Residue-by-residue listing for refined_14 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 180.8 - - - 2 SER 2 B - - -57.1 - - - - - - - 179.5 - 34.5 - 3 ASP 3 B - - -61.0 - - - - - - - 177.8 -.6 34.4 - +* +* 4 PRO 4 S - - - - - -55.0 - - - - - 179.9 - 39.1 - * * 5 GLY 5 h - - - - - - - - - - - 181.1 - - - 6 PRO 6 H - - - - - -59.1 -59.1 -35.3 - - - 177.9 - 37.7 - * * 7 GLU 7 H A - - -64.6 - - -61.7 -48.6 - - - 180.6 - 34.2 - 8 ALA 8 H A - - - - - -65.7 -41.9 - - - 180.8 - 34.3 - 9 ALA 9 H A - - - - - -62.1 -47.4 - - - 179.3 -2.8 33.5 - * * 10 ARG 10 H A - 187.2 - 191.7 - -64.8 -36.1 - - - 180.5 -2.7 34.2 - 11 LEU 11 H A - 171.7 - - - -61.2 -46.5 - - - 177.5 -1.9 34.6 - 12 ARG 12 H A - - -60.7 180.1 - -64.2 -40.3 - - - 178.5 -2.5 34.3 - 13 PHE 13 H A - 179.9 - - - -63.4 -39.2 - - - 175.5 -2.4 34.7 - 14 ARG 14 H A - - -81.1 - - -71.3 -26.9 - - - 180.8 -2.8 33.5 - * * 15 CYS 15 h A - - -60.2 - - - - - - - 180.3 -1.5 33.7 - 16 PHE 16 t B - 185.9 - - - - - - - - 176.6 -.7 34.7 - +* +* 17 HIS 17 B 74.4 - - - - - - - - - 176.2 - 34.0 - 18 TYR 18 B - 167.2 - - - - - - - - 179.3 -.8 32.0 - +* +* 19 GLU 19 t B 53.9 - - 175.4 - - - - - - 181.3 -.7 32.0 - +* +* Residue-by-residue listing for refined_14 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 - - -60.4 170.9 - - - - - - 180.2 -.6 35.5 - +* +* 21 ALA 21 T A - - - - - - - - - - 180.5 - 33.7 - 22 THR 22 T A - 197.4 - - - - - - - - 181.0 -1.1 34.3 - * * 23 GLY 23 h - - - - - - - - - - - 184.1 -1.1 - - * * 24 PRO 24 H - - - - - -62.3 -62.3 -32.8 - - - 180.6 - 37.9 - * * 25 GLN 25 H A - - -83.6 - - -75.0 -38.8 - - - 176.8 - 32.0 - * * 26 GLU 26 H A - 176.3 - 171.2 - -70.2 -33.7 - - - 174.1 - 32.4 - * * 27 ALA 27 H A - - - - - -60.6 -46.4 - - - 177.1 -2.5 34.2 - 28 LEU 28 H A - - -65.8 178.0 - -55.1 -43.6 - - - 179.9 -2.2 34.1 - 29 ALA 29 H A - - - - - -58.6 -46.0 - - - 178.9 -1.8 34.3 - 30 GLN 30 H A - - -69.8 168.4 - -67.2 -40.2 - - - 177.3 -2.0 34.1 - 31 LEU 31 H A - - -71.9 169.4 - -64.7 -46.8 - - - 178.9 -2.9 33.2 - * * 32 ARG 32 H A 54.4 - - 185.8 - -67.7 -28.5 - - - 172.2 -3.5 26.1 - * +* ** ** 33 GLU 33 H A - 178.8 - 188.1 - -60.4 -48.7 - - - 182.1 -1.6 36.7 - 34 LEU 34 H A - - -60.7 173.1 - -68.9 -48.9 - - - 182.4 -1.8 35.0 - 35 CYS 35 H A 70.2 - - - - -63.9 -33.1 - - - 178.0 -3.6 33.2 - ** ** 36 ARG 36 H A - 186.1 - 193.6 - -64.2 -35.4 - - - 180.9 -1.8 35.8 - 37 GLN 37 H A - - -62.2 183.1 - -71.6 -16.6 - - - 179.8 -1.1 33.1 - ** * ** 38 TRP 38 H A - 167.3 - - - -97.7 -43.0 - - - 182.7 -.7 34.7 - +** +* +** 39 LEU 39 H A - - -62.4 158.4 - -90.1 -42.8 - - - 175.1 -3.3 33.8 - * ** +* ** 40 ARG 40 h l - - -50.1 185.1 - - - - - - 182.8 -2.1 31.9 - * * 41 PRO 41 T - - - - - -68.7 - - - - - 182.5 - 38.6 - * * 42 GLU 42 T A - 192.0 - - - - - - - - 182.6 - 34.0 - 43 VAL 43 T A - - -61.4 - - - - - - - 180.5 - 32.3 - 44 ARG 44 t B - - -68.1 180.6 - - - - - - 182.4 -2.9 32.3 - * * 45 SER 45 h B - - -52.7 - - - - - - - 177.3 - 36.3 - 46 LYS 46 H A - - -64.4 170.0 - -51.8 -37.7 - - - 181.6 - 36.7 - * * 47 GLU 47 H A - 179.8 - 180.9 - -52.2 -44.5 - - - 180.9 - 36.7 - * * 48 GLN 48 H A - - -60.6 - - -70.6 -37.3 - - - 181.7 -1.0 34.2 - * * 49 MET 49 H A - - -60.8 180.2 - -62.9 -43.5 - - - 175.3 -1.3 33.4 - 50 LEU 50 H A - - -80.4 - - -52.7 -53.7 - - - 184.4 -2.3 34.2 - * * * 51 GLU 51 H A - - -57.3 - - -64.8 -39.9 - - - 179.3 -1.5 33.3 - 52 LEU 52 H A - - -63.2 177.7 - -64.0 -40.4 - - - 179.2 -2.6 34.1 - 53 LEU 53 H A - 181.6 - - - -72.2 -30.1 - - - 173.5 -2.5 31.6 - * * 54 VAL 54 H A - 188.1 - - - -60.8 -49.1 - - - 178.9 -2.0 35.4 - 55 LEU 55 H A - 178.7 - - - -54.4 -44.0 - - - 181.7 -2.5 36.2 - 56 GLU 56 H A - 184.7 - - - -56.0 -46.6 - - - 178.3 -2.0 34.1 - Residue-by-residue listing for refined_14 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 GLN 57 H A - 190.3 - - - -75.3 -46.1 - - - 184.0 -1.6 33.2 - 58 PHE 58 H A - 176.3 - - - -53.0 -43.8 - - - 180.7 -3.2 34.4 - * +* +* 59 LEU 59 H A - - -63.0 188.1 - -66.2 -35.8 - - - 177.8 -3.0 31.2 - * * 60 GLY 60 H - - - - - - -81.4 -21.0 - - - 177.5 -.8 - - * +* +* +* 61 ALA 61 H A - - - - - -72.3 -24.8 - - - 175.1 -1.9 33.8 - * * 62 LEU 62 h B - - -65.9 171.3 - - - - - - 177.5 -1.1 37.0 - * * 63 PRO 63 h - - - - - -68.6 - - - - - 181.6 - 38.9 - * * 64 PRO 64 H - - - - - -39.1 -39.1 -49.8 - - - 182.2 - 39.5 - ** ** +* ** 65 GLU 65 H A 62.2 - - 