Residue-by-residue listing for refined_8 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 - - - - - - - - - - - 181.1 - - - 2 SER 2 b 51.6 - - - - - - - - - 177.4 - 31.7 - 3 ASP 3 b 69.3 - - - - - - - - - 176.2 -1.8 34.5 - 4 PRO 4 S - - - - - -101.1 - - - - - 185.1 - 40.7 - *** +* *** 5 GLY 5 h - - - - - - - - - - - 182.9 - - - 6 PRO 6 H - - - - - -52.5 -52.5 -35.5 - - - 179.0 - 38.2 - * * * * 7 GLU 7 H A - - -67.7 - - -66.5 -45.7 - - - 179.9 - 33.0 - 8 ALA 8 H A - - - - - -75.3 -26.5 - - - 175.1 - 33.0 - * * 9 ALA 9 H A - - - - - -63.0 -48.6 - - - 177.4 -2.6 34.0 - 10 ARG 10 H A - 183.1 - 181.0 - -64.9 -34.3 - - - 178.9 -2.4 33.8 - 11 LEU 11 H A - 167.7 - - - -60.0 -51.4 - - - 177.9 -1.6 34.6 - * * 12 ARG 12 H A - - -65.5 180.6 - -63.3 -37.7 - - - 178.7 -2.7 33.6 - 13 PHE 13 H A - 178.1 - - - -63.3 -37.5 - - - 178.4 -2.2 34.5 - 14 ARG 14 H A - - -67.5 - - -90.5 -9.5 - - - 177.8 -2.4 32.2 - ** +** +** 15 CYS 15 h A - 189.1 - - - - - - - - 178.2 -1.1 34.0 - * * 16 PHE 16 B - 184.8 - - - - - - - - 177.9 - 35.6 - 17 HIS 17 B 70.7 - - - - - - - - - 175.7 - 34.3 - 18 TYR 18 B - 172.8 - - - - - - - - 180.9 -.8 31.9 - +* +* 19 GLU 19 t B 47.9 - - 179.3 - - - - - - 181.0 -.6 32.9 - * +* +* Residue-by-residue listing for refined_8 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 - - -48.8 - - - - - - - 179.6 -.6 34.7 - * +* +* 21 ALA 21 T A - - - - - - - - - - 181.2 - 33.6 - 22 THR 22 T A - 202.9 - - - - - - - - 183.8 -1.7 34.1 - * * 23 GLY 23 h - - - - - - - - - - - 185.2 -1.0 - - * * 24 PRO 24 H - - - - - -77.9 -77.9 -32.7 - - - 185.4 - 38.5 - * * * * 25 GLN 25 H A - 198.5 - 165.4 - -78.6 -32.6 - - - 174.1 - 34.0 - * * * 26 GLU 26 H A - 177.1 - 170.0 - -71.9 -34.1 - - - 174.2 - 32.8 - * * 27 ALA 27 H A - - - - - -62.9 -44.6 - - - 176.9 -1.5 34.3 - 28 LEU 28 H A - - -65.7 178.9 - -55.7 -44.6 - - - 179.0 -2.3 33.7 - 29 ALA 29 H A - - - - - -56.8 -44.7 - - - 179.2 -1.9 34.1 - 30 GLN 30 H A - - -68.4 168.7 - -68.8 -45.9 - - - 177.4 -1.7 34.1 - 31 LEU 31 H A - - -69.4 171.1 - -61.5 -43.0 - - - 177.9 -3.3 34.0 - +* +* 32 ARG 32 H A - 179.9 - 178.8 - -58.6 -45.0 - - - 178.5 -3.5 35.1 - +* +* 33 GLU 33 H A - 178.0 - 183.4 - -62.3 -50.7 - - - 180.1 -1.9 35.6 - 34 LEU 34 H A - - -61.2 175.6 - -63.0 -41.8 - - - 180.0 -2.9 34.4 - * * 35 CYS 35 H A - 185.5 - - - -65.9 -41.6 - - - 177.0 -3.4 34.2 - +* +* 36 ARG 36 H A - 172.6 - - - -65.4 -33.0 - - - 175.4 -2.6 30.4 - * * 37 GLN 37 H A - - -67.8 180.2 - -64.4 -31.0 - - - 182.1 -1.9 35.1 - 38 TRP 38 H A - 161.9 - - - -86.4 -52.8 - - - 182.0 -1.2 33.6 - * +* * * +* 39 LEU 39 H A - - -62.4 172.6 - -77.1 -40.8 - - - 182.6 -3.5 33.8 - +* +* 40 ARG 40 h l - - -72.6 181.1 - - - - - - 181.3 -1.6 29.1 - * * 41 PRO 41 T - - - - - -62.0 - - - - - 181.9 - 38.3 - * * 42 GLU 42 T A 63.3 - - 181.1 - - - - - - 184.9 - 33.7 - 43 VAL 43 T A - 181.9 - - - - - - - - 182.7 -.9 36.2 - +* +* 44 ARG 44 t B - - -62.2 186.8 - - - - - - 180.8 -3.6 32.4 - ** ** 45 SER 45 h B - - -55.7 - - - - - - - 179.2 - 36.8 - 46 LYS 46 H A - - -64.6 172.8 - -54.2 -38.9 - - - 182.1 - 36.0 - 47 GLU 47 H A - - -54.8 - - -55.5 -40.9 - - - 182.1 - 36.7 - 48 GLN 48 H A - - -61.8 176.7 - -70.0 -31.4 - - - 180.0 -.8 34.4 - +* +* 49 MET 49 H A - - -60.7 182.3 - -63.8 -39.2 - - - 172.8 -1.0 32.1 - * * * 50 LEU 50 H A - - -73.0 - - -53.9 -52.3 - - - 181.5 -1.3 34.4 - * * 51 GLU 51 H A - 177.1 - 177.8 - -56.2 -48.3 - - - 179.3 -1.3 34.5 - * * 52 LEU 52 H A - - -62.1 178.8 - -61.4 -43.0 - - - 181.1 -2.4 34.4 - 53 LEU 53 H A - 183.1 - - - -72.7 -31.3 - - - 174.5 -2.6 33.3 - 54 VAL 54 H A - 176.5 - - - -60.7 -43.6 - - - 176.5 -2.7 33.3 - 55 LEU 55 H A - 175.1 - - - -59.9 -41.9 - - - 182.3 -2.0 36.5 - Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 GLU 56 H A - 186.6 - - - -56.4 -52.2 - - - 182.2 -1.7 35.8 - * * 57 GLN 57 H A - 211.7 - - - -74.2 -40.5 - - - 182.4 -2.2 35.0 - +* +* 58 PHE 58 H A - 181.8 - - - -53.8 -47.9 - - - 177.9 -2.9 33.2 - * * 59 LEU 59 H A - - -95.4 - - -60.2 -38.7 - - - 180.0 -2.8 29.9 - +* * * +* 60 GLY 60 H - - - - - - -80.8 -24.0 - - - 177.4 -1.2 - - * * * * 61 ALA 61 H A - - - - - -70.3 -28.9 - - - 172.9 -2.5 33.4 - * * 62 LEU 62 h B - - -67.2 170.9 - - - - - - 177.0 -1.5 36.8 - 63 PRO 63 h - - - - - -72.6 - - - - - 181.1 - 38.5 - * * 64 PRO 64 H - - - - - -35.8 -35.8 -45.6 - - - 180.8 - 38.7 - +** ** * +** 65 