Residue-by-residue listing for refined_17 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 - - - - - - - - - - - 177.5 - - - 2 SER 2 B - - -58.2 - - - - - - - 178.2 - 35.0 - 3 ASP 3 B 61.6 - - - - - - - - - 183.2 - 33.0 - 4 PRO 4 - - - - - -77.9 - - - - - 180.7 - 39.0 - * * * 5 GLY 5 h - - - - - - - - - - - 180.2 - - - 6 PRO 6 H - - - - - -53.9 -53.9 -35.2 - - - 180.1 - 39.0 - * * * 7 GLU 7 H A 59.2 - - 175.9 - -56.9 -33.2 - - - 182.5 - 34.6 - 8 ALA 8 H A - - - - - -71.4 -40.5 - - - 177.6 -1.6 33.6 - 9 ALA 9 H A - - - - - -70.7 -37.8 - - - 177.9 -1.0 34.3 - * * 10 ARG 10 H A - 184.5 - 191.1 - -63.8 -33.6 - - - 180.0 -2.6 34.5 - 11 LEU 11 H A - 175.2 - - - -62.4 -32.4 - - - 175.8 -1.7 34.8 - 12 ARG 12 H A - - -59.5 180.5 - -76.5 -42.1 - - - 185.0 -.9 34.9 - +* +* 13 PHE 13 H A - 172.4 - - - -74.2 -50.5 - - - 185.0 -2.2 34.8 - 14 ARG 14 H A - 180.2 - - - -77.2 -29.0 - - - 178.8 -3.8 33.0 - * ** ** 15 CYS 15 h A - - -59.5 - - - - - - - 177.4 -.6 32.5 - +* +* 16 PHE 16 t B - 179.6 - - - - - - - - 177.0 -.5 35.4 - ** ** 17 HIS 17 B 72.4 - - - - - - - - - 175.6 - 34.2 - 18 TYR 18 B - 166.9 - - - - - - - - 181.2 -.9 32.4 - * * 19 GLU 19 t B 49.1 - - 181.6 - - - - - - 182.1 -.7 32.7 - +* +* Residue-by-residue listing for refined_17 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 - - -64.5 170.2 - - - - - - 179.6 -.6 34.9 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.5 - 33.9 - 22 THR 22 T A - 196.3 - - - - - - - - 182.5 -1.0 34.5 - * * 23 GLY 23 h - - - - - - - - - - - 182.4 -.9 - - +* +* 24 PRO 24 H - - - - - -61.3 -61.3 -32.3 - - - 180.3 - 38.2 - * * 25 GLN 25 H A - - -84.4 - - -70.9 -43.9 - - - 178.3 - 32.2 - * * 26 GLU 26 H A - 182.1 - 166.9 - -68.7 -33.2 - - - 173.5 - 31.8 - * * 27 ALA 27 H A - - - - - -59.2 -43.5 - - - 176.1 -2.4 34.1 - 28 LEU 28 H A - - -65.4 177.2 - -60.1 -44.4 - - - 178.8 -2.0 34.3 - 29 ALA 29 H A - - - - - -56.3 -37.8 - - - 177.2 -2.0 33.8 - 30 GLN 30 H A - - -69.1 167.6 - -75.0 -47.1 - - - 178.4 -1.8 33.6 - 31 LEU 31 H A - - -70.6 171.8 - -58.8 -47.0 - - - 181.1 -3.2 33.3 - +* +* 32 ARG 32 H A 67.9 - - 187.7 - -64.8 -28.1 - - - 175.7 -3.7 31.8 - * ** ** 33 GLU 33 H A - 179.1 - 186.5 - -72.7 -51.1 - - - 182.7 -.7 36.7 - * +* +* 34 LEU 34 H A - - -59.0 177.2 - -63.0 -46.7 - - - 179.5 -2.9 33.9 - * * 35 CYS 35 H A 65.4 - - - - -65.0 -36.6 - - - 179.6 -3.6 33.5 - ** ** 36 ARG 36 H A - 173.2 - - - -68.5 -31.9 - - - 176.4 -1.1 30.9 - * * 37 GLN 37 H A - - -65.8 178.5 - -75.2 -18.4 - - - 178.6 -1.9 33.8 - +* +* 38 TRP 38 H A - 167.2 - - - -83.9 -57.2 - - - 181.2 -.9 33.3 - +* +* * +* 39 LEU 39 H A - - -52.6 - - -84.0 -41.8 - - - 178.9 -2.9 31.4 - +* * +* 40 ARG 40 h l - - -63.6 184.9 - - - - - - 176.7 -1.1 31.7 - * * 41 PRO 41 T - - - - - -62.5 - - - - - 176.8 - 38.7 - * * 42 GLU 42 T A 55.0 - - 184.1 - - - - - - 180.6 - 35.1 - 43 VAL 43 T a - - -60.5 - - - - - - - 181.6 -1.6 32.1 - 44 ARG 44 t B - - -70.5 185.7 - - - - - - 179.2 -3.6 32.3 - ** ** 45 SER 45 h B - - -57.9 - - - - - - - 184.8 - 34.2 - 46 LYS 46 H A - - -65.1 170.2 - -53.1 -40.9 - - - 184.4 - 35.8 - * * 47 GLU 47 H A 65.4 - - - - -72.9 -29.9 - - - 174.7 - 31.5 - 48 GLN 48 H A - - -68.0 171.1 - -72.4 -27.0 - - - 174.0 -.7 33.4 - * * +* +* 49 MET 49 H A - - -58.8 184.1 - -71.4 -37.5 - - - 172.5 -1.1 32.5 - * * * 50 LEU 50 H A - - -64.2 178.8 - -53.5 -49.9 - - - 183.4 -1.7 35.0 - 51 GLU 51 H A - 175.4 - 188.6 - -53.0 -54.3 - - - 182.0 -2.0 37.9 - * * * * 52 LEU 52 H A - - -60.6 178.5 - -62.9 -41.1 - - - 183.1 -1.9 34.6 - 53 LEU 53 H A - 183.0 - - - -77.1 -30.1 - - - 175.1 -2.2 31.5 - Residue-by-residue listing for refined_17 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 54 VAL 54 H A - 181.1 - - - -60.9 -43.7 - - - 181.1 -2.8 35.0 - * * 55 LEU 55 H A - 182.0 - - - -54.8 -42.7 - - - 181.8 -1.8 35.7 - 56 GLU 56 H A - - -67.4 - - -53.4 -52.4 - - - 182.2 -1.1 34.1 - * * * 57 GLN 57 H A - 189.2 - - - -74.4 -43.6 - - - 181.9 -1.2 33.9 - * * 58 PHE 58 H A - 177.2 - - - -53.7 -46.0 - - - 180.9 -2.7 34.0 - 59 LEU 59 H A - - -62.0 182.8 - -66.4 -35.7 - - - 180.0 -3.0 31.8 - * * 60 GLY 60 H - - - - - - -80.9 -18.6 - - - 178.0 -1.2 - - * +* * +* 61 ALA 61 H A - - - - - -75.0 -26.2 - - - 175.9 -1.9 33.7 - * * 62 LEU 62 h B - - -64.7 171.4 - - - - - - 176.7 -1.0 37.2 - * * 63 PRO 63 h - - - - - -66.7 - - - - - 183.1 - 39.3 - +* +* 64 PRO 64 H - - - - - -46.0 -46.0 -41.4 - - - 