Residue-by-residue listing for refined_3 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 - - - - - - - - - - - 179.4 - - - 2 SER 2 B - 183.9 - - - - - - - - 177.3 - 33.8 - 3 ASP 3 B - 173.7 - - - - - - - - 178.8 -.5 34.8 - ** ** 4 PRO 4 h - - - - - -53.7 - - - - - 181.0 - 39.2 - * +* +* 5 GLY 5 H - - - - - - 90.3 148.9 - - - 178.9 - - - *13.1**16.7* *16.7* 6 PRO 6 H - - - - - -52.1 -52.1 -29.4 - - - 175.9 - 38.3 - * * * * 7 GLU 7 H A 50.8 - - 181.8 - -59.1 -54.4 - - - 180.4 - 34.3 - * * 8 ALA 8 H A - - - - - -75.8 -31.0 - - - 178.7 -.7 33.5 - +* +* 9 ALA 9 H A - - - - - -59.0 -49.2 - - - 178.8 -2.9 33.8 - * * 10 ARG 10 H A - 178.8 - 178.5 - -62.9 -36.6 - - - 179.9 -2.6 33.3 - 11 LEU 11 H A - 172.8 - - - -63.0 -52.1 - - - 180.1 -1.3 35.0 - * * * 12 ARG 12 H A - - -60.4 178.1 - -62.6 -36.9 - - - 179.4 -3.0 34.8 - * * 13 PHE 13 H A - 167.4 - - - -67.9 -49.8 - - - 184.8 -2.5 34.7 - 14 ARG 14 H A - 183.3 - 171.0 - -81.7 -21.6 - - - 177.4 -3.3 30.6 - * +* +* +* 15 CYS 15 h A - 181.6 - - - - - - - - 179.1 -2.3 33.8 - 16 PHE 16 t B - 179.2 - - - - - - - - 179.2 -.7 34.8 - +* +* 17 HIS 17 B 75.7 - - - - - - - - - 176.1 - 34.5 - Residue-by-residue listing for refined_3 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 - 170.6 - - - - - - - - 177.2 -.9 32.9 - * * 19 GLU 19 t B 47.5 - - 172.8 - - - - - - 180.7 -.7 31.3 - * +* +* 20 GLU 20 T A - - -59.9 170.0 - - - - - - 180.9 -.7 36.0 - +* +* 21 ALA 21 T A - - - - - - - - - - 183.0 - 33.5 - 22 THR 22 T A - 201.5 - - - - - - - - 179.7 -1.2 33.7 - * * * 23 GLY 23 h - - - - - - - - - - - 182.7 -1.1 - - * * 24 PRO 24 H - - - - - -72.7 -72.7 -36.4 - - - 182.8 - 38.7 - * * 25 GLN 25 H A - - -52.4 - - -67.3 -39.2 - - - 181.3 - 35.5 - 26 GLU 26 H A - 180.0 - 168.0 - -75.1 -34.7 - - - 175.8 - 32.7 - 27 ALA 27 H A - - - - - -61.6 -39.6 - - - 177.5 -1.9 34.1 - 28 LEU 28 H A - - -64.5 178.5 - -60.1 -41.0 - - - 179.9 -2.2 33.9 - 29 ALA 29 H A - - - - - -61.3 -32.8 - - - 178.3 -1.3 34.0 - 30 GLN 30 H A - - -62.1 169.6 - -76.0 -48.9 - - - 178.2 -1.2 35.4 - * * 31 LEU 31 H A - - -72.1 169.8 - -60.1 -44.9 - - - 181.7 -3.0 33.6 - * * 32 ARG 32 H A 66.1 - - 180.2 - -64.8 -31.8 - - - 177.4 -3.6 31.1 - ** ** 33 GLU 33 H A - 178.8 - - - -67.1 -51.4 - - - 181.1 -.9 37.4 - * +* +* 34 LEU 34 H A - - -59.9 174.9 - -63.2 -45.0 - - - 176.8 -2.4 34.1 - 35 CYS 35 H A - 184.5 - - - -63.7 -37.9 - - - 180.3 -3.4 34.8 - +* +* 36 ARG 36 H A - 185.2 - - - -67.2 -36.7 - - - 177.3 -2.0 33.3 - 37 GLN 37 H A - - -59.5 190.1 - -66.7 -21.8 - - - 180.9 -2.3 34.6 - +* +* 38 TRP 38 H A - 169.0 - - - -85.2 -54.4 - - - 181.1 -.9 32.6 - +* * +* +* 39 LEU 39 H A - - -55.0 - - -88.1 -40.5 - - - 178.1 -2.8 30.6 - +* * +* 40 ARG 40 h l - - -55.5 178.4 - - - - - - 181.8 -1.5 31.5 - 41 PRO 41 T - - - - - -72.3 - - - - - 182.8 - 38.4 - * * 42 GLU 42 T A 62.9 - - - - - - - - - 180.7 - 30.9 - 43 VAL 43 T A - - -61.8 - - - - - - - 182.5 - 32.1 - 44 ARG 44 t B - - -64.6 180.5 - - - - - - 181.2 -2.4 32.4 - 45 SER 45 h B - - -59.4 - - - - - - - 179.8 - 35.5 - 46 LYS 46 H A - - -63.5 169.1 - -55.8 -41.2 - - - 181.3 - 36.6 - 47 GLU 47 H A - 178.6 - 180.5 - -55.8 -40.2 - - - 180.8 - 35.5 - 48 GLN 48 H A - - -57.4 - - -63.4 -31.3 - - - 181.2 -.7 35.2 - +* +* 49 MET 49 H A - - -54.0 184.5 - -73.3 -39.2 - - - 177.0 -.9 32.7 - * * 50 LEU 50 H A - - -75.9 - - -55.5 -48.5 - - - 179.5 -1.5 32.1 - 51 GLU 51 H A - - -68.2 - - -57.8 -48.8 - - - 180.2 -1.6 33.4 - 52 LEU 52 H A - - -62.5 179.2 - -61.7 -37.7 - - - 181.8 -1.6 34.4 - 53 LEU 53 H A - 181.2 - - - -77.2 -32.7 - - - 174.2 -2.3 32.4 - * * 54 VAL 54 H A - 175.1 - - - -64.0 -39.0 - - - 176.9 -2.5 33.1 - 55 LEU 55 H A - 180.6 - - - -57.7 -44.6 - - - 179.1 -2.3 35.7 - Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 GLU 56 H A - - -69.9 - - -54.4 -51.0 - - - 182.3 -1.5 33.5 - * * 57 GLN 57 H A - 194.9 - - - -73.8 -45.7 - - - 182.3 -1.8 33.6 - 58 PHE 58 H A - 180.5 - - - -53.5 -46.8 - - - 178.5 -3.1 34.0 - * * 59 LEU 59 H A - - -95.4 - - -61.2 -39.3 - - - 179.5 -2.8 30.2 - +* * * +* 60 GLY 60 H - - - - - - -80.8 -23.9 - - - 177.5 -1.2 - - * * * * 61 ALA 61 H A - - - - - -67.4 -31.2 - - - 174.3 -2.4 34.0 - 62 LEU 62 h B - - -65.2 170.4 - - - - - - 175.4 -1.4 37.0 - 63 PRO 63 h - - - - - -67.0 - - - - - 182.4 - 39.1 - * * 64 PRO 64 H - - - - - -45.4 -45.4 -34.8 - - - 179.5 - 38.2 - +* +* * +* 