GLU 65 H A 57.6 - - 184.2 - -60.9 -47.7 - - - 178.7 - 32.0 - 66 ILE 66 H A - - -58.0 178.2 - -74.0 -42.5 - - - 182.6 -.9 34.9 - * * 67 GLN 67 H A - 180.6 - 178.7 - -59.6 -46.2 - - - 182.5 -3.4 33.9 - +* +* 68 ALA 68 H A - - - - - -60.5 -30.7 - - - 178.5 -3.2 33.3 - * * 69 ARG 69 H A - - -58.8 - - -66.7 -52.0 - - - 181.1 -.7 35.6 - * +* +* 70 VAL 70 H A - 178.8 - - - -66.7 -35.4 - - - 184.0 -1.7 37.2 - 71 GLN 71 H A - 198.4 - - - -50.2 -45.7 - - - 181.9 -2.9 36.6 - * * * 72 GLY 72 H - - - - - - -61.1 -36.9 - - - 181.7 -1.0 - - * * 73 GLN 73 H A - - -62.7 - - -83.8 -51.8 - - - 190.2 -.8 34.1 - +* * +* +* +* 74 ARG 74 h l - - -65.3 - - - - - - - 183.7 -3.1 31.2 - * * 75 PRO 75 - - - - - -40.0 - - - - - 180.6 - 38.8 - ** * ** 76 GLY 76 S - - - - - - - - - - - 174.0 - - - * * 77 SER 77 h B 56.0 - - - - - - - - - 182.7 - 33.0 - 78 PRO 78 H - - - - - -60.7 -60.7 -44.1 - - - 180.5 - 37.9 - * * 79 GLU 79 H A - - -66.2 178.7 - -65.9 -29.9 - - - 175.5 - 32.0 - 80 GLU 80 H A - 182.4 - - - -65.0 -48.8 - - - 176.4 - 34.4 - 81 ALA 81 H A - - - - - -55.9 -43.1 - - - 180.3 -1.9 34.4 - 82 ALA 82 H A - - - - - -53.6 -36.5 - - - 180.6 -2.5 34.3 - 83 ALA 83 H A - - - - - -65.9 -50.2 - - - 179.0 -1.2 33.1 - * * 84 LEU 84 H A 51.1 - - 161.1 - -71.3 -42.6 - - - 181.4 -1.3 28.1 - +* +* 85 VAL 85 H A - - -61.1 - - -63.7 -31.0 - - - 175.3 -3.1 29.3 - * * * 86 ASP 86 H A - 180.3 - - - -55.3 -35.8 - - - 176.9 -1.7 34.1 - 87 GLY 87 H - - - - - - -84.3 -37.4 - - - 181.6 -1.1 - - +* * +* 88 LEU 88 H A - - -58.6 175.8 - -67.8 -27.5 - - - 178.3 -2.3 33.9 - * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 89 ARG 89 h A 59.3 - - 173.9 - - - - - - 178.7 -2.7 33.0 - 90 ARG 90 T A - - -63.2 172.3 - - - - - - 181.3 -1.3 35.5 - 91 GLU 91 t b - 185.7 - - - - - - - - 179.0 -1.7 35.7 - 92 PRO 92 - - - - - -78.6 - - - - - 179.8 - 38.8 - * * * 93 GLY 93 - - - - - - - - - - - 180.6 -.6 - - +* +* 94 GLY 94 - - - - - - - - - - - - -2.1 - - 95 GLY 301 - - - - - - - - - - - 180.5 - - - 96 SER 302 B - - -58.1 - - - - - - - 180.1 - 34.3 - 97 ASP 303 B 68.6 - - - - - - - - - 178.7 - 35.0 - 98 PRO 304 S - - - - - -93.9 - - - - - 185.9 - 40.6 - +** * +* +** 99 GLY 305 h - - - - - - - - - - - 184.9 - - - 100 PRO 306 H - - - - - -58.9 -58.9 -36.5 - - - 180.0 - 38.3 - * * 101 GLU 307 H A - - -62.4 - - -70.3 -36.2 - - - 178.1 - 32.7 - 102 ALA 308 H A - - - - - -75.5 -30.6 - - - 178.2 - 33.8 - 103 ALA 309 H A - - - - - -65.8 -38.3 - - - 177.2 -2.5 33.8 - 104 ARG 310 H A - 185.3 - 179.7 - -61.1 -33.9 - - - 179.9 -1.9 34.2 - 105 LEU 311 H A - 172.2 - - - -65.5 -43.0 - - - 175.5 -.9 34.2 - +* +* 106 ARG 312 H A - - -65.7 181.9 - -61.3 -45.3 - - - 180.8 -1.6 35.0 - 107 PHE 313 H A - 180.3 - - - -58.5 -42.0 - - - 176.1 -2.5 34.3 - 108 ARG 314 H A - - -79.5 - - -79.4 -27.0 - - - 179.0 -2.4 32.6 - * * * 109 CYS 315 H A - 181.9 - - - -66.7 -35.0 - - - 179.8 -2.1 34.2 - 110 PHE 316 h B - 186.1 - - - - - - - - 179.7 -2.0 35.0 - 111 HIS 317 B 73.2 - - - - - - - - - 176.4 - 34.7 - 112 TYR 318 B - 168.9 - - - - - - - - 178.7 -1.3 31.2 - 113 GLU 319 g B 43.7 - - 181.6 - - - - - - 182.7 -.6 33.2 - * +* +* 114 GLU 320 G A - - -52.3 - - - - - - - 181.4 -.6 33.9 - +* +* 115 ALA 321 G A - - - - - - - - - - 183.6 - 33.6 - 116 THR 322 G A - 201.5 - - - - - - - - 182.2 -1.6 34.4 - * * 117 GLY 323 h - - - - - - - - - - - 186.0 -.9 - - * +* +* 118 PRO 324 H - - - - - -80.2 -80.2 -33.5 - - - 185.0 - 38.8 - * * * * 119 GLN 325 H A - 193.5 - 170.4 - -78.5 -28.9 - - - 175.0 - 34.5 - * * 120 GLU 326 H A - 181.3 - 169.4 - -75.1 -33.5 - - - 173.3 - 33.3 - * * 121 ALA 327 H A - - - - - -64.0 -41.0 - - - 177.8 -1.3 34.5 - 122 LEU 328 H A - - -63.2 180.8 - -58.0 -40.9 - - - 179.6 -2.1 34.2 - 123 ALA 329 H A - - - - - -60.9 -47.5 - - - 178.8 -1.4 33.9 - 124 GLN 330 H A - - -68.3 172.5 - -63.9 -44.0 - - - 176.2 -1.8 34.3 - 125 LEU 331 H A - - -74.0 169.8 - -63.0 -43.1 - - - 178.5 -3.1 33.4 - * * 126 ARG 332 H A - 177.6 - 177.9 - -59.6 -46.1 - - - 178.1 -3.2 34.0 - +* +* 127 GLU 333 H A - 180.2 - 184.3 - -58.9 -50.4 - - - 180.8 -2.5 35.7 - 128 LEU 334 H A - - -61.0 174.9 - -64.5 -42.8 - - - 178.1 -2.6 33.9 - 129 CYS 335 H A - 181.2 - - - -65.2 -34.2 - - - 180.2 -3.4 34.8 - +* +* Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 130 ARG 336 H A - 182.4 - - - -71.3 -33.7 - - - 175.4 -2.3 31.4 - 131 GLN 337 H A - - -67.8 174.5 - -68.4 -21.6 - - - 178.8 -1.8 34.3 - +* +* 132 TRP 338 H a - 163.7 - - - -90.5 -61.3 - - - 181.7 -.8 32.1 - * ** +* +* ** 133 LEU 339 H A - - -61.6 184.2 - -69.6 -41.6 - - - 179.3 -3.6 32.3 - ** ** 134 ARG 340 h l - - -57.0 189.3 - - - - - - 178.8 -1.4 31.5 - 135 PRO 341 T - - - - - -66.4 - - - - - 178.6 - 38.7 - * * 136 GLU 342 T A 57.5 - - 177.6 - - - - - - 181.9 - 35.3 - 137 VAL 343 T A - - -61.8 - - - - - - - 181.0 -1.1 32.3 - * * 138 ARG 344 t B - - -63.7 188.5 - - - - - - 180.7 -3.4 31.7 - +* +* 139 SER 345 h B - - -57.6 - - - - - - - 184.1 - 34.7 - 140 LYS 346 H A 58.0 - - - - -58.6 -39.6 - - - 180.3 - 32.1 - 141 GLU 347 H A - - -45.5 - - -55.5 -44.3 - - - 180.4 - 35.9 - * * 142 GLN 348 H A - - -59.6 179.0 - -66.9 -33.8 - - - 177.7 -.5 34.1 - ** ** 143 MET 349 H A - - -60.7 180.8 - -65.2 -42.3 - - - 172.0 -1.3 32.4 - * * * 144 LEU 350 H A - - -78.7 - - -53.8 -52.0 - - - 180.6 -2.1 33.6 - * * 145 GLU 351 H A - 179.0 - 182.5 - -54.8 -49.5 - - - 180.1 -2.0 35.4 - 146 LEU 352 H A - - -64.9 175.4 - -63.6 -43.8 - - - 182.3 -2.7 34.5 - 147 LEU 353 H A - 181.6 - - - -75.1 -30.7 - - - 172.4 -2.9 31.3 - * * * 148 VAL 354 H A - 175.2 - - - -64.9 -41.9 - - - 176.5 -3.0 33.3 - * * 149 LEU 355 H A - 178.5 - - - -57.1 -44.9 - - - 179.5 -2.2 36.1 - 150 GLU 356 H A - 175.2 - - - -53.7 -51.9 - - - 182.0 -2.0 33.5 - * * 151 GLN 357 H A - 191.5 - - - -71.6 -46.8 - - - 184.2 -1.9 33.6 - 152 PHE 358 H A - 180.4 - - - -55.3 -48.0 - - - 179.0 -3.0 33.5 - * * 153 LEU 359 H A - - -102.5 - - -62.0 -37.0 - - - 180.1 -2.9 31.2 - ** * ** 154 GLY 360 H - - - - - - -80.5 -25.9 - - - 177.3 -1.4 - - * * * 155 ALA 361 H A - - - - - -66.4 -34.2 - - - 175.1 -2.5 33.5 - 156 LEU 362 h B - - -65.5 171.4 - - - - - - 178.0 -1.6 37.5 - * * 157 PRO 363 h - - - - - -69.5 - - - - - 182.4 - 38.0 - * * 158 PRO 364 H - - - - - -39.4 -39.4 -45.4 - - - 181.1 - 38.2 - ** ** * ** 159 GLU 365 H A 59.8 - - 180.4 - -63.6 -48.3 - - - 180.1 - 33.0 - 160 ILE 366 H A - - -60.5 180.4 - -68.8 -39.6 - - - 179.6 -.5 34.7 - ** ** 161 GLN 367 H A - 179.9 - 177.4 - -61.9 -46.4 - - - 180.1 -3.2 34.2 - +* +* 162 ALA 368 H A - - - - - -62.2 -34.2 - - - 176.6 -3.0 33.2 - * * 163 ARG 369 H A - - -63.0 - - -64.5 -40.2 - - - 175.2 -1.5 33.8 - 164 VAL 370 H A - 171.9 - - - -60.3 -50.3 - - - 177.4 -1.7 34.8 - Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 165 GLN 371 H A - - -93.6 - - -51.5 -29.6 - - - 178.4 -2.5 34.0 - +* * +* 166 GLY 372 H - - - - - - -67.3 -40.1 - - - 182.7 -1.2 - - * * 167 GLN 373 H A - - -65.3 - - -96.0 -39.6 - - - 183.4 -1.0 32.9 - +** * +** 168 ARG 374 h l - - -56.4 - - - - - - - 178.9 -3.5 32.6 - +* +* 169 PRO 375 - - - - - -65.0 - - - - - 178.9 - 39.0 - * * 170 GLY 376 S - - - - - - - - - - - 176.9 - - - 171 SER 377 h B 53.8 - - - - - - - - - 183.6 - 32.8 - 172 PRO 378 H - - - - - -60.0 -60.0 -44.0 - - - 181.4 - 38.0 - * * 173 GLU 379 H A - - -63.1 171.4 - -67.3 -30.1 - - - 175.9 - 33.0 - 174 GLU 380 H A - 186.4 - - - -72.8 -42.0 - - - 175.8 - 33.9 - 175 ALA 381 H A - - - - - -58.0 -37.3 - - - 178.8 -2.4 33.8 - 176 ALA 382 H A - - - - - -54.6 -35.5 - - - 181.1 -2.2 34.6 - 177 ALA 383 H A - - - - - -66.5 -48.9 - - - 179.4 -.8 33.8 - +* +* 178 LEU 384 H A 48.9 - - 161.1 - -71.4 -42.1 - - - 180.3 -1.1 28.4 - * +* +* 179 VAL 385 H A - - -59.8 - - -63.7 -31.4 - - - 173.2 -2.8 29.4 - * * * * 180 ASP 386 H A - 175.3 - - - -50.4 -40.8 - - - 177.0 -1.8 35.7 - * * 181 GLY 387 H - - - - - - -85.7 -41.2 - - - 183.4 -1.1 - - +* * +* 182 LEU 388 H A - - -58.9 174.6 - -62.2 -33.5 - - - 180.1 -2.8 34.6 - * * 183 ARG 389 h A 63.4 - - 181.5 - - - - - - 181.8 -2.8 35.0 - * * 184 ARG 390 T A - - -50.8 178.1 - - - - - - 183.4 -1.5 36.4 - * * 185 GLU 391 t B - 183.2 - - - - - - - - 176.6 -2.0 34.8 - 186 PRO 392 - - - - - -74.2 - - - - - 183.7 - 38.5 - * * 187 GLY 393 - - - - - - - - - - - 179.7 -.8 - - +* +* 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* ** *** +** +** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.5 181.6 -64.5 177.1 -66.0 -64.9 -40.1 - - - 179.6 -2.0 34.3 Standard deviations: 8.4 9.2 9.8 5.9 17.6 9.6 7.8 - - - 3.0 .8 2.2 Numbers of values: 18 54 60 59 18 125 125 0 0 0 186 131 170 0 Residue-by-residue listing for refined_8 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_8 Page 8 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.235 