Residue-by-residue listing for refined_7 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 - - - - - - - - - - - 172.9 - - - * * 2 SER 2 b - - -58.7 - - - - - - - 187.8 - 33.4 - * * 3 ASP 3 B - - -59.1 - - - - - - - 181.4 -1.4 34.3 - 4 PRO 4 - - - - - -73.6 - - - - - 180.5 - 38.6 - * * 5 GLY 5 h - - - - - - - - - - - 183.3 - - - 6 PRO 6 H - - - - - -61.3 -61.3 -36.0 - - - 178.1 - 38.3 - * * 7 GLU 7 H A - - -87.1 - - -65.6 -47.2 - - - 179.9 - 32.1 - * * 8 ALA 8 H A - - - - - -64.7 -43.3 - - - 179.5 - 33.7 - 9 ALA 9 H A - - - - - -67.1 -43.2 - - - 177.6 -2.6 33.3 - 10 ARG 10 H A - 174.6 - 169.7 - -64.6 -34.1 - - - 179.5 -2.8 33.1 - * * 11 LEU 11 H A - 177.7 - - - -62.6 -47.6 - - - 177.2 -2.3 34.9 - 12 ARG 12 H A - - -60.5 177.1 - -55.9 -47.6 - - - 181.9 -2.0 36.4 - 13 PHE 13 H A - 175.5 - - - -63.5 -43.4 - - - 180.1 -2.1 34.6 - 14 ARG 14 H A - - -66.9 - - -77.8 -27.1 - - - 179.2 -2.9 32.3 - * * * * 15 CYS 15 h A - - -58.9 - - - - - - - 177.3 -2.3 33.4 - 16 PHE 16 B - 181.1 - - - - - - - - 179.8 - 35.1 - 17 HIS 17 B 74.4 - - - - - - - - - 176.4 - 34.2 - 18 TYR 18 B - 169.1 - - - - - - - - 180.4 -.9 32.0 - +* +* 19 GLU 19 t B 47.9 - - 178.8 - - - - - - 184.5 -.7 33.2 - * +* +* Residue-by-residue listing for refined_7 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 GLU 20 T A - - -58.3 177.2 - - - - - - 180.8 -.5 34.7 - ** ** 21 ALA 21 T A - - - - - - - - - - 180.5 - 33.6 - 22 THR 22 T A - 198.5 - - - - - - - - 182.9 -.8 34.4 - +* +* 23 GLY 23 h - - - - - - - - - - - 183.2 -.8 - - +* +* 24 PRO 24 H - - - - - -68.5 -68.5 -30.0 - - - 182.4 - 38.4 - * * 25 GLN 25 H A - 212.8 - - - -65.2 -46.2 - - - 180.0 - 37.1 - +* +* 26 GLU 26 H A - 176.8 - 168.1 - -73.6 -33.0 - - - 173.5 - 32.5 - * * 27 ALA 27 H A - - - - - -57.4 -42.6 - - - 176.2 -2.2 34.0 - 28 LEU 28 H A - - -66.3 179.5 - -60.9 -43.2 - - - 179.6 -2.3 33.7 - 29 ALA 29 H A - - - - - -58.3 -37.0 - - - 177.0 -1.5 34.0 - 30 GLN 30 H A - - -70.5 167.2 - -73.8 -48.5 - - - 179.4 -1.9 33.7 - 31 LEU 31 H A - - -70.1 169.7 - -61.4 -45.3 - - - 181.2 -3.1 33.1 - * * 32 ARG 32 H A 63.0 - - 182.2 - -66.3 -29.2 - - - 175.4 -3.6 30.1 - ** * ** 33 GLU 33 H A - 177.3 - - - -71.4 -50.6 - - - 181.6 -.8 36.2 - +* +* 34 LEU 34 H A - - -61.3 176.1 - -63.9 -42.1 - - - 176.2 -2.8 33.0 - 35 CYS 35 H A - 180.3 - - - -64.7 -32.9 - - - 178.0 -3.4 34.3 - +* +* 36 ARG 36 H A - 186.7 - - - -72.3 -38.3 - - - 175.5 -1.0 33.0 - * * 37 GLN 37 H A - - -62.2 185.3 - -61.0 -32.9 - - - 179.0 -2.5 35.4 - 38 TRP 38 H A - 163.2 - - - -79.7 -59.4 - - - 182.9 -1.6 31.9 - * * +* +* 39 LEU 39 H A - - -61.2 181.3 - -73.0 -45.8 - - - 182.4 -3.6 32.9 - ** ** 40 ARG 40 h l - - -53.8 191.9 - - - - - - 183.2 -1.5 30.2 - * * 41 PRO 41 T - - - - - -70.7 - - - - - 182.6 - 39.0 - * * 42 GLU 42 T A 58.8 - - - - - - - - - 179.4 - 30.4 - 43 VAL 43 T A - - -60.2 - - - - - - - 180.2 -.8 31.9 - +* +* 44 ARG 44 t B - - -64.1 178.8 - - - - - - 181.1 -2.6 33.4 - 45 SER 45 h B - - -54.3 - - - - - - - 180.8 - 35.0 - 46 LYS 46 H A 65.1 - - - - -52.3 -44.0 - - - 185.4 - 34.8 - * * 47 GLU 47 H A 53.7 - - 183.7 - -60.8 -32.9 - - - 176.6 - 31.1 - 48 GLN 48 H A - - -68.3 - - -70.4 -30.5 - - - 180.7 -.8 33.2 - +* +* 49 MET 49 H A - - -57.4 181.6 - -72.6 -42.9 - - - 171.7 -1.0 32.8 - * * * 50 LEU 50 H A - - -77.8 - - -54.3 -50.5 - - - 180.8 -2.1 34.1 - 51 GLU 51 H A - 181.4 - 180.4 - -54.5 -51.0 - - - 180.3 -2.2 35.7 - * * 52 LEU 52 H A - - -62.6 177.0 - -65.2 -43.7 - - - 182.9 -2.6 34.3 - 53 LEU 53 H A - 183.7 - - - -73.6 -30.4 - - - 172.5 -2.9 31.4 - * * * 54 VAL 54 H A - 174.1 - - - -66.0 -43.4 - - - 177.0 -2.9 33.8 - * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 LEU 55 H A - 180.4 - - - -55.9 -39.6 - - - 180.5 -2.1 35.7 - 56 GLU 56 H A - 184.8 - - - -57.1 -53.1 - - - 181.6 -1.7 36.0 - * * 57 GLN 57 H A - 178.7 - - - -72.1 -41.6 - - - 180.3 -1.6 33.1 - 58 PHE 58 H A - 177.4 - - - -56.9 -48.2 - - - 181.5 -3.1 33.4 - * * 59 LEU 59 H A - - -62.9 184.4 - -66.2 -37.3 - - - 179.4 -2.9 31.5 - * * 60 GLY 60 H - - - - - - -80.5 -18.5 - - - 177.4 -1.7 - - * +* +* 61 ALA 61 H A - - - - - -75.1 -27.1 - - - 174.9 -2.0 33.4 - * * 62 LEU 62 h b - - -66.7 170.2 - - - - - - 176.1 -1.2 37.4 - * * * 63 PRO 63 h - - - - - -66.8 - - - - - 182.2 - 39.4 - +* +* 64 PRO 64 H - - - - - -43.8 -43.8 -41.2 - - - 179.1 - 39.0 - +* +* * +* 65 GLU 65 