65 GLU 65 H A 58.0 - - 187.5 - -69.1 -47.5 - - - 177.8 - 32.2 - 66 ILE 66 H A - - -61.0 180.3 - -71.1 -39.6 - - - 180.7 -.6 34.5 - +* +* 67 GLN 67 H A - 180.3 - 177.9 - -60.4 -39.0 - - - 179.2 -3.3 34.5 - +* +* 68 ALA 68 H A - - - - - -63.0 -30.7 - - - 180.1 -1.9 33.6 - 69 ARG 69 H A - - -52.7 - - -67.8 -53.0 - - - 179.8 -.8 35.9 - * +* +* 70 VAL 70 H A - 177.9 - - - -59.9 -41.0 - - - 181.5 -1.7 36.5 - 71 GLN 71 H A - 211.7 - - - -51.6 -35.5 - - - 180.2 -2.6 37.3 - +* * +* 72 GLY 72 H - - - - - - -79.5 -40.9 - - - 182.2 -.9 - - * * * 73 GLN 73 H A - - -68.7 - - -80.3 -45.2 - - - 186.8 -1.3 32.1 - * * * 74 ARG 74 h l - - -60.4 - - - - - - - 181.2 -3.3 31.8 - +* +* 75 PRO 75 - - - - - -53.7 - - - - - 178.6 - 39.2 - * +* +* 76 GLY 76 S - - - - - - - - - - - 180.1 - - - 77 SER 77 h B - - -53.4 - - - - - - - 180.1 - 35.4 - 78 PRO 78 H - - - - - -58.9 -58.9 -45.0 - - - 179.3 - 37.8 - * * 79 GLU 79 H A - - -67.8 170.6 - -63.9 -30.7 - - - 180.5 - 34.4 - 80 GLU 80 H A - 189.3 - - - -73.4 -44.7 - - - 174.8 - 33.5 - 81 ALA 81 H A - - - - - -59.5 -42.8 - - - 178.7 -2.5 34.5 - 82 ALA 82 H A - - - - - -56.0 -33.6 - - - 180.9 -3.0 33.8 - * * 83 ALA 83 H A - - - - - -66.3 -47.4 - - - 178.8 -1.1 33.3 - * * 84 LEU 84 H A 48.4 - - 159.7 - -71.7 -43.5 - - - 181.5 -1.3 28.6 - +* +* 85 VAL 85 H A - - -57.1 - - -65.8 -31.0 - - - 177.0 -2.6 31.1 - 86 ASP 86 H A - 183.1 - - - -55.9 -36.4 - - - 176.6 -1.8 34.7 - 87 GLY 87 H - - - - - - -84.2 -40.9 - - - 181.0 -.9 - - +* +* +* 88 LEU 88 H A - - -63.9 173.9 - -57.8 -34.0 - - - 179.3 -2.4 34.2 - 89 ARG 89 H A 56.5 - - 178.0 - -61.9 -60.7 - - - 181.1 -2.5 31.1 - +* +* 90 ARG 90 h ~a - - -82.0 177.6 - - - - - - 183.9 -.8 32.6 - ** * +* ** 91 GLU 91 B 55.2 - - 187.2 - - - - - - 181.8 - 33.1 - Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 92 PRO 92 - - - - - -94.3 - - - - - 182.0 - 40.0 - +** +* +** 93 GLY 93 - - - - - - - - - - - 181.9 - - - 94 GLY 94 - - - - - - - - - - - - -.6 - - +* +* 95 GLY 301 - - - - - - - - - - - 179.3 - - - 96 SER 302 B - 188.3 - - - - - - - - 179.0 - 34.8 - 97 ASP 303 B - - -62.9 - - - - - - - 177.0 - 34.7 - 98 PRO 304 - - - - - -73.4 - - - - - 180.2 - 38.7 - * * 99 GLY 305 h - - - - - - - - - - - 179.1 - - - 100 PRO 306 H - - - - - -60.3 -60.3 -32.2 - - - 177.6 - 38.7 - * * 101 GLU 307 H A 57.2 - - 175.2 - -64.4 -37.6 - - - 180.7 - 34.2 - 102 ALA 308 H A - - - - - -74.3 -39.1 - - - 175.9 - 34.0 - 103 ALA 309 H A - - - - - -58.0 -46.6 - - - 177.3 -2.3 34.8 - 104 ARG 310 H A - 180.9 - 186.9 - -60.8 -40.9 - - - 184.3 -2.5 35.0 - 105 LEU 311 H A - 176.5 - - - -63.1 -32.1 - - - 177.2 -1.9 34.5 - 106 ARG 312 H A - - -55.7 177.7 - -76.5 -43.9 - - - 180.0 -1.6 35.2 - 107 PHE 313 H A - 166.4 - - - -66.1 -43.6 - - - 186.6 -2.2 35.7 - * * * 108 ARG 314 h A - 199.0 - - - - - - - - 178.2 -3.8 35.5 - ** ** 109 CYS 315 T A - 185.0 - - - - - - - - 181.9 -.5 34.1 - ** ** 110 PHE 316 t B - 178.2 - - - - - - - - 174.6 -1.1 34.7 - * * 111 HIS 317 B 73.9 - - - - - - - - - 174.3 - 34.0 - 112 TYR 318 B - 163.2 - - - - - - - - 179.5 -1.5 32.6 - * * 113 GLU 319 t B 43.3 - - 179.0 - - - - - - 182.1 -.6 31.5 - * +* +* 114 GLU 320 T A - - -63.4 176.9 - - - - - - 179.8 -.6 34.4 - +* +* 115 ALA 321 T A - - - - - - - - - - 184.6 - 34.3 - 116 THR 322 T A - 201.0 - - - - - - - - 181.0 -1.2 34.5 - * * * 117 GLY 323 h - - - - - - - - - - - 183.5 -1.1 - - * * 118 PRO 324 H - - - - - -73.3 -73.3 -31.0 - - - 182.1 - 39.2 - +* +* 119 GLN 325 H A - - -52.5 - - -70.0 -39.4 - - - 178.8 - 35.1 - 120 GLU 326 H A - 179.4 - 161.1 - -71.2 -39.2 - - - 176.7 - 32.1 - 121 ALA 327 H A - - - - - -56.9 -43.0 - - - 177.1 -2.1 34.0 - 122 LEU 328 H A - - -64.8 182.5 - -58.0 -40.7 - - - 179.8 -2.2 33.6 - 123 ALA 329 H A - - - - - -60.3 -40.9 - - - 180.9 -1.3 34.7 - 124 GLN 330 H A - - -47.1 187.0 - -69.9 -48.8 - - - 180.2 -1.7 36.2 - * * 125 LEU 331 H A - - -69.1 173.8 - -59.6 -47.1 - - - 181.5 -3.1 33.1 - * * 126 ARG 332 H A 62.7 - - 180.6 - -63.7 -37.4 - - - 176.4 -3.3 31.2 - +* +* 127 GLU 333 H A - 173.9 - - - -60.6 -51.7 - - - 182.2 -1.5 36.7 - * * 128 LEU 334 H A - - -57.3 175.7 - -66.1 -41.2 - - - 177.9 -2.5 34.2 - 129 CYS 335 H A - 183.6 - - - -64.3 -39.5 - - - 179.0 -3.3 34.9 - +* +* Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 130 ARG 336 H A - 179.0 - - - -67.9 -35.1 - - - 175.9 -2.6 32.4 - 131 GLN 337 