184.8 - -61.5 -48.0 - - - 181.7 - 33.6 - 66 ILE 66 H A - - -58.5 180.0 - -71.9 -40.3 - - - 180.7 - 34.4 - 67 GLN 67 H A - 178.3 - 178.3 - -62.9 -44.7 - - - 180.0 -3.3 34.3 - +* +* 68 ALA 68 H A - - - - - -60.3 -37.7 - - - 178.7 -3.0 33.2 - * * 69 ARG 69 H A - - -58.1 - - -63.9 -46.2 - - - 177.7 -1.4 33.3 - 70 VAL 70 H A - 173.4 - - - -58.8 -48.7 - - - 180.4 -2.0 34.9 - 71 GLN 71 H A - - -98.5 - - -57.4 -25.9 - - - 174.2 -2.8 27.6 - ** * * * +* ** 72 GLY 72 H - - - - - - -69.7 -25.1 - - - 181.3 -1.0 - - * * * 73 GLN 73 H a - - -69.3 - - -107.3 -58.4 - - - 191.3 -2.0 34.0 - +*** +* +* +*** 74 ARG 74 h ~l - - -71.6 - - - - - - - 177.5 -2.6 28.5 - ** +* ** 75 PRO 75 - - - - - -58.0 - - - - - 179.4 - 39.5 - +* +* 76 GLY 76 S - - - - - - - - - - - 177.8 - - - 77 SER 77 h B - - -56.8 - - - - - - - 183.6 - 34.2 - 78 PRO 78 H - - - - - -61.3 -61.3 -45.5 - - - 181.7 - 38.4 - * * 79 GLU 79 H A - - -60.8 179.3 - -73.9 -29.2 - - - 174.7 - 31.2 - 80 GLU 80 H A - 186.9 - - - -64.3 -45.0 - - - 177.0 - 35.2 - 81 ALA 81 H A - - - - - -63.7 -40.0 - - - 179.9 -2.4 34.3 - 82 ALA 82 H A - - - - - -54.6 -34.3 - - - 179.6 -2.5 34.1 - 83 ALA 83 H A - - - - - -70.3 -47.7 - - - 179.3 -1.2 32.4 - * * 84 LEU 84 H A 51.2 - - 156.8 - -70.2 -38.3 - - - 179.7 -1.3 28.2 - * * +* +* 85 VAL 85 H A - - -56.0 - - -68.3 -30.9 - - - 175.0 -2.9 30.8 - * * 86 ASP 86 H A - 180.5 - - - -56.3 -45.4 - - - 176.8 -1.4 34.7 - 87 GLY 87 H - - - - - - -68.6 -31.6 - - - 181.9 -1.4 - - 88 LEU 88 H A - - -61.7 175.4 - -75.0 -17.1 - - - 175.5 -1.5 33.2 - +* +* 89 ARG 89 h A 63.8 - - 177.5 - - - - - - 177.8 -1.2 32.7 - * * 90 ARG 90 T l - - -58.7 184.3 - - - - - - 179.2 -1.3 31.8 - 91 GLU 91 t b - - -57.3 184.6 - - - - - - 183.9 -1.2 33.8 - * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 92 PRO 92 - - - - - -86.2 - - - - - 177.6 - 38.8 - +* * +* 93 GLY 93 - - - - - - - - - - - 177.7 -.6 - - +* +* 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 181.5 - - - 96 SER 302 B - - -58.3 - - - - - - - 179.2 - 34.1 - 97 ASP 303 B - 187.5 - - - - - - - - 180.2 -.7 35.4 - +* +* 98 PRO 304 - - - - - -59.1 - - - - - 179.2 - 38.3 - * * 99 GLY 305 h - - - - - - - - - - - 177.3 - - - 100 PRO 306 H - - - - - -59.8 -59.8 -31.6 - - - 177.3 - 38.0 - * * 101 GLU 307 H A - - -63.4 - - -62.1 -43.3 - - - 178.7 - 34.7 - 102 ALA 308 H A - - - - - -70.7 -38.9 - - - 178.9 - 34.4 - 103 ALA 309 H A - - - - - -63.1 -41.3 - - - 177.9 -2.6 33.4 - 104 ARG 310 H A - 187.9 - 189.4 - -66.8 -33.7 - - - 178.9 -2.7 33.7 - 105 LEU 311 H A - 174.4 - - - -62.3 -45.1 - - - 176.7 -1.5 34.7 - 106 ARG 312 H A - - -59.5 177.6 - -58.6 -44.5 - - - 181.1 -2.3 36.2 - 107 PHE 313 H A - 179.9 - - - -65.6 -41.5 - - - 179.5 -2.2 34.8 - 108 ARG 314 H A - - -72.8 - - -83.3 -8.0 - - - 175.9 -3.0 31.2 - +* +** * +** 109 CYS 315 h A - - -63.0 - - - - - - - 179.4 -1.0 32.5 - * * 110 PHE 316 t B - 182.6 - - - - - - - - 176.6 -.7 34.7 - +* +* 111 HIS 317 B 72.7 - - - - - - - - - 173.6 - 34.3 - * * 112 TYR 318 B - 166.9 - - - - - - - - 180.8 -1.1 31.8 - * * 113 GLU 319 t B 48.6 - - 174.3 - - - - - - 181.9 -.7 32.3 - +* +* 114 GLU 320 T A - - -61.0 172.8 - - - - - - 182.0 -.6 35.0 - +* +* 115 ALA 321 T A - - - - - - - - - - 182.5 - 33.4 - 116 THR 322 T A - 195.7 - - - - - - - - 180.3 -.9 34.1 - * * 117 GLY 323 h - - - - - - - - - - - 182.8 -1.1 - - * * 118 PRO 324 H - - - - - -59.4 -59.4 -38.5 - - - 180.8 - 38.1 - * * 119 GLN 325 H A - - -81.4 - - -65.1 -44.1 - - - 180.5 - 33.0 - 120 GLU 326 H A - 181.4 - 166.1 - -71.6 -32.8 - - - 173.6 - 31.9 - * * 121 ALA 327 H A - - - - - -63.3 -42.2 - - - 177.3 -2.4 34.3 - 122 LEU 328 H A - - -66.3 175.0 - -60.5 -40.2 - - - 177.9 -2.5 33.8 - 123 ALA 329 H A - - - - - -56.5 -36.0 - - - 178.0 -1.7 34.5 - 124 GLN 330 H A - - -71.0 169.3 - -78.0 -44.0 - - - 179.3 -1.2 34.4 - * * * 125 LEU 331 H A - - -72.5 171.3 - -64.5 -46.1 - - - 179.9 -2.8 32.5 - * * 126 ARG 332 H A 59.9 - - 184.9 - -67.5 -29.0 - - - 172.6 -3.7 27.1 - * ** +* ** 127 GLU 333 H A - 174.7 - 180.0 - -62.5 -48.3 - - - 181.4 -.8 36.3 - +* +* 128 LEU 334 H A - - -63.1 173.8 - -68.1 -41.1 - - - 180.1 -2.1 33.9 - Residue-by-residue listing for refined_14 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 129 CYS 335 H A 66.9 - - - - -72.7 -36.4 - - - 179.1 -3.1 32.5 - * * 130 ARG 336 H A - 168.1 - - - -65.3 -32.4 - - - 176.3 -2.2 29.6 - * * 131 GLN 337 