Residue-by-residue listing for refined_2 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 - - - - - - - - - - - 178.5 - - - 2 SER 2 B 49.5 - - - - - - - - - 182.4 - 32.9 - 3 ASP 3 B - - -61.9 - - - - - - - 180.4 - 34.1 - 4 PRO 4 - - - - - -59.5 - - - - - 179.4 - 38.8 - * * 5 GLY 5 h - - - - - - - - - - - 181.4 - - - 6 PRO 6 H - - - - - -56.5 -56.5 -34.5 - - - 178.2 - 38.0 - * * 7 GLU 7 H A 55.5 - - 182.0 - -62.3 -44.6 - - - 181.4 - 32.9 - 8 ALA 8 H A - - - - - -75.3 -36.8 - - - 178.9 - 33.9 - 9 ALA 9 H A - - - - - -64.8 -44.4 - - - 176.6 -2.8 33.5 - 10 ARG 10 H A - 178.5 - 178.1 - -64.5 -33.4 - - - 178.4 -2.7 33.1 - 11 LEU 11 H A - 176.0 - - - -67.4 -40.5 - - - 174.4 -1.4 33.7 - 12 ARG 12 H A - - -62.9 178.9 - -59.4 -43.1 - - - 180.8 -2.3 35.7 - 13 PHE 13 H A - 180.8 - - - -63.8 -36.8 - - - 178.3 -2.3 35.4 - 14 ARG 14 H A - - -68.6 - - -87.4 -17.4 - - - 177.4 -2.1 32.3 - +* +* +* 15 CYS 15 H A - 184.6 - - - -84.2 -12.1 - - - 179.0 -1.6 34.1 - +* ** ** 16 PHE 16 h B - 183.6 - - - - - - - - 176.6 -.7 35.0 - +* +* 17 HIS 17 B 75.2 - - - - - - - - - 173.6 - 33.6 - * * 18 TYR 18 B - 165.4 - - - - - - - - 178.5 -1.1 31.5 - * * * 19 GLU 19 t B 51.8 - - 174.0 - - - - - - 182.2 -.8 32.4 - +* +* Residue-by-residue listing for refined_2 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 - - -56.8 175.7 - - - - - - 179.6 -.5 35.0 - ** ** 21 ALA 21 T A - - - - - - - - - - 182.4 - 34.3 - 22 THR 22 T A - 203.5 - - - - - - - - 180.6 -1.0 34.3 - * * * 23 GLY 23 h - - - - - - - - - - - 181.6 -1.1 - - * * 24 PRO 24 H - - - - - -62.7 -62.7 -36.7 - - - 179.8 - 37.9 - * * 25 GLN 25 H A - - -81.8 - - -65.1 -42.8 - - - 179.5 - 33.3 - * * 26 GLU 26 H A - 177.7 - 171.3 - -69.4 -36.6 - - - 176.8 - 33.0 - 27 ALA 27 H A - - - - - -60.3 -40.1 - - - 179.3 -2.5 34.3 - 28 LEU 28 H A - - -62.7 179.2 - -61.5 -42.2 - - - 179.8 -2.1 34.2 - 29 ALA 29 H A - - - - - -61.2 -38.4 - - - 178.4 -1.4 33.9 - 30 GLN 30 H A - - -69.1 170.0 - -72.1 -45.5 - - - 177.3 -1.6 34.4 - 31 LEU 31 H A - - -73.1 171.1 - -62.2 -44.0 - - - 177.9 -3.0 33.2 - * * 32 ARG 32 H A - 171.4 - 164.5 - -62.4 -41.7 - - - 175.0 -3.5 32.3 - +* +* 33 GLU 33 H A - 178.3 - 186.6 - -57.7 -50.2 - - - 181.6 -1.7 36.0 - 34 LEU 34 H A - - -60.7 175.2 - -64.8 -41.5 - - - 180.6 -2.5 33.8 - 35 CYS 35 H A 68.6 - - - - -71.2 -35.5 - - - 176.9 -3.2 32.7 - +* +* 36 ARG 36 H A - 175.9 - - - -67.8 -31.0 - - - 174.7 -2.6 31.2 - 37 GLN 37 H A - - -65.9 182.1 - -71.3 -21.0 - - - 179.9 -1.8 34.6 - +* +* 38 TRP 38 H a - 162.2 - - - -89.8 -61.0 - - - 181.3 -.8 34.3 - * ** +* +* ** 39 LEU 39 H A - - -63.8 153.8 - -67.9 -50.2 - - - 179.8 -3.7 35.1 - * ** ** 40 ARG 40 h l - - -56.4 184.3 - - - - - - 176.9 -1.0 32.0 - * * 41 PRO 41 T - - - - - -61.8 - - - - - 176.6 - 38.7 - * * 42 GLU 42 T A 56.3 - - 183.9 - - - - - - 180.7 - 34.3 - 43 VAL 43 T a - - -61.6 - - - - - - - 181.6 -1.6 32.2 - 44 ARG 44 t B - - -64.9 188.1 - - - - - - 178.3 -3.6 31.8 - ** ** 45 SER 45 h B - - -55.2 - - - - - - - 185.3 - 34.8 - 46 LYS 46 H A - - -64.9 169.5 - -60.3 -41.8 - - - 185.8 - 34.5 - 47 GLU 47 H A 67.8 - - - - -66.2 -29.4 - - - 176.4 - 30.5 - 48 GLN 48 H A - - -59.8 - - -68.0 -34.0 - - - 179.2 -.6 34.3 - +* +* 49 MET 49 H A - - -60.3 181.3 - -66.7 -38.0 - - - 173.7 -1.0 33.1 - * * * 50 LEU 50 H A - - -76.5 - - -56.2 -53.0 - - - 181.9 -1.6 34.1 - * * 51 GLU 51 H A - - -62.3 - - -54.4 -50.6 - - - 180.5 -1.9 35.2 - 52 LEU 52 H A - - -62.0 176.5 - -59.2 -43.9 - - - 182.6 -2.4 34.9 - 53 LEU 53 H A - 178.2 - - - -77.2 -30.7 - - - 175.1 -2.4 31.1 - 54 VAL 54 H A - 186.0 - - - -61.3 -43.6 - - - 178.5 -2.9 34.5 - * * 55 LEU 55 H A - 182.1 - - - -59.3 -47.8 - - - 185.5 -2.1 36.1 - 56 GLU 56 H A - 197.7 - - - -58.5 -42.9 - - - 179.1 -1.9 34.4 - 57 GLN 57 H A - 199.2 - - - -74.8 -46.6 - - - 184.1 -2.1 35.5 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 PHE 58 H A - 177.8 - - - -53.6 -43.6 - - - 179.6 -3.0 33.2 - * * 59 LEU 59 H A - - -61.6 190.3 - -61.7 -33.3 - - - 178.9 -2.8 31.2 - * * 60 GLY 60 H - - - - - - -81.5 -24.5 - - - 179.1 -.9 - - * * * * 61 ALA 61 H A - - - - - -69.5 -20.4 - - - 175.3 -1.8 33.0 - +* +* 62 LEU 62 h B - - -63.8 171.3 - - - - - - 176.2 -1.0 37.2 - * * 63 PRO 63 h - - - - - -70.0 - - - - - 181.4 - 39.3 - +* +* 64 PRO 64 H - - - - - -41.4 -41.4 -45.6 - - - 181.2 - 38.6 - ** ** * ** 65 GLU 65 H A 60.7 - - 191.9 - -62.2 -46.2 - - - 178.4 - 31.4 - 66 ILE 66 