Residue-by-residue listing for refined_1 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 181.1 - - - 2 SER 2 b - 184.9 - - - - - - - - 178.4 - 35.1 - 3 ASP 3 B - - -55.9 - - - - - - - 180.4 - 35.0 - 4 PRO 4 - - - - - -63.1 - - - - - 182.8 - 38.7 - * * 5 GLY 5 h - - - - - - - - - - - 185.9 - - - * * 6 PRO 6 H - - - - - -56.2 -56.2 -36.0 - - - 181.2 - 37.8 - * * 7 GLU 7 H A 56.8 - - 180.9 - -68.2 -46.2 - - - 180.4 - 33.3 - 8 ALA 8 H A - - - - - -75.6 -29.6 - - - 178.5 - 33.6 - 9 ALA 9 H A - - - - - -64.2 -42.0 - - - 177.8 -2.9 33.5 - * * 10 ARG 10 H A - 188.1 - 184.7 - -65.3 -33.4 - - - 178.3 -1.9 32.7 - 11 LEU 11 H A - - -56.7 181.2 - -60.4 -51.8 - - - 179.3 -1.1 34.7 - * * * 12 ARG 12 H A - - -59.5 180.8 - -61.1 -36.0 - - - 179.5 -2.4 34.2 - 13 PHE 13 H A - 179.0 - - - -69.4 -42.8 - - - 179.2 -2.2 34.4 - 14 ARG 14 H A - - -76.9 - - -81.8 -26.7 - - - 178.2 -3.0 31.8 - * * * * 15 CYS 15 h A - 183.7 - - - - - - - - 178.8 -2.8 33.9 - * * 16 PHE 16 B - 184.6 - - - - - - - - 178.2 - 34.9 - 17 HIS 17 B 73.0 - - - - - - - - - 176.1 - 34.4 - 18 TYR 18 B - 171.6 - - - - - - - - 177.3 -1.3 32.7 - 19 GLU 19 t B 48.2 - - 174.2 - - - - - - 182.4 -.6 32.4 - * +* +* Residue-by-residue listing for refined_1 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 - - -50.5 - - - - - - - 180.0 -.5 34.2 - * +* +* 21 ALA 21 T A - - - - - - - - - - 178.8 - 33.3 - 22 THR 22 T A - 201.5 - - - - - - - - 181.0 -1.6 33.7 - * * 23 GLY 23 h - - - - - - - - - - - 183.4 -1.0 - - * * 24 PRO 24 H - - - - - -67.7 -67.7 -38.5 - - - 181.9 - 38.1 - * * 25 GLN 25 H A - - -91.5 157.1 - -77.6 -27.4 - - - 172.1 - 30.1 - +* * * * * * +* 26 GLU 26 H A - 173.0 - 170.9 - -75.6 -38.1 - - - 174.5 - 32.0 - 27 ALA 27 H A - - - - - -63.0 -39.9 - - - 174.9 -2.3 34.3 - 28 LEU 28 H A - - -68.0 181.8 - -56.7 -45.3 - - - 179.9 -2.3 33.5 - 29 ALA 29 H A - - - - - -58.2 -36.2 - - - 179.5 -1.6 33.3 - 30 GLN 30 H A - - -44.6 - - -72.6 -51.2 - - - 179.4 -1.5 36.0 - * * * 31 LEU 31 H A - - -69.0 169.4 - -59.2 -40.1 - - - 181.0 -3.2 34.6 - +* +* 32 ARG 32 H A - 190.8 - 176.1 - -65.0 -32.6 - - - 178.9 -3.6 36.1 - ** ** 33 GLU 33 H A - 178.2 - 180.9 - -79.3 -49.3 - - - 179.5 -1.0 36.3 - * * * 34 LEU 34 H A - - -63.6 176.9 - -61.8 -43.3 - - - 179.7 -3.2 33.8 - +* +* 35 CYS 35 H A 63.9 - - - - -68.4 -29.6 - - - 178.8 -3.2 33.2 - +* +* 36 ARG 36 H A - 180.9 - - - -72.6 -30.7 - - - 175.8 -.7 32.8 - +* +* 37 GLN 37 H A - - -64.5 181.2 - -74.0 -16.6 - - - 179.1 -1.6 34.2 - ** ** 38 TRP 38 H a - 164.1 - - - -93.8 -56.9 - - - 181.2 -.7 33.3 - * ** +* +* ** 39 LEU 39 H A - - -60.0 158.5 - -74.6 -46.2 - - - 175.6 -3.6 35.1 - * ** ** 40 ARG 40 h l - - -54.0 187.3 - - - - - - 174.5 -1.2 32.0 - * * 41 PRO 41 T - - - - - -58.4 - - - - - 178.4 - 39.5 - +* +* 42 GLU 42 T A 52.7 - - 183.2 - - - - - - 180.7 - 35.1 - 43 VAL 43 T A - - -59.5 - - - - - - - 182.9 -1.3 31.6 - * * 44 ARG 44 t B - - -62.7 186.0 - - - - - - 179.0 -3.6 32.6 - ** ** 45 SER 45 h B 39.1 - - - - - - - - - 189.3 - 33.3 - +* +* +* 46 LYS 46 H A - - -49.7 175.6 - -66.0 -37.2 - - - 183.2 - 36.8 - * * 47 GLU 47 H A 70.8 - - - - -70.5 -29.9 - - - 174.6 - 31.0 - 48 GLN 48 H A - - -61.2 - - -64.1 -38.2 - - - 179.1 - 35.1 - 49 MET 49 H A - - -60.0 180.9 - -68.5 -36.5 - - - 174.4 -1.2 33.1 - * * 50 LEU 50 H A - - -65.8 177.1 - -56.0 -53.6 - - - 182.4 -1.9 35.1 - * * 51 GLU 51 H A - - -59.5 - - -57.2 -51.2 - - - 180.6 -2.2 34.2 - * * 52 LEU 52 H A - - -62.9 177.8 - -58.7 -40.0 - - - 180.9 -2.7 34.3 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 53 LEU 53 H A - 180.8 - - - -76.9 -30.0 - - - 173.8 -2.3 31.6 - * * 54 VAL 54 H A - 185.3 - - - -61.1 -46.3 - - - 177.4 -2.4 34.2 - 55 LEU 55 H A - 177.9 - - - -54.2 -47.9 - - - 181.7 -2.4 36.2 - 56 GLU 56 H A - 185.5 - - - -53.3 -52.1 - - - 182.3 -1.8 34.9 - * * * 57 GLN 57 H A - 207.9 - - - -74.6 -39.9 - - - 181.2 -2.1 34.7 - * * 58 PHE 58 H A - 178.1 - - - -53.1 -44.9 - - - 176.7 -3.3 33.9 - * +* +* 59 LEU 59 H A - - -88.3 - - -61.2 -39.2 - - - 180.9 -2.7 30.7 - * * 60 GLY 60 H - - - - - - -80.7 -21.1 - - - 177.4 -1.2 - - * +* * +* 61 ALA 61 H A - - - - - -71.4 -29.4 - - - 175.7 -2.2 33.5 - 62 LEU 62 h B - - -65.4 170.8 - - - - - - 177.0 -1.3 37.6 - * * * 63 PRO 63 h - - - - - -71.6 - - - - - 181.7 - 38.8 - * * 64 PRO 64 H - - - - - -42.9 -42.9 -44.2 - - - 180.4 - 38.3 - ** +* * ** 65 GLU 65 H A 