181.3 - 38.0 - +* +* * +* 65 GLU 65 H A 60.8 - - 183.8 - -68.2 -47.9 - - - 180.0 - 32.0 - 66 ILE 66 H A - - -61.0 179.4 - -68.4 -41.2 - - - 180.0 - 34.5 - 67 GLN 67 H A - 179.3 - 175.5 - -59.2 -41.2 - - - 180.0 -3.4 34.3 - +* +* 68 ALA 68 H A - - - - - -66.6 -30.8 - - - 177.5 -2.0 33.0 - 69 ARG 69 H A - - -67.8 - - -65.7 -37.3 - - - 174.9 -1.2 33.0 - * * 70 VAL 70 H A - 167.0 - - - -61.9 -46.6 - - - 184.8 -1.5 36.0 - 71 GLN 71 H A - - -55.8 - - -56.0 -27.6 - - - 177.3 -1.9 32.3 - * * 72 GLY 72 H - - - - - - -76.1 -24.4 - - - 182.8 -.9 - - * +* +* 73 GLN 73 H a - - -57.3 192.5 - -104.7 -50.6 - - - 190.3 -1.9 35.0 - *** +* *** 74 ARG 74 h l - - -67.7 - - - - - - - 178.3 -2.9 29.6 - * * * 75 PRO 75 - - - - - -58.0 - - - - - 178.8 - 39.2 - +* +* 76 GLY 76 S - - - - - - - - - - - 179.3 - - - 77 SER 77 h B 56.2 - - - - - - - - - 182.8 - 34.1 - 78 PRO 78 H - - - - - -60.8 -60.8 -44.5 - - - 181.3 - 37.9 - * * 79 GLU 79 H A - - -63.8 178.3 - -68.5 -29.9 - - - 175.4 - 30.9 - 80 GLU 80 H A - 183.0 - - - -67.8 -45.2 - - - 177.2 - 35.1 - 81 ALA 81 H A - - - - - -59.0 -41.7 - - - 179.4 -2.2 34.3 - 82 ALA 82 H A - - - - - -56.3 -30.7 - - - 180.4 -2.5 34.4 - 83 ALA 83 H A - - - - - -69.4 -50.4 - - - 178.6 -.9 33.2 - +* +* 84 LEU 84 H A 47.4 - - 155.1 - -69.3 -46.0 - - - 183.8 -1.3 29.5 - * * * * 85 VAL 85 H A - - -60.3 - - -64.6 -32.1 - - - 176.8 -2.8 29.7 - * * * 86 ASP 86 H A - 183.7 - - - -55.9 -45.3 - - - 180.1 -1.6 34.8 - 87 GLY 87 H - - - - - - -74.3 -38.3 - - - 180.6 -1.1 - - * * 88 LEU 88 H A - - -61.6 177.0 - -62.3 -22.5 - - - 177.1 -2.5 33.6 - * * Residue-by-residue listing for refined_17 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 - - -62.0 178.4 - -59.9 -42.4 - - - 183.6 -1.4 35.3 - 90 ARG 90 h XX - 193.6 - - - - - - - - 179.1 -1.1 32.6 - **** * **** 91 GLU 91 S B 61.4 - - 177.9 - - - - - - 173.1 -2.7 35.2 - * * 92 PRO 92 - - - - - -88.0 - - - - - 180.3 - 39.1 - ** * ** 93 GLY 93 - - - - - - - - - - - 181.8 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 178.8 - - - 96 SER 302 b - - -55.5 - - - - - - - 179.3 - 34.7 - 97 ASP 303 B 72.7 - - - - - - - - - 180.9 - 34.0 - 98 PRO 304 - - - - - -68.7 - - - - - 181.6 - 38.9 - * * 99 GLY 305 h - - - - - - - - - - - 183.5 - - - 100 PRO 306 H - - - - - -58.2 -58.2 -36.9 - - - 183.5 - 38.4 - * * 101 GLU 307 H A 83.4 - - - - -75.1 -24.7 - - - 172.9 - 27.1 - * * * +* +* 102 ALA 308 H A - - - - - -65.6 -27.3 - - - 174.8 -.7 33.5 - * +* +* 103 ALA 309 H A - - - - - -75.5 -32.7 - - - 174.6 -.9 33.1 - * * 104 ARG 310 H A - 176.0 - 185.3 - -59.9 -36.6 - - - 180.0 -1.3 34.9 - 105 LEU 311 H A - 172.6 - - - -61.8 -39.9 - - - 178.0 -1.5 35.0 - 106 ARG 312 H A - - -56.8 178.8 - -66.3 -48.4 - - - 179.5 -1.0 35.6 - * * 107 PHE 313 H A - 162.7 - - - -60.1 -49.5 - - - 182.8 -2.5 34.7 - * * 108 ARG 314 H A - 171.2 - 172.6 - -72.6 -18.0 - - - 177.6 -3.6 29.9 - +* ** * ** 109 CYS 315 h A - - -63.6 - - - - - - - 178.9 -1.1 32.4 - * * 110 PHE 316 t B - 178.1 - - - - - - - - 178.9 -1.3 34.9 - 111 HIS 317 B 73.1 - - - - - - - - - 175.0 - 34.7 - 112 TYR 318 B - 169.2 - - - - - - - - 178.7 -.9 32.5 - +* +* 113 GLU 319 t B 47.5 - - 174.2 - - - - - - 184.5 -.7 32.4 - * +* +* 114 GLU 320 T A - - -60.1 179.1 - - - - - - 181.3 -.6 34.4 - +* +* 115 ALA 321 T A - - - - - - - - - - 184.4 - 33.9 - 116 THR 322 T A - 198.9 - - - - - - - - 181.7 - 34.3 - 117 GLY 323 h - - - - - - - - - - - 185.5 -.8 - - +* +* 118 PRO 324 H - - - - - -82.3 -82.3 -31.8 - - - 185.2 - 39.0 - +* * * +* 119 GLN 325 H A - 191.1 - 170.2 - -78.1 -32.0 - - - 175.1 - 34.5 - * * 120 GLU 326 H A - 180.7 - 165.0 - -75.5 -32.5 - - - 171.6 - 31.9 - * * 121 ALA 327 H A - - - - - -62.9 -40.9 - - - 175.7 -1.2 34.2 - * * 122 LEU 328 H A - - -63.6 179.9 - -60.0 -38.5 - - - 177.9 -2.1 33.7 - 123 ALA 329 H A - - - - - -57.4 -37.2 - - - 178.4 -1.5 34.6 - 124 GLN 330 H A - - -69.7 167.6 - -78.5 -44.7 - - - 179.5 -1.2 34.3 - * * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 125 LEU 331 H A - - -71.0 171.6 - -64.4 -48.9 - - - 180.7 -3.0 32.5 - * * 126 ARG 332 H A 66.2 - - 179.2 - -65.4 -28.4 - - - 175.1 -3.6 29.3 - ** * ** 127 GLU 333 H A - 180.4 - 183.1 - -66.0 -50.3 - - - 182.4 -.6 36.4 - +* +* 128 LEU 334 H A - - -63.3 175.5 - -68.9 -42.1 - - - 177.7 -2.3 32.8 - 129 CYS 335 H A 67.8 - - - - -67.5 -29.6 - - - 177.0 -3.5 33.3 - +* +* 130 ARG 336 H A - 180.2 - - - -73.1 -30.3 - - - 174.2 -1.2 31.5 - * * * 131 GLN 337 H A - - -61.3 - - -68.4 -16.8 - - - 179.7 -1.5 34.9 - +* +* 132 TRP 338 H a - 164.2 - - - -94.8 -61.4 - - - 183.2 -.6 34.4 - * ** +* +* ** 133 LEU 339 H A - - -60.7 160.6 - -71.4 -38.3 - - - 178.7 -3.5 35.1 - ** ** 134 ARG 340 h l - - -57.0 181.7 - - - - - - 174.1 -1.5 31.3 - * * 135 PRO 341 T - - - - - -53.6 - - - - - 179.2 - 39.3 - * +* +* 136 GLU 342 T A 54.6 - - - - - - - - - 180.2 - 31.8 - 137 VAL 343 T A - - -57.2 - - - - - - - 178.4 -1.5 31.0 - 138 ARG 344 t B - - -72.3 187.0 - - - - - - 179.1 -3.9 32.4 - ** ** 139 SER 345 h B - - -55.7 - - - - - - - 183.9 - 34.8 - 140 LYS 346 H A - - -66.6 171.9 - -53.4 -41.1 - - - 184.6 - 34.2 - 141 GLU 347 H A 70.3 - - - - -64.7 -36.6 - - - 178.0 - 31.7 - 142 GLN 348 H A - - -67.1 162.9 - -70.9 -27.4 - - - 175.6 -.6 33.9 - * +* +* 143 MET 349 H A - - -63.0 179.5 - -69.4 -41.3 - - - 174.0 -1.1 32.8 - * * * 144 LEU 350 H A - - -79.5 - - -55.8 -46.5 - - - 180.4 -1.9 32.5 - 145 GLU 351 H A - 174.4 - 186.8 - -53.6 -52.3 - - - 179.9 -1.8 37.7 - * * * 146 LEU 352 H A - - -63.0 175.6 - -63.2 -38.0 - - - 182.3 -2.0 35.2 - 147 LEU 353 H A - 180.4 - - - -76.0 -30.9 - - - 176.2 -2.3 32.9 - 148 VAL 354 H A - 185.2 - - - -65.0 -42.9 - - - 178.2 -2.7 34.1 - 149 LEU 355 H A - 180.0 - - - -63.5 -37.2 - - - 182.8 -1.9 35.9 - 150 GLU 356 H A - 206.1 - - - -56.1 -54.2 - - - 180.5 -1.6 37.1 - * * * 151 GLN 357 H A - 173.9 - - - -74.5 -40.9 - - - 181.4 -1.8 32.2 - 152 PHE 358 H A - 180.8 - - - -55.5 -46.3 - - - 180.2 -2.6 33.5 - 153 LEU 359 H A - - -68.1 189.1 - -64.4 -39.0 - - - 179.4 -2.8 30.2 - * * * 154 GLY 360 H - - - - - - -80.5 -23.0 - - - 178.3 -1.3 - - * * * 155 ALA 361 H A - - - - - -68.5 -27.0 - - - 175.5 -2.5 33.4 - * * 156 LEU 362 h B - - -63.6 171.6 - - - - - - 176.5 -1.1 37.0 - * * 157 PRO 363 h - - - - - -67.3 - - - - - 182.6 - 39.1 - * * 158 PRO 364 H - - - - - -42.0 -42.0 -40.7 - - - 181.0 - 39.0 - ** +* * ** 159 GLU 365 H A 60.7 - - 185.3 - -69.5 -47.9 - - - 179.4 - 32.9 - 160 ILE 366 H A - - -61.7 178.4 - -67.6 -40.8 - - - 179.7 - 34.6 - Residue-by-residue listing for refined_17 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 161 GLN 367 H A - 180.0 - 176.7 - -61.2 -41.6 - - - 180.0 -3.4 34.2 - +* +* 162 ALA 368 H A - - - - - -60.7 -38.2 - - - 179.9 -2.1 34.1 - 163 ARG 369 H A - - -58.9 - - -63.8 -36.7 - - - 177.2 -1.5 34.7 - 164 VAL 370 H A - 169.9 - - - -65.3 -41.6 - - - 184.5 -1.4 35.9 - 165 GLN 371 H A - - -56.3 - - -58.3 -29.9 - - - 178.6 -1.8 34.9 - 166 GLY 372 h - - - - - - - - - - - 179.7 -1.0 - - * * 167 GLN 373 T a - - -54.4 191.0 - - - - - - 185.4 -2.4 34.1 - 168 ARG 374 t l - - -58.6 - - - - - - - 184.9 -3.1 31.9 - * * 169 PRO 375 - - - - - -56.5 - - - - - 181.6 - 38.5 - * * 170 GLY 376 S - - - - - - - - - - - 177.5 - - - 171 SER 377 h B 53.2 - - - - - - - - - 182.9 - 32.9 - 172 PRO 378 H - - - - - -55.1 -55.1 -45.3 - - - 183.9 - 38.5 - * * 173 GLU 379 H A - - -60.6 171.0 - -71.7 -31.0 - - - 176.1 - 32.9 - 174 GLU 380 H A - 181.1 - - - -65.1 -45.5 - - - 176.2 - 34.5 - 175 ALA 381 H A - - - - - -59.5 -45.8 - - - 179.2 -2.1 34.5 - 176 ALA 382 H A - - - - - -56.9 -35.5 - - - 179.4 -2.6 34.6 - 177 ALA 383 H A - - - - - -65.2 -49.4 - - - 177.7 -1.7 32.9 - 178 LEU 384 H A 49.1 - - 153.8 - -68.5 -43.3 - - - 183.1 -1.7 28.3 - * +* +* 179 VAL 385 H A - - -57.9 - - -63.3 -31.5 - - - 175.4 -2.8 30.1 - * * 180 ASP 386 H A - 178.0 - - - -52.3 -46.7 - - - 179.4 -1.7 35.2 - * * 181 GLY 387 H - - - - - - -78.7 -28.7 - - - 179.5 -.9 - - * * * 182 LEU 388 H A - - -61.4 176.5 - -67.8 -14.1 - - - 175.9 -1.9 33.4 - ** ** 183 ARG 389 h A - - -60.7 183.8 - - - - - - 182.1 -1.0 35.3 - * * 184 ARG 390 t XX - 193.5 - - - - - - - - 179.4 -2.0 32.0 - **** **** 185 GLU 391 S B 60.3 - - 184.3 - - - - - - 181.4 -2.3 33.0 - 186 PRO 392 S - - - - - -68.1 - - - - - 179.0 - 37.9 - * * 187 GLY 393 - - - - - - - - - - - 179.6 -1.1 - - * * 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * * ** *** ** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.7 179.6 -62.9 177.5 -62.6 -66.1 -38.4 - - - 179.5 -1.8 34.1 Standard deviations: 9.2 9.0 5.7 8.2 11.8 9.2 9.1 - - - 3.1 .9 2.3 Numbers of values: 24 46 62 65 18 123 123 0 0 0 186 128 170 0 Residue-by-residue listing for refined_17 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_17 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 - 1.237 1.503 - 1.459 - 