Residue-by-residue listing for refined_6 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 ~a - - -58.7 - - - - - - - 166.4 - 34.5 - ** ** ** 3 ASP 3 l - - -61.7 - - - - - - - 173.9 - 32.0 - * * 4 PRO 4 - - - - - -79.3 - - - - - 180.4 - 39.2 - * +* +* 5 GLY 5 h - - - - - - - - - - - 182.5 - - - 6 PRO 6 H - - - - - -66.1 -66.1 -36.5 - - - 177.3 - 38.5 - * * 7 GLU 7 H A - - -89.5 - - -70.2 -37.2 - - - 177.2 - 32.4 - +* +* 8 ALA 8 H A - - - - - -69.1 -43.6 - - - 179.2 - 33.8 - 9 ALA 9 H A - - - - - -66.5 -44.6 - - - 176.7 -3.0 32.6 - * * 10 ARG 10 H A - 175.7 - 170.5 - -63.2 -33.6 - - - 177.9 -3.0 31.7 - * * 11 LEU 11 H A - 175.6 - - - -65.1 -44.0 - - - 177.1 -1.8 34.7 - 12 ARG 12 H A - - -63.7 178.9 - -64.6 -40.4 - - - 177.5 -2.2 34.4 - 13 PHE 13 H A - 173.1 - - - -62.0 -41.9 - - - 176.4 -2.5 34.5 - 14 ARG 14 h A - - -73.5 185.3 - - - - - - 178.9 -2.5 32.5 - 15 CYS 15 T A - 185.5 - - - - - - - - 177.3 - 34.1 - 16 PHE 16 t B - 181.6 - - - - - - - - 177.4 -.7 35.7 - +* +* 17 HIS 17 B 73.5 - - - - - - - - - 175.2 -.6 33.7 - +* +* 18 TYR 18 B - 170.8 - - - - - - - - 179.0 -1.1 31.8 - * * Residue-by-residue listing for refined_6 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 GLU 19 t B 46.9 - - 179.0 - - - - - - 181.5 -.6 33.0 - * +* +* 20 GLU 20 T A - - -58.0 - - - - - - - 180.4 -.6 34.0 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.1 - 33.4 - 22 THR 22 T A - 202.6 - - - - - - - - 181.7 -1.6 34.3 - * * 23 GLY 23 h - - - - - - - - - - - 182.2 -.9 - - +* +* 24 PRO 24 H - - - - - -63.2 -63.2 -32.3 - - - 180.5 - 38.3 - * * 25 GLN 25 H A - - -83.0 - - -70.7 -38.5 - - - 177.7 - 32.8 - * * 26 GLU 26 H A - 180.2 - 166.9 - -69.4 -43.2 - - - 177.1 - 32.4 - 27 ALA 27 H A - - - - - -54.6 -37.2 - - - 177.3 -2.8 34.8 - * * 28 LEU 28 H A - - -65.2 179.5 - -60.3 -38.0 - - - 180.3 -1.7 33.8 - 29 ALA 29 H A - - - - - -62.0 -42.1 - - - 177.3 -.9 33.5 - * * 30 GLN 30 H A - - -75.6 - - -68.6 -49.2 - - - 178.4 -1.4 33.3 - 31 LEU 31 H A - - -72.5 168.2 - -60.4 -43.5 - - - 180.2 -3.1 33.2 - * * 32 ARG 32 H A - 180.8 - 173.3 - -64.7 -37.1 - - - 177.5 -3.4 34.1 - +* +* 33 GLU 33 H A - 175.9 - - - -62.2 -51.2 - - - 181.4 -1.6 34.7 - * * 34 LEU 34 H A - - -64.1 164.9 - -70.5 -38.3 - - - 177.4 -2.6 34.1 - 35 CYS 35 H A - 185.9 - - - -63.2 -38.1 - - - 179.0 -3.3 35.1 - +* +* 36 ARG 36 H A - 186.6 - 193.1 - -65.2 -42.2 - - - 182.7 -2.1 35.0 - 37 GLN 37 H A - - -48.1 - - -61.0 -23.7 - - - 180.1 -1.8 35.4 - * * * 38 TRP 38 H A - 166.6 - - - -87.8 -42.5 - - - 183.4 -.9 34.4 - * +* * +* 39 LEU 39 H A - - -63.2 154.6 - -92.2 -46.8 - - - 180.1 -2.2 34.0 - * ** ** 40 ARG 40 h l - - -70.6 179.4 - - - - - - 176.7 -2.6 27.7 - +* +* 41 PRO 41 T - - - - - -64.4 - - - - - 179.4 - 39.0 - * * 42 GLU 42 T A - 181.6 - 189.1 - - - - - - 184.8 - 36.0 - 43 VAL 43 T A - - -60.5 - - - - - - - 181.0 -.8 33.3 - +* +* 44 ARG 44 t B - - -67.5 177.7 - - - - - - 180.8 -3.4 32.2 - +* +* 45 SER 45 h B - - -58.4 - - - - - - - 189.8 - 32.3 - +* +* 46 LYS 46 H A - - -46.2 177.1 - -61.9 -35.9 - - - 183.0 - 37.7 - * * * 47 GLU 47 H A 71.9 - - - - -60.4 -41.8 - - - 177.8 - 31.1 - 48 GLN 48 H A - - -65.5 - - -76.1 -32.0 - - - 176.7 -.7 31.1 - +* +* 49 MET 49 H A - - -63.7 182.0 - -57.9 -42.0 - - - 176.5 -1.6 33.1 - 50 LEU 50 H A - - -66.1 180.8 - -55.9 -52.1 - - - 182.5 -2.3 33.9 - * * 51 GLU 51 H A - - -64.2 183.7 - -62.0 -40.5 - - - 179.1 -1.3 32.2 - 52 LEU 52 H A - - -57.7 182.0 - -65.2 -36.6 - - - 180.0 -2.5 34.7 - Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 53 LEU 53 H A - 179.5 - - - -75.1 -34.4 - - - 173.9 -2.2 33.5 - * * 54 VAL 54 H A - 176.7 - - - -60.4 -45.0 - - - 178.6 -2.5 34.4 - 55 LEU 55 H A - 180.0 - - - -56.8 -44.5 - - - 181.0 -2.3 36.0 - 56 GLU 56 H A - 183.6 - - - -53.9 -52.9 - - - 181.2 -1.7 34.4 - * * 57 GLN 57 H A - 181.3 - - - -74.5 -41.6 - - - 181.5 -1.8 33.4 - 58 PHE 58 H A - 177.5 - - - -53.8 -44.5 - - - 180.6 -3.2 33.9 - +* +* 59 LEU 59 H A - - -62.3 186.8 - -63.0 -39.8 - - - 179.6 -2.6 31.3 - 60 GLY 60 H - - - - - - -80.9 -13.8 - - - 178.1 -1.1 - - * ** * ** 61 ALA 61 H A - - - - - -77.0 -21.5 - - - 176.7 -1.5 33.5 - +* +* 62 LEU 62 h B - - -64.9 168.2 - - - - - - 175.5 -.9 37.5 - +* * +* 63 PRO 63 h - - - - - -75.1 - - - - - 184.8 - 37.2 - 64 PRO 64 H - - - - - -42.4 -42.4 -51.2 - - - 185.5 - 38.5 - ** +* * * ** 65 GLU 65 H A 64.9 - - - - -71.5 -42.4 - - - 