H A - - -64.9 180.5 - -67.8 -19.4 - - - 179.9 -2.1 34.9 - +* +* 132 TRP 338 H A - 169.8 - - - -88.9 -59.5 - - - 182.1 -.7 33.3 - +* +* +* +* 133 LEU 339 H A - - -56.0 - - -80.5 -35.6 - - - 174.9 -3.0 30.3 - * * * * 134 ARG 340 h l - - -52.8 176.8 - - - - - - 180.4 -1.6 33.1 - 135 PRO 341 T - - - - - -64.2 - - - - - 181.0 - 39.1 - * * 136 GLU 342 T A - - -57.3 - - - - - - - 184.9 - 35.8 - 137 VAL 343 T A - - -61.0 - - - - - - - 179.3 -1.1 32.8 - * * 138 ARG 344 t B - - -64.0 182.2 - - - - - - 183.2 -3.4 32.3 - +* +* 139 SER 345 h B 56.5 - - - - - - - - - 174.6 - 36.4 - 140 LYS 346 H A 57.9 - - - - -55.6 -40.9 - - - 181.7 - 33.9 - 141 GLU 347 H A - 180.1 - 174.7 - -55.5 -44.9 - - - 179.4 - 34.4 - 142 GLN 348 H A - - -60.2 - - -68.3 -27.3 - - - 178.8 - 32.7 - * * 143 MET 349 H A - - -57.0 183.3 - -66.8 -37.8 - - - 174.7 -1.1 32.3 - * * 144 LEU 350 H A - - -74.3 - - -61.2 -41.8 - - - 180.1 -1.5 32.7 - 145 GLU 351 H A - - -51.1 - - -57.4 -51.0 - - - 180.9 -1.4 34.2 - * * * 146 LEU 352 H A - - -61.4 178.2 - -63.5 -38.1 - - - 182.7 -2.2 34.6 - 147 LEU 353 H A - 181.9 - - - -76.7 -33.2 - - - 174.1 -2.3 32.2 - * * 148 VAL 354 H A - 173.8 - - - -64.2 -38.7 - - - 176.8 -2.8 33.2 - * * 149 LEU 355 H A - 178.8 - - - -55.7 -45.2 - - - 180.0 -2.0 35.9 - 150 GLU 356 H A - - -70.8 - - -52.9 -51.1 - - - 182.0 -1.5 32.1 - * * * 151 GLN 357 H A - 194.4 - - - -74.0 -45.5 - - - 183.4 -1.5 33.7 - 152 PHE 358 H A - 179.4 - - - -53.6 -46.8 - - - 180.3 -3.0 34.0 - * * 153 LEU 359 H A - - -64.3 185.2 - -62.8 -38.9 - - - 181.1 -3.0 31.3 - * * 154 GLY 360 H - - - - - - -81.1 -20.0 - - - 177.5 -1.2 - - * +* * +* 155 ALA 361 H A - - - - - -72.5 -27.6 - - - 175.9 -2.0 33.9 - * * 156 LEU 362 h B - - -64.5 170.7 - - - - - - 174.9 -1.2 36.9 - * * 157 PRO 363 h - - - - - -64.7 - - - - - 181.0 - 39.5 - +* +* 158 PRO 364 H - - - - - -42.5 -42.5 -39.6 - - - 180.8 - 38.9 - ** +* * ** 159 GLU 365 H A 62.0 - - 188.9 - -69.0 -47.3 - - - 178.8 - 32.9 - 160 ILE 366 H A - - -61.8 180.1 - -68.1 -41.3 - - - 179.8 - 34.5 - 161 GLN 367 H A - 181.5 - 178.1 - -62.1 -37.2 - - - 179.5 -3.3 34.7 - +* +* 162 ALA 368 H A - - - - - -64.3 -35.7 - - - 180.8 -1.9 34.1 - 163 ARG 369 H A - - -61.7 - - -67.4 -39.8 - - - 178.2 -1.2 33.7 - * * 164 VAL 370 H A - 175.0 - - - -71.1 -35.3 - - - 187.4 -1.5 36.5 - * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 165 GLN 371 H A - 212.1 - - - -56.4 -40.1 - - - 180.6 -2.1 35.3 - +* +* 166 GLY 372 H - - - - - - -64.1 -36.0 - - - 180.5 -1.2 - - * * 167 GLN 373 H A - - -68.5 - - -86.1 -49.7 - - - 187.9 -.8 33.3 - +* * +* +* 168 ARG 374 h l - - -63.8 - - - - - - - 179.6 -3.1 32.5 - * * 169 PRO 375 - - - - - -56.1 - - - - - 181.0 - 38.8 - * * 170 GLY 376 S - - - - - - - - - - - 176.9 - - - 171 SER 377 h B - - -54.4 - - - - - - - 184.9 - 34.9 - 172 PRO 378 H - - - - - -62.8 -62.8 -45.2 - - - 181.0 - 37.5 - * * 173 GLU 379 H A - - -61.6 178.1 - -69.9 -29.6 - - - 175.1 - 31.6 - 174 GLU 380 H A - 183.4 - - - -63.3 -49.5 - - - 178.0 - 34.9 - 175 ALA 381 H A - - - - - -62.4 -42.5 - - - 179.7 -2.2 34.1 - 176 ALA 382 H A - - - - - -54.7 -35.4 - - - 179.8 -3.0 33.6 - * * 177 ALA 383 H A - - - - - -66.2 -46.7 - - - 179.5 -1.5 33.0 - 178 LEU 384 H A 50.2 - - 160.4 - -73.2 -36.7 - - - 180.3 -1.3 27.7 - * +* +* 179 VAL 385 H A - - -59.3 - - -69.1 -30.8 - - - 176.9 -2.7 30.3 - * * 180 ASP 386 H A - 179.8 - - - -57.0 -33.5 - - - 178.2 -1.7 34.1 - 181 GLY 387 h - - - - - - - - - - - 181.5 -.7 - - +* +* 182 LEU 388 T A - - -61.8 174.7 - - - - - - 186.5 -.8 34.8 - * +* +* 183 ARG 389 t b 58.4 - - 173.8 - - - - - - 177.6 -1.9 32.9 - 184 ARG 390 S XX - - -69.3 176.7 - - - - - - 170.2 -2.4 28.2 - **** +* +* **** 185 GLU 391 S B - - -71.9 - - - - - - - 175.6 -2.3 33.1 - 186 PRO 392 - - - - - -57.2 - - - - - 177.6 - 39.0 - * * 187 GLY 393 - - - - - - - - - - - 178.3 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +* +***13.1**16.7* +* ** +* *16.7* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.0 181.7 -62.4 177.1 -62.5 -64.1 -38.5 - - - 179.7 -1.9 34.3 Standard deviations: 8.5 10.1 7.8 6.6 12.2 16.5 18.7 - - - 2.7 .9 2.2 Numbers of values: 18 51 63 56 18 123 123 0 0 0 186 127 170 0 Residue-by-residue listing for refined_3 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_3 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 1.504 - 1.462 - 116.96 