Residue-by-residue listing for refined_16 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 - - - - - - - - - - - 180.9 - - - 2 SER 2 B 55.2 - - - - - - - - - 177.9 - 34.1 - 3 ASP 3 B - 187.3 - - - - - - - - 183.5 - 35.1 - 4 PRO 4 - - - - - -66.3 - - - - - 186.2 - 39.0 - * * * 5 GLY 5 h - - - - - - - - - - - 183.6 - - - 6 PRO 6 H - - - - - -66.8 -66.8 -39.2 - - - 179.5 - 38.4 - * * 7 GLU 7 H A 72.8 - - 168.6 - -76.5 -25.9 - - - 173.7 - 27.1 - * * +* +* 8 ALA 8 H A - - - - - -63.4 -38.6 - - - 174.9 - 33.8 - 9 ALA 9 H A - - - - - -65.9 -41.2 - - - 175.6 -1.9 33.8 - 10 ARG 10 H A - 177.3 - 179.9 - -57.5 -40.0 - - - 179.3 -2.2 35.0 - 11 LEU 11 H A - 172.9 - - - -62.8 -47.5 - - - 178.3 -2.4 35.1 - 12 ARG 12 H A - - -56.0 178.3 - -60.1 -42.4 - - - 177.0 -2.1 35.4 - 13 PHE 13 H A - 170.3 - - - -59.7 -48.8 - - - 177.6 -2.7 34.8 - 14 ARG 14 H A - - -75.3 181.0 - -70.6 -24.4 - - - 179.6 -3.0 33.0 - * * * 15 CYS 15 h A - - -62.7 - - - - - - - 176.0 -1.9 32.4 - 16 PHE 16 t B - 177.7 - - - - - - - - 177.6 -1.0 35.2 - * * 17 HIS 17 B 78.9 - - - - - - - - - 172.5 - 33.2 - * * 18 TYR 18 B - 167.9 - - - - - - - - 178.9 -.8 31.8 - +* +* 19 GLU 19 t B 51.2 - - 176.5 - - - - - - 180.2 -.6 32.9 - +* +* Residue-by-residue listing for refined_16 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 GLU 20 T A - - -54.7 - - - - - - - 179.9 -.6 34.6 - +* +* 21 ALA 21 T A - - - - - - - - - - 181.0 - 34.3 - 22 THR 22 T A - 201.1 - - - - - - - - 180.6 -2.0 34.3 - * * 23 GLY 23 h - - - - - - - - - - - 183.6 -1.2 - - * * 24 PRO 24 H - - - - - -78.6 -78.6 -35.3 - - - 186.4 - 39.5 - * * * +* +* 25 GLN 25 H A - 193.8 - 169.4 - -77.9 -32.5 - - - 175.9 - 35.0 - * * 26 GLU 26 H A - 180.7 - 165.2 - -75.1 -37.1 - - - 175.1 - 32.7 - 27 ALA 27 H A - - - - - -58.9 -38.2 - - - 177.1 -1.5 34.6 - 28 LEU 28 H A - - -63.0 179.4 - -57.6 -39.6 - - - 180.1 -1.8 33.6 - 29 ALA 29 H A - - - - - -60.6 -38.2 - - - 178.5 -1.0 34.0 - * * 30 GLN 30 H A - - -81.2 - - -75.8 -40.9 - - - 178.0 -1.3 33.6 - * * 31 LEU 31 H A - - -71.2 171.4 - -66.1 -44.7 - - - 178.4 -2.8 32.2 - * * 32 ARG 32 H A 57.9 - - 176.2 - -65.1 -29.7 - - - 175.5 -3.6 31.1 - ** ** 33 GLU 33 H A - 174.4 - 176.3 - -66.9 -48.3 - - - 181.6 -1.0 34.7 - * * 34 LEU 34 H A - - -62.1 173.8 - -69.3 -42.7 - - - 179.9 -2.2 33.4 - 35 CYS 35 H A 68.4 - - - - -66.4 -35.0 - - - 175.2 -3.4 33.0 - +* +* 36 ARG 36 H A - 172.5 - - - -61.8 -32.0 - - - 179.0 -1.6 31.9 - 37 GLN 