Residue-by-residue listing for refined_9 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 - - - - - - - - - - - 178.3 - - - 2 SER 2 B - 182.8 - - - - - - - - 178.1 - 34.7 - 3 ASP 3 B - 182.2 - - - - - - - - 182.9 - 34.5 - 4 PRO 4 - - - - - -57.0 - - - - - 181.1 - 38.2 - * * 5 GLY 5 h - - - - - - - - - - - 179.1 - - - 6 PRO 6 H - - - - - -58.3 -58.3 -32.4 - - - 177.7 - 38.9 - * * 7 GLU 7 H A 55.0 - - 185.7 - -61.8 -40.0 - - - 179.3 - 33.8 - 8 ALA 8 H A - - - - - -74.9 -32.8 - - - 176.5 -.6 33.7 - +* +* 9 ALA 9 H A - - - - - -64.8 -45.3 - - - 176.2 -1.9 34.4 - 10 ARG 10 H A - 173.4 - 170.6 - -62.0 -33.8 - - - 178.1 -3.0 32.7 - * * 11 LEU 11 H A - 173.7 - - - -62.9 -45.3 - - - 177.1 -1.5 34.3 - 12 ARG 12 H A - - -57.9 180.8 - -60.6 -47.6 - - - 181.8 -2.0 35.8 - 13 PHE 13 H A - 174.7 - - - -62.0 -45.4 - - - 179.1 -2.6 34.3 - 14 ARG 14 H A - - -72.1 - - -73.7 -24.2 - - - 178.1 -3.4 31.2 - * +* +* 15 CYS 15 h A - - -60.6 - - - - - - - 179.3 -1.7 33.2 - 16 PHE 16 t B - 184.0 - - - - - - - - 178.0 -.8 34.0 - +* +* 17 HIS 17 B 73.5 - - - - - - - - - 175.0 - 34.7 - 18 TYR 18 B - 167.2 - - - - - - - - 179.6 -1.4 30.9 - 19 GLU 19 g B 39.7 - - 187.9 - - - - - - 183.8 -.6 32.8 - +* +* +* 20 GLU 20 G A - - -63.0 172.1 - - - - - - 180.1 -.7 35.0 - +* +* Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 ALA 21 G A - - - - - - - - - - 185.5 - 36.7 - 22 THR 22 G A - - -63.4 - - - - - - - 179.7 -1.0 37.1 - * * 23 GLY 23 h - - - - - - - - - - - 181.3 -.8 - - +* +* 24 PRO 24 H - - - - - -63.4 -63.4 -31.1 - - - 180.3 - 38.5 - * * 25 GLN 25 H A - - -86.4 - - -68.3 -41.7 - - - 180.3 - 33.1 - * * 26 GLU 26 H A - 184.7 - 178.4 - -71.1 -39.3 - - - 177.0 - 33.4 - 27 ALA 27 H A - - - - - -58.1 -37.2 - - - 176.4 -2.3 34.1 - 28 LEU 28 H A - - -66.5 177.6 - -61.2 -37.7 - - - 179.4 -1.7 33.8 - 29 ALA 29 H A - - - - - -59.5 -40.6 - - - 177.1 -1.1 33.8 - * * 30 GLN 30 H A - - -82.7 - - -73.0 -47.8 - - - 179.8 -1.4 33.5 - * * 31 LEU 31 H A - - -70.1 171.9 - -61.2 -44.9 - - - 180.9 -3.2 32.4 - +* +* 32 ARG 32 H A 72.8 - - 182.9 - -67.3 -29.1 - - - 177.7 -3.5 31.3 - +* +* 33 GLU 33 H A - 183.8 - 184.0 - -70.9 -50.1 - - - 182.2 -.9 35.7 - * * 34 LEU 34 H A - - -61.9 178.8 - -64.7 -43.4 - - - 178.6 -3.0 33.0 - * * 35 CYS 35 H A 59.6 - - - - -67.8 -29.8 - - - 176.5 -3.0 32.7 - * * 36 ARG 36 H A - 171.7 - - - -69.3 -29.8 - - - 175.2 -1.1 30.1 - * * * 37 GLN 37 H A - - -58.0 - - -71.6 -18.4 - - - 182.1 -1.3 36.0 - +* +* 38 TRP 38 H a - 163.8 - - - -96.4 -55.8 - - - 180.5 -.6 34.3 - * +** * +* +** 39 LEU 39 H A - - -62.7 158.3 - -72.5 -36.9 - - - 175.2 -3.7 34.3 - * ** ** 40 ARG 40 h l - - -48.8 181.3 - - - - - - 184.4 -1.4 32.0 - * * 41 PRO 41 T - - - - - -64.7 - - - - - 183.2 - 38.8 - * * 42 GLU 42 T A - 183.9 - 181.5 - - - - - - 183.1 - 33.2 - 43 VAL 43 T A - - -61.8 - - - - - - - 179.7 - 31.9 - 44 ARG 44 t B - - -67.2 180.4 - - - - - - 181.0 -2.9 32.7 - * * 45 SER 45 h B - - -56.3 - - - - - - - 178.1 - 35.2 - 46 LYS 46 H A 59.6 - - - - -51.7 -44.0 - - - 184.9 - 33.7 - * * 47 GLU 47 H A 45.6 - - - - -57.1 -35.7 - - - 174.9 - 27.2 - * +* +* 48 GLN 48 H A - - -66.8 - - -65.5 -37.4 - - - 183.0 -.8 34.4 - +* +* 49 MET 49 H A - - -59.1 180.9 - -63.7 -36.9 - - - 175.9 -1.0 32.8 - * * 50 LEU 50 H A - - -74.2 - - -57.5 -53.3 - - - 184.4 -1.3 34.3 - * * 51 GLU 51 H A - - -56.2 - - -62.8 -44.3 - - - 179.3 -1.4 33.5 - 52 LEU 52 H A - - -63.4 177.3 - -59.0 -41.6 - - - 181.2 -2.6 34.3 - 53 LEU 53 H A - 179.1 - - - -77.0 -30.3 - - - 175.4 -2.2 32.3 - 54 VAL 54 H A - 183.0 - - - -61.6 -40.2 - - - 177.9 -2.3 33.6 - Residue-by-residue listing for refined_9 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 - 185.1 - - - -56.5 -46.8 - - - 181.3 -2.0 35.5 - 56 GLU 56 H A - - -60.6 - - -53.4 -46.3 - - - 181.2 -1.2 34.5 - * * * 57 GLN 57 H A - 193.9 - - - -74.7 -47.4 - - - 186.1 -1.6 34.8 - * * 58 PHE 58 H A - 181.7 - - - -54.0 -47.2 - - - 179.0 -3.0 33.1 - * * 59 LEU 59 H A - - -92.5 - - -61.1 -39.5 - - - 180.9 -2.8 29.2 - +* * +* 60 GLY 60 H - - - - - - -80.8 -19.5 - - - 178.0 -1.0 - - * +* * +* 61 ALA 61 H A - - - - - -72.8 -28.8 - - - 176.1 -2.0 34.0 - 62 LEU 62 h B - - -67.0 170.6 - - - - - - 176.5 -1.3 36.9 - 63 PRO 63 h - - - - - -69.0 - - - - - 181.3 - 39.2 - +* +* 64 PRO 64 H - - - - - -41.9 -41.9 -47.3 - - - 180.9 - 38.7 - ** +* * ** 65 GLU 65 H A 58.0 - - 182.7 - -60.7 -47.5 - - - 180.0 - 