116.44 120.76 - 111.98 - 122.77 2 SER 2 1.317 1.240 1.522 1.529 1.441 122.71 116.79 120.39 109.66 109.17 110.42 122.81 3 ASP 3 1.304 1.235 1.531 1.548 1.451 121.62 117.65 120.54 111.53 109.62 111.37 121.81 +* +* 4 PRO 4 1.347 1.242 1.538 1.530 1.480 123.25 116.27 121.00 110.19 113.35 102.63 122.71 5 GLY 5 1.310 1.239 1.507 - 1.425 120.80 118.02 119.92 - 110.83 - 122.07 * +* +* 6 PRO 6 1.344 1.236 1.538 1.536 1.473 122.92 115.36 121.35 110.34 111.58 102.96 123.25 * * 7 GLU 7 1.325 1.232 1.541 1.525 1.458 123.68 117.12 120.09 109.33 112.70 109.98 122.78 * * 8 ALA 8 1.331 1.235 1.515 1.519 1.458 121.72 115.53 121.28 110.95 110.42 110.61 123.17 9 ALA 9 1.314 1.235 1.516 1.507 1.444 121.69 115.53 121.42 110.70 109.23 110.10 123.02 * * 10 ARG 10 1.327 1.210 1.527 1.514 1.446 122.01 116.70 120.65 108.62 110.34 111.59 122.65 * * 11 LEU 11 1.324 1.224 1.534 1.524 1.419 122.98 116.08 121.35 112.18 110.07 107.94 122.56 ** * +* ** 12 ARG 12 1.313 1.226 1.531 1.529 1.446 121.52 115.01 121.41 109.50 109.60 110.50 123.55 * * 13 PHE 13 1.316 1.219 1.548 1.526 1.459 124.00 117.63 120.43 110.32 115.01 107.93 121.94 * * * +* +* Residue-by-residue listing for refined_17 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 1.308 1.227 1.527 1.549 1.461 121.32 116.33 121.05 111.70 111.00 110.69 122.60 +* +* 15 CYS 15 1.313 1.234 1.535 1.524 1.451 121.27 115.91 120.83 111.95 111.31 110.83 123.26 * * 16 PHE 16 1.337 1.242 1.519 1.548 1.462 123.05 116.51 120.59 109.89 109.47 109.63 122.86 17 HIS 17 1.310 1.241 1.506 1.572 1.436 120.62 117.50 119.92 110.05 107.36 112.43 122.57 * ** * * * ** 18 TYR 18 1.294 1.232 1.504 1.533 1.425 119.41 114.53 121.69 112.37 109.06 111.82 123.77 ** * +* * * ** 19 GLU 19 1.285 1.234 1.498 1.535 1.408 122.80 114.83 121.58 113.13 109.95 110.38 123.58 *** * +** +* *** 20 GLU 20 1.294 1.225 1.517 1.501 1.441 123.17 115.78 120.58 110.60 111.44 108.68 123.63 +** * * +** 21 ALA 21 1.321 1.230 1.532 1.516 1.446 122.87 117.51 120.05 110.33 112.26 110.16 122.44 22 THR 22 1.332 1.226 1.544 1.592 1.455 120.10 115.65 121.48 110.84 108.77 110.67 122.77 +* +* 23 GLY 23 1.330 1.237 1.522 - 1.446 121.38 119.33 119.72 - 110.71 - 120.95 * * * 24 PRO 24 1.348 1.224 1.528 1.511 1.466 122.07 117.46 120.12 110.18 113.90 103.60 122.41 25 GLN 25 1.332 1.229 1.509 1.537 1.459 120.09 115.79 121.13 109.67 110.51 113.99 123.07 ** ** 26 GLU 26 1.312 1.238 1.529 1.524 1.446 121.15 116.13 121.00 112.94 110.25 111.25 122.87 * * * 27 ALA 27 1.328 1.218 1.526 1.522 1.456 121.70 116.17 120.57 110.60 109.12 110.60 123.25 28 LEU 28 1.331 1.214 1.505 1.513 1.469 122.59 116.70 120.00 108.24 111.63 111.82 123.30 29 ALA 29 1.333 1.229 1.525 1.525 1.468 122.13 115.24 121.33 110.68 110.22 110.54 123.41 30 GLN 30 1.311 1.218 1.525 1.504 1.438 122.66 116.55 120.54 112.11 111.46 109.01 122.89 * * * * * 31 LEU 31 1.327 1.214 1.513 1.530 1.469 122.68 116.92 119.95 109.99 112.42 111.39 123.12 32 ARG 32 1.326 1.215 1.527 1.540 1.463 121.93 116.15 120.99 111.90 110.77 112.21 122.83 * * 33 GLU 33 1.312 1.229 1.525 1.528 1.448 122.43 115.39 120.89 109.22 108.68 108.27 123.66 * * * 34 LEU 34 1.322 1.228 1.522 1.531 1.450 123.00 116.90 120.28 110.49 111.64 110.42 122.81 35 CYS 35 1.329 1.220 1.536 1.549 1.444 121.35 116.92 120.96 111.36 110.05 110.74 122.08 36 ARG 36 1.327 1.212 1.516 1.538 1.429 121.54 116.99 120.05 114.59 111.92 110.45 122.95 +* ** ** 37 GLN 37 1.311 1.238 1.524 1.500 1.452 121.54 114.62 121.24 110.99 110.84 109.82 124.13 * * * 38 TRP 38 1.321 1.225 1.538 1.558 1.449 124.60 118.36 119.94 113.11 111.76 108.77 121.70 * +* * +* * +* 39 LEU 39 1.331 1.226 1.510 1.551 1.467 118.69 116.03 120.20 110.01 110.99 114.71 123.77 * +* ** ** 40 ARG 40 1.338 1.225 1.532 1.537 1.455 123.52 118.14 120.43 110.37 113.88 112.52 121.43 * * * 41 PRO 41 1.355 1.238 1.530 1.539 1.484 122.97 114.30 121.49 110.17 111.20 103.68 124.21 * +* +* +* 42 GLU 42 1.318 1.230 1.542 1.538 1.442 124.74 117.47 120.55 110.68 111.58 108.62 121.97 +* * +* 43 VAL 43 1.332 1.226 1.520 1.565 1.459 120.17 117.12 120.38 109.93 112.33 113.34 122.48 * * 44 ARG 44 1.319 1.234 1.498 1.528 1.451 121.04 114.26 121.43 109.55 113.01 113.03 124.31 * * * 45 SER 45 1.304 1.244 1.548 1.522 1.427 123.70 115.52 120.89 112.26 110.65 108.33 123.59 +* * +* * * * +* Residue-by-residue listing for refined_17 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 