Residue-by-residue listing for refined_18 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 - - - - - - - - - - - 179.2 - - - 2 SER 2 A - - -59.7 - - - - - - - 176.1 - 33.4 - 3 ASP 3 B - - -64.1 - - - - - - - 179.9 - 34.1 - 4 PRO 4 - - - - - -71.0 - - - - - 182.2 - 38.8 - * * 5 GLY 5 h - - - - - - - - - - - 179.8 - - - 6 PRO 6 H - - - - - -51.0 -51.0 -33.7 - - - 177.9 - 38.4 - * * * * 7 GLU 7 H A 57.8 - - 174.8 - -57.6 -48.6 - - - 183.0 - 33.2 - 8 ALA 8 H A - - - - - -73.0 -38.5 - - - 178.7 -.7 34.4 - +* +* 9 ALA 9 H A - - - - - -61.2 -47.0 - - - 179.5 -2.2 34.1 - 10 ARG 10 H A - 182.8 - 185.5 - -63.5 -38.9 - - - 181.6 -2.9 34.8 - * * 11 LEU 11 H A - 175.6 - - - -60.3 -51.5 - - - 178.1 -1.8 34.6 - * * 12 ARG 12 H A - - -63.7 181.0 - -62.7 -45.1 - - - 179.4 -2.5 33.5 - 13 PHE 13 H A - 166.6 - - - -58.5 -49.9 - - - 185.3 -2.8 34.4 - * * * 14 ARG 14 H A - 180.1 - 159.3 - -91.7 -11.1 - - - 174.8 -3.5 28.1 - ** +** +* +* +** 15 CYS 15 H A - 183.4 - - - -88.7 -5.3 - - - 176.4 -1.8 33.3 - +* *** *** 16 PHE 16 h B - 176.2 - - - - - - - - 176.7 -.6 35.2 - +* +* 17 HIS 17 B 76.3 - - - - - - - - - 174.8 - 34.2 - 18 TYR 18 B - 162.5 - - - - - - - - 176.6 -1.5 32.2 - * * Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 19 GLU 19 t B 45.2 - - 175.3 - - - - - - 184.3 -.7 31.6 - * +* +* 20 GLU 20 T A - - -55.5 175.4 - - - - - - 178.8 -.6 35.4 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.1 - 33.6 - 22 THR 22 T A - 198.1 - - - - - - - - 180.0 -1.4 34.1 - 23 GLY 23 h - - - - - - - - - - - 183.8 -1.0 - - * * 24 PRO 24 H - - - - - -71.5 -71.5 -33.0 - - - 182.9 - 38.7 - * * 25 GLN 25 H A - - -51.5 - - -68.7 -39.1 - - - 179.6 - 35.3 - * * 26 GLU 26 H A - 175.8 - 167.4 - -75.3 -34.5 - - - 175.7 - 32.1 - 27 ALA 27 H A - - - - - -63.1 -41.0 - - - 175.8 -2.1 33.9 - 28 LEU 28 H A - - -65.3 180.1 - -59.0 -36.1 - - - 178.9 -2.4 33.6 - 29 ALA 29 H A - - - - - -64.3 -35.2 - - - 179.9 -1.1 34.1 - * * 30 GLN 30 H A - - -46.3 - - -71.4 -51.7 - - - 181.9 -1.4 36.4 - * * * 31 LEU 31 H A - - -65.8 171.7 - -60.9 -41.5 - - - 182.9 -2.9 34.6 - * * 32 ARG 32 H A - 183.7 - 176.2 - -59.9 -46.9 - - - 181.5 -3.2 32.8 - +* +* 33 GLU 33 H A 80.9 - - 183.7 - -72.0 -40.0 - - - 180.1 -1.2 31.4 - * * * 34 LEU 34 H A - - -62.0 177.7 - -62.3 -39.6 - - - 177.4 -2.1 33.7 - 35 CYS 35 H A - 184.1 - - - -65.1 -37.4 - - - 177.9 -3.0 34.4 - * * 36 ARG 36 H A - 170.2 - - - -70.7 -30.9 - - - 176.4 -1.7 30.6 - 37 GLN 37 H A - - -54.1 188.3 - -66.1 -30.3 - - - 181.2 -2.0 35.8 - 38 TRP 38 H a - 171.3 - - - -77.2 -63.5 - - - 184.4 -1.3 33.4 - * ** ** 39 LEU 39 H A - - -54.0 - - -82.0 -43.7 - - - 178.4 -2.5 31.5 - * * 40 ARG 40 h l - - -56.9 180.2 - - - - - - 171.4 -.7 33.1 - * +* +* 41 PRO 41 T - - - - - -48.5 - - - - - 176.7 - 39.7 - +* +* +* 42 GLU 42 T A - 175.0 - 179.1 - - - - - - 182.0 - 35.6 - 43 VAL 43 T A - - -59.4 - - - - - - - 182.8 -1.9 32.1 - 44 ARG 44 t B - - -74.8 187.1 - - - - - - 176.1 -3.7 31.1 - ** ** 45 SER 45 h B - - -55.0 - - - - - - - 184.3 - 35.8 - 46 LYS 46 H A - - -51.2 176.1 - -64.9 -39.5 - - - 179.2 - 35.5 - * * 47 GLU 47 H A - 180.2 - - - -56.5 -40.0 - - - 181.3 - 36.7 - 48 GLN 48 H A - - -57.2 - - -70.5 -26.4 - - - 178.0 - 33.8 - * * 49 MET 49 H A - - -57.3 182.7 - -73.8 -39.4 - - - 173.1 -.9 33.0 - * +* +* 50 LEU 50 H A - - -79.1 - - -57.6 -44.7 - - - 179.2 -1.9 33.2 - 51 GLU 51 H A - 179.8 - 187.8 - -54.0 -54.0 - - - 181.2 -2.0 37.2 - * * 52 LEU 52 H A - - -62.5 177.5 - -63.9 -37.8 - - - 183.3 -1.9 34.9 - 53 LEU 53 H A - 181.6 - - - -76.6 -32.8 - - - 174.0 -2.3 32.5 - * * Residue-by-residue listing for refined_18 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 54 VAL 54 H A - 173.9 - - - -60.4 -43.7 - - - 177.8 -2.8 33.6 - * * 55 LEU 55 H A - 176.1 - - - -57.2 -44.1 - - - 184.0 -1.8 36.4 - 56 GLU 56 H A - 182.9 - - - -55.8 -52.9 - - - 181.8 -1.5 34.2 - * * 57 GLN 57 H A - 191.3 - - - -73.6 -40.8 - - - 181.6 -1.8 33.4 - 58 PHE 58 H A - 178.3 - - - -53.6 -45.9 - - - 180.8 -2.7 33.8 - 59 LEU 59 H A - - -63.7 187.1 - -63.4 -39.3 - - - 179.8 -2.9 31.5 - * * 60 GLY 60 H - - - - - - -80.8 -15.3 - - - 178.1 -1.2 - - * ** * ** 61 ALA 61 H A - - - - - -76.8 -24.7 - - - 176.4 -1.7 33.9 - * * 62 LEU 62 h B - - -66.9 168.0 - - - - - - 177.2 -1.1 36.5 - * * 63 PRO 63 h - - - - - -66.7 - - - - - 181.6 - 39.1 - * * 64 PRO 64 H - - - - - -43.2 -43.2 -47.2 - - - 181.7 - 38.6 - +* +* * +* 