53.6 - - 183.7 - -65.7 -47.7 - - - 178.5 - 31.8 - 66 ILE 66 H A - - -61.4 184.0 - -70.1 -38.5 - - - 179.9 - 34.1 - 67 GLN 67 H A - 181.1 - 177.9 - -62.3 -39.8 - - - 179.1 -3.5 34.0 - +* +* 68 ALA 68 H A - - - - - -59.2 -35.4 - - - 179.4 -2.2 33.9 - 69 ARG 69 H A - - -62.1 - - -68.9 -45.5 - - - 178.1 -1.0 33.3 - * * 70 VAL 70 H A - 179.0 - - - -63.5 -46.9 - - - 178.0 -1.8 34.5 - 71 GLN 71 H A - - -101.6 - - -58.6 -28.8 - - - 176.8 -3.2 31.2 - ** +* ** 72 GLY 72 H - - - - - - -78.7 -25.4 - - - 180.5 -1.3 - - * * * 73 GLN 73 H A - - -48.8 196.5 - -97.8 -45.9 - - - 181.9 -1.1 34.5 - * * +** * +** 74 ARG 74 h l - - -60.5 - - - - - - - 175.8 -3.7 31.7 - ** ** 75 PRO 75 - - - - - -70.0 - - - - - 179.3 - 38.8 - * * 76 GLY 76 - - - - - - - - - - - 177.2 - - - 77 SER 77 h B - - -54.1 - - - - - - - 183.3 - 34.8 - 78 PRO 78 H - - - - - -54.8 -54.8 -45.5 - - - 182.3 - 38.0 - * * 79 GLU 79 H A - - -53.3 - - -70.2 -32.8 - - - 176.8 - 32.1 - 80 GLU 80 H A - 185.8 - - - -65.3 -45.7 - - - 175.7 - 33.7 - 81 ALA 81 H A - - - - - -59.7 -40.9 - - - 178.8 -2.5 34.1 - 82 ALA 82 H A - - - - - -58.6 -33.4 - - - 179.6 -2.5 34.3 - 83 ALA 83 H A - - - - - -69.1 -49.5 - - - 178.2 -1.4 32.6 - 84 LEU 84 H A 51.5 - - 154.1 - -67.3 -39.6 - - - 180.9 -1.7 28.3 - * +* +* 85 VAL 85 H A - - -58.5 - - -66.1 -32.2 - - - 175.9 -2.6 31.0 - 86 ASP 86 H A - 181.0 - - - -63.7 -31.2 - - - 177.4 -1.6 33.5 - 87 GLY 87 H - - - - - - -81.7 -38.6 - - - 180.0 -1.0 - - * * * 88 LEU 88 H A - - -61.3 174.4 - -65.0 -26.8 - - - 179.7 -2.7 34.9 - * * 89 ARG 89 h A 66.0 - - 177.5 - - - - - - 177.8 -1.7 33.8 - Residue-by-residue listing for refined_1 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 T B - - -58.8 178.0 - - - - - - 188.6 -1.4 34.0 - * * 91 GLU 91 T l - - -55.3 172.8 - - - - - - 190.1 -1.0 33.5 - +* * +* 92 PRO 92 T - - - - - -20.9 - - - - - 182.2 - 37.3 - +*** +*** 93 GLY 93 T - - - - - - - - - - - 179.7 -2.8 - - * * 94 GLY 94 t - - - - - - - - - - - - -2.6 - - 95 GLY 301 - - - - - - - - - - - 179.3 - - - 96 SER 302 B - 187.5 - - - - - - - - 178.6 - 34.8 - 97 ASP 303 B - - -63.1 - - - - - - - 178.9 - 34.6 - 98 PRO 304 - - - - - -58.9 - - - - - 180.9 - 38.8 - * * 99 GLY 305 h - - - - - - - - - - - 181.3 - - - 100 PRO 306 H - - - - - -65.0 -65.0 -36.0 - - - 182.7 - 38.6 - * * 101 GLU 307 H A 68.2 - - - - -70.6 -42.1 - - - 178.7 - 31.2 - 102 ALA 308 H A - - - - - -63.8 -40.5 - - - 178.7 - 34.0 - 103 ALA 309 H A - - - - - -65.3 -38.4 - - - 179.2 -2.3 33.4 - 104 ARG 310 H A - 189.7 - 189.5 - -67.2 -34.1 - - - 179.5 -2.2 34.2 - 105 LEU 311 H A - - -55.2 183.4 - -64.2 -44.6 - - - 177.6 -1.9 33.8 - 106 ARG 312 H A - - -59.7 178.9 - -63.4 -37.7 - - - 177.3 -2.1 34.2 - 107 PHE 313 H A - 174.5 - - - -61.4 -39.7 - - - 177.2 -2.2 34.1 - 108 ARG 314 H A - - -70.5 197.0 - -91.4 -16.1 - - - 175.6 -2.1 29.1 - * ** ** * ** 109 CYS 315 H A - 180.3 - - - -71.0 -20.8 - - - 177.9 -2.0 34.2 - +* +* 110 PHE 316 h B - 181.1 - - - - - - - - 177.6 -.9 34.9 - * * 111 HIS 317 B 69.7 - - - - - - - - - 175.4 - 34.7 - 112 TYR 318 B - 166.8 - - - - - - - - 179.5 -1.1 32.8 - * * 113 GLU 319 t B 50.1 - - 171.7 - - - - - - 179.8 -.5 31.6 - ** ** 114 GLU 320 T A - - -63.5 166.5 - - - - - - 180.7 -.5 36.0 - +* +* 115 ALA 321 T A - - - - - - - - - - 181.6 - 33.6 - 116 THR 322 T A - 195.8 - - - - - - - - 183.3 -.6 34.5 - +* +* 117 GLY 323 h - - - - - - - - - - - 183.5 -.8 - - +* +* 118 PRO 324 H - - - - - -59.8 -59.8 -33.4 - - - 180.0 - 37.6 - * * 119 GLN 325 H A - - -84.5 - - -70.8 -40.0 - - - 177.7 - 31.9 - * * 120 GLU 326 H A - 180.3 - 167.7 - -71.8 -33.6 - - - 174.3 - 31.7 - 121 ALA 327 H A - - - - - -63.0 -36.5 - - - 175.3 -2.5 34.1 - 122 LEU 328 H A - - -67.2 175.2 - -59.2 -41.2 - - - 179.6 -1.8 34.3 - 123 ALA 329 H A - - - - - -62.6 -27.9 - - - 178.9 -1.3 33.4 - * * 124 GLN 330 H A - - -46.3 - - -78.4 -51.2 - - - 179.7 -1.0 36.4 - * * * * * 125 LEU 331 H A - - -70.0 170.6 - -60.0 -42.4 - - - 179.0 -2.9 33.7 - * * 126 ARG 332 H A - 184.0 - 177.7 - -61.7 -44.3 - - - 177.9 -3.6 34.5 - ** ** Residue-by-residue listing for refined_1 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 127 GLU 333 H A - 175.3 - 179.9 - -61.4 -50.4 - - - 180.5 -1.2 35.7 - * * 128 LEU 334 H A - - -62.8 175.2 - -64.7 -43.4 - - - 180.2 -3.0 33.3 - * * 129 CYS 335 H A 70.3 - - - - -67.1 -33.1 - - - 180.3 -3.4 33.5 - +* +* 130 ARG 