120.29 - 110.76 - 122.75 2 SER 2 1.309 1.247 1.525 1.544 1.431 121.23 115.45 121.42 111.25 109.62 110.66 123.11 * * * 3 ASP 3 1.303 1.225 1.511 1.544 1.448 122.48 118.60 119.12 110.63 108.19 110.26 122.24 +* * * +* 4 PRO 4 1.351 1.238 1.530 1.532 1.473 122.64 115.61 121.40 109.54 111.88 103.51 122.99 5 GLY 5 1.305 1.232 1.496 - 1.419 121.24 118.43 119.62 - 110.41 - 121.95 +* * ** ** 6 PRO 6 1.344 1.232 1.538 1.530 1.479 123.05 115.14 121.33 111.25 111.87 102.89 123.51 * * * 7 GLU 7 1.322 1.235 1.546 1.539 1.449 123.91 116.70 120.63 111.47 111.56 108.78 122.65 * * * * 8 ALA 8 1.326 1.230 1.511 1.519 1.447 121.86 115.69 120.74 110.80 110.16 110.98 123.56 9 ALA 9 1.326 1.227 1.518 1.517 1.453 122.47 116.66 120.31 110.48 110.67 110.59 123.00 10 ARG 10 1.338 1.230 1.522 1.530 1.457 121.21 116.25 120.62 109.71 111.03 112.07 123.12 11 LEU 11 1.321 1.224 1.531 1.523 1.412 122.56 116.31 120.49 111.48 110.22 108.39 123.14 ** * ** 12 ARG 12 1.329 1.233 1.518 1.527 1.468 122.48 114.85 121.21 109.62 110.45 110.20 123.93 13 PHE 13 1.314 1.209 1.524 1.531 1.442 123.71 117.55 120.46 110.79 112.88 108.64 121.98 * * * * * 14 ARG 14 1.308 1.238 1.536 1.540 1.444 119.88 116.58 120.79 113.74 112.43 111.27 122.59 * * +* +* Residue-by-residue listing for refined_3 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 1.320 1.245 1.539 1.545 1.459 121.63 115.84 120.95 110.86 110.00 110.72 123.21 16 PHE 16 1.330 1.238 1.514 1.536 1.451 123.01 116.20 121.13 110.30 110.29 109.84 122.66 17 HIS 17 1.296 1.238 1.506 1.557 1.430 120.12 117.47 119.99 109.95 107.62 111.76 122.54 ** * * * ** 18 TYR 18 1.287 1.230 1.502 1.531 1.419 119.11 115.06 121.50 111.71 109.11 111.69 123.41 +** * ** * +** 19 GLU 19 1.288 1.237 1.503 1.546 1.408 121.93 114.44 121.42 113.29 109.95 112.33 124.12 +** * +** +* * +** 20 GLU 20 1.318 1.223 1.530 1.526 1.459 124.48 115.61 120.94 109.61 110.85 108.41 123.42 +* * +* 21 ALA 21 1.322 1.236 1.533 1.518 1.450 123.18 117.93 119.90 110.48 112.96 110.33 122.16 22 THR 22 1.337 1.218 1.539 1.585 1.458 119.70 115.88 121.06 110.70 109.12 111.74 123.01 +* * +* 23 GLY 23 1.331 1.231 1.519 - 1.445 121.11 119.17 120.06 - 111.38 - 120.77 * * * 24 PRO 24 1.339 1.229 1.517 1.503 1.453 121.67 116.88 120.09 110.25 113.67 103.01 123.02 * * 25 GLN 25 1.326 1.236 1.525 1.530 1.448 121.06 115.45 121.43 108.24 108.38 111.21 123.11 * * 26 GLU 26 1.325 1.235 1.520 1.524 1.437 121.91 116.30 120.58 113.13 110.83 109.69 123.10 * +* +* 27 ALA 27 1.330 1.228 1.526 1.521 1.457 121.87 115.91 120.99 110.42 109.87 110.46 123.09 28 LEU 28 1.327 1.216 1.517 1.522 1.464 122.44 116.83 120.21 108.92 111.70 111.68 122.96 29 ALA 29 1.329 1.239 1.530 1.522 1.468 122.11 114.90 121.63 110.59 110.43 110.30 123.46 30 GLN 30 1.313 1.228 1.523 1.501 1.435 123.39 115.40 121.28 111.34 109.80 107.68 123.28 * * * +* +* 31 LEU 31 1.324 1.218 1.504 1.518 1.458 123.24 117.45 119.92 109.80 112.90 110.98 122.64 * * 32 ARG 32 1.324 1.187 1.505 1.533 1.447 120.44 116.55 120.01 111.65 111.21 113.24 123.40 ** +* ** 33 GLU 33 1.317 1.227 1.526 1.536 1.464 123.17 115.57 120.84 109.29 108.90 107.18 123.52 +* +* 34 LEU 34 1.320 1.230 1.528 1.530 1.454 122.85 115.98 120.94 111.38 110.50 109.50 123.07 35 CYS 35 1.322 1.227 1.543 1.538 1.440 122.61 116.67 121.06 110.90 109.95 109.21 122.24 36 ARG 36 1.326 1.211 1.525 1.537 1.426 122.54 117.53 119.80 113.32 110.76 108.92 122.66 * +* +* +* 37 GLN 37 1.329 1.234 1.521 1.509 1.468 121.29 114.64 121.79 108.86 110.28 110.99 123.56 * * 38 TRP 38 1.304 1.238 1.548 1.540 1.428 124.07 118.70 119.69 114.03 112.67 108.35 121.59 +* * +* * * ** * ** 39 LEU 39 1.334 1.224 1.510 1.547 1.469 118.55 116.34 119.75 110.23 111.63 115.17 123.90 +* +** +** 40 ARG 40 1.342 1.231 1.533 1.536 1.464 123.65 116.79 121.54 112.34 112.26 111.49 121.63 * * * 41 PRO 41 1.342 1.231 1.516 1.527 1.456 122.77 117.16 120.02 110.14 113.77 103.81 122.82 42 GLU 42 1.316 1.235 1.519 1.543 1.436 120.18 116.56 120.67 111.58 111.56 113.59 122.75 * +* +* 43 VAL 43 1.324 1.233 1.530 1.560 1.455 120.58 117.58 120.08 109.93 112.85 113.07 122.34 44 ARG 44 1.325 1.242 1.515 1.532 1.462 121.08 114.67 121.70 110.23 113.14 112.13 123.63 45 SER 45 1.309 1.240 1.529 1.526 1.427 123.37 115.11 120.88 110.41 110.91 108.40 124.00 * +* * +* 46 LYS 46 1.322 1.216 1.520 1.522 1.465 124.96 115.35 121.15 109.30 