65 GLU 65 H A 60.4 - - 175.1 - -66.1 -46.9 - - - 181.2 - 31.6 - 66 ILE 66 H A - - -58.4 181.2 - -68.2 -40.5 - - - 180.4 - 33.8 - 67 GLN 67 H A - 181.2 - 176.2 - -63.9 -40.1 - - - 178.4 -3.3 34.2 - +* +* 68 ALA 68 H A - - - - - -60.5 -35.5 - - - 178.4 -2.3 33.7 - 69 ARG 69 H A - - -65.6 - - -65.5 -43.3 - - - 179.2 -1.3 34.6 - 70 VAL 70 H A - 172.6 - - - -57.1 -52.9 - - - 180.6 -1.7 34.4 - * * 71 GLN 71 H A - - -89.8 - - -57.6 -28.9 - - - 178.7 -2.2 31.0 - +* +* 72 GLY 72 H - - - - - - -79.7 -13.9 - - - 183.5 -1.1 - - * ** * ** 73 GLN 73 H a - 187.9 - - - -118.2 -40.3 - - - 179.9 -1.8 33.4 - **** **** 74 ARG 74 h l - - -57.5 - - - - - - - 177.7 -4.0 32.3 - +** +** 75 PRO 75 - - - - - -62.4 - - - - - 180.2 - 39.0 - * * 76 GLY 76 S - - - - - - - - - - - 178.3 - - - 77 SER 77 h B - - -60.5 - - - - - - - 185.5 - 33.5 - 78 PRO 78 H - - - - - -58.6 -58.6 -45.6 - - - 181.4 - 37.5 - * * 79 GLU 79 H A - - -64.3 177.9 - -72.4 -30.2 - - - 175.7 - 31.4 - 80 GLU 80 H A - 185.5 - - - -63.2 -45.9 - - - 176.6 - 34.9 - 81 ALA 81 H A - - - - - -60.4 -45.8 - - - 179.3 -2.5 34.3 - 82 ALA 82 H A - - - - - -55.6 -33.8 - - - 179.2 -2.6 33.4 - 83 ALA 83 H A - - - - - -67.2 -50.2 - - - 181.0 -1.6 32.7 - 84 LEU 84 H A 56.2 - - 161.7 - -70.7 -37.9 - - - 180.5 -1.6 28.1 - +* +* 85 VAL 85 H A - - -56.1 - - -67.9 -31.6 - - - 173.9 -2.7 30.6 - * * 86 ASP 86 H A - 174.9 - - - -62.8 -38.6 - - - 177.2 -1.5 33.7 - 87 GLY 87 H - - - - - - -70.1 -27.6 - - - 179.6 -1.4 - - * * 88 LEU 88 H A - - -62.6 175.0 - -75.6 -31.2 - - - 177.7 -1.4 33.5 - 89 ARG 89 h b 62.0 - - 180.1 - - - - - - 182.4 -1.6 30.2 - * * 90 ARG 90 A 58.6 - - 181.2 - - - - - - 179.2 -2.0 34.2 - Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 91 GLU 91 B 62.0 - - 176.4 - - - - - - 178.8 - 33.5 - 92 PRO 92 - - - - - -84.4 - - - - - 183.6 - 39.3 - +* +* +* 93 GLY 93 - - - - - - - - - - - 181.7 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 179.5 - - - 96 SER 302 A - - -54.5 - - - - - - - 176.8 - 33.8 - 97 ASP 303 S B - - -69.3 - - - - - - - 179.9 - 33.6 - 98 PRO 304 h - - - - - -63.9 - - - - - 180.9 - 38.8 - * * 99 GLY 305 H - - - - - - 80.7 166.8 - - - 180.0 - - - *12.3**18.2* *18.2* 100 PRO 306 H - - - - - -52.3 -52.3 -35.2 - - - 182.0 - 39.3 - * * +* +* 101 GLU 307 H A 56.0 - - 181.3 - -62.9 -56.0 - - - 181.9 - 34.0 - * * 102 ALA 308 H A - - - - - -77.2 -31.9 - - - 181.9 -1.1 32.8 - * * * 103 ALA 309 H A - - - - - -66.0 -43.8 - - - 178.2 -2.9 32.9 - * * 104 ARG 310 H A - 184.5 - 183.0 - -63.7 -33.5 - - - 178.6 -2.0 33.3 - 105 LEU 311 H A - 172.1 - - - -62.4 -51.7 - - - 177.6 -1.0 34.7 - * * * 106 ARG 312 H A - - -62.0 178.1 - -56.7 -48.2 - - - 183.0 -2.5 36.6 - 107 PHE 313 H A - 171.6 - - - -62.3 -49.4 - - - 183.9 -2.9 34.7 - * * 108 ARG 314 H A - 178.1 - 166.4 - -84.9 -18.4 - - - 177.0 -3.3 29.9 - +* +* +* * +* 109 CYS 315 H A - 184.3 - - - -78.6 -15.9 - - - 179.7 -2.1 33.8 - * ** ** 110 PHE 316 h B - 179.8 - - - - - - - - 178.8 -.8 34.6 - +* +* 111 HIS 317 B 73.8 - - - - - - - - - 173.4 - 35.0 - * * 112 TYR 318 B - 167.4 - - - - - - - - 181.0 -1.5 31.8 - 113 GLU 319 t B 39.0 - - 187.9 - - - - - - 182.9 - 32.3 - +* +* 114 GLU 320 T A - - -55.6 - - - - - - - 179.4 -.6 33.9 - +* +* 115 ALA 321 T A - - - - - - - - - - 185.7 - 36.6 - 116 THR 322 T A - - -63.4 - - - - - - - 179.2 -1.4 36.5 - 117 GLY 323 h - - - - - - - - - - - 181.9 -.9 - - * * 118 PRO 324 H - - - - - -72.2 -72.2 -31.1 - - - 182.2 - 38.9 - * * 119 GLN 325 H A - - -53.1 - - -67.3 -40.2 - - - 181.2 - 35.1 - 120 GLU 326 H A - 187.2 - 177.6 - -75.1 -33.8 - - - 177.4 - 33.6 - 121 ALA 327 H A - - - - - -63.9 -37.9 - - - 175.4 -1.8 33.5 - 122 LEU 328 H A - - -65.9 179.9 - -60.5 -35.4 - - - 179.0 -2.2 33.8 - 123 ALA 329 H A - - - - - -63.6 -38.3 - - - 180.2 -1.0 34.4 - * * 124 GLN 330 H A - - -49.2 - - -67.4 -51.9 - - - 182.0 -1.4 36.6 - * * * 125 LEU 331 H A - - -67.1 171.8 - -62.5 -38.0 - - - 182.9 -2.7 34.3 - 126 ARG 332 H A - 187.7 - 176.9 - -61.8 -45.8 - - - 181.4 -2.9 33.0 - * * 127 GLU 333 H A 76.5 - - 182.0 - -75.2 -39.6 - - - 178.8 -1.4 30.7 - Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 128 LEU 334 H A - - -63.4 177.7 - -59.4 -43.2 - - - 176.3 -2.3 33.4 - 129 CYS 335 H A - 185.4 - - - -63.4 -39.2 - - - 179.2 -3.1 34.7 - * * 130 ARG 336 H A - 174.6 - - - -69.6 -30.3 - - - 175.5 -1.8 29.9 - * * 131 GLN 337 H A - - -53.7 186.8 - -64.9 -25.4 - - - 