32.6 - 66 ILE 66 H A - - -61.0 179.4 - -72.2 -43.4 - - - 181.0 - 34.8 - 67 GLN 67 H A - 178.9 - 178.8 - -59.2 -42.4 - - - 180.5 -3.5 34.5 - ** ** 68 ALA 68 H A - - - - - -62.8 -38.0 - - - 178.1 -2.8 33.4 - * * 69 ARG 69 H A - - -66.4 - - -62.6 -50.0 - - - 177.8 -1.1 34.8 - * * 70 VAL 70 H A - 174.7 - - - -60.4 -45.1 - - - 181.6 -2.1 35.6 - 71 GLN 71 H A - 212.7 - - - -58.1 -29.9 - - - 179.4 -3.1 35.2 - +* * +* 72 GLY 72 H - - - - - - -70.6 -28.0 - - - 180.4 -1.3 - - * * 73 GLN 73 H A - - -51.6 191.1 - -97.0 -47.1 - - - 185.1 -1.3 35.0 - * +** * +** 74 ARG 74 h l - - -70.2 - - - - - - - 180.8 -3.5 30.1 - ** * ** 75 PRO 75 - - - - - -67.4 - - - - - 177.7 - 39.4 - +* +* 76 GLY 76 - - - - - - - - - - - 178.7 - - - 77 SER 77 h B - - -60.8 - - - - - - - 183.3 - 34.3 - 78 PRO 78 H - - - - - -56.1 -56.1 -45.3 - - - 180.8 - 39.0 - * * 79 GLU 79 H A - - -65.1 173.3 - -65.6 -29.6 - - - 177.8 - 32.2 - 80 GLU 80 H A - 186.5 - - - -72.5 -47.4 - - - 175.5 - 35.3 - 81 ALA 81 H A - - - - - -56.2 -39.8 - - - 178.5 -2.5 34.2 - 82 ALA 82 H A - - - - - -55.0 -44.8 - - - 179.7 -2.6 34.5 - 83 ALA 83 H A - - - - - -67.2 -39.0 - - - 181.2 -1.4 34.1 - 84 LEU 84 H A - - -43.5 182.0 - -64.2 -48.8 - - - 184.0 -1.9 36.7 - +* +* 85 VAL 85 H A - - -58.6 - - -69.6 -30.8 - - - 175.1 -3.0 29.6 - * * * 86 ASP 86 H A - 174.7 - - - -53.0 -37.0 - - - 178.4 -1.9 33.5 - * * 87 GLY 87 H - - - - - - -82.8 -14.0 - - - 181.2 -.9 - - * ** * ** 88 LEU 88 H A - - -59.0 177.6 - -91.2 -41.5 - - - 180.2 -.9 34.3 - ** +* ** 89 ARG 89 H A 58.9 - - 177.9 - -61.9 -40.3 - - - 176.2 -3.2 32.6 - +* +* Residue-by-residue listing for refined_9 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 90 ARG 90 h B - - -68.0 180.0 - - - - - - 180.9 -1.0 34.7 - * * 91 GLU 91 B - - -68.2 184.8 - - - - - - 180.4 - 32.0 - 92 PRO 92 - - - - - -48.2 - - - - - 179.5 - 38.9 - +* * +* 93 GLY 93 - - - - - - - - - - - 178.2 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 179.9 - - - 96 SER 302 B - 184.3 - - - - - - - - 180.8 - 34.3 - 97 ASP 303 B - 192.3 - - - - - - - - 179.4 -1.0 35.6 - * * 98 PRO 304 h - - - - - -57.4 - - - - - 182.6 - 38.7 - * * 99 GLY 305 H - - - - - - 82.1 149.0 - - - 180.4 - - - *12.4**16.7* *16.7* 100 PRO 306 H - - - - - -55.9 -55.9 -22.8 - - - 177.4 - 38.1 - * * * 101 GLU 307 H A 57.0 - - 174.5 - -75.1 -54.4 - - - 184.4 - 32.3 - * * 102 ALA 308 H A - - - - - -75.7 -35.7 - - - 180.4 -.9 32.5 - +* +* 103 ALA 309 H A - - - - - -62.8 -45.1 - - - 177.1 -3.1 33.4 - * * 104 ARG 310 H A - 168.9 - 168.6 - -65.3 -34.0 - - - 179.4 -.8 33.3 - +* +* 105 LEU 311 H A - 173.7 - - - -62.8 -47.6 - - - 176.8 -1.3 35.1 - 106 ARG 312 H A - - -57.8 176.3 - -60.0 -48.4 - - - 183.2 -2.5 37.0 - 107 PHE 313 H A - 169.5 - - - -61.7 -49.5 - - - 183.4 -2.5 34.1 - 108 ARG 314 H A - - -66.5 - - -75.9 -27.7 - - - 179.1 -3.5 30.8 - * +* +* 109 CYS 315 h A - - -58.3 - - - - - - - 179.8 -1.7 33.8 - 110 PHE 316 t B - 180.9 - - - - - - - - 177.4 -.7 35.1 - +* +* 111 HIS 317 B 74.3 - - - - - - - - - 174.4 - 33.9 - 112 TYR 318 B - 163.3 - - - - - - - - 180.2 -1.2 32.8 - * * * 113 GLU 319 t B 48.7 - - 180.0 - - - - - - 183.1 -.6 31.9 - +* +* 114 GLU 320 T A - - -58.0 171.5 - - - - - - 181.6 -.7 36.3 - +* +* 115 ALA 321 T A - - - - - - - - - - 182.9 - 34.5 - 116 THR 322 T A - 210.7 - - - - - - - - 181.3 -1.1 34.2 - +* * +* 117 GLY 323 h - - - - - - - - - - - 184.5 -.9 - - * * 118 PRO 324 H - - - - - -81.4 -81.4 -34.0 - - - 184.4 - 38.5 - * * * * 119 GLN 325 H A - 193.0 - 170.3 - -78.2 -32.0 - - - 174.9 - 34.5 - * * 120 GLU 326 H A - 183.4 - 175.3 - -73.8 -33.5 - - - 174.4 - 33.5 - 121 ALA 327 H A - - - - - -66.2 -36.9 - - - 174.7 -1.3 33.9 - * * 122 LEU 328 H A - - -65.3 180.2 - -60.1 -38.2 - - - 177.7 -1.9 33.9 - 123 ALA 329 H A - - - - - -61.5 -33.1 - - - 179.1 -1.4 33.7 - 124 GLN 330 H A - - -45.5 - - -75.9 -47.9 - - - 179.8 -1.1 36.0 - * * * Residue-by-residue listing for refined_9 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 - - -68.8 171.5 - -60.4 -44.2 - - - 179.4 -3.0 33.0 - * * 126 ARG 332 H A 66.5 - - 185.0 - -67.5 -29.9 - - - 174.8 -3.5 30.5 - ** ** 127 GLU 333 H A - 174.2 - 177.3 - -67.8 -51.2 - - - 181.4 -1.0 34.7 - * * * 128 LEU 334 H A - - -59.8 177.7 - -64.7 -42.5 - - - 178.5 -3.2 33.4 - +* +* 129 CYS 335 H A 71.3 - - - - -65.2 -36.0 - - - 177.2 -3.4 33.1 - +* +* 130 ARG 336 H A - 172.4 - - - -68.8 -30.5 - - - 175.3 -1.7 30.7 - 131 GLN 337 H A - - -62.8 184.3 - -67.9 -24.8 - - - 181.9 -1.7 35.4 - * * 132 TRP 338 H a - 165.0 - - - -91.7 -62.7 - - - 183.4 -1.0 35.2 - * ** ** * ** 133 LEU 339 H A - - -61.0 158.1 - -70.2 -36.2 - - - 177.0 -3.6 35.1 - * ** ** 134 ARG 340 h l - - -57.6 182.3 - - - - - - 182.1 -1.1 31.5 - * * 135 PRO 341 T - - - - - -66.7 - - - - - 182.1 - 39.2 - +* +* 136 GLU 342 T A - - -52.4 174.1 - - - - - - 186.1 - 37.3 - * * 137 VAL 343 T A - - -61.2 - - - - - - - 180.1 -.9 33.8 - +* +* 138 ARG 344 t B - - -66.2 184.4 - - - - - - 180.8 -2.8 31.9 - * * 139 SER 345 h B - - -58.5 - - - - - - - 180.8 - 35.3 - 140 LYS 346 H A 64.1 - - - - -55.5 -41.3 - - - 186.0 - 34.7 - * * 141 GLU 347 H A 45.0 - - - - -52.6 -43.2 - - - 177.3 - 28.0 - * * +* +* 142 GLN 348 H A - - -68.2 - - -66.9 -33.0 - - - 181.7 -.6 32.9 - +* +* 143 MET 349 H A - - -58.3 183.1 - -65.1 -40.0 - - - 174.6 -.9 32.7 - +* +* 144 LEU 350 H A - - -75.5 - - -57.8 -53.9 - - - 182.9 -1.6 34.6 - * * 145 GLU 351 H A - - -58.3 - - -56.7 -49.7 - - - 181.2 -1.8 35.0 - 146 LEU 352 H A - - -62.6 176.9 - -60.8 -39.0 - - - 180.6 -3.1 34.4 - * * 147 LEU 353 H A - 178.8 - - - -77.2 -30.1 - - - 175.2 -2.0 31.3 - * * 148 VAL 354 H A - 187.4 - - - -59.1 -46.3 - - - 178.8 -2.3 34.7 - 149 LEU 355 H A - 180.4 - - - -56.0 -43.4 - - - 183.7 -1.9 36.0 - 150 GLU 356 H A - 201.9 - - - -54.7 -52.7 - - - 181.8 -1.3 36.1 - * * * * 151 GLN 357 H A - 190.2 - - - -74.2 -41.6 - - - 182.0 -1.8 33.2 - 152 PHE 358 H A - 175.5 - - - -53.0 -47.9 - - - 177.5 -3.1 33.2 - * * * 153 LEU 359 H A - - -92.1 - - -60.7 -39.7 - - - 179.8 -2.8 29.8 - +* * * +* 154 GLY 360 H - - - - - - -81.5 -10.0 - - - 176.9 -1.2 - - * +** * +** 155 ALA 361 H A - - - - - -81.1 -26.4 - - - 176.5 -1.3 34.1 - * * * * Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 156 LEU 362 h B - - -65.8 170.2 - - - - - - 176.0 -1.1 37.0 - * * 157 PRO 363 h - - - - - -67.5 - - - - - 182.2 - 39.3 - +* +* 158 PRO 364 H - - - - - -42.5 -42.5 -45.8 - - - 181.6 - 38.6 - ** +* * ** 159 GLU 365 H A 61.2 - - 187.7 - -63.7 -47.8 - - - 180.2 - 33.0 - 160 ILE 366 H A - - -58.8 179.2 - -71.4 -41.2 - - - 181.3 - 34.8 - 161 GLN 367 H A - 179.6 - 178.9 - -60.7 -43.3 - - - 180.5 -3.4 34.1 - +* +* 162 ALA 368 H A - - - - - -60.9 -33.8 - - - 180.2 -2.7 33.5 - 163 ARG 369 H A - - -50.0 - - -65.8 -48.7 - - - 179.8 -1.0 35.8 - * * * 164 VAL 370 H A - 180.1 - - - -66.7 -40.1 - - - 181.7 -1.8 36.0 - 165 GLN 371 H A - 199.9 - - - -55.0 -30.3 - - - 178.5 -3.1 35.8 - * * 166 GLY 372 H - - - - - - -75.3 -40.7 - - - 181.7 -1.0 - - * * 167 GLN 373 H A - - -61.2 182.7 - -77.2 -50.2 - - - 184.0 -1.0 34.8 - * * 168 ARG 374 h l - - -60.7 - - - - - - - 177.5 -3.4 31.4 - +* +* 169 PRO 375 - - - - - -61.9 - - - - - 177.4 - 39.3 - +* +* 170 GLY 376 - - - - - - - - - - - 177.1 - - - 171 SER 377 h B - - -55.2 - - - - - - - 186.7 - 34.7 - * * 172 PRO 378 H - - - - - -58.8 -58.8 -45.4 - - - 183.4 - 37.4 - 173 GLU 379 H A - - -45.9 - - -73.6 -30.7 - - - 178.0 - 33.2 - * * 174 GLU 380 H A - 185.7 - - - -65.1 -45.5 - - - 175.4 - 33.6 - 175 ALA 381 H A - - - - - -60.1 -47.2 - - - 179.7 -2.4 34.1 - 176 ALA 382 H A - - - - - -55.8 -35.9 - - - 178.9 -2.7 34.2 - 177 ALA 383 H A - - - - - -64.0 -40.5 - - - 175.3 -2.0 32.7 - 178 LEU 384 H A 50.9 - - 152.5 - -78.0 -37.1 - - - 179.2 -1.3 28.6 - * * +* +* 179 VAL 385 H A - 176.7 - - - -59.8 -35.3 - - - 176.3 -3.0 33.2 - * * 180 ASP 386 H A - 175.8 - - - -58.2 -36.4 - - - 177.7 -2.3 33.8 - 181 GLY 387 H - - - - - - -84.8 -14.6 - - - 181.7 -.8 - - +* ** +* ** 182 LEU 388 H A - - -59.8 177.4 - -89.5 -42.5 - - - 180.9 -.8 34.6 - ** +* ** 183 ARG 389 H A 58.6 - - 173.3 - -62.5 -31.2 - - - 180.2 -3.1 33.9 - * * 184 ARG 390 h B - - -67.0 178.1 - - - - - - 174.4 -.6 35.1 - +* +* 185 GLU 391 B - - -55.9 185.6 - - - - - - 185.0 - 34.0 - 186 PRO 392 - - - - - -58.5 - - - - - 177.9 - 38.2 - * * 187 GLY 393 - - - - - - - - - - - 178.5 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +* +* +* * ***12.4**16.7* * ** +* *16.7* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_9 Page 7 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.0 181.3 -62.8 177.6 -59.8 -64.8 -37.9 - - - 179.7 -1.9 34.3 Standard deviations: 10.0 10.7 9.2 7.2 9.6 16.3 19.0 - - - 2.8 .9 2.3 Numbers of values: 19 47 66 57 18 127 127 0 0 0 186 126 170 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_9 