H A 58.1 - - 184.8 - -76.5 -15.6 - - - 177.0 -1.6 30.6 - ** ** 132 TRP 338 H A - 159.2 - - - -92.7 -39.9 - - - 181.3 -.7 33.8 - * ** +* ** 133 LEU 339 H A - - -64.0 157.0 - -88.0 -43.2 - - - 180.2 -3.0 34.6 - * +* * +* 134 ARG 340 h l - - -59.8 187.6 - - - - - - 180.7 -2.0 30.4 - 135 PRO 341 T - - - - - -66.1 - - - - - 180.4 - 38.7 - * * 136 GLU 342 T A - 184.0 - - - - - - - - 183.8 - 34.6 - 137 VAL 343 T A - - -59.7 - - - - - - - 179.4 -.6 32.6 - +* +* 138 ARG 344 t B - - -70.0 180.6 - - - - - - 180.6 -3.1 31.6 - * * 139 SER 345 h B - - -56.4 - - - - - - - 178.0 - 36.0 - 140 LYS 346 H A - - -64.6 168.7 - -53.6 -43.3 - - - 182.3 - 36.7 - 141 GLU 347 H A - 179.9 - 177.7 - -55.1 -41.5 - - - 179.4 - 34.7 - 142 GLN 348 H A - - -59.9 - - -68.1 -33.4 - - - 178.8 -.5 33.8 - +* +* 143 MET 349 H A - - -61.1 179.9 - -66.2 -40.3 - - - 173.9 -1.3 33.1 - * * 144 LEU 350 H A - - -77.6 - - -55.4 -53.6 - - - 180.5 -1.9 34.6 - * * 145 GLU 351 H A - - -64.6 - - -55.2 -52.0 - - - 180.3 -2.0 35.4 - * * 146 LEU 352 H A - - -63.8 175.4 - -59.7 -40.2 - - - 179.6 -3.1 34.6 - * * 147 LEU 353 H A - 180.8 - - - -74.5 -30.0 - - - 172.6 -2.5 31.2 - * * 148 VAL 354 H A - 184.2 - - - -62.9 -46.6 - - - 177.3 -2.3 34.7 - 149 LEU 355 H A - 176.9 - - - -53.9 -46.0 - - - 179.5 -2.8 36.2 - 150 GLU 356 H A - 179.7 - - - -52.8 -52.3 - - - 181.5 -2.1 35.0 - * * * 151 GLN 357 H A - 191.1 - - - -72.0 -44.7 - - - 182.9 -1.9 33.4 - 152 PHE 358 H A - 179.9 - - - -53.6 -47.2 - - - 181.1 -3.4 34.3 - +* +* 153 LEU 359 H A - - -63.6 185.6 - -62.9 -37.6 - - - 180.1 -3.1 31.2 - * * 154 GLY 360 H - - - - - - -80.4 -26.6 - - - 178.3 -1.2 - - * * * * 155 ALA 361 H A - - - - - -65.6 -29.7 - - - 175.3 -2.4 33.4 - 156 LEU 362 h B - - -63.6 173.0 - - - - - - 177.3 -1.4 37.3 - 157 PRO 363 h - - - - - -68.2 - - - - - 180.6 - 39.2 - +* +* 158 PRO 364 H - - - - - -41.5 -41.5 -38.4 - - - 179.8 - 38.2 - ** ** * ** 159 GLU 365 H A 60.4 - - 177.7 - -68.3 -48.3 - - - 180.3 - 32.6 - 160 ILE 366 H A - - -61.3 180.1 - -71.8 -39.9 - - - 179.8 - 34.6 - 161 GLN 367 H A - 178.2 - 177.9 - -60.7 -42.0 - - - 179.4 -3.5 34.3 - ** ** 162 ALA 368 H A - - - - - -65.5 -30.7 - - - 178.7 -2.1 33.2 - 163 ARG 369 H A - - -62.2 - - -68.2 -34.6 - - - 174.5 -1.1 32.9 - * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 164 VAL 370 H A - 173.3 - - - -77.2 -39.9 - - - 186.1 -1.4 36.7 - * * 165 GLN 371 H A - 206.3 - - - -54.9 -27.3 - - - 177.3 -2.9 33.8 - * * * * 166 GLY 372 h - - - - - - - - - - - 184.4 -1.0 - - * * 167 GLN 373 T a - - -58.9 - - - - - - - 190.9 -1.8 34.0 - +* +* 168 ARG 374 t l - - -66.2 - - - - - - - 178.4 -2.4 30.1 - * * 169 PRO 375 - - - - - -60.2 - - - - - 177.7 - 39.4 - +* +* 170 GLY 376 S - - - - - - - - - - - 175.3 - - - 171 SER 377 h B - - -55.2 - - - - - - - 182.9 - 34.3 - 172 PRO 378 H - - - - - -57.8 -57.8 -38.0 - - - 184.4 - 37.4 - 173 GLU 379 H A - - -34.5 - - -73.8 -31.8 - - - 178.3 - 33.5 - ** ** 174 GLU 380 H A - 186.2 - - - -69.2 -45.2 - - - 175.0 - 34.7 - 175 ALA 381 H A - - - - - -58.3 -42.3 - - - 178.4 -2.4 34.6 - 176 ALA 382 H A - - - - - -60.4 -41.6 - - - 178.5 -2.7 34.1 - 177 ALA 383 H A - - - - - -71.6 -29.9 - - - 177.9 -2.2 33.2 - 178 LEU 384 H A - - -49.3 184.6 - -66.3 -49.1 - - - 183.2 -1.9 35.8 - * * 179 VAL 385 H A - - -55.2 - - -72.1 -31.1 - - - 174.4 -2.6 30.7 - 180 ASP 386 H A - 180.8 - - - -53.3 -34.8 - - - 175.6 -2.0 34.4 - * * 181 GLY 387 H - - - - - - -84.5 -39.0 - - - 182.0 -.9 - - +* * +* 182 LEU 388 H A - - -62.0 174.6 - -60.5 -26.5 - - - 177.5 -1.9 33.4 - * * 183 ARG 389 h a 58.1 - - 181.6 - - - - - - 180.2 -2.0 33.5 - 184 ARG 390 T l - - -64.4 186.0 - - - - - - 175.6 -1.2 27.4 - * +* +* 185 GLU 391 t B - - -64.6 187.9 - - - - - - 181.6 -1.4 33.6 - 186 PRO 392 S - - - - - -51.4 - - - - - 179.8 - 38.0 - * * * 187 GLY 393 - - - - - - - - - - - 177.2 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * ** * ** +*** +** +* ** ** +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.1 181.0 -63.5 178.0 -60.1 -65.5 -39.1 - - - 179.3 -1.9 34.1 Standard deviations: 7.9 8.6 8.6 7.9 10.4 9.9 8.5 - - - 2.9 .8 2.4 Numbers of values: 14 46 72 60 18 122 122 0 0 0 186 128 170 0 Residue-by-residue listing for refined_14 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_14 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 - 1.235 1.496 - 1.460 - 116.67 120.18 - 111.10 - 