H A - - -59.9 177.9 - -73.2 -43.1 - - - 182.2 -.6 34.8 - +* +* 67 GLN 67 H A - 181.2 - 177.8 - -60.1 -41.3 - - - 180.3 -3.5 34.0 - +* +* 68 ALA 68 H A - - - - - -63.1 -30.7 - - - 180.6 -2.8 33.3 - * * 69 ARG 69 H A - - -58.0 - - -73.2 -37.3 - - - 178.8 -.8 34.8 - +* +* 70 VAL 70 H A - 176.9 - - - -77.7 -31.8 - - - 191.1 -1.5 36.6 - * +* +* 71 GLN 71 H A - 197.8 - - - -51.2 -33.9 - - - 180.2 -2.3 34.5 - * * 72 GLY 72 h - - - - - - - - - - - 182.4 -.5 - - ** ** 73 GLN 73 T A - 186.6 - 173.9 - - - - - - 184.0 -1.6 34.5 - 74 ARG 74 t l - - -60.8 - - - - - - - 184.2 -2.8 32.9 - * * 75 PRO 75 - - - - - -30.3 - - - - - 179.7 - 39.2 - *** +* *** 76 GLY 76 S - - - - - - - - - - - 174.6 - - - 77 SER 77 h B 47.4 - - - - - - - - - 187.6 - 33.7 - * * * 78 PRO 78 H - - - - - -56.2 -56.2 -45.3 - - - 184.5 - 38.3 - * * 79 GLU 79 H A - - -62.8 176.1 - -72.6 -29.0 - - - 172.0 - 29.7 - * * * 80 GLU 80 H A - 173.4 - - - -60.4 -48.0 - - - 178.0 - 35.2 - 81 ALA 81 H A - - - - - -56.6 -43.1 - - - 178.9 -1.9 34.1 - 82 ALA 82 H A - - - - - -53.8 -44.3 - - - 180.5 -2.0 34.7 - 83 ALA 83 H A - - - - - -60.5 -50.1 - - - 179.1 -1.8 32.7 - 84 LEU 84 H A 53.8 - - 162.8 - -68.6 -40.9 - - - 180.0 -1.7 26.4 - ** ** 85 VAL 85 H A - - -61.8 - - -68.5 -32.0 - - - 175.6 -3.0 29.5 - * * * 86 ASP 86 H A - 179.8 - - - -56.7 -33.5 - - - 176.4 -2.6 33.6 - 87 GLY 87 H - - - - - - -84.8 -30.1 - - - 182.1 -.9 - - +* * +* 88 LEU 88 H A - - -64.1 174.6 - -80.9 -20.4 - - - 184.7 -1.6 35.4 - * +* +* 89 ARG 89 h b 63.5 - - 174.1 - - - - - - 182.2 -2.3 33.6 - 90 ARG 90 B 52.9 - - 195.1 - - - - - - 179.8 - 36.8 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 91 GLU 91 S XX - - -62.2 177.7 - - - - - - 183.0 - 30.4 - **** **** 92 PRO 92 S - - - - - -70.6 - - - - - 178.8 - 38.9 - * * 93 GLY 93 - - - - - - - - - - - 179.9 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 178.4 - - - 96 SER 302 B 53.5 - - - - - - - - - 180.6 - 33.3 - 97 ASP 303 B - - -62.5 - - - - - - - 172.5 - 35.9 - * * 98 PRO 304 h - - - - - -68.3 - - - - - 179.8 - 39.0 - * * 99 GLY 305 H - - - - - - 90.6 136.6 - - - 177.8 - - - *13.1**15.6* *15.6* 100 PRO 306 H - - - - - -54.5 -54.5 -25.3 - - - 177.1 - 38.8 - * * * 101 GLU 307 H A 56.5 - - 186.1 - -66.2 -48.7 - - - 179.1 - 33.0 - 102 ALA 308 H A - - - - - -75.2 -29.8 - - - 176.7 -.5 33.3 - ** ** 103 ALA 309 H A - - - - - -60.6 -46.7 - - - 178.7 -2.6 34.0 - 104 ARG 310 H A - 184.0 - 180.7 - -67.3 -33.7 - - - 178.4 -2.3 33.3 - 105 LEU 311 H A - 174.1 - - - -62.2 -45.9 - - - 178.1 -1.5 35.0 - 106 ARG 312 H A - - -59.9 178.3 - -66.6 -35.2 - - - 178.9 -2.7 34.3 - 107 PHE 313 H A - 178.2 - - - -67.2 -34.7 - - - 175.8 -2.1 34.3 - 108 ARG 314 H A - - -78.8 - - -86.0 -27.4 - - - 178.4 -2.2 32.1 - +* * +* 109 CYS 315 H A - 183.2 - - - -74.6 -17.9 - - - 180.8 -2.3 34.7 - +* +* 110 PHE 316 h B - 184.4 - - - - - - - - 177.9 -1.0 35.3 - * * 111 HIS 317 B 70.7 - - - - - - - - - 172.9 - 33.7 - * * 112 TYR 318 B - 166.9 - - - - - - - - 180.6 -.9 32.5 - +* +* 113 GLU 319 t B 50.0 - - 171.2 - - - - - - 182.3 -.8 31.6 - +* +* 114 GLU 320 T A - - -58.2 179.9 - - - - - - 179.6 -.6 33.9 - +* +* 115 ALA 321 T A - - - - - - - - - - 182.2 - 33.8 - 116 THR 322 T A - 193.2 - - - - - - - - 180.8 -1.1 33.0 - * * 117 GLY 323 h - - - - - - - - - - - 184.1 -1.0 - - * * 118 PRO 324 H - - - - - -82.4 -82.4 -29.9 - - - 187.1 - 39.0 - +* * * * +* 119 GLN 325 H A - 195.8 - 166.6 - -77.5 -27.8 - - - 172.5 - 33.0 - * * * * 120 GLU 326 H A - 179.5 - - - -73.0 -41.8 - - - 178.6 - 34.6 - 121 ALA 327 H A - - - - - -55.4 -39.9 - - - 176.5 -1.2 34.0 - * * 122 LEU 328 H A - - -64.4 175.2 - -63.2 -40.5 - - - 179.1 -2.1 35.1 - 123 ALA 329 H A - - - - - -61.3 -48.6 - - - 178.9 -1.3 34.8 - 124 GLN 330 H A - - -49.7 183.6 - -61.9 -48.2 - - - 177.3 -2.6 35.3 - * * 125 LEU 331 H A - - -73.7 171.8 - -59.8 -45.5 - - - 178.9 -3.2 33.1 - +* +* Residue-by-residue listing for refined_2 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 126 ARG 332 H A - 172.7 - 158.3 - -60.5 -44.7 - - - 173.3 -3.3 32.1 - * * +* +* 127 GLU 333 H A - 176.1 - 187.4 - -58.0 -50.7 - - - 181.3 -2.4 37.2 - 128 LEU 334 H A - - -63.8 174.9 - -62.7 -46.8 - - - 180.2 -2.9 33.3 - * * 129 CYS 335 H A 60.1 - - - - -69.9 -29.9 - - - 175.8 -3.5 32.5 - +* +* 130 ARG 336 H A - 180.1 - - - -65.9 -32.3 - - - 177.0 -2.0 32.5 - 131 GLN 337 H A - - -65.7 180.7 - -73.6 -17.7 - - - 179.2 -1.5 33.8 - +* +* 132 TRP 338 H a - 163.9 - - - -93.0 -57.1 - - - 181.9 -.7 34.8 - * ** +* +* ** 133 LEU 339 H A - - -64.5 157.2 - -74.9 -45.5 - - - 176.3 -3.8 34.8 - * ** ** 134 ARG 340 h l - - -65.7 180.7 - - - - - - 176.5 -1.2 31.0 - * * 135 PRO 341 T - - - - - -71.4 - - - - - 180.7 - 39.2 - +* +* 136 GLU 342 T A 53.4 - - 186.0 - - - - - - 181.9 - 34.7 - 137 VAL 343 T A - - -60.5 - - - - - - - 183.0 - 31.8 - 138 ARG 344 t B - - -69.7 180.2 - - - - - - 181.4 -2.6 32.2 - 139 SER 345 h B - - -50.0 - - - - - - - 179.3 - 36.6 - * * 140 LYS 346 H A - - -63.0 170.7 - -53.4 -42.0 - - - 184.2 - 36.5 - * * 141 GLU 347 H A 58.3 - - 177.8 - -60.5 -29.8 - - - 177.7 - 31.9 - 142 GLN 348 H A - - -65.4 - - -69.5 -36.2 - - - 181.1 -1.1 34.8 - * * 143 MET 349 H A - - -59.4 179.6 - -66.8 -37.9 - - - 175.7 -1.0 33.5 - * * 144 LEU 350 H A - - -76.3 - - -56.7 -53.4 - - - 182.2 -1.6 34.0 - * * 145 GLU 351 H A - - -63.9 - - -58.7 -51.0 - - - 180.6 -1.6 33.6 - * * 146 LEU 352 H A - - -61.4 178.1 - -57.5 -43.5 - - - 182.5 -2.6 34.8 - 147 LEU 353 H A - 182.2 - - - -73.2 -30.0 - - - 174.9 -2.5 31.6 - 148 VAL 354 H A - 185.4 - - - -60.7 -45.3 - - - 179.6 -2.2 34.7 - 149 LEU 355 H A - 182.2 - - - -59.1 -45.5 - - - 183.4 -2.0 35.3 - 150 GLU 356 H A - 196.1 - - - -58.0 -42.6 - - - 178.4 -1.9 33.0 - 151 GLN 357 H A - 200.3 - - - -74.6 -44.4 - - - 183.6 -1.9 35.7 - 152 PHE 358 H A - 176.2 - - - -52.9 -43.9 - - - 179.0 -3.0 33.9 - * * * 153 LEU 359 H A - - -62.1 187.2 - -63.9 -37.6 - - - 179.1 -2.8 30.7 - * * 154 GLY 360 H - - - - - - -81.4 -16.4 - - - 177.1 -.9 - - * ** * ** 155 ALA 361 H A - - - - - -77.2 -26.2 - - - 174.5 -1.7 33.4 - * * * 156 LEU 362 h B - - -67.5 172.5 - - - - - - 177.5 -1.3 36.5 - * * 157 PRO 363 h - - - - - -65.9 - - - - - 182.0 - 39.6 - +* +* 158 PRO 364 H - - - - - -42.9 -42.9 -42.3 - - - 181.0 - 38.6 - ** +* * ** 159 GLU 365 H A 56.3 - - 183.9 - -64.3 -47.9 - - - 179.0 - 32.0 - 160 ILE 366 H A - - -59.3 178.4 - -73.5 -42.0 - - - 182.5 -.6 35.5 - +* +* Residue-by-residue listing for refined_2 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 - 179.0 - 180.5 - -58.7 -50.1 - - - 183.2 -3.5 33.8 - ** ** 162 ALA 368 H A - - - - - -58.0 -30.7 - - - 179.3 -2.8 33.1 - * * 163 ARG 369 H A - - -57.0 - - -67.0 -45.0 - - - 180.5 -.8 34.7 - +* +* 164 VAL 370 H A - 178.9 - - - -76.2 -33.4 - - - 185.8 -1.5 36.7 - 165 GLN 371 H A - 199.0 - - - -54.1 -29.5 - - - 177.2 -3.1 35.3 - * * 166 GLY 372 h - - - - - - - - - - - 181.6 -.7 - - +* +* 167 GLN 373 T A - - -65.5 - - - - - - - 189.3 -1.2 33.9 - +* * +* 168 ARG 374 t l - - -72.5 - - - - - - - 178.4 -2.8 31.3 - * * 169 PRO 375 - - - - - -53.7 - - - - - 177.7 - 39.3 - * +* +* 170 GLY 376 - - - - - - - - - - - 175.9 - - - 171 SER 377 h B 45.0 - - - - - - - - - 186.3 - 32.9 - * * * 172 PRO 378 H - - - - - -54.8 -54.8 -45.8 - - - 184.8 - 39.3 - +* +* 173 GLU 379 H A - - -59.3 173.9 - -75.1 -30.3 - - - 174.9 - 31.8 - 174 GLU 380 H A - 183.3 - - - -60.1 -49.9 - - - 177.2 - 35.7 - 175 ALA 381 H A - - - - - -61.4 -43.8 - - - 179.9 -2.2 34.0 - 176 ALA 382 H A - - - - - -55.0 -31.8 - - - 180.0 -2.6 34.0 - 177 ALA 383 H A - - - - - -73.2 -50.1 - - - 178.8 -1.5 32.4 - 178 LEU 384 H A 53.7 - - 157.9 - -68.5 -39.3 - - - 179.9 -1.6 27.9 - * +* +* 179 VAL 385 H A - - -58.1 - - -65.2 -31.0 - - - 174.5 -2.9 29.6 - * * * 180 ASP 386 H A - 174.6 - - - -54.7 -36.5 - - - 178.0 -1.2 33.9 - * * 181 GLY 387 H - - - - - - -84.6 -28.0 - - - 181.5 -.9 - - +* * +* +* 182 LEU 388 H A - - -60.5 176.7 - -80.2 -28.6 - - - 184.4 -1.6 35.3 - * * 183 ARG 389 h B 61.8 - - 175.9 - - - - - - 176.8 -2.8 33.0 - * * 184 ARG 390 S B 54.3 - - 183.4 - - - - - - 185.4 - 34.5 - 185 GLU 391 S l - - -61.6 186.6 - - - - - - 180.6 - 31.5 - 186 PRO 392 - - - - - -77.7 - - - - - 176.2 - 37.3 - * * 187 GLY 393 - - - - - - - - - - - 181.5 -1.5 - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * * ****13.1**15.6* +* ** ** *15.6* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.4 181.8 -63.4 177.1 -60.0 -64.5 -37.2 - - - 179.6 -1.9 34.2 Standard deviations: 7.5 9.6 6.0 8.3 13.1 17.0 18.3 - - - 3.2 .9 2.3 Numbers of values: 24 48 60 64 18 123 123 0 0 0 186 125 170 0 Residue-by-residue listing for refined_2 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_2 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 - 1.233 1.498 - 1.463 - 116.72 120.14 - 111.24 - 123.14 * * 2 SER 2 