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 - 1.236 1.499 - 1.457 - 116.77 120.18 - 110.82 - 123.04 2 SER 2 1.305 1.235 1.515 1.543 1.434 122.32 116.45 120.53 110.53 108.44 110.47 122.99 +* * +* 3 ASP 3 1.301 1.238 1.521 1.533 1.447 121.55 118.08 119.61 110.61 108.49 110.40 122.31 ** ** 4 PRO 4 1.353 1.241 1.535 1.539 1.475 123.04 116.62 120.65 110.21 113.67 103.99 122.72 5 GLY 5 1.315 1.240 1.513 - 1.430 120.42 118.27 120.29 - 111.83 - 121.44 * * 6 PRO 6 1.343 1.222 1.523 1.522 1.475 122.93 115.71 121.18 110.02 111.69 103.33 123.10 7 GLU 7 1.315 1.231 1.538 1.523 1.447 122.94 116.72 120.63 111.63 111.35 109.37 122.60 * * 8 ALA 8 1.329 1.235 1.517 1.517 1.449 121.46 115.42 121.22 110.97 109.68 110.67 123.35 9 ALA 9 1.321 1.232 1.522 1.505 1.448 122.42 115.85 120.92 110.42 109.73 110.02 123.22 10 ARG 10 1.333 1.220 1.516 1.530 1.447 122.11 116.34 120.68 110.94 110.93 111.88 122.97 11 LEU 11 1.321 1.221 1.534 1.524 1.406 122.43 116.72 120.26 112.43 109.86 108.57 122.97 +** * * +** 12 ARG 12 1.335 1.231 1.529 1.534 1.474 121.90 114.27 121.69 107.79 109.22 110.75 124.03 * * 13 PHE 13 1.316 1.216 1.544 1.534 1.456 124.80 117.37 120.51 112.48 112.69 107.40 122.11 +* * +* +* 14 ARG 14 1.319 1.231 1.527 1.541 1.465 121.25 117.01 120.36 111.61 112.62 112.47 122.63 * * Residue-by-residue listing for refined_9 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 1.316 1.233 1.521 1.525 1.457 121.28 116.56 120.80 110.48 111.25 111.35 122.64 16 PHE 16 1.316 1.247 1.522 1.534 1.438 121.25 115.81 121.10 110.67 109.32 110.85 123.07 * * 17 HIS 17 1.304 1.240 1.499 1.566 1.439 121.55 117.67 119.85 109.30 107.38 112.29 122.47 +* * +* * * +* 18 TYR 18 1.289 1.228 1.518 1.525 1.415 118.62 114.11 121.80 112.64 110.42 112.91 124.05 +** ** +* * * * +** 19 GLU 19 1.290 1.236 1.533 1.557 1.425 124.40 115.26 121.27 114.68 109.83 108.77 123.44 +** * +* +* ** * +** 20 GLU 20 1.338 1.232 1.508 1.518 1.476 123.95 115.54 120.69 108.85 111.73 110.23 123.78 * * 21 ALA 21 1.316 1.225 1.517 1.507 1.457 123.49 114.40 121.81 108.39 110.78 108.44 123.78 * * * 22 THR 22 1.287 1.237 1.537 1.493 1.419 124.09 116.15 121.07 111.59 112.69 104.10 122.63 +** +* ** * * **** **** 23 GLY 23 1.312 1.245 1.516 - 1.436 120.78 118.44 120.36 - 111.73 - 121.20 * * * 24 PRO 24 1.341 1.222 1.531 1.521 1.459 122.35 117.20 120.15 110.72 113.00 103.08 122.62 25 GLN 25 1.339 1.236 1.509 1.536 1.462 120.75 115.82 120.85 108.52 110.94 113.65 123.34 +* +* 26 GLU 26 1.316 1.227 1.519 1.515 1.448 121.13 116.23 120.85 110.85 110.54 110.89 122.91 27 ALA 27 1.322 1.224 1.528 1.518 1.461 121.91 116.00 120.70 110.83 109.91 109.99 123.29 28 LEU 28 1.328 1.220 1.511 1.516 1.462 122.49 117.00 120.00 108.91 112.05 111.82 123.00 29 ALA 29 1.329 1.233 1.519 1.524 1.464 121.59 114.90 121.44 110.72 109.65 110.70 123.62 30 GLN 30 1.308 1.219 1.530 1.545 1.446 123.38 116.72 120.52 111.97 111.25 109.76 122.73 * * 31 LEU 31 1.318 1.226 1.508 1.519 1.464 122.14 117.70 119.77 110.54 113.35 111.55 122.51 32 ARG 32 1.330 1.208 1.518 1.547 1.457 120.34 115.73 121.01 112.02 109.75 113.31 123.23 * * +* +* 33 GLU 33 1.318 1.232 1.538 1.528 1.438 122.33 115.74 121.01 109.75 109.54 109.07 123.23 * * 34 LEU 34 1.328 1.232 1.511 1.523 1.462 122.95 117.05 120.22 110.56 112.78 111.03 122.73 35 CYS 35 1.319 1.215 1.527 1.534 1.452 120.28 116.24 121.07 111.85 109.71 111.37 122.67 36 ARG 36 1.323 1.218 1.538 1.543 1.429 122.59 117.00 120.34 115.40 111.86 110.62 122.65 +* +** +** 37 GLN 37 1.326 1.230 1.533 1.528 1.483 121.93 114.84 121.79 107.72 109.66 110.33 123.35 * * * 38 TRP 38 1.302 1.229 1.542 1.539 1.442 124.33 116.37 120.87 113.05 112.20 107.15 122.76 +* * +* +* +* 39 LEU 39 1.300 1.226 1.533 1.526 1.454 123.09 115.18 120.73 112.80 110.21 107.71 124.07 ** * +* ** 40 ARG 40 1.336 1.227 1.537 1.535 1.474 125.16 116.93 121.17 111.99 113.03 110.83 121.90 +* +* 41 PRO 41 1.346 1.234 1.521 1.529 1.473 123.49 117.36 120.17 109.46 115.04 103.63 122.47 * * 42 GLU 42 1.311 1.234 1.523 1.528 1.443 119.59 116.56 120.70 110.58 110.96 111.55 122.69 * * * 43 VAL 43 1.317 1.232 1.521 1.552 1.452 120.67 116.99 120.41 110.72 112.79 112.62 122.58 44 ARG 44 1.312 1.238 1.505 1.525 1.453 121.05 115.49 120.96 110.55 111.31 112.08 123.54 * * 45 SER 45 1.300 1.244 1.533 1.530 1.426 122.50 115.67 120.71 110.08 110.43 109.38 123.62 ** +* ** 