336 H A - 183.1 - - - -68.4 -31.0 - - - 177.9 -2.1 32.3 - 131 GLN 337 H A - - -61.6 185.6 - -76.1 -16.2 - - - 178.3 -1.4 33.2 - ** ** 132 TRP 338 H A - 159.9 - - - -94.5 -49.6 - - - 181.6 -.7 34.1 - * ** +* ** 133 LEU 339 H A - - -62.3 159.4 - -78.2 -50.0 - - - 176.8 -3.5 34.4 - * +* +* 134 ARG 340 h l - - -57.1 182.4 - - - - - - 174.6 -1.5 31.5 - 135 PRO 341 T - - - - - -47.9 - - - - - 179.2 - 40.1 - +* +* +* 136 GLU 342 T A 54.5 - - 185.4 - - - - - - 184.2 - 36.0 - 137 VAL 343 T A - - -62.2 - - - - - - - 179.6 -1.6 32.5 - 138 ARG 344 t B - - -64.0 187.2 - - - - - - 178.0 -3.6 31.2 - ** ** 139 SER 345 h B 39.7 - - - - - - - - - 191.6 - 32.4 - +* +* +* 140 LYS 346 H A - - -49.2 176.8 - -66.7 -37.0 - - - 183.0 - 37.1 - * * 141 GLU 347 H A 69.0 - - - - -72.0 -29.2 - - - 176.3 - 30.9 - 142 GLN 348 H A - - -57.5 - - -71.5 -31.1 - - - 175.6 -.5 33.6 - ** ** 143 MET 349 H A - - -62.1 179.5 - -67.6 -36.2 - - - 174.8 -1.2 33.5 - * * 144 LEU 350 H A - - -64.4 177.8 - -54.6 -53.1 - - - 183.0 -1.6 35.3 - * * 145 GLU 351 H A - - -58.3 - - -54.5 -48.7 - - - 180.5 -1.8 35.5 - 146 LEU 352 H A - - -62.4 177.7 - -61.3 -41.6 - - - 180.7 -1.9 34.7 - 147 LEU 353 H A - 180.2 - - - -76.0 -29.6 - - - 174.5 -2.3 31.1 - 148 VAL 354 H A - 187.5 - - - -59.5 -47.9 - - - 177.6 -2.6 34.7 - 149 LEU 355 H A - 177.4 - - - -53.1 -44.7 - - - 183.4 -2.1 36.4 - * * 150 GLU 356 H A - 182.9 - - - -56.2 -52.6 - - - 182.0 -1.4 34.5 - * * 151 GLN 357 H A - 208.0 - - - -73.9 -38.7 - - - 182.2 -1.8 35.1 - * * 152 PHE 358 H A - 178.7 - - - -53.3 -48.1 - - - 177.8 -2.8 34.0 - * * 153 LEU 359 H A - - -94.1 - - -59.8 -41.6 - - - 181.6 -2.8 30.5 - +* * +* 154 GLY 360 H - - - - - - -81.1 -13.7 - - - 177.4 -1.3 - - * ** ** 155 ALA 361 H A - - - - - -79.1 -27.0 - - - 176.4 -1.6 33.8 - * * * 156 LEU 362 h B - - -66.2 170.1 - - - - - - 177.1 -1.2 37.1 - * * 157 PRO 363 h - - - - - -69.4 - - - - - 182.6 - 38.6 - * * 158 PRO 364 H - - - - - -42.4 -42.4 -42.9 - - - 180.9 - 37.8 - ** +* * ** 159 GLU 365 H A 56.2 - - 178.5 - -69.6 -47.6 - - - 177.9 - 31.8 - 160 ILE 366 H A - - -62.6 182.7 - -66.7 -40.4 - - - 179.4 - 33.9 - Residue-by-residue listing for refined_1 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 - 179.9 - 176.7 - -61.6 -39.7 - - - 178.4 -3.5 34.0 - +* +* 162 ALA 368 H A - - - - - -62.7 -35.5 - - - 178.4 -2.0 33.8 - 163 ARG 369 H A - - -64.2 - - -65.0 -41.2 - - - 176.6 -1.3 33.7 - 164 VAL 370 H A - 174.1 - - - -64.7 -52.8 - - - 179.2 -1.7 34.8 - * * 165 GLN 371 H A - - -100.2 - - -56.9 -29.2 - - - 176.9 -3.0 30.4 - ** * ** 166 GLY 372 h - - - - - - - - - - - 178.6 -1.8 - - 167 GLN 373 T a - - -56.5 191.4 - - - - - - 181.4 -2.3 34.1 - 168 ARG 374 t l - - -56.8 - - - - - - - 177.9 -3.8 32.2 - ** ** 169 PRO 375 - - - - - -72.8 - - - - - 178.5 - 38.9 - * * 170 GLY 376 - - - - - - - - - - - 177.3 - - - 171 SER 377 h B 58.9 - - - - - - - - - 186.2 - 33.0 - * * 172 PRO 378 H - - - - - -57.5 -57.5 -44.8 - - - 182.0 - 37.1 - 173 GLU 379 H A - - -62.3 171.7 - -69.4 -29.9 - - - 177.8 - 33.0 - 174 GLU 380 H A - 185.8 - - - -71.8 -45.7 - - - 174.6 - 34.5 - 175 ALA 381 H A - - - - - -57.3 -41.9 - - - 177.7 -2.5 34.6 - 176 ALA 382 H A - - - - - -58.9 -43.6 - - - 178.8 -2.7 34.4 - 177 ALA 383 H A - - - - - -66.5 -33.8 - - - 179.1 -2.1 33.2 - 178 LEU 384 H A - - -45.4 182.9 - -65.7 -48.8 - - - 184.1 -2.0 36.5 - * * 179 VAL 385 H A - - -55.9 - - -74.3 -30.5 - - - 177.6 -2.5 30.9 - 180 ASP 386 H A - 180.3 - - - -51.0 -36.6 - - - 176.5 -2.4 33.7 - * * 181 GLY 387 H - - - - - - -84.1 -32.9 - - - 181.9 -.8 - - +* +* +* 182 LEU 388 H A - - -61.7 175.2 - -67.2 -29.2 - - - 178.9 -1.1 34.8 - * * 183 ARG 389 h A 61.2 - - 177.4 - - - - - - 179.6 -2.3 33.6 - 184 ARG 390 t b - - -56.9 176.9 - - - - - - 181.3 -1.2 34.8 - * * 185 GLU 391 S l - - -56.7 176.0 - - - - - - 185.6 -1.8 32.5 - 186 PRO 392 S - - - - - -49.8 - - - - - 181.6 - 38.2 - * * * 187 GLY 393 - - - - - - - - - - - 179.9 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +* * ** * +*** +** ** +* ** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.7 182.2 -62.8 177.7 -57.2 -66.4 -38.7 - - - 179.4 -2.0 34.2 Standard deviations: 10.2 9.3 11.4 8.1 13.0 9.4 8.8 - - - 2.9 .8 2.1 Numbers of values: 20 44 68 63 18 123 123 0 0 0 186 126 170 0 Residue-by-residue listing for refined_1 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_1 