Residue-by-residue listing for refined_12 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 - - - - - - - - - - - 179.5 - - - 2 SER 2 B - - -57.6 - - - - - - - 179.8 - 34.6 - 3 ASP 3 B - - -69.7 - - - - - - - 177.2 - 33.8 - 4 PRO 4 - - - - - -66.3 - - - - - 178.8 - 38.8 - * * 5 GLY 5 h - - - - - - - - - - - 181.1 - - - 6 PRO 6 H - - - - - -72.6 -72.6 -22.4 - - - 182.0 - 38.9 - +* * +* 7 GLU 7 H A - - -51.3 181.1 - -70.3 -43.8 - - - 177.4 - 34.6 - * * 8 ALA 8 H A - - - - - -67.1 -39.6 - - - 178.2 - 34.2 - 9 ALA 9 H A - - - - - -60.9 -42.3 - - - 179.0 -1.6 34.3 - 10 ARG 10 H A - 203.5 - - - -58.5 -40.8 - - - 180.1 -2.4 37.0 - * * 11 LEU 11 H A - - -55.0 181.6 - -66.1 -52.5 - - - 181.6 -1.5 35.1 - * * 12 ARG 12 H A - - -61.7 175.6 - -57.6 -40.1 - - - 178.0 -2.8 34.8 - * * 13 PHE 13 H A - 173.2 - - - -59.0 -43.2 - - - 178.5 -2.8 34.0 - * * 14 ARG 14 H A - - -71.8 187.5 - -82.9 -26.5 - - - 179.4 -1.5 31.7 - * * * 15 CYS 15 H A - - -60.2 - - -74.1 -19.1 - - - 176.5 -2.4 33.1 - +* +* 16 PHE 16 h B - 179.9 - - - - - - - - 179.8 -1.3 35.0 - * * 17 HIS 17 B 72.1 - - - - - - - - - 174.7 - 34.7 - Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 18 TYR 18 B - 166.6 - - - - - - - - 181.0 -1.3 31.9 - * * 19 GLU 19 t B 50.3 - - 181.6 - - - - - - 180.6 -.7 32.5 - +* +* 20 GLU 20 T A - - -59.9 175.1 - - - - - - 179.3 -.6 35.1 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.5 - 33.6 - 22 THR 22 T A - 192.6 - - - - - - - - 181.5 -1.2 33.6 - * * 23 GLY 23 h - - - - - - - - - - - 184.3 -1.2 - - * * 24 PRO 24 H - - - - - -75.3 -75.3 -29.6 - - - 184.9 - 38.4 - * * 25 GLN 25 H A - 206.4 - - - -64.5 -44.5 - - - 179.0 - 36.3 - * * 26 GLU 26 H A - 180.9 - 173.8 - -75.3 -36.1 - - - 178.4 - 32.6 - 27 ALA 27 H A - - - - - -62.2 -37.0 - - - 175.9 -1.7 33.6 - 28 LEU 28 H A - - -71.6 179.1 - -60.2 -43.8 - - - 180.6 -2.5 34.2 - 29 ALA 29 H A - - - - - -59.2 -36.0 - - - 179.9 -1.2 33.8 - * * 30 GLN 30 H A - - -46.7 - - -69.1 -52.0 - - - 178.5 -1.5 35.8 - * * * 31 LEU 31 H A - - -71.6 168.7 - -59.2 -38.9 - - - 181.9 -2.7 34.8 - 32 ARG 32 H A - 192.8 - 176.9 - -62.0 -45.9 - - - 179.9 -3.3 35.2 - +* +* 33 GLU 33 H A 69.3 - - 178.3 - -75.8 -37.9 - - - 177.7 -1.9 31.4 - 34 LEU 34 H A - - -63.3 178.5 - -59.7 -43.2 - - - 177.0 -2.9 33.6 - * * 35 CYS 35 H A - 185.0 - - - -62.8 -41.6 - - - 178.7 -3.2 35.3 - +* +* 36 ARG 36 H A - 172.1 - - - -68.2 -29.3 - - - 176.2 -1.9 29.0 - * * 37 GLN 37 H A - - -48.6 - - -69.0 -25.6 - - - 183.2 -2.0 36.1 - * * * 38 TRP 38 H A - 164.6 - - - -85.8 -56.9 - - - 180.0 -1.0 32.7 - * +* +* * +* 39 LEU 39 H A - - -52.3 - - -82.6 -38.2 - - - 181.3 -2.9 31.2 - * * * 40 ARG 40 h l - - -60.3 182.4 - - - - - - 181.2 -.9 31.3 - +* +* 41 PRO 41 T - - - - - -62.7 - - - - - 179.2 - 38.6 - * * 42 GLU 42 T A - 181.8 - 179.4 - - - - - - 181.9 - 34.1 - 43 VAL 43 T A - - -60.6 - - - - - - - 178.1 -1.1 32.2 - * * 44 ARG 44 t B - - -70.4 179.7 - - - - - - 182.5 -3.5 32.9 - +* +* 45 SER 45 h B - - -58.4 - - - - - - - 183.7 - 33.7 - 46 LYS 46 H A 62.9 - - - - -50.6 -37.7 - - - 179.9 - 32.6 - * * 47 GLU 47 H A - - -46.4 - - -53.6 -50.1 - - - 182.1 - 35.9 - * * 48 GLN 48 H A - - -57.4 - - -65.3 -35.0 - - - 181.3 -.8 35.3 - +* +* 49 MET 49 H A - - -54.9 182.2 - -67.6 -36.1 - - - 173.6 -1.4 32.0 - * * Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 50 LEU 50 H A - - -67.0 174.3 - -54.4 -52.4 - - - 182.9 -2.0 36.2 - * * 51 GLU 51 H A - - -55.4 - - -55.6 -54.2 - - - 182.5 -1.5 35.5 - * * 52 LEU 52 H A - - -60.4 179.0 - -58.6 -41.8 - - - 181.6 -2.4 34.3 - 53 LEU 53 H A - 181.6 - - - -73.8 -30.3 - - - 173.9 -2.2 31.7 - * * 54 VAL 54 H A - 176.8 - - - -63.3 -41.7 - - - 178.1 -2.2 33.4 - 55 LEU 55 H A - 180.4 - - - -55.7 -48.4 - - - 180.2 -2.1 35.4 - 56 GLU 56 H A - - -70.7 - - -52.5 -51.9 - - - 182.5 -1.8 34.7 - * * * 57 GLN 57 H A - 197.6 - - - -74.1 -40.3 - - - 181.6 -1.8 33.8 - 58 PHE 58 H A - 179.9 - - - -56.0 -46.9 - - - 179.6 -3.0 33.1 - * * 59 LEU 59 H A - - -65.1 185.0 - -61.8 -36.3 - - - 179.3 -2.9 30.5 - * * 60 GLY 60 H - - - - - - -81.1 -24.7 - - - 178.3 -1.2 - - * * * * 61 ALA 61 H A - - - - - -65.5 -27.7 - - - 176.9 -2.2 33.7 - * * 62 LEU 62 h B - - -64.1 170.3 - - - - - - 175.8 -1.1 36.9 - * * 63 PRO 63 h - - - - - -72.5 - - - - - 186.2 - 37.4 - * * 64 PRO 64 H - - - - - -45.3 -45.3 -42.9 - - - 183.3 - 37.6 - +* +* * +* 65 GLU 65 H A 61.2 - - - - -77.8 -44.6 - - - 178.4 - 29.7 - * * * 66 ILE 66 H A - - -56.8 180.2 - -64.0 -41.7 - - - 179.0 - 34.2 - 67 GLN 67 H A - 180.9 - 176.3 - -63.0 -46.1 - - - 180.6 -3.3 33.5 - +* +* 68 ALA 68 H A - - - - - -60.5 -39.2 - - - 179.1 -2.1 33.3 - 69 ARG 69 H A - - -70.3 - - -60.9 -53.9 - - - 180.7 -2.2 34.7 - * * 70 VAL 70 H A 62.8 - - - - -67.1 -31.6 - - - 179.5 -2.0 32.7 - 71 GLN 71 H A - 205.8 - - - -56.5 -27.1 - - - 177.6 -2.4 34.4 - * * * 72 GLY 72 h - - - - - - - - - - - 184.1 -1.2 - - * * 73 GLN 73 T a - - -65.5 - - - - - - - 190.7 -2.2 34.5 - +* +* 74 ARG 74 t l - - -75.3 - - - - - - - 179.0 -2.6 28.5 - +* +* 75 PRO 75 - - - - - -54.9 - - - - - 178.7 - 39.4 - +* +* 76 GLY 76 S - - - - - - - - - - - 176.8 - - - 77 SER 77 h B - - -58.2 - - - - - - - 184.1 - 34.0 - 78 PRO 78 H - - - - - -55.2 -55.2 -45.4 - - - 184.9 - 38.6 - * * 79 GLU 79 H A - - -40.1 - - -70.4 -31.9 - - - 177.1 - 33.3 - +* +* 80 GLU 80 H A - 185.2 - - - -65.4 -46.7 - - - 175.2 - 33.9 - 81 ALA 81 H A - - - - - -59.6 -45.4 - - - 178.7 -2.2 33.9 - 82 ALA 82 H A - - - - - -54.3 -38.0 - - - 179.4 -3.0 34.5 - * * 83 ALA 83 H A - - - - - -67.1 -51.0 - - - 179.9 -1.8 32.8 - * * Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 84 LEU 84 H A 63.7 - - 163.8 - -71.0 -35.3 - - - 180.1 -2.0 26.7 - ** ** 85 VAL 85 H A - - -61.0 - - -65.1 -32.2 - - - 175.5 -3.3 30.0 - +* * +* 86 ASP 86 H A - 184.4 - - - -64.0 -31.1 - - - 174.6 -1.6 33.2 - 87 GLY 87 H - - - - - - -77.8 -46.5 - - - 181.9 -1.0 - - * * * 88 LEU 88 H A - - -59.2 174.6 - -58.5 -33.2 - - - 179.0 -3.2 34.8 - +* +* 89 ARG 89 h A 59.6 - - 173.8 - - - - - - 182.5 -2.4 34.9 - 90 ARG 90 T a - 186.4 - 176.4 - - - - - - 172.6 -1.9 36.2 - * * 91 GLU 91 t ~l - 185.7 - 176.2 - - - - - - 176.1 -4.1 31.1 - ** +** +** 92 PRO 92 S - - - - - -57.4 - - - - - 181.9 - 38.6 - * * 93 GLY 93 - - - - - - - - - - - 178.9 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 178.2 - - - 96 SER 302 B - - -59.8 - - - - - - - 180.9 - 34.4 - 97 ASP 303 B - - -66.7 - - - - - - - 173.5 - 35.7 - * * 98 PRO 304 - - - - - -63.8 - - - - - 176.1 - 38.5 - * * 99 GLY 305 h - - - - - - - - - - - 182.9 - - - 100 PRO 306 H - - - - - -66.4 -66.4 -30.5 - - - 181.5 - 38.9 - * * 101 GLU 307 H A - - -55.9 175.3 - -69.2 -46.0 - - - 178.5 - 34.7 - 102 ALA 308 H A - - - - - -65.2 -36.3 - - - 177.2 - 34.1 - 103 ALA 309 H A - - - - - -63.4 -44.1 - - - 177.8 -2.0 33.1 - 104 ARG 310 H A - - -70.0 195.7 - -56.5 -40.6 - - - 180.6 -2.4 33.5 - 105 LEU 311 H A - - -57.4 177.7 - -60.2 -52.1 - - - 179.4 -1.7 34.6 - * * 106 ARG 312 H A - - -63.8 176.6 - -61.6 -43.9 - - - 180.1 -2.0 34.6 - 107 PHE 313 H A - 170.4 - - - -63.7 -42.5 - - - 178.1 -3.1 33.3 - * * 108 ARG 314 H A - - -74.7 186.6 - -79.1 -25.0 - - - 178.9 -3.0 31.8 - * * * * 109 CYS 315 h A - - -61.1 - - - - - - - 178.3 -1.9 33.0 - 110 PHE 316 B - 181.0 - - - - - - - - 179.4 - 35.0 - 111 HIS 317 B 69.7 - - - - - - - - - 176.4 - 34.4 - 112 TYR 318 B - 171.4 - - - - - - - - 182.3 -1.2 32.6 - * * 113 GLU 319 t B 47.4 - - 179.8 - - - - - - 182.4 -.7 32.3 - * +* +* 114 GLU 320 T A - - -62.1 173.9 - - - - - - 179.3 -.6 35.1 - +* +* 115 ALA 321 T A - - - - - - - - - - 182.1 - 33.8 - 116 THR 322 T A - 200.5 - - - - - - - - 181.8 -1.1 34.5 - * * * 117 GLY 323 h - - - - - - - - - - - 183.2 -1.0 - - * * 118 PRO 324 H - - - - - -62.9 -62.9 -33.5 - - - 179.6 - 38.3 - * * 119 GLN 325 H A - - -84.1 - - -64.0 -43.7 - - - 181.1 - 34.0 - * * 120 GLU 326 H A - 182.0 - 168.6 - -75.2 -33.8 - - - 175.5 - 33.2 - Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 121 ALA 327 H A - - - - - -63.2 -35.5 - - - 174.6 -2.5 33.9 - 122 LEU 328 H A - - -69.8 176.1 - -62.0 -43.0 - - - 179.5 -2.0 34.6 - 123 ALA 329 H A - - - - - -59.3 -27.8 - - - 178.0 -1.4 33.5 - * * 124 GLN 330 H A - - -49.0 - - -76.8 -52.4 - - - 181.0 -1.0 36.3 - * * * * 125 LEU 331 H A - - -69.0 170.3 - -62.6 -34.9 - - - 183.1 -2.7 34.7 - 126 ARG 332 H A - 186.1 - 175.9 - -61.8 -43.0 - - - 179.2 -3.5 33.8 - +* +* 127 GLU 333 H A 75.0 - - 180.4 - -75.6 -41.3 - - - 180.4 -.9 31.4 - +* +* 128 LEU 334 H A - - -59.1 179.4 - -58.0 -43.3 - - - 178.7 -2.2 34.1 - 129 CYS 335 H A - 185.5 - - - -64.6 -36.7 - - - 177.7 -3.3 34.3 - +* +* 130 ARG 336 H A - 173.3 - - - -72.6 -32.3 - - - 177.1 -1.4 31.8 - 131 GLN 337 H A - - -56.6 182.8 - -65.2 -27.6 - - - 178.9 -2.4 35.8 - * * 132 TRP 338 H a - 161.1 - - - -85.5 -63.6 - - - 182.1 -1.2 33.5 - * +* ** * ** 133 LEU 339 H A - - -63.7 165.8 - -64.4 -47.2 - - - 182.5 -3.3 34.5 - +* +* 134 ARG 340 h l - - -60.0 184.8 - - - - - - 177.1 -1.5 30.3 - * * 135 PRO 341 T - - - - - -52.4 - - - - - 180.1 - 40.0 - * +* +* 136 GLU 342 T A - 187.3 - 182.1 - - - - - - 181.4 - 35.1 - 137 VAL 343 T A - - -58.0 - - - - - - - 180.2 -1.7 32.1 - 138 ARG 344 t B - - -63.7 190.4 - - - - - - 177.1 -3.4 30.4 - +* +* 139 SER 345 h B - - -54.7 - - - - - - - 183.4 - 35.5 - 140 LYS 346 H A 60.7 - - - - -57.9 -33.5 - - - 181.1 - 32.3 - 141 GLU 347 H A - - -46.2 - - -57.5 -48.0 - - - 183.2 - 35.6 - * * 142 GLN 348 H A - - -66.9 - - -65.1 -27.6 - - - 178.3 -.6 32.6 - * +* +* 143 MET 349 H A - - -56.1 - - -64.2 -43.6 - - - 176.0 -1.0 34.7 - * * 144 LEU 350 H A - - -79.6 - - -55.9 -50.9 - - - 182.6 -1.3 34.3 - * * 145 GLU 351 H A - - -55.1 - - -54.6 -50.0 - - - 179.5 -1.6 35.3 - 146 LEU 352 H A - - -60.6 178.2 - -61.7 -44.1 - - - 183.0 -2.2 35.4 - 147 LEU 353 H A - 181.6 - - - -69.9 -30.7 - - - 174.2 -2.5 33.0 - 148 VAL 354 H A - 175.7 - - - -62.5 -45.1 - - - 178.4 -2.5 34.1 - 149 LEU 355 H A - 181.6 - - - -57.7 -46.5 - - - 180.4 -1.9 34.8 - 150 GLU 356 H A - - -65.5 - - -52.6 -50.2 - - - 180.6 -2.0 33.4 - * * 151 GLN 357 H A - 205.6 - - - -74.9 -43.7 - - - 183.2 -1.8 34.7 - * * 152 PHE 358 H A - 176.2 - - - -53.1 -42.9 - - - 179.9 -3.2 33.8 - * +* +* 153 LEU 359 H A - - -62.9 192.3 - -64.3 -34.2 - - - 177.7 -2.8 30.2 - * * * 154 GLY 360 H - - - - - - -81.5 -25.0 - - - 177.9 -.8 - - * * +* +* 155 ALA 361 H A - - - - - -68.9 -23.3 - - - 174.7 -2.2 33.5 - * * Residue-by-residue listing for refined_12 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 156 LEU 362 h B - - -66.9 171.2 - - - - - - 177.3 -1.1 36.5 - * * 157 PRO 363 h - - - - - -73.5 - - - - - 183.2 - 37.8 - * * 158 PRO 364 H - - - - - -36.1 -36.1 -51.7 - - - 182.5 - 37.9 - +** ** * * +** 159 GLU 365 H A 52.8 - - - - -67.3 -44.9 - - - 180.7 - 30.0 - * * 160 ILE 366 H A - - -56.0 182.1 - -68.4 -39.6 - - - 180.1 - 34.0 - 161 GLN 367 H A - 181.3 - 176.9 - -66.9 -35.3 - - - 178.9 -3.2 34.2 - +* +* 162 ALA 368 H A - - - - - -65.5 -33.6 - - - 181.2 -2.2 33.6 - 163 ARG 369 H A - - -61.3 - - -72.1 -52.9 - - - 183.6 -1.3 35.8 - * * 164 VAL 370 H A 57.2 - - - - -56.6 -39.3 - - - 178.0 -2.0 33.3 - 165 GLN 371 H A - - -94.2 - - -58.9 -28.4 - - - 179.1 -1.5 30.5 - +* +* 166 GLY 372 H - - - - - - -64.4 -40.2 - - - 180.4 -1.4 - - 167 GLN 373 H A - - -68.5 - - -94.5 -38.9 - - - 183.2 -.7 34.1 - ** +* ** 168 ARG 374 h l - 196.4 - - - - - - - - 184.8 -3.5 32.4 - +* +* 169 PRO 375 - - - - - -59.9 - - - - - 179.4 - 39.0 - * * 170 GLY 376 - - - - - - - - - - - 176.7 - - - 171 SER 377 h B - - -53.9 - - - - - - - 184.2 - 34.8 - 172 PRO 378 H - - - - - -58.9 -58.9 -45.0 - - - 183.5 - 37.8 - * * 173 GLU 379 H A - - -59.7 175.2 - -74.4 -29.5 - - - 175.6 - 31.2 - 174 GLU 380 H A - 186.5 - - - -64.3 -46.5 - - - 175.5 - 35.8 - 175 ALA 381 H A - - - - - -58.8 -43.5 - - - 179.4 -2.5 34.3 - 176 ALA 382 H A - - - - - -56.4 -39.0 - - - 179.1 -2.4 33.7 - 177 ALA 383 H A - - - - - -74.1 -29.9 - - - 180.0 -1.8 32.9 - 178 LEU 384 H A - - -44.3 181.4 - -72.7 -49.5 - - - 184.8 -1.5 37.5 - * * * 179 VAL 385 H A - - -57.7 - - -69.6 -29.7 - - - 176.6 -3.2 30.0 - * * * 180 ASP 386 H A - 182.5 - - - -58.1 -33.8 - - - 177.2 -1.5 33.0 - 181 GLY 387 H - - - - - - -75.5 -17.8 - - - 181.1 -.8 - - +* +* +* 182 LEU 388 H A - - -58.8 175.8 - -88.5 -29.0 - - - 173.4 -.7 34.3 - +* * +* +* 183 ARG 389 H A 55.2 - - 180.7 - -79.2 -23.5 - - - 178.6 -1.9 33.7 - * * * 184 ARG 390 h A - 186.8 - 185.2 - - - - - - 183.1 -1.2 36.2 - * * 185 GLU 391 t b - 177.3 - 183.7 - - - - - - 175.6 -.6 35.5 - +* +* 186 PRO 392 S - - - - - -93.3 - - - - - 179.0 - 38.6 - ** * ** 187 GLY 393 - - - - - - - - - - - 180.2 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +* +** ** ** +* +** ** +** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 Page 7 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.3 183.5 -61.5 178.5 -62.8 -65.3 -39.4 - - - 179.7 -2.0 34.2 Standard deviations: 8.0 10.6 9.0 6.0 12.6 9.0 8.8 - - - 2.8 .8 2.2 Numbers of values: 15 44 73 56 18 124 124 0 0 0 186 125 170 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_12 Page 8 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.237 1.503 - 1.461 - 116.88 120.16 - 110.46 - 122.94 2 SER 2 1.308 1.235 1.518 1.526 1.436 121.73 116.25 120.88 110.56 109.60 109.94 122.85 +* * +* 3 ASP 3 1.302 1.236 1.499 1.537 1.444 121.42 117.53 120.17 109.80 110.49 111.76 122.30 +* * +* 4 PRO 4 1.351 1.226 1.529 1.540 1.472 122.52 115.28 121.39 110.37 110.78 103.59 123.32 * * 5 GLY 5 1.320 1.241 1.512 - 1.430 122.00 118.17 120.17 - 111.80 - 121.66 * * 6 PRO 6 1.343 1.227 1.525 1.540 1.462 122.62 116.10 120.95 109.87 111.76 103.90 122.93 7 GLU 7 1.322 1.237 1.523 1.528 1.448 121.95 115.48 121.01 110.62 109.21 110.01 123.48 8 ALA 8 1.327 1.228 1.516 1.522 1.450 122.77 115.86 120.85 110.32 109.83 110.59 123.27 9 ALA 9 1.327 1.229 1.527 1.515 1.455 122.37 115.65 120.83 110.31 110.30 110.14 123.49 10 ARG 10 1.335 1.235 1.544 1.546 1.438 124.26 115.83 121.20 110.77 108.31 106.67 122.97 * * * ** ** 11 LEU 11 1.333 1.226 1.516 1.538 1.457 122.07 115.52 120.68 108.84 109.83 110.96 123.78 12 ARG 12 1.323 1.239 1.521 1.519 1.473 123.79 115.13 120.91 109.71 111.61 109.57 123.96 * * 13 PHE 13 1.314 1.224 1.531 1.533 1.447 123.96 117.18 120.43 112.28 111.46 108.57 122.38 * * * * * 14 ARG 14 1.324 1.232 1.514 1.512 1.460 120.48 117.13 120.12 109.77 113.41 113.20 122.75 +* +* Residue-by-residue listing for refined_12 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 1.315 1.240 1.521 1.526 1.454 121.09 115.65 120.75 111.14 110.81 111.10 123.60 16 PHE 16 1.332 1.248 1.517 1.538 1.445 122.72 116.07 120.84 109.74 109.49 110.35 123.09 17 HIS 17 1.302 1.229 1.502 1.568 1.436 120.97 118.04 119.76 109.84 107.93 111.59 122.18 +* * +* * * +* 18 TYR 18 1.299 1.234 1.499 1.527 1.426 118.34 114.72 121.43 111.90 109.24 112.87 123.85 ** * +* +* * ** 19 GLU 19 1.286 1.241 1.510 1.536 1.409 122.53 115.15 121.49 113.34 110.77 110.17 123.35 *** +** +* *** 20 GLU 20 1.319 1.221 1.525 1.520 1.456 122.97 115.79 120.70 109.21 110.55 110.05 123.51 21 ALA 21 1.322 1.235 1.537 1.521 1.449 122.98 117.54 120.29 110.55 112.29 110.29 122.17 22 THR 22 1.324 1.242 1.531 1.556 1.445 119.69 115.93 121.27 110.17 110.80 111.70 122.77 * * 23 GLY 23 1.312 1.234 1.514 - 1.430 120.49 118.62 120.32 - 110.74 - 121.05 * * * * * 24 PRO 24 1.321 1.219 1.506 1.510 1.449 121.95 116.05 120.62 110.86 112.60 103.17 123.33 * * * 25 GLN 25 1.319 1.238 1.542 1.509 1.406 122.58 116.25 120.92 109.77 109.38 108.24 122.82 * +** * +** 26 GLU 26 1.338 1.228 1.516 1.539 1.446 121.14 116.22 120.72 111.31 110.62 111.89 123.04 27 ALA 27 1.321 1.235 1.531 1.520 1.459 121.74 116.40 120.63 110.91 110.72 110.48 122.96 28 LEU 28 1.334 1.204 1.489 1.519 1.460 121.76 116.39 120.04 108.15 111.12 112.38 123.57 * +* * * +* 29 ALA 29 1.320 1.234 1.525 1.522 1.452 121.85 115.61 120.87 110.99 110.47 110.32 123.47 30 GLN 30 1.330 1.222 1.523 1.536 1.454 122.07 115.49 121.22 108.69 108.63 110.27 123.24 31 LEU 31 1.328 1.206 1.503 1.525 1.463 123.19 115.71 120.69 109.50 111.60 110.05 123.60 * * * 32 ARG 32 1.298 1.230 1.503 1.508 1.440 123.39 116.82 120.50 110.65 110.38 108.71 122.66 ** * * * ** 33 GLU 33 1.319 1.198 1.515 1.521 1.423 119.02 117.67 119.37 111.58 110.45 113.25 122.95 +* +* * +* +* 34 LEU 34 1.348 1.226 1.516 1.541 1.475 121.89 115.34 121.03 109.98 110.12 111.81 123.60 * * 35 CYS 35 1.317 1.228 1.531 1.543 1.444 123.11 115.79 121.63 111.03 108.67 108.86 122.54 36 ARG 36 1.318 1.211 1.535 1.550 1.422 122.35 117.68 119.79 116.15 112.75 110.95 122.52 +* *** *** 37 GLN 37 1.336 1.236 1.542 1.547 1.477 121.64 114.51 121.46 106.41 108.42 111.97 124.03 * +* +* 38 TRP 38 1.320 1.235 1.548 1.546 1.450 125.21 118.99 119.78 114.00 113.57 107.79 121.23 * +* * ** +* * ** 39 LEU 39 1.333 1.219 1.517 1.559 1.472 118.17 115.79 120.37 109.80 110.64 115.29 123.83 * +* +** +** 40 ARG 40 1.330 1.226 1.541 1.540 1.468 124.19 117.67 120.54 111.06 113.20 112.59 121.78 * * * 41 PRO 41 1.357 1.228 1.530 1.534 1.483 123.34 116.25 120.97 109.74 113.32 103.81 122.78 * * 42 GLU 42 1.311 1.242 1.527 1.528 1.441 121.66 116.35 120.93 110.61 110.46 110.39 122.72 * * 43 VAL 43 1.323 1.232 1.522 1.560 1.454 120.96 116.72 120.36 110.37 111.82 113.00 122.92 44 ARG 44 1.320 1.223 1.504 1.528 1.448 122.02 115.44 121.24 110.04 110.91 112.49 123.31 * * 45 SER 45 1.289 1.241 1.542 1.515 1.432 122.53 116.15 120.36 111.66 111.20 109.42 123.48 +** * +** 46 LYS 46 1.343 1.233 1.534 1.549 1.480 123.86 116.23 120.21 109.41 113.80 112.31 123.56 * * * * * Residue-by-residue listing for refined_12 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 47 GLU 47 1.327 1.226 1.514 1.554 1.492 122.85 113.97 122.02 105.80 109.57 112.78 123.99 * +* * ** * ** 48 GLN 48 1.308 1.230 1.516 1.525 1.454 123.39 116.10 120.97 109.30 111.04 109.69 122.92 +* +* 49 MET 49 1.322 1.232 1.512 1.508 1.445 121.20 116.40 120.02 112.04 111.57 111.32 123.57 * * * 50 LEU 50 1.348 1.227 1.522 1.544 1.464 121.82 115.01 120.88 106.69 108.97 111.68 124.07 * +* +* 51 GLU 51 1.333 1.234 1.523 1.529 1.463 123.76 115.92 120.86 108.41 111.46 110.12 123.22 * * 52 LEU 52 1.324 1.228 1.522 1.528 1.447 122.45 116.17 120.84 110.44 111.63 109.88 122.96 53 LEU 53 1.309 1.239 1.556 1.515 1.418 121.89 117.54 120.53 115.95 112.46 107.40 121.91 * * ** *** +* *** 54 VAL 54 1.334 1.236 1.540 1.568 1.471 120.51 115.52 120.79 109.75 109.17 112.80 123.66 * * 55 LEU 55 1.339 1.238 1.523 1.562 1.476 123.97 114.69 121.04 111.28 109.62 108.17 124.26 +* * * +* 56 GLU 56 1.316 1.240 1.527 1.526 1.460 123.74 117.03 120.45 109.57 112.95 109.66 122.51 * * 57 GLN 57 1.316 1.222 1.523 1.546 1.452 120.09 116.40 120.32 111.69 109.03 110.36 123.24 58 PHE 58 1.338 1.233 1.526 1.540 1.462 121.99 116.69 120.30 110.50 111.55 111.53 123.00 59 LEU 59 1.329 1.219 1.519 1.535 1.458 120.81 117.45 120.03 112.40 113.29 112.36 122.49 * * * 60 GLY 60 1.316 1.236 1.517 - 1.456 119.59 116.29 120.59 - 112.86 - 123.12 61 ALA 61 1.332 1.235 1.525 1.529 1.463 122.29 115.49 120.94 110.54 110.41 110.81 123.57 62 LEU 62 1.322 1.238 1.540 1.527 1.451 123.67 118.21 120.30 108.45 110.35 108.31 121.49 * * * * 63 PRO 63 1.342 1.243 1.541 1.535 1.445 121.75 118.00 119.62 111.39 109.82 104.91 122.39 * +* +* 64 PRO 64 1.354 1.227 1.539 1.523 1.477 123.75 118.36 119.74 110.63 115.84 103.58 121.90 +* +* 65 GLU 65 1.322 1.237 1.522 1.558 1.464 120.08 117.22 120.13 112.24 112.44 114.08 122.63 * * ** ** 66 ILE 66 1.330 1.245 1.526 1.544 1.451 120.76 115.55 121.03 109.54 109.57 111.59 123.39 67 GLN 67 1.331 1.208 1.514 1.524 1.439 121.82 116.81 120.16 110.33 110.49 111.55 123.01 * * * 68 ALA 68 1.326 1.228 1.526 1.515 1.459 121.93 116.78 120.30 110.14 111.92 111.13 122.92 69 ARG 69 1.326 1.227 1.536 1.521 1.464 121.43 116.25 120.88 108.49 111.43 111.04 122.85 70 VAL 70 1.328 1.245 1.527 1.561 1.470 122.21 114.53 121.55 110.76 110.45 112.33 123.91 71 GLN 71 1.318 1.198 1.526 1.517 1.448 124.97 117.45 120.52 109.88 110.93 110.29 121.95 +* +* +* 72 GLY 72 1.306 1.236 1.538 - 1.443 119.59 117.24 120.32 - 112.93 - 122.43 +* * +* 73 GLN 73 1.335 1.230 1.529 1.552 1.460 121.44 115.84 120.63 107.59 112.74 112.12 123.53 * * * 74 ARG 74 1.336 1.226 1.512 1.545 1.481 123.44 116.96 120.76 110.38 112.66 117.13 122.26 * +*** +*** 75 PRO 75 1.343 1.222 1.528 1.527 1.476 123.37 115.88 121.09 109.63 112.83 102.83 123.03 76 GLY 76 1.317 1.229 1.508 - 1.458 120.96 115.64 121.34 - 111.88 - 123.00 77 SER 77 1.307 1.246 1.534 1.529 1.433 123.18 117.55 119.97 111.60 108.15 110.23 122.41 +* * * +* 78 PRO 78 1.346 1.230 1.531 1.531 1.469 123.29 117.50 119.96 109.11 114.93 104.19 122.54 * * * 79 GLU 79 1.325 1.232 1.504 1.537 1.475 121.14 115.40 121.19 109.24 110.34 112.86 123.41 * * Residue-by-residue listing for refined_12 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 1.310 1.224 1.531 1.535 1.431 122.28 116.75 120.29 112.46 108.30 109.57 122.92 * * * * * 81 ALA 81 1.354 1.222 1.517 1.515 1.461 121.72 116.10 120.23 110.32 110.36 110.67 123.65 +* +* 82 ALA 82 1.335 1.228 1.522 1.522 1.463 123.29 115.55 121.30 109.95 110.94 110.12 123.15 83 ALA 83 1.288 1.234 1.526 1.514 1.430 122.21 118.69 119.41 111.34 111.38 111.05 121.85 +** * * +** 84 LEU 84 1.349 1.209 1.501 1.557 1.454 117.27 118.01 119.38 110.99 112.94 118.78 122.59 * * * * ** *4.9* *4.9* 85 VAL 85 1.335 1.228 1.516 1.547 1.467 120.58 116.77 120.23 110.86 111.98 115.16 122.99 ** ** 86 ASP 86 1.332 1.232 1.526 1.528 1.465 121.20 115.19 121.91 110.24 109.01 112.25 122.90 * * 87 GLY 87 1.309 1.192 1.520 - 1.426 121.03 116.57 120.30 - 110.67 - 123.08 * +* +* +* 88 LEU 88 1.331 1.242 1.535 1.530 1.492 124.61 116.40 120.80 109.01 112.87 109.83 122.79 +* +* +* 89 ARG 89 1.328 1.232 1.531 1.532 1.477 122.19 115.76 121.03 108.68 110.98 110.75 123.21 90 ARG 90 1.298 1.229 1.537 1.521 1.435 123.24 114.37 121.10 112.32 107.56 106.16 124.50 ** * * * +** +** 