Residue-by-residue listing for refined_11 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 - - - - - - - - - - - 179.6 - - - 2 SER 2 B - - -56.2 - - - - - - - 177.1 - 35.4 - 3 ASP 3 B 63.5 - - - - - - - - - 182.6 - 33.2 - 4 PRO 4 - - - - - -78.8 - - - - - 182.1 - 39.2 - * +* +* 5 GLY 5 h - - - - - - - - - - - 177.7 - - - 6 PRO 6 H - - - - - -46.9 -46.9 -35.1 - - - 179.0 - 38.8 - +* +* * +* 7 GLU 7 H A 59.3 - - 179.3 - -63.2 -41.3 - - - 181.4 - 32.6 - 8 ALA 8 H A - - - - - -74.1 -40.7 - - - 177.6 -.9 33.9 - * * 9 ALA 9 H A - - - - - -61.5 -44.6 - - - 177.9 -2.4 33.8 - 10 ARG 10 H A - 183.2 - 187.9 - -65.0 -35.6 - - - 181.1 -2.9 34.7 - * * 11 LEU 11 H A - 173.6 - - - -65.4 -45.6 - - - 177.6 -1.8 34.3 - 12 ARG 12 H A - - -63.2 176.6 - -60.2 -37.5 - - - 179.0 -2.7 34.1 - 13 PHE 13 H A - 168.7 - - - -73.8 -49.8 - - - 185.0 -1.9 35.3 - 14 ARG 14 H A - 181.6 - - - -74.3 -32.7 - - - 180.2 -3.8 32.8 - ** ** 15 CYS 15 h A - 181.7 - - - - - - - - 178.5 -2.7 33.3 - 16 PHE 16 t B - 178.1 - - - - - - - - 178.6 -.8 34.5 - +* +* 17 HIS 17 B 72.3 - - - - - - - - - 175.8 - 34.3 - 18 TYR 18 B - 169.7 - - - - - - - - 179.8 -1.0 32.8 - * * 19 GLU 19 t B 49.9 - - 171.4 - - - - - - 181.3 -.7 31.6 - +* +* Residue-by-residue listing for refined_11 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 - - -58.1 164.8 - - - - - - 181.1 -.6 36.1 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.6 - 33.7 - 22 THR 22 T A - 200.8 - - - - - - - - 180.1 -1.0 34.1 - * * * 23 GLY 23 h - - - - - - - - - - - 183.7 -1.0 - - * * 24 PRO 24 H - - - - - -70.4 -70.4 -30.7 - - - 184.1 - 38.5 - * * 25 GLN 25 H A - 214.5 - - - -67.2 -46.0 - - - 180.8 - 36.7 - +* +* 26 GLU 26 H A - 175.5 - 170.7 - -73.6 -33.3 - - - 175.4 - 32.5 - 27 ALA 27 H A - - - - - -61.5 -40.7 - - - 175.9 -2.0 34.0 - 28 LEU 28 H A - - -66.0 179.7 - -59.8 -38.8 - - - 178.7 -2.2 34.3 - 29 ALA 29 H A - - - - - -61.3 -37.2 - - - 179.6 -1.2 34.3 - * * 30 GLN 30 H A - - -46.2 - - -70.4 -50.4 - - - 181.2 -1.5 36.3 - * * 31 LEU 31 H A - - -68.5 172.1 - -59.6 -46.3 - - - 181.5 -2.9 33.6 - * * 32 ARG 32 H A - 185.4 - 176.7 - -60.6 -39.2 - - - 178.8 -3.4 34.0 - +* +* 33 GLU 33 H A - 179.8 - - - -67.6 -50.5 - - - 179.6 -1.3 36.7 - * * 34 LEU 34 H A - - -62.1 173.6 - -64.5 -38.7 - - - 174.8 -2.7 33.4 - 35 CYS 35 H A - 178.4 - - - -60.2 -38.0 - - - 180.1 -3.3 35.5 - +* +* 36 ARG 36 H A - 178.9 - - - -71.1 -36.7 - - - 179.7 -1.6 33.7 - 37 GLN 37 H A - - -63.8 181.1 - -68.3 -21.5 - - - 178.5 -2.0 34.1 - +* +* 38 TRP 38 H a - 155.3 - - - -96.3 -54.5 - - - 178.9 -1.0 31.8 - +* +** * * +** 39 LEU 39 H A - - -63.2 178.0 - -68.5 -48.5 - - - 178.5 -3.5 33.5 - ** ** 40 ARG 40 h l - - -57.8 176.3 - - - - - - 177.9 -1.5 32.2 - 41 PRO 41 T - - - - - -60.4 - - - - - 176.6 - 38.9 - * * 42 GLU 42 T A - 184.2 - - - - - - - - 184.8 - 36.1 - 43 VAL 43 T A - - -58.3 - - - - - - - 181.4 -1.4 32.7 - 44 ARG 44 t B - - -64.0 187.9 - - - - - - 180.9 -3.6 31.3 - ** ** 45 SER 45 h B - - -54.5 - - - - - - - 179.7 - 35.9 - 46 LYS 46 H A - - -68.4 170.8 - -58.1 -40.6 - - - 181.2 - 34.3 - 47 GLU 47 H A - - -57.2 186.1 - -57.4 -42.0 - - - 176.1 - 34.0 - 48 GLN 48 H A - - -78.8 - - -59.5 -38.2 - - - 181.1 - 33.9 - 49 MET 49 H A - - -59.7 179.5 - -66.2 -40.1 - - - 174.1 -1.2 32.8 - * * * 50 LEU 50 H A - - -75.4 - - -58.4 -52.8 - - - 182.2 -1.8 33.9 - * * 51 GLU 51 H A - - -63.4 184.5 - -57.1 -45.0 - - - 180.6 -2.3 32.6 - 52 LEU 52 H A - - -59.8 180.6 - -64.9 -40.4 - - - 178.2 -2.8 33.4 - 53 LEU 53 H A - 173.0 - - - -73.5 -30.0 - - - 171.9 -2.2 31.1 - * * 54 VAL 54 H A - 175.0 - - - -58.7 -44.8 - - - 176.9 -2.6 34.0 - 55 LEU 55 H A - 179.0 - - - -57.2 -48.0 - - - 180.3 -2.1 35.4 - 56 GLU 56 H A - - -68.6 - - -52.9 -47.7 - - - 179.8 -1.8 33.3 - * * Residue-by-residue listing for refined_11 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 - - - -74.5 -43.4 - - - 183.0 -2.0 33.6 - 58 PHE 58 H A - 180.5 - - - -53.4 -46.8 - - - 178.5 -3.0 33.9 - * * 59 LEU 59 H A - - -93.4 - - -58.5 -40.7 - - - 179.4 -2.9 29.4 - +* * * +* 60 GLY 60 H - - - - - - -80.5 -20.5 - - - 178.1 -.9 - - * +* * +* 61 ALA 61 H A - - - - - -71.1 -28.3 - - - 175.1 -1.9 33.7 - 62 LEU 62 h B - - -65.9 171.1 - - - - - - 177.0 -1.4 37.1 - 63 PRO 63 h - - - - - -73.0 - - - - - 181.7 - 38.2 - * * 64 PRO 64 H - - - - - -31.4 -31.4 -56.5 - - - 182.0 - 38.6 - *** +** +* * *** 65 GLU 65 H A 57.0 - - 189.3 - -59.2 -47.3 - - - 180.9 - 32.3 - 66 ILE 66 H A - - -56.0 181.8 - -72.3 -41.1 - - - 180.7 -.7 34.7 - +* +* 67 GLN 67 H A - 179.1 - 178.8 - -63.0 -43.5 - - - 180.8 -3.2 34.4 - +* +* 68 ALA 68 H A - - - - - -60.2 -33.5 - - - 179.3 -3.0 33.9 - * * 69 ARG 69 H A - - -59.3 - - -64.3 -49.7 - - - 178.2 -1.0 35.1 - * * 70 VAL 70 H A - 175.8 - - - -62.7 -44.2 - - - 180.4 -1.5 35.9 - 71 GLN 71 H A - 209.3 - - - -56.5 -29.9 - - - 178.4 -2.9 36.0 - +* * +* 72 GLY 72 H - - - - - - -79.6 -24.3 - - - 182.4 -1.2 - - * * * * 73 GLN 73 H a - - -54.9 193.1 - -101.5 -46.0 - - - 181.4 -1.1 34.0 - *** * *** 74 ARG 74 h l - - -56.5 - - - - - - - 177.5 -3.3 31.8 - +* +* 75 PRO 75 - - - - - -73.3 - - - - - 181.0 - 39.1 - * * 76 GLY 76 - - - - - - - - - - - 180.3 - - - 77 SER 77 h B - - -52.2 - - - - - - - 185.1 - 35.1 - 78 PRO 78 H - - - - - -58.8 -58.8 -44.7 - - - 182.9 - 37.5 - * * 79 GLU 79 H A - - -62.3 175.1 - -72.5 -30.2 - - - 175.7 - 31.6 - 80 GLU 80 H A - 183.4 - - - -66.2 -49.2 - - - 174.9 - 34.6 - 81 ALA 81 H A - - - - - -56.0 -43.9 - - - 178.7 -2.6 34.3 - 82 ALA 82 H A - - - - - -58.1 -40.6 - - - 178.5 -2.7 34.0 - 83 ALA 83 H A - - - - - -72.6 -36.6 - - - 178.3 -2.1 33.4 - 84 LEU 84 H A - - -48.8 182.3 - -62.3 -48.9 - - - 182.8 -2.5 36.8 - * * 85 VAL 85 H A - - -56.0 - - -70.1 -30.5 - - - 175.9 -3.0 30.1 - * * * 86 ASP 86 H A - 185.6 - - - -61.7 -31.9 - - - 176.1 -1.5 32.8 - 87 GLY 87 H - - - - - - -80.2 -16.1 - - - 179.6 -1.2 - - * ** * ** 88 LEU 88 H A - - -59.6 176.0 - -86.5 -38.0 - - - 174.6 -.6 34.2 - +* +* +* 89 ARG 89 h b 54.6 - - 183.8 - - - - - - 183.9 -2.7 32.7 - 90 ARG 90 B - 180.7 - 178.9 - - - - - - 179.4 -1.6 34.2 - 91 GLU 91 t B - - -57.1 177.4 - - - - - - 181.4 - 35.5 - 92 PRO 92 T - - - - - -57.3 - - - - - 178.8 - 37.8 - * * 93 GLY 93 T - - - - - - - - - - - 180.0 - - - Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 GLY 94 t - - - - - - - - - - - - -2.4 - - 95 GLY 301 - - - - - - - - - - - 177.7 - - - 96 SER 302 B - - -54.2 - - - - - - - 183.1 - 35.2 - 97 ASP 303 B 68.3 - - - - - - - - - 183.6 - 34.6 - 98 PRO 304 S - - - - - -79.3 - - - - - 179.6 - 38.5 - * * * 99 GLY 305 h - - - - - - - - - - - 181.2 - - - 100 PRO 306 H - - - - - -56.4 -56.4 -35.6 - - - 180.6 - 38.5 - * * 101 GLU 307 H A 62.0 - - 178.5 - -67.7 -38.4 - - - 179.3 - 32.3 - 102 ALA 308 H A - - - - - -75.1 -30.2 - - - 177.1 - 34.0 - 103 ALA 309 H A - - - - - -63.3 -43.8 - - - 178.8 -2.2 34.8 - 104 ARG 310 H A - 188.0 - 192.8 - -63.7 -33.6 - - - 180.4 -2.2 34.2 - 105 LEU 311 H A - 172.4 - - - -64.0 -49.8 - - - 179.1 -1.2 34.5 - * * 106 ARG 312 H A - - -61.4 179.7 - -61.6 -34.2 - - - 179.6 -2.2 34.7 - 107 PHE 313 H A - 169.3 - - - -74.2 -49.9 - - - 183.6 -2.0 35.4 - 108 ARG 314 H A - 176.9 - - - -77.1 -21.5 - - - 179.5 -3.6 32.9 - +* ** ** 109 CYS 315 h A - 186.6 - - - - - - - - 179.5 -2.3 33.6 - 110 PHE 316 t B - 178.9 - - - - - - - - 177.6 -.8 34.9 - +* +* 111 HIS 317 B 74.2 - - - - - - - - - 174.8 - 34.1 - 112 TYR 318 B - 167.5 - - - - - - - - 180.0 -1.4 32.4 - 113 GLU 319 t B 52.0 - - 181.8 - - - - - - 179.6 - 32.0 - 114 GLU 320 T A - - -61.4 169.9 - - - - - - 178.6 - 35.4 - 115 ALA 321 T A - - - - - - - - - - 183.3 - 34.2 - 116 THR 322 T A - 196.4 - - - - - - - - 180.9 -1.1 34.4 - * * 117 GLY 323 h - - - - - - - - - - - 183.3 -1.1 - - * * 118 PRO 324 H - - - - - -63.5 -63.5 -33.9 - - - 180.6 - 38.1 - * * 119 GLN 325 H A - - -83.2 - - -70.4 -41.7 - - - 179.1 - 32.8 - * * 120 GLU 326 H A - 177.7 - 167.7 - -70.3 -34.1 - - - 175.5 - 32.0 - 121 ALA 327 H A - - - - - -65.5 -38.9 - - - 176.1 -2.4 33.9 - 122 LEU 328 H A - - -67.8 179.6 - -59.4 -37.6 - - - 179.9 -2.2 34.3 - 123 ALA 329 H A - - - - - -63.8 -40.2 - - - 178.1 -1.4 33.6 - 124 GLN 330 H A - - -47.9 - - -63.0 -51.4 - - - 180.0 -1.5 36.9 - * * * 125 LEU 331 H A - - -68.8 172.7 - -58.3 -47.9 - - - 180.4 -2.8 33.9 - * * 126 ARG 332 H A - 179.2 - 177.2 - -58.2 -47.0 - - - 177.7 -3.5 33.2 - +* +* 127 GLU 333 H A - 176.8 - - - -60.4 -50.2 - - - 180.8 -2.2 35.8 - 128 LEU 334 H A - - -62.0 176.9 - -64.9 -41.4 - - - 177.0 -2.8 33.3 - * * 129 CYS 335 H A - 186.8 - - - -64.0 -31.7 - - - 180.3 -3.5 35.3 - +* +* 130 ARG 336 H A - 183.0 - - - -72.8 -30.9 - - - 178.1 -1.9 33.6 - 131 GLN 337 H A - - -57.8 - - -70.9 -16.7 - - - 182.6 -1.5 35.8 - ** ** 