37 H A - - -59.3 187.1 - -73.6 -17.7 - - - 180.4 -1.1 34.2 - +* * +* 38 TRP 38 H a - 165.4 - - - -94.7 -59.5 - - - 181.9 -.7 34.9 - * ** +* +* ** 39 LEU 39 H A - - -62.7 160.1 - -72.1 -42.4 - - - 175.5 -3.6 34.5 - ** ** 40 ARG 40 h l - - -53.8 177.6 - - - - - - 179.8 -1.3 33.1 - * * 41 PRO 41 T - - - - - -65.6 - - - - - 182.6 - 38.8 - * * 42 GLU 42 T A - 182.8 - 178.3 - - - - - - 183.5 - 34.6 - 43 VAL 43 T A - - -60.3 - - - - - - - 180.8 - 32.7 - 44 ARG 44 t B - - -68.4 184.4 - - - - - - 180.6 -2.9 32.0 - * * 45 SER 45 h B 58.4 - - - - - - - - - 179.5 - 35.9 - 46 LYS 46 H A - - -60.6 167.0 - -68.1 -30.4 - - - 179.8 - 37.2 - 47 GLU 47 H A - 180.9 - 179.8 - -63.4 -44.3 - - - 178.5 - 35.6 - 48 GLN 48 H A - - -62.7 - - -62.8 -33.6 - - - 178.6 - 34.0 - 49 MET 49 H A - - -60.5 180.5 - -69.6 -39.8 - - - 173.2 -1.1 32.5 - * * * 50 LEU 50 H A - - -66.8 180.4 - -55.6 -52.4 - - - 181.4 -2.0 34.3 - * * 51 GLU 51 H A - - -56.8 - - -54.8 -51.8 - - - 180.4 -2.4 34.7 - * * 52 LEU 52 H A - - -63.9 174.2 - -60.5 -43.3 - - - 182.4 -2.7 34.4 - 53 LEU 53 H A - 180.8 - - - -75.2 -30.6 - - - 173.3 -2.7 30.8 - * * 54 VAL 54 H A - 182.6 - - - -62.5 -44.4 - - - 177.3 -2.8 33.8 - 55 LEU 55 H A - 177.8 - - - -58.7 -43.6 - - - 181.6 -2.3 36.3 - Residue-by-residue listing for refined_16 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 - 183.0 - - - -56.9 -49.7 - - - 180.7 -2.1 33.7 - 57 GLN 57 H A - 188.6 - - - -74.0 -45.1 - - - 182.4 -2.1 33.0 - 58 PHE 58 H A - 178.9 - - - -53.6 -45.5 - - - 180.3 -3.0 33.9 - * * 59 LEU 59 H A - - -63.8 185.5 - -65.4 -35.3 - - - 178.3 -2.8 31.4 - 60 GLY 60 H - - - - - - -81.0 -21.7 - - - 177.4 -1.1 - - * +* * +* 61 ALA 61 H A - - - - - -69.1 -28.0 - - - 175.4 -2.1 33.9 - * * 62 LEU 62 h B - - -64.2 170.0 - - - - - - 176.3 -1.2 37.4 - * * 63 PRO 63 h - - - - - -72.0 - - - - - 183.0 - 38.2 - * * 64 PRO 64 H - - - - - -42.2 -42.2 -44.7 - - - 180.8 - 38.8 - ** +* * ** 65 GLU 65 H A 55.8 - - 187.6 - -61.5 -47.7 - - - 179.1 - 32.5 - 66 ILE 66 H A - - -59.2 180.4 - -73.3 -42.1 - - - 180.8 -.6 34.7 - +* +* 67 GLN 67 H A - 177.3 - 176.9 - -58.1 -42.7 - - - 180.6 -3.4 34.4 - +* +* 68 ALA 68 H A - - - - - -63.2 -33.5 - - - 180.3 -2.7 33.6 - 69 ARG 69 H A - - -58.0 - - -66.8 -41.4 - - - 177.5 -.9 34.1 - +* +* 70 VAL 70 H A - 167.9 - - - -56.8 -44.0 - - - 184.9 -1.5 36.2 - 71 GLN 71 H A - - -51.4 - - -58.3 -31.7 - - - 178.6 -1.5 35.3 - * * 72 GLY 72 h - - - - - - - - - - - 