46 LYS 46 1.341 1.216 1.523 1.562 1.468 123.09 115.35 121.18 108.77 112.07 112.37 123.44 +* * +* Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 47 GLU 47 1.302 1.243 1.545 1.551 1.462 123.06 117.55 119.92 115.06 115.73 112.37 122.52 +* * +** +* * +** 48 GLN 48 1.328 1.233 1.520 1.535 1.464 121.57 115.58 121.10 108.95 110.51 111.50 123.30 49 MET 49 1.321 1.232 1.508 1.508 1.451 122.56 116.55 119.96 111.73 112.15 110.27 123.48 * * 50 LEU 50 1.345 1.211 1.513 1.570 1.468 121.40 116.21 120.46 108.83 109.34 112.61 123.12 * ** * ** 51 GLU 51 1.331 1.236 1.524 1.531 1.463 122.02 116.42 120.70 109.99 111.65 111.29 122.87 52 LEU 52 1.326 1.232 1.524 1.528 1.446 121.88 115.92 120.75 110.14 110.97 110.30 123.32 53 LEU 53 1.317 1.239 1.551 1.520 1.427 122.46 117.59 120.29 114.83 112.68 107.76 122.11 * +* ** +* ** 54 VAL 54 1.331 1.232 1.543 1.570 1.473 120.73 115.58 120.99 109.19 109.10 113.04 123.41 * * 55 LEU 55 1.341 1.242 1.520 1.560 1.476 123.54 114.96 120.78 110.53 109.57 108.78 124.26 +* * * +* 56 GLU 56 1.326 1.234 1.523 1.538 1.462 123.61 116.53 120.72 109.52 111.80 110.48 122.74 * * 57 GLN 57 1.321 1.230 1.512 1.546 1.446 120.38 115.70 120.15 110.24 109.48 110.23 124.09 58 PHE 58 1.332 1.236 1.516 1.534 1.455 123.07 116.59 120.48 110.93 112.13 110.83 122.92 59 LEU 59 1.322 1.214 1.510 1.543 1.452 120.68 117.77 119.52 113.20 113.74 113.11 122.65 +* +* +* 60 GLY 60 1.319 1.234 1.508 - 1.449 119.28 115.98 120.68 - 112.24 - 123.34 61 ALA 61 1.323 1.241 1.518 1.518 1.451 122.40 115.33 120.83 110.49 110.19 110.63 123.83 62 LEU 62 1.326 1.240 1.536 1.533 1.452 123.57 118.78 119.80 108.17 109.64 108.83 121.41 * * * * 63 PRO 63 1.348 1.237 1.517 1.542 1.455 121.77 118.13 119.04 109.26 108.95 104.54 122.83 * * * * 64 PRO 64 1.346 1.225 1.537 1.517 1.477 123.85 116.84 120.29 110.60 113.74 102.51 122.83 65 GLU 65 1.334 1.236 1.542 1.532 1.463 121.83 117.00 120.29 111.48 112.51 110.74 122.68 66 ILE 66 1.331 1.239 1.533 1.551 1.448 121.80 115.33 121.25 110.10 110.11 110.19 123.39 67 GLN 67 1.321 1.227 1.520 1.522 1.449 123.24 116.49 120.31 110.14 111.62 109.87 123.21 68 ALA 68 1.324 1.235 1.529 1.515 1.463 122.32 116.54 120.43 110.49 111.86 110.71 123.03 69 ARG 69 1.328 1.232 1.520 1.525 1.469 121.74 115.20 121.31 109.31 109.55 110.73 123.48 70 VAL 70 1.322 1.230 1.512 1.541 1.452 122.77 115.09 121.13 108.34 110.32 110.67 123.78 71 GLN 71 1.314 1.226 1.535 1.524 1.447 123.75 116.30 120.62 109.13 111.06 109.88 123.08 * * * 72 GLY 72 1.325 1.240 1.521 - 1.447 121.31 116.85 120.69 - 112.64 - 122.46 73 GLN 73 1.319 1.228 1.512 1.519 1.447 120.61 114.80 121.20 108.41 109.93 111.34 123.98 74 ARG 74 1.331 1.219 1.517 1.534 1.453 123.91 116.66 121.12 112.43 112.00 113.46 122.17 * * +* +* 75 PRO 75 1.343 1.222 1.525 1.534 1.470 122.58 114.97 121.55 110.14 111.82 102.70 123.45 * * * 76 GLY 76 1.307 1.230 1.511 - 1.445 122.37 116.09 120.27 - 112.80 - 123.56 +* * +* 77 SER 77 1.319 1.242 1.535 1.531 1.444 122.76 117.59 120.11 110.93 109.36 110.07 122.28 78 PRO 78 1.355 1.223 1.525 1.528 1.479 123.25 116.31 120.68 109.14 113.52 103.86 123.00 79 GLU 79 1.317 1.229 1.521 1.517 1.464 122.63 116.12 120.84 112.91 111.94 109.98 123.02 * * 80 GLU 80 1.315 1.222 1.531 1.528 1.419 122.27 116.03 120.67 111.31 107.27 108.91 123.27 * ** * ** 81 ALA 81 1.355 1.222 1.532 1.514 1.453 122.46 116.18 120.29 110.42 111.08 109.99 123.52 +* +* 82 ALA 82 1.336 1.228 1.523 1.522 1.467 123.27 115.39 121.36 110.13 111.09 109.80 123.23 83 ALA 83 1.299 1.237 1.523 1.515 1.447 122.68 116.18 120.56 110.42 110.94 110.17 123.25 ** ** Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 84 LEU 84 1.335 1.237 1.525 1.542 1.460 121.79 114.69 121.65 106.28 108.56 111.37 123.64 ** ** 85 VAL 85 1.332 1.228 1.501 1.539 1.449 123.12 116.69 120.17 111.89 113.16 114.11 123.11 * * +* +* 86 ASP 86 1.319 1.226 1.538 1.531 1.466 121.79 115.88 120.80 110.33 111.04 111.03 123.27 87 GLY 87 1.324 1.236 1.528 - 1.456 121.98 116.00 121.18 - 112.51 - 122.77 88 LEU 88 1.313 1.233 1.530 1.532 1.455 122.27 116.38 120.65 110.45 111.25 109.84 122.97 * * 89 ARG 89 1.337 1.226 1.529 1.545 1.469 121.77 115.50 120.85 111.10 110.86 111.84 123.64 90 ARG 90 1.316 1.232 1.492 1.544 1.447 124.55 117.49 119.07 109.17 106.41 112.41 123.44 +* +* * +* * +* 91 GLU 91 1.313 1.248 1.520 1.520 1.446 120.60 116.41 120.37 110.83 111.99 112.33 