H A 50.3 - - 189.1 - -60.6 -48.3 - - - 177.3 - 33.3 - 66 ILE 66 H A - - -63.3 179.9 - -73.4 -40.4 - - - 181.1 -.7 35.2 - +* +* 67 GLN 67 H A - 178.2 - 177.8 - -58.1 -43.8 - - - 179.8 -3.5 34.7 - +* +* 68 ALA 68 H A - - - - - -65.0 -34.9 - - - 178.9 -2.8 33.4 - 69 ARG 69 H A - - -64.3 - - -63.6 -37.7 - - - 176.1 -1.0 33.9 - * * 70 VAL 70 H A - 168.2 - - - -57.8 -47.2 - - - 187.1 -1.6 36.0 - * * 71 GLN 71 H A - - -46.3 - - -63.2 -28.6 - - - 177.5 -1.5 32.4 - * * 72 GLY 72 H - - - - - - -69.9 -21.0 - - - 180.8 -1.2 - - +* * +* 73 GLN 73 H a - - -50.7 193.4 - -107.4 -43.0 - - - 184.0 -1.8 34.7 - * +*** +*** 74 ARG 74 h l - - -55.5 - - - - - - - 179.9 -3.6 33.1 - ** ** 75 PRO 75 - - - - - -62.0 - - - - - 179.9 - 38.8 - * * 76 GLY 76 S - - - - - - - - - - - 178.8 - - - 77 SER 77 h B 52.5 - - - - - - - - - 184.8 - 33.1 - 78 PRO 78 H - - - - - -58.8 -58.8 -44.5 - - - 181.5 - 36.9 - 79 GLU 79 H A - - -60.4 168.4 - -70.7 -29.4 - - - 175.4 - 32.4 - 80 GLU 80 H A - 187.0 - - - -69.0 -42.8 - - - 177.1 - 35.3 - 81 ALA 81 H A - - - - - -60.0 -41.0 - - - 178.4 -2.3 34.2 - 82 ALA 82 H A - - - - - -53.8 -41.2 - - - 180.7 -2.3 35.1 - 83 ALA 83 H A - - - - - -62.8 -41.3 - - - 176.8 -1.2 32.5 - * * 84 LEU 84 H A 48.0 - - 154.3 - -75.7 -43.4 - - - 182.4 -1.1 29.1 - * * * * * 85 VAL 85 H A - - -59.9 - - -62.3 -32.5 - - - 175.5 -2.8 30.4 - * * * 86 ASP 86 H A - 180.5 - - - -57.3 -41.1 - - - 181.2 -2.3 35.9 - 87 GLY 87 H - - - - - - -84.2 -15.8 - - - 181.5 -.9 - - +* ** +* ** 88 LEU 88 H A - - -61.0 175.8 - -86.0 -8.1 - - - 183.8 -1.2 34.6 - +* +** * +** Residue-by-residue listing for refined_7 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 - - -64.5 182.3 - - - - - - 175.3 -.7 33.6 - +* +* 90 ARG 90 T a 58.5 - - - - - - - - - 175.5 - 29.0 - * * 91 GLU 91 t b - 185.2 - 185.7 - - - - - - 182.8 -2.1 34.0 - 92 PRO 92 - - - - - -90.8 - - - - - 179.0 - 39.1 - ** * ** 93 GLY 93 - - - - - - - - - - - 178.2 -.6 - - +* +* 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 178.9 - - - 96 SER 302 B - - -56.2 - - - - - - - 181.7 - 35.0 - 97 ASP 303 B - - -64.8 - - - - - - - 173.9 - 33.8 - * * 98 PRO 304 S - - - - - -84.3 - - - - - 185.2 - 39.5 - +* +* +* 99 GLY 305 h - - - - - - - - - - - 180.9 - - - 100 PRO 306 H - - - - - -59.1 -59.1 -33.0 - - - 177.1 - 38.2 - * * 101 GLU 307 H A - - -61.8 - - -66.8 -40.6 - - - 176.7 - 33.2 - 102 ALA 308 H A - - - - - -66.8 -38.2 - - - 177.2 - 34.5 - 103 ALA 309 H A - - - - - -60.0 -45.4 - - - 178.6 -2.6 34.7 - 104 ARG 310 H A - 186.8 - 193.8 - -63.0 -36.3 - - - 180.2 -2.4 35.1 - 105 LEU 311 H A - 173.3 - - - -64.6 -45.6 - - - 177.9 -1.7 34.5 - 106 ARG 312 H A - - -58.5 180.4 - -60.4 -39.1 - - - 177.9 -2.5 35.0 - 107 PHE 313 H A - 175.6 - - - -65.8 -46.5 - - - 177.5 -2.1 34.7 - 108 ARG 314 H A - - -78.9 - - -68.7 -28.7 - - - 180.2 -3.0 33.2 - * * 109 CYS 315 h A - - -60.9 - - - - - - - 181.2 -2.2 33.7 - 110 PHE 316 t B - 184.1 - - - - - - - - 177.0 -.7 34.3 - +* +* 111 HIS 317 B 72.7 - - - - - - - - - 173.7 - 34.3 - * * 112 TYR 318 B - 166.2 - - - - - - - - 179.7 -1.2 32.6 - * * * 113 GLU 319 t B 54.4 - - 174.6 - - - - - - 181.9 -.8 32.5 - +* +* 114 GLU 320 T A - - -65.8 176.6 - - - - - - 180.1 -.5 34.2 - ** ** 115 ALA 321 T A - - - - - - - - - - 182.5 - 33.6 - 116 THR 322 T A - 200.3 - - - - - - - - 181.2 -.8 33.8 - +* +* 117 GLY 323 h - - - - - - - - - - - 185.1 -1.0 - - * * 118 PRO 324 H - - - - - -62.9 -62.9 -41.0 - - - 181.8 - 37.2 - 119 GLN 325 H A - - -83.7 153.9 - -74.9 -29.4 - - - 173.7 - 29.3 - * * * * * 120 GLU 326 H A - 175.7 - 170.3 - -74.8 -33.2 - - - 173.5 - 32.1 - * * 121 ALA 327 H A - - - - - -65.5 -40.0 - - - 178.3 -2.2 34.5 - 122 LEU 328 H A - - -67.0 176.8 - -61.5 -40.1 - - - 178.4 -2.3 33.5 - 123 ALA 329 H A - - - - - -57.7 -47.8 - - - 176.9 -1.7 34.1 - 124 GLN 330 H A - - -70.5 171.5 - -62.6 -48.6 - - - 178.7 -1.6 34.4 - 125 LEU 331 H A - - -70.2 170.7 - -59.2 -46.7 - - - 178.8 -3.1 32.1 - * * 126 ARG 332 H A 56.0 - - 186.5 - -71.0 -29.1 - - - 173.0 -3.6 26.3 - * ** ** ** Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 127 GLU 333 H A - 179.4 - 178.4 - -64.4 -50.1 - - - 180.9 -2.0 35.0 - 128 LEU 334 H A - - -59.8 179.1 - -67.0 -43.9 - - - 178.3 -3.1 33.7 - * * 129 CYS 335 H A - 187.3 - - - -61.5 -39.4 - - - 174.8 -3.3 34.2 - +* +* 130 ARG 336 H A - 178.8 - - - -58.5 -40.7 - - - 