123.15 * * 2 SER 2 1.306 1.233 1.521 1.526 1.431 121.45 116.00 120.76 110.73 110.32 109.74 123.24 +* * +* 3 ASP 3 1.307 1.235 1.536 1.553 1.458 122.65 120.41 118.46 111.32 107.78 110.18 121.09 +* * ** * * * ** 4 PRO 4 1.375 1.242 1.524 1.526 1.482 121.93 115.55 120.90 109.42 112.06 103.66 123.55 ** * * ** 5 GLY 5 1.320 1.235 1.506 - 1.431 121.17 118.27 119.78 - 111.15 - 121.95 * * 6 PRO 6 1.344 1.237 1.533 1.536 1.467 122.50 116.37 120.59 110.92 112.47 104.29 123.03 * * 7 GLU 7 1.331 1.236 1.527 1.545 1.452 122.11 115.52 120.84 109.51 109.79 111.54 123.60 8 ALA 8 1.333 1.234 1.517 1.526 1.459 122.77 115.72 120.99 109.89 110.84 110.50 123.29 9 ALA 9 1.315 1.238 1.523 1.502 1.443 122.45 117.17 120.16 110.78 111.79 110.30 122.65 10 ARG 10 1.343 1.217 1.516 1.525 1.460 120.33 115.94 120.80 107.74 109.55 113.13 123.26 * * +* +* 11 LEU 11 1.322 1.228 1.536 1.523 1.414 123.16 116.63 120.40 112.45 110.63 107.79 122.93 ** * +* ** 12 ARG 12 1.330 1.224 1.530 1.533 1.468 122.01 114.99 121.34 110.06 109.98 110.63 123.64 13 PHE 13 1.318 1.221 1.553 1.540 1.463 124.30 116.44 120.98 113.17 110.48 106.75 122.55 * * +* ** ** Residue-by-residue listing for refined_14 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 1.327 1.233 1.520 1.532 1.468 122.85 116.96 120.42 109.58 112.36 111.46 122.61 15 CYS 15 1.313 1.231 1.524 1.531 1.456 121.41 116.77 120.63 110.15 111.44 110.95 122.60 * * 16 PHE 16 1.319 1.240 1.513 1.530 1.442 120.98 116.36 120.79 109.44 109.73 110.89 122.84 17 HIS 17 1.305 1.238 1.502 1.575 1.438 120.29 118.36 119.50 110.47 106.93 112.47 122.13 +* * ** * * +* * ** 18 TYR 18 1.297 1.233 1.487 1.530 1.424 118.01 114.94 121.34 111.57 108.87 113.28 123.72 ** +* +* ** +* ** 19 GLU 19 1.280 1.237 1.504 1.541 1.398 121.61 114.85 121.44 113.15 109.83 111.48 123.71 *** * *** +* *** 20 GLU 20 1.306 1.223 1.526 1.522 1.451 123.65 115.51 120.84 110.13 110.28 108.79 123.63 +* * * +* 21 ALA 21 1.324 1.231 1.534 1.518 1.448 123.37 117.71 120.36 110.46 112.29 110.21 121.92 22 THR 22 1.331 1.215 1.543 1.590 1.452 119.15 115.63 121.73 110.95 108.12 110.98 122.49 +* * * +* 23 GLY 23 1.318 1.227 1.512 - 1.437 121.22 118.75 120.14 - 110.96 - 121.11 * * * 24 PRO 24 1.328 1.221 1.539 1.508 1.463 122.36 117.94 120.05 110.79 114.67 103.21 121.99 * * * 25 GLN 25 1.331 1.239 1.504 1.537 1.467 120.00 115.25 121.39 109.68 110.32 114.30 123.35 * ** ** 26 GLU 26 1.308 1.239 1.531 1.530 1.448 121.44 115.82 121.23 112.75 109.79 110.74 122.95 * * * 27 ALA 27 1.323 1.221 1.518 1.522 1.451 122.10 116.01 120.45 110.52 109.15 110.56 123.51 28 LEU 28 1.341 1.215 1.512 1.528 1.467 122.62 116.60 120.15 108.66 111.50 111.80 123.24 29 ALA 29 1.326 1.239 1.524 1.514 1.462 122.07 115.34 121.27 110.23 110.65 110.09 123.38 30 GLN 30 1.314 1.228 1.521 1.507 1.433 123.18 115.72 120.86 112.20 111.11 108.43 123.40 * * * * * * 31 LEU 31 1.316 1.217 1.515 1.520 1.453 123.32 117.58 119.79 110.87 112.38 110.66 122.63 32 ARG 32 1.327 1.214 1.498 1.536 1.457 120.51 116.28 120.53 114.64 113.40 115.49 123.19 * ** +** +** 33 GLU 33 1.309 1.234 1.538 1.520 1.450 121.58 114.84 121.36 108.33 108.57 109.08 123.79 * * 34 LEU 34 1.327 1.231 1.518 1.531 1.454 123.81 116.64 120.41 109.74 111.81 109.48 122.94 * * 35 CYS 35 1.328 1.216 1.531 1.551 1.445 121.37 116.94 120.65 111.40 109.94 111.28 122.39 * * 36 ARG 36 1.338 1.194 1.520 1.477 1.429 122.24 117.50 120.08 108.04 111.56 109.66 122.42 +* +** +* * +** 37 GLN 37 1.315 1.237 1.526 1.517 1.462 121.39 114.33 121.89 111.80 111.04 110.08 123.79 * * 38 TRP 38 1.306 1.232 1.551 1.547 1.439 124.81 116.47 120.89 113.17 111.46 106.78 122.63 +* * +* +* ** ** 39 LEU 39 1.310 1.223 1.531 1.523 1.459 122.78 116.50 119.95 112.61 111.49 108.26 123.54 * * * * 40 ARG 40 1.344 1.222 1.540 1.542 1.467 124.66 117.86 120.67 111.42 113.56 111.29 121.47 * +* +* 41 PRO 41 1.344 1.228 1.527 1.532 1.475 122.73 117.07 120.56 109.95 113.99 103.54 122.37 42 GLU 42 1.307 1.234 1.536 1.532 1.440 120.53 116.41 121.04 110.96 110.50 110.14 122.52 +* +* 43 VAL 43 1.322 1.233 1.524 1.556 1.460 120.83 116.98 120.70 110.39 112.52 112.45 122.31 44 ARG 44 1.310 1.232 1.494 1.521 1.443 120.76 114.97 121.25 110.78 111.20 112.56 123.78 * * * * 45 SER 45 1.287 1.249 1.524 1.523 1.430 123.11 115.45 120.46 110.20 110.27 107.61 124.09 *** * +* *** Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 