182.6 -2.2 36.2 - * * 132 TRP 338 H A - 169.8 - - - -83.6 -58.8 - - - 183.6 -.9 33.2 - +* +* +* +* 133 LEU 339 H A - - -47.0 - - -87.2 -31.3 - - - 178.8 -2.5 31.4 - * +* +* 134 ARG 340 h l - - -56.9 179.2 - - - - - - 180.6 -1.5 31.6 - 135 PRO 341 T - - - - - -61.0 - - - - - 178.6 - 38.5 - * * 136 GLU 342 T A - 178.3 - 184.8 - - - - - - 182.5 - 35.4 - 137 VAL 343 T A - - -61.8 - - - - - - - 178.8 -1.2 32.3 - * * 138 ARG 344 t B - - -67.3 186.3 - - - - - - 173.5 -3.0 32.2 - * * * 139 SER 345 h B - - -64.7 - - - - - - - 193.2 - 32.8 - ** ** 140 LYS 346 H A - - -50.2 178.0 - -48.4 -37.3 - - - 181.7 - 36.5 - * * * 141 GLU 347 H A - 179.1 - 173.8 - -63.6 -31.4 - - - 181.0 - 34.1 - 142 GLN 348 H A - - -61.9 - - -77.2 -26.8 - - - 173.0 -2.5 31.7 - * * * * 143 MET 349 H A - - -68.7 - - -67.1 -43.6 - - - 176.5 -.8 33.0 - +* +* 144 LEU 350 H A - - -63.0 180.9 - -54.5 -44.9 - - - 179.3 -2.0 34.0 - 145 GLU 351 H A - 174.9 - 183.3 - -54.2 -54.2 - - - 182.4 -1.8 36.8 - * * 146 LEU 352 H A - - -60.1 179.7 - -65.7 -35.3 - - - 183.2 -1.9 35.0 - 147 LEU 353 H A - 186.0 - - - -77.5 -32.1 - - - 172.2 -2.5 32.4 - * * * 148 VAL 354 H A - 174.4 - - - -64.8 -43.8 - - - 177.0 -2.7 33.8 - 149 LEU 355 H A - 179.5 - - - -56.8 -47.6 - - - 179.5 -2.3 35.0 - 150 GLU 356 H A - 181.9 - - - -52.9 -48.4 - - - 182.2 -2.3 35.9 - * * 151 GLN 357 H A - 195.8 - - - -74.6 -46.9 - - - 183.2 -1.9 34.0 - 152 PHE 358 H A - 179.2 - - - -53.9 -45.8 - - - 180.4 -3.5 33.5 - +* +* 153 LEU 359 H A - - -63.6 190.1 - -64.2 -35.8 - - - 178.3 -3.0 30.4 - * * 154 GLY 360 H - - - - - - -81.3 -25.4 - - - 178.6 -1.1 - - * * * * 155 ALA 361 H A - - - - - -70.3 -18.9 - - - 176.0 -2.5 33.9 - +* +* 156 LEU 362 h B - - -66.5 171.9 - - - - - - 173.7 -.9 36.2 - * +* +* 157 PRO 363 h - - - - - -69.7 - - - - - 181.9 - 39.0 - * * 158 PRO 364 H - - - - - -44.1 -44.1 -40.5 - - - 178.7 - 37.9 - +* +* * +* 159 GLU 365 H A 48.7 - - - - -62.5 -47.6 - - - 179.8 - 30.9 - 160 ILE 366 H A - - -60.1 179.9 - -71.8 -40.3 - - - 180.2 -.6 34.7 - +* +* Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 161 GLN 367 H A - 180.9 - 176.0 - -60.8 -40.8 - - - 177.0 -3.2 33.8 - +* +* 162 ALA 368 H A - - - - - -62.7 -37.4 - - - 178.5 -2.6 34.2 - 163 ARG 369 H A - - -66.9 - - -65.7 -43.0 - - - 178.3 -1.3 34.2 - 164 VAL 370 H A - 172.5 - - - -60.0 -53.4 - - - 179.0 -2.3 33.6 - * * 165 GLN 371 H A - - -89.2 - - -57.9 -29.6 - - - 177.6 -2.6 31.4 - * * 166 GLY 372 h - - - - - - - - - - - 182.4 -1.4 - - 167 GLN 373 T a - 189.7 - - - - - - - - 175.8 -2.2 33.3 - 168 ARG 374 t l - - -59.7 - - - - - - - 176.2 -4.0 31.3 - +** +** 169 PRO 375 - - - - - -72.7 - - - - - 179.9 - 38.9 - * * 170 GLY 376 - - - - - - - - - - - 179.3 - - - 171 SER 377 h B 52.2 - - - - - - - - - 186.8 - 33.1 - * * 172 PRO 378 H - - - - - -61.8 -61.8 -44.4 - - - 183.3 - 37.2 - 173 GLU 379 H A - - -60.3 170.3 - -74.2 -30.2 - - - 173.1 - 31.7 - * * 174 GLU 380 H A - 182.1 - - - -65.3 -46.1 - - - 176.8 - 34.7 - 175 ALA 381 H A - - - - - -57.5 -46.7 - - - 179.7 -2.5 33.8 - 176 ALA 382 H A - - - - - -57.0 -30.3 - - - 178.3 -2.8 33.3 - * * 177 ALA 383 H A - - - - - -66.5 -50.2 - - - 177.7 -1.2 33.2 - * * 178 LEU 384 H A 52.5 - - 161.9 - -71.6 -40.8 - - - 179.6 -1.6 28.3 - +* +* 179 VAL 385 H A - 174.3 - - - -57.8 -34.0 - - - 176.5 -3.3 32.8 - +* +* 180 ASP 386 H A - 177.6 - - - -59.4 -38.8 - - - 178.5 -1.7 33.8 - 181 GLY 387 H - - - - - - -84.9 -19.8 - - - 182.3 -.9 - - +* +* +* +* 182 LEU 388 H A - - -60.2 176.9 - -83.9 -22.5 - - - 179.8 -1.6 34.0 - +* * +* 183 ARG 389 h a 58.8 - - 175.4 - - - - - - 185.0 -1.9 34.2 - 184 ARG 390 A 56.3 - - - - - - - - - 176.2 - 28.3 - +* +* 185 GLU 391 b 57.6 - - 187.1 - - - - - - 172.8 - 29.7 - * * * 186 PRO 392 S - - - - - -86.7 - - - - - 180.1 - 39.1 - +* * +* 187 GLY 393 - - - - - - - - - - - 179.9 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +* * +* +**12.3**18.2* ** +** +* *18.2* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.5 179.3 -61.5 178.2 -63.4 -65.1 -37.1 - - - 179.5 -2.0 34.1 Standard deviations: 10.9 7.0 8.2 6.7 12.5 16.7 20.9 - - - 3.1 .8 2.3 Numbers of values: 19 54 59 60 18 125 125 0 0 0 186 124 170 0 Residue-by-residue listing for refined_18 Page 7 ---------------------------------------- KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_18 Page 8 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.232 1.491 - 1.464 - 