1.466 .015 18 1.453 1.481 1.468 .009 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 2.0 152 112.32 119.07 116.24 1.01 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.97 119.26 117.17 1.04 * CH1E-C-N (Pro) 116.9 1.5 18 115.23 118.66 116.56 .93 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.83 125.42 123.00 .71 * +* O-C-N (Pro) 122.0 1.4 18 122.21 123.71 122.84 .38 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.08 128.93 122.14 1.37 +** **** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.26 121.84 121.05 .66 C-N-CH1E (Pro) 122.6 5.0 18 121.47 123.63 122.67 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.91 122.02 120.67 .53 * CH2G*-C-O (Gly) 120.8 2.1 17 119.73 121.00 120.36 .36 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.77 111.46 110.71 .47 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 108.08 112.20 109.96 1.15 * CH2E-CH1E-C (the rest) 110.1 1.9 138 105.74 115.85 110.69 1.56 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.32 114.06 110.65 1.45 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.45 114.25 112.09 1.07 N-CH1E-C (Pro) 111.8 2.5 18 108.89 115.43 112.53 1.65 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.69 111.57 110.62 .48 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.34 113.55 112.11 .95 * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.56 104.68 103.55 .54 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.60 114.23 110.72 1.62 ** ** ------------------------------------------------------------------------------------------------------------- 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_15 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] 140 92.1% Residues in additional allowed regions [a,b,l,p] 12 7.9% 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 92.1 83.8 10.0 .8 Inside b. Omega angle st dev 186 2.7 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 126 .8 .8 .2 .0 Inside f. Overall G-factor 188 .2 -.4 .3 2.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 16 8.1 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 50 8.2 19.0 5.3 -2.0 BETTER c. Chi-1 gauche plus st dev 66 9.9 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 132 9.8 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 60 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% 92.1 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 .82 2 Residue-by-residue listing for refined_15 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .12 Chi1-chi2 distribution -.01 Chi1 only .02 Chi3 & chi4 .36 Omega .22 ------ .16 ===== Main-chain covalent forces:- Main-chain bond lengths .36 Main-chain bond angles .42 ------ .40 ===== OVERALL AVERAGE .25 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.