182.7 -1.9 31.7 - 131 GLN 337 H A - - -50.1 - - -67.6 -21.3 - - - 180.7 -1.6 34.7 - * +* +* 132 TRP 338 H a - 164.5 - - - -92.4 -51.7 - - - 181.1 -1.0 33.6 - * ** * * ** 133 LEU 339 H A - - -61.1 172.4 - -80.1 -40.8 - - - 181.4 -3.5 33.7 - * +* +* 134 ARG 340 h l - - -61.6 186.6 - - - - - - 184.1 -2.0 28.5 - +* +* 135 PRO 341 T - - - - - -65.3 - - - - - 181.0 - 38.3 - * * 136 GLU 342 T A 61.3 - - - - - - - - - 181.1 - 29.5 - * * 137 VAL 343 T A - - -61.5 - - - - - - - 178.8 - 32.0 - 138 ARG 344 t B - - -70.3 181.0 - - - - - - 182.6 -2.9 32.0 - * * 139 SER 345 h B - - -52.6 - - - - - - - 180.5 - 35.3 - 140 LYS 346 H A 62.5 - - - - -50.8 -41.8 - - - 182.2 - 33.8 - * * 141 GLU 347 H A 49.3 - - 172.7 - -57.4 -32.9 - - - 177.1 - 32.7 - 142 GLN 348 H A - - -75.0 - - -71.2 -38.1 - - - 183.9 -1.5 34.0 - 143 MET 349 H A - - -58.6 181.1 - -64.6 -45.2 - - - 172.8 -1.2 32.7 - * * * 144 LEU 350 H A - - -76.7 - - -53.8 -52.8 - - - 182.9 -2.0 34.4 - * * 145 GLU 351 H A - 180.5 - 172.9 - -60.6 -44.8 - - - 177.8 -1.6 33.6 - 146 LEU 352 H A - - -63.6 177.2 - -61.5 -43.5 - - - 181.1 -3.1 35.0 - * * 147 LEU 353 H A - 185.6 - - - -72.2 -31.8 - - - 173.4 -2.6 33.7 - * * 148 VAL 354 H A - 175.6 - - - -64.0 -43.0 - - - 176.8 -2.6 33.4 - 149 LEU 355 H A - 183.1 - - - -58.4 -44.4 - - - 179.3 -2.5 35.6 - 150 GLU 356 H A - 180.0 - - - -52.9 -52.4 - - - 180.2 -2.2 34.5 - * * * 151 GLN 357 H A - 177.6 - - - -74.1 -42.9 - - - 182.3 -2.1 32.6 - 152 PHE 358 H A - 181.1 - - - -56.7 -47.8 - - - 180.9 -3.2 33.2 - +* +* 153 LEU 359 H A - - -64.4 185.5 - -65.9 -36.4 - - - 180.1 -3.0 31.6 - * * 154 GLY 360 H - - - - - - -80.4 -23.6 - - - 177.9 -1.4 - - * * * 155 ALA 361 H A - - - - - -70.9 -29.0 - - - 174.0 -2.4 33.5 - * * 156 LEU 362 h B - - -67.2 172.1 - - - - - - 179.4 -1.2 37.1 - * * 157 PRO 363 h - - - - - -72.7 - - - - - 181.8 - 37.8 - * * 158 PRO 364 H - - - - - -29.9 -29.9 -51.5 - - - 183.3 - 38.4 - *** +** * * *** 159 GLU 365 H A 58.7 - - - - -71.0 -46.8 - - - 180.6 - 30.4 - * * 160 ILE 366 H A - - -57.5 181.4 - -66.0 -39.1 - - - 178.1 - 34.2 - Residue-by-residue listing for refined_7 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 - 179.1 - 176.8 - -63.2 -40.8 - - - 179.5 -3.2 34.6 - +* +* 162 ALA 368 H A - - - - - -65.1 -35.0 - - - 179.5 -2.2 33.5 - 163 ARG 369 H A - - -55.1 - - -58.8 -45.8 - - - 180.7 -1.9 36.0 - 164 VAL 370 H A - 168.1 - - - -56.8 -44.5 - - - 186.7 -1.5 35.9 - * * 165 GLN 371 H A - - -51.3 - - -57.3 -34.1 - - - 180.7 -1.4 35.0 - * * 166 GLY 372 H - - - - - - -79.3 -17.3 - - - 182.7 -1.0 - - * +* * +* 167 GLN 373 H a - 175.5 - 178.9 - -103.7 -49.2 - - - 185.6 -1.5 34.4 - *** *** 168 ARG 374 h l - - -55.3 - - - - - - - 178.0 -3.3 32.6 - +* +* 169 PRO 375 - - - - - -60.8 - - - - - 179.1 - 39.1 - * * 170 GLY 376 S - - - - - - - - - - - 179.4 - - - 171 SER 377 h B 56.3 - - - - - - - - - 179.4 - 34.6 - 172 PRO 378 H - - - - - -58.5 -58.5 -38.8 - - - 182.4 - 38.5 - * * 173 GLU 379 H A - - -63.0 176.0 - -69.8 -31.8 - - - 174.8 - 31.6 - 174 GLU 380 H A - 181.0 - - - -73.9 -39.2 - - - 175.4 - 33.0 - 175 ALA 381 H A - - - - - -55.8 -43.5 - - - 178.4 -2.4 33.8 - 176 ALA 382 H A - - - - - -58.8 -30.2 - - - 180.6 -2.5 34.3 - 177 ALA 383 H A - - - - - -72.6 -50.4 - - - 179.2 -.8 32.8 - +* +* 178 LEU 384 H A 51.5 - - 156.4 - -67.6 -42.7 - - - 183.2 -1.9 28.9 - * * * 179 VAL 385 H A - - -59.4 - - -62.0 -32.3 - - - 177.8 -2.7 30.1 - * * 180 ASP 386 H A - 183.0 - - - -60.8 -39.3 - - - 179.3 -1.2 34.3 - * * 181 GLY 387 H - - - - - - -84.1 -25.0 - - - 177.9 -1.0 - - +* * * +* 182 LEU 388 H A - - -63.4 177.0 - -66.7 -22.6 - - - 173.4 -2.0 33.5 - * * * 183 ARG 389 h b - - -60.8 181.6 - - - - - - 183.2 -1.1 34.9 - * * 184 ARG 390 T ~b 56.5 - - 179.3 - - - - - - 184.5 -1.4 34.8 - ** ** 185 GLU 391 t b - 178.4 - 178.1 - - - - - - 175.8 -1.7 34.3 - 186 PRO 392 - - - - - -96.6 - - - - - 176.6 - 39.5 - +** +* +** 187 GLY 393 - - - - - - - - - - - 179.5 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * +* * * *** +*** +** * ** ** +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.6 179.9 -62.8 177.4 -65.9 -65.7 -39.3 - - - 179.5 -2.0 34.0 Standard deviations: 7.4 8.7 7.6 8.0 15.4 10.0 8.8 - - - 3.1 .8 2.3 Numbers of values: 20 48 64 59 18 124 124 0 0 0 186 126 170 0 Residue-by-residue listing for refined_7 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_7 