111.12 107.66 123.48 +* +* +* 47 GLU 47 1.313 1.234 1.525 1.517 1.462 124.15 115.40 121.18 109.77 111.38 108.62 123.40 * * * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 48 GLN 48 1.317 1.234 1.524 1.536 1.455 122.75 115.32 121.26 109.25 110.13 110.27 123.42 49 MET 49 1.314 1.235 1.511 1.506 1.447 122.16 116.85 119.82 111.34 112.55 110.62 123.33 * * * 50 LEU 50 1.344 1.220 1.518 1.571 1.470 121.21 116.14 120.35 110.79 110.24 113.41 123.42 * ** +* ** 51 GLU 51 1.322 1.238 1.531 1.519 1.465 122.84 116.99 120.45 110.72 112.92 110.08 122.56 52 LEU 52 1.327 1.227 1.520 1.527 1.454 121.60 115.84 121.13 109.91 111.09 110.35 123.01 53 LEU 53 1.304 1.236 1.539 1.516 1.431 121.81 116.96 120.63 113.74 111.90 108.91 122.40 +* * +* +* 54 VAL 54 1.328 1.223 1.530 1.568 1.459 120.94 115.74 120.79 110.76 108.87 112.51 123.41 * * 55 LEU 55 1.336 1.234 1.531 1.535 1.468 123.21 115.23 120.83 109.22 109.90 109.46 123.94 56 GLU 56 1.329 1.243 1.504 1.533 1.469 123.34 116.33 120.40 109.85 113.12 111.09 123.27 * * 57 GLN 57 1.313 1.223 1.516 1.544 1.438 120.77 116.23 119.96 112.00 109.16 110.38 123.75 * * * * 58 PHE 58 1.339 1.238 1.523 1.543 1.465 123.04 116.33 120.57 110.25 111.35 110.59 123.09 59 LEU 59 1.323 1.212 1.510 1.542 1.454 121.43 117.56 119.70 113.07 113.20 112.20 122.69 +* +* 60 GLY 60 1.315 1.230 1.510 - 1.445 119.60 116.10 120.75 - 112.42 - 123.14 * * 61 ALA 61 1.317 1.248 1.521 1.521 1.444 122.61 115.39 120.78 110.93 109.79 110.23 123.82 62 LEU 62 1.333 1.243 1.525 1.535 1.448 123.45 118.37 120.03 107.85 109.33 109.17 121.60 * * * 63 PRO 63 1.340 1.240 1.519 1.539 1.448 121.51 118.57 119.13 109.76 108.14 104.42 122.29 * * * * * 64 PRO 64 1.345 1.224 1.541 1.521 1.479 123.49 116.95 120.49 110.80 113.97 102.95 122.55 65 GLU 65 1.326 1.232 1.551 1.533 1.459 121.76 117.56 120.29 112.45 112.22 110.38 122.13 * * * 66 ILE 66 1.341 1.239 1.533 1.555 1.456 121.25 115.26 121.40 109.49 109.77 111.22 123.32 67 GLN 67 1.318 1.237 1.528 1.517 1.453 123.01 116.00 120.51 110.74 111.24 109.17 123.48 68 ALA 68 1.329 1.234 1.527 1.521 1.466 122.91 116.39 120.56 110.26 111.73 110.74 123.05 69 ARG 69 1.327 1.227 1.524 1.533 1.461 121.74 114.99 121.52 108.35 108.60 110.44 123.48 70 VAL 70 1.329 1.238 1.508 1.536 1.467 123.43 113.67 121.58 107.20 110.39 110.36 124.74 * * * 71 GLN 71 1.299 1.228 1.548 1.519 1.451 125.65 116.46 120.64 109.21 110.59 106.74 122.89 ** * ** ** ** 72 GLY 72 1.328 1.234 1.526 - 1.445 120.56 117.38 120.37 - 113.56 - 122.23 73 GLN 73 1.328 1.226 1.507 1.554 1.466 120.27 115.92 120.28 109.09 112.22 114.15 123.76 * ** ** 74 ARG 74 1.322 1.228 1.538 1.533 1.463 123.49 116.83 120.98 110.74 110.56 113.20 122.10 +* +* 75 PRO 75 1.348 1.224 1.536 1.533 1.484 124.19 116.27 120.78 109.61 114.11 102.88 122.93 * * 76 GLY 76 1.316 1.229 1.520 - 1.456 121.36 116.92 120.67 - 113.35 - 122.41 77 SER 77 1.318 1.243 1.537 1.533 1.455 121.81 118.21 119.79 109.38 109.18 109.89 122.00 * * 78 PRO 78 1.354 1.226 1.529 1.536 1.470 122.82 117.09 120.12 110.22 112.93 104.71 122.77 +* +* 79 GLU 79 1.339 1.234 1.500 1.509 1.477 121.68 115.50 121.22 108.99 110.93 111.06 123.29 * * * * 80 GLU 80 1.304 1.215 1.535 1.526 1.420 121.27 117.04 120.20 112.23 108.87 110.22 122.74 +* +* * +* 81 ALA 81 1.355 1.235 1.514 1.516 1.464 121.91 115.60 120.51 109.84 110.40 110.37 123.88 +* +* Residue-by-residue listing for refined_3 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 82 ALA 82 1.337 1.199 1.524 1.537 1.456 123.03 116.28 120.69 110.80 110.90 110.52 123.00 +* +* 83 ALA 83 1.308 1.234 1.534 1.507 1.455 123.02 117.72 120.09 110.72 112.27 110.38 122.19 +* +* 84 LEU 84 1.333 1.233 1.511 1.563 1.459 119.45 116.47 120.65 111.25 112.48 116.45 122.84 +* * *** *** 85 VAL 85 1.319 1.232 1.525 1.536 1.457 121.53 115.52 120.84 111.21 111.74 113.42 123.63 * * 86 ASP 86 1.327 1.223 1.516 1.528 1.461 123.65 115.91 120.53 110.40 110.36 109.66 123.54 * * 87 GLY 87 1.326 1.228 1.517 - 1.441 121.13 115.79 120.78 - 111.39 - 123.42 88 LEU 88 1.336 1.246 1.528 1.532 1.477 123.65 116.63 120.29 109.41 112.80 110.44 123.07 * * 89 ARG 89 1.329 1.219 1.535 1.554 1.456 121.22 116.86 120.15 112.32 111.85 112.40 122.93 * * * * 90 ARG 90 1.320 1.230 1.511 1.554 1.474 123.42 115.63 120.71 109.55 111.98 113.16 123.66 * +* +* 91 GLU 91 1.312 1.216 1.538 1.531 1.451 122.91 117.72 