46 LYS 46 1.336 1.219 1.521 1.531 1.476 124.28 114.59 121.46 108.58 109.99 108.54 123.89 * * * 47 GLU 47 1.314 1.244 1.526 1.518 1.454 125.13 115.58 121.00 109.32 111.41 107.50 123.40 * +* +* +* 48 GLN 48 1.317 1.229 1.517 1.538 1.444 121.89 115.80 120.62 110.21 110.32 110.75 123.55 49 MET 49 1.325 1.235 1.500 1.499 1.459 122.96 116.38 119.93 110.66 111.98 110.48 123.69 * +* +* 50 LEU 50 1.345 1.218 1.507 1.563 1.463 121.49 116.23 119.95 108.47 110.13 112.78 123.62 * +* * +* 51 GLU 51 1.333 1.236 1.533 1.531 1.461 122.09 116.90 120.51 110.31 111.86 111.23 122.58 52 LEU 52 1.329 1.229 1.512 1.523 1.451 121.63 116.09 120.89 110.02 110.75 110.84 123.02 53 LEU 53 1.311 1.236 1.542 1.518 1.414 121.43 117.05 120.42 115.31 111.47 108.69 122.51 * ** +** * +** 54 VAL 54 1.337 1.225 1.524 1.550 1.470 120.67 114.64 121.25 106.82 107.58 113.05 124.08 * * * 55 LEU 55 1.339 1.226 1.523 1.537 1.464 124.15 115.36 120.92 108.74 110.57 109.07 123.72 * * 56 GLU 56 1.319 1.238 1.544 1.541 1.454 123.25 117.13 120.69 110.70 111.57 109.84 122.17 57 GLN 57 1.322 1.226 1.511 1.540 1.458 120.24 115.39 120.49 111.54 109.41 111.10 124.07 58 PHE 58 1.327 1.232 1.515 1.538 1.459 123.85 116.66 120.46 110.56 112.09 109.55 122.87 * * 59 LEU 59 1.314 1.223 1.516 1.528 1.442 120.75 116.86 120.24 112.10 112.64 112.09 122.90 * * * 60 GLY 60 1.314 1.228 1.513 - 1.445 120.06 116.31 120.50 - 112.31 - 123.17 * * 61 ALA 61 1.328 1.244 1.519 1.528 1.457 122.32 115.14 121.00 110.75 109.66 110.76 123.84 62 LEU 62 1.328 1.234 1.518 1.525 1.446 123.58 118.29 119.65 107.82 109.53 109.14 122.04 * * * * 63 PRO 63 1.345 1.240 1.519 1.539 1.445 121.79 117.66 119.26 109.53 108.98 104.85 123.08 * * +* +* 64 PRO 64 1.346 1.224 1.531 1.518 1.472 124.30 116.31 120.58 110.03 113.64 102.11 123.06 65 GLU 65 1.328 1.226 1.548 1.534 1.456 121.94 117.24 120.50 110.89 112.44 109.92 122.22 * * 66 ILE 66 1.334 1.243 1.532 1.554 1.443 121.33 115.29 121.35 110.38 109.90 110.56 123.32 67 GLN 67 1.317 1.239 1.528 1.523 1.446 122.93 116.38 120.64 110.69 111.27 109.56 122.98 68 ALA 68 1.320 1.241 1.523 1.519 1.459 121.96 116.35 120.69 110.86 111.24 110.89 122.94 69 ARG 69 1.327 1.228 1.526 1.530 1.450 121.11 116.54 120.41 110.37 110.02 111.81 123.03 70 VAL 70 1.339 1.233 1.507 1.536 1.474 122.17 114.94 121.07 107.18 111.13 112.39 123.98 71 GLN 71 1.307 1.212 1.520 1.532 1.441 123.51 117.18 120.49 114.83 113.79 113.23 122.26 +* * ** +* ** 72 GLY 72 1.310 1.234 1.549 - 1.446 119.76 117.38 120.13 - 112.54 - 122.49 * +* +* 73 GLN 73 1.349 1.222 1.534 1.562 1.480 121.75 115.54 120.68 107.08 112.88 113.28 123.78 * +* * +* +* +* 74 ARG 74 1.332 1.227 1.524 1.552 1.480 124.53 116.83 120.92 110.82 112.04 116.97 122.16 * * +* +*** +*** 75 PRO 75 1.356 1.227 1.534 1.538 1.478 123.26 116.01 120.97 109.27 112.87 103.20 123.00 76 GLY 76 1.322 1.220 1.516 - 1.452 121.02 116.95 120.93 - 113.13 - 122.12 77 SER 77 1.312 1.241 1.535 1.523 1.446 121.63 117.83 119.92 110.93 109.54 110.09 122.24 * * 78 PRO 78 1.351 1.223 1.522 1.536 1.475 123.12 117.01 120.32 109.75 113.81 104.20 122.65 * * 79 GLU 79 1.316 1.232 1.512 1.526 1.456 121.68 115.62 121.09 113.30 110.81 111.51 123.28 +* +* Residue-by-residue listing for refined_14 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 1.325 1.234 1.538 1.535 1.439 121.80 115.91 121.01 110.31 107.57 109.84 123.05 * * * 81 ALA 81 1.352 1.232 1.511 1.515 1.453 122.31 115.44 120.58 110.03 110.49 110.50 123.95 +* +* 82 ALA 82 1.332 1.208 1.521 1.526 1.454 123.67 116.28 120.68 110.36 111.51 110.25 123.04 * * * 83 ALA 83 1.298 1.235 1.541 1.509 1.444 122.08 118.22 119.92 111.78 112.11 110.66 121.85 ** * ** 84 LEU 84 1.351 1.232 1.509 1.560 1.467 118.67 116.76 120.51 110.87 112.47 117.24 122.72 +* * +* +*** +*** 85 VAL 85 1.317 1.229 1.527 1.538 1.454 120.89 115.50 120.90 111.60 111.01 113.76 123.59 * * * 86 ASP 86 1.325 1.222 1.525 1.533 1.465 123.24 116.28 121.21 110.68 109.46 109.67 122.46 87 GLY 87 1.314 1.234 1.528 - 1.444 120.13 116.14 120.91 - 111.67 - 122.90 * * 88 LEU 88 1.327 1.240 1.536 1.530 1.468 123.13 117.09 120.62 110.85 112.58 110.44 122.29 89 ARG 89 1.334 1.229 1.529 1.550 1.471 120.89 114.68 121.23 110.66 109.39 112.67 124.09 * * * 90 ARG 90 1.346 1.228 1.519 1.537 1.470 125.49 116.79 120.69 110.79 112.43 112.60 122.50 * ** * ** 91 GLU 91 1.310 1.214 1.509 1.525 1.441 120.76 