1.520 - 1.468 - 117.98 120.05 - 113.80 - 121.97 * * 2 SER 2 1.324 1.242 1.533 1.529 1.438 120.45 115.37 121.25 112.53 112.66 110.97 123.28 * * * 3 ASP 3 1.321 1.235 1.515 1.557 1.457 123.46 118.14 119.92 108.68 108.17 112.67 121.91 * * * * 4 PRO 4 1.330 1.232 1.540 1.526 1.449 122.72 116.27 120.96 109.96 111.17 100.92 122.77 * +* +* 5 GLY 5 1.322 1.225 1.520 - 1.440 121.05 119.29 119.13 - 110.39 - 121.58 * * 6 PRO 6 1.357 1.240 1.540 1.530 1.490 123.35 116.83 120.62 110.50 113.77 103.33 122.54 * +* +* 7 GLU 7 1.327 1.237 1.525 1.542 1.448 121.55 115.94 120.86 110.44 110.56 112.09 123.17 8 ALA 8 1.325 1.233 1.527 1.513 1.451 122.08 115.86 121.16 111.32 110.58 110.92 122.98 9 ALA 9 1.323 1.232 1.514 1.521 1.449 122.32 116.17 120.68 110.61 109.26 110.71 123.11 10 ARG 10 1.344 1.223 1.527 1.524 1.450 121.06 115.94 120.96 109.12 110.04 112.17 123.10 * * 11 LEU 11 1.326 1.212 1.525 1.519 1.421 123.18 116.93 120.06 112.04 110.50 108.24 122.98 +* * * +* 12 ARG 12 1.326 1.223 1.521 1.526 1.465 121.70 115.39 121.09 110.15 110.97 111.20 123.51 13 PHE 13 1.313 1.214 1.542 1.538 1.455 123.71 116.84 120.87 112.53 110.63 107.76 122.26 * * * +* +* Residue-by-residue listing for refined_8 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 14 ARG 14 1.322 1.230 1.515 1.527 1.466 121.80 116.53 120.96 111.09 112.40 111.64 122.51 15 CYS 15 1.296 1.235 1.526 1.534 1.438 121.34 115.05 121.55 111.40 108.64 110.33 123.40 ** * ** 16 PHE 16 1.325 1.243 1.516 1.542 1.439 123.19 116.39 120.71 109.87 108.69 109.66 122.89 * * 17 HIS 17 1.301 1.238 1.509 1.565 1.437 120.66 118.09 119.53 110.28 107.62 111.74 122.37 ** +* * * ** 18 TYR 18 1.306 1.233 1.499 1.536 1.438 119.13 114.74 121.20 111.78 108.89 113.06 124.00 +* * * * +* +* 19 GLU 19 1.289 1.238 1.512 1.537 1.418 122.97 115.09 121.49 112.64 110.33 110.37 123.40 +** ** * +** 20 GLU 20 1.310 1.227 1.518 1.543 1.455 123.63 115.33 120.84 108.52 109.99 111.80 123.83 * * * 21 ALA 21 1.321 1.235 1.533 1.521 1.453 123.62 117.64 120.20 110.39 112.40 110.49 122.16 * * 22 THR 22 1.328 1.217 1.542 1.583 1.447 119.66 116.33 121.00 111.03 108.98 110.85 122.50 +* * +* 23 GLY 23 1.332 1.231 1.514 - 1.458 120.89 120.73 119.29 - 109.75 - 119.97 ** +* ** 24 PRO 24 1.341 1.215 1.510 1.516 1.438 119.93 115.58 121.15 110.79 111.99 103.43 123.24 +* +* 25 GLN 25 1.296 1.229 1.527 1.494 1.402 122.90 116.33 120.80 114.36 110.22 106.68 122.84 ** +* +** ** ** +** 26 GLU 26 1.337 1.241 1.524 1.535 1.450 120.84 115.92 121.17 112.02 109.09 111.34 122.90 * * 27 ALA 27 1.330 1.218 1.518 1.522 1.449 121.72 115.87 120.54 110.58 108.97 110.45 123.57 28 LEU 28 1.331 1.207 1.508 1.523 1.466 122.90 117.26 119.73 108.90 112.07 111.97 123.00 * * 29 ALA 29 1.330 1.238 1.529 1.521 1.465 121.93 115.23 121.30 110.36 110.57 110.28 123.44 30 GLN 30 1.313 1.223 1.523 1.500 1.440 123.25 116.14 120.73 112.11 111.40 108.26 123.11 * * * * * 31 LEU 31 1.322 1.207 1.507 1.518 1.463 122.90 116.14 120.46 110.32 111.59 110.25 123.40 * * 32 ARG 32 1.314 1.221 1.513 1.530 1.455 123.14 115.13 121.11 110.39 109.55 109.41 123.73 * * 33 GLU 33 1.311 1.231 1.538 1.525 1.445 123.21 116.29 120.62 110.64 110.49 108.03 123.06 * * * 34 LEU 34 1.326 1.230 1.523 1.536 1.465 122.60 115.80 120.94 110.11 110.98 110.24 123.25 35 CYS 35 1.316 1.224 1.527 1.536 1.443 122.57 116.53 120.68 110.94 110.01 110.16 122.78 36 ARG 36 1.329 1.219 1.535 1.549 1.431 122.32 117.56 119.51 115.14 112.72 110.18 122.92 * +** +** 37 GLN 37 1.335 1.228 1.518 1.502 1.472 121.59 114.01 121.91 108.56 111.05 110.33 124.08 * * * 38 TRP 38 1.304 1.229 1.553 1.544 1.437 124.51 117.63 120.11 113.38 113.29 107.40 122.26 +* * * +* +* +* +* 39 LEU 39 1.326 1.226 1.525 1.541 1.470 121.19 116.18 120.16 109.77 111.49 111.24 123.65 40 ARG 40 1.346 1.216 1.521 1.530 1.467 123.50 117.56 120.69 112.15 114.66 113.64 121.75 * * * +* +* 41 PRO 41 1.340 1.230 1.531 1.535 1.472 122.68 116.09 121.09 110.53 113.28 103.59 122.82 42 GLU 42 1.314 1.238 1.529 1.537 1.450 121.61 116.25 120.98 110.61 111.03 110.81 122.77 * * 43 VAL 43 1.331 1.241 1.526 1.547 1.435 121.35 116.63 120.84 108.04 111.25 110.01 122.50 * * 44 ARG 44 1.309 1.235 1.503 1.540 1.431 120.99 114.20 121.73 110.60 111.83 112.55 124.08 * * * * * * Residue-by-residue listing for refined_8 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 45 SER 45 