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 - 1.239 1.501 - 1.461 - 116.34 120.24 - 111.06 - 123.42 2 SER 2 1.317 1.237 1.531 1.553 1.439 122.89 117.14 120.31 110.81 108.05 109.64 122.55 * * * 3 ASP 3 1.305 1.235 1.515 1.547 1.447 121.63 118.78 119.57 109.76 107.41 111.07 121.65 +* * * +* 4 PRO 4 1.347 1.234 1.539 1.538 1.477 122.33 116.15 120.96 110.04 112.72 103.51 122.89 5 GLY 5 1.317 1.226 1.504 - 1.439 121.26 118.95 119.23 - 109.80 - 121.81 * * 6 PRO 6 1.343 1.235 1.529 1.538 1.473 122.79 116.04 121.12 110.64 113.75 104.04 122.79 7 GLU 7 1.306 1.245 1.537 1.527 1.439 121.68 115.96 120.61 111.95 111.20 109.90 123.40 +* +* 8 ALA 8 1.331 1.229 1.518 1.517 1.451 122.65 115.91 121.11 110.85 110.80 110.53 122.97 9 ALA 9 1.318 1.229 1.512 1.510 1.444 122.10 116.86 120.28 110.85 110.44 110.76 122.84 10 ARG 10 1.344 1.219 1.528 1.530 1.451 120.00 116.53 120.55 109.37 109.78 113.70 122.92 * +* +* 11 LEU 11 1.337 1.212 1.511 1.531 1.465 121.65 115.71 120.87 108.84 109.29 111.50 123.39 12 ARG 12 1.322 1.234 1.533 1.536 1.467 122.58 115.24 121.27 110.61 110.75 110.05 123.48 13 PHE 13 1.315 1.220 1.545 1.538 1.456 124.00 116.93 120.48 112.05 111.64 107.97 122.59 * * * * 14 ARG 14 1.325 1.232 1.516 1.536 1.472 122.40 116.65 120.36 111.49 112.94 111.66 122.99 15 CYS 15 1.317 1.243 1.529 1.543 1.452 121.87 115.49 121.24 111.04 109.74 110.55 123.26 Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 16 PHE 16 1.319 1.244 1.518 1.537 1.434 122.44 116.08 120.98 110.24 109.25 110.09 122.94 * * 17 HIS 17 1.298 1.234 1.501 1.562 1.432 121.18 117.56 119.77 109.85 107.17 112.20 122.66 ** * +* * * ** 18 TYR 18 1.294 1.231 1.511 1.527 1.427 119.43 114.97 121.16 111.79 109.69 111.57 123.81 ** +* * ** 19 GLU 19 1.295 1.236 1.515 1.550 1.422 123.17 115.33 121.15 112.86 109.22 111.42 123.50 ** +* * ** 20 GLU 20 1.317 1.219 1.513 1.540 1.457 123.73 115.77 120.69 108.44 111.15 112.19 123.54 * * 21 ALA 21 1.310 1.232 1.536 1.515 1.451 123.03 117.86 120.32 110.92 112.40 110.26 121.82 * * 22 THR 22 1.331 1.200 1.541 1.584 1.444 119.13 116.28 121.48 110.84 108.14 111.98 122.18 +* +* * * +* 23 GLY 23 1.320 1.230 1.513 - 1.444 120.63 119.06 119.97 - 111.25 - 120.96 * * * 24 PRO 24 1.339 1.209 1.518 1.514 1.452 121.65 116.66 120.50 110.71 113.17 103.65 122.82 * * 25 GLN 25 1.302 1.234 1.504 1.496 1.441 122.22 116.28 120.85 114.42 113.72 110.42 122.86 +* +* ** ** 26 GLU 26 1.293 1.225 1.513 1.522 1.438 120.91 115.76 120.93 112.84 108.96 111.62 123.29 +** * * +** 27 ALA 27 1.325 1.227 1.520 1.518 1.452 122.07 116.33 120.48 110.32 109.30 110.47 123.19 28 LEU 28 1.340 1.188 1.487 1.531 1.457 121.91 117.02 119.71 108.35 110.56 113.49 123.26 ** +* +* ** 29 ALA 29 1.325 1.223 1.530 1.521 1.458 121.77 116.18 120.67 110.95 111.00 110.71 123.11 30 GLN 30 1.328 1.214 1.528 1.543 1.463 121.93 115.44 121.34 108.14 108.32 110.64 123.21 * * * 31 LEU 31 1.324 1.210 1.525 1.534 1.464 123.52 115.96 120.82 110.26 111.86 109.48 123.21 * * * 32 ARG 32 1.309 1.214 1.517 1.520 1.465 124.49 114.37 121.81 110.39 109.88 107.55 123.81 * +* +* +* 33 GLU 33 1.281 1.227 1.540 1.513 1.429 124.42 116.44 120.46 112.59 109.53 105.24 123.05 *** +* +* * *** *** 34 LEU 34 1.328 1.228 1.523 1.535 1.467 122.77 116.76 120.62 109.94 111.99 110.93 122.61 35 CYS 35 1.327 1.217 1.523 1.541 1.454 121.17 116.35 121.06 111.10 109.68 111.51 122.56 36 ARG 36 1.327 1.208 1.527 1.541 1.416 122.32 116.73 120.22 114.16 109.93 109.20 123.04 * ** ** ** 37 GLN 37 1.321 1.233 1.530 1.511 1.464 122.33 114.71 121.65 110.58 110.82 109.70 123.64 38 TRP 38 1.308 1.230 1.544 1.546 1.441 124.17 116.31 120.82 113.61 111.92 108.02 122.87 +* * +* * +* 39 LEU 39 1.303 1.232 1.532 1.523 1.459 123.03 115.52 120.69 111.67 110.34 107.63 123.80 +* +* +* 40 ARG 40 1.339 1.220 1.539 1.552 1.465 124.71 118.95 119.96 109.70 114.48 112.69 121.09 * +* * * * * +* 41 PRO 41 1.359 1.233 1.526 1.538 1.488 122.90 113.63 122.00 109.62 110.74 103.10 124.37 * * ** +* ** 42 GLU 42 1.311 1.226 1.541 1.539 1.440 125.51 117.22 120.57 111.18 111.99 108.00 122.20 * ** * ** 43 VAL 43 1.330 1.230 1.526 1.559 1.459 120.53 117.01 120.34 110.53 112.99 113.12 122.65 44 ARG 44 1.321 1.236 1.514 1.536 1.453 120.71 114.39 121.79 109.80 112.90 112.40 123.81 * * 45 SER 45 1.296 1.241 1.544 1.519 1.424 125.15 115.46 121.13 113.98 111.78 107.59 123.41 ** +* +* ** +* ** Residue-by-residue listing for refined_1 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 1.316 1.228 1.524 1.500 1.472 124.35 116.64 120.92 107.99 113.19 107.87 122.44 * * * +* +* 47 GLU 47 1.305 1.232 1.518 1.556 1.477 120.36 115.73 120.81 111.16 110.32 114.28 123.46 +* * ** ** 48 GLN 48 1.331 1.230 1.513 1.535 1.449 122.22 115.29 121.22 109.13 109.05 110.89 123.49 49 MET 49 1.322 1.228 1.490 1.505 1.445 122.34 116.31 119.83 111.34 110.96 110.77 123.86 +* * +* 50 LEU 50 1.346 1.208 1.513 1.554 1.454 120.94 115.75 120.33 108.18 108.37 112.18 123.72 * * * * * * 51 GLU 51 1.335 1.238 1.533 1.530 1.467 122.94 116.50 120.68 109.42 111.79 110.73 122.82 52 LEU 52 1.330 1.236 1.525 1.531 1.451 122.16 116.06 120.99 110.19 111.23 110.21 122.93 53 LEU 53 1.310 1.241 1.553 1.515 1.416 121.68 117.71 120.24 115.55 112.50 108.01 122.04 * * ** +** * +** 54 VAL 54 1.342 1.225 1.529 1.561 1.473 120.44 114.99 121.03 107.70 108.21 113.84 123.96 * * * 55 LEU 55 1.337 1.238 1.511 1.559 1.474 124.40 114.66 121.05 110.51 109.57 107.87 124.28 * * +* +* 56 GLU 56 1.316 1.246 1.541 1.533 1.446 123.38 116.50 120.89 109.68 111.37 109.78 122.62 57 GLN 57 1.325 1.208 1.522 1.521 1.455 120.89 116.72 120.14 109.54 109.21 110.69 123.11 * * 58 PHE 58 1.339 1.233 1.514 1.546 1.468 122.32 115.85 120.78 110.39 110.25 111.05 123.35 59 LEU 59 1.317 1.213 1.514 1.536 1.450 121.36 117.40 119.85 112.90 113.27 111.69 122.69 * * 60 GLY 60 1.316 1.233 1.518 - 1.451 120.00 116.39 120.49 - 112.69 - 123.10 61 ALA 61 1.324 1.233 1.523 1.535 1.455 122.02 115.50 120.89 111.13 109.66 110.93 123.61 62 LEU 62 1.330 1.243 1.528 1.522 1.457 123.69 118.29 119.98 107.34 109.85 108.37 121.71 * * * * * 63 PRO 63 1.345 1.237 1.528 1.533 1.450 121.56 118.17 119.39 110.26 109.22 103.95 122.44 * * * 64 PRO 64 1.352 1.226 1.536 1.543 1.475 124.23 116.70 120.38 110.44 113.68 103.55 122.90 65 GLU 65 1.328 1.230 1.550 1.535 1.461 121.93 117.60 120.12 112.49 113.01 110.49 122.25 * * * 66 ILE 66 1.336 1.242 1.534 1.552 1.456 121.34 115.58 121.42 110.31 110.40 110.82 122.99 67 GLN 67 1.319 1.234 1.526 1.525 1.447 122.34 116.13 120.51 110.86 110.54 110.06 123.33 68 ALA 68 1.324 1.235 1.524 1.521 1.464 122.81 116.30 120.74 110.10 111.37 110.64 122.95 69 ARG 69 1.324 1.224 1.516 1.525 1.453 121.36 116.58 120.66 110.35 110.55 111.63 122.75 70 VAL 70 1.326 1.218 1.505 1.527 1.458 121.09 114.96 121.30 107.63 109.99 112.77 123.74 71 GLN 71 1.297 1.228 1.533 1.530 1.443 123.30 116.58 120.35 113.40 112.70 110.67 123.06 ** +* ** 72 GLY 72 1.318 1.229 1.533 - 1.444 121.00 117.79 120.37 - 113.07 - 121.84 73 GLN 73 1.330 1.233 1.523 1.522 1.471 120.22 114.63 121.23 108.19 110.48 111.85 124.14 * * 74 ARG 74 1.327 1.221 1.531 1.528 1.460 125.24 117.73 120.64 110.68 112.68 112.62 121.54 +* * +* 75 PRO 75 1.344 1.222 1.533 1.532 1.465 121.83 115.36 121.57 110.27 111.03 103.55 123.06 * * 76 GLY 76 1.321 1.226 1.513 - 1.452 121.97 116.36 120.66 - 112.63 - 122.97 77 SER 77 1.306 1.244 1.538 1.521 1.440 122.16 117.65 119.91 110.73 108.51 109.59 122.41 +* +* 78 PRO 78 1.349 1.235 1.527 1.532 1.470 123.11 117.03 120.28 109.56 114.17 104.81 122.67 +* +* 79 GLU 79 1.317 1.230 1.513 1.530 1.451 120.85 115.94 120.74 110.59 111.45 112.87 123.32 * * 80 GLU 80 1.309 1.228 1.530 1.530 1.439 121.63 116.61 120.54 111.14 109.26 110.79 122.84 * * Residue-by-residue listing for refined_1 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 81 ALA 81 1.347 1.232 1.524 1.511 1.450 121.60 115.68 120.71 110.47 110.46 110.28 123.59 * * 82 ALA 82 1.332 1.221 1.533 1.526 1.459 123.32 115.56 121.28 110.62 110.91 109.70 123.15 83 ALA 83 1.296 1.241 1.533 1.516 1.444 122.97 118.22 119.69 111.39 111.98 110.95 122.09 ** * ** 84 LEU 84 1.351 1.220 1.505 1.553 1.463 118.48 117.25 120.18 110.38 112.64 117.51 122.55 +* * +* **** **** 85 VAL 85 1.326 1.230 1.519 1.538 1.459 120.45 116.16 120.76 111.22 111.60 113.68 123.07 * * 86 ASP 86 1.327 1.223 1.518 1.528 1.454 121.90 115.75 120.81 110.37 109.83 111.54 123.44 87 GLY 87 1.323 1.222 1.525 - 1.444 121.59 116.20 120.76 - 111.88 - 123.04 88 LEU 88 1.325 1.240 1.527 1.530 1.477 123.21 116.19 121.32 109.37 111.65 109.86 122.49 * * 89 ARG 89 1.316 1.231 1.526 1.519 1.451 121.15 116.22 121.12 109.91 110.76 111.18 122.66 90 ARG 90 1.314 1.243 1.485 1.523 1.459 121.00 115.45 119.97 109.99 