120.77 112.58 112.36 109.09 121.51 * * * 92 PRO 92 1.345 1.231 1.544 1.527 1.461 122.91 117.13 120.60 110.11 113.54 101.43 122.24 * * 93 GLY 93 1.321 1.242 1.519 - 1.458 120.87 115.81 121.03 - 112.33 - 123.16 94 GLY 94 1.307 1.247 1.503 - 1.439 121.83 - 119.53 - 110.77 - - +* +* 95 GLY 301 - 1.236 1.510 - 1.451 - 115.88 120.98 - 112.02 - 123.13 96 SER 302 1.314 1.227 1.524 1.550 1.435 122.37 116.95 120.09 110.93 108.25 110.03 122.96 * * * * 97 ASP 303 1.312 1.237 1.504 1.543 1.452 121.61 117.88 120.14 108.47 109.14 112.18 121.98 * * * 98 PRO 304 1.340 1.232 1.534 1.533 1.462 122.30 115.75 121.12 110.45 111.39 103.41 123.13 99 GLY 305 1.320 1.232 1.516 - 1.435 121.32 118.50 120.03 - 111.70 - 121.47 100 PRO 306 1.351 1.228 1.528 1.535 1.476 122.65 115.59 121.29 110.37 111.02 103.63 123.11 101 GLU 307 1.325 1.234 1.530 1.533 1.451 122.57 116.08 120.72 110.18 110.74 110.57 123.18 102 ALA 308 1.325 1.232 1.506 1.512 1.444 122.37 115.57 120.78 110.81 109.70 110.39 123.65 103 ALA 309 1.330 1.238 1.514 1.515 1.453 122.29 115.36 121.26 110.02 109.13 110.21 123.35 104 ARG 310 1.331 1.195 1.516 1.524 1.445 121.97 116.71 120.44 107.98 110.40 111.58 122.83 +* * +* 105 LEU 311 1.314 1.229 1.546 1.523 1.420 123.31 116.63 120.76 112.47 111.62 107.61 122.61 * * ** * +* ** 106 ARG 312 1.318 1.234 1.531 1.525 1.464 121.93 114.22 121.95 110.19 109.36 109.30 123.81 107 PHE 313 1.313 1.212 1.536 1.541 1.463 125.12 116.32 121.18 110.97 112.82 106.97 122.48 * +* ** ** 108 ARG 314 1.297 1.233 1.538 1.529 1.453 122.90 115.79 121.18 111.22 110.80 107.48 123.03 ** +* ** 109 CYS 315 1.316 1.240 1.538 1.539 1.448 122.48 115.50 121.19 111.06 109.47 110.21 123.30 110 PHE 316 1.330 1.235 1.517 1.538 1.451 122.98 116.51 120.99 109.96 111.52 109.86 122.49 111 HIS 317 1.310 1.239 1.506 1.571 1.433 119.60 117.64 119.97 109.76 107.10 113.02 122.37 * ** * * * * ** 112 TYR 318 1.296 1.231 1.495 1.528 1.423 119.12 114.89 121.22 111.76 108.91 112.08 123.86 ** * +* * ** 113 GLU 319 1.276 1.241 1.505 1.539 1.408 122.33 114.61 121.52 114.17 110.33 110.89 123.85 +*** +** ** +*** 114 GLU 320 1.319 1.230 1.522 1.533 1.452 123.64 115.54 120.89 110.67 110.83 109.76 123.55 * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 115 ALA 321 1.315 1.227 1.535 1.516 1.444 123.18 117.99 120.01 109.93 112.98 109.80 122.00 * * 116 THR 322 1.330 1.230 1.535 1.570 1.459 119.58 116.02 121.07 110.40 110.32 110.42 122.86 * * * 117 GLY 323 1.320 1.233 1.516 - 1.438 120.75 118.73 120.20 - 111.25 - 121.07 * * * 118 PRO 324 1.332 1.231 1.514 1.501 1.462 122.09 116.50 120.44 109.73 113.40 102.85 123.05 * * 119 GLN 325 1.322 1.234 1.524 1.530 1.437 121.22 115.58 121.47 109.10 107.79 111.25 122.92 * * * 120 GLU 326 1.334 1.220 1.511 1.534 1.439 121.30 116.41 120.14 112.89 110.03 111.16 123.39 * * * 121 ALA 327 1.329 1.220 1.528 1.520 1.461 122.17 116.48 120.58 110.49 110.39 110.38 122.93 122 LEU 328 1.331 1.225 1.514 1.522 1.471 122.12 116.54 120.07 108.52 112.23 112.34 123.40 * * 123 ALA 329 1.328 1.228 1.516 1.523 1.463 122.12 114.73 121.45 109.90 109.88 110.21 123.78 124 GLN 330 1.311 1.228 1.521 1.510 1.440 123.11 114.80 121.72 109.85 108.98 108.18 123.45 * * * * 125 LEU 331 1.325 1.212 1.506 1.522 1.451 123.56 117.93 119.53 110.45 113.32 110.90 122.53 * * 126 ARG 332 1.326 1.205 1.519 1.535 1.460 120.32 116.64 120.00 111.68 111.14 113.00 123.33 * * * 127 GLU 333 1.328 1.223 1.530 1.544 1.464 122.68 116.00 120.75 109.67 109.26 107.88 123.12 +* +* 128 LEU 334 1.323 1.227 1.531 1.530 1.458 122.40 115.90 121.00 110.74 110.85 109.81 123.09 129 CYS 335 1.321 1.228 1.536 1.544 1.450 123.02 116.27 121.43 110.90 109.47 109.23 122.27 130 ARG 336 1.322 1.217 1.523 1.539 1.421 122.46 116.66 120.26 114.09 110.89 109.39 123.07 +* ** ** 131 GLN 337 1.320 1.237 1.529 1.507 1.459 122.31 114.81 121.55 109.67 110.86 109.69 123.64 * * 132 TRP 338 1.314 1.231 1.544 1.546 1.436 124.21 118.41 119.73 113.02 112.10 108.68 121.86 * * * * +* * +* 133 LEU 339 1.334 1.223 1.509 1.543 1.469 119.07 116.24 119.92 110.64 111.89 115.06 123.84 * +** +** 134 ARG 340 1.335 1.230 1.543 1.536 1.462 123.52 118.06 120.60 110.77 112.88 110.59 121.33 * * * 135 PRO 341 1.357 1.232 1.529 1.539 1.485 123.30 116.02 121.00 109.53 113.12 103.46 122.97 * * 136 GLU 342 1.307 1.242 1.510 1.515 1.444 122.26 115.72 121.25 109.05 110.98 