117.16 119.89 - 110.42 - 122.95 * * 2 SER 2 1.313 1.231 1.530 1.530 1.443 121.12 115.80 120.94 112.06 109.94 110.10 123.25 * * * 3 ASP 3 1.320 1.231 1.505 1.545 1.450 123.09 118.11 119.89 109.08 108.40 112.74 121.99 * * 4 PRO 4 1.341 1.234 1.530 1.534 1.468 122.36 115.99 121.01 110.30 112.17 103.36 122.99 5 GLY 5 1.316 1.243 1.518 - 1.433 120.83 117.98 119.94 - 111.13 - 122.07 * * 6 PRO 6 1.352 1.235 1.538 1.532 1.477 123.42 116.43 120.56 110.50 112.74 103.44 123.00 7 GLU 7 1.335 1.239 1.544 1.548 1.461 122.36 116.27 120.60 110.49 111.86 111.24 123.09 8 ALA 8 1.327 1.239 1.503 1.516 1.452 122.63 115.35 120.96 110.31 110.45 110.16 123.68 * * 9 ALA 9 1.319 1.229 1.520 1.511 1.443 122.03 116.20 120.70 110.66 110.18 110.16 123.05 10 ARG 10 1.332 1.229 1.512 1.517 1.452 121.80 116.07 120.53 107.83 110.99 111.82 123.40 * * 11 LEU 11 1.326 1.215 1.517 1.523 1.404 122.63 116.51 120.34 111.78 109.83 108.89 123.11 +** +** 12 ARG 12 1.320 1.229 1.527 1.525 1.456 121.54 115.67 120.88 110.79 110.78 110.77 123.42 13 PHE 13 1.313 1.212 1.531 1.536 1.455 123.22 117.63 120.59 110.67 113.26 109.00 121.77 * * Residue-by-residue listing for refined_18 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 14 ARG 14 1.305 1.235 1.537 1.547 1.443 119.63 117.23 120.68 116.01 113.98 111.44 122.06 +* * *** *** 15 CYS 15 1.323 1.245 1.530 1.537 1.460 120.54 115.10 121.54 110.99 108.95 111.51 123.37 16 PHE 16 1.324 1.244 1.513 1.544 1.438 123.03 116.36 120.92 110.42 109.11 109.70 122.67 * * 17 HIS 17 1.295 1.241 1.490 1.566 1.423 120.09 117.46 119.91 109.92 106.92 112.69 122.62 ** +* +* +* +* * ** 18 TYR 18 1.285 1.234 1.500 1.526 1.407 118.55 114.73 121.64 111.92 109.28 112.42 123.61 *** * +** +* * *** 19 GLU 19 1.283 1.230 1.499 1.533 1.406 122.13 114.79 121.54 113.50 109.76 111.59 123.67 *** * +** +* *** 20 GLU 20 1.298 1.235 1.515 1.512 1.445 124.08 115.02 121.06 110.78 110.44 108.17 123.90 ** * * ** 21 ALA 21 1.318 1.227 1.535 1.521 1.441 123.10 117.90 120.04 110.80 112.01 110.24 122.06 22 THR 22 1.334 1.228 1.538 1.583 1.452 119.43 115.84 121.25 110.60 108.78 111.35 122.83 +* * +* 23 GLY 23 1.332 1.237 1.514 - 1.449 120.80 119.16 119.99 - 111.74 - 120.84 * * * 24 PRO 24 1.343 1.228 1.516 1.515 1.457 121.64 116.50 120.40 110.42 112.86 103.14 123.07 25 GLN 25 1.324 1.237 1.528 1.522 1.442 121.18 115.46 121.36 108.57 108.57 111.05 123.17 26 GLU 26 1.336 1.224 1.520 1.534 1.447 122.15 116.76 120.49 112.85 111.20 110.75 122.73 * * 27 ALA 27 1.321 1.224 1.522 1.514 1.459 121.67 116.29 120.57 110.66 109.64 110.53 123.13 28 LEU 28 1.332 1.212 1.513 1.526 1.466 121.84 116.70 120.26 108.99 111.29 112.24 123.04 * * 29 ALA 29 1.324 1.235 1.516 1.516 1.457 121.56 115.66 121.02 110.04 110.49 110.68 123.32 30 GLN 30 1.322 1.229 1.523 1.546 1.450 121.80 114.32 121.83 108.54 107.79 109.94 123.75 * * 31 LEU 31 1.318 1.219 1.515 1.523 1.452 124.26 116.77 120.23 110.33 112.93 109.12 122.99 * * 32 ARG 32 1.313 1.238 1.521 1.528 1.450 121.90 117.48 120.09 111.08 112.17 111.03 122.40 * * 33 GLU 33 1.330 1.211 1.527 1.549 1.448 118.68 116.79 120.00 111.50 109.73 113.67 123.14 +* +* +* 34 LEU 34 1.346 1.230 1.523 1.534 1.469 122.25 116.06 120.99 110.18 110.97 111.16 122.94 * * 35 CYS 35 1.320 1.234 1.524 1.536 1.445 122.05 116.31 121.11 110.71 109.36 110.23 122.56 36 ARG 36 1.321 1.203 1.525 1.553 1.421 121.55 117.49 119.47 114.73 111.46 110.99 123.03 * * +* ** ** 37 GLN 37 1.336 1.231 1.527 1.518 1.470 122.04 114.34 121.77 107.84 109.75 110.49 123.89 * * 38 TRP 38 1.322 1.234 1.540 1.553 1.450 124.35 118.13 120.06 112.86 112.75 108.40 121.80 * * * * * 39 LEU 39 1.328 1.225 1.504 1.542 1.467 119.05 115.69 120.28 110.09 111.25 114.25 124.02 * * ** ** 40 ARG 40 1.324 1.221 1.527 1.531 1.462 124.02 118.26 119.89 108.96 113.74 112.08 121.79 * * * 41 PRO 41 1.349 1.234 1.539 1.522 1.484 123.36 114.78 121.42 109.62 112.02 102.40 123.80 * * * * 42 GLU 42 1.324 1.236 1.536 1.533 1.450 124.59 117.23 120.62 109.94 111.87 108.38 122.16 +* * +* 43 VAL 43 1.321 1.231 1.523 1.563 1.457 120.25 117.30 120.34 110.12 112.66 113.08 122.35 44 ARG 44 1.320 1.234 1.505 1.534 1.448 120.17 114.17 121.97 110.29 114.26 113.33 123.86 * * +* +* Residue-by-residue listing for refined_18 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 45 SER 45 1.305 1.243 1.536 1.530 1.432 123.87 116.35 120.52 110.93 108.75 108.03 123.11 +* * * * +* 