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 - 1.238 1.493 - 1.463 - 117.42 119.92 - 109.60 - 122.65 * * * 2 SER 2 1.306 1.230 1.525 1.533 1.438 120.43 115.49 121.43 112.01 107.38 111.09 122.96 +* * * * +* 3 ASP 3 1.314 1.236 1.515 1.541 1.448 121.68 117.35 120.51 110.15 111.11 110.55 122.14 * * 4 PRO 4 1.341 1.242 1.538 1.532 1.469 122.92 116.24 120.99 110.66 112.63 103.04 122.77 5 GLY 5 1.312 1.243 1.514 - 1.437 120.94 118.30 119.64 - 111.03 - 122.06 * * 6 PRO 6 1.346 1.220 1.528 1.537 1.469 122.91 117.18 120.04 110.54 112.83 103.74 122.76 7 GLU 7 1.325 1.222 1.514 1.538 1.462 121.64 116.60 120.32 111.24 111.83 112.05 123.06 8 ALA 8 1.317 1.232 1.526 1.518 1.455 121.89 116.23 120.82 110.71 110.76 110.46 122.94 9 ALA 9 1.322 1.237 1.528 1.511 1.451 121.49 116.44 120.68 111.19 110.89 110.53 122.86 10 ARG 10 1.333 1.228 1.529 1.531 1.449 121.70 116.22 120.82 110.61 111.08 111.47 122.95 11 LEU 11 1.330 1.228 1.526 1.523 1.413 123.23 116.18 120.19 111.41 109.93 108.63 123.61 ** * ** 12 ARG 12 1.337 1.234 1.518 1.528 1.474 122.73 114.01 121.67 107.43 109.79 110.22 124.31 * * * 13 PHE 13 1.309 1.220 1.545 1.530 1.444 125.04 117.44 120.49 112.53 112.52 107.05 122.06 * +* * ** ** 14 ARG 14 1.321 1.236 1.518 1.530 1.469 121.32 116.84 120.62 110.60 112.66 111.93 122.54 Residue-by-residue listing for refined_7 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.309 1.234 1.518 1.519 1.451 120.88 115.88 120.86 110.84 110.68 110.94 123.26 * * 16 PHE 16 1.328 1.242 1.505 1.538 1.441 122.08 116.38 120.64 109.72 108.45 110.67 122.97 17 HIS 17 1.296 1.241 1.507 1.561 1.431 120.23 117.61 119.70 110.37 107.75 111.82 122.68 ** +* * * ** 18 TYR 18 1.303 1.237 1.503 1.540 1.423 119.23 114.07 122.01 112.41 109.29 112.33 123.92 +* * +* * * * * +* 19 GLU 19 1.285 1.235 1.501 1.538 1.410 123.48 115.17 121.39 112.90 109.03 110.31 123.43 *** * +** * *** 20 GLU 20 1.293 1.224 1.530 1.519 1.438 122.73 115.77 120.76 110.84 110.90 109.00 123.45 +** * +** 21 ALA 21 1.324 1.234 1.531 1.521 1.457 123.17 117.55 120.33 110.45 112.53 110.34 122.12 22 THR 22 1.328 1.228 1.540 1.586 1.447 119.54 115.50 121.25 110.73 108.18 111.11 123.12 +* * * +* 23 GLY 23 1.336 1.235 1.523 - 1.446 121.64 119.35 120.03 - 111.07 - 120.62 * * * 24 PRO 24 1.339 1.227 1.520 1.512 1.454 121.73 116.31 120.58 110.40 112.59 103.52 123.11 25 GLN 25 1.332 1.230 1.532 1.514 1.416 122.33 115.13 121.64 108.66 108.13 108.38 123.20 ** * * ** 26 GLU 26 1.319 1.239 1.521 1.522 1.445 122.80 116.30 120.85 113.05 110.94 109.88 122.85 +* +* 27 ALA 27 1.325 1.224 1.527 1.523 1.455 121.47 116.02 120.69 110.61 109.17 110.77 123.26 28 LEU 28 1.331 1.217 1.510 1.520 1.462 122.49 116.89 119.91 108.93 111.86 111.92 123.20 29 ALA 29 1.334 1.237 1.527 1.523 1.471 122.05 115.10 121.53 110.47 110.28 110.40 123.37 30 GLN 30 1.310 1.226 1.533 1.507 1.436 122.92 116.04 120.94 112.25 111.36 108.68 122.98 * * * * * * 31 LEU 31 1.326 1.215 1.515 1.526 1.469 123.02 117.69 119.86 110.12 113.18 111.12 122.45 32 ARG 32 1.325 1.208 1.512 1.544 1.459 120.42 116.34 120.44 112.60 111.52 113.56 123.22 * * +* +* 33 GLU 33 1.318 1.217 1.531 1.535 1.455 122.36 116.35 120.57 109.28 109.01 108.96 123.05 34 LEU 34 1.326 1.230 1.522 1.528 1.464 122.37 116.31 120.75 111.55 111.47 110.49 122.92 35 CYS 35 1.317 1.224 1.525 1.531 1.444 121.91 116.42 120.86 110.47 109.72 110.39 122.72 36 ARG 36 1.326 1.210 1.528 1.534 1.418 122.57 117.32 119.73 113.83 110.51 108.92 122.95 * ** +* ** 37 GLN 37 1.331 1.229 1.515 1.509 1.468 121.86 114.42 121.92 108.12 110.10 110.62 123.65 * * * 38 TRP 38 1.304 1.227 1.552 1.548 1.424 123.56 118.39 119.47 114.14 113.04 109.08 122.14 +* * +* * * ** ** 39 LEU 39 1.332 1.229 1.533 1.557 1.471 120.66 115.84 120.58 110.05 111.01 112.54 123.53 * * * 40 ARG 40 1.329 1.234 1.537 1.541 1.469 124.94 116.66 121.34 111.72 112.17 113.77 121.99 +* +* +* 41 PRO 41 1.345 1.232 1.512 1.528 1.470 123.48 116.83 120.18 109.57 114.08 103.43 123.00 42 GLU 42 1.311 1.235 1.514 1.533 1.444 120.84 116.83 120.47 111.26 112.76 113.87 122.69 * +* +* 43 VAL 43 1.320 1.235 1.532 1.561 1.454 120.38 117.32 120.44 110.63 112.24 112.93 122.24 44 ARG 44 1.325 1.239 1.509 1.528 1.463 121.07 115.54 120.92 109.61 111.39 111.96 123.54 45 SER 45 1.307 1.242 1.543 1.532 1.426 122.82 115.75 120.70 