1.307 1.239 1.521 1.537 1.433 121.99 115.98 120.79 112.55 110.51 110.32 123.22 +* * * +* 3 ASP 3 1.313 1.233 1.511 1.538 1.451 122.07 117.79 119.97 110.06 110.20 111.04 122.25 * * 4 PRO 4 1.350 1.239 1.532 1.540 1.475 123.18 115.94 120.94 110.05 112.39 103.51 123.12 5 GLY 5 1.311 1.242 1.500 - 1.423 120.95 118.16 119.71 - 110.71 - 122.13 * +* +* 6 PRO 6 1.344 1.226 1.526 1.539 1.463 122.85 116.03 120.93 110.66 111.91 104.31 123.04 * * 7 GLU 7 1.323 1.229 1.535 1.537 1.450 122.28 116.46 120.49 111.93 111.52 110.30 122.97 8 ALA 8 1.324 1.228 1.514 1.512 1.450 121.99 116.14 120.82 110.66 110.68 110.35 123.03 9 ALA 9 1.319 1.235 1.522 1.502 1.449 121.84 116.21 120.71 110.93 110.56 110.57 123.06 10 ARG 10 1.333 1.224 1.530 1.528 1.450 121.41 116.64 120.94 110.54 110.39 111.76 122.41 11 LEU 11 1.328 1.218 1.538 1.520 1.409 122.06 116.93 120.26 112.30 110.14 109.39 122.79 +** * +** 12 ARG 12 1.339 1.236 1.531 1.535 1.478 121.91 113.97 121.81 107.85 109.12 110.93 124.21 * * * * 13 PHE 13 1.314 1.222 1.544 1.536 1.455 125.68 116.66 120.72 112.70 111.27 106.04 122.61 * ** * +** +** 14 ARG 14 1.322 1.233 1.525 1.533 1.465 122.16 116.81 120.71 111.18 112.56 111.41 122.48 Residue-by-residue listing for refined_2 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 15 CYS 15 1.313 1.240 1.527 1.542 1.452 121.53 115.53 121.38 111.05 108.89 110.45 123.08 * * 16 PHE 16 1.324 1.243 1.513 1.538 1.436 122.01 116.74 120.45 109.53 109.36 110.70 122.80 * * 17 HIS 17 1.307 1.234 1.503 1.590 1.437 119.81 118.72 119.51 110.70 106.81 113.00 121.71 +* * *** * * * +* * *** 18 TYR 18 1.291 1.230 1.486 1.534 1.416 117.22 114.89 121.35 111.53 108.47 114.25 123.74 +** +* ** ** ** +** 19 GLU 19 1.275 1.242 1.503 1.535 1.397 121.71 115.16 121.12 112.87 109.46 111.28 123.72 +*** * *** * +*** 20 GLU 20 1.302 1.232 1.529 1.530 1.443 123.72 115.02 121.11 111.25 109.68 108.67 123.82 +* * * +* 21 ALA 21 1.320 1.226 1.538 1.516 1.444 123.65 118.25 120.11 109.95 112.73 109.83 121.63 * * * 22 THR 22 1.334 1.218 1.544 1.591 1.461 119.05 115.74 121.34 111.00 108.49 110.83 122.77 +* * +* 23 GLY 23 1.333 1.232 1.518 - 1.444 121.07 119.01 119.82 - 111.39 - 121.17 * * * 24 PRO 24 1.346 1.218 1.525 1.510 1.463 122.14 117.63 119.82 110.64 113.68 103.66 122.53 25 GLN 25 1.337 1.233 1.522 1.547 1.463 120.61 115.35 121.37 108.78 109.44 113.68 123.26 +* +* 26 GLU 26 1.320 1.242 1.530 1.526 1.453 121.81 115.93 121.14 111.62 110.94 110.65 122.93 27 ALA 27 1.318 1.222 1.519 1.520 1.452 122.23 115.73 120.78 110.35 110.11 110.28 123.48 28 LEU 28 1.320 1.215 1.505 1.509 1.459 122.89 117.04 120.01 108.85 112.54 111.05 122.95 * * 29 ALA 29 1.324 1.234 1.525 1.521 1.464 121.39 115.16 121.38 110.73 109.99 110.41 123.43 30 GLN 30 1.310 1.227 1.519 1.492 1.432 123.16 116.10 120.62 111.57 111.29 108.37 123.28 * +* * * +* 31 LEU 31 1.321 1.212 1.508 1.526 1.458 122.75 116.83 120.22 110.86 111.86 110.87 122.95 32 ARG 32 1.312 1.217 1.508 1.500 1.434 121.73 116.02 120.67 112.11 111.93 110.62 123.31 * * * * * 33 GLU 33 1.294 1.222 1.533 1.527 1.452 121.88 115.93 120.68 109.38 109.21 108.96 123.34 ** ** 34 LEU 34 1.317 1.232 1.531 1.528 1.455 122.64 117.05 120.42 110.66 112.11 110.12 122.53 35 CYS 35 1.327 1.219 1.521 1.544 1.451 120.57 116.71 120.79 111.06 109.84 112.29 122.50 * * 36 ARG 36 1.327 1.212 1.532 1.549 1.423 122.44 117.17 119.93 115.01 111.36 109.95 122.88 +* +** +** 37 GLN 37 1.330 1.237 1.531 1.515 1.469 122.04 114.68 121.75 109.64 110.81 110.10 123.57 38 TRP 38 1.309 1.231 1.538 1.544 1.447 124.51 116.09 120.67 112.71 111.87 107.62 123.24 * +* * +* +* 39 LEU 39 1.306 1.230 1.518 1.532 1.452 123.43 115.32 120.54 111.62 109.99 108.05 124.09 +* * +* 40 ARG 40 1.332 1.227 1.526 1.540 1.460 124.36 118.16 120.19 109.94 112.99 112.93 121.64 * * * 41 PRO 41 1.348 1.233 1.528 1.540 1.478 122.81 114.56 121.61 110.38 110.91 103.58 123.83 +* * +* 42 GLU 42 1.320 1.231 1.534 1.536 1.440 123.88 117.34 120.33 110.81 111.19 109.68 122.32 * * 43 VAL 43 1.334 1.229 1.522 1.563 1.457 120.52 117.38 120.10 109.95 112.60 113.15 122.48 44 ARG 44 1.321 1.231 1.498 1.531 1.452 120.19 114.47 121.39 109.86 112.62 113.51 124.14 * +* +* 45 SER 45 1.298 1.249 1.541 1.523 1.422 123.84 115.59 120.96 112.01 109.83 108.17 123.45 ** +* * * * ** Residue-by-residue listing for refined_2 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 46 LYS 46 1.313 