91 GLU 91 1.323 1.240 1.536 1.527 1.458 127.00 116.46 121.43 112.44 114.76 110.76 122.10 +** * * +** 92 PRO 92 1.345 1.234 1.538 1.533 1.464 123.24 117.10 120.56 110.09 112.24 103.73 122.32 93 GLY 93 1.330 1.244 1.509 - 1.443 119.51 115.89 120.50 - 113.42 - 123.62 94 GLY 94 1.319 1.239 1.512 - 1.456 122.28 - 120.13 - 113.05 - - 95 GLY 301 - 1.235 1.508 - 1.450 - 115.55 121.26 - 111.17 - 123.19 96 SER 302 1.304 1.235 1.514 1.531 1.438 122.84 116.43 120.33 110.71 108.97 110.38 123.21 +* * +* 97 ASP 303 1.305 1.229 1.498 1.543 1.448 122.52 118.18 119.85 108.15 109.26 111.15 121.97 +* * * +* 98 PRO 304 1.345 1.240 1.543 1.539 1.466 122.08 115.35 121.44 111.08 110.33 103.27 123.21 * * 99 GLY 305 1.321 1.237 1.515 - 1.437 121.84 117.59 120.35 - 113.10 - 122.05 100 PRO 306 1.347 1.227 1.519 1.536 1.467 123.01 116.28 120.78 109.41 112.73 104.00 122.94 101 GLU 307 1.317 1.237 1.517 1.522 1.447 121.69 115.46 121.11 110.36 109.10 110.13 123.40 102 ALA 308 1.314 1.240 1.524 1.511 1.447 122.14 115.73 120.85 110.70 110.09 110.12 123.41 * * 103 ALA 309 1.331 1.223 1.521 1.519 1.448 121.88 117.06 120.21 110.99 110.56 111.24 122.71 104 ARG 310 1.349 1.225 1.511 1.514 1.466 121.32 116.13 120.58 107.58 112.01 113.35 123.29 * * +* +* 105 LEU 311 1.324 1.226 1.511 1.527 1.455 122.07 115.50 120.77 110.02 109.75 110.35 123.70 106 ARG 312 1.317 1.234 1.529 1.524 1.468 122.71 114.96 121.36 110.06 111.10 109.79 123.66 107 PHE 313 1.307 1.217 1.543 1.533 1.451 124.33 117.88 119.98 113.14 112.73 108.12 122.13 +* * +* * +* 108 ARG 314 1.328 1.237 1.519 1.523 1.472 120.59 117.16 120.41 109.50 113.20 113.45 122.43 +* +* 109 CYS 315 1.320 1.240 1.515 1.530 1.459 120.71 115.88 120.67 110.62 110.73 111.80 123.45 110 PHE 316 1.329 1.233 1.514 1.540 1.436 122.12 115.99 121.03 110.41 108.82 109.96 122.97 * * 111 HIS 317 1.293 1.245 1.503 1.561 1.437 120.96 117.62 119.69 110.28 107.53 111.64 122.67 +** * +* * * +** 112 TYR 318 1.294 1.226 1.512 1.529 1.421 119.24 114.86 121.67 112.56 108.79 111.36 123.47 ** +* * * ** 113 GLU 319 1.287 1.236 1.507 1.540 1.417 122.76 114.71 121.79 113.50 110.58 110.38 123.50 +** ** +* +** Residue-by-residue listing for refined_12 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 1.304 1.231 1.520 1.511 1.448 123.69 115.85 120.76 110.22 111.40 108.88 123.38 +* * +* 115 ALA 321 1.317 1.224 1.522 1.518 1.444 122.50 117.14 120.32 110.54 111.27 110.54 122.51 116 THR 322 1.329 1.224 1.552 1.580 1.449 120.15 116.23 121.23 111.00 109.20 110.24 122.46 * * * 117 GLY 323 1.331 1.229 1.521 - 1.447 121.20 119.28 119.91 - 111.38 - 120.81 * * * 118 PRO 324 1.344 1.225 1.526 1.509 1.469 122.25 117.42 119.94 110.27 113.86 103.41 122.63 * * 119 GLN 325 1.343 1.228 1.521 1.552 1.471 120.73 114.93 121.74 108.76 109.23 112.80 123.31 * * * 120 GLU 326 1.309 1.227 1.526 1.509 1.441 122.31 116.45 120.76 112.75 111.09 109.01 122.79 * * * * 121 ALA 327 1.322 1.232 1.528 1.520 1.461 121.98 116.13 121.01 110.66 109.84 110.49 122.86 122 LEU 328 1.324 1.203 1.483 1.505 1.457 121.90 116.44 120.13 107.95 110.79 111.97 123.43 * +* * * +* 123 ALA 329 1.319 1.235 1.530 1.519 1.452 121.74 115.95 120.83 111.02 110.62 110.58 123.22 124 GLN 330 1.330 1.227 1.538 1.543 1.450 121.86 115.43 121.33 108.29 108.21 110.05 123.16 * * 125 LEU 331 1.336 1.213 1.503 1.527 1.474 123.33 116.12 120.46 108.60 112.43 110.77 123.42 * * 126 ARG 332 1.301 1.238 1.508 1.518 1.441 122.79 116.99 120.28 110.95 111.09 110.25 122.71 +* +* 127 GLU 333 1.327 1.199 1.517 1.545 1.428 118.40 117.17 119.56 111.86 109.01 113.78 123.17 +* +* +* +* +* 128 LEU 334 1.352 1.230 1.529 1.541 1.477 122.51 115.81 121.09 109.56 110.82 111.13 123.09 +* * +* 129 CYS 335 1.319 1.227 1.537 1.542 1.447 122.70 116.46 121.11 111.31 109.47 109.73 122.40 130 ARG 336 1.332 1.214 1.536 1.556 1.432 122.14 117.11 120.02 114.29 111.18 109.87 122.86 * * ** ** 131 GLN 337 1.334 1.233 1.513 1.508 1.472 122.72 114.03 121.85 108.27 109.77 110.05 124.12 * * * 132 TRP 338 1.305 1.232 1.545 1.540 1.429 124.71 117.16 119.97 113.19 112.53 108.05 122.87 +* +* +* +* * +* 133 LEU 339 1.326 1.230 1.521 1.537 1.471 122.27 115.57 120.78 110.36 111.17 109.77 123.60 134 ARG 340 1.320 1.229 1.524 1.536 1.460 124.28 117.36 120.65 111.54 113.32 113.41 121.92 * +* +* 135 PRO 341 1.349 1.232 1.522 1.533 1.471 124.26 115.88 120.64 109.08 113.50 102.67 123.47 * * 136 GLU 342 1.319 1.235 1.535 1.526 1.443 122.93 116.59 121.01 110.56 110.12 108.94 122.38 137 VAL 343 1.329 1.231 1.526 1.563 1.451 120.43 117.82 120.09 110.24 112.39 113.12 122.09 138 ARG 344 1.327 1.240 1.485 1.526 1.442 119.08 113.78 122.13 109.97 113.48 114.88 124.09 +* * * +** +** 139 SER 345 1.287 1.242 1.518 1.510 1.403 123.27 115.81 120.77 111.11 108.74 108.33 123.43 +** +** * +** 140 LYS 346 1.313 1.216 1.521 1.539 1.451 122.74 115.98 120.58 110.82 112.94 111.81 123.42 * * 141 GLU 347 1.305 1.230 1.511 1.535 1.493 122.58 114.31 121.75 105.19 110.35 113.34 123.94 +* +* +** +* +** 142 GLN 348 1.309 1.230 1.510 1.525 1.461 123.24 116.22 120.55 111.28 112.67 110.88 123.23 * * 143 MET 349 1.311 1.232 1.512 1.513 1.455 121.96 115.32 120.81 110.08 109.25 110.13 123.86 * * 144 LEU 350 1.334 1.214 1.502 1.546 1.458 122.62 115.60 120.33 109.08 110.41 111.76 124.03 * * Residue-by-residue listing for refined_12 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 1.317 1.239 1.535 1.524 1.462 123.53 116.06 120.86 109.52 111.14 109.24 123.06 * * 146 LEU 352 1.327 1.228 1.521 1.530 1.451 122.48 115.38 121.34 109.33 110.63 109.75 123.25 147 LEU 353 1.309 1.239 1.544 1.517 1.435 122.76 116.71 120.62 114.01 112.34 107.73 122.67 * * ** +* ** 148 VAL 354 1.329 1.223 1.518 1.561 1.462 121.52 115.42 120.69 109.53 108.81 112.25 123.86 149 LEU 355 1.329 1.235 1.528 1.560 1.459 123.39 115.68 120.50 111.62 109.68 108.74 123.82 +* * +* 150 GLU 356 1.328 1.241 1.525 1.543 1.464 123.02 117.03 120.13 110.24 112.55 111.05 122.84 151 GLN 357 1.321 1.224 1.530 1.529 1.453 120.46 116.26 120.47 109.76 108.95 110.70 123.22 152 PHE 358 1.341 1.234 1.510 1.545 1.467 122.55 116.59 120.31 109.84 111.81 111.18 123.08 153 LEU 359 1.316 1.226 1.526 1.531 1.442 120.18 117.33 120.12 112.67 113.25 112.45 122.54 * * * 154 GLY 360 1.320 1.233 1.514 - 1.451 119.91 115.98 120.87 - 111.75 - 123.15 155 ALA 361 1.332 1.240 1.527 1.530 1.457 122.38 115.56 121.01 111.05 110.07 110.85 123.42 156 LEU 362 1.325 1.238 1.528 1.530 1.448 123.20 118.35 119.90 108.50 109.63 109.20 121.75 * * 157 PRO 363 1.339 1.242 1.533 1.534 1.445 121.65 117.56 119.54 110.79 109.94 104.93 122.90 * +* +* 158 PRO 364 1.358 1.229 1.537 1.513 1.473 124.66 118.14 119.41 110.80 115.76 103.01 122.42 * +* +* 159 GLU 365 1.334 1.230 1.515 1.550 1.466 120.29 117.06 120.25 110.97 112.98 114.71 122.67 ** ** 160 ILE 366 1.319 1.239 1.540 1.547 1.442 120.78 115.53 121.27 110.53 109.95 110.86 123.15 161 GLN 367 1.321 1.227 1.536 1.523 1.452 122.71 116.07 121.32 110.70 110.89 109.79 122.61 162 ALA 368 1.307 1.227 1.536 1.521 1.462 121.66 116.05 120.73 110.58 111.29 110.53 123.20 +* +* 163 ARG 369 1.327 1.228 1.538 1.523 1.468 122.66 116.06 120.86 107.87 111.31 110.00 123.08 * * 164 VAL 370 1.344 1.229 1.533 1.566 1.482 123.04 116.27 120.50 110.21 112.23 111.38 123.22 * * * 165 GLN 371 1.314 1.237 1.525 1.529 1.466 122.86 116.69 120.08 112.47 113.84 111.90 123.22 * * * 166 GLY 372 1.324 1.228 1.527 - 1.446 120.96 116.94 120.61 - 112.61 - 122.44 167 GLN 373 1.320 1.235 1.513 1.553 1.462 120.86 114.17 121.32 109.43 109.74 112.02 124.49 * * * 168 ARG 374 1.319 1.221 1.550 1.530 1.447 125.59 117.48 120.63 110.41 110.43 112.77 121.88 * ** * ** 169 PRO 375 1.345 1.219 1.529 1.535 1.492 123.69 116.03 120.96 109.75 114.25 102.99 122.98 +* +* 170 GLY 376 1.317 1.215 1.512 - 1.457 121.40 116.34 120.79 - 112.63 - 122.87 171 SER 377 1.306 1.251 1.531 1.516 1.439 121.90 117.77 119.89 110.37 108.22 109.96 122.33 +* * +* 172 PRO 378 1.345 1.229 1.523 1.538 1.468 123.07 116.73 120.59 110.28 113.61 104.59 122.63 * * 173 GLU 379 1.308 1.236 1.520 1.520 1.450 121.70 115.84 120.77 113.94 111.67 110.53 123.36 +* ** ** 174 GLU 380 1.331 1.230 1.530 1.540 1.426 122.85 115.67 120.80 111.12 106.61 108.53 123.48 +* +* * +* 175 ALA 381 1.357 1.219 1.519 1.511 1.452 122.59 116.37 120.25 109.77 110.86 110.48 123.36 +* +* 176 ALA 382 1.337 1.223 1.523 1.531 1.465 122.75 116.24 121.11 110.26 111.28 110.84 122.65 177 ALA 383 1.298 1.231 1.540 1.514 1.443 121.75 117.20 120.26 111.58 111.43 110.46 122.54 ** ** Residue-by-residue listing for refined_12 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 1.342 1.237 1.521 1.540 1.474 120.95 114.11 122.13 104.55 108.06 111.72 123.74 * +** * +** 179 VAL 385 1.324 1.227 1.503 1.540 1.441 123.58 116.45 