117.92 120.25 110.25 109.81 111.31 121.79 * * 92 PRO 92 1.330 1.240 1.517 1.538 1.442 122.45 116.15 120.88 110.33 112.31 103.58 122.96 +* +* 93 GLY 93 1.310 1.237 1.513 - 1.446 120.65 115.86 121.09 - 111.77 - 123.03 * * 94 GLY 94 1.309 1.252 1.508 - 1.442 121.67 - 119.61 - 110.99 - - * * * 95 GLY 301 - 1.237 1.506 - 1.452 - 115.28 121.38 - 111.18 - 123.34 96 SER 302 1.304 1.239 1.525 1.521 1.433 122.13 115.70 120.95 111.10 111.05 109.63 123.34 +* * +* 97 ASP 303 1.319 1.249 1.529 1.541 1.457 122.30 118.33 119.65 109.81 108.46 109.87 122.01 * * 98 PRO 304 1.353 1.232 1.535 1.539 1.475 122.95 116.54 120.70 110.32 112.77 103.89 122.76 99 GLY 305 1.315 1.231 1.500 - 1.421 120.88 118.45 119.69 - 111.84 - 121.85 +* +* 100 PRO 306 1.350 1.230 1.524 1.536 1.462 122.31 115.39 121.31 110.41 110.64 104.71 123.29 * +* +* 101 GLU 307 1.325 1.240 1.532 1.541 1.444 122.87 115.45 121.18 109.66 109.64 110.77 123.34 102 ALA 308 1.327 1.225 1.520 1.521 1.452 122.82 115.98 121.09 110.14 110.19 110.32 122.92 103 ALA 309 1.320 1.235 1.523 1.508 1.450 122.04 116.93 120.43 110.70 111.07 110.71 122.62 104 ARG 310 1.336 1.221 1.520 1.526 1.453 120.46 116.35 120.71 108.81 109.29 113.02 122.94 * * 105 LEU 311 1.333 1.216 1.528 1.526 1.413 122.40 116.18 120.54 111.80 109.11 108.83 123.23 ** ** 106 ARG 312 1.329 1.231 1.528 1.523 1.472 122.87 114.68 121.42 107.94 110.06 109.79 123.89 * * 107 PHE 313 1.315 1.215 1.546 1.541 1.456 124.65 116.86 120.77 112.68 111.36 107.01 122.35 * +* * ** ** 108 ARG 314 1.322 1.227 1.525 1.537 1.466 121.96 117.34 120.19 111.49 113.59 112.14 122.46 109 CYS 315 1.310 1.244 1.519 1.528 1.461 121.01 115.64 121.17 110.92 110.74 112.03 123.18 * * 110 PHE 316 1.318 1.244 1.514 1.537 1.435 121.93 116.21 121.03 109.98 109.48 110.58 122.74 * * Residue-by-residue listing for refined_14 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 111 HIS 317 1.298 1.234 1.503 1.573 1.440 120.55 118.47 119.42 110.07 107.29 112.15 122.09 ** * ** * * ** 112 TYR 318 1.298 1.227 1.494 1.532 1.425 117.84 114.77 121.38 111.94 108.51 113.31 123.83 ** * +* ** +* ** 113 GLU 319 1.282 1.241 1.506 1.535 1.403 122.20 114.61 121.50 113.32 110.25 110.72 123.87 *** +** +* *** 114 GLU 320 1.309 1.222 1.532 1.531 1.451 124.15 116.16 120.34 110.37 111.56 108.99 123.47 * * * 115 ALA 321 1.326 1.236 1.532 1.523 1.463 123.19 117.76 120.15 110.39 113.19 110.44 122.09 116 THR 322 1.328 1.230 1.539 1.580 1.454 119.56 115.92 121.36 110.67 109.08 111.20 122.62 * * * 117 GLY 323 1.313 1.234 1.516 - 1.433 121.02 118.25 120.12 - 111.27 - 121.63 * * * 118 PRO 324 1.332 1.219 1.528 1.509 1.467 122.97 117.83 119.67 110.48 114.49 103.39 122.49 * * * 119 GLN 325 1.338 1.228 1.523 1.553 1.470 120.52 115.26 121.53 108.99 109.81 113.78 123.18 * +* +* 120 GLU 326 1.314 1.238 1.533 1.525 1.447 122.04 116.15 121.18 113.84 110.86 109.91 122.67 * +* +* 121 ALA 327 1.320 1.226 1.531 1.522 1.458 121.96 116.12 120.76 110.38 109.54 110.41 123.11 122 LEU 328 1.327 1.217 1.508 1.518 1.464 122.68 116.78 119.94 109.29 111.71 111.46 123.28 123 ALA 329 1.335 1.232 1.524 1.521 1.474 122.22 114.88 121.71 109.95 110.14 110.28 123.41 124 GLN 330 1.306 1.225 1.522 1.497 1.430 123.40 115.96 120.81 111.45 111.55 108.43 123.23 +* +* * * +* 125 LEU 331 1.317 1.220 1.510 1.515 1.459 122.95 117.84 119.68 110.86 113.56 111.09 122.47 126 ARG 332 1.327 1.205 1.504 1.544 1.451 119.78 115.63 121.01 114.89 111.91 114.95 123.34 * * +** +** +** 127 GLU 333 1.303 1.239 1.546 1.526 1.449 122.74 115.36 121.26 110.45 109.33 107.38 123.35 +* +* +* 128 LEU 334 1.322 1.227 1.523 1.529 1.454 123.14 117.12 120.54 110.62 112.12 110.00 122.34 129 CYS 335 1.315 1.222 1.531 1.543 1.443 120.11 116.79 120.81 111.64 110.17 111.83 122.38 * * 130 ARG 336 1.329 1.217 1.525 1.547 1.437 122.24 117.83 119.84 115.20 113.32 110.84 122.31 * +** +** 131 GLN 337 1.319 1.237 1.550 1.526 1.462 120.59 115.34 121.34 113.09 111.79 111.96 123.32 * +* +* 132 TRP 338 1.327 1.233 1.554 1.560 1.472 124.48 116.54 121.05 112.58 111.94 108.39 122.40 * * +* * * +* 133 LEU 339 1.311 1.224 1.521 1.532 1.462 122.58 115.55 120.46 111.53 111.14 108.51 123.97 * * * 134 ARG 340 1.331 1.231 1.532 1.530 1.467 125.00 117.71 120.68 110.91 114.31 113.34 121.61 +* * +* +* 135 PRO 341 1.346 1.227 1.528 1.534 1.474 123.06 116.68 120.77 110.08 112.93 103.54 122.55 136 GLU 342 1.310 1.233 