1.288 1.241 1.521 1.514 1.419 124.09 115.74 120.67 110.64 109.90 106.62 123.59 +** ** * ** +** 46 LYS 46 1.325 1.215 1.519 1.517 1.465 123.38 115.23 120.88 108.81 110.91 109.06 123.84 47 GLU 47 1.324 1.236 1.524 1.520 1.472 123.98 114.87 121.34 107.70 110.66 109.20 123.79 * * * 48 GLN 48 1.319 1.228 1.526 1.525 1.450 123.17 116.79 120.58 110.41 111.77 109.66 122.63 49 MET 49 1.328 1.230 1.507 1.504 1.458 121.39 116.02 120.29 112.06 111.64 111.00 123.68 * * * 50 LEU 50 1.336 1.207 1.512 1.551 1.463 122.07 116.24 120.26 108.67 109.82 112.17 123.46 * * * 51 GLU 51 1.330 1.245 1.535 1.518 1.433 123.16 116.19 120.69 111.16 111.77 108.79 123.11 * * * 52 LEU 52 1.320 1.237 1.519 1.523 1.440 122.08 116.24 120.76 110.22 111.20 110.10 123.00 53 LEU 53 1.317 1.238 1.547 1.490 1.417 121.87 117.44 120.32 113.39 112.78 107.55 122.24 * +* ** +* +* ** 54 VAL 54 1.327 1.227 1.528 1.563 1.464 120.91 115.64 120.86 110.42 109.09 112.39 123.44 55 LEU 55 1.332 1.241 1.517 1.523 1.465 122.96 114.64 121.07 107.77 110.40 109.54 124.29 * * 56 GLU 56 1.317 1.238 1.529 1.525 1.439 123.70 116.33 121.07 109.16 110.89 109.26 122.59 * * * 57 GLN 57 1.317 1.207 1.515 1.518 1.440 120.11 116.49 120.12 109.12 108.59 110.98 123.37 * * 58 PHE 58 1.337 1.233 1.521 1.534 1.460 122.07 116.42 120.44 110.23 111.53 111.64 123.13 59 LEU 59 1.321 1.209 1.504 1.535 1.454 121.07 117.58 119.56 113.13 113.25 112.44 122.78 * +* * +* 60 GLY 60 1.317 1.230 1.510 - 1.445 119.42 116.09 120.64 - 112.23 - 123.26 61 ALA 61 1.327 1.235 1.516 1.530 1.449 122.53 115.66 120.65 111.12 109.66 111.08 123.67 62 LEU 62 1.336 1.240 1.528 1.536 1.446 122.81 118.48 119.93 107.85 108.76 109.56 121.60 * * * 63 PRO 63 1.339 1.239 1.518 1.540 1.441 121.34 118.01 118.95 110.12 108.60 104.90 123.03 +* * * +* +* 64 PRO 64 1.350 1.222 1.535 1.516 1.475 124.59 117.31 120.01 110.56 114.68 102.44 122.66 * * 65 GLU 65 1.332 1.228 1.543 1.545 1.467 121.23 117.04 120.48 111.99 112.50 111.13 122.46 66 ILE 66 1.320 1.240 1.529 1.550 1.448 121.66 115.43 121.17 109.61 109.79 110.60 123.37 67 GLN 67 1.323 1.224 1.515 1.522 1.449 123.00 116.53 120.10 110.08 111.66 110.72 123.33 68 ALA 68 1.329 1.235 1.519 1.505 1.462 122.60 116.33 120.56 110.36 112.39 110.74 123.10 69 ARG 69 1.319 1.222 1.525 1.531 1.458 121.93 114.91 121.30 108.90 109.04 110.23 123.75 70 VAL 70 1.321 1.246 1.519 1.535 1.468 124.30 113.85 121.64 106.79 111.26 109.38 124.51 * * * * * 71 GLN 71 1.301 1.222 1.537 1.531 1.442 125.56 116.93 120.04 109.25 111.25 107.85 122.98 +* ** +* ** 72 GLY 72 1.321 1.238 1.521 - 1.457 120.95 116.37 120.79 - 113.64 - 122.84 73 GLN 73 1.313 1.225 1.511 1.554 1.446 121.04 115.38 120.66 108.32 111.07 112.70 123.91 * * * * 74 ARG 74 1.332 1.215 1.543 1.551 1.458 123.20 116.78 120.58 110.99 109.65 114.41 122.58 * ** ** 75 PRO 75 1.372 1.227 1.536 1.540 1.491 125.27 116.09 120.87 109.93 115.63 102.82 123.03 +* +* +* +* 76 GLY 76 1.304 1.223 1.514 - 1.456 121.40 116.21 120.46 - 112.52 - 123.33 +* +* 77 SER 77 1.316 1.251 1.541 1.540 1.441 122.83 117.90 120.15 112.28 108.76 110.84 121.89 * * * 78 PRO 78 1.349 1.231 1.527 1.533 1.468 123.14 116.57 120.62 110.57 113.28 104.13 122.81 * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 79 GLU 79 1.322 1.233 1.509 1.503 1.457 121.88 116.16 120.61 111.89 112.02 111.16 123.23 * * 80 GLU 80 1.317 1.223 1.529 1.522 1.437 121.36 116.32 120.45 111.09 108.56 109.96 123.20 * * 81 ALA 81 1.350 1.228 1.517 1.514 1.459 122.18 115.88 120.20 109.78 110.89 110.40 123.89 * * 82 ALA 82 1.339 1.228 1.526 1.522 1.465 123.71 115.72 120.90 110.14 111.83 109.90 123.37 * * 83 ALA 83 1.306 1.237 1.529 1.521 1.447 122.83 117.39 120.14 111.05 111.34 110.85 122.45 +* +* 84 LEU 84 1.339 1.231 1.512 1.562 1.454 119.30 116.88 120.53 111.44 112.72 116.79 122.55 +* * +*** +*** 85 VAL 85 1.324 1.219 1.512 1.533 1.457 121.16 116.75 120.10 111.35 112.92 115.10 123.14 * ** ** 86 ASP 86 1.328 1.228 1.531 1.529 1.468 121.74 115.83 121.07 109.67 110.34 111.16 123.09 87 GLY 87 1.319 1.230 1.518 - 1.438 120.90 115.97 121.06 - 111.47 - 122.95 88 LEU 88 1.323 1.225 1.530 1.525 1.469 122.85 117.08 120.45 109.95 112.38 110.50 122.47 89 ARG 89 1.333 1.220 1.523 1.546 1.474 121.69 115.57 121.27 110.12 110.88 112.28 123.16 * * 90 ARG 90 1.308 1.232 1.526 1.517 1.441 122.93 115.70 121.07 110.03 109.91 108.96 123.23 +* +* 91 