120.56 112.15 112.69 113.64 122.96 * * * * * 180 ASP 386 1.313 1.217 1.532 1.511 1.456 121.31 116.57 121.02 110.42 110.95 111.56 122.35 * * 181 GLY 387 1.318 1.219 1.524 - 1.449 120.26 115.68 121.11 - 111.25 - 123.20 182 LEU 388 1.325 1.221 1.528 1.525 1.461 123.27 116.80 121.18 110.71 110.93 109.69 122.02 183 ARG 389 1.316 1.233 1.526 1.541 1.469 120.92 114.33 121.97 111.11 108.40 111.09 123.67 * * 184 ARG 390 1.319 1.229 1.550 1.545 1.447 123.93 115.47 121.44 110.36 108.17 108.16 123.09 * * * * * 185 GLU 391 1.330 1.236 1.530 1.526 1.467 124.25 117.75 120.36 109.08 112.28 109.08 121.88 * * 186 PRO 392 1.342 1.232 1.540 1.527 1.441 122.51 116.14 120.92 110.96 111.61 103.03 122.94 +* +* 187 GLY 393 1.326 1.230 1.510 - 1.443 121.40 116.27 120.39 - 111.88 - 123.33 188 GLY 394 1.315 - 1.502 - 1.434 121.43 - - - 110.45 - - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* +* +** +** * *** +* *4.9* * *4.9* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 1.286 1.357 1.322 .013 *** +* C-N (Pro) 1.341 .016 18 1.321 1.358 1.345 .008 * * C-O C-O 1.231 .020 187 1.192 1.251 1.230 .010 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.483 1.556 1.524 .013 +* * CH2G*-C (Gly) 1.516 .018 18 1.502 1.538 1.515 .009 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.511 1.531 1.520 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.540 1.580 1.558 .011 * CH1E-CH2E (the rest) 1.530 .020 138 1.505 1.568 1.532 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.403 1.493 1.453 .016 +** +* NH1-CH2G* (Gly) 1.451 .016 18 1.426 1.461 1.445 .010 +* N-CH1E (Pro) 1.466 .015 18 1.441 1.492 1.466 .013 +* +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 2.0 152 113.78 118.99 116.23 1.01 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.55 119.28 116.81 1.08 * CH1E-C-N (Pro) 116.9 1.5 18 115.28 118.36 116.67 .93 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.81 124.50 123.01 .65 * O-C-N (Pro) 122.0 1.4 18 121.90 123.47 122.81 .40 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.27 127.00 122.17 1.44 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.51 122.28 120.87 .86 C-N-CH1E (Pro) 122.6 5.0 18 121.65 124.66 122.95 .83 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.37 122.13 120.69 .58 CH2G*-C-O (Gly) 120.8 2.1 17 119.91 121.34 120.54 .40 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.77 111.58 110.63 .45 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 109.53 112.15 110.42 .70 * CH2E-CH1E-C (the rest) 110.1 1.9 138 104.55 116.15 110.38 1.78 +** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.61 114.76 110.72 1.55 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.45 113.42 111.89 .95 N-CH1E-C (Pro) 111.8 2.5 18 109.82 115.84 112.76 1.78 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 110.12 111.24 110.59 .32 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.24 115.16 112.34 1.27 ** N-CH1E-CH2E (Pro) 103.0 1.1 18 102.67 104.93 103.64 .66 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.16 118.78 110.83 1.95 +** *4.9* ------------------------------------------------------------------------------------------------------------- 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_12 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] 143 94.1% Residues in additional allowed regions [a,b,l,p] 8 5.3% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 94.1 83.8 10.0 1.0 BETTER b. Omega angle st dev 186 2.8 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.2 3.1 1.6 -.5 Inside e. H-bond energy st dev 125 .8 .8 .2 .0 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 15 8.0 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 44 10.6 19.0 5.3 -1.6 BETTER c. Chi-1 gauche plus st dev 73 9.0 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 132 10.3 18.2 4.8 -1.6 BETTER e. Chi-2 trans st dev 56 6.0 20.4 5.0 -2.9 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% 94.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .82 2 Residue-by-residue listing for refined_12 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .11 Chi1-chi2 distribution -.14 Chi1 only -.11 Chi3 & chi4 .32 Omega .19 ------ .11 ===== Main-chain covalent forces:- Main-chain bond lengths .30 Main-chain bond angles .37 ------ .34 ===== OVERALL AVERAGE .20 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.