107.11 112.12 124.57 * +* * +* 91 GLU 91 1.327 1.239 1.525 1.535 1.449 123.25 116.17 119.91 111.65 106.90 111.33 123.84 +* +* 92 PRO 92 1.385 1.227 1.518 1.512 1.469 125.87 115.25 121.30 112.10 115.49 102.64 123.37 +** * * * +** 93 GLY 93 1.316 1.239 1.507 - 1.437 121.63 115.80 120.91 - 110.73 - 123.28 94 GLY 94 1.313 1.249 1.513 - 1.447 120.98 - 120.08 - 111.75 - - * * 95 GLY 301 - 1.237 1.510 - 1.453 - 115.80 121.12 - 111.63 - 123.08 96 SER 302 1.301 1.237 1.529 1.546 1.435 121.77 116.81 120.46 110.96 108.39 109.88 122.72 +* * * +* 97 ASP 303 1.305 1.227 1.512 1.549 1.452 122.00 118.81 119.46 109.53 108.31 111.58 121.72 +* * * +* 98 PRO 304 1.347 1.242 1.528 1.535 1.472 122.29 115.60 121.36 110.01 111.36 103.66 123.03 99 GLY 305 1.306 1.242 1.494 - 1.417 120.97 118.00 119.84 - 110.83 - 122.16 +* * ** ** 100 PRO 306 1.329 1.230 1.529 1.536 1.454 122.23 116.88 120.73 110.43 111.83 103.71 122.29 101 GLU 307 1.325 1.228 1.516 1.560 1.441 120.05 115.99 120.25 112.04 109.93 113.55 123.69 +* * +* +* 102 ALA 308 1.336 1.236 1.520 1.521 1.456 122.55 116.04 120.98 110.38 110.45 110.60 122.97 103 ALA 309 1.327 1.231 1.519 1.518 1.449 121.55 116.70 120.52 110.63 110.59 111.11 122.76 104 ARG 310 1.336 1.230 1.526 1.520 1.450 120.77 116.28 120.82 108.18 109.98 112.64 122.90 * * * 105 LEU 311 1.330 1.208 1.504 1.531 1.458 121.11 115.90 120.75 110.07 109.34 111.77 123.32 * * 106 ARG 312 1.319 1.233 1.531 1.524 1.466 122.13 114.94 121.32 110.55 110.08 110.18 123.72 107 PHE 313 1.316 1.223 1.536 1.539 1.455 124.24 117.37 120.34 112.58 111.33 108.05 122.29 * * * * 108 ARG 314 1.328 1.230 1.503 1.510 1.463 120.32 116.72 120.39 111.38 114.32 114.39 122.88 * * ** ** 109 CYS 315 1.309 1.238 1.522 1.540 1.444 121.82 115.28 121.05 111.04 108.75 110.43 123.67 * * 110 PHE 316 1.330 1.237 1.514 1.538 1.435 122.87 115.78 121.02 109.91 109.65 110.41 123.20 * * 111 HIS 317 1.301 1.235 1.503 1.566 1.435 120.75 117.73 119.58 109.87 107.24 111.85 122.69 ** * +* * * ** 112 TYR 318 1.299 1.229 1.506 1.534 1.431 119.46 115.34 121.26 111.80 108.97 111.77 123.35 ** * * ** 113 GLU 319 1.289 1.232 1.501 1.538 1.410 121.64 114.51 121.78 112.66 110.88 112.01 123.69 +** * +** * +** Residue-by-residue listing for refined_1 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 114 GLU 320 1.296 1.230 1.526 1.511 1.440 123.89 115.72 120.80 110.07 110.45 108.01 123.47 ** * * ** 115 ALA 321 1.323 1.222 1.531 1.520 1.459 122.91 117.48 120.42 110.40 112.49 110.40 122.09 116 THR 322 1.320 1.227 1.550 1.584 1.451 120.04 116.09 121.12 111.05 109.06 110.25 122.66 * +* +* 117 GLY 323 1.332 1.234 1.515 - 1.446 121.27 119.21 119.72 - 110.39 - 121.07 * * * 118 PRO 324 1.343 1.223 1.536 1.514 1.462 121.99 117.80 119.94 110.75 114.15 103.92 122.22 119 GLN 325 1.338 1.228 1.508 1.539 1.467 120.10 115.57 121.50 109.36 110.79 114.59 122.92 ** ** 120 GLU 326 1.294 1.228 1.530 1.524 1.442 121.22 116.41 120.78 113.26 110.66 110.98 122.80 ** +* ** 121 ALA 327 1.327 1.229 1.529 1.521 1.461 121.96 116.07 120.83 110.49 109.60 110.45 123.10 122 LEU 328 1.329 1.203 1.503 1.524 1.464 122.24 116.69 120.18 108.77 110.59 111.83 123.11 * * * 123 ALA 329 1.324 1.226 1.530 1.523 1.459 121.63 116.13 120.93 110.85 110.93 110.70 122.94 124 GLN 330 1.321 1.219 1.518 1.536 1.462 122.15 114.98 121.52 108.11 108.11 110.11 123.50 * * * 125 LEU 331 1.319 1.215 1.512 1.524 1.450 123.21 116.35 120.50 111.17 111.83 109.85 123.14 126 ARG 332 1.309 1.222 1.515 1.521 1.444 122.53 115.08 121.01 110.78 109.67 109.83 123.86 * * 127 GLU 333 1.300 1.235 1.538 1.524 1.441 123.72 116.00 120.89 111.60 110.49 106.91 123.06 ** * ** ** 128 LEU 334 1.316 1.233 1.527 1.529 1.451 122.57 117.05 120.29 111.23 112.14 110.23 122.64 129 CYS 335 1.330 1.218 1.523 1.548 1.457 120.89 115.97 121.28 110.48 109.59 111.68 122.71 130 ARG 336 1.325 1.206 1.519 1.550 1.443 122.39 117.08 119.86 113.68 110.89 109.95 123.03 * * +* +* 131 GLN 337 1.327 1.240 1.538 1.515 1.468 122.18 114.72 121.66 111.24 111.37 110.27 123.61 132 TRP 338 1.314 1.230 1.547 1.553 1.455 124.76 116.35 120.79 112.86 111.66 107.75 122.86 * * * +* * +* +* 133 LEU 339 1.315 1.227 1.524 1.528 1.458 122.81 115.94 120.37 111.90 110.63 108.42 123.68 * * 134 ARG 340 1.339 1.230 1.544 1.537 1.467 124.05 117.47 120.32 111.00 114.68 111.81 122.16 * * * 135 PRO 341 1.360 1.229 1.528 1.524 