1.322 1.230 1.539 1.514 1.483 125.35 116.87 120.94 108.52 114.39 108.42 122.19 * ** * * ** 47 GLU 47 1.302 1.233 1.518 1.552 1.473 121.56 115.22 121.63 112.08 110.61 112.59 123.15 +* * * * +* 48 GLN 48 1.304 1.229 1.519 1.506 1.438 122.57 116.38 120.95 111.66 110.43 110.11 122.65 +* * * +* 49 MET 49 1.321 1.235 1.499 1.503 1.448 120.86 115.89 120.25 111.44 110.25 111.72 123.86 * * * 50 LEU 50 1.350 1.203 1.516 1.556 1.457 121.44 115.42 120.41 107.92 108.03 112.58 123.95 +* * * * * * +* 51 GLU 51 1.333 1.239 1.536 1.523 1.445 125.31 116.37 120.44 109.12 111.80 105.88 123.17 ** +** +** 52 LEU 52 1.317 1.228 1.520 1.528 1.442 122.23 116.05 121.06 110.24 111.35 109.75 122.87 53 LEU 53 1.307 1.235 1.555 1.515 1.418 121.68 117.76 120.11 115.31 113.11 108.06 122.13 +* * ** +** * +** 54 VAL 54 1.340 1.237 1.523 1.568 1.481 121.07 114.49 121.45 107.30 108.63 112.98 124.03 * * * 55 LEU 55 1.330 1.228 1.526 1.531 1.454 123.75 115.51 120.69 109.28 110.92 109.15 123.79 * * 56 GLU 56 1.322 1.240 1.508 1.517 1.458 123.49 116.41 120.32 109.88 113.44 109.96 123.26 57 GLN 57 1.309 1.228 1.508 1.538 1.440 120.97 115.89 120.17 111.93 109.01 110.00 123.90 * * 58 PHE 58 1.330 1.236 1.523 1.541 1.452 122.56 116.23 120.78 110.25 111.50 110.57 122.97 59 LEU 59 1.319 1.219 1.515 1.533 1.442 121.09 117.26 120.09 111.80 112.22 111.84 122.62 60 GLY 60 1.322 1.234 1.512 - 1.449 119.86 116.17 120.57 - 112.46 - 123.25 61 ALA 61 1.322 1.243 1.528 1.531 1.451 122.24 115.46 120.81 111.15 110.06 110.47 123.72 62 LEU 62 1.332 1.236 1.532 1.529 1.457 123.71 118.69 119.72 107.69 109.91 108.66 121.58 * * * * * 63 PRO 63 1.353 1.241 1.520 1.542 1.460 122.07 118.28 119.18 109.49 108.86 104.17 122.54 * * * 64 PRO 64 1.347 1.234 1.532 1.540 1.469 123.57 116.78 120.46 110.68 113.37 103.96 122.73 65 GLU 65 1.331 1.239 1.544 1.536 1.452 120.99 117.54 119.98 111.92 112.40 111.12 122.43 66 ILE 66 1.336 1.238 1.530 1.552 1.457 121.51 115.36 121.17 109.94 109.99 110.69 123.44 67 GLN 67 1.321 1.230 1.526 1.530 1.452 123.13 116.13 120.82 110.88 110.89 109.53 123.03 68 ALA 68 1.324 1.236 1.535 1.519 1.461 121.86 116.96 120.54 110.77 111.72 111.05 122.49 69 ARG 69 1.332 1.237 1.515 1.532 1.469 121.25 115.49 121.23 110.63 110.01 111.95 123.27 70 VAL 70 1.315 1.240 1.492 1.526 1.447 122.16 114.77 120.77 106.63 110.65 111.62 124.46 +* * +* 71 GLN 71 1.314 1.199 1.514 1.516 1.439 122.92 116.82 120.21 110.76 111.97 112.10 122.94 * +* +* 72 GLY 72 1.322 1.225 1.540 - 1.447 120.67 117.76 120.25 - 113.39 - 121.99 * * 73 GLN 73 1.335 1.225 1.521 1.527 1.469 120.78 115.41 120.97 106.71 112.72 112.06 123.62 +* +* 74 ARG 74 1.329 1.232 1.517 1.553 1.472 124.11 116.69 120.94 110.70 110.92 116.26 122.26 * * *** *** 75 PRO 75 1.347 1.227 1.533 1.541 1.468 123.07 115.54 121.17 110.03 112.36 103.02 123.29 76 GLY 76 1.321 1.226 1.514 - 1.448 121.63 116.53 120.48 - 112.86 - 122.98 77 SER 77 1.309 1.250 1.537 1.532 1.438 122.40 117.86 120.17 111.76 109.31 109.55 121.94 * * * 78 PRO 78 1.348 1.233 1.534 1.538 1.469 122.99 117.24 120.23 110.76 113.69 103.78 122.51 79 GLU 79 1.328 1.232 1.519 1.528 1.462 121.41 116.44 120.57 113.30 111.67 111.53 122.98 +* +* 80 GLU 80 1.326 1.223 1.535 1.524 1.450 121.71 116.40 120.83 110.11 108.27 109.82 122.76 * * Residue-by-residue listing for refined_17 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 1.352 1.231 1.515 1.516 1.459 121.92 115.32 120.68 110.10 110.47 110.34 123.97 +* +* 82 ALA 82 1.329 1.227 1.530 1.522 1.457 123.71 116.04 120.97 110.28 111.69 109.63 122.99 * * 83 ALA 83 1.305 1.240 1.524 1.511 1.449 122.21 117.30 120.12 110.90 111.37 110.72 122.57 +* +* 84 LEU 84 1.337 1.232 1.511 1.560 1.453 119.45 116.80 120.49 110.63 112.38 116.03 122.67 * * *** *** 85 VAL 85 1.327 1.228 1.517 1.540 1.454 120.83 117.16 119.71 111.19 113.20 114.65 123.12 +* +* 86 ASP 86 1.345 1.235 1.513 1.538 1.476 121.35 115.38 120.79 108.73 108.94 111.67 123.78 * * 87 GLY 87 1.325 1.231 1.516 - 1.444 121.73 116.39 120.38 - 112.34 - 123.22 88 LEU 88 1.333 1.227 1.527 1.536 1.475 122.75 116.78 120.28 109.89 112.02 111.12 122.94 89 ARG 89 1.332 1.240 1.514 1.523 1.467 121.82 115.26 120.34 107.66 110.56 111.37 124.40 * * 90 ARG 90 1.349 1.233 1.527 1.567 1.477 125.13 116.08 120.66 113.37 108.25 110.62 123.24 * +* * +* +* * +* 91 GLU 91 1.308 1.238 1.538 1.545 1.434 122.86 117.94 120.52 109.57 109.56 110.22 121.48 +* * +* 92 PRO 92 1.326 1.239 1.530 1.524 1.441 122.15 117.54 120.32 110.81 109.38 102.84 122.15 +* +* 93 GLY 93 1.298 1.232 1.496 - 1.440 119.74 115.53 120.78 - 111.69 - 123.69 ** * ** 94 GLY 94 1.304 1.244 1.501 - 1.437 121.78 - 119.32 - 110.46 - - +* +* 95 GLY 301 - 1.229 1.501 - 1.449 - 115.35 121.12 - 111.72 - 123.52 96 SER 302 1.302 1.242 1.531 1.530 1.433 122.20 117.27 120.25 110.88 108.81 109.78 122.47 +* * +* 97 ASP 303 1.305 1.232 1.525 1.544 1.441 121.20 118.19 119.90 110.86 108.88 110.96 121.88 +* +* 98 PRO 304 1.348 1.246 1.530 1.537 1.476 122.62 115.38 121.43 110.15 112.08 103.24 123.18 * * 99 GLY 305 1.304 1.241 1.505 - 1.420 121.51 118.15 119.92 - 110.42 - 121.92 +* +* +* 100 PRO 306 1.336 1.228 1.531 1.539 1.456 122.52 118.43 120.05 110.31 113.99 103.63 121.44 * * 101 GLU 307 1.329 1.235 1.535 1.560 1.451 118.93 116.02 121.18 116.14 111.29 114.05 122.80 * +* *** ** *** 102 ALA 308 1.329 1.239 1.535 1.523 1.459 121.99 116.17 121.01 110.66 109.62 111.23 122.82 103 ALA 309 1.337 1.232 1.520 1.522 1.453 121.71 116.01 120.78 110.89 109.03 111.79 123.19 104 ARG 310 1.344 1.218 1.514 1.532 1.467 121.93 115.72 120.98 107.86 109.53 112.16 123.30 * * * 105 LEU 311 1.321 1.218 1.532 1.521 1.410 123.24 116.15 120.66 112.08 110.17 107.75 123.14 +** * +* +** 106 ARG 312 1.323 1.233 1.532 1.531 1.462 121.98 114.51 121.62 109.67 109.07 109.39 123.81 107 PHE 313 1.314 1.217 1.543 1.535 1.456 124.69 117.21 120.71 111.81 113.21 107.40 122.06 * +* +* +* 108 ARG 314 1.309 1.243 1.552 1.557 1.452 121.65 117.32 120.73 114.35 113.43 111.12 121.91 * * * ** ** 109 CYS 315 1.319 1.232 1.533 1.528 1.467 120.96 116.21 120.60 110.92 111.77 111.75 123.19 110 PHE 316 1.328 1.243 1.531 1.539 1.457 122.68 116.71 120.72 110.52 110.22 109.41 122.57 111 HIS 317 1.308 1.232 1.505 1.564 1.446 120.74 117.74 119.90 109.32 108.28 111.98 122.36 +* +* * +* Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 112 TYR 318 1.302 1.237 1.502 1.534 1.430 118.95 114.67 121.49 111.91 108.99 112.02 123.82 +* * * +* +* 113 GLU 319 1.285 1.236 1.511 1.540 1.415 122.96 115.20 121.38 113.29 109.47 110.75 123.41 *** ** +* *** 114 GLU 320 1.305 1.228 1.517 1.524 1.445 123.05 115.77 120.72 110.54 111.24 109.73 123.50 +* +* 115 ALA 321 1.316 1.230 1.526 1.512 1.448 122.81 117.18 120.26 110.14 112.61 110.18 122.54 116 THR 322 1.319 1.225 1.544 1.576 1.453 120.67 116.20 121.04 110.81 109.69 110.54 122.73 * * 117 GLY 323 1.321 1.230 1.508 - 1.442 120.64 119.88 119.69 - 109.86 - 120.40 +* +* +* 118 PRO 324 1.324 1.219 1.511 1.508 1.445 120.78 115.55 121.36 110.36 112.58 102.85 123.07 * * * * 119 GLN 325 1.290 1.227 1.523 1.495 1.403 123.06 115.91 121.12 114.06 110.04 106.37 122.93 +** +* +** ** ** +** 120 GLU 326 1.321 1.238 1.523 1.523 1.439 121.68 115.58 121.58 113.76 109.06 110.80 122.84 * +* +* 121 ALA 327 1.326 1.219 1.530 1.520 1.447 121.42 116.23 120.70 110.73 108.65 110.52 123.05 122 LEU 328 1.340 1.217 1.513 1.528 1.470 122.55 116.91 119.91 108.58 111.45 112.45 123.18 * * 123 ALA 329 1.333 1.235 1.520 1.524 1.470 122.25 114.93 121.51 109.81 110.07 110.37 123.56 124 GLN 330 1.305 1.226 1.530 1.504 1.428 123.62 116.13 120.88 112.21 111.36 108.03 122.98 +* * +* * * * +* 125 LEU 331 1.319 1.221 1.505 1.514 1.464 123.11 117.95 119.50 110.48 113.84 111.31 122.54 126 ARG 332 1.332 1.197 1.505 1.546 1.457 119.93 115.87 120.88 112.58 110.77 115.00 123.25 +* * +** +** 127 GLU 333 1.305 1.225 1.532 1.522 1.443 122.71 115.77 120.94 109.76 109.23 108.07 123.25 +* * +* 128 LEU 334 1.320 1.228 1.517 1.520 1.454 122.85 117.43 120.11 111.27 112.80 110.50 122.46 129 CYS 335 1.322 1.216 1.529 1.534 1.450 120.35 116.42 121.07 110.73 109.16 111.73 122.51 130 ARG 336 1.329 1.204 1.532 1.544 1.419 122.32 117.38 120.04 114.92 110.43 109.95 122.57 * ** +** +** 131 GLN 337 1.336 1.228 1.536 1.542 1.482 121.77 114.84 121.53 108.74 109.52 111.18 123.63 * * 132 TRP 338 1.306 1.223 1.552 1.552 1.441 124.85 116.72 120.68 113.12 111.66 107.21 122.58 +* * * +* +* +* +* 133 LEU 339 1.313 1.228 1.526 1.529 1.465 122.93 114.73 120.91 111.35 110.74 107.90 124.35 * +* +* 134 ARG 340 1.323 1.214 1.533 1.540 1.467 125.69 118.54 119.90 110.21 114.88 112.75 121.52 ** * * * ** 135 PRO 341 1.351 1.241 1.533 1.525 1.478 123.21 116.26 120.69 109.32 112.94 103.22 123.04 136 GLU 342 1.326 1.240 1.535 1.540 1.437 122.00 117.55 120.32 110.55 112.82 