178.2 - 30.9 - 66 ILE 66 H A - - -59.0 181.0 - -65.8 -41.7 - - - 179.6 - 34.0 - 67 GLN 67 H A - 182.1 - 176.2 - -64.5 -40.8 - - - 179.4 -3.3 34.0 - +* +* 68 ALA 68 H A - - - - - -60.2 -36.5 - - - 179.2 -2.5 33.8 - 69 ARG 69 H A - - -63.7 - - -65.9 -43.7 - - - 178.8 -1.6 33.8 - 70 VAL 70 H A - 174.7 - - - -62.9 -50.1 - - - 182.4 -1.6 35.2 - 71 GLN 71 H A - - -97.5 - - -60.8 -29.6 - - - 176.4 -2.7 31.0 - ** ** 72 GLY 72 H - - - - - - -79.6 -14.6 - - - 183.2 -1.5 - - * ** ** 73 GLN 73 H a - 183.3 - 183.4 - -106.5 -47.8 - - - 183.1 -1.4 35.4 - *** *** 74 ARG 74 h l - - -58.2 - - - - - - - 180.9 -3.8 30.8 - ** ** 75 PRO 75 - - - - - -62.4 - - - - - 180.6 - 39.5 - +* +* 76 GLY 76 S - - - - - - - - - - - 177.7 - - - 77 SER 77 h B 56.9 - - - - - - - - - 179.6 - 33.8 - 78 PRO 78 H - - - - - -58.4 -58.4 -41.2 - - - 180.7 - 37.6 - * * 79 GLU 79 H A - - -66.6 172.0 - -67.9 -31.8 - - - 177.4 - 32.8 - 80 GLU 80 H A - 187.5 - - - -72.0 -43.7 - - - 176.4 - 34.8 - 81 ALA 81 H A - - - - - -58.4 -45.5 - - - 178.9 -2.5 34.5 - 82 ALA 82 H A - - - - - -59.3 -33.4 - - - 178.2 -3.0 34.5 - * * 83 ALA 83 H A - - - - - -74.1 -41.5 - - - 180.1 -1.3 33.8 - * * 84 LEU 84 H A - - -43.9 180.6 - -61.8 -50.2 - - - 186.8 -2.3 37.5 - +* * * +* 85 VAL 85 H A - - -58.3 - - -68.3 -32.0 - - - 179.2 -2.9 30.9 - * * 86 ASP 86 H A - 187.0 - - - -64.8 -29.8 - - - 174.3 -1.4 31.0 - 87 GLY 87 H - - - - - - -83.5 -39.0 - - - 180.8 -1.0 - - +* * +* 88 LEU 88 H A - - -60.9 174.7 - -66.0 -39.4 - - - 179.9 -2.3 34.6 - 89 ARG 89 h A 55.9 - - 173.4 - - - - - - 179.9 -3.3 34.6 - +* +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 90 ARG 90 S B - 189.9 - 177.3 - - - - - - 187.3 - 33.7 - * * 91 GLU 91 S l - 184.1 - 190.3 - - - - - - 180.6 -1.0 32.7 - * * 92 PRO 92 - - - - - -77.3 - - - - - 180.1 - 38.6 - * * * 93 GLY 93 - - - - - - - - - - - 179.9 - - - 94 GLY 94 - - - - - - - - - - - - -1.5 - - 95 GLY 301 - - - - - - - - - - - 179.3 - - - 96 SER 302 a - - -55.4 - - - - - - - 180.1 - 34.5 - 97 ASP 303 ~l - - -64.9 - - - - - - - 174.0 - 32.4 - ** * ** 98 PRO 304 S - - - - - -77.5 - - - - - 181.2 - 39.0 - * * * 99 GLY 305 h - - - - - - - - - - - 177.7 - - - 100 PRO 306 H - - - - - -58.7 -58.7 -35.4 - - - 177.2 - 38.6 - * * 101 GLU 307 H A - - -76.1 - - -73.0 -28.0 - - - 177.2 - 32.8 - * * 102 ALA 308 H A - - - - - -73.6 -46.1 - - - 177.2 - 34.4 - 103 ALA 309 H A - - - - - -60.1 -44.0 - - - 176.6 -3.1 34.3 - * * 104 ARG 310 H A - 169.3 - 161.1 - -64.7 -33.5 - - - 177.6 -2.5 31.4 - 105 LEU 311 H A - 172.2 - - - -67.8 -46.5 - - - 176.9 -1.5 34.1 - 106 ARG 312 H A - - -62.9 177.7 - -61.4 -32.8 - - - 179.0 -2.8 34.8 - * * 107 PHE 313 H A - 176.1 - - - -70.0 -48.5 - - - 177.6 -1.9 34.4 - 108 ARG 314 H A - - -75.0 184.7 - -75.7 -29.6 - - - 180.6 -2.8 32.3 - 109 CYS 315 h A - 184.1 - - - - - - - - 178.3 -2.8 33.8 - * * 110 PHE 316 B - 182.3 - - - - - - - - 178.0 - 35.1 - 111 HIS 317 B 71.1 - - - - - - - - - 175.4 - 34.0 - 112 TYR 318 B - 168.9 - - - - - - - - 180.0 -1.2 32.7 - * * 113 GLU 319 t B 52.6 - - 182.9 - - - - - - 181.4 -.6 32.2 - +* +* 114 GLU 320 T A - - -64.6 172.5 - - - - - - 179.6 -.5 35.3 - ** ** 115 ALA 321 T A - - - - - - - - - - 180.5 - 34.1 - 116 THR 322 T A - 200.2 - - - - - - - - 179.7 -1.0 33.5 - * * 117 GLY 323 h - - - - - - - - - - - 182.4 -1.0 - - * * 118 PRO 324 H - - - - - -60.3 -60.3 -31.1 - - - 179.6 - 38.0 - * * 119 GLN 325 H A - - -86.0 - - -69.8 -45.2 - - - 178.6 - 32.2 - * * 120 GLU 326 H A - 182.0 - 169.9 - -71.4 -33.1 - - - 174.0 - 32.0 - * * 121 ALA 327 H A - - - - - -62.3 -39.3 - - - 173.9 -2.8 33.6 - * * * 122 LEU 328 H A - - -68.2 179.5 - -58.5 -43.5 - - - 179.3 -2.1 34.5 - 123 ALA 329 H A - - - - - -58.9 -38.5 - - - 178.9 -1.6 33.4 - 124 GLN 330 H A - - -49.6 - - -67.1 -51.1 - - - 179.3 -1.8 35.4 - * * * 125 LEU 331 H A - - -70.5 168.6 - -60.2 -40.8 - - - 179.1 -2.9 34.2 - * * Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 126 ARG 332 H A - 182.9 - 175.6 - -62.6 -44.3 - - - 177.1 -3.6 34.9 - ** ** 127 GLU 333 H A - 177.5 - 176.9 - -61.3 -47.9 - - - 178.3 -2.1 35.0 - 128 LEU 334 H A - - -62.2 174.2 - -63.1 -47.9 - - - 177.3 -2.7 34.2 - 129 CYS 335 H A - 181.1 - - - -58.7 -43.9 - - - 179.4 -3.7 34.5 - ** ** 130 ARG 336 H A - 170.4 - - - -65.9 -36.3 - - - 176.7 -3.0 30.4 - * * * 131 GLN 337 H A - - -68.5 178.4 - -73.7 -19.4 - - - 177.5 -2.2 33.1 - +* +* 132 