1.488 124.20 115.01 121.09 108.58 112.98 102.72 123.90 * * * * * 136 GLU 342 1.312 1.229 1.538 1.531 1.451 124.30 116.70 120.83 109.87 111.97 107.79 122.44 * * +* +* 137 VAL 343 1.318 1.230 1.505 1.557 1.444 120.97 117.13 120.49 110.42 112.03 112.55 122.38 138 ARG 344 1.313 1.235 1.489 1.527 1.432 119.60 114.03 121.97 110.86 112.22 113.65 123.98 * +* * * * +* +* 139 SER 345 1.274 1.243 1.542 1.521 1.403 123.79 115.64 121.04 115.05 111.02 108.13 123.32 +*** +** * +** * +*** 140 LYS 346 1.304 1.230 1.518 1.493 1.464 124.26 115.90 121.28 108.37 112.72 107.22 122.82 +* +* * +* +* 141 GLU 347 1.296 1.227 1.521 1.554 1.463 120.98 116.29 120.82 111.86 110.83 113.60 122.89 ** * +* ** 142 GLN 348 1.322 1.234 1.519 1.533 1.446 121.48 115.75 121.14 110.81 109.56 111.18 123.10 143 MET 349 1.328 1.236 1.500 1.504 1.451 121.88 115.74 120.30 110.94 110.42 110.67 123.95 * * * 144 LEU 350 1.348 1.207 1.513 1.551 1.456 121.81 115.81 120.21 108.08 108.79 111.75 123.79 * * * * * 145 GLU 351 1.341 1.240 1.534 1.531 1.478 123.52 115.89 120.91 108.41 111.39 110.04 123.20 * * * 146 LEU 352 1.326 1.232 1.523 1.528 1.445 122.50 116.04 121.01 110.20 111.18 109.74 122.95 Residue-by-residue listing for refined_1 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 1.311 1.238 1.556 1.520 1.419 121.92 117.79 120.15 115.77 112.69 108.35 122.05 * * ** +** * +** 148 VAL 354 1.338 1.234 1.535 1.561 1.477 120.69 114.51 121.31 107.33 108.16 113.45 124.15 * * * 149 LEU 355 1.337 1.238 1.515 1.563 1.475 124.90 114.62 121.05 110.60 109.90 107.39 124.33 +* +* +* +* 150 GLU 356 1.312 1.238 1.539 1.535 1.434 123.82 117.53 120.55 111.30 112.01 108.66 121.89 * * * * * 151 GLN 357 1.320 1.217 1.517 1.525 1.457 119.61 115.85 120.59 108.98 108.20 111.06 123.51 * * * 152 PHE 358 1.331 1.238 1.524 1.535 1.453 122.59 116.25 120.51 110.48 111.11 110.49 123.22 153 LEU 359 1.321 1.221 1.513 1.537 1.455 121.40 117.52 119.76 112.62 113.60 111.99 122.67 * * 154 GLY 360 1.318 1.233 1.508 - 1.451 119.56 116.31 120.68 - 112.62 - 123.00 155 ALA 361 1.317 1.236 1.519 1.521 1.444 122.06 115.54 120.60 110.88 109.95 110.67 123.85 156 LEU 362 1.327 1.241 1.536 1.529 1.461 123.58 118.49 119.92 108.01 109.88 108.59 121.59 * * * * * 157 PRO 363 1.348 1.238 1.522 1.536 1.450 121.49 118.16 119.28 109.98 109.15 104.73 122.56 * * +* +* 158 PRO 364 1.349 1.233 1.540 1.541 1.472 123.94 116.93 120.11 110.75 113.93 103.86 122.93 159 GLU 365 1.336 1.234 1.542 1.533 1.460 121.67 117.70 119.88 111.61 112.86 111.53 122.41 160 ILE 366 1.341 1.237 1.538 1.557 1.454 121.25 115.57 121.25 110.17 110.16 111.38 123.15 161 GLN 367 1.325 1.237 1.531 1.529 1.456 122.73 116.00 120.84 111.04 110.79 109.78 123.15 162 ALA 368 1.323 1.225 1.525 1.517 1.465 122.43 116.23 120.86 110.25 111.08 110.67 122.89 163 ARG 369 1.328 1.227 1.522 1.527 1.462 121.54 116.05 120.76 110.22 110.05 111.31 123.18 164 VAL 370 1.328 1.222 1.503 1.533 1.454 121.58 115.28 121.04 107.75 110.09 112.43 123.68 * * 165 GLN 371 1.308 1.225 1.529 1.533 1.451 123.07 116.45 120.54 113.29 113.14 111.62 122.99 +* +* +* 166 GLY 372 1.314 1.225 1.535 - 1.442 121.10 117.55 120.09 - 113.23 - 122.34 * * * 167 GLN 373 1.331 1.235 1.520 1.521 1.465 121.31 114.73 121.01 109.31 110.85 111.37 124.25 168 ARG 374 1.336 1.217 1.529 1.527 1.465 125.39 117.51 120.72 109.94 111.72 112.97 121.71 ** * ** 169 PRO 375 1.336 1.214 1.540 1.531 1.470 122.48 115.84 121.22 110.42 111.90 102.99 122.94 170 GLY 376 1.316 1.227 1.517 - 1.451 121.86 116.39 120.59 - 112.84 - 123.01 171 SER 377 1.309 1.252 1.545 1.538 1.431 121.75 117.98 119.97 113.12 108.92 110.06 122.02 * * * +* +* 172 PRO 378 1.356 1.226 1.536 1.540 1.476 123.06 117.10 120.21 110.96 114.87 104.37 122.67 * * * 173 GLU 379 1.308 1.231 1.518 1.515 1.467 122.75 116.53 120.66 111.73 111.82 110.11 122.81 * * 174 GLU 380 1.321 1.217 1.524 1.527 1.424 121.47 116.40 120.47 111.73 107.29 109.69 123.08 +* * +* 175 ALA 381 1.354 1.229 1.525 1.509 1.454 121.89 115.72 120.88 109.97 110.21 110.04 123.39 +* +* 176 ALA 382 1.328 1.210 1.510 1.503 1.448 123.16 116.13 120.62 110.08 111.08 110.01 123.25 * * 177 ALA 383 1.301 1.228 1.530 1.517 1.450 122.48 117.04 120.30 110.97 111.50 110.66 122.66 ** ** 178 LEU 384 1.334 1.239 1.527 1.550 1.467 121.14 114.35 122.07 106.66 108.12 111.41 123.55 * +* * +* 179 VAL 385 1.318 1.229 1.519 1.540 