1.218 1.524 1.517 1.457 124.07 117.54 120.11 110.22 113.82 108.86 122.29 * * * 47 GLU 47 1.320 1.242 1.522 1.556 1.479 120.86 115.91 120.93 111.58 111.31 114.10 123.16 * * ** ** 48 GLN 48 1.325 1.232 1.518 1.528 1.451 121.85 115.94 120.87 109.62 110.19 111.13 123.19 49 MET 49 1.326 1.231 1.505 1.510 1.451 122.04 115.89 120.38 111.50 110.71 110.67 123.73 * * 50 LEU 50 1.339 1.202 1.513 1.564 1.462 121.86 116.32 120.03 109.27 109.19 112.37 123.47 * +* * +* 51 GLU 51 1.337 1.239 1.532 1.533 1.474 122.82 115.95 120.67 109.10 111.15 109.93 123.37 52 LEU 52 1.326 1.235 1.533 1.535 1.449 122.54 116.10 121.06 109.95 111.32 109.62 122.83 53 LEU 53 1.314 1.243 1.550 1.524 1.431 121.87 118.09 119.81 115.15 113.34 108.64 122.09 * * * +** * +** 54 VAL 54 1.339 1.230 1.525 1.565 1.473 120.18 114.55 121.44 107.58 107.67 113.72 123.98 * * * 55 LEU 55 1.329 1.240 1.512 1.560 1.454 123.99 114.79 121.02 110.09 109.90 108.46 124.19 +* * * +* 56 GLU 56 1.314 1.250 1.536 1.534 1.436 123.03 116.34 120.90 110.53 111.06 109.86 122.76 * * * 57 GLN 57 1.327 1.221 1.525 1.533 1.453 121.05 116.24 120.32 109.41 108.48 110.05 123.38 58 PHE 58 1.340 1.235 1.509 1.536 1.467 122.39 116.70 120.22 109.87 112.22 111.80 123.08 59 LEU 59 1.319 1.216 1.511 1.525 1.446 120.29 116.83 120.26 111.90 112.30 112.42 122.87 * * 60 GLY 60 1.316 1.217 1.507 - 1.438 120.06 116.62 120.38 - 111.95 - 122.99 61 ALA 61 1.329 1.235 1.533 1.535 1.464 122.27 115.61 121.00 111.42 110.60 111.02 123.39 62 LEU 62 1.323 1.240 1.540 1.526 1.448 123.37 118.65 119.88 107.98 109.66 108.52 121.46 * * * * 63 PRO 63 1.352 1.235 1.521 1.543 1.460 121.85 118.52 118.83 109.30 108.93 104.29 122.65 * * * * * 64 PRO 64 1.353 1.219 1.535 1.523 1.476 123.74 117.08 120.21 110.50 113.82 102.81 122.68 65 GLU 65 1.330 1.227 1.548 1.538 1.463 121.42 117.36 120.40 112.75 112.75 110.89 122.22 * * * 66 ILE 66 1.330 1.236 1.531 1.549 1.454 121.42 115.50 121.18 109.75 109.92 110.45 123.28 67 GLN 67 1.323 1.220 1.521 1.525 1.450 122.93 116.39 120.35 110.35 111.54 110.40 123.25 68 ALA 68 1.320 1.227 1.530 1.518 1.465 122.85 116.91 120.53 110.32 112.35 110.78 122.55 69 ARG 69 1.317 1.215 1.530 1.531 1.469 121.79 114.97 121.58 109.94 110.00 110.04 123.45 70 VAL 70 1.307 1.241 1.525 1.546 1.465 124.21 113.84 121.86 107.58 111.14 109.62 124.28 +* * * * +* 71 GLN 71 1.300 1.227 1.530 1.514 1.446 125.80 117.81 119.68 110.40 114.71 108.50 122.51 ** ** * * ** 72 GLY 72 1.304 1.235 1.513 - 1.441 119.89 116.00 120.83 - 112.46 - 123.16 +* +* 73 GLN 73 1.315 1.232 1.515 1.510 1.425 122.31 115.96 120.40 110.46 111.45 109.53 123.63 +* +* 74 ARG 74 1.348 1.217 1.547 1.559 1.483 123.09 117.52 119.67 110.07 110.57 112.54 122.79 * * * * * * 75 PRO 75 1.373 1.221 1.540 1.515 1.494 125.30 116.17 121.03 110.11 115.70 101.70 122.80 ** +* +* * ** 76 GLY 76 1.312 1.221 1.506 - 1.467 121.26 114.99 121.46 - 111.41 - 123.55 * * * 77 SER 77 1.291 1.244 1.538 1.528 1.412 123.83 117.62 120.31 113.84 107.54 108.74 122.00 +** ** * +* * * +** 78 PRO 78 1.347 1.232 1.523 1.543 1.472 123.08 116.46 120.64 110.13 114.00 103.88 122.86 79 GLU 79 1.304 1.232 1.520 1.519 1.446 122.10 116.16 120.74 115.78 112.36 110.27 123.09 +* +** +** Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 80 GLU 80 1.327 1.227 1.519 1.528 1.457 121.76 115.70 120.81 110.17 108.31 109.75 123.46 * * 81 ALA 81 1.345 1.231 1.508 1.506 1.456 122.48 115.92 120.00 109.76 110.95 110.73 124.06 * * 82 ALA 82 1.337 1.216 1.509 1.518 1.459 122.78 115.56 120.75 109.51 110.54 110.47 123.67 83 ALA 83 1.309 1.235 1.531 1.513 1.445 122.66 118.42 119.62 111.18 112.10 110.96 121.96 * * * 84 LEU 84 1.341 1.237 1.510 1.565 1.459 118.19 117.18 120.02 112.04 113.07 118.00 122.75 +* +* * **** **** 85 VAL 85 1.328 1.206 1.512 1.540 1.456 120.51 117.30 119.99 111.17 112.62 115.24 122.72 * ** ** 86 ASP 86 1.328 1.229 1.530 1.534 1.474 122.05 115.80 121.05 110.47 110.57 110.99 123.14 87 GLY 87 1.323 1.223 1.530 - 1.448 121.14 116.55 120.66 - 112.43 - 122.79 88 LEU 88 1.328 1.237 1.519 1.530 1.477 122.82 116.41 120.43 107.85 112.52 110.42 123.15 * * 89 ARG 89 1.309 1.246 1.512 1.536 1.432 122.04 113.35 122.41 109.59 112.63 111.51 124.23 * * * * 90 ARG 90 1.272 1.235 1.515 1.528 1.426 125.64 116.61 119.40 111.22 107.13 106.76 123.98 **** +* ** * ** **** 91 GLU 91 1.325 1.238 1.546 1.541 1.466 123.61 116.64 121.73 113.09 112.69 111.89 121.62 * * +* +* 92 PRO 92 1.337 1.240 1.526 1.527 1.462 122.80 115.82 121.26 110.19 112.64 103.22 122.92 93 GLY 93 1.305 1.213 1.491 - 1.422 120.75 116.54 120.47 - 111.22 - 122.97 +* * +* +* 94 GLY 94 1.298 1.246 1.499 - 1.447 121.14 - 118.92 - 110.97 - - ** ** 95 GLY 301 - 1.237 1.503 - 1.451 - 115.34 121.32 - 111.28 - 123.34 96 SER 302 1.301 1.242 1.520 1.536 1.423 122.26 116.41 120.64 112.19 109.85 110.36 122.94 +* +* * +* 97 ASP 303 1.299 1.233 1.505 1.546 1.444 122.21 118.34 120.00 108.40 108.95 110.66 121.65 ** * ** 98 PRO 304 1.348 1.229 1.530 1.542 1.463 121.70 115.17 121.78 109.99 109.47 103.92 123.04 * * 99 GLY 305 1.320 1.233 1.507 - 1.424 121.58 118.41 119.73 - 111.34 - 121.86 +* +* 100 PRO 306 1.349 1.230 1.536 1.528 1.480 123.14 115.91 121.10 110.31 112.09 103.12 122.99 101 GLU 307 1.322 1.232 1.538 1.539 1.448 122.55 116.38 120.83 112.33 110.83 110.03 122.74 * * 102 ALA 308 1.329 1.225 1.512 1.519 1.446 121.63 116.09 120.74 110.96 109.96 111.16 123.16 103 ALA 309 1.328 1.232 1.517 1.518 1.452 122.08 116.15 120.81 110.34 109.90 110.86 123.00 104 ARG 310 1.332 1.226 1.525 1.521 1.446 121.12 116.42 120.69 109.88 110.46 112.07 122.89 105 LEU 311 1.325 1.216 1.531 1.521 1.413 122.64 116.41 120.73 111.24 109.79 108.65 122.83 ** * ** 106 ARG 312 1.325 1.224 1.530 1.530 1.463 122.10 115.22 121.14 110.27 110.13 110.29 123.63 107 PHE 313 1.318 1.225 1.548 1.537 1.459 124.05 116.75 120.69 112.57 111.14 107.81 122.55 * * * +* +* 108 ARG 314 1.326 1.227 1.518 1.531 1.469 122.12 116.74 120.62 110.55 112.52 112.31 122.64 * * 109 CYS 315 1.310 1.241 1.533 1.542 1.458 121.91 115.16 121.43 110.76 109.60 109.58 123.41 * * 110 PHE 316 1.326 1.237 1.521 1.532 1.444 123.37 116.41 120.76 109.29 110.82 109.89 122.83 111 HIS 317 1.304 1.231 1.506 1.571 1.442 120.21 118.00 119.95 110.24 108.75 112.41 122.02 +* ** * ** 112 TYR 318 1.296 1.232 1.504 1.540 1.423 118.08 115.19 121.30 112.33 108.16 112.10 123.51 ** +* ** * * ** Residue-by-residue listing for refined_2 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 113 GLU 319 1.293 1.239 1.502 1.541 1.414 121.69 114.82 121.52 112.81 110.67 112.02 123.66 +** * ** * +** 114 GLU 320 1.305 1.217 1.531 1.533 1.443 123.01 116.24 120.83 111.49 111.09 109.59 122.91 +* +* 115 ALA 321 1.318 1.236 1.538 1.519 1.448 122.59 117.84 120.03 110.24 112.78 110.24 122.13 116 THR 322 1.334 1.235 1.538 1.575 1.454 119.84 116.38 120.72 110.60 110.93 112.12 122.90 * * * 117 GLY 323 1.322 1.234 1.507 - 1.451 120.67 119.71 119.54 - 110.73 - 120.74 +* * +* 118 PRO 324 1.340 1.222 1.514 1.514 1.439 121.01 116.14 121.06 110.55 112.27 102.85 122.79 +* +* 119 GLN 325 1.305 1.235 1.518 1.484 1.400 121.98 117.05 120.47 113.92 111.52 108.04 122.48 +* ** *** ** * *** 120 GLU 326 1.330 1.214 1.508 1.518 1.439 119.66 115.49 120.97 108.82 107.38 112.29 123.51 * * * * 121 ALA 327 1.333 1.218 1.521 1.523 1.454 122.50 115.96 120.75 110.83 110.11 110.29 123.27 122 LEU 328 1.324 1.212 1.501 1.503 1.457 122.78 116.55 120.17 108.29 111.57 110.67 123.27 * * * 123 ALA 329 1.318 1.235 1.513 1.518 1.452 121.90 114.86 121.08 110.17 109.28 109.96 124.01 124 GLN 330 1.323 1.221 1.536 1.509 1.451 123.05 116.13 121.00 110.82 110.06 108.19 122.86 * * * 125 LEU 331 1.334 1.213 1.513 1.532 1.466 122.88 117.22 120.04 110.20 112.39 111.40 122.74 126 ARG 332 1.317 1.210 1.515 1.515 1.441 122.45 115.76 120.78 113.41 111.60 109.86 123.43 * +* +* 127 GLU 333 1.286 1.236 1.555 1.521 1.462 123.14 116.42 120.45 109.38 110.25 106.70 123.11 *** * ** *** 128 LEU 334 1.332 1.231 1.527 1.536 1.468 122.76 116.85 120.62 110.63 112.28 110.74 122.53 129 CYS 335 1.319 1.211 1.519 1.532 1.450 121.06 117.15 120.44 111.41 110.65 111.74 122.41 130 ARG 336 1.328 1.212 1.523 1.538 1.422 121.96 116.89 120.18 113.98 110.72 109.40 122.91 +* ** ** 131 GLN 337 1.316 1.235 1.532 1.508 1.458 122.11 114.64 121.44 111.26 111.05 109.60 123.91 * * 132 TRP 338 1.314 1.235 1.549 1.549 1.452 125.26 115.94 121.11 112.23 111.89 107.32 122.95 * * +* * +* +* 133 LEU 339 1.306 1.227 1.509 1.522 1.451 123.52 115.68 120.46 111.72 110.25 108.31 123.85 +* * * +* 134 ARG 340 1.334 1.219 1.515 1.530 1.447 123.41 117.71 120.68 111.12 114.62 112.49 121.61 * * * 135 PRO 341 1.342 1.231 1.525 1.536 1.474 122.32 113.85 122.03 110.19 109.76 103.21 124.11 ** +* ** 136 GLU 342 1.314 1.224 1.536 1.542 1.432 124.43 117.53 120.41 111.55 112.05 