TRP 338 H A - 164.4 - - - -81.0 -55.2 - - - 181.7 -1.2 32.8 - * * * * * 133 LEU 339 H A - - -55.1 - - -87.0 -43.5 - - - 182.7 -3.0 31.2 - +* * +* 134 ARG 340 h l - - -74.0 179.3 - - - - - - 174.5 -1.4 28.4 - +* +* 135 PRO 341 T - - - - - -49.4 - - - - - 178.5 - 40.0 - * +* +* 136 GLU 342 T A - 176.8 - 178.4 - - - - - - 181.3 - 35.1 - 137 VAL 343 T A - - -59.3 - - - - - - - 181.4 -1.8 32.5 - 138 ARG 344 t B - - -72.0 183.9 - - - - - - 178.3 -3.6 32.1 - ** ** 139 SER 345 h B - - -55.8 - - - - - - - 188.1 - 34.5 - * * 140 LYS 346 H A - - -51.4 177.9 - -65.5 -45.9 - - - 183.5 - 35.8 - * * 141 GLU 347 H A 53.6 - - - - -62.1 -29.3 - - - 177.7 - 30.6 - 142 GLN 348 H A - - -60.0 - - -67.0 -34.5 - - - 180.9 - 35.0 - 143 MET 349 H A - - -55.8 183.0 - -69.1 -35.9 - - - 174.8 -1.0 33.6 - * * 144 LEU 350 H A - - -77.6 - - -54.7 -52.5 - - - 181.5 -1.4 34.5 - * * 145 GLU 351 H A - - -63.3 181.8 - -60.7 -40.7 - - - 179.5 -1.6 33.0 - 146 LEU 352 H A - - -59.0 181.5 - -63.8 -44.3 - - - 181.0 -1.9 34.2 - 147 LEU 353 H A - 177.8 - - - -75.6 -30.5 - - - 174.0 -2.7 32.1 - * * 148 VAL 354 H A - 174.8 - - - -58.7 -38.9 - - - 179.3 -2.8 33.5 - * * 149 LEU 355 H A - 181.3 - - - -57.5 -43.6 - - - 181.6 -1.6 35.3 - 150 GLU 356 H A - - -109.0 - - -54.5 -53.0 - - - 179.6 -.9 33.2 - +** * * +** 151 GLN 357 H A - 182.0 - - - -75.2 -35.5 - - - 177.9 -1.4 31.8 - 152 PHE 358 H A - 174.6 - - - -56.4 -45.2 - - - 180.7 -2.7 33.6 - 153 LEU 359 H A - - -58.8 185.8 - -68.7 -37.1 - - - 179.1 -3.0 31.7 - * * 154 GLY 360 H - - - - - - -76.4 -22.5 - - - 177.0 -1.6 - - * * 155 ALA 361 H A - - - - - -71.1 -28.8 - - - 176.4 -2.2 33.2 - 156 LEU 362 h b - - -66.1 172.9 - - - - - - 175.7 -1.1 37.2 - * * 157 PRO 363 h - - - - - -76.1 - - - - - 185.5 - 37.5 - * * 158 PRO 364 H - - - - - -48.5 -48.5 -48.2 - - - 185.5 - 37.8 - +* * * +* 159 GLU 365 H A 69.1 - - - - -71.2 -47.0 - - - 178.6 - 30.8 - 160 ILE 366 H A - - -60.4 181.1 - -62.4 -45.9 - - - 180.0 - 34.4 - Residue-by-residue listing for refined_6 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 161 GLN 367 H A - 178.4 - 180.3 - -58.5 -44.2 - - - 181.5 -3.2 34.4 - +* +* 162 ALA 368 H A - - - - - -60.3 -43.7 - - - 181.1 -2.2 33.8 - 163 ARG 369 H A - - -59.3 - - -61.5 -42.9 - - - 177.2 -1.9 33.1 - 164 VAL 370 H A - 177.0 - - - -69.5 -34.6 - - - 185.9 -1.9 36.3 - * * 165 GLN 371 H A - 203.5 - - - -64.1 -32.6 - - - 178.6 -2.4 35.2 - * * 166 GLY 372 H - - - - - - -77.2 -22.0 - - - 181.0 -1.7 - - * +* +* 167 GLN 373 H a - 180.4 - 179.9 - -91.4 -50.5 - - - 185.3 -.8 35.2 - ** +* ** 168 ARG 374 h l - - -62.1 - - - - - - - 181.3 -3.6 30.2 - ** * ** 169 PRO 375 - - - - - -61.6 - - - - - 177.4 - 39.4 - +* +* 170 GLY 376 S - - - - - - - - - - - 178.6 - - - 171 SER 377 h B 51.2 - - - - - - - - - 181.5 - 33.5 - 172 PRO 378 H - - - - - -55.2 -55.2 -43.3 - - - 182.1 - 37.7 - * * 173 GLU 379 H A - - -63.8 174.6 - -68.3 -30.3 - - - 177.4 - 32.8 - 174 GLU 380 H A - 185.4 - - - -70.8 -46.1 - - - 176.0 - 35.0 - 175 ALA 381 H A - - - - - -58.9 -42.5 - - - 178.4 -2.3 34.3 - 176 ALA 382 H A - - - - - -58.9 -36.8 - - - 178.5 -2.9 34.4 - * * 177 ALA 383 H A - - - - - -74.4 -29.9 - - - 179.0 -1.5 33.7 - 178 LEU 384 H A - - -43.3 177.9 - -71.4 -48.9 - - - 184.1 -1.6 36.3 - +* +* 179 VAL 385 H A - - -56.3 - - -69.9 -31.0 - - - 176.2 -2.9 31.1 - * * 180 ASP 386 H A - 179.5 - - - -49.6 -38.2 - - - 176.9 -1.7 34.7 - * * 181 GLY 387 H - - - - - - -84.8 -45.2 - - - 183.6 -.9 - - +* +* +* 182 LEU 388 H A - - -61.0 175.4 - -62.7 -29.7 - - - 179.3 -2.0 34.0 - 183 ARG 389 h A 60.2 - - 176.8 - - - - - - 183.4 -3.0 34.8 - * * 184 ARG 390 t b - 188.8 - 177.6 - - - - - - 185.8 -1.2 35.0 - * * 185 GLU 391 l - 179.2 - 181.5 - - - - - - 178.1 -1.1 31.0 - * * 186 PRO 392 - - - - - -80.8 - - - - - 179.6 - 38.8 - * * * 187 GLY 393 - - - - - - - - - - - 181.8 - - - 188 GLY 394 - - - - - - - - - - - - -1.8 - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +** * ** *** ** ** ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.7 180.4 -64.5 177.7 -64.3 -66.2 -39.6 - - - 179.4 -2.0 34.1 Standard deviations: 9.1 7.7 11.2 6.8 11.5 9.2 8.0 - - - 3.0 .8 2.2 Numbers of values: 12 54 66 60 18 123 123 0 0 0 186 125 170 0 Residue-by-residue listing for refined_6 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_6 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 - 1.228 1.510 - 