1.447 123.26 116.10 120.54 111.69 112.97 112.74 123.32 * * Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 180 ASP 386 1.321 1.221 1.528 1.540 1.472 123.52 116.33 120.55 110.95 111.05 110.38 123.08 * * 181 GLY 387 1.324 1.227 1.531 - 1.450 120.99 116.53 120.67 - 112.27 - 122.79 182 LEU 388 1.327 1.232 1.522 1.527 1.480 123.24 116.17 121.20 109.27 111.91 110.04 122.63 * * 183 ARG 389 1.316 1.224 1.521 1.526 1.450 121.05 116.49 120.75 110.04 110.66 111.50 122.75 184 ARG 390 1.321 1.238 1.507 1.524 1.452 121.34 115.41 120.16 108.24 108.96 112.07 124.35 185 GLU 391 1.329 1.236 1.546 1.532 1.458 124.15 117.27 120.58 112.62 110.41 110.38 122.14 * * * * 186 PRO 392 1.361 1.236 1.523 1.540 1.480 123.54 115.98 121.04 110.26 113.07 104.02 122.98 * * 187 GLY 393 1.306 1.235 1.507 - 1.444 121.25 115.62 121.09 - 111.74 - 123.28 +* +* 188 GLY 394 1.302 - 1.496 - 1.425 122.15 - - - 109.57 - - +* * +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** ** +* +* +** ** ** +** +* **** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 1.274 1.354 1.320 .014 +*** +* C-N (Pro) 1.341 .016 18 1.329 1.385 1.350 .012 +** C-O C-O 1.231 .020 187 1.188 1.252 1.229 .010 ** * CA-C CH1E-C (except Gly) 1.525 .021 170 1.485 1.556 1.524 .013 +* * CH2G*-C (Gly) 1.516 .018 18 1.494 1.535 1.513 .011 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.503 1.535 1.518 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.527 1.584 1.554 .017 +* CH1E-CH2E (the rest) 1.530 .020 138 1.493 1.566 1.532 .013 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.403 1.480 1.452 .014 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.417 1.461 1.444 .010 ** N-CH1E (Pro) 1.466 .015 18 1.450 1.488 1.469 .011 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 16 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 152 114.03 118.95 116.24 .96 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.62 119.21 117.02 1.19 * CH1E-C-N (Pro) 116.9 1.5 18 113.63 118.17 116.35 1.13 ** O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.96 124.57 122.99 .66 * O-C-N (Pro) 122.0 1.4 18 122.22 124.37 122.93 .51 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.48 125.51 122.20 1.36 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.56 122.15 121.14 .65 C-N-CH1E (Pro) 122.6 5.0 18 121.49 125.87 122.86 1.12 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.28 122.07 120.70 .54 CH2G*-C-O (Gly) 120.8 2.1 17 119.23 121.12 120.38 .50 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.97 111.39 110.62 .37 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.33 111.69 109.72 1.55 * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.66 115.77 110.72 1.63 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.90 114.68 110.60 1.58 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.57 113.23 111.67 1.07 * N-CH1E-C (Pro) 111.8 2.5 18 109.15 115.49 112.62 1.75 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.70 111.11 110.53 .33 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.25 113.84 112.42 1.08 * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.64 104.81 103.71 .58 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 105.24 117.51 110.61 1.85 *** **** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_1 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] 10 6.6% 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 93.4 83.8 10.0 1.0 Inside b. Omega angle st dev 186 2.9 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 126 .8 .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 20 10.2 18.1 6.5 -1.2 BETTER b. Chi-1 trans st dev 44 9.3 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 68 11.4 17.5 4.9 -1.3 BETTER d. Chi-1 pooled st dev 132 11.1 18.2 4.8 -1.5 BETTER e. Chi-2 trans st dev 63 8.1 20.4 5.0 -2.5 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 93.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 12.1 2 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .85 2 Residue-by-residue listing for refined_1 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .07 Chi1-chi2 distribution -.02 Chi1 only -.20 Chi3 & chi4 .32 Omega .14 ------ .10 ===== Main-chain covalent forces:- Main-chain bond lengths .29 Main-chain bond angles .39 ------ .35 ===== OVERALL AVERAGE .19 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.