112.76 122.12 * * * 137 VAL 343 1.330 1.221 1.524 1.554 1.465 119.98 117.04 120.56 110.80 112.76 113.61 122.40 * * 138 ARG 344 1.314 1.232 1.493 1.540 1.445 121.02 115.03 121.25 109.53 111.06 113.83 123.71 * +* +* +* 139 SER 345 1.287 1.250 1.522 1.523 1.419 123.09 115.45 120.57 112.39 109.03 108.16 123.97 *** ** * * *** 140 LYS 346 1.304 1.224 1.528 1.513 1.453 124.46 117.49 120.04 110.39 114.29 108.92 122.43 +* +* * +* 141 GLU 347 1.319 1.237 1.532 1.553 1.473 120.71 115.05 121.37 111.28 110.93 112.85 123.54 * * * 142 GLN 348 1.314 1.227 1.525 1.512 1.446 123.63 116.73 120.64 111.60 111.22 109.14 122.62 * * * Residue-by-residue listing for refined_17 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 1.321 1.229 1.494 1.497 1.457 121.26 116.14 120.24 111.28 110.92 111.02 123.61 * +* +* 144 LEU 350 1.338 1.198 1.506 1.555 1.458 121.05 115.96 120.01 110.40 109.79 113.27 123.86 +* * +* +* 145 GLU 351 1.322 1.242 1.541 1.515 1.446 124.76 116.06 120.86 109.69 111.21 105.55 123.07 +* +** +** 146 LEU 352 1.321 1.232 1.518 1.523 1.445 122.58 115.68 121.14 109.68 111.06 109.51 123.17 147 LEU 353 1.307 1.234 1.536 1.507 1.423 122.07 117.40 120.38 113.16 112.62 108.58 122.22 +* * +* +* * +* 148 VAL 354 1.322 1.231 1.530 1.560 1.456 120.42 114.89 121.49 108.94 107.97 112.96 123.59 * * 149 LEU 355 1.329 1.231 1.530 1.535 1.456 123.30 115.28 120.78 109.12 110.55 109.22 123.93 150 GLU 356 1.330 1.237 1.543 1.557 1.473 123.93 116.01 120.93 108.84 109.21 108.06 123.00 * * * * 151 GLN 357 1.324 1.216 1.500 1.535 1.449 121.20 116.83 119.93 111.48 111.52 111.84 123.21 * * 152 PHE 358 1.321 1.231 1.523 1.526 1.452 121.48 116.22 120.63 110.41 111.26 111.11 123.12 153 LEU 359 1.320 1.217 1.514 1.535 1.440 121.21 117.49 119.74 112.85 113.31 112.36 122.74 * * * 154 GLY 360 1.319 1.231 1.516 - 1.451 119.52 116.43 120.44 - 112.65 - 123.13 155 ALA 361 1.334 1.233 1.520 1.531 1.457 122.30 115.78 120.95 110.92 110.18 111.04 123.27 156 LEU 362 1.319 1.243 1.527 1.518 1.444 122.64 118.30 119.96 107.75 109.32 109.00 121.74 * * * 157 PRO 363 1.340 1.239 1.515 1.531 1.448 121.82 117.83 119.36 109.45 108.78 104.49 122.82 * * * * 158 PRO 364 1.339 1.229 1.535 1.509 1.471 124.06 117.12 119.96 109.99 114.59 102.51 122.91 * * * 159 GLU 365 1.331 1.231 1.547 1.535 1.459 121.48 117.17 120.38 111.79 111.77 110.33 122.39 * * 160 ILE 366 1.344 1.235 1.517 1.551 1.457 121.53 115.07 121.33 109.77 109.64 110.86 123.56 * * 161 GLN 367 1.316 1.223 1.521 1.524 1.441 122.69 116.14 120.43 110.69 110.57 110.06 123.41 162 ALA 368 1.329 1.228 1.522 1.515 1.466 122.84 116.01 120.84 110.09 111.38 110.26 123.13 163 ARG 369 1.320 1.236 1.523 1.519 1.461 122.20 115.26 121.33 109.80 110.13 110.10 123.41 164 VAL 370 1.319 1.240 1.507 1.538 1.451 122.97 114.90 121.10 107.64 110.72 110.74 124.00 165 GLN 371 1.307 1.224 1.528 1.509 1.446 123.27 116.16 120.69 109.72 111.31 109.58 123.15 +* * +* 166 GLY 372 1.328 1.241 1.531 - 1.451 121.37 116.95 120.79 - 112.93 - 122.26 167 GLN 373 1.323 1.231 1.525 1.518 1.443 120.93 115.67 120.53 109.06 111.69 111.38 123.79 168 ARG 374 1.342 1.232 1.547 1.548 1.479 124.14 116.88 120.87 111.27 110.09 112.74 122.16 * * * * * 169 PRO 375 1.359 1.231 1.531 1.535 1.497 124.28 116.31 120.77 110.09 115.47 103.08 122.91 * ** * ** 170 GLY 376 1.303 1.227 1.520 - 1.454 121.00 116.69 120.52 - 112.54 - 122.78 +* +* 171 SER 377 1.312 1.247 1.545 1.534 1.437 121.89 117.51 120.41 112.74 110.12 110.10 122.02 * * * * 172 PRO 378 1.359 1.231 1.537 1.544 1.477 123.45 117.34 120.26 109.83 114.77 103.73 122.38 * * * 173 GLU 379 1.323 1.234 1.506 1.513 1.471 121.30 115.90 120.61 111.72 111.38 110.35 123.47 174 GLU 380 1.317 1.223 1.528 1.527 1.443 121.72 116.09 120.69 111.49 108.49 109.50 123.18 175 ALA 381 1.342 1.232 1.522 1.514 1.459 122.20 115.53 120.82 109.93 110.36 110.19 123.63 176 ALA 382 1.331 1.228 1.529 1.522 1.461 123.41 115.18 121.30 110.31 111.19 109.51 123.52 177 ALA 383 1.296 1.235 1.525 1.515 1.446 123.50 118.20 119.55 111.03 111.81 111.01 122.24 ** * ** Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 178 LEU 384 1.349 1.234 1.504 1.560 1.462 118.69 116.73 120.13 110.55 112.69 117.37 123.11 * * * +* **** **** 179 VAL 385 1.326 1.222 1.512 1.532 1.460 121.37 116.47 120.07 111.15 112.77 114.36 123.46 +* +* 180 ASP 386 1.329 1.233 1.520 1.528 1.468 122.37 115.48 120.91 108.93 109.88 110.44 123.58 