1.528 1.528 1.443 121.06 116.45 120.89 109.94 110.39 110.30 122.64 * * 137 VAL 343 1.322 1.224 1.519 1.553 1.457 120.68 117.06 120.57 110.07 112.42 112.42 122.37 138 ARG 344 1.311 1.233 1.498 1.528 1.441 120.46 114.76 121.26 111.27 111.86 112.75 123.97 * * * * 139 SER 345 1.292 1.244 1.520 1.526 1.434 123.34 115.64 120.42 110.32 110.16 107.99 123.94 +** * * +** 140 LYS 346 1.327 1.211 1.509 1.523 1.465 123.92 114.92 121.15 108.39 109.91 108.75 123.87 * * * 141 GLU 347 1.312 1.235 1.527 1.520 1.453 124.14 115.64 121.06 110.72 111.42 108.85 123.27 * * * 142 GLN 348 1.320 1.218 1.515 1.535 1.448 121.89 116.37 120.60 110.45 110.36 111.01 123.02 Residue-by-residue listing for refined_14 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 1.325 1.231 1.500 1.500 1.455 122.11 116.37 120.03 110.96 111.08 110.95 123.60 * +* +* 144 LEU 350 1.345 1.211 1.505 1.563 1.464 121.18 115.48 120.30 108.88 108.59 112.28 124.02 * * +* * +* 145 GLU 351 1.327 1.234 1.541 1.522 1.468 123.89 116.49 120.67 109.56 111.82 108.80 122.83 * * * 146 LEU 352 1.327 1.229 1.519 1.520 1.455 122.72 116.30 120.89 109.79 111.53 109.99 122.81 147 LEU 353 1.305 1.234 1.546 1.521 1.421 121.38 117.15 120.62 115.71 111.45 108.81 122.22 +* +* +** +** 148 VAL 354 1.333 1.222 1.530 1.556 1.464 120.54 115.08 121.01 107.84 107.55 113.14 123.89 * * 149 LEU 355 1.340 1.228 1.520 1.534 1.472 124.17 115.11 120.85 108.65 110.23 109.18 124.03 * * 150 GLU 356 1.323 1.245 1.540 1.542 1.460 123.34 116.69 120.83 109.72 111.25 109.64 122.46 151 GLN 357 1.320 1.234 1.509 1.550 1.449 120.62 115.72 120.05 111.78 109.39 110.85 124.17 152 PHE 358 1.332 1.236 1.523 1.545 1.454 123.41 116.46 120.55 110.05 111.48 110.44 122.97 153 LEU 359 1.323 1.217 1.508 1.531 1.449 121.18 117.29 119.99 111.94 112.81 112.14 122.68 154 GLY 360 1.316 1.227 1.505 - 1.441 119.26 116.23 120.38 - 111.93 - 123.39 155 ALA 361 1.332 1.228 1.531 1.534 1.457 122.43 115.91 120.94 111.26 110.39 110.71 123.14 156 LEU 362 1.326 1.236 1.531 1.520 1.458 123.10 119.05 119.46 107.45 109.57 108.80 121.48 * * * 157 PRO 363 1.351 1.233 1.518 1.543 1.458 121.60 118.40 119.05 109.36 108.99 104.48 122.55 * * * * 158 PRO 364 1.351 1.226 1.542 1.520 1.475 123.85 117.83 120.01 110.56 114.44 103.16 122.15 * * 159 GLU 365 1.336 1.229 1.547 1.544 1.467 120.72 117.00 120.56 111.01 111.80 111.54 122.37 * * 160 ILE 366 1.333 1.236 1.528 1.551 1.451 121.84 115.36 121.19 110.24 110.00 110.28 123.42 161 GLN 367 1.315 1.227 1.525 1.523 1.449 123.04 116.39 120.39 110.90 110.82 109.54 123.20 162 ALA 368 1.329 1.230 1.516 1.513 1.466 122.36 116.36 120.67 110.32 111.55 111.22 122.97 163 ARG 369 1.320 1.209 1.521 1.525 1.455 121.48 116.58 120.66 111.28 110.50 111.29 122.76 * * 164 VAL 370 1.324 1.242 1.507 1.544 1.466 121.62 113.79 121.62 105.84 109.19 111.66 124.59 * * * 165 GLN 371 1.318 1.200 1.517 1.520 1.442 125.44 117.05 120.07 110.42 111.86 110.49 122.82 +* ** ** 166 GLY 372 1.313 1.235 1.536 - 1.442 120.30 117.61 120.37 - 113.54 - 122.02 * * * 167 GLN 373 1.333 1.222 1.512 1.562 1.461 120.52 115.40 120.75 107.45 111.82 113.41 123.82 +* * +* +* 168 ARG 374 1.330 1.222 1.515 1.550 1.471 123.84 117.14 120.93 109.88 110.53 116.57 121.83 * * +*** +*** 169 PRO 375 1.338 1.227 1.528 1.529 1.472 122.79 115.19 121.62 110.17 111.68 102.54 123.18 * * 170 GLY 376 1.311 1.222 1.505 - 1.445 121.37 116.18 120.81 - 112.75 - 123.00 * * 171 SER 377 1.308 1.248 1.528 1.522 1.438 122.23 117.19 120.19 110.60 108.33 110.70 122.59 * * * * 172 PRO 378 1.336 1.220 1.520 1.535 1.463 123.62 117.56 120.00 110.33 114.45 104.89 122.43 * +* +* 173 GLU 379 1.316 1.225 1.507 1.527 1.458 120.81 115.85 120.85 109.65 110.15 112.20 123.29 174 GLU 380 1.322 1.211 1.516 1.533 1.423 121.99 116.12 120.63 111.89 107.07 109.43 123.18 +* * +* 175 ALA 381 1.350 1.229 1.528 1.511 1.455 122.29 115.78 120.81 110.06 110.31 109.87 123.41 +* +* Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 176 ALA 382 1.329 1.213 1.520 1.529 1.454 123.00 115.99 121.01 110.53 110.57 110.28 123.00 177 ALA 383 1.294 1.238 1.532 1.517 1.446 122.64 117.21 120.27 111.07 111.54 110.60 122.52 +** +** 178 LEU 384 1.340 1.236 1.515 1.553 1.465 120.79 114.68 121.73 106.76 107.79 112.57 123.53 * +* * * +* 179 VAL 385 1.320 1.232 1.520 1.538 1.443 122.71 115.73 120.72 112.51 111.72 112.72 123.55 +* +* 180 ASP 386 1.328 1.224 