110.84 109.87 109.02 123.55 +* +* +* 46 LYS 46 1.325 1.224 1.536 1.555 1.467 124.14 115.49 121.28 108.19 112.73 111.12 123.23 * * * * 47 GLU 47 1.307 1.234 1.525 1.529 1.457 123.12 116.75 120.47 113.17 113.43 110.62 122.75 +* +* +* 48 GLN 48 1.324 1.222 1.526 1.548 1.450 121.07 116.08 121.13 110.04 109.97 112.51 122.77 * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 49 MET 49 1.318 1.229 1.505 1.503 1.450 121.83 116.28 120.14 111.97 110.97 110.47 123.59 * * 50 LEU 50 1.343 1.205 1.518 1.568 1.473 121.64 115.87 120.56 109.27 108.61 112.52 123.47 * * +* * +* 51 GLU 51 1.329 1.243 1.545 1.519 1.435 123.97 116.49 120.62 110.68 111.67 107.42 122.88 * * +* +* 52 LEU 52 1.327 1.232 1.522 1.529 1.449 122.37 116.68 120.73 109.83 111.93 110.33 122.59 53 LEU 53 1.314 1.232 1.551 1.519 1.422 121.34 117.30 120.63 115.81 112.52 107.95 122.05 * * +* *** * *** 54 VAL 54 1.322 1.234 1.523 1.555 1.466 121.07 115.42 120.98 109.89 109.05 112.08 123.59 55 LEU 55 1.331 1.230 1.526 1.533 1.459 123.30 115.40 120.88 109.25 110.29 109.40 123.72 56 GLU 56 1.322 1.246 1.533 1.530 1.458 123.23 115.85 121.17 108.51 110.97 109.38 122.96 57 GLN 57 1.317 1.206 1.495 1.524 1.442 121.11 116.64 120.09 110.94 110.68 111.52 123.26 * * * 58 PHE 58 1.316 1.235 1.519 1.523 1.446 121.57 116.43 120.55 110.50 111.64 110.98 123.00 59 LEU 59 1.321 1.217 1.511 1.533 1.442 120.55 117.01 120.26 111.86 112.10 112.16 122.70 60 GLY 60 1.319 1.223 1.513 - 1.446 119.65 116.69 120.38 - 112.56 - 122.93 61 ALA 61 1.325 1.233 1.520 1.534 1.454 121.99 115.72 120.77 111.01 109.80 111.15 123.50 62 LEU 62 1.333 1.237 1.523 1.523 1.454 123.11 118.77 119.82 107.29 109.50 108.83 121.40 * * * 63 PRO 63 1.342 1.231 1.515 1.539 1.451 121.38 118.59 118.78 109.64 107.94 104.02 122.62 * * * +* +* 64 PRO 64 1.347 1.223 1.535 1.521 1.483 123.67 115.62 121.16 110.28 112.93 102.54 123.19 * * 65 GLU 65 1.312 1.239 1.554 1.528 1.456 123.31 117.30 120.15 112.69 112.80 108.36 122.50 * * * * * 66 ILE 66 1.335 1.237 1.530 1.556 1.456 122.20 114.92 121.53 109.74 109.81 110.10 123.53 67 GLN 67 1.315 1.229 1.529 1.523 1.449 123.80 116.47 120.53 110.78 111.63 108.88 123.00 * * 68 ALA 68 1.320 1.233 1.529 1.511 1.457 121.99 116.48 120.61 110.72 111.56 110.51 122.89 69 ARG 69 1.335 1.230 1.521 1.529 1.471 121.44 115.48 121.12 109.67 109.90 111.56 123.39 70 VAL 70 1.329 1.234 1.492 1.544 1.455 122.58 115.25 120.94 106.61 111.03 111.77 123.80 +* * +* 71 GLN 71 1.305 1.223 1.526 1.522 1.434 121.81 116.19 120.77 111.73 111.06 111.38 123.04 +* * +* 72 GLY 72 1.321 1.233 1.531 - 1.446 121.07 117.48 120.42 - 112.80 - 122.09 73 GLN 73 1.331 1.234 1.524 1.518 1.460 120.64 115.18 120.56 108.08 111.21 111.52 124.26 * * 74 ARG 74 1.342 1.222 1.546 1.535 1.474 125.14 117.98 120.50 109.35 110.37 112.81 121.42 * +* * +* 75 PRO 75 1.348 1.227 1.534 1.534 1.482 122.90 115.92 120.94 109.81 113.36 103.51 123.13 * * 76 GLY 76 1.315 1.231 1.523 - 1.451 121.78 116.83 120.77 - 113.18 - 122.38 * * 77 SER 77 1.310 1.243 1.540 1.532 1.444 121.79 117.95 120.04 112.66 110.16 109.77 121.98 * * * 78 PRO 78 1.356 1.229 1.542 1.535 1.471 122.87 117.48 120.22 111.13 115.03 104.38 122.29 * * * 79 GLU 79 1.318 1.232 1.528 1.530 1.472 121.97 116.04 121.09 113.23 110.61 109.88 122.87 +* +* 80 GLU 80 1.322 1.234 1.534 1.531 1.446 122.10 115.66 121.04 110.05 107.83 109.81 123.29 * * 81 ALA 81 1.346 1.230 1.515 1.515 1.454 122.69 115.34 120.75 110.32 110.72 110.24 123.91 * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 82 ALA 82 1.325 1.226 1.521 1.505 1.455 123.76 115.33 121.10 109.73 111.48 109.11 123.55 * * 83 ALA 83 1.303 1.236 1.536 1.514 1.447 123.09 118.26 119.82 111.70 112.38 110.61 121.91 +* * +* 84 LEU 84 1.343 1.221 1.498 1.551 1.460 118.68 116.98 120.10 110.02 112.19 117.09 122.90 * * +* +*** +*** 85 VAL 85 1.329 1.224 1.515 1.543 1.461 121.01 115.89 120.41 111.76 112.12 113.72 123.66 * * * 86 ASP 86 1.327 1.236 1.530 1.539 1.464 123.27 115.33 121.46 109.60 109.68 108.87 123.15 87 GLY 87 1.321 1.223 1.525 - 1.443 121.79 117.23 120.55 - 113.34 - 122.22 88 LEU 88 1.314 1.229 1.526 1.531 1.472 121.77 115.55 121.17 109.88 111.28 110.01 123.25 * * 89 ARG 89 1.319 1.229 1.548 1.519 1.475 124.43 118.42 119.90 109.47 115.58 110.00 121.66 * +* * +* +* 90 ARG 90 1.311 1.229 1.511 1.562 1.460 120.46 116.23 120.81 112.05 111.98 