46 LYS 46 1.312 1.214 1.514 1.514 1.467 123.22 115.31 120.97 110.26 110.36 108.51 123.66 * * * 47 GLU 47 1.313 1.228 1.531 1.520 1.465 124.20 115.12 121.85 109.46 110.18 107.54 122.99 * * +* +* 48 GLN 48 1.312 1.226 1.519 1.515 1.438 122.26 116.11 120.79 110.37 110.79 110.77 123.05 * * * 49 MET 49 1.316 1.229 1.504 1.507 1.446 121.95 115.94 120.32 112.03 110.59 110.35 123.73 * * * * 50 LEU 50 1.336 1.209 1.517 1.563 1.462 121.79 115.54 120.71 110.53 109.27 112.38 123.64 * +* * +* 51 GLU 51 1.325 1.238 1.549 1.521 1.439 124.49 116.23 120.89 109.68 110.95 106.42 122.86 * * +* ** ** 52 LEU 52 1.325 1.235 1.524 1.530 1.449 122.51 116.04 121.05 109.65 111.66 109.76 122.90 53 LEU 53 1.308 1.237 1.542 1.512 1.428 121.79 117.24 120.27 114.18 112.47 108.19 122.48 +* +* ** * ** 54 VAL 54 1.330 1.229 1.531 1.565 1.466 121.34 115.58 120.85 110.00 109.21 112.32 123.53 55 LEU 55 1.334 1.232 1.519 1.527 1.468 123.09 115.14 120.80 107.82 110.81 109.56 124.07 * * 56 GLU 56 1.320 1.242 1.526 1.542 1.446 123.25 116.56 120.64 110.99 111.86 109.52 122.74 57 GLN 57 1.310 1.230 1.513 1.539 1.440 120.26 116.28 119.85 112.06 109.12 110.58 123.83 * * * 58 PHE 58 1.340 1.236 1.518 1.540 1.460 122.45 116.40 120.56 109.71 111.55 111.41 123.03 59 LEU 59 1.323 1.222 1.518 1.527 1.445 120.67 117.11 120.16 111.53 112.55 112.30 122.70 * * 60 GLY 60 1.319 1.226 1.513 - 1.446 119.63 116.51 120.57 - 112.49 - 122.92 61 ALA 61 1.323 1.244 1.520 1.521 1.450 122.03 115.17 120.90 110.69 109.95 110.60 123.93 62 LEU 62 1.331 1.241 1.530 1.534 1.456 123.95 118.07 120.08 108.60 110.30 108.85 121.85 * * 63 PRO 63 1.346 1.241 1.521 1.537 1.456 122.26 117.98 119.39 109.48 109.59 104.34 122.63 * * 64 PRO 64 1.354 1.229 1.534 1.519 1.472 123.60 117.09 120.10 110.28 113.67 103.06 122.78 65 GLU 65 1.334 1.235 1.539 1.533 1.454 120.64 117.62 120.07 111.07 112.66 112.38 122.30 * * 66 ILE 66 1.334 1.234 1.535 1.550 1.448 120.85 115.78 121.09 110.46 110.44 111.01 123.09 67 GLN 67 1.317 1.237 1.536 1.525 1.451 122.59 116.14 120.82 111.36 110.92 109.24 123.02 68 ALA 68 1.328 1.235 1.529 1.517 1.464 122.20 116.19 120.82 110.40 111.14 110.65 122.98 69 ARG 69 1.327 1.234 1.514 1.527 1.464 121.94 115.17 121.09 109.41 109.92 110.94 123.73 70 VAL 70 1.323 1.217 1.509 1.534 1.448 122.81 116.40 120.41 108.74 111.48 111.56 123.19 71 GLN 71 1.304 1.231 1.531 1.529 1.455 122.45 116.70 120.62 112.77 113.58 111.13 122.67 +* * +* 72 GLY 72 1.316 1.225 1.522 - 1.449 120.78 117.26 120.34 - 113.35 - 122.40 73 GLN 73 1.322 1.232 1.547 1.561 1.450 120.73 115.67 120.72 113.57 110.72 108.44 123.59 * +* +* * +* 74 ARG 74 1.334 1.222 1.543 1.534 1.477 125.36 117.58 120.63 110.33 112.55 112.15 121.72 * ** ** 75 PRO 75 1.352 1.224 1.535 1.533 1.481 122.74 115.93 121.13 109.46 112.99 103.58 122.93 76 GLY 76 1.322 1.224 1.521 - 1.447 121.28 116.94 120.66 - 112.98 - 122.40 77 SER 77 1.319 1.241 1.544 1.537 1.460 122.52 118.13 119.69 111.84 109.77 110.12 122.16 78 PRO 78 1.363 1.231 1.525 1.536 1.479 123.00 117.29 120.19 110.05 114.44 104.86 122.49 * * +* +* 79 GLU 79 1.320 1.235 1.507 1.521 1.455 120.58 115.69 120.83 112.66 110.91 111.84 123.45 * * Residue-by-residue listing for refined_18 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 80 GLU 80 1.321 1.226 1.534 1.531 1.442 121.85 115.93 120.86 110.54 107.98 109.90 123.18 * * 81 ALA 81 1.349 1.230 1.508 1.514 1.457 122.62 115.96 120.24 109.92 110.89 110.38 123.79 * * 82 ALA 82 1.333 1.216 1.530 1.534 1.456 122.72 116.02 120.98 111.20 110.89 110.51 122.97 83 ALA 83 1.310 1.233 1.539 1.518 1.448 122.35 118.17 119.79 111.26 111.92 110.88 122.02 * * 84 LEU 84 1.352 1.226 1.507 1.564 1.473 118.76 116.80 120.50 110.65 112.69 117.57 122.68 +* +* +* **** **** 85 VAL 85 1.321 1.233 1.526 1.539 1.454 120.68 115.86 121.05 111.98 111.09 113.57 123.09 * * * 86 ASP 86 1.326 1.226 1.525 1.525 1.454 121.98 116.21 120.92 110.11 110.22 111.32 122.86 87 GLY 87 1.323 1.234 1.522 - 1.453 121.04 115.66 121.15 - 111.73 - 123.19 88 LEU 88 1.318 1.235 1.525 1.529 1.451 122.78 117.25 120.17 110.82 111.86 110.53 122.58 89 ARG 89 1.337 1.237 1.546 1.560 1.457 120.46 114.51 122.49 112.98 110.62 113.36 122.89 * * +* +* +* 90 ARG 90 1.307 1.232 1.513 1.539 1.448 123.21 116.53 120.46 110.54 111.16 110.26 123.02 +* +* 91 GLU 91 1.325 1.228 1.531 1.544 1.444 120.81 118.08 120.42 110.58 109.63 111.58 121.48 92 PRO 