183.8 -.9 - - +* +* 73 GLN 73 T a - - -55.4 181.2 - - - - - - 180.5 -2.0 35.0 - 74 ARG 74 t l - - -62.0 - - - - - - - 179.9 -3.3 30.4 - +* * +* 75 PRO 75 - - - - - -67.7 - - - - - 182.7 - 39.0 - * * 76 GLY 76 S - - - - - - - - - - - 180.4 - - - 77 SER 77 h B - - -55.3 - - - - - - - 185.4 - 34.1 - 78 PRO 78 H - - - - - -59.1 -59.1 -44.9 - - - 182.7 - 38.1 - * * 79 GLU 79 H A - - -60.6 178.1 - -74.1 -28.7 - - - 174.2 - 30.3 - * * * 80 GLU 80 H A - 187.3 - - - -65.7 -45.5 - - - 176.3 - 35.8 - 81 ALA 81 H A - - - - - -58.7 -42.6 - - - 179.0 -2.4 34.6 - 82 ALA 82 H A - - - - - -59.5 -37.8 - - - 178.7 -2.4 34.1 - 83 ALA 83 H A - - - - - -73.3 -31.9 - - - 179.3 -1.7 33.5 - 84 LEU 84 H A - - -44.9 181.4 - -68.5 -49.9 - - - 185.1 -1.7 37.4 - * * * 85 VAL 85 H A - - -58.4 - - -70.4 -30.3 - - - 175.1 -2.9 29.6 - * * * 86 ASP 86 H A - 172.6 - - - -50.2 -38.9 - - - 177.7 -1.7 33.3 - * * 87 GLY 87 H - - - - - - -82.9 -36.9 - - - 181.8 -.9 - - * +* +* 88 LEU 88 H A - - -60.0 174.3 - -65.7 -34.4 - - - 181.0 -1.5 34.8 - 89 ARG 89 h A 61.0 - - 173.6 - - - - - - 183.6 -3.1 34.3 - * * 90 ARG 90 t B - - -52.4 182.4 - - - - - - 181.4 -.9 34.3 - * * 91 GLU 91 t B - 197.5 - - - - - - - - 179.6 - 36.1 - Residue-by-residue listing for refined_16 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 T - - - - - -58.8 - - - - - 179.9 - 38.6 - * * 93 GLY 93 T - - - - - - - - - - - 180.9 - - - 94 GLY 94 t - - - - - - - - - - - - -1.7 - - 95 GLY 301 - - - - - - - - - - - 180.4 - - - 96 SER 302 B 54.0 - - - - - - - - - 177.1 - 34.9 - 97 ASP 303 B - 183.2 - - - - - - - - 181.7 - 34.6 - 98 PRO 304 - - - - - -60.4 - - - - - 184.3 - 38.4 - * * 99 GLY 305 h - - - - - - - - - - - 179.8 - - - 100 PRO 306 H - - - - - -57.3 -57.3 -27.9 - - - 178.5 - 38.9 - * * * 101 GLU 307 H A 60.6 - - 179.7 - -63.7 -35.8 - - - 179.6 - 34.1 - 102 ALA 308 H A - - - - - -75.6 -32.9 - - - 176.0 -1.3 33.9 - 103 ALA 309 H A - - - - - -63.3 -47.5 - - - 178.7 -1.4 35.0 - 104 ARG 310 H A - 188.0 - 190.8 - -63.4 -33.7 - - - 181.3 -2.6 34.9 - 105 LEU 311 H A - 175.8 - - - -61.0 -40.8 - - - 176.3 -1.5 34.4 - 106 ARG 312 H A - - -58.9 179.9 - -70.2 -49.2 - - - 184.5 -1.6 36.7 - 107 PHE 313 H A - 172.5 - - - -60.8 -46.3 - - - 187.3 -2.5 34.9 - * * 108 ARG 314 H A - 193.3 - - - -81.8 -15.1 - - - 178.2 -3.8 33.5 - * ** ** ** 109 CYS 315 H A - - -58.2 - - -96.9 -4.9 - - - 179.3 -.7 33.5 - +** *** +* *** 110 PHE 316 h B - 178.6 - - - - - - - - 