123.21 * * * 92 PRO 92 1.358 1.247 1.519 1.527 1.464 123.76 115.66 121.12 109.93 113.01 103.41 123.22 * * 93 GLY 93 1.299 1.239 1.491 - 1.414 121.45 116.41 120.19 - 110.75 - 123.39 ** * ** ** 94 GLY 94 1.298 1.252 1.504 - 1.437 120.88 - 119.83 - 111.10 - - ** * ** 95 GLY 301 - 1.240 1.510 - 1.450 - 115.45 121.12 - 111.44 - 123.43 96 SER 302 1.303 1.243 1.522 1.538 1.431 122.11 116.09 121.21 110.95 108.99 110.33 122.64 +* * +* 97 ASP 303 1.303 1.239 1.501 1.535 1.438 121.38 118.46 119.21 109.42 107.71 110.40 122.31 +* * * * * +* 98 PRO 304 1.344 1.235 1.523 1.538 1.460 122.57 116.46 120.93 109.98 112.09 104.02 122.60 99 GLY 305 1.312 1.246 1.511 - 1.421 120.08 117.95 120.27 - 111.35 - 121.78 * +* +* 100 PRO 306 1.337 1.238 1.548 1.531 1.474 123.14 116.96 120.89 110.92 113.29 103.26 122.15 * * 101 GLU 307 1.323 1.234 1.545 1.548 1.443 120.91 116.76 120.40 111.37 111.40 111.93 122.79 102 ALA 308 1.332 1.225 1.516 1.518 1.457 121.99 116.95 120.29 110.90 112.44 111.37 122.76 103 ALA 309 1.325 1.230 1.521 1.505 1.459 120.99 115.94 120.92 110.95 110.52 110.69 123.09 104 ARG 310 1.324 1.225 1.521 1.511 1.444 121.80 116.11 120.53 110.87 111.70 110.65 123.35 105 LEU 311 1.319 1.232 1.530 1.522 1.415 123.19 116.01 120.50 111.82 109.93 107.90 123.47 ** +* ** 106 ARG 312 1.335 1.234 1.520 1.529 1.472 122.55 113.88 121.80 106.76 109.15 110.05 124.31 * +* +* 107 PHE 313 1.315 1.203 1.533 1.532 1.443 124.82 118.19 120.11 111.77 114.04 108.02 121.70 * +* * * +* 108 ARG 314 1.309 1.234 1.523 1.533 1.463 120.55 117.04 120.30 112.77 113.01 111.70 122.62 * * * 109 CYS 315 1.314 1.235 1.531 1.517 1.455 121.20 115.81 120.62 110.37 111.13 110.52 123.58 * * 110 PHE 316 1.331 1.246 1.522 1.539 1.459 123.52 116.24 121.03 110.26 110.81 109.25 122.71 * * 111 HIS 317 1.309 1.244 1.505 1.571 1.434 120.27 117.06 120.11 109.85 107.89 112.85 122.80 * ** * * * ** 112 TYR 318 1.300 1.228 1.507 1.530 1.427 119.53 115.17 121.33 111.75 109.19 111.65 123.49 ** +* * ** 113 GLU 319 1.288 1.235 1.513 1.538 1.418 122.25 114.39 121.81 113.94 110.30 110.53 123.79 +** ** ** +** 114 GLU 320 1.310 1.234 1.522 1.510 1.454 124.60 115.52 120.57 109.05 111.48 108.20 123.90 * +* * +* 115 ALA 321 1.321 1.230 1.519 1.519 1.450 123.49 117.05 120.38 109.77 112.05 110.00 122.56 Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 116 THR 322 1.326 1.218 1.544 1.579 1.442 120.18 115.80 121.40 111.35 108.72 110.45 122.76 * * * 117 GLY 323 1.331 1.226 1.507 - 1.453 121.53 120.52 119.28 - 110.13 - 120.19 +* +* +* 118 PRO 324 1.339 1.215 1.504 1.511 1.444 120.26 115.44 121.20 110.60 112.07 103.42 123.34 * * * 119 GLN 325 1.292 1.231 1.520 1.488 1.400 123.30 116.09 121.06 113.66 110.10 106.68 122.82 +** ** *** +* ** *** 120 GLU 326 1.326 1.225 1.522 1.525 1.439 120.97 115.80 121.29 111.49 108.38 111.06 122.91 * * * 121 ALA 327 1.330 1.222 1.526 1.521 1.455 121.99 116.26 120.74 110.74 109.29 110.75 122.99 122 LEU 328 1.333 1.209 1.504 1.526 1.462 122.09 116.57 120.29 108.55 110.75 112.58 123.14 * * * * 123 ALA 329 1.327 1.230 1.526 1.523 1.456 121.85 115.90 120.97 110.72 110.26 110.78 123.11 124 GLN 330 1.324 1.211 1.517 1.541 1.459 122.29 115.60 121.11 108.37 107.97 110.45 123.29 * * 125 LEU 331 1.321 1.214 1.500 1.515 1.455 122.93 117.45 119.88 110.56 112.58 111.08 122.67 * * 126 ARG 332 1.324 1.222 1.523 1.541 1.444 120.12 116.15 120.61 113.04 110.24 113.18 123.17 +* +* +* 127 GLU 333 1.324 1.229 1.523 1.536 1.448 122.09 115.80 120.74 110.49 109.79 109.84 123.38 128 LEU 334 1.318 1.231 1.526 1.531 1.453 122.64 117.03 120.41 110.90 111.56 110.67 122.56 129 CYS 335 1.332 1.214 1.536 1.551 1.448 120.87 116.99 120.75 111.28 109.61 111.53 122.24 * * 130 ARG 336 1.337 1.217 1.531 1.548 1.432 122.19 117.32 119.95 114.71 112.08 110.52 122.72 * ** ** 131 GLN 337 1.328 1.225 1.528 1.513 1.471 121.90 114.51 121.67 108.42 110.57 110.24 123.82 132 TRP 338 1.311 1.232 1.543 1.549 1.449 124.91 115.64 121.11 112.21 112.31 106.70 123.26 * +* * ** ** 133 LEU 339 1.306 1.230 1.529 1.531 1.454 123.91 115.43 120.58 111.91 110.65 107.56 123.98 +* * +* +* 134 ARG 340 1.341 1.225 1.535 1.536 1.468 124.48 117.69 120.86 111.77 113.57 111.50 121.45 +* +* 135 PRO 341 1.351 1.221 1.512 1.528 1.475 122.90 115.37 120.76 109.54 112.69 103.44 123.86 * * * 136 GLU 342 1.311 1.224 1.518 1.524 1.447 123.37 115.45 121.46 107.98 109.90 108.37 123.07 * * * * 137 VAL 343 1.313 1.238 1.530 1.554 1.448 121.69 116.88 120.84 110.43 112.40 110.46 122.27 * * 138 ARG 344 1.310 1.251 1.506 1.532 1.441 120.61 114.06 121.88 110.76 112.54 112.61 124.06 * * * * 139 SER 345 1.291 1.238 1.504 1.524 1.413 123.98 115.07 121.05 111.20 109.57 108.50 123.87 +** * ** * * +** 140 LYS 346 1.305 1.213 1.529 1.541 1.446 123.43 115.68 120.88 109.38 112.37 110.31 123.40 +* +* 141 GLU 347 1.309 1.230 1.543 1.548 1.464 123.14 117.99 119.94 114.30 115.72 112.27 122.05 * ** +* * ** 142 GLN 348 1.320 1.226 1.509 1.527 1.456 120.33 116.24 120.61 110.00 111.37 112.29 123.13 * * 143 MET 349 1.315 1.231 1.502 1.501 1.453 121.71 116.28 120.05 111.39 111.36 111.01 123.66 * * * * 144 LEU 350 1.343 1.219 1.514 1.568 1.460 121.15 115.50 120.50 108.73 109.01 112.28 123.76 +* * +* 145 GLU 351 1.330 1.245 1.531 1.524 1.465 123.36 115.88 121.04 109.08 112.04 109.92 123.08 146 LEU 352 1.324 1.245 1.525 1.532 1.444 122.79 116.02 120.80 110.34 111.38 109.91 123.17 Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 147 LEU 353 1.308 1.235 1.550 1.523 1.423 122.10 117.75 120.07 115.37 112.59 108.56 122.17 +* * +* +** * +** 148 VAL 354 1.338 1.227 1.534 1.560 1.476 120.53 114.82 121.29 107.36 108.61 113.35 123.87 * * 149 LEU 355 1.334 1.240 1.521 1.556 1.470 124.19 114.91 120.82 110.54 110.30 107.96 124.27 * * * * 150 GLU 356 1.325 1.245 1.544 1.553 1.454 123.52 116.28 120.88 109.99 109.16 108.53 122.81 * * * * 151 GLN 357 1.325 1.223 1.514 1.543 1.452 121.41 116.64 119.54 112.06 110.08 110.50 123.77 * * 152 PHE 358 1.339 1.234 1.523 1.545 1.464 122.38 116.69 120.47 110.52 111.56 111.38 122.83 153 LEU 359 1.322 1.210 1.513 1.537 1.458 120.72 117.55 119.85 113.16 113.24 112.52 122.56 * +* * +* 154 GLY 360 1.318 1.241 1.523 - 1.457 119.71 116.42 120.55 - 113.16 - 123.00 155 ALA 361 1.325 1.242 1.511 1.529 1.452 122.27 114.73 120.98 110.56 109.04 110.80 124.28 156 LEU 362 1.330 1.242 1.526 1.534 1.442 124.00 117.91 120.12 108.07 110.01 108.91 121.96 * * * 157 PRO 363 1.348 1.240 1.517 1.541 1.454 122.07 118.21 119.06 109.28 108.72 104.44 122.73 * * * * 158 PRO 364 1.350 1.224 1.536 1.525 1.475 123.55 116.68 120.26 110.57 113.65 102.81 123.02 159 GLU 365 1.329 1.224 1.546 1.530 1.459 122.06 117.62 120.09 111.33 112.72 110.26 122.27 160 ILE 366 1.339 1.237 1.521 1.551 1.454 121.30 115.23 121.24 109.25 109.72 111.11 123.50 161 GLN 367 1.319 1.218 1.515 1.519 1.440 122.74 116.38 120.14 110.17 111.17 110.48 123.48 162 ALA 368 1.326 1.238 1.527 1.519 1.468 122.75 116.47 120.46 110.18 112.22 110.79 123.07 163 ARG 369 1.330 1.236 1.523 1.530 1.464 121.42 114.79 121.76 107.98 108.39 110.86 123.44 * * * 164 VAL 370 1.322 1.229 1.513 1.540 1.455 123.02 114.34 121.49 107.62 110.13 110.75 124.17 165 GLN 371 1.304 1.223 1.533 1.520 1.449 124.96 116.70 120.37 109.31 111.51 108.73 122.93 +* +* * +* 166 GLY 372 1.321 1.234 1.521 - 1.445 120.14 116.20 120.53 - 112.21 - 123.22 167 GLN 373 1.330 1.224 1.515 1.534 1.461 122.12 115.17 121.03 108.75 111.18 110.95 123.79 168 ARG 374 1.324 1.226 1.533 1.544 1.462 123.86 117.31 120.68 111.43 112.14 112.64 121.92 * * * 169 PRO 375 1.353 1.223 1.518 1.535 1.471 122.50 114.76 121.90 109.74 110.67 103.41 123.34 * * 170 GLY 376 1.311 1.236 1.508 - 1.433 121.83 115.97 120.55 - 112.70 - 123.45 * * * 171 SER 377 1.299 1.248 1.526 1.508 1.425 122.26 117.38 120.08 111.02 108.09 109.66 122.54 ** * +* * ** 172 PRO 378 1.338 1.237 1.528 1.536 1.462 122.99 117.39 120.07 110.62 114.45 104.58 122.50 * * * 173 GLU 379 1.322 1.225 1.497 1.529 1.456 120.81 115.87 120.68 110.08 110.31 112.33 123.44 * * * 174 GLU 380 1.320 1.233 1.528 1.532 1.436 121.13 116.25 120.58 111.19 108.66 111.06 123.16 * * 175 ALA 381 1.347 1.225 1.515 1.509 1.446 121.72 116.03 120.50 110.27 110.22 110.49 123.44 * * 176 ALA 382 1.331 1.225 1.528 1.524 1.463 122.92 115.54 121.04 110.44 111.25 109.94 123.42 177 ALA 383 1.302 1.237 1.531 1.518 1.451 123.35 118.12 120.11 111.32 111.67 110.99 121.77 +* +* 178 LEU 384 1.346 1.225 1.508 1.552 1.457 118.13 116.31 120.32 110.79 111.41 117.43 123.34 * * +* **** **** 179 VAL 385 1.334 1.236 1.528 1.554 1.466 122.77 115.96 121.07 110.28 111.03 111.89 122.95 180 ASP 386 1.314 1.236 1.536 1.529 1.459 122.59 115.57 121.02 111.08 110.80 109.96 123.38 * * Residue-by-residue listing for refined_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 