132 TRP 338 H a - 163.9 - - - -102.6 -57.7 - - - 179.3 -.6 33.6 - * *** +* +* *** 133 LEU 339 H A - - -60.7 174.7 - -70.3 -44.3 - - - 171.7 -3.7 33.4 - * ** ** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 134 ARG 340 h l - - -51.1 169.0 - - - - - - 181.8 -1.0 33.5 - * * * 135 PRO 341 T - - - - - -64.0 - - - - - 182.3 - 39.0 - * * 136 GLU 342 T A - 190.7 - - - - - - - - 183.0 - 34.5 - 137 VAL 343 T A - - -60.3 - - - - - - - 181.0 - 32.1 - 138 ARG 344 t B - - -65.0 186.2 - - - - - - 180.3 -3.2 31.7 - +* +* 139 SER 345 h B - - -55.8 - - - - - - - 180.1 - 35.6 - 140 LYS 346 H A - - -66.7 170.6 - -52.0 -40.1 - - - 183.4 - 35.6 - * * 141 GLU 347 H A - - -66.7 - - -52.6 -50.2 - - - 178.4 - 36.0 - * * 142 GLN 348 H A - - -67.8 - - -55.6 -40.6 - - - 182.9 -.6 34.9 - +* +* 143 MET 349 H A - - -59.1 181.0 - -64.1 -42.0 - - - 174.6 -1.0 32.7 - * * 144 LEU 350 H A - - -74.4 - - -56.0 -51.2 - - - 182.0 -1.7 33.3 - * * 145 GLU 351 H A - - -60.4 184.9 - -61.8 -42.5 - - - 179.7 -1.9 33.5 - 146 LEU 352 H A - - -61.5 179.5 - -64.8 -39.0 - - - 175.6 -2.8 33.1 - 147 LEU 353 H A - 177.4 - - - -67.7 -33.8 - - - 175.9 -2.4 34.8 - 148 VAL 354 H A - 176.5 - - - -59.7 -43.8 - - - 177.6 -2.1 33.9 - 149 LEU 355 H A - 181.4 - - - -56.5 -47.6 - - - 179.4 -2.1 35.1 - 150 GLU 356 H A - - -66.9 - - -55.8 -44.1 - - - 180.2 -1.7 34.0 - 151 GLN 357 H A - 194.9 - - - -74.9 -46.9 - - - 183.9 -1.9 33.5 - 152 PHE 358 H A - 182.7 - - - -53.9 -48.8 - - - 178.7 -3.3 34.0 - +* +* 153 LEU 359 H A - - -95.7 - - -61.8 -39.1 - - - 180.3 -3.0 30.1 - +* * * +* 154 GLY 360 H - - - - - - -80.9 -18.1 - - - 177.2 -1.1 - - * +* * +* 155 ALA 361 H A - - - - - -75.1 -28.7 - - - 175.0 -2.0 33.9 - 156 LEU 362 h B - - -64.5 171.3 - - - - - - 175.8 -1.3 36.8 - 157 PRO 363 h - - - - - -62.7 - - - - - 182.9 - 39.3 - +* +* 158 PRO 364 H - - - - - -49.9 -49.9 -29.1 - - - 179.6 - 38.0 - * * * * 159 GLU 365 H A 58.5 - - 177.0 - -78.5 -47.9 - - - 180.8 - 33.2 - * * 160 ILE 366 H A - - -58.8 180.0 - -68.6 -38.8 - - - 178.3 - 34.4 - 161 GLN 367 H A - 179.0 - 176.8 - -61.7 -40.8 - - - 178.5 -3.3 34.7 - +* +* 162 ALA 368 H A - - - - - -63.1 -35.5 - - - 180.6 -1.2 33.8 - * * 163 ARG 369 H A - - -50.8 - - -65.5 -43.4 - - - 176.1 -1.4 34.4 - * * 164 VAL 370 H A - 173.0 - - - -59.2 -52.3 - - - 177.2 -1.9 35.2 - * * 165 GLN 371 H A - - -101.8 - - -54.5 -28.5 - - - 175.9 -2.7 30.3 - ** * ** 166 GLY 372 H - - - - - - -69.9 -38.8 - - - 181.5 -1.4 - - 167 GLN 373 H A - - -52.4 191.4 - -90.5 -48.0 - - - 181.8 -1.4 34.4 - ** ** 168 ARG 374 h ~l - - -60.9 - - - - - - - 176.6 -3.6 31.3 - ** ** ** Residue-by-residue listing for refined_11 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 169 PRO 375 - - - - - -68.7 - - - - - 178.7 - 38.5 - * * 170 GLY 376 - - - - - - - - - - - 179.8 - - - 171 SER 377 h B - - -54.4 - - - - - - - 187.3 - 34.3 - * * 172 PRO 378 H - - - - - -61.0 -61.0 -45.6 - - - 182.6 - 38.0 - * * 173 GLU 379 H A - - -63.2 171.9 - -72.4 -30.1 - - - 175.6 - 32.0 - 174 GLU 380 H A - 185.9 - - - -67.8 -46.6 - - - 176.8 - 33.8 - 175 ALA 381 H A - - - - - -57.8 -41.3 - - - 179.5 -2.7 34.1 - 176 ALA 382 H A - - - - - -55.1 -38.4 - - - 181.5 -2.5 33.9 - 177 ALA 383 H A - - - - - -62.5 -50.3 - - - 179.2 -1.2 33.5 - * * 178 LEU 384 H A 46.3 - - 153.5 - -68.2 -44.8 - - - 182.2 -1.3 29.3 - * * * * 179 VAL 385 H A - - -59.9 - - -63.9 -32.3 - - - 174.8 -2.6 29.8 - * * 180 ASP 386 H A - 177.1 - - - -60.7 -42.5 - - - 178.2 -2.0 35.0 - 181 GLY 387 H - - - - - - -74.1 -29.8 - - - 178.9 -1.4 - - 182 LEU 388 H A - - -61.5 175.8 - -68.8 -48.5 - - - 176.8 -2.1 33.8 - 183 ARG 389 h B 44.4 - - - - - - - - - 185.9 -2.9 22.9 - * * * *** *** 184 ARG 390 B - 182.4 - 184.2 - - - - - - 173.3 -1.2 36.0 - * * * 185 GLU 391 t B - - -62.0 185.3 - - - - - - 177.0 - 34.6 - 186 PRO 392 T - - - - - -52.2 - - - - - 183.2 - 38.8 - * * * 187 GLY 393 T - - - - - - - - - - - 180.2 - - - 188 GLY 394 t - - - - - - - - - - - - -3.0 - - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * +* ** * *** *** ** * ** *** *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.6 180.9 -62.7 178.2 -61.6 -65.4 -40.2 - - - 179.5 -2.0 34.3 Standard deviations: 9.4 10.1 10.1 7.2 11.9 9.9 8.4 - - - 2.7 .8 2.2 Numbers of values: 13 52 67 57 18 124 124 0 0 0 186 124 170 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_11 