GLU 91 1.322 1.238 1.537 1.539 1.441 122.67 117.98 120.34 109.98 109.01 109.16 121.59 92 PRO 92 1.337 1.240 1.525 1.545 1.457 122.57 116.54 120.64 110.14 111.17 103.90 122.82 93 GLY 93 1.313 1.232 1.509 - 1.444 121.37 115.93 120.87 - 111.87 - 123.19 * * 94 GLY 94 1.306 1.243 1.508 - 1.442 121.27 - 120.56 - 112.38 - - +* +* 95 GLY 301 - 1.243 1.508 - 1.452 - 115.40 121.15 - 111.41 - 123.44 96 SER 302 1.310 1.244 1.526 1.532 1.440 122.47 115.97 120.93 110.65 110.27 110.10 123.08 * * 97 ASP 303 1.315 1.237 1.524 1.546 1.451 122.35 117.79 120.34 109.17 109.19 111.08 121.86 98 PRO 304 1.334 1.241 1.534 1.523 1.461 122.79 116.34 120.85 109.38 111.98 101.53 122.80 * * 99 GLY 305 1.318 1.224 1.512 - 1.436 120.67 119.22 119.21 - 109.19 - 121.57 * * * 100 PRO 306 1.341 1.234 1.529 1.527 1.478 122.60 116.96 120.79 110.48 113.52 103.35 122.18 101 GLU 307 1.318 1.237 1.534 1.542 1.436 120.58 115.95 121.03 110.81 110.01 112.40 123.00 * * * 102 ALA 308 1.324 1.228 1.528 1.521 1.458 122.06 115.92 121.25 110.65 110.26 110.59 122.82 103 ALA 309 1.317 1.237 1.510 1.503 1.448 122.46 116.25 120.56 110.37 110.60 110.64 123.17 104 ARG 310 1.340 1.230 1.526 1.522 1.451 121.24 115.40 121.36 108.81 109.86 111.95 123.23 105 LEU 311 1.321 1.216 1.533 1.519 1.403 123.18 117.15 119.94 112.74 110.33 108.25 122.88 +** * * +** 106 ARG 312 1.339 1.228 1.520 1.528 1.477 121.33 114.35 121.64 107.98 109.60 111.60 123.99 * * 107 PHE 313 1.314 1.224 1.543 1.528 1.450 124.41 116.93 120.40 112.66 111.62 107.52 122.66 * +* * +* +* 108 ARG 314 1.327 1.243 1.520 1.528 1.468 121.98 116.47 120.32 109.94 112.63 112.19 123.21 109 CYS 315 1.319 1.238 1.515 1.537 1.448 122.13 115.65 120.56 110.47 109.89 110.66 123.78 110 PHE 316 1.327 1.242 1.523 1.537 1.449 123.09 116.07 121.05 109.60 110.25 110.19 122.89 111 HIS 317 1.302 1.231 1.502 1.564 1.436 121.26 118.43 119.51 109.96 107.07 111.70 122.05 +* * +* * * * +* 112 TYR 318 1.295 1.231 1.506 1.524 1.426 118.20 114.15 121.84 112.25 110.08 113.01 123.99 ** +* +* * * * ** Residue-by-residue listing for refined_8 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 113 GLU 319 1.286 1.238 1.508 1.543 1.416 123.70 115.53 120.88 113.02 109.12 110.14 123.56 *** ** * +* *** 114 GLU 320 1.325 1.215 1.510 1.537 1.456 123.34 115.90 120.47 108.47 111.58 112.45 123.62 * * 115 ALA 321 1.311 1.226 1.531 1.519 1.449 123.08 117.60 119.89 110.29 112.73 110.41 122.48 * * 116 THR 322 1.333 1.233 1.539 1.580 1.452 120.09 115.95 121.02 110.58 109.52 110.73 122.98 * * 117 GLY 323 1.331 1.233 1.513 - 1.453 120.99 120.41 119.38 - 109.92 - 120.19 +* +* +* 118 PRO 324 1.340 1.215 1.508 1.511 1.445 120.31 115.59 121.29 110.64 112.55 102.92 123.10 * * 119 GLN 325 1.287 1.231 1.522 1.486 1.399 122.97 115.73 121.18 113.73 110.14 106.54 123.08 +** ** *** +* ** *** 120 GLU 326 1.324 1.242 1.522 1.522 1.442 121.56 115.04 121.83 112.06 108.63 110.58 123.13 * * 121 ALA 327 1.320 1.224 1.523 1.520 1.440 122.23 116.11 120.46 110.46 109.12 110.20 123.41 122 LEU 328 1.343 1.206 1.505 1.531 1.464 122.67 116.85 119.85 108.20 111.39 112.33 123.30 * * * 123 ALA 329 1.324 1.228 1.525 1.520 1.458 121.47 115.37 121.20 110.84 110.14 110.33 123.38 124 GLN 330 1.320 1.229 1.521 1.497 1.443 122.89 115.98 120.78 111.42 111.45 108.61 123.23 +* * +* 125 LEU 331 1.325 1.210 1.509 1.528 1.458 122.77 116.55 120.25 110.68 111.46 110.86 123.19 * * 126 ARG 332 1.316 1.219 1.507 1.531 1.452 122.34 115.46 120.64 110.50 110.20 110.80 123.89 127 GLU 333 1.308 1.234 1.541 1.521 1.442 123.15 116.02 120.96 110.29 110.36 108.21 122.99 +* * +* 128 LEU 334 1.321 1.229 1.525 1.530 1.462 122.59 116.05 120.82 110.95 111.18 109.98 123.11 129 CYS 335 1.320 1.222 1.519 1.531 1.447 122.65 116.43 120.90 109.97 110.18 110.03 122.66 130 ARG 336 1.317 1.214 1.513 1.546 1.442 121.89 116.78 120.05 114.17 110.94 110.63 123.17 ** ** 131 GLN 337 1.317 1.229 1.518 1.494 1.455 121.96 114.56 121.57 110.49 110.81 109.62 123.87 +* +* 132 TRP 338 1.314 1.227 1.550 1.553 1.432 123.82 118.37 119.68 113.67 112.60 109.50 121.95 * * * * * * +* +* 133 LEU 339 1.332 1.226 1.515 1.550 1.462 119.93 115.86 120.20 110.34 110.55 113.29 123.93 * +* +* 134 ARG 340 1.349 1.224 1.518 1.538 1.457 123.91 117.82 120.51 109.98 113.12 113.62 121.67 * * +* +* 135 PRO 341 1.343 1.230 1.523 1.535 1.475 122.61 114.38 121.76 110.53 110.82 