92 1.333 1.232 1.533 1.526 1.462 122.15 115.95 121.19 110.28 111.74 102.56 122.85 93 GLY 93 1.318 1.236 1.505 - 1.432 120.75 115.78 120.96 - 109.96 - 123.22 * * 94 GLY 94 1.308 1.249 1.511 - 1.446 121.38 - 120.00 - 111.36 - - * * 95 GLY 301 - 1.239 1.512 - 1.441 - 116.98 120.18 - 111.05 - 122.83 96 SER 302 1.316 1.238 1.525 1.520 1.440 121.25 116.32 120.76 111.68 109.81 109.85 122.90 97 ASP 303 1.327 1.239 1.513 1.543 1.453 121.36 117.55 120.12 109.76 109.75 112.35 122.32 * * 98 PRO 304 1.346 1.239 1.523 1.541 1.469 122.69 115.36 121.46 110.25 111.39 103.59 123.17 * * 99 GLY 305 1.317 1.239 1.506 - 1.431 121.37 118.13 119.64 - 111.31 - 122.22 * * 100 PRO 306 1.344 1.238 1.532 1.536 1.473 123.17 115.30 121.19 109.77 112.26 103.11 123.48 * * * 101 GLU 307 1.320 1.241 1.554 1.544 1.444 122.87 116.75 120.60 111.57 112.53 108.87 122.61 * * 102 ALA 308 1.323 1.229 1.511 1.514 1.449 121.94 116.43 120.87 111.09 111.89 111.10 122.70 103 ALA 309 1.318 1.232 1.512 1.497 1.448 121.22 116.99 120.12 110.84 111.56 111.16 122.87 104 ARG 310 1.339 1.225 1.522 1.530 1.456 120.64 116.11 120.86 109.57 109.71 112.72 123.02 * * 105 LEU 311 1.333 1.220 1.531 1.525 1.411 122.66 116.53 120.14 111.82 109.63 108.76 123.29 ** * ** 106 ARG 312 1.336 1.234 1.523 1.527 1.474 122.38 114.14 121.65 106.80 110.16 110.35 124.20 * +* +* 107 PHE 313 1.312 1.211 1.528 1.531 1.445 124.66 117.66 120.31 111.52 113.29 107.78 122.01 * +* +* +* 108 ARG 314 1.304 1.239 1.538 1.540 1.443 120.06 117.15 120.74 114.10 113.29 111.41 122.08 +* ** ** 109 CYS 315 1.319 1.239 1.534 1.542 1.454 120.56 115.56 120.87 110.94 109.31 110.91 123.56 110 PHE 316 1.333 1.243 1.523 1.545 1.455 123.84 115.72 121.30 110.48 110.84 109.74 122.98 * * 111 HIS 317 1.309 1.232 1.501 1.570 1.434 120.91 117.70 119.91 109.13 107.43 112.05 122.39 * * ** * * ** 112 TYR 318 1.292 1.224 1.505 1.523 1.420 118.90 114.84 121.01 112.21 109.02 112.76 124.06 +** +* +* * * +** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 113 GLU 319 1.287 1.233 1.533 1.555 1.422 123.91 115.28 121.05 114.89 110.53 108.90 123.60 *** * +* * +** *** 114 GLU 320 1.347 1.226 1.513 1.553 1.478 124.66 115.41 120.57 108.05 111.98 112.75 124.03 * * * +* * * +* 115 ALA 321 1.312 1.227 1.521 1.517 1.465 123.84 114.39 121.88 108.38 111.08 108.48 123.72 * * * * * 116 THR 322 1.285 1.239 1.537 1.498 1.418 124.28 116.04 121.09 112.20 112.23 104.53 122.76 *** +* ** * * **** **** 117 GLY 323 1.310 1.244 1.513 - 1.428 120.55 118.14 120.61 - 112.17 - 121.25 * * * * 118 PRO 324 1.330 1.231 1.511 1.503 1.450 121.99 116.36 120.47 110.18 112.75 103.04 123.13 * * * 119 GLN 325 1.324 1.232 1.527 1.531 1.436 121.32 115.97 121.04 108.73 108.42 111.38 122.95 * * 120 GLU 326 1.341 1.230 1.520 1.528 1.449 121.61 116.00 121.11 110.62 110.13 111.15 122.90 121 ALA 327 1.315 1.228 1.529 1.516 1.455 121.61 116.43 120.56 111.12 110.06 110.60 123.00 122 LEU 328 1.333 1.215 1.513 1.529 1.465 121.75 116.43 120.40 108.89 110.89 112.23 123.16 * * 123 ALA 329 1.324 1.238 1.517 1.516 1.453 121.87 115.34 121.10 110.10 110.07 110.34 123.55 124 GLN 330 1.324 1.231 1.516 1.540 1.451 122.32 114.26 121.73 108.21 108.39 109.79 123.93 * * 125 LEU 331 1.311 1.215 1.501 1.518 1.446 123.79 116.92 120.01 110.46 112.83 109.39 123.06 * * * * 126 ARG 332 1.311 1.234 1.512 1.521 1.443 121.49 117.49 120.08 110.62 111.53 111.42 122.40 * * 127 GLU 333 1.329 1.201 1.515 1.537 1.432 118.15 117.36 119.42 111.95 110.08 114.07 123.15 +* * +* ** ** 128 LEU 334 1.350 1.228 1.523 1.536 1.473 121.99 116.02 120.88 110.24 110.79 111.51 123.10 +* +* 129 CYS 335 1.321 1.224 1.538 1.536 1.440 122.47 116.80 121.17 111.08 109.47 109.35 121.98 130 ARG 336 1.324 1.216 1.534 1.554 1.428 121.63 117.09 119.78 115.53 111.80 110.89 123.11 * +* +** +** 131 GLN 337 1.339 1.235 1.531 1.522 1.472 122.39 114.06 121.76 107.49 109.37 110.28 124.18 * * * 132 TRP 338 1.329 1.226 1.541 1.562 1.447 125.21 118.56 119.74 113.28 112.95 108.35 121.69 +* +* * +* * +* 133 LEU 339 1.331 1.219 1.523 1.551 1.473 118.56 116.14 120.24 110.22 111.93 113.99 123.63 * +* ** ** 134 ARG 340 1.333 1.231 1.551 1.539 1.474 124.31 117.77 120.82 111.72 113.74 111.22 121.40 * * * * 135 PRO 341 1.361 1.233 1.526 1.535 1.485 123.49 115.70 121.14 110.20 113.01 103.64 123.15 * * * 136 GLU 342 1.312 1.234 1.529 1.522 1.439 122.53 116.50 120.77 109.70 110.30 109.36 122.70 * * * 