Page 7 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.229 1.494 - 1.463 - 117.11 119.85 - 110.25 - 123.03 * * 2 SER 2 1.302 1.235 1.526 1.529 1.440 121.58 117.21 120.30 110.23 109.19 109.26 122.48 +* +* 3 ASP 3 1.309 1.237 1.527 1.548 1.447 120.79 118.00 120.22 111.30 108.53 111.75 121.75 * * 4 PRO 4 1.344 1.242 1.528 1.530 1.471 122.61 115.99 121.08 110.19 112.67 102.72 122.93 5 GLY 5 1.312 1.243 1.511 - 1.423 120.74 117.73 119.81 - 111.11 - 122.43 * +* +* 6 PRO 6 1.349 1.225 1.536 1.525 1.472 123.81 117.33 120.17 110.25 113.35 102.88 122.50 7 GLU 7 1.337 1.234 1.533 1.536 1.463 121.04 116.30 120.44 110.86 111.30 111.80 123.20 8 ALA 8 1.325 1.230 1.510 1.522 1.451 122.29 115.77 120.83 110.76 109.90 110.67 123.38 9 ALA 9 1.323 1.234 1.524 1.518 1.452 121.98 115.94 121.01 110.94 109.84 110.45 123.03 10 ARG 10 1.333 1.205 1.517 1.522 1.445 121.74 116.75 120.54 108.28 110.34 111.84 122.71 * * 11 LEU 11 1.322 1.222 1.527 1.522 1.416 122.37 116.28 120.59 112.02 110.27 108.85 123.09 ** * ** 12 ARG 12 1.324 1.232 1.533 1.532 1.463 122.18 115.06 121.22 110.84 110.27 110.01 123.68 13 PHE 13 1.315 1.210 1.538 1.533 1.455 123.91 117.06 120.62 110.46 112.75 108.05 122.31 * * * * 14 ARG 14 1.306 1.235 1.532 1.548 1.458 122.04 116.72 120.39 112.13 111.81 110.33 122.86 +* * +* Residue-by-residue listing for refined_11 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.323 1.239 1.537 1.541 1.459 121.78 116.43 120.49 111.12 111.00 110.70 123.08 16 PHE 16 1.331 1.246 1.522 1.538 1.454 122.51 116.06 121.23 110.32 110.29 110.26 122.69 17 HIS 17 1.302 1.234 1.498 1.565 1.435 120.27 117.57 119.88 110.01 107.24 112.26 122.54 +* * +* * * * +* 18 TYR 18 1.293 1.232 1.505 1.530 1.423 118.87 115.21 121.36 112.05 108.93 111.48 123.41 +** +* +* * +** 19 GLU 19 1.288 1.240 1.507 1.537 1.413 121.76 114.21 122.02 112.85 110.70 111.82 123.76 +** ** * +** 20 GLU 20 1.297 1.235 1.534 1.520 1.450 124.31 115.76 120.76 110.36 110.69 107.46 123.47 ** * +* ** 21 ALA 21 1.330 1.233 1.541 1.521 1.458 123.10 117.76 120.21 110.32 113.09 110.10 122.04 22 THR 22 1.329 1.230 1.548 1.583 1.462 120.09 115.42 121.61 111.09 108.81 110.77 122.92 * +* +* 23 GLY 23 1.331 1.233 1.511 - 1.438 121.58 119.23 119.93 - 110.77 - 120.84 * * * 24 PRO 24 1.333 1.225 1.520 1.511 1.450 121.32 116.65 120.35 110.45 113.31 103.25 122.99 * * 25 GLN 25 1.325 1.229 1.538 1.512 1.418 122.12 115.24 121.34 109.07 108.95 108.37 123.37 ** * ** 26 GLU 26 1.321 1.225 1.523 1.535 1.442 122.84 116.61 120.60 113.35 110.69 109.90 122.79 +* +* 27 ALA 27 1.323 1.229 1.530 1.519 1.461 121.66 116.30 120.63 110.51 109.90 110.52 123.05 28 LEU 28 1.334 1.221 1.510 1.525 1.469 122.17 116.04 120.71 108.60 110.94 111.79 123.24 29 ALA 29 1.319 1.237 1.529 1.521 1.456 122.06 115.67 121.05 110.45 110.24 110.02 123.27 30 GLN 30 1.324 1.229 1.518 1.542 1.459 122.33 114.52 121.68 108.19 108.32 110.24 123.79 * * * 31 LEU 31 1.317 1.204 1.505 1.517 1.447 123.74 117.20 119.79 110.76 112.83 110.02 122.99 * * * 32 ARG 32 1.314 1.223 1.523 1.521 1.457 121.80 115.15 121.27 110.62 111.00 110.20 123.56 * * 33 GLU 33 1.297 1.222 1.536 1.514 1.446 123.70 116.61 120.61 110.52 109.94 106.52 122.76 ** * ** ** 34 LEU 34 1.322 1.228 1.530 1.525 1.466 122.03 115.78 120.94 111.50 110.86 110.09 123.26 35 CYS 35 1.322 1.223 1.526 1.538 1.450 123.41 115.76 121.27 110.27 109.52 108.95 122.94 36 ARG 36 1.321 1.207 1.526 1.545 1.417 123.09 117.01 119.95 113.40 110.71 108.46 123.04 * ** +* * ** 37 GLN 37 1.319 1.232 1.517 1.506 1.467 122.50 114.84 121.62 110.65 111.56 109.60 123.54 * * 38 TRP 38 1.298 1.234 1.552 1.540 1.426 123.38 118.04 119.74 114.60 112.57 108.92 122.22 ** * +* ** ** 39 LEU 39 1.336 1.228 1.515 1.537 1.467 120.53 115.84 120.41 109.45 110.31 112.46 123.75 * * 40 ARG 40 1.343 1.228 1.530 1.540 1.454 123.50 117.85 120.52 111.11 112.59 111.68 121.62 * * * 41 PRO 41 1.360 1.235 1.526 1.538 1.484 123.61 115.16 121.32 109.84 112.08 103.58 123.50 * * * * * 42 GLU 42 1.308 1.222 1.530 1.531 1.426 123.34 116.83 120.81 109.50 109.91 108.82 122.32 * +* +* 43 VAL 43 1.329 1.232 1.523 1.560 1.456 120.21 117.82 120.01 109.67 113.01 112.60 122.17 44 ARG 44 1.322 1.237 1.497 1.531 1.450 119.48 114.86 121.16 110.81 111.90 113.62 123.97 * * +* +* 45 SER 45 1.299 1.243 1.526 1.524 1.432 123.33 115.46 120.79 