1.465 - 115.37 121.27 - 111.76 - 123.36 2 SER 2 1.303 1.227 1.510 1.544 1.456 125.08 113.26 121.97 110.91 105.01 111.20 124.75 +* +* * ** * ** 3 ASP 3 1.339 1.238 1.520 1.545 1.460 124.79 116.97 121.24 111.41 114.83 110.93 121.77 +* * +* 4 PRO 4 1.347 1.222 1.528 1.547 1.458 122.62 115.66 121.06 109.73 110.36 103.85 123.28 5 GLY 5 1.321 1.229 1.513 - 1.436 121.90 119.35 119.33 - 110.78 - 121.32 * * * 6 PRO 6 1.348 1.227 1.534 1.535 1.473 122.35 116.83 120.57 110.33 112.48 103.60 122.56 7 GLU 7 1.319 1.221 1.505 1.535 1.453 121.83 116.13 120.39 112.16 110.85 111.15 123.46 * * 8 ALA 8 1.317 1.232 1.527 1.522 1.446 121.97 116.32 120.85 110.83 110.22 110.60 122.82 9 ALA 9 1.331 1.233 1.520 1.517 1.454 121.50 116.91 120.27 111.20 110.95 111.56 122.81 10 ARG 10 1.338 1.226 1.530 1.544 1.454 121.07 116.35 120.80 111.59 110.84 112.63 122.83 * * 11 LEU 11 1.328 1.202 1.527 1.521 1.413 122.83 117.02 119.98 111.47 109.93 108.93 122.98 * ** ** 12 ARG 12 1.335 1.233 1.518 1.520 1.476 122.28 114.98 121.34 109.44 110.56 110.80 123.68 13 PHE 13 1.308 1.223 1.538 1.531 1.450 123.99 116.46 121.07 112.95 110.62 107.32 122.45 +* * * +* +* 14 ARG 14 1.317 1.225 1.525 1.523 1.454 121.66 116.43 120.63 110.25 112.43 112.05 122.94 Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.313 1.228 1.519 1.542 1.454 122.32 115.43 121.67 110.91 108.94 110.68 122.87 * * 16 PHE 16 1.309 1.239 1.521 1.533 1.427 122.21 117.03 120.44 109.98 108.53 109.46 122.52 * +* +* 17 HIS 17 1.311 1.241 1.501 1.569 1.447 120.07 117.61 119.76 109.88 107.89 112.97 122.61 * * +* * * +* 18 TYR 18 1.298 1.233 1.503 1.528 1.428 118.80 114.54 121.53 112.15 109.38 112.64 123.85 ** * +* +* * * ** 19 GLU 19 1.285 1.237 1.507 1.542 1.415 123.37 115.10 121.33 112.78 109.13 110.60 123.52 *** ** * *** 20 GLU 20 1.310 1.225 1.512 1.539 1.447 123.49 115.38 120.58 109.31 111.20 111.73 124.02 * * 21 ALA 21 1.313 1.222 1.536 1.518 1.458 123.41 118.21 119.93 110.38 113.12 110.38 121.86 * * * 22 THR 22 1.330 1.223 1.534 1.576 1.454 119.27 115.60 121.46 110.47 108.50 111.28 122.87 * * * 23 GLY 23 1.328 1.236 1.512 - 1.435 121.46 118.67 120.18 - 111.24 - 121.14 * * * * 24 PRO 24 1.338 1.221 1.531 1.512 1.462 122.19 117.54 120.12 110.27 113.74 103.47 122.33 25 GLN 25 1.340 1.230 1.499 1.543 1.464 120.29 115.17 121.35 109.05 109.61 114.23 123.48 * ** ** 26 GLU 26 1.309 1.220 1.521 1.522 1.440 121.08 116.45 120.42 112.19 110.48 111.18 123.11 * * * 27 ALA 27 1.328 1.228 1.522 1.518 1.470 122.79 115.99 120.52 110.07 110.52 109.64 123.48 28 LEU 28 1.324 1.205 1.505 1.518 1.455 122.40 117.47 119.60 108.76 112.02 112.03 122.93 * * 29 ALA 29 1.324 1.228 1.522 1.524 1.462 121.21 115.20 121.23 110.91 109.87 110.92 123.54 30 GLN 30 1.320 1.227 1.531 1.554 1.459 122.90 116.43 120.76 111.11 110.83 110.99 122.79 * * 31 LEU 31 1.322 1.203 1.511 1.525 1.462 122.14 116.73 120.40 110.75 111.91 110.89 122.85 * * 32 ARG 32 1.308 1.229 1.510 1.516 1.452 122.48 115.38 120.83 110.95 110.78 109.78 123.79 +* +* 33 GLU 33 1.307 1.224 1.518 1.553 1.442 123.20 115.59 120.60 113.57 109.70 107.05 123.55 +* * +* ** ** 34 LEU 34 1.299 1.232 1.520 1.504 1.449 123.36 116.24 120.52 112.17 112.37 107.91 123.23 ** * * +* ** 35 CYS 35 1.316 1.234 1.521 1.538 1.447 122.52 116.02 121.08 110.00 108.91 110.01 122.89 36 ARG 36 1.336 1.184 1.508 1.490 1.405 122.11 117.42 119.45 109.16 110.88 110.31 123.09 ** +* +** +** 37 GLN 37 1.332 1.236 1.535 1.537 1.494 122.58 114.24 122.00 108.86 110.36 109.90 123.76 +* +* 38 TRP 38 1.296 1.231 1.556 1.538 1.427 124.58 117.32 120.62 113.28 112.13 106.73 122.04 ** * +* +* +* ** ** 39 LEU 39 1.314 1.220 1.535 1.526 1.469 121.54 116.14 120.23 111.61 111.83 108.84 123.60 * * 40 ARG 40 1.335 1.216 1.515 1.522 1.466 124.92 117.23 120.72 112.72 117.00 113.42 122.04 +* * ** +* ** 41 PRO 41 1.350 1.227 1.535 1.539 1.477 123.06 115.57 121.14 110.09 111.78 103.25 123.29 42 GLU 42 1.325 1.234 1.527 1.531 1.452 122.64 116.31 120.99 108.39 110.55 109.69 122.69 43 VAL 43 1.321 1.227 1.517 1.560 1.454 120.88 116.84 120.62 109.75 112.00 112.16 122.53 44 ARG 44 1.311 1.235 1.488 1.534 1.433 120.95 114.38 121.89 111.05 111.26 112.60 123.72 * +* * * +* 45 SER 45 1.267 1.250 1.520 1.516 1.393 123.26 114.48 121.38 113.99 110.74 109.66 124.14 **** *** ** **** Residue-by-residue listing for refined_6 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 