181 GLY 387 1.326 1.234 1.516 - 1.444 121.32 116.32 120.81 - 112.04 - 122.85 182 LEU 388 1.329 1.226 1.520 1.527 1.469 122.57 116.11 120.52 110.03 111.38 111.40 123.37 183 ARG 389 1.338 1.237 1.520 1.537 1.466 122.48 115.04 120.58 108.10 109.99 111.26 124.37 * * 184 ARG 390 1.350 1.235 1.511 1.576 1.459 125.55 116.71 120.35 114.06 107.50 111.36 122.89 * ** ** ** * ** 185 GLU 391 1.298 1.244 1.533 1.534 1.431 121.19 117.33 120.50 112.40 109.60 110.56 122.13 ** * * ** 186 PRO 392 1.342 1.246 1.529 1.536 1.458 122.68 115.96 121.18 110.65 113.04 104.19 122.83 * * 187 GLY 393 1.309 1.235 1.492 - 1.431 121.24 115.89 120.20 - 111.44 - 123.91 * * * * 188 GLY 394 1.303 - 1.493 - 1.420 122.35 - - - 109.54 - - +* * +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* ** +** ** +* *** * **** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 1.285 1.352 1.321 .013 *** +* C-N (Pro) 1.341 .016 18 1.324 1.359 1.345 .009 * * C-O C-O 1.231 .020 187 1.197 1.250 1.230 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.492 1.555 1.524 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.492 1.540 1.511 .012 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.507 1.531 1.519 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.526 1.592 1.555 .018 +* CH1E-CH2E (the rest) 1.530 .020 138 1.495 1.576 1.532 .015 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.403 1.483 1.451 .015 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.420 1.459 1.442 .011 +* N-CH1E (Pro) 1.466 .015 18 1.441 1.497 1.468 .014 +* ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 114.26 118.69 116.30 .97 * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.35 119.88 116.99 1.26 +* CH1E-C-N (Pro) 116.9 1.5 18 114.30 118.43 116.61 1.10 +* * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.40 124.46 122.97 .70 +* O-C-N (Pro) 122.0 1.4 18 121.44 124.21 122.80 .55 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.69 125.69 122.18 1.36 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.52 122.35 121.03 .77 * C-N-CH1E (Pro) 122.6 5.0 18 120.78 124.28 122.80 .82 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.18 121.69 120.66 .52 CH2G*-C-O (Gly) 120.8 2.1 17 119.32 121.12 120.33 .47 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.81 111.15 110.55 .38 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.63 111.19 109.58 1.53 * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.71 116.14 110.79 1.65 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.36 115.01 110.79 1.52 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.54 113.39 111.66 1.09 * N-CH1E-C (Pro) 111.8 2.5 18 108.78 115.47 112.55 1.91 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.51 111.79 110.51 .52 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.54 114.65 112.25 1.49 +* N-CH1E-CH2E (Pro) 103.0 1.1 18 102.51 104.49 103.42 .56 * NH1-CH1E-CH2E (the rest) 110.5 1.7 120 105.55 117.37 110.64 2.00 +** **** ------------------------------------------------------------------------------------------------------------- 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_17 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] 141 92.8% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 2 1.3% ---- ------ 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 92.8 83.8 10.0 .9 Inside b. Omega angle st dev 186 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.3 3.1 1.6 -.5 Inside e. H-bond energy st dev 128 .9 .8 .2 .3 Inside f. Overall G-factor 188 .2 -.4 .3 1.9 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 24 9.2 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 46 9.0 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 62 5.7 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 132 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 65 8.2 20.4 5.0 -2.4 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% 92.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 6.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 3 Residue-by-residue listing for refined_17 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .11 Chi1-chi2 distribution -.04 Chi1 only -.04 Chi3 & chi4 .39 Omega .06 ------ .10 ===== Main-chain covalent forces:- Main-chain bond lengths .28 Main-chain bond angles .38 ------ .34 ===== OVERALL AVERAGE .19 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.