110.25 110.53 108.07 123.74 ** * * ** 46 LYS 46 1.318 1.214 1.516 1.516 1.452 123.61 116.73 120.21 110.80 112.16 109.14 123.01 * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 47 GLU 47 1.328 1.232 1.518 1.513 1.482 121.86 114.95 121.39 109.70 110.89 110.93 123.65 * * 48 GLN 48 1.309 1.221 1.508 1.521 1.457 122.97 116.25 120.54 110.05 112.10 110.54 123.20 * * 49 MET 49 1.309 1.234 1.502 1.504 1.446 121.77 116.18 120.24 111.97 111.02 110.42 123.57 * * * * 50 LEU 50 1.342 1.209 1.507 1.559 1.458 120.98 116.25 120.19 108.69 109.34 113.21 123.46 * * +* +* 51 GLU 51 1.334 1.234 1.531 1.531 1.461 122.12 116.77 120.45 110.56 112.63 111.61 122.77 52 LEU 52 1.317 1.227 1.530 1.526 1.442 121.54 116.54 120.80 111.47 111.20 110.16 122.64 53 LEU 53 1.317 1.238 1.555 1.527 1.430 122.08 117.01 120.57 116.60 111.91 107.82 122.41 * * *** +* *** 54 VAL 54 1.332 1.225 1.540 1.572 1.472 121.73 115.56 120.86 109.88 108.89 111.94 123.55 * * 55 LEU 55 1.334 1.240 1.531 1.562 1.476 123.79 115.16 120.91 111.32 109.64 108.10 123.93 +* * * +* 56 GLU 56 1.324 1.242 1.520 1.527 1.460 123.58 116.76 120.40 110.74 113.13 110.37 122.84 * * 57 GLN 57 1.314 1.238 1.523 1.547 1.449 120.91 115.92 120.28 111.94 109.24 110.27 123.76 * * 58 PHE 58 1.338 1.236 1.519 1.539 1.465 123.23 116.43 120.45 110.24 111.60 110.61 123.12 59 LEU 59 1.323 1.213 1.509 1.534 1.459 121.10 117.80 119.69 113.37 113.91 112.55 122.45 +* * +* 60 GLY 60 1.314 1.233 1.517 - 1.454 119.34 116.24 120.68 - 112.31 - 123.08 * * 61 ALA 61 1.330 1.239 1.523 1.527 1.454 122.13 115.29 121.01 110.96 109.80 110.64 123.69 62 LEU 62 1.324 1.241 1.535 1.526 1.449 123.61 118.24 120.04 107.92 109.77 108.70 121.72 * * * * * 63 PRO 63 1.342 1.237 1.527 1.538 1.443 121.60 117.72 119.15 110.38 109.53 104.91 123.13 +* +* +* 64 PRO 64 1.359 1.223 1.532 1.520 1.474 125.04 116.84 120.04 110.44 115.16 102.56 123.10 * * * 65 GLU 65 1.327 1.224 1.535 1.536 1.464 122.21 117.06 120.24 112.11 112.92 110.32 122.65 * * 66 ILE 66 1.324 1.241 1.542 1.551 1.446 121.73 115.71 121.17 109.77 110.49 110.49 123.10 67 GLN 67 1.322 1.240 1.523 1.522 1.454 122.51 115.91 120.66 110.08 111.30 110.09 123.42 68 ALA 68 1.329 1.235 1.523 1.519 1.463 123.02 116.16 120.82 110.35 111.59 110.29 123.01 69 ARG 69 1.323 1.234 1.516 1.511 1.458 121.95 115.54 121.05 108.66 110.11 110.65 123.41 70 VAL 70 1.328 1.231 1.501 1.534 1.458 122.38 114.62 121.13 106.99 109.89 111.56 124.25 * * 71 GLN 71 1.312 1.222 1.549 1.530 1.449 124.08 115.83 121.18 109.71 109.54 108.63 122.99 * * * * * 72 GLY 72 1.323 1.224 1.532 - 1.445 121.90 118.04 119.87 - 114.14 - 122.09 73 GLN 73 1.336 1.233 1.519 1.525 1.472 120.32 114.86 120.95 108.86 111.09 111.85 124.18 74 ARG 74 1.331 1.227 1.531 1.527 1.469 125.28 117.12 120.97 110.41 112.66 112.70 121.86 +* * +* 75 PRO 75 1.339 1.230 1.542 1.530 1.470 122.54 115.70 121.16 110.11 112.30 102.84 123.13 76 GLY 76 1.327 1.220 1.519 - 1.450 122.10 116.41 120.59 - 112.28 - 122.98 77 SER 77 1.316 1.248 1.539 1.517 1.441 121.90 117.74 120.01 110.90 108.96 108.81 122.25 78 PRO 78 1.352 1.225 1.522 1.536 1.471 123.22 117.11 120.22 110.21 114.34 104.90 122.65 * +* +* 79 GLU 79 1.314 1.227 1.511 1.517 1.457 121.52 116.24 120.41 113.07 111.64 110.80 123.31 * +* +* 80 GLU 80 1.328 1.214 1.525 1.535 1.425 121.80 116.72 120.29 111.45 107.33 109.95 122.95 +* * +* Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 81 ALA 81 1.355 1.223 1.528 1.508 1.452 121.95 116.37 120.33 109.95 110.97 110.29 123.29 +* +* 82 ALA 82 1.336 1.220 1.525 1.528 1.464 122.76 115.78 121.18 110.30 110.94 110.44 123.04 83 ALA 83 1.291 1.235 1.532 1.513 1.443 122.68 117.04 120.07 110.97 111.34 110.43 122.89 +** +** 84 LEU 84 1.344 1.229 1.506 1.543 1.473 121.62 114.66 121.80 105.45 108.09 112.19 123.53 * ** * ** 85 VAL 85 1.319 1.224 1.500 1.537 1.436 122.55 116.49 120.53 112.18 112.10 113.82 122.97 * * * * * 86 ASP 86 1.314 1.229 1.534 1.521 1.455 121.09 116.02 121.24 110.58 110.38 112.08 122.71 * * 87 GLY 87 1.321 1.227 1.521 - 1.449 120.90 115.99 121.19 - 111.67 - 122.82 88 LEU 88 1.321 1.237 1.515 1.519 1.456 122.75 115.98 120.62 110.46 110.14 110.30 123.40 89 ARG 89 1.326 1.231 1.526 1.558 1.456 122.25 115.26 122.06 112.22 108.75 111.63 122.54 * * * 90 ARG 90 1.293 1.239 1.500 1.530 1.421 121.37 115.47 121.01 111.21 109.97 110.03 123.51 +** * +* +** 91 GLU 91 1.287 1.230 1.523 1.525 1.425 122.67 118.56 119.52 111.28 108.01 108.46 121.91 *** +* * * * *** 92 PRO 92 1.346 1.238 1.544 1.535 1.477 123.05 116.87 120.35 110.60 113.70 103.93 122.78 93 GLY 93 1.328 1.240 1.518 - 1.451 120.98 115.90 121.24 - 111.73 - 122.86 94 GLY 94 1.315 1.245 1.505 - 1.440 121.33 - 120.12 - 111.67 - - * * 95 GLY 301 - 1.224 1.490 - 1.446 - 115.44 121.05 - 111.05 - 123.50 * * 96 SER 302 1.292 1.241 1.532 1.528 1.424 122.00 117.08 120.26 111.44 107.88 108.82 122.65 +** +* * +** 97 ASP 303 1.309 1.240 1.542 1.548 1.459 122.04 119.06 119.76 110.67 109.22 110.03 121.18 * * * * 98 PRO 304 1.360 1.232 1.536 1.526 1.466 122.24 117.86 120.17 110.28 114.26 103.22 121.98 * * 99 GLY 305 1.313 1.239 1.518 - 1.437 119.99 118.09 120.04 - 111.98 - 121.87 * * 100 PRO 306 1.347 1.234 1.537 1.530 1.475 123.05 117.18 120.57 109.91 113.34 103.77 122.23 101 GLU 307 1.327 1.242 1.536 1.533 1.459 120.62 116.37 120.75 111.19 111.41 111.88 122.85 102 ALA 308 1.329 1.234 1.510 1.519 1.454 121.80 115.15 121.29 110.58 109.34 110.68 123.55 103 ALA 309 1.314 1.235 1.514 1.504 1.441 122.72 116.17 120.67 110.01 109.89 109.81 123.14 * * 104 ARG 310 1.339 1.208 1.518 1.528 1.453 121.07 116.59 120.57 108.38 109.67 112.61 122.84 * * * 105 LEU 311 1.327 1.216 1.531 1.524 1.414 122.34 116.50 120.35 111.64 110.31 108.95 123.11 ** ** 106 ARG 312 1.325 1.230 1.534 1.526 1.473 122.12 114.98 121.61 109.54 110.56 110.22 123.40 107 PHE 313 1.305 1.217 1.540 1.529 1.446 123.61 116.55 120.98 110.95 112.40 107.50 122.45 +* * +* +* 108 ARG 314 1.304 1.229 1.538 1.552 1.454 122.30 117.24 120.57 112.64 111.96 109.61 122.17 +* * * +* 109 CYS 315 1.315 1.242 1.541 1.540 1.456 120.84 115.96 120.86 111.11 110.53 110.49 123.18 * * 110 PHE 316 1.326 1.244 1.527 1.543 1.455 122.94 116.68 120.83 110.46 110.19 109.51 122.48 111 HIS 317 1.311 1.241 1.505 1.568 1.442 120.67 117.29 119.97 109.55 108.19 112.64 122.74 * +* * * +* 112 TYR 318 1.297 1.233 1.498 1.524 1.428 119.78 115.23 121.20 111.46 109.44 112.47 123.54 ** * +* * * ** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 113 GLU 319 1.286 1.242 1.508 1.533 1.409 121.65 114.82 121.49 113.17 110.92 110.92 123.69 *** +** +* *** 114 GLU 320 1.310 1.215 1.519 1.514 1.451 123.65 115.59 120.74 109.91 110.33 108.97 123.67 * * * 115 ALA 321 1.322 1.229 1.536 1.522 1.451 123.21 117.19 120.32 110.30 112.24 109.80 122.49 116 THR 322 1.329 1.229 1.551 1.580 1.453 120.26 116.45 121.06 111.05 110.10 110.02 122.44 * * * 117 GLY 323 1.326 1.232 1.518 - 1.442 120.67 118.83 119.94 - 111.07 - 121.23 * * * 118 PRO 324 1.342 1.219 1.526 1.511 1.466 122.48 117.85 119.85 110.40 114.53 103.50 122.29 * * 119 GLN 325 1.333 1.233 1.506 1.544 1.465 119.96 115.33 121.24 109.09 109.56 114.11 123.41 ** ** 120 GLU 326 1.315 1.232 1.531 1.532 1.445 121.24 116.20 120.97 112.92 110.58 110.87 122.81 * * 121 ALA 327 1.325 1.228 1.529 1.520 1.454 121.93 116.53 120.51 110.70 110.09 110.50 122.96 122 LEU 328 1.338 1.210 1.498 1.520 1.469 121.92 116.33 120.38 107.74 111.00 112.62 123.29 * * * * * 123 ALA 329 1.316 1.237 1.529 1.512 1.445 121.58 115.66 120.66 111.26 110.44 110.12 123.64 124 GLN 330 1.338 1.228 1.516 1.544 1.470 122.81 114.21 121.80 107.59 107.61 109.95 123.96 * * * 125 LEU 331 1.322 1.202 1.500 1.520 1.443 123.68 116.88 119.90 110.77 112.07 109.97 123.21 * * * * 126 ARG 332 1.310 1.217 1.525 1.526 1.446 122.27 116.23 120.38 111.26 111.20 110.61 123.37 * * 127 GLU 333 1.312 1.232 1.538 1.530 1.460 122.93 116.33 120.86 110.19 110.42 108.16 122.80 * * * 128 LEU 334 1.314 1.231 1.519 1.519 1.457 122.21 116.09 120.69 111.42 111.65 110.03 123.21 * * 129 CYS 335 1.315 1.220 1.534 1.536 1.438 122.90 116.03 121.17 110.84 109.37 108.74 122.75 * * * 130 ARG 336 1.325 1.212 1.530 1.546 1.425 123.33 116.80 120.33 113.42 110.67 108.47 122.85 +* +* * +* 131 GLN 337 1.321 1.241 1.535 1.533 1.477 122.40 114.51 121.81 108.76 109.60 109.73 123.67 * * 132 TRP 338 1.307 1.232 1.557 1.535 1.434 124.73 117.65 119.99 113.81 112.65 107.12 122.36 +* +* * +* +* +* +* 133 LEU 339 1.332 1.230 1.525 1.528 1.475 121.81 115.51 120.59 111.07 110.16 110.80 123.90 134 ARG 340 1.344 1.222 1.538 1.533 1.471 123.99 117.65 120.78 111.64 113.14 109.05 121.57 * * * 135 PRO 341 1.346 1.227 1.527 1.538 1.479 123.41 116.97 120.54 