1.288 1.235 1.530 1.503 1.444 125.05 115.87 121.00 108.07 111.90 107.00 123.13 +** * +* * ** +** 47 GLU 47 1.322 1.238 1.528 1.556 1.462 121.76 117.14 120.30 111.46 111.90 113.28 122.56 * +* +* 48 GLN 48 1.328 1.229 1.509 1.533 1.438 120.43 116.70 120.11 112.30 111.32 112.68 123.17 * * * * 49 MET 49 1.337 1.230 1.505 1.509 1.461 121.40 116.12 120.22 110.49 111.30 111.37 123.64 * * 50 LEU 50 1.338 1.213 1.524 1.544 1.454 121.63 116.66 120.52 109.20 110.62 112.07 122.77 51 GLU 51 1.331 1.238 1.527 1.527 1.467 121.78 116.79 120.35 110.76 112.91 111.81 122.86 52 LEU 52 1.320 1.235 1.527 1.530 1.449 121.56 115.29 121.60 110.14 110.00 110.02 123.08 53 LEU 53 1.312 1.241 1.539 1.511 1.424 122.57 116.76 120.51 113.62 111.59 107.72 122.73 * +* +* +* +* 54 VAL 54 1.328 1.229 1.525 1.560 1.461 121.41 115.13 121.04 109.02 108.87 112.27 123.79 55 LEU 55 1.328 1.231 1.518 1.528 1.459 123.68 115.51 120.61 109.21 110.38 108.87 123.87 * * 56 GLU 56 1.325 1.236 1.542 1.550 1.461 122.94 116.68 120.66 110.11 111.19 110.26 122.64 * * 57 GLN 57 1.324 1.227 1.515 1.522 1.457 121.10 116.37 120.18 110.10 111.47 111.37 123.44 58 PHE 58 1.336 1.236 1.508 1.540 1.462 122.21 115.90 120.82 109.83 111.04 111.32 123.27 59 LEU 59 1.314 1.223 1.522 1.528 1.438 120.88 117.24 120.07 112.49 112.96 111.39 122.67 * * * * 60 GLY 60 1.316 1.235 1.515 - 1.454 119.99 116.63 120.36 - 113.03 - 123.00 61 ALA 61 1.327 1.230 1.527 1.529 1.458 121.92 115.38 121.21 111.04 110.09 110.81 123.41 62 LEU 62 1.317 1.246 1.534 1.518 1.454 123.53 118.50 120.01 108.12 109.91 107.78 121.50 * * * +* +* 63 PRO 63 1.346 1.246 1.545 1.539 1.445 121.51 117.64 119.89 111.48 110.15 105.01 122.47 * +* +* 64 PRO 64 1.355 1.229 1.534 1.518 1.477 124.33 117.69 119.81 110.07 115.66 102.97 122.47 +* +* 65 GLU 65 1.329 1.238 1.524 1.564 1.463 120.90 116.99 120.38 111.59 111.63 113.62 122.61 +* +* +* 66 ILE 66 1.330 1.242 1.533 1.545 1.448 120.87 115.72 121.22 110.12 109.92 111.22 123.03 67 GLN 67 1.322 1.239 1.531 1.527 1.447 122.20 116.21 120.90 110.71 110.55 110.34 122.88 68 ALA 68 1.322 1.233 1.527 1.519 1.461 122.27 116.21 120.77 110.23 111.31 110.67 123.01 69 ARG 69 1.326 1.230 1.523 1.523 1.461 121.51 116.21 120.71 109.31 111.03 111.75 123.07 70 VAL 70 1.328 1.217 1.511 1.534 1.459 121.61 115.97 120.71 106.94 110.70 112.31 123.32 71 GLN 71 1.313 1.226 1.526 1.538 1.454 122.36 116.65 120.44 112.73 112.87 111.57 122.91 * * * 72 GLY 72 1.319 1.233 1.532 - 1.447 120.39 116.91 120.63 - 112.57 - 122.45 73 GLN 73 1.326 1.230 1.533 1.521 1.457 121.79 115.23 121.01 108.86 111.57 109.71 123.76 74 ARG 74 1.325 1.223 1.541 1.529 1.465 125.17 116.70 121.16 111.81 111.98 112.89 122.06 +* * +* 75 PRO 75 1.353 1.224 1.532 1.531 1.487 123.77 116.11 121.03 108.90 114.00 103.22 122.86 * * 76 GLY 76 1.308 1.226 1.526 - 1.447 121.04 117.69 120.35 - 113.62 - 121.96 +* +* 77 SER 77 1.311 1.248 1.530 1.539 1.452 121.19 118.21 119.75 111.22 109.94 110.35 122.01 * * * 78 PRO 78 1.364 1.222 1.522 1.540 1.467 122.74 116.64 120.51 110.81 112.66 104.57 122.84 * * * 79 GLU 79 1.316 1.231 1.516 1.512 1.459 121.92 116.70 120.35 111.89 112.21 110.03 122.93 80 GLU 80 1.317 1.214 1.526 1.526 1.425 121.56 115.99 120.83 111.47 107.45 109.41 123.12 +* * +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 81 ALA 81 1.343 1.221 1.525 1.512 1.455 122.25 115.76 120.82 109.91 110.56 110.17 123.40 * * 82 ALA 82 1.329 1.222 1.532 1.523 1.460 123.40 115.55 121.45 110.62 111.04 109.41 123.00 83 ALA 83 1.290 1.240 1.523 1.520 1.445 122.80 116.67 120.10 110.44 110.67 110.72 123.23 +** +** 84 LEU 84 1.345 1.233 1.512 1.553 1.469 121.43 114.44 121.92 104.82 108.13 111.70 123.53 * * +** * +** 85 VAL 85 1.322 1.207 1.497 1.537 1.438 122.63 117.32 119.65 111.15 113.20 113.30 123.02 * * * * * 86 ASP 86 1.319 1.237 1.537 1.520 1.463 121.27 115.95 121.47 112.31 111.05 112.52 122.58 * * * 87 GLY 87 1.316 1.237 1.533 - 1.447 120.33 115.82 120.83 - 111.12 - 123.34 88 LEU 88 1.336 1.226 1.531 1.531 1.478 123.53 116.24 120.65 109.23 112.36 110.19 123.11 * * * 89 ARG 89 1.333 1.239 1.519 1.530 1.473 123.05 116.09 120.83 108.92 111.61 110.78 123.08 90 ARG 90 1.314 1.234 1.507 1.526 1.422 121.41 114.77 120.54 112.23 107.28 110.47 124.64 * +* * * * +* 91 GLU 91 1.325 1.240 1.543 1.537 1.458 124.52 117.75 120.87 110.41 109.33 112.84 121.28 +* * * +* 92 