108.20 122.04 * * +* * +* 137 VAL 343 1.325 1.231 1.524 1.556 1.464 120.38 116.98 120.61 110.24 113.36 112.95 122.41 138 ARG 344 1.309 1.225 1.498 1.523 1.452 121.08 114.85 121.00 110.82 112.57 112.07 124.15 * * * 139 SER 345 1.306 1.245 1.524 1.521 1.437 123.68 115.59 120.57 109.94 110.11 107.45 123.84 +* * * +* +* 140 LYS 346 1.331 1.213 1.515 1.528 1.468 124.07 115.83 120.98 108.21 110.73 109.09 123.15 * * 141 GLU 347 1.321 1.234 1.532 1.528 1.465 122.58 116.45 120.42 111.45 112.85 111.53 123.11 142 GLN 348 1.329 1.228 1.516 1.535 1.456 121.73 115.13 121.40 109.66 109.34 110.61 123.46 143 MET 349 1.321 1.228 1.505 1.508 1.446 122.64 116.43 120.04 111.21 111.09 110.24 123.52 * * 144 LEU 350 1.348 1.216 1.512 1.565 1.467 121.26 116.14 119.98 108.78 109.64 112.89 123.75 * +* * +* Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 145 GLU 351 1.336 1.234 1.528 1.536 1.467 122.54 116.60 120.41 110.05 111.67 111.07 122.97 146 LEU 352 1.329 1.236 1.527 1.531 1.454 122.09 115.95 121.01 109.62 111.13 110.07 123.02 147 LEU 353 1.313 1.241 1.549 1.518 1.420 121.99 117.82 119.98 115.18 112.87 108.23 122.19 * * +* +** * +** 148 VAL 354 1.344 1.231 1.527 1.565 1.476 120.33 114.80 121.26 107.35 108.02 113.60 123.92 * * * * 149 LEU 355 1.329 1.237 1.514 1.559 1.457 123.76 115.26 120.88 110.78 110.12 108.87 123.85 * * * 150 GLU 356 1.311 1.239 1.541 1.535 1.444 122.47 117.16 120.52 111.66 111.54 110.42 122.31 * * 151 GLN 357 1.329 1.213 1.520 1.527 1.465 120.66 115.77 120.64 108.54 107.97 110.52 123.55 * * 152 PHE 358 1.338 1.235 1.518 1.541 1.465 123.28 116.68 120.29 110.41 111.85 110.36 123.01 153 LEU 359 1.319 1.213 1.510 1.529 1.447 120.38 117.27 120.01 112.43 112.53 112.47 122.66 * * * 154 GLY 360 1.318 1.230 1.510 - 1.449 119.81 116.11 120.66 - 112.00 - 123.22 155 ALA 361 1.323 1.231 1.519 1.531 1.447 122.26 115.81 120.72 111.15 109.70 111.10 123.46 156 LEU 362 1.331 1.239 1.530 1.531 1.445 122.90 118.62 119.71 108.30 109.52 109.30 121.67 * * 157 PRO 363 1.346 1.234 1.512 1.540 1.455 122.15 118.57 118.74 109.15 108.37 104.21 122.70 * * * * * 158 PRO 364 1.348 1.224 1.537 1.526 1.478 123.35 116.34 120.63 110.62 113.16 102.84 122.98 159 GLU 365 1.324 1.224 1.545 1.532 1.458 122.01 117.57 120.10 112.23 113.27 110.47 122.31 * * 160 ILE 366 1.326 1.239 1.514 1.543 1.456 121.39 114.90 121.37 108.72 109.66 110.62 123.71 161 GLN 367 1.318 1.213 1.509 1.515 1.433 122.62 116.96 119.67 109.92 111.64 111.12 123.34 * * 162 ALA 368 1.334 1.236 1.529 1.517 1.470 122.26 116.32 120.71 110.55 112.23 110.93 122.95 163 ARG 369 1.319 1.226 1.531 1.534 1.453 121.93 115.62 121.03 110.04 109.61 110.30 123.32 164 VAL 370 1.325 1.236 1.515 1.545 1.478 123.84 113.81 121.65 106.98 110.78 110.15 124.54 * * * * 165 GLN 371 1.295 1.228 1.531 1.525 1.449 126.48 116.31 120.65 112.07 111.91 106.65 123.04 ** +** * ** +** 166 GLY 372 1.318 1.226 1.523 - 1.439 120.69 116.93 120.62 - 112.39 - 122.46 167 GLN 373 1.323 1.224 1.509 1.562 1.461 121.43 115.72 120.58 107.88 111.31 113.43 123.68 +* * +* +* 168 ARG 374 1.332 1.223 1.542 1.551 1.459 122.62 117.56 120.44 110.60 110.91 114.08 121.88 * ** ** 169 PRO 375 1.364 1.223 1.527 1.541 1.486 123.26 115.26 121.39 109.80 112.12 103.05 123.35 * * * * 170 GLY 376 1.315 1.224 1.501 - 1.457 121.69 115.76 120.97 - 112.32 - 123.27 171 SER 377 1.290 1.247 1.542 1.520 1.418 122.67 117.15 120.50 113.99 109.68 108.96 122.28 +** ** ** +** 172 PRO 378 1.354 1.235 1.523 1.531 1.479 123.45 116.71 120.59 108.94 114.54 103.47 122.67 * * 173 GLU 379 1.309 1.232 1.512 1.522 1.450 121.43 116.00 120.54 113.57 110.96 110.32 123.44 * +* +* 174 GLU 380 1.325 1.235 1.533 1.528 1.452 122.27 115.77 121.00 109.97 108.11 109.13 123.21 * * 175 ALA 381 1.347 1.229 1.513 1.509 1.453 122.21 116.06 120.13 110.08 110.94 110.68 123.79 * * 176 ALA 382 1.340 1.227 1.528 1.532 1.470 123.31 115.34 121.30 110.48 111.23 110.22 123.35 177 ALA 383 1.295 1.232 1.532 1.510 1.438 122.78 118.66 119.52 111.81 112.11 110.79 121.81 ** * * ** Residue-by-residue listing for refined_2 Page 14 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 178 LEU 384 1.350 1.232 1.508 1.562 1.470 118.31 116.67 120.60 110.90 112.25 117.72 122.68 * +* +* **** **** 179 VAL 385 1.327 1.207 1.517 1.541 1.449 120.70 116.64 120.38 111.81 111.58 114.89 122.98 * * +* +* 180 ASP 386 1.329 1.232 1.533 1.536 1.475 122.40 116.21 120.82 