178.7 -.7 34.7 - +* +* 111 HIS 317 B 74.7 - - - - - - - - - 172.6 - 34.5 - * * 112 TYR 318 B - 167.4 - - - - - - - - 179.9 -1.5 32.8 - 113 GLU 319 t B 46.7 - - 176.8 - - - - - - 182.4 -.6 32.2 - * +* +* 114 GLU 320 T A - - -49.5 - - - - - - - 180.3 -.6 34.6 - * +* +* 115 ALA 321 T A - - - - - - - - - - 183.0 - 34.1 - 116 THR 322 T A - 202.8 - - - - - - - - 182.3 -1.2 34.8 - * * * 117 GLY 323 h - - - - - - - - - - - 183.9 -1.0 - - * * 118 PRO 324 H - - - - - -63.0 -63.0 -32.3 - - - 180.3 - 38.2 - * * 119 GLN 325 H A - - -85.4 - - -69.8 -39.9 - - - 179.2 - 33.2 - * * 120 GLU 326 H A - 181.7 - 172.1 - -72.2 -36.3 - - - 175.2 - 33.2 - 121 ALA 327 H A - - - - - -60.6 -40.9 - - - 176.1 -2.6 34.0 - 122 LEU 328 H A - - -66.9 176.9 - -62.3 -37.3 - - - 178.7 -2.1 33.9 - 123 ALA 329 H A - - - - - -63.5 -33.1 - - - 177.5 -1.4 33.4 - 124 GLN 330 H A - - -50.4 - - -68.6 -51.9 - - - 183.8 -1.5 37.1 - * * * 125 LEU 331 H A - - -67.0 172.6 - -63.7 -45.5 - - - 187.8 -2.6 35.3 - * * 126 ARG 332 H A 68.7 - - 190.8 - -65.1 -29.0 - - - 174.9 -3.6 28.4 - ** +* ** 127 GLU 333 H A 72.4 - - 182.8 - -79.2 -37.0 - - - 182.2 -.8 31.8 - * +* +* 128 LEU 334 H A - - -62.5 177.2 - -63.2 -46.1 - - - 179.8 -1.4 33.9 - 129 CYS 335 H A 63.9 - - - - -64.0 -34.4 - - - 178.3 -3.2 34.0 - +* +* Residue-by-residue listing for refined_16 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 - 171.1 - - - -69.9 -30.0 - - - 177.2 -.9 29.9 - +* * +* 131 GLN 337 H A - - -44.8 - - -71.2 -21.1 - - - 182.5 -1.5 36.3 - * +* +* 132 TRP 338 H a - 166.9 - - - -91.7 -58.4 - - - 182.1 -.9 34.9 - ** +* +* ** 133 LEU 339 H A - - -61.0 161.0 - -73.4 -38.7 - - - 175.8 -3.6 34.7 - ** ** 134 ARG 340 h l - - -58.0 178.0 - - - - - - 177.1 -1.4 32.8 - 135 PRO 341 T - - - - - -61.8 - - - - - 181.7 - 39.4 - +* +* 136 GLU 342 T A - 190.6 - - - - - - - - 183.1 - 35.1 - 137 VAL 343 T A - - -61.1 - - - - - - - 179.9 -.8 32.1 - +* +* 138 ARG 344 t B - - -69.0 182.8 - - - - - - 180.9 -3.4 32.1 - +* +* 139 SER 345 h B 55.7 - - - - - - - - - 175.7 - 36.3 - 140 LYS 346 H A - - -65.4 169.7 - -55.5 -38.4 - - - 180.6 - 36.6 - 141 GLU 347 H A - 178.4 - 176.3 - -53.0 -45.6 - - - 178.3 - 34.8 - * * 142 GLN 348 H A - - -72.2 - - -64.6 -31.3 - - - 180.6 -.6 33.3 - +* +* 143 MET 349 H A - - -58.0 181.1 - -69.2 -38.4 - - - 172.4 -1.0 32.5 - * * * 144 LEU 350 H A - - -72.8 - - -58.2 -51.3 - - - 182.5 -1.8 33.0 - * * 145 GLU 351 H A - - -63.1 - - -53.3 -53.8 - - - 182.0 -2.1 36.4 - * * * 146 LEU 352 H A - - -62.2 176.2 - -60.6 -43.0 - - - 183.1 -2.8 34.8 - 147 LEU 353 H A - 181.9 - - - -77.2 -30.4 - - - 174.7 -2.2 31.6 - 148 VAL 354 H A - 180.9 - - - -60.8 -44.5 - - - 178.6 -2.8 34.1 - * * 149 LEU 355 H A - 177.2 - - - -55.9 -47.8 - - - 183.8 -2.0 36.4 - 150 GLU 356 H A - 187.1 - - - -53.1 -52.2 - - - 180.7 -1.6 34.1 - * * * 151 GLN 357 H A - 189.3 - - - -73.7 -41.2 - - - 181.4 -1.7 33.2 - 152 PHE 358 H A - 172.6 - - - -53.1 -46.0 - - - 181.2 -2.8 34.1 - * * 153 LEU 359 H A - - -60.2 184.7 - -63.0 -36.1 - - - 180.3 -3.0 32.0 - * * 154 GLY 360 H - - - - - - -80.3 -23.7 - - - 177.8 -1.1 - - * * * * 155 ALA 361 H A - - - - - -68.6 -26.3 - - - 177.6 -2.0 33.2 - * * 156 LEU 362 h B - - -64.5 170.5 - - - - - - 175.0 -1.2 37.0 - * * 157 PRO 363 h - - - - - -66.8 - - - - - 182.1 - 39.7 - +* +* 158 PRO 364 H - - - - - -44.4 -44.4 -45.3 - - - 181.8 - 38.7 - +* +* * +* 159 GLU 365 H A 58.2 - - 189.9 - -65.7 -47.5 - - - 179.6 - 31.3 - 160 ILE 366 H A - - -58.0 179.3 - -69.0 -41.3 - - - 181.7 - 34.4 - 161 GLN 367 H A - 179.0 - 175.5 - -61.2 -47.2 - - - 181.1 -3.3 34.1 - +* +* 162 ALA 368 H A - - - - - -66.8 -34.5 - - - 176.3 -2.7 32.7 - 163 ARG 369 H A - - -72.7 - - -60.3 -41.4 - - - 175.1 -1.6 33.2 - Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 164 VAL 370 H A - 168.9 - - - -58.1 -51.0 - - - 184.4 -1.9 35.2 - * * 165 GLN 371 H A - - -52.1 - - -58.7 -35.9 - - - 179.3 -2.1 33.8 - 166 GLY 372 H - - - - - - -64.5 -26.0 - - - 180.9 -2.0 - - * * 167 GLN 373 H a - - -49.5 193.8 - -101.1 -45.5 - - - 187.2 -1.4 35.1 - * *** * *** 168 ARG 374 h l - - -69.3 - - - - - - - 179.4 -3.6 31.2 - ** ** 169 PRO 375 - - - - - -62.5 - - - - - 178.1 - 38.7 - * * 170 GLY 376 - - - - - - - - - - - 178.5 - - - 171 SER 377 h B - - -57.0 - - - - - - - 182.0 - 34.7 - 172 PRO 378 H - - - - - -60.1 -60.1 -44.5 - - - 179.5 - 37.1 - 173 GLU 379 H A - - -62.9 166.6 - -69.0 -29.8 - - - 177.9 - 33.7 - 174 GLU 380 H A - 189.6 - - - -69.6 -42.9 - - - 176.1 - 34.9 - 175 ALA 381 H A - - - - - -61.1 -42.1 - - - 179.0 -2.4 34.2 - 176 ALA 382 H A - - - - - -55.6 -31.9 - - - 179.7 -2.5 34.1 - 177 ALA 383 H A - - - - - -64.0 -49.7 - - - 177.3 -1.1 33.1 - * * 178 LEU 384 H A 46.4 - - 156.9 - -73.2 -42.8 - - - 180.5 -1.2 30.2 - * * * * * 179 VAL 385 H A - 174.7 - - - -58.8 -36.2 - - - 178.6 -3.2 33.2 - +* +* 180 ASP 386 H A - 187.0 - - - -57.5 -35.5 - - - 177.0 -2.3 33.9 - 181