109.21 123.03 +* +* 137 VAL 343 1.311 1.234 1.520 1.549 1.442 121.04 117.30 120.34 110.68 112.43 111.63 122.36 * * 138 ARG 344 1.317 1.235 1.506 1.530 1.443 120.64 115.95 120.72 111.50 110.44 112.04 123.33 139 SER 345 1.296 1.243 1.528 1.520 1.435 122.62 116.36 120.29 109.63 111.03 107.84 123.35 ** * +* ** 140 LYS 346 1.350 1.212 1.506 1.565 1.475 122.15 114.16 121.61 108.67 109.76 113.07 124.19 * +* * +* +* 141 GLU 347 1.303 1.225 1.534 1.517 1.444 124.49 116.74 120.54 111.78 111.87 108.07 122.69 +* +* * +* 142 GLN 348 1.325 1.233 1.520 1.527 1.461 120.88 116.33 120.90 109.95 111.50 112.47 122.77 * * 143 MET 349 1.321 1.233 1.505 1.508 1.445 121.20 116.49 120.18 111.81 111.35 111.27 123.30 * * 144 LEU 350 1.334 1.216 1.511 1.561 1.457 120.96 116.31 120.39 110.06 109.55 113.48 123.25 +* +* +* Residue-by-residue listing for refined_3 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 1.328 1.234 1.537 1.542 1.460 122.11 116.17 121.06 109.86 110.42 110.95 122.74 146 LEU 352 1.318 1.228 1.528 1.520 1.447 122.33 116.36 120.85 109.93 111.78 109.75 122.77 147 LEU 353 1.309 1.238 1.538 1.516 1.434 121.31 116.93 120.59 113.84 112.16 109.06 122.47 * * +* +* 148 VAL 354 1.319 1.231 1.526 1.557 1.457 121.03 115.61 120.77 110.79 109.32 112.12 123.57 149 LEU 355 1.336 1.234 1.523 1.525 1.462 122.85 115.27 120.79 108.36 109.97 109.89 123.94 150 GLU 356 1.327 1.242 1.509 1.535 1.461 122.81 116.87 120.28 110.45 113.62 112.10 122.85 151 GLN 357 1.308 1.228 1.516 1.542 1.441 120.22 115.83 120.23 111.70 108.87 110.52 123.86 +* +* 152 PHE 358 1.333 1.236 1.521 1.535 1.457 122.92 116.49 120.46 110.09 112.04 110.47 123.04 153 LEU 359 1.323 1.215 1.507 1.536 1.447 121.02 117.30 119.94 111.73 112.46 112.41 122.71 * * 154 GLY 360 1.322 1.232 1.510 - 1.446 119.70 116.33 120.46 - 112.65 - 123.19 155 ALA 361 1.324 1.233 1.519 1.522 1.449 122.27 115.47 121.06 110.78 109.74 110.55 123.47 156 LEU 362 1.325 1.248 1.533 1.529 1.447 122.97 117.94 120.22 107.73 109.81 109.23 121.84 * * 157 PRO 363 1.344 1.240 1.517 1.539 1.450 122.05 117.97 119.25 109.31 108.46 104.12 122.78 * * * * 158 PRO 364 1.345 1.221 1.536 1.523 1.477 123.85 116.59 120.34 110.54 113.70 102.35 123.05 159 GLU 365 1.329 1.231 1.547 1.533 1.462 122.13 117.26 120.45 111.67 112.24 110.23 122.28 * * 160 ILE 366 1.337 1.235 1.528 1.556 1.453 121.52 115.11 121.42 110.31 109.49 110.68 123.42 161 GLN 367 1.317 1.235 1.536 1.524 1.447 123.08 115.88 120.79 110.73 110.71 109.13 123.32 162 ALA 368 1.329 1.225 1.518 1.520 1.467 122.94 116.40 120.74 109.71 111.65 110.60 122.85 163 ARG 369 1.317 1.221 1.520 1.532 1.465 121.46 115.70 121.08 110.69 110.19 110.92 123.20 164 VAL 370 1.317 1.247 1.512 1.542 1.461 122.64 114.06 121.54 107.04 110.53 110.45 124.40 * * 165 GLN 371 1.302 1.229 1.536 1.522 1.436 124.36 116.25 120.42 111.00 111.20 107.99 123.29 +* * * * +* 166 GLY 372 1.326 1.238 1.526 - 1.457 121.53 116.84 120.62 - 113.56 - 122.54 167 GLN 373 1.324 1.229 1.511 1.555 1.461 120.99 115.72 120.36 108.77 111.35 113.24 123.87 * +* +* 168 ARG 374 1.334 1.226 1.545 1.545 1.468 123.36 117.67 120.54 109.59 110.09 113.57 121.65 +* +* 169 PRO 375 1.358 1.225 1.534 1.543 1.480 123.10 116.23 121.00 110.03 113.24 103.44 122.77 * * 170 GLY 376 1.318 1.231 1.515 - 1.450 120.58 116.02 120.94 - 111.87 - 123.03 171 SER 377 1.324 1.244 1.546 1.523 1.445 122.99 118.12 119.86 110.63 108.03 109.70 121.99 * * * 172 PRO 378 1.346 1.223 1.531 1.532 1.477 123.12 117.52 119.88 110.37 114.75 104.50 122.58 * * * 173 GLU 379 1.321 1.241 1.512 1.530 1.465 121.68 115.39 121.15 112.46 110.55 111.90 123.46 * * 174 GLU 380 1.324 1.233 1.531 1.535 1.439 122.00 115.96 120.69 110.74 107.96 109.87 123.30 * * * 175 ALA 381 1.347 1.233 1.520 1.516 1.455 122.20 115.96 120.35 110.27 110.91 110.35 123.68 * * 176 ALA 382 1.338 1.217 1.530 1.533 1.461 123.21 116.06 120.94 110.96 111.14 110.40 122.97 177 ALA 383 1.306 1.231 1.535 1.512 1.451 122.46 118.06 119.92 111.16 111.89 110.51 122.02 +* +* 178 LEU 384 1.347 1.227 1.511 1.568 1.466 119.04 116.57 120.67 111.47 112.78 117.16 122.73 * +* * +*** +*** 179 VAL 385 1.319 1.224 1.522 1.536 1.458 121.27 116.31 120.54 111.28 112.52 113.99 123.13 * * 180 ASP 386 1.326 1.220 1.525 1.528 1.471 122.37 115.85 120.87 110.05 110.82 110.61 123.25 Residue-by-residue listing for refined_3 Page 14 