PRO 92 1.346 1.241 1.532 1.532 1.465 122.07 116.01 121.14 110.64 112.14 103.27 122.84 93 GLY 93 1.323 1.232 1.511 - 1.441 121.49 115.94 120.82 - 111.70 - 123.24 94 GLY 94 1.307 1.247 1.511 - 1.441 121.48 - 119.67 - 111.33 - - +* +* 95 GLY 301 - 1.231 1.500 - 1.447 - 115.49 121.24 - 111.23 - 123.27 96 SER 302 1.308 1.238 1.534 1.531 1.435 121.84 115.64 120.53 110.92 109.58 109.79 123.80 * * * 97 ASP 303 1.336 1.230 1.509 1.544 1.483 124.72 117.89 120.59 108.27 113.22 113.99 121.50 * +* ** ** 98 PRO 304 1.340 1.241 1.536 1.533 1.468 121.86 114.22 122.10 110.62 109.40 103.11 123.69 +* * +* 99 GLY 305 1.320 1.224 1.504 - 1.413 122.91 119.13 119.25 - 110.24 - 121.58 ** * * ** 100 PRO 306 1.344 1.226 1.531 1.531 1.475 122.42 116.06 121.03 110.54 111.09 103.41 122.87 101 GLU 307 1.322 1.224 1.512 1.538 1.452 122.14 116.01 120.64 111.30 110.66 111.59 123.33 102 ALA 308 1.322 1.225 1.515 1.516 1.451 122.25 115.72 120.90 110.28 109.23 110.40 123.37 103 ALA 309 1.328 1.224 1.520 1.520 1.452 122.34 115.55 121.04 110.68 109.39 110.23 123.38 104 ARG 310 1.325 1.234 1.534 1.528 1.440 122.54 117.12 120.49 112.78 112.52 111.05 122.38 * * 105 LEU 311 1.324 1.215 1.523 1.526 1.418 122.00 116.20 120.58 111.96 109.37 109.44 123.17 ** ** 106 ARG 312 1.325 1.233 1.530 1.532 1.468 122.76 114.75 121.46 109.89 110.29 109.89 123.79 107 PHE 313 1.307 1.220 1.538 1.522 1.443 124.48 117.45 120.37 112.53 111.70 107.51 122.18 +* +* * +* +* 108 ARG 314 1.322 1.227 1.522 1.521 1.468 120.63 116.96 120.40 109.18 112.81 113.12 122.63 +* +* 109 CYS 315 1.319 1.235 1.530 1.544 1.462 121.85 115.75 121.07 111.17 110.17 110.28 123.17 110 PHE 316 1.323 1.238 1.519 1.538 1.439 122.69 116.38 120.84 110.22 109.32 109.84 122.76 * * 111 HIS 317 1.304 1.237 1.507 1.564 1.440 120.68 117.56 119.88 110.14 108.23 112.23 122.54 +* +* * * +* 112 TYR 318 1.299 1.229 1.511 1.533 1.433 119.51 115.14 121.27 112.03 109.39 111.51 123.58 ** * * * ** 113 GLU 319 1.295 1.237 1.509 1.546 1.421 122.39 114.83 121.59 113.10 110.04 111.07 123.57 ** +* +* ** Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 114 GLU 320 1.299 1.237 1.520 1.505 1.449 123.98 115.25 120.97 110.13 111.31 108.58 123.78 ** * * * ** 115 ALA 321 1.319 1.228 1.526 1.509 1.447 123.29 117.38 120.17 110.26 112.15 109.90 122.44 116 THR 322 1.328 1.225 1.549 1.586 1.446 119.62 115.79 121.19 111.62 108.64 111.25 122.96 * +* * * +* 117 GLY 323 1.340 1.221 1.511 - 1.457 121.69 119.67 119.40 - 111.05 - 120.93 +* * +* 118 PRO 324 1.353 1.219 1.533 1.514 1.467 121.99 117.79 119.95 110.27 114.07 103.77 122.25 119 GLN 325 1.340 1.229 1.510 1.543 1.465 119.91 115.63 121.22 109.82 110.15 113.94 123.13 ** ** 120 GLU 326 1.307 1.233 1.536 1.523 1.441 121.63 116.47 120.80 113.30 110.61 110.47 122.71 +* +* +* 121 ALA 327 1.326 1.234 1.525 1.523 1.464 121.93 116.29 120.50 110.66 109.68 111.05 123.21 122 LEU 328 1.342 1.191 1.482 1.521 1.461 121.56 116.43 120.05 107.34 109.98 113.14 123.53 +* ** * +* ** 123 ALA 329 1.320 1.226 1.527 1.519 1.450 121.87 116.45 120.52 111.05 110.65 110.74 123.00 124 GLN 330 1.335 1.229 1.530 1.553 1.463 121.37 115.45 120.95 107.55 108.13 112.17 123.59 * * * * 125 LEU 331 1.334 1.200 1.505 1.527 1.469 123.51 116.35 120.37 109.82 111.98 110.45 123.28 +* * +* 126 ARG 332 1.306 1.219 1.500 1.524 1.450 123.32 115.11 121.01 110.54 109.57 109.54 123.87 +* * +* 127 GLU 333 1.302 1.233 1.534 1.516 1.431 123.31 115.99 120.67 111.69 110.37 107.86 123.33 +* * +* +* 128 LEU 334 1.322 1.219 1.523 1.531 1.459 122.73 116.03 120.54 110.63 110.71 109.99 123.43 129 CYS 335 1.321 1.225 1.531 1.537 1.444 123.37 116.99 120.84 110.89 110.37 109.56 122.15 130 ARG 336 1.319 1.203 1.515 1.538 1.422 121.36 117.42 119.55 114.55 112.00 111.15 123.01 * +* ** ** 131 GLN 337 1.323 1.225 1.517 1.495 1.459 121.52 114.79 121.47 111.21 111.71 110.32 123.75 +* +* 132 TRP 338 1.303 1.232 1.536 1.548 1.431 123.82 118.38 119.78 113.35 111.95 109.10 121.84 +* * * * +* +* 133 LEU 339 1.333 1.224 1.517 1.561 1.462 118.96 116.62 119.81 109.95 111.60 114.76 123.55 +* +* +** +** 134 ARG 340 1.335 1.224 1.529 1.548 1.464 123.03 117.17 120.79 112.53 114.89 114.04 122.01 * * ** ** 135 PRO 341 1.363 1.232 1.523 1.524 1.484 124.00 114.73 121.23 108.98 112.56 102.55 124.04 * * * * * 136 GLU 342 1.314 1.234 1.535 1.528 1.444 124.14 116.85 120.63 110.91 111.36 108.24 122.51 * * * * 137 VAL 343 1.326 1.238 1.531 1.559 1.454 120.54 117.37 120.39 110.00 112.28 112.71 122.24 138 ARG 344 1.323 1.231 1.503 1.524 1.454 120.62 114.55 121.64 109.60 113.18 113.14 123.80 * +* +* 139 SER 345 1.299 1.240 1.533 1.519 1.431 123.47 116.08 120.56 112.03 109.61 108.53 123.36 ** * * * ** 140 LYS 346 1.310 1.213 1.508 1.502 1.460 123.41 116.17 120.65 109.32 112.06 108.49 123.13 * * * * 141 GLU 347 1.313 1.233 1.513 1.545 1.466 122.21 115.93 120.58 110.90 112.41 114.14 123.48 * ** ** 142 GLN 348 1.319 1.229 1.525 1.531 1.450 121.89 115.44 121.38 109.60 109.43 110.28 123.16 143 MET 349 1.327 1.229 1.502 1.508 1.448 122.50 115.63 120.47 110.99 110.76 110.42 123.89 * * * 144 LEU 350 1.335 1.206 1.505 1.558 1.463 122.34 116.28 120.41 109.06 109.61 111.92 123.23 * * * 145 GLU 351 1.326 1.235 1.521 1.524 1.457 121.94 116.43 120.58 110.85 112.05 110.99 122.97 Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 146 LEU 352 1.316 1.230 1.527 1.527 1.436 121.52 116.16 120.46 110.30 110.82 110.40 123.37 * * 147 LEU 353 1.322 1.235 1.554 1.526 1.432 122.63 117.74 120.22 115.11 112.86 107.68 122.02 * * +** +* +** 148 VAL 354 1.335 1.236 1.529 1.570 1.478 121.13 115.59 120.87 109.36 109.59 112.89 123.51 * * * 149 LEU 355 1.335 1.225 1.524 1.534 1.457 122.79 115.44 120.86 108.82 110.53 110.34 123.70 150 GLU 356 1.318 1.246 1.521 1.530 1.458 123.31 116.90 120.22 111.48 113.26 109.72 122.87 151 GLN 357 1.312 1.214 1.508 1.514 1.442 120.16 116.88 120.06 111.55 111.35 112.29 123.06 * * * 152 PHE 358 1.329 1.233 1.516 1.541 1.457 121.13 115.85 120.91 110.28 110.46 111.46 123.22 153 LEU 359 1.319 1.211 1.509 1.530 1.435 120.89 117.15 120.06 111.88 111.76 112.01 122.77 * * 154 GLY 360 1.317 1.231 1.515 - 1.449 119.65 116.39 120.57 - 112.42 - 123.04 155 ALA 361 1.325 1.238 1.526 1.539 1.449 122.00 115.64 120.57 111.34 109.77 111.18 123.79 156 LEU 362 1.334 1.241 1.536 1.529 1.459 123.98 118.21 120.41 107.61 110.44 108.71 121.39 * * * * * * 157 PRO 363 1.340 1.242 1.540 1.531 1.441 121.60 118.09 119.79 111.21 109.93 104.78 122.11 +* +* +* 158 PRO 364 1.351 1.233 1.531 1.539 1.471 123.63 117.56 119.85 110.27 115.11 104.09 122.57 * * 159 GLU 365 1.327 1.240 1.532 1.562 1.458 120.32 116.63 120.41 112.38 111.65 112.87 122.93 +* * * +* 160 ILE 366 1.331 1.244 1.532 1.544 1.450 121.97 116.01 120.71 109.69 110.47 110.91 123.26 161 GLN 367 1.332 1.226 1.513 1.521 1.452 122.08 116.08 120.40 109.17 111.04 111.10 123.52 162 ALA 368 1.326 1.229 1.523 1.520 1.457 122.62 116.57 120.73 110.40 111.48 110.48 122.67 163 ARG 369 1.321 1.228 1.522 1.525 1.462 121.28 116.05 121.18 110.97 110.88 111.10 122.74 164 VAL 370 1.310 1.235 1.525 1.537 1.456 121.84 115.20 121.24 107.17 110.07 110.65 123.55 * * 165 GLN 371 1.317 1.227 1.524 1.525 1.444 123.52 116.00 120.63 110.02 110.55 109.34 123.36 * * 166 GLY 372 1.320 1.231 1.519 - 1.444 121.03 116.45 120.64 - 112.56 - 122.91 167 GLN 373 1.321 1.232 1.513 1.528 1.450 121.59 114.90 121.01 109.23 110.64 110.16 124.08 168 ARG 374 1.328 1.224 1.523 1.533 1.455 124.28 116.53 121.05 112.22 111.76 113.61 122.35 * * +* +* 169 PRO 375 1.352 1.223 1.525 1.531 1.478 123.14 114.88 121.64 110.05 111.97 102.61 123.48 * * * 170 GLY 376 1.304 1.232 1.506 - 1.448 122.03 116.21 120.49 - 112.90 - 123.23 +* +* 171 SER 377 1.306 1.251 1.540 1.530 1.429 122.26 117.31 120.48 112.51 110.15 109.39 122.14 +* +* * +* 172 PRO 378 1.352 1.223 1.533 1.540 1.468 123.50 117.32 120.24 110.66 113.91 104.17 122.44 * * 173 GLU 379 1.320 1.236 1.513 1.507 1.466 121.74 116.37 120.52 111.27 112.23 110.59 123.11 * * 174 GLU 380 1.315 1.215 1.523 1.526 1.424 122.11 116.19 120.62 111.77 107.44 108.89 123.12 +* * +* 175 ALA 381 1.346 1.226 1.522 1.501 1.454 122.02 115.84 120.74 109.93 110.68 110.33 123.41 * * 176 ALA 382 1.327 1.220 1.527 1.525 1.454 123.24 115.53 121.42 110.63 110.67 109.71 123.04 177 ALA 383 1.291 1.232 1.533 1.519 1.451 122.96 116.99 120.68 110.64 111.31 110.46 122.34 +** +** 178 LEU 384 1.330 1.237 1.528 1.555 1.467 120.89 114.57 122.01 107.07 107.60 111.49 123.35 * +* * +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 179 VAL 385 1.326 1.223 1.514 1.538 1.447 122.94 116.37 120.08 111.42 112.66 112.94 123.54 * * 180 ASP 386 1.337 1.233 1.529 1.542 1.483 123.06 115.63 121.00 109.62 110.43 110.44 123.36 * * 181 GLY 387 1.321 1.228 1.526 - 1.437 