103.38 123.87 +* * +* 136 GLU 342 1.312 1.232 1.541 1.536 1.428 124.31 116.94 120.72 110.24 111.03 108.89 122.34 * +* * +* 137 VAL 343 1.332 1.222 1.516 1.558 1.457 121.08 117.16 120.50 109.88 112.50 113.03 122.34 138 ARG 344 1.311 1.234 1.499 1.534 1.439 120.12 114.85 121.42 110.70 111.38 113.49 123.73 * * +* +* 139 SER 345 1.291 1.235 1.529 1.511 1.421 123.00 115.43 120.91 111.59 110.78 108.32 123.65 +** +* * +** 140 LYS 346 1.316 1.220 1.514 1.538 1.456 123.76 116.06 120.50 110.83 113.66 111.73 123.43 * * 141 GLU 347 1.305 1.235 1.512 1.538 1.488 123.02 113.77 122.26 106.21 109.50 112.24 123.97 +* +* * ** * ** 142 GLN 348 1.299 1.225 1.522 1.512 1.443 123.29 116.55 120.55 110.92 111.33 109.54 122.89 ** ** Residue-by-residue listing for refined_8 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 143 MET 349 1.324 1.228 1.512 1.505 1.454 121.57 116.33 120.15 112.17 111.06 110.71 123.52 * * * 144 LEU 350 1.340 1.209 1.516 1.565 1.473 121.96 116.39 120.26 109.58 109.71 112.54 123.30 * +* * +* 145 GLU 351 1.332 1.241 1.542 1.523 1.436 123.29 115.99 120.81 110.06 111.49 108.65 123.20 * * * 146 LEU 352 1.320 1.234 1.523 1.526 1.444 122.69 116.64 120.72 110.13 111.91 109.74 122.64 147 LEU 353 1.311 1.240 1.555 1.516 1.418 121.45 117.56 120.35 116.16 112.66 107.66 122.06 * * ** *** +* *** 148 VAL 354 1.328 1.232 1.534 1.567 1.468 120.80 115.73 120.91 109.97 108.77 112.91 123.34 149 LEU 355 1.337 1.231 1.518 1.531 1.467 123.01 114.70 121.09 108.57 109.60 109.66 124.21 150 GLU 356 1.324 1.238 1.532 1.550 1.441 123.73 117.25 120.30 111.98 111.96 109.53 122.43 * * 151 GLN 357 1.316 1.223 1.507 1.540 1.448 119.77 116.27 119.84 111.08 109.79 110.97 123.83 * * 152 PHE 358 1.326 1.239 1.521 1.527 1.454 122.27 115.98 120.84 110.54 111.76 110.81 123.18 153 LEU 359 1.316 1.214 1.509 1.532 1.441 121.65 117.46 119.76 112.67 112.78 111.46 122.74 * * 154 GLY 360 1.321 1.227 1.513 - 1.446 119.54 116.41 120.46 - 112.13 - 123.12 155 ALA 361 1.331 1.241 1.523 1.528 1.454 122.20 115.62 120.83 111.04 109.92 110.93 123.55 156 LEU 362 1.333 1.239 1.526 1.523 1.454 123.22 118.71 119.65 107.17 109.12 108.91 121.64 * +* +* 157 PRO 363 1.341 1.242 1.516 1.533 1.443 121.07 117.91 119.19 110.52 109.03 105.19 122.89 +* * +* +* 158 PRO 364 1.351 1.221 1.536 1.519 1.473 124.09 117.50 119.78 110.98 114.42 102.69 122.69 * * 159 GLU 365 1.331 1.228 1.550 1.535 1.465 121.39 116.98 120.48 111.08 112.29 110.58 122.48 * * 160 ILE 366 1.334 1.240 1.519 1.554 1.452 121.90 114.86 121.54 109.96 109.51 110.73 123.58 161 GLN 367 1.313 1.227 1.534 1.524 1.436 122.88 116.52 120.65 111.39 110.51 109.33 122.78 * * * 162 ALA 368 1.329 1.233 1.522 1.514 1.464 122.38 116.56 120.57 110.59 111.57 110.98 122.87 163 ARG 369 1.323 1.224 1.527 1.523 1.458 121.32 116.40 120.82 110.41 109.68 111.08 122.77 164 VAL 370 1.334 1.231 1.506 1.536 1.465 121.79 114.82 120.99 107.60 110.10 112.46 124.18 165 GLN 371 1.319 1.224 1.540 1.537 1.469 123.25 116.79 120.30 109.60 112.18 110.79 122.91 166 GLY 372 1.319 1.232 1.529 - 1.443 120.86 117.20 120.15 - 113.02 - 122.63 167 GLN 373 1.334 1.225 1.517 1.545 1.470 120.89 115.87 120.06 108.65 112.47 113.32 124.07 +* +* 168 ARG 374 1.331 1.227 1.544 1.536 1.475 124.15 117.57 120.87 110.12 111.29 112.44 121.46 * * * 169 PRO 375 1.347 1.231 1.544 1.539 1.483 122.66 115.63 121.44 110.22 112.65 102.94 122.93 * * 170 GLY 376 1.316 1.231 1.520 - 1.457 121.61 116.52 120.80 - 112.95 - 122.68 171 SER 377 1.307 1.244 1.538 1.538 1.432 121.97 117.73 120.27 112.82 109.73 110.31 121.98 +* * * +* 172 PRO 378 1.354 1.228 1.524 1.536 1.472 123.06 116.08 120.90 110.27 113.20 104.39 123.01 * * 173 GLU 379 1.313 1.229 1.511 1.508 1.455 122.43 116.23 120.80 112.63 111.23 109.40 122.96 * * * * 174 GLU 380 1.316 1.221 1.533 1.521 1.436 120.91 116.56 120.60 111.41 108.68 110.32 122.82 * * 175 ALA 381 1.348 1.235 1.525 1.515 1.459 122.04 115.66 120.64 110.51 110.85 110.45 123.68 * * 176 ALA 382 1.338 1.224 1.527 1.523 1.462 123.74 115.61 120.84 109.96 111.54 109.74 123.54 * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 177 ALA 383 1.308 1.237 1.517 1.506 1.455 123.26 117.10 120.42 110.08 112.05 110.49 122.48 +* +* 178 LEU 384 1.326 1.230 1.504 1.555 1.445 119.47 116.75 120.37 111.79 112.27 116.38 122.83 * * * *** *** 179 VAL 385 1.327 1.221 1.515 1.536 1.456 120.85 