115.43 122.93 * +* * +** +** 91 GLU 91 1.318 1.231 1.534 1.534 1.440 121.27 117.69 120.55 110.49 108.16 111.29 121.64 * * 92 PRO 92 1.342 1.240 1.523 1.541 1.441 122.66 115.94 121.20 110.37 112.21 103.16 122.86 +* +* 93 GLY 93 1.300 1.244 1.506 - 1.437 120.85 115.43 121.03 - 111.02 - 123.54 ** ** 94 GLY 94 1.311 1.247 1.511 - 1.443 122.14 - 120.20 - 111.55 - - * * 95 GLY 301 - 1.232 1.502 - 1.449 - 115.28 121.33 - 111.19 - 123.37 96 SER 302 1.307 1.239 1.526 1.518 1.437 122.28 117.11 120.34 110.87 109.37 108.93 122.54 +* * +* 97 ASP 303 1.315 1.224 1.504 1.541 1.452 120.87 118.18 120.35 108.47 111.84 112.60 121.47 * * * 98 PRO 304 1.341 1.233 1.518 1.530 1.458 121.90 114.38 121.80 109.63 109.46 103.55 123.81 +* * +* 99 GLY 305 1.309 1.223 1.503 - 1.409 122.18 118.61 119.69 - 109.02 - 121.66 * +** * * +** 100 PRO 306 1.344 1.232 1.529 1.530 1.473 122.54 116.27 121.04 110.78 111.84 103.70 122.68 101 GLU 307 1.324 1.239 1.535 1.545 1.441 121.77 115.82 120.82 110.62 109.55 112.08 123.35 102 ALA 308 1.332 1.228 1.520 1.525 1.458 122.80 115.70 121.10 109.98 109.79 110.50 123.20 103 ALA 309 1.324 1.235 1.513 1.516 1.451 122.84 115.75 120.86 109.95 109.91 110.19 123.37 104 ARG 310 1.330 1.219 1.525 1.516 1.445 121.92 116.28 120.77 108.01 109.85 111.49 122.95 * * 105 LEU 311 1.325 1.222 1.530 1.523 1.411 122.88 116.69 120.21 111.77 110.34 108.81 123.08 ** ** 106 ARG 312 1.333 1.233 1.529 1.528 1.473 122.21 114.48 121.53 109.11 109.71 110.52 123.99 107 PHE 313 1.314 1.222 1.550 1.539 1.453 124.75 116.71 120.71 112.89 111.03 106.93 122.57 * * +* * ** ** 108 ARG 314 1.326 1.237 1.532 1.536 1.474 122.70 117.05 120.64 109.51 113.01 111.74 122.31 109 CYS 315 1.316 1.235 1.519 1.525 1.459 121.09 116.34 120.68 109.92 111.56 111.17 122.98 110 PHE 316 1.313 1.244 1.525 1.532 1.435 121.44 116.23 120.85 110.53 110.11 110.30 122.90 * * * 111 HIS 317 1.313 1.235 1.503 1.577 1.454 120.93 118.02 119.71 109.44 107.87 112.64 122.26 * * ** * * ** 112 TYR 318 1.295 1.232 1.492 1.530 1.424 118.39 115.15 121.29 111.42 108.37 112.72 123.56 ** +* +* +* * * ** 113 GLU 319 1.282 1.240 1.492 1.529 1.401 121.39 115.13 121.15 112.28 109.75 111.70 123.71 *** +* +** * *** Residue-by-residue listing for refined_7 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 114 GLU 320 1.297 1.223 1.519 1.505 1.436 122.60 116.14 120.59 110.92 111.52 109.36 123.26 ** * * ** 115 ALA 321 1.322 1.231 1.522 1.514 1.451 122.22 117.66 120.17 110.03 112.32 110.79 122.16 116 THR 322 1.324 1.215 1.550 1.581 1.445 119.36 116.63 120.97 111.11 109.39 111.02 122.31 * +* * +* 117 GLY 323 1.329 1.237 1.522 - 1.459 120.93 119.42 119.66 - 110.82 - 120.91 * * * 118 PRO 324 1.350 1.211 1.522 1.523 1.458 121.77 117.20 120.38 111.15 113.74 104.43 122.39 * * 119 GLN 325 1.305 1.233 1.510 1.495 1.453 121.43 116.52 120.84 114.89 114.26 110.58 122.60 +* +* +** * +** 120 GLU 326 1.295 1.238 1.526 1.521 1.448 120.57 115.31 121.67 112.99 108.85 111.20 123.01 ** +* ** 121 ALA 327 1.321 1.218 1.527 1.522 1.446 122.14 116.03 120.81 110.53 109.13 110.16 123.15 122 LEU 328 1.331 1.214 1.496 1.517 1.461 122.95 116.93 119.52 109.32 112.27 111.82 123.55 * * 123 ALA 329 1.326 1.224 1.512 1.515 1.457 121.49 114.93 121.18 110.59 109.18 110.52 123.83 124 GLN 330 1.317 1.216 1.523 1.499 1.435 123.11 116.42 120.66 111.18 111.33 108.79 122.90 +* * * +* 125 LEU 331 1.324 1.216 1.515 1.526 1.460 122.41 118.08 119.75 111.23 112.89 111.56 122.16 126 ARG 332 1.323 1.220 1.504 1.552 1.449 119.57 116.41 120.18 115.05 112.58 115.38 123.39 * * +** +** +** 127 GLU 333 1.319 1.235 1.536 1.531 1.451 121.76 115.94 120.91 109.59 109.72 110.27 123.14 128 LEU 334 1.325 1.230 1.516 1.530 1.460 122.74 116.28 120.44 110.44 111.51 110.69 123.27 129 CYS 335 1.322 1.227 1.530 1.536 1.448 122.13 116.18 121.02 111.26 108.97 110.04 122.79 130 ARG 336 1.337 1.191 1.519 1.558 1.450 122.09 118.44 119.17 112.34 112.14 111.55 122.38 +* * * * +* 131 GLN 337 1.326 1.232 1.535 1.536 1.488 120.88 114.66 121.76 108.86 110.26 111.08 123.58 +* +* 132 TRP 338 1.302 1.235 1.553 1.539 1.433 124.04 117.51 120.38 113.36 112.46 107.65 122.11 +* * * * +* +* +* 133 LEU 339 1.321 1.226 1.521 1.540 1.462 121.02 115.79 120.23 110.39 110.80 111.02 123.97 134 ARG 340 1.338 1.228 1.527 1.530 1.461 124.62 116.14 121.55 113.69 113.60 113.33 122.30 +* +* +* +* 135 PRO 341 1.344 1.233 1.522 1.531 1.465 123.53 116.95 120.40 110.38 114.72 103.49 122.64 * * 136 GLU 342 1.296 1.237 1.526 1.541 1.439 120.76 117.02 120.28 112.87 112.80 113.49 122.69 ** * * +* ** 137 VAL 343 1.330 1.231 1.533 1.558 1.469 120.72 117.34 120.53 110.10 112.76 113.02 122.13 138 ARG 344 1.309 1.236 1.508 1.533 1.456 120.96 115.55 121.09 110.67 111.42 112.86 123.36 * * * 139 SER 345 1.302 1.246 1.528 1.520 1.433 122.36 116.46 120.13 110.63 110.24 108.63 123.41 +* * * +* 140 LYS 346 1.348 1.220 1.525 1.558 1.482 122.91 114.78 121.58 108.46 111.70 112.65 123.62 * * * * * 141 GLU 347 1.303 1.233 1.538 1.521 1.461 123.84 117.17 120.49 111.54 113.12 110.14 122.34 +* * +* 142 GLN 348 1.327 1.209 1.509 1.544 1.459 120.99 115.74 120.75 108.92 109.76 112.46 123.48 * * * 143 MET 349 1.319 1.229 1.507 1.503 1.457 122.55 116.46 120.04 112.05 112.01 110.00 123.50 * * * 144 LEU 350 1.335 1.210 1.511 1.562 1.471 121.92 116.04 120.46 108.82 109.80 112.24 123.40 * +* * +* 145 GLU 351 1.321 1.241 1.543 1.516 1.424 123.03 116.70 120.41 112.53 112.18 108.52 122.87 +* * * +* Residue-by-residue listing for refined_7 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 146 LEU 352 1.329 1.233 1.515 1.528 1.448 122.33 116.23 120.93 109.17 110.81 110.41 122.84 147 LEU 353 1.316 1.244 1.544 1.489 1.408 121.53 117.01 120.48 113.49 111.95 107.23 122.50 ** +** +* +* +** 148 VAL 354 1.327 1.230 1.523 1.562 1.457 121.26 115.81 120.65 110.10 108.99 112.65 123.51 149 LEU 355 1.334 1.232 1.524 1.538 1.462 122.89 114.86 121.06 109.38 109.26 109.68 124.06 150 GLU 356 1.327 1.240 1.542 1.554 1.462 124.13 116.88 120.87 111.14 111.29 109.10 122.25 * * * 151 GLN 357 1.316 1.214 1.501 1.522 1.453 120.38 116.83 119.83 110.84 111.67 111.83 123.33 * * 152 PHE 358 1.319 1.235 1.520 1.530 1.449 121.48 116.29 120.56 110.53 111.59 111.34 123.12 153 LEU 359 1.319 1.216 1.514 1.536 1.441 121.16 117.01 120.17 111.97 112.38 111.84 122.78 154 GLY 360 1.320 1.235 1.513 - 1.449 119.85 116.53 120.27 - 112.85 - 123.19 155 ALA 361 1.331 1.235 1.519 1.532 1.458 122.45 115.67 120.74 111.01 109.81 111.05 123.58 156 LEU 362 1.330 1.241 1.528 1.523 1.448 122.99 118.44 119.97 107.70 109.26 109.06 121.58 * * * 157 PRO 363 1.335 1.242 1.524 1.533 1.436 121.26 117.16 119.38 110.82 109.86 104.96 123.44 ** +* * ** 158 PRO 364 1.358 1.221 1.537 1.512 1.467 125.33 118.22 119.59 110.57 115.92 102.46 122.16 * +* +* 159 GLU 365 1.334 1.229 1.526 1.546 1.459 120.05 117.48 120.11 110.83 112.61 114.41 122.40 ** ** 160 ILE 366 1.332 1.239 1.528 1.543 1.455 121.00 115.18 121.35 109.90 109.57 111.18 123.44 161 GLN 367 1.315 1.230 1.527 1.524 1.440 122.66 115.80 120.84 110.60 110.16 109.70 123.35 162 ALA 368 1.328 1.234 1.530 1.524 1.458 122.74 116.58 120.23 110.57 111.72 110.65 123.17 163 ARG 369 1.339 1.238 1.527 1.531 1.481 121.99 114.53 121.68 106.52 109.29 111.60 123.79 * +* +* 164 VAL 370 1.329 1.242 1.503 1.543 1.457 123.92 115.23 120.62 107.31 112.38 110.67 124.15 * * * 165 GLN 371 1.306 1.221 1.540 1.516 1.447 123.00 116.17 120.85 109.70 110.95 109.56 122.95 +* +* 166 GLY 372 1.324 1.236 1.528 - 1.447 120.93 117.01 120.55 - 113.39 - 122.43 167 GLN 373 1.318 1.232 1.520 1.527 1.453 121.37 115.64 120.44 109.68 112.06 110.32 123.90 168 ARG 374 1.329 1.217 1.528 1.538 1.471 124.41 117.68 120.52 109.61 110.69 113.28 121.69 +* +* +* 169 PRO 375 1.347 1.227 1.534 1.538 1.476 122.55 115.55 121.27 109.80 112.19 103.35 123.17 170 GLY 376 1.322 1.230 1.514 - 1.454 121.98 116.29 120.72 - 112.66 - 122.98 171 SER 377 1.313 1.247 1.530 1.534 1.437 122.35 118.12 119.95 111.05 109.52 109.55 121.90 * * * 172 PRO 378 1.356 1.227 1.520 1.537 1.466 122.79 116.16 120.88 109.67 112.39 104.53 122.95 * * 173 GLU 379 1.316 1.236 1.518 1.522 1.446 121.55 116.68 120.55 113.33 111.77 110.56 122.76 +* +* 174 GLU 380 1.324 1.217 1.523 1.533 1.442 120.59 116.66 120.49 111.91 108.68 111.33 122.83 175 ALA 381 1.347 1.229 1.524 1.516 1.457 121.67 115.81 120.57 110.55 110.38 110.56 123.56 * * 176 ALA 382 1.334 1.232 1.539 1.529 1.463 123.11 115.65 121.36 110.34 111.43 109.83 122.98 177 ALA 383 1.299 1.234 1.524 1.518 1.443 122.64 117.98 119.72 111.23 111.36 111.14 122.29 ** ** 178 LEU 384 1.344 1.229 1.505 1.557 1.461 118.78 116.90 119.94 110.15 112.67 117.12 123.13 * * +* +*** +*** 179 VAL 385 1.337 