110.03 110.98 110.93 122.97 181 GLY 387 1.320 1.227 1.526 - 1.451 120.90 116.10 120.79 - 112.45 - 123.11 182 LEU 388 1.324 1.233 1.525 1.531 1.466 122.77 116.37 120.44 108.27 112.09 110.29 123.19 183 ARG 389 1.320 1.245 1.501 1.550 1.434 122.37 113.13 122.39 109.65 112.73 112.44 124.48 * * +* * +* 184 ARG 390 1.264 1.237 1.523 1.540 1.432 124.52 116.30 120.11 111.77 107.25 109.71 123.58 *4.6* * +* * *4.6* 185 GLU 391 1.320 1.245 1.533 1.547 1.468 123.45 117.37 121.33 110.65 110.15 114.03 121.26 ** * ** 186 PRO 392 1.333 1.232 1.520 1.528 1.428 121.65 115.40 121.25 111.55 111.96 104.48 123.18 +** * +** 187 GLY 393 1.315 1.250 1.504 - 1.427 120.93 115.93 120.25 - 110.93 - 123.81 * +* +* 188 GLY 394 1.308 - 1.510 - 1.434 121.80 - - - 110.67 - - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * +* *** *** +** ** * +** +* **** +* *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 1.264 1.350 1.320 .014 *4.6* * C-N (Pro) 1.341 .016 18 1.333 1.373 1.349 .009 ** C-O C-O 1.231 .020 187 1.202 1.250 1.229 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.486 1.555 1.524 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.491 1.530 1.508 .010 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.502 1.535 1.518 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.540 1.591 1.557 .015 +* CH1E-CH2E (the rest) 1.530 .020 138 1.484 1.590 1.532 .015 ** *** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.397 1.483 1.450 .016 *** * NH1-CH2G* (Gly) 1.451 .016 18 1.422 1.467 1.443 .013 +* * N-CH1E (Pro) 1.466 .015 18 1.428 1.494 1.468 .016 +** +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 2.0 152 113.13 118.72 116.29 1.06 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 16 114.99 119.71 116.80 1.29 +* CH1E-C-N (Pro) 116.9 1.5 18 113.85 118.57 116.20 1.18 ** * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.74 124.54 123.01 .70 * O-C-N (Pro) 122.0 1.4 18 122.53 124.11 123.01 .40 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.22 126.48 122.25 1.42 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.81 121.80 120.90 .57 C-N-CH1E (Pro) 122.6 5.0 18 121.01 125.30 122.77 .95 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.74 122.41 120.67 .60 * CH2G*-C-O (Gly) 120.8 2.1 17 118.92 121.46 120.37 .65 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.51 111.81 110.57 .56 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.98 111.81 109.40 1.61 * CH2E-CH1E-C (the rest) 110.1 1.9 138 107.85 115.78 110.81 1.56 * +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.81 114.71 110.83 1.52 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.67 112.46 111.55 .64 N-CH1E-C (Pro) 111.8 2.5 18 108.37 115.70 112.10 1.93 * +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.83 111.16 110.58 .37 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 109.62 115.24 112.28 1.83 * ** N-CH1E-CH2E (Pro) 103.0 1.1 18 101.70 104.48 103.45 .67 * * NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.04 118.00 110.50 1.96 +** **** ------------------------------------------------------------------------------------------------------------- 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_2 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] 142 93.4% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 1 .7% ---- ------ 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 93.4 83.8 10.0 1.0 Inside b. Omega angle st dev 186 3.2 6.0 3.0 -.9 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 125 .9 .8 .2 .2 Inside f. Overall G-factor 188 .2 -.4 .3 1.9 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 24 7.5 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 48 9.6 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 60 6.0 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 132 8.6 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 64 8.3 20.4 5.0 -2.4 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 93.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 6.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .86 2 Residue-by-residue listing for refined_2 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 .01 Chi3 & chi4 .35 Omega .08 ------ .10 ===== Main-chain covalent forces:- Main-chain bond lengths .23 Main-chain bond angles .37 ------ .31 ===== OVERALL AVERAGE .18 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.