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 181 GLY 387 1.320 1.223 1.517 - 1.441 121.27 116.13 120.94 - 112.33 - 122.90 182 LEU 388 1.316 1.228 1.532 1.532 1.461 123.03 117.04 120.18 109.22 112.82 109.93 122.77 183 ARG 389 1.323 1.241 1.549 1.534 1.485 122.72 116.44 120.81 110.23 114.38 110.66 122.75 * * * * 184 ARG 390 1.325 1.240 1.535 1.533 1.476 124.13 118.20 119.73 114.19 114.49 112.68 122.06 * * ** * * ** 185 GLU 391 1.319 1.234 1.515 1.554 1.447 119.87 118.26 119.58 108.85 107.80 114.62 122.08 * * * * ** ** 186 PRO 392 1.342 1.230 1.538 1.528 1.471 122.57 116.10 120.57 109.91 111.99 103.35 123.33 187 GLY 393 1.331 1.235 1.503 - 1.447 121.63 116.59 120.58 - 112.06 - 122.83 188 GLY 394 1.294 - 1.491 - 1.431 120.56 - - - 110.95 - - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** ** * ** +** ** * ** * +*** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 1.276 1.355 1.322 .012 +*** +* C-N (Pro) 1.341 .016 18 1.332 1.358 1.346 .006 * C-O C-O 1.231 .020 187 1.187 1.248 1.230 .009 ** CA-C CH1E-C (except Gly) 1.525 .021 170 1.495 1.551 1.524 .012 * * CH2G*-C (Gly) 1.516 .018 18 1.491 1.526 1.512 .009 * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.507 1.537 1.520 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.536 1.585 1.554 .015 +* CH1E-CH2E (the rest) 1.530 .020 138 1.501 1.571 1.533 .013 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.408 1.485 1.452 .014 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.419 1.462 1.445 .010 ** N-CH1E (Pro) 1.466 .015 18 1.448 1.485 1.469 .011 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 2.0 152 113.67 118.70 116.29 1.01 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.79 119.17 116.97 1.10 * CH1E-C-N (Pro) 116.9 1.5 18 115.14 118.57 116.61 .86 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.77 124.74 122.97 .67 * * O-C-N (Pro) 122.0 1.4 18 122.24 123.51 122.88 .32 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.55 125.65 122.17 1.30 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.60 121.83 120.94 .61 C-N-CH1E (Pro) 122.6 5.0 18 121.51 124.19 122.78 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.12 121.95 120.65 .57 CH2G*-C-O (Gly) 120.8 2.1 17 119.53 121.03 120.46 .44 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.71 111.16 110.47 .41 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.04 111.28 109.98 1.37 CH2E-CH1E-C (the rest) 110.1 1.9 138 107.73 114.19 110.61 1.41 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.10 114.49 110.82 1.45 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 110.41 113.56 111.93 .93 N-CH1E-C (Pro) 111.8 2.5 18 108.14 114.75 112.50 1.78 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.80 110.98 110.42 .23 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.36 113.99 111.80 1.19 * N-CH1E-CH2E (Pro) 103.0 1.1 18 101.43 104.71 103.37 .78 * +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.74 117.16 110.64 1.95 ** +*** ------------------------------------------------------------------------------------------------------------- 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_3 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] 145 95.4% Residues in additional allowed regions [a,b,l,p] 5 3.3% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 1 .7% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 95.4 83.8 10.0 1.2 BETTER b. Omega angle st dev 186 2.7 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 127 .9 .8 .2 .2 Inside f. Overall G-factor 188 .2 -.4 .3 2.1 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 18 8.5 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 51 10.1 19.0 5.3 -1.7 BETTER c. Chi-1 gauche plus st dev 63 7.8 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 132 9.6 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 56 6.6 20.4 5.0 -2.8 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% 95.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 2 Residue-by-residue listing for refined_3 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .14 Chi1-chi2 distribution -.01 Chi1 only .11 Chi3 & chi4 .22 Omega .20 ------ .14 ===== Main-chain covalent forces:- Main-chain bond lengths .35 Main-chain bond angles .41 ------ .39 ===== OVERALL AVERAGE .23 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.