1.227 1.515 1.543 1.463 121.53 116.63 120.12 111.21 112.99 114.19 123.24 +* +* 180 ASP 386 1.329 1.226 1.526 1.534 1.464 121.59 115.65 121.10 109.94 109.66 110.95 123.20 181 GLY 387 1.326 1.220 1.520 - 1.447 121.42 116.42 120.75 - 112.24 - 122.83 182 LEU 388 1.333 1.245 1.514 1.532 1.470 122.42 115.25 120.91 110.51 110.37 111.19 123.83 Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 183 ARG 389 1.327 1.240 1.519 1.518 1.443 122.66 115.20 120.88 108.67 109.27 111.29 123.88 184 ARG 390 1.305 1.224 1.506 1.551 1.450 124.34 115.95 120.99 109.10 109.29 111.54 123.05 +* * * +* 185 GLU 391 1.316 1.242 1.525 1.524 1.429 121.10 117.02 121.05 111.24 111.63 109.14 121.86 +* +* 186 PRO 392 1.328 1.243 1.532 1.531 1.423 122.51 116.47 120.80 110.64 110.47 102.59 122.73 +** +** 187 GLY 393 1.301 1.231 1.497 - 1.430 120.90 115.25 121.33 - 109.69 - 123.41 ** * * ** 188 GLY 394 1.302 - 1.489 - 1.418 122.11 - - - 109.62 - - +* +* ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* ** +** +* +* * *** +* +*** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 1.282 1.348 1.321 .012 *** * C-N (Pro) 1.341 .016 18 1.328 1.358 1.345 .007 * C-O C-O 1.231 .020 187 1.191 1.247 1.230 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.492 1.554 1.524 .013 +* * CH2G*-C (Gly) 1.516 .018 18 1.489 1.531 1.513 .012 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.505 1.534 1.519 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.543 1.586 1.556 .014 +* CH1E-CH2E (the rest) 1.530 .020 138 1.489 1.577 1.531 .014 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.401 1.488 1.451 .015 +** +* NH1-CH2G* (Gly) 1.451 .016 18 1.409 1.463 1.443 .013 +** N-CH1E (Pro) 1.466 .015 18 1.423 1.483 1.462 .015 +** * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 2.0 152 114.01 118.77 116.33 .96 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.25 119.42 117.10 1.27 * CH1E-C-N (Pro) 116.9 1.5 18 114.38 118.59 116.58 .97 +* * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.62 124.31 122.93 .66 * O-C-N (Pro) 122.0 1.4 18 122.16 123.81 122.87 .39 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.39 125.14 122.05 1.27 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 16 119.65 122.18 121.26 .74 C-N-CH1E (Pro) 122.6 5.0 18 121.26 125.33 122.71 .93 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.78 122.01 120.65 .55 * CH2G*-C-O (Gly) 120.8 2.1 17 119.64 121.33 120.42 .52 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.73 111.70 110.58 .47 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.61 111.76 109.93 1.46 * * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.52 115.81 110.70 1.61 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.38 115.58 110.86 1.47 * +* NH1-CH2G*-C (Gly) 112.5 2.9 18 109.02 113.39 111.53 1.38 * N-CH1E-C (Pro) 111.8 2.5 18 107.94 115.92 112.46 1.97 +* +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.11 111.15 110.48 .45 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.10 114.19 112.04 1.22 +* N-CH1E-CH2E (Pro) 103.0 1.1 18 102.46 104.96 103.58 .68 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.93 117.12 110.85 1.85 ** +*** ------------------------------------------------------------------------------------------------------------- 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_7 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] 137 90.1% Residues in additional allowed regions [a,b,l,p] 14 9.2% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 90.1 83.8 10.0 .6 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 126 .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 20 7.4 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 48 8.7 19.0 5.3 -2.0 BETTER c. Chi-1 gauche plus st dev 64 7.6 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 132 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 59 8.0 20.4 5.0 -2.5 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 90.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_7 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .11 Chi1-chi2 distribution -.06 Chi1 only -.23 Chi3 & chi4 .34 Omega .11 ------ .10 ===== Main-chain covalent forces:- Main-chain bond lengths .30 Main-chain bond angles .40 ------ .36 ===== OVERALL AVERAGE .20 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.