121.14 116.25 120.52 - 112.30 - 123.21 182 LEU 388 1.334 1.226 1.538 1.534 1.486 123.49 116.93 120.34 109.53 113.36 110.40 122.73 * * 183 ARG 389 1.333 1.239 1.518 1.544 1.476 122.17 115.22 121.31 108.84 110.62 111.10 123.46 184 ARG 390 1.306 1.230 1.516 1.523 1.417 122.47 114.98 120.84 111.95 108.06 108.64 124.10 +* ** * * ** 185 GLU 391 1.322 1.245 1.539 1.536 1.463 124.87 117.07 121.33 110.78 111.90 113.79 121.59 +* +* +* 186 PRO 392 1.340 1.231 1.530 1.531 1.456 122.27 115.73 121.34 110.69 110.98 103.14 122.92 187 GLY 393 1.322 1.236 1.505 - 1.434 121.36 115.60 120.56 - 111.60 - 123.80 * * 188 GLY 394 1.299 - 1.491 - 1.421 122.56 - - - 108.87 - - ** * +* * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** ** ** +* *** +* +* +** ** +** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 1.267 1.346 1.320 .013 **** * C-N (Pro) 1.341 .016 18 1.338 1.364 1.349 .007 * C-O C-O 1.231 .020 187 1.184 1.251 1.229 .010 ** CA-C CH1E-C (except Gly) 1.525 .021 170 1.482 1.556 1.523 .012 ** * CH2G*-C (Gly) 1.516 .018 18 1.491 1.533 1.513 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.501 1.539 1.520 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.534 1.586 1.554 .017 +* CH1E-CH2E (the rest) 1.530 .020 138 1.490 1.569 1.531 .014 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.393 1.494 1.451 .016 *** +* NH1-CH2G* (Gly) 1.451 .016 18 1.413 1.465 1.442 .012 ** N-CH1E (Pro) 1.466 .015 18 1.441 1.487 1.468 .012 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 2.0 152 113.26 118.50 116.20 .92 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.37 119.67 116.97 1.41 +* CH1E-C-N (Pro) 116.9 1.5 18 114.22 118.09 116.45 1.14 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.93 124.75 123.02 .66 * * O-C-N (Pro) 122.0 1.4 18 122.11 124.04 122.85 .51 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.80 125.17 122.24 1.26 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 16 119.65 122.91 121.28 .85 * C-N-CH1E (Pro) 122.6 5.0 18 121.51 124.33 122.73 .82 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.45 122.10 120.72 .54 CH2G*-C-O (Gly) 120.8 2.1 17 119.25 121.27 120.36 .60 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.91 111.34 110.58 .39 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.94 111.62 109.72 1.42 * CH2E-CH1E-C (the rest) 110.1 1.9 138 104.82 115.11 110.70 1.57 +** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 105.01 117.00 110.80 1.55 ** ** NH1-CH2G*-C (Gly) 112.5 2.9 18 108.87 113.62 111.68 1.10 * N-CH1E-C (Pro) 111.8 2.5 18 109.40 115.66 112.33 1.77 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.41 111.56 110.47 .52 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.65 113.30 111.99 .85 * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.55 105.01 103.60 .68 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.73 114.76 110.76 1.76 ** +** ------------------------------------------------------------------------------------------------------------- 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_6 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] 138 90.8% Residues in additional allowed regions [a,b,l,p] 12 7.9% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% 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 90.8 83.8 10.0 .7 Inside b. Omega angle st dev 186 3.0 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 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 125 .8 .8 .2 .2 Inside f. Overall G-factor 188 .2 -.4 .3 2.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 12 9.1 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 54 7.7 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 66 11.2 17.5 4.9 -1.3 BETTER d. Chi-1 pooled st dev 132 10.0 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 60 6.8 20.4 5.0 -2.7 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 90.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 11.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .85 2 Residue-by-residue listing for refined_6 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .12 Chi1-chi2 distribution .08 Chi1 only .11 Chi3 & chi4 .46 Omega .14 ------ .17 ===== Main-chain covalent forces:- Main-chain bond lengths .29 Main-chain bond angles .41 ------ .36 ===== OVERALL AVERAGE .24 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.