181 GLY 387 1.323 1.223 1.530 - 1.451 122.28 116.56 120.64 - 112.63 - 122.77 182 LEU 388 1.325 1.229 1.525 1.529 1.468 122.57 116.25 120.45 109.15 111.81 110.50 123.30 183 ARG 389 1.337 1.222 1.530 1.541 1.476 122.34 116.04 121.32 109.62 111.54 111.14 122.64 184 ARG 390 1.300 1.232 1.497 1.536 1.436 122.07 116.23 120.62 109.04 109.09 111.10 123.14 ** * * ** 185 GLU 391 1.288 1.234 1.506 1.518 1.423 121.68 117.12 120.34 110.96 107.22 111.18 122.47 +** +* * +** 186 PRO 392 1.337 1.237 1.524 1.531 1.464 122.93 115.91 120.97 110.27 113.03 104.04 123.09 187 GLY 393 1.323 1.233 1.504 - 1.442 121.26 115.73 120.92 - 111.27 - 123.36 188 GLY 394 1.303 - 1.494 - 1.424 121.96 - - - 109.59 - - +* * +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +** * +* ** *** +* +* * +** +* **** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_9 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 1.287 1.355 1.320 .013 +** +* C-N (Pro) 1.341 .016 18 1.337 1.358 1.346 .006 * C-O C-O 1.231 .020 187 1.203 1.252 1.231 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 170 1.492 1.551 1.523 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.491 1.530 1.511 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.505 1.529 1.517 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.493 1.579 1.549 .020 +* * CH1E-CH2E (the rest) 1.530 .020 138 1.488 1.571 1.533 .013 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.400 1.483 1.451 .015 *** * NH1-CH2G* (Gly) 1.451 .016 18 1.414 1.457 1.442 .013 ** N-CH1E (Pro) 1.466 .015 18 1.444 1.479 1.467 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_9 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 113.88 118.78 116.20 .96 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.45 120.52 116.85 1.28 +* CH1E-C-N (Pro) 116.9 1.5 18 114.76 118.21 116.44 .98 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.19 124.31 123.05 .65 +* O-C-N (Pro) 122.0 1.4 18 122.15 123.86 122.94 .40 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.13 125.16 122.24 1.27 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 16 119.28 122.37 121.08 .91 * C-N-CH1E (Pro) 122.6 5.0 18 120.26 123.85 122.77 .81 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.04 121.90 120.69 .56 * CH2G*-C-O (Gly) 120.8 2.1 17 119.28 121.18 120.44 .45 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 108.39 111.32 110.46 .58 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.36 111.89 109.84 1.45 * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.28 115.40 110.66 1.69 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.41 115.73 110.77 1.59 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 18 109.59 113.16 111.72 .96 * N-CH1E-C (Pro) 111.8 2.5 18 108.72 115.04 112.51 1.65 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 108.44 111.37 110.39 .61 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 104.10 114.11 111.06 2.44 **** +* N-CH1E-CH2E (Pro) 103.0 1.1 18 102.51 104.58 103.58 .59 * NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.68 117.43 110.63 1.65 ** **** ------------------------------------------------------------------------------------------------------------- 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_9 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] 146 96.1% Residues in additional allowed regions [a,b,l,p] 6 3.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 96.1 83.8 10.0 1.2 BETTER b. Omega angle st dev 186 2.8 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.3 3.1 1.6 -.5 Inside e. H-bond energy st dev 126 .9 .8 .2 .6 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 19 10.0 18.1 6.5 -1.2 BETTER b. Chi-1 trans st dev 47 10.7 19.0 5.3 -1.6 BETTER c. Chi-1 gauche plus st dev 66 9.2 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 132 10.5 18.2 4.8 -1.6 BETTER e. Chi-2 trans st dev 57 7.2 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 96.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .94 3 Residue-by-residue listing for refined_9 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .21 Chi1-chi2 distribution -.16 Chi1 only .10 Chi3 & chi4 .33 Omega .13 ------ .13 ===== Main-chain covalent forces:- Main-chain bond lengths .30 Main-chain bond angles .40 ------ .36 ===== OVERALL AVERAGE .21 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.