137 VAL 343 1.322 1.232 1.516 1.553 1.453 120.76 117.27 120.38 110.25 112.45 112.77 122.34 138 ARG 344 1.314 1.234 1.505 1.533 1.448 119.99 114.53 121.95 109.37 113.12 113.38 123.52 * +* +* 139 SER 345 1.291 1.232 1.517 1.519 1.420 123.11 115.36 120.15 113.09 108.80 110.29 124.42 +** +* +* +** 140 LYS 346 1.309 1.235 1.524 1.494 1.484 126.10 116.02 120.98 108.62 114.52 107.22 123.00 * +* * ** * +* ** 141 GLU 347 1.299 1.242 1.530 1.513 1.456 122.17 115.56 121.67 110.37 111.62 109.88 122.76 ** ** 142 GLN 348 1.293 1.231 1.510 1.515 1.425 121.97 115.88 120.83 113.18 110.25 111.23 123.28 +** +* +* +** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 143 MET 349 1.324 1.229 1.496 1.535 1.447 121.30 115.74 120.24 109.72 109.69 113.25 124.01 * +* +* 144 LEU 350 1.342 1.208 1.524 1.549 1.456 121.81 115.76 120.65 109.92 109.37 111.70 123.48 * * 145 GLU 351 1.329 1.240 1.539 1.516 1.441 124.24 115.95 121.06 109.38 111.70 107.12 122.99 * +* +* 146 LEU 352 1.319 1.228 1.513 1.525 1.445 122.33 115.63 121.20 109.77 111.12 109.67 123.17 147 LEU 353 1.298 1.248 1.542 1.507 1.419 121.75 116.73 120.40 114.11 112.09 108.50 122.87 ** * ** ** * ** 148 VAL 354 1.332 1.219 1.523 1.568 1.462 121.43 115.37 120.86 110.00 108.13 112.45 123.73 * * * 149 LEU 355 1.331 1.231 1.526 1.556 1.468 123.71 115.42 120.51 111.78 109.84 108.18 124.06 * * * * 150 GLU 356 1.325 1.235 1.532 1.545 1.459 123.89 116.31 121.09 109.24 110.73 109.15 122.60 * * 151 GLN 357 1.325 1.223 1.509 1.541 1.442 120.45 116.03 120.08 111.22 109.59 110.32 123.84 152 PHE 358 1.328 1.232 1.512 1.537 1.454 122.99 116.52 120.46 110.38 111.66 111.08 123.02 153 LEU 359 1.319 1.225 1.523 1.526 1.445 120.38 117.26 120.16 112.29 113.23 112.53 122.57 * * * 154 GLY 360 1.317 1.230 1.511 - 1.444 119.62 116.07 120.63 - 111.88 - 123.30 155 ALA 361 1.327 1.237 1.517 1.524 1.458 122.78 115.59 120.86 110.44 110.50 110.66 123.53 156 LEU 362 1.320 1.245 1.523 1.528 1.436 123.28 117.54 120.58 108.53 111.07 109.30 121.88 * * 157 PRO 363 1.335 1.242 1.524 1.542 1.439 121.68 118.39 119.31 110.06 107.80 104.35 122.28 +* +* * +* 158 PRO 364 1.345 1.224 1.533 1.515 1.475 123.68 117.32 119.88 111.20 114.18 102.89 122.77 159 GLU 365 1.332 1.234 1.540 1.555 1.455 121.27 117.23 120.23 111.24 112.44 113.47 122.50 * +* +* 160 ILE 366 1.327 1.236 1.525 1.540 1.456 121.56 115.39 121.29 109.45 110.16 110.73 123.31 161 GLN 367 1.315 1.237 1.540 1.526 1.445 122.53 116.05 120.98 111.82 110.60 109.47 122.94 * * 162 ALA 368 1.328 1.237 1.530 1.520 1.467 122.48 115.95 121.02 110.11 110.60 110.33 123.02 163 ARG 369 1.326 1.237 1.518 1.527 1.464 121.93 115.80 120.78 109.18 110.26 111.61 123.42 164 VAL 370 1.329 1.218 1.504 1.534 1.450 122.29 116.63 120.13 108.83 111.36 112.66 123.24 * * 165 GLN 371 1.313 1.222 1.521 1.528 1.457 121.72 116.28 120.73 112.35 112.57 111.45 122.97 * * * 166 GLY 372 1.309 1.230 1.530 - 1.435 120.96 117.70 120.01 - 113.65 - 122.29 * * 167 GLN 373 1.326 1.227 1.554 1.556 1.458 121.27 115.64 120.79 113.60 110.56 108.54 123.57 * * +* * +* 168 ARG 374 1.333 1.225 1.546 1.529 1.479 125.25 117.55 120.83 110.79 115.08 111.84 121.60 * * +* * +* 169 PRO 375 1.355 1.236 1.551 1.535 1.480 122.76 116.12 121.09 109.62 112.84 103.47 122.79 * * 170 GLY 376 1.331 1.227 1.525 - 1.452 121.89 116.96 120.32 - 113.27 - 122.71 171 SER 377 1.316 1.245 1.543 1.530 1.447 122.17 117.98 120.01 112.64 110.08 109.77 122.01 * * 172 PRO 378 1.360 1.230 1.527 1.536 1.471 122.83 117.19 120.30 110.61 114.56 104.74 122.50 * * +* +* 173 GLU 379 1.313 1.233 1.520 1.518 1.460 121.00 116.33 120.50 113.44 111.41 110.36 123.16 * +* +* 174 GLU 380 1.330 1.219 1.520 1.530 1.450 121.41 116.08 120.79 110.21 107.86 110.65 123.10 * * Residue-by-residue listing for refined_18 Page 14 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 175 ALA 381 1.345 1.219 1.517 1.515 1.447 122.01 116.46 120.15 110.61 110.43 110.65 123.34 * * 176 ALA 382 1.329 1.225 1.538 1.535 1.465 122.74 116.29 120.73 111.31 111.35 110.34 122.97 177 ALA 383 1.319 1.234 1.524 1.522 1.461 122.52 117.51 120.24 110.54 110.92 111.32 122.25 178 LEU 384 1.339 1.216 1.503 1.562 1.456 118.93 116.35 120.30 111.31 111.64 117.24 123.29 * +* +* +*** +*** 179 VAL 385 1.327 1.233 1.534 1.553 1.461 122.68 116.47 120.72 110.90 111.56 111.65 122.80 180 ASP 386 1.324 1.226 1.527 1.525 1.464 121.67 115.95 120.97 110.07 