115.80 120.43 112.29 111.97 114.48 123.77 * +* +* 180 ASP 386 1.329 1.229 1.537 1.537 1.468 123.74 115.94 120.95 110.13 110.20 108.48 123.11 * * * 181 GLY 387 1.327 1.230 1.534 - 1.450 121.46 116.21 120.79 - 112.83 - 123.00 182 LEU 388 1.328 1.225 1.527 1.523 1.482 123.75 116.57 120.70 109.32 112.80 109.91 122.72 * * * 183 ARG 389 1.326 1.220 1.531 1.535 1.476 122.49 115.89 121.16 109.15 110.91 110.20 122.94 184 ARG 390 1.316 1.233 1.520 1.530 1.448 122.79 116.03 121.17 109.02 108.99 108.91 122.81 185 GLU 391 1.309 1.233 1.531 1.539 1.434 121.90 117.74 120.34 110.76 110.42 109.29 121.84 * * * 186 PRO 392 1.344 1.242 1.523 1.544 1.456 122.60 116.42 120.92 110.49 110.04 104.28 122.63 * * 187 GLY 393 1.300 1.237 1.493 - 1.433 120.82 115.40 120.98 - 111.81 - 123.61 ** * * ** 188 GLY 394 1.296 - 1.481 - 1.418 121.97 - - - 108.66 - - ** +* ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** * +* ** *** ** ** * *** +* +*** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 1.286 1.350 1.321 .012 *** * C-N (Pro) 1.341 .016 18 1.330 1.372 1.345 .009 +* C-O C-O 1.231 .020 187 1.206 1.251 1.230 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 170 1.499 1.555 1.524 .011 * * CH2G*-C (Gly) 1.516 .018 18 1.481 1.534 1.513 .012 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.503 1.530 1.518 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.533 1.583 1.554 .017 +* CH1E-CH2E (the rest) 1.530 .020 138 1.486 1.565 1.530 .015 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.399 1.488 1.450 .016 *** +* NH1-CH2G* (Gly) 1.451 .016 18 1.418 1.468 1.446 .011 ** * N-CH1E (Pro) 1.466 .015 18 1.438 1.491 1.465 .016 +* +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 2.0 152 113.77 118.71 116.24 .97 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.40 120.73 117.21 1.70 ** CH1E-C-N (Pro) 116.9 1.5 18 114.38 118.01 116.45 .87 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 119.97 124.51 123.01 .71 +* O-C-N (Pro) 122.0 1.4 18 122.18 123.87 122.88 .33 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.20 125.56 122.27 1.20 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.42 121.97 120.95 .65 C-N-CH1E (Pro) 122.6 5.0 18 119.93 125.27 122.63 1.31 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.95 122.26 120.67 .54 * CH2G*-C-O (Gly) 120.8 2.1 17 119.13 121.15 120.34 .67 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.78 111.32 110.53 .39 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.79 112.29 109.79 1.53 * * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.21 116.16 110.62 1.57 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.07 114.66 110.76 1.34 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 108.66 113.80 111.66 1.47 * N-CH1E-C (Pro) 111.8 2.5 18 108.60 115.63 112.32 1.86 * +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.74 111.08 110.53 .34 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 109.38 115.10 111.89 1.71 * ** N-CH1E-CH2E (Pro) 103.0 1.1 18 100.92 105.19 103.34 1.05 +* +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.54 116.79 110.54 1.81 ** +*** ------------------------------------------------------------------------------------------------------------- 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_8 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] 144 94.7% Residues in additional allowed regions [a,b,l,p] 8 5.3% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 94.7 83.8 10.0 1.1 BETTER 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 131 .8 .8 .2 .2 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 8.4 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 54 9.2 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 60 9.8 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 132 9.8 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 59 5.9 20.4 5.0 -2.9 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 10.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .85 2 Residue-by-residue listing for refined_8 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .06 Chi1-chi2 distribution -.02 Chi1 only .03 Chi3 & chi4 .45 Omega .15 ------ .14 ===== Main-chain covalent forces:- Main-chain bond lengths .30 Main-chain bond angles .41 ------ .36 ===== OVERALL AVERAGE .22 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.