1.531 1.544 1.472 123.31 115.82 120.85 110.72 109.76 109.95 123.31 181 GLY 387 1.329 1.228 1.530 - 1.447 121.26 116.10 120.84 - 112.15 - 123.05 182 LEU 388 1.336 1.227 1.528 1.525 1.485 123.59 116.81 120.74 110.07 113.05 110.66 122.45 * * * 183 ARG 389 1.319 1.235 1.544 1.533 1.476 122.22 114.46 121.48 111.23 110.63 110.27 124.02 184 ARG 390 1.321 1.242 1.504 1.528 1.455 126.20 114.14 121.94 112.92 114.80 114.87 123.87 * +** * * * +** +** 185 GLU 391 1.296 1.229 1.516 1.555 1.433 124.79 119.41 118.45 111.44 105.85 112.15 122.10 ** * * +* +* * +* ** 186 PRO 392 1.352 1.233 1.523 1.523 1.471 122.63 115.34 121.11 110.78 113.05 103.72 123.49 * * * 187 GLY 393 1.306 1.220 1.502 - 1.436 121.82 116.10 120.49 - 110.96 - 123.41 +* +* 188 GLY 394 1.324 - 1.502 - 1.444 121.80 - - - 112.17 - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* +** *** +** ** * +** +* +*** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 Page 15 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 168 1.280 1.352 1.321 .013 *** +* C-N (Pro) 1.341 .016 18 1.328 1.375 1.346 .011 ** C-O C-O 1.231 .020 187 1.194 1.252 1.229 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 170 1.487 1.554 1.523 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.496 1.549 1.513 .014 * +* CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.502 1.534 1.519 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.536 1.590 1.554 .016 +* CH1E-CH2E (the rest) 1.530 .020 138 1.477 1.575 1.532 .014 +** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.398 1.485 1.453 .015 *** * NH1-CH2G* (Gly) 1.451 .016 18 1.421 1.460 1.442 .008 +* N-CH1E (Pro) 1.466 .015 18 1.442 1.482 1.468 .010 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 113.79 120.41 116.25 1.07 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.28 118.75 116.91 1.04 * CH1E-C-N (Pro) 116.9 1.5 18 115.19 118.40 116.71 .97 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 121.09 124.59 122.99 .68 * O-C-N (Pro) 122.0 1.4 18 121.99 123.55 122.81 .43 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.84 126.20 122.22 1.45 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.26 121.82 120.84 .73 C-N-CH1E (Pro) 122.6 5.0 18 121.60 124.30 122.79 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.45 121.94 120.67 .58 * CH2G*-C-O (Gly) 120.8 2.1 17 119.61 121.38 120.43 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.89 111.78 110.52 .46 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 105.84 112.51 109.54 2.00 * +* CH2E-CH1E-C (the rest) 110.1 1.9 138 106.76 115.71 110.68 1.62 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 105.85 114.80 110.71 1.53 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.96 113.54 111.86 .76 N-CH1E-C (Pro) 111.8 2.5 18 108.98 114.67 112.68 1.68 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.87 111.22 110.48 .30 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.28 113.76 112.05 1.06 * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.11 104.89 103.72 .74 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.75 117.24 110.80 2.01 ** +*** ------------------------------------------------------------------------------------------------------------- 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_14 Page 17 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 142 93.4% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 93.4 83.8 10.0 1.0 Inside b. Omega angle st dev 186 2.9 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.4 3.1 1.6 -.5 Inside e. H-bond energy st dev 128 .8 .8 .2 .1 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 14 7.9 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 46 8.6 19.0 5.3 -2.0 BETTER c. Chi-1 gauche plus st dev 72 8.6 17.5 4.9 -1.8 BETTER d. Chi-1 pooled st dev 132 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 60 7.9 20.4 5.0 -2.5 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 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .83 2 Residue-by-residue listing for refined_14 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .11 Chi1-chi2 distribution -.06 Chi1 only -.08 Chi3 & chi4 .36 Omega .17 ------ .13 ===== Main-chain covalent forces:- Main-chain bond lengths .31 Main-chain bond angles .37 ------ .34 ===== OVERALL AVERAGE .21 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.