109.78 113.81 103.29 122.49 136 GLU 342 1.312 1.234 1.535 1.532 1.446 120.87 116.67 120.98 110.30 110.22 110.07 122.33 * * 137 VAL 343 1.321 1.238 1.526 1.554 1.460 120.50 117.34 120.48 110.23 113.08 112.65 122.17 138 ARG 344 1.315 1.234 1.509 1.538 1.449 120.43 114.85 121.31 110.52 112.36 113.17 123.84 * +* +* 139 SER 345 1.304 1.245 1.535 1.529 1.431 123.69 115.29 120.80 110.71 110.38 108.21 123.92 +* * * * +* 140 LYS 346 1.326 1.221 1.530 1.530 1.470 125.08 115.78 120.64 109.62 112.67 108.33 123.53 +* * +* 141 GLU 347 1.319 1.239 1.504 1.524 1.482 124.29 113.95 121.56 107.59 111.17 110.21 124.49 * * * * * * 142 GLN 348 1.299 1.224 1.520 1.526 1.465 123.61 116.39 120.44 108.91 111.75 110.38 123.15 ** * ** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 143 MET 349 1.317 1.230 1.504 1.500 1.454 121.97 116.26 120.19 111.87 111.79 110.34 123.53 * * * 144 LEU 350 1.335 1.222 1.518 1.553 1.460 121.47 116.26 120.18 109.14 110.26 113.14 123.52 * +* +* 145 GLU 351 1.335 1.235 1.524 1.527 1.469 122.29 116.46 120.73 109.62 111.99 111.48 122.81 146 LEU 352 1.320 1.229 1.527 1.528 1.439 121.67 116.43 120.84 112.08 110.67 110.26 122.72 * * 147 LEU 353 1.324 1.240 1.546 1.492 1.426 121.78 116.69 120.51 111.61 111.37 107.69 122.80 * +* +* +* +* 148 VAL 354 1.335 1.222 1.526 1.565 1.468 122.08 115.42 120.80 109.84 109.31 111.95 123.75 149 LEU 355 1.327 1.238 1.531 1.559 1.465 123.54 115.40 120.76 111.83 109.71 108.12 123.83 * * * * 150 GLU 356 1.327 1.235 1.522 1.528 1.462 123.26 117.05 120.69 109.93 112.60 110.30 122.26 151 GLN 357 1.318 1.229 1.507 1.540 1.446 119.64 115.66 120.14 111.24 109.28 111.13 124.14 * * 152 PHE 358 1.328 1.236 1.517 1.536 1.454 123.45 116.22 120.60 110.51 111.43 110.32 123.18 153 LEU 359 1.320 1.214 1.508 1.538 1.449 121.18 117.80 119.63 112.93 113.39 112.39 122.52 * * * 154 GLY 360 1.322 1.229 1.507 - 1.447 119.39 116.13 120.58 - 112.14 - 123.29 155 ALA 361 1.324 1.231 1.515 1.522 1.447 122.41 115.71 121.01 110.62 109.66 110.86 123.26 156 LEU 362 1.321 1.244 1.537 1.527 1.445 122.69 118.25 120.02 108.06 109.17 109.14 121.73 * * * 157 PRO 363 1.345 1.242 1.524 1.539 1.459 122.23 118.31 119.41 109.33 109.24 104.12 122.27 * * * 158 PRO 364 1.347 1.226 1.537 1.539 1.478 123.52 116.86 120.72 110.53 113.74 103.93 122.41 159 GLU 365 1.322 1.222 1.543 1.525 1.446 120.91 117.35 120.21 111.05 111.82 110.60 122.40 160 ILE 366 1.339 1.238 1.525 1.552 1.459 121.93 115.12 121.37 109.99 109.73 110.90 123.49 161 GLN 367 1.314 1.239 1.530 1.520 1.444 123.02 115.83 121.13 111.22 110.19 108.80 123.02 * * 162 ALA 368 1.320 1.232 1.524 1.518 1.456 122.11 116.43 120.47 110.25 111.07 110.71 123.08 163 ARG 369 1.332 1.234 1.525 1.528 1.466 121.44 115.37 121.32 109.23 109.10 111.47 123.31 164 VAL 370 1.336 1.218 1.494 1.535 1.461 122.32 114.91 121.04 107.58 109.83 112.01 124.04 * * 165 GLN 371 1.307 1.217 1.536 1.535 1.443 123.21 116.72 120.48 113.65 112.84 111.53 122.79 +* +* +* 166 GLY 372 1.316 1.232 1.535 - 1.439 120.95 117.38 120.43 - 112.51 - 122.19 * * 167 GLN 373 1.331 1.234 1.528 1.519 1.472 120.90 114.91 121.09 108.51 111.14 111.41 123.99 168 ARG 374 1.329 1.226 1.529 1.526 1.471 125.71 117.58 120.51 110.39 113.34 113.12 121.87 ** +* ** 169 PRO 375 1.345 1.223 1.538 1.535 1.465 122.39 116.30 120.88 110.43 111.84 103.69 122.81 170 GLY 376 1.331 1.226 1.518 - 1.454 121.23 116.76 120.67 - 113.01 - 122.57 171 SER 377 1.314 1.244 1.545 1.519 1.448 122.08 118.30 119.63 111.67 109.13 109.12 122.07 * * * 172 PRO 378 1.359 1.233 1.528 1.537 1.479 122.99 116.93 120.46 109.83 114.62 104.35 122.57 * * * * 173 GLU 379 1.312 1.232 1.510 1.529 1.452 121.58 116.03 120.94 112.65 110.66 111.26 123.02 * * * 174 GLU 380 1.319 1.225 1.538 1.529 1.435 120.88 116.44 120.59 111.06 108.44 110.87 122.95 * * 175 ALA 381 1.351 1.234 1.526 1.516 1.460 122.27 115.97 120.53 110.21 111.32 110.23 123.49 +* +* 176 ALA 382 1.335 1.222 1.529 1.532 1.463 122.97 115.77 120.74 110.39 111.43 110.41 123.46 177 ALA 383 1.309 1.243 1.525 1.520 1.457 123.10 117.16 120.17 110.61 111.88 110.58 122.66 * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 178 LEU 384 1.339 1.218 1.499 1.547 1.457 119.71 117.25 119.98 110.31 112.81 116.35 122.74 * * *** *** 179 VAL 385 1.327 1.224 1.518 1.543 1.458 120.55 116.22 120.60 112.13 112.16 114.07 123.17 * +* +* 180 ASP 386 1.319 1.235 1.533 1.538 1.465 122.41 115.81 121.22 110.39 109.46 109.50 122.93 181 GLY 387 1.321 1.229 1.525 - 1.445 120.94 116.25 120.63 - 111.89 - 123.12 182 LEU 388 1.326 1.236 1.515 1.532 1.462 122.79 116.78 120.39 110.20 111.07 110.92 122.83 183 ARG 389 1.327 1.231 1.510 1.547 1.430 119.72 113.78 122.53 117.72 114.03 115.60 123.64 * * * * **** * +** **** 184 ARG 390 1.305 1.230 1.509 1.525 1.431 123.34 116.23 120.77 108.42 111.56 109.66 123.00 +* * +* 185 GLU 391 1.300 1.228 1.523 1.530 1.432 121.67 118.43 119.41 109.85 107.93 111.26 122.08 ** * * * ** 186 PRO 392 1.347 1.240 1.531 1.530 1.473 122.81 115.82 120.94 110.44 111.36 103.19 123.24 187 GLY 393 1.316 1.233 1.511 - 1.438 121.29 116.03 120.99 - 111.07 - 122.98 188 GLY 394 1.316 - 1.496 - 1.428 121.01 - - - 111.52 - - * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** * +* +* +** ** * * **** * *** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 Page 14 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 168 1.286 1.355 1.321 .012 *** +* C-N (Pro) 1.341 .016 18 1.333 1.360 1.348 .007 * C-O C-O 1.231 .020 187 1.202 1.248 1.230 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.494 1.557 1.525 .013 * +* CH2G*-C (Gly) 1.516 .018 18 1.490 1.535 1.514 .012 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.504 1.532 1.519 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.534 1.583 1.556 .016 +* CH1E-CH2E (the rest) 1.530 .020 138 1.492 1.568 1.531 .012 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.409 1.482 1.451 .015 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.423 1.463 1.444 .009 +* N-CH1E (Pro) 1.466 .015 18 1.443 1.484 1.470 .010 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 Page 15 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 113.78 119.06 116.24 .99 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.44 119.23 116.97 1.09 * CH1E-C-N (Pro) 116.9 1.5 18 115.16 118.31 116.86 .80 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.84 124.49 122.99 .64 * O-C-N (Pro) 122.0 1.4 18 121.98 123.50 122.72 .40 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.87 125.71 122.18 1.20 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.34 122.10 120.90 .75 C-N-CH1E (Pro) 122.6 5.0 18 121.32 125.04 122.88 .83 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.15 122.53 120.67 .55 * CH2G*-C-O (Gly) 120.8 2.1 17 119.81 121.24 120.45 .48 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.95 111.26 110.52 .33 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.99 112.18 110.03 1.49 * CH2E-CH1E-C (the rest) 110.1 1.9 138 105.45 117.72 110.70 1.62 ** **** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.24 114.03 110.69 1.42 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.25 114.14 111.79 .87 N-CH1E-C (Pro) 111.8 2.5 18 109.24 115.16 112.95 1.61 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.80 110.86 110.38 .29 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.02 114.07 111.90 1.20 +* N-CH1E-CH2E (Pro) 103.0 1.1 18 102.56 104.91 103.59 .66 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.52 116.35 110.40 1.69 ** *** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_11 Page 16 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 144 94.7% Residues in additional allowed regions [a,b,l,p] 7 4.6% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 94.7 83.8 10.0 1.1 BETTER b. Omega angle st dev 186 2.7 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 124 .8 .8 .2 .2 Inside f. Overall G-factor 188 .3 -.4 .3 2.2 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 13 9.4 18.1 6.5 -1.3 BETTER b. Chi-1 trans st dev 52 10.1 19.0 5.3 -1.7 BETTER c. Chi-1 gauche plus st dev 67 10.1 17.5 4.9 -1.5 BETTER d. Chi-1 pooled st dev 132 10.7 18.2 4.8 -1.5 BETTER e. Chi-2 trans st dev 57 7.2 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 94.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .85 2 Residue-by-residue listing for refined_11 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .18 Chi1-chi2 distribution .01 Chi1 only .09 Chi3 & chi4 .45 Omega .21 ------ .20 ===== Main-chain covalent forces:- Main-chain bond lengths .32 Main-chain bond angles .43 ------ .38 ===== OVERALL AVERAGE .27 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.