110.75 111.01 123.07 181 GLY 387 1.315 1.220 1.520 - 1.441 121.06 116.63 120.54 - 112.40 - 122.83 * * 182 LEU 388 1.325 1.230 1.526 1.530 1.469 122.50 116.78 120.69 109.82 112.17 110.58 122.52 183 ARG 389 1.322 1.232 1.540 1.548 1.478 122.11 116.48 121.06 109.79 111.04 110.71 122.34 * * 184 ARG 390 1.317 1.235 1.528 1.553 1.444 121.44 117.04 120.55 114.86 115.16 111.87 122.31 * +** * +** 185 GLU 391 1.324 1.235 1.537 1.531 1.445 120.64 116.52 121.75 112.86 113.55 112.76 121.64 * * * 186 PRO 392 1.343 1.238 1.533 1.544 1.462 123.38 114.86 121.67 110.08 110.20 103.59 123.47 * * * 187 GLY 393 1.314 1.241 1.506 - 1.430 122.87 115.96 120.79 - 110.33 - 123.20 * * * * 188 GLY 394 1.301 - 1.498 - 1.436 121.39 - - - 110.36 - - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* ** +** ** * *** +* **** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 15 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 168 1.283 1.352 1.322 .013 *** +* C-N (Pro) 1.341 .016 18 1.330 1.363 1.347 .009 * C-O C-O 1.231 .020 187 1.201 1.249 1.231 .008 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.490 1.554 1.525 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.491 1.530 1.513 .009 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.497 1.535 1.518 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.498 1.583 1.548 .021 +* +* CH1E-CH2E (the rest) 1.530 .020 138 1.494 1.570 1.534 .014 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.404 1.484 1.451 .015 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.428 1.464 1.442 .010 * N-CH1E (Pro) 1.466 .015 18 1.439 1.485 1.469 .012 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 114.06 118.56 116.29 .96 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.66 119.16 117.06 .95 * CH1E-C-N (Pro) 116.9 1.5 18 114.78 118.39 116.36 .99 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.84 124.42 122.94 .66 * O-C-N (Pro) 122.0 1.4 18 122.28 123.80 122.96 .37 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.15 126.10 122.04 1.47 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.62 122.87 121.01 .75 * C-N-CH1E (Pro) 122.6 5.0 18 121.64 123.68 122.79 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.31 122.49 120.69 .56 CH2G*-C-O (Gly) 120.8 2.1 17 119.64 121.15 120.37 .41 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 108.38 111.31 110.52 .64 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 108.74 112.20 110.29 1.02 * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.80 116.01 110.79 1.67 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.92 115.16 110.91 1.54 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.96 113.65 111.76 1.09 N-CH1E-C (Pro) 111.8 2.5 18 107.80 114.56 112.29 1.67 +* * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 108.48 111.32 110.49 .56 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 104.53 113.57 111.47 2.25 **** * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.40 104.86 103.51 .67 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.42 117.57 110.77 1.85 ** **** ------------------------------------------------------------------------------------------------------------- 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_18 Page 17 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 142 93.4% Residues in additional allowed regions [a,b,l,p] 10 6.6% 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 93.4 83.8 10.0 1.0 Inside b. Omega angle st dev 186 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.3 3.1 1.6 -.5 Inside e. H-bond energy st dev 124 .8 .8 .2 .0 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 19 10.9 18.1 6.5 -1.1 BETTER b. Chi-1 trans st dev 54 7.0 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 59 8.2 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 132 9.5 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 60 6.7 20.4 5.0 -2.7 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 93.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .80 2 Residue-by-residue listing for refined_18 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .12 Chi1-chi2 distribution -.09 Chi1 only .24 Chi3 & chi4 .40 Omega .11 ------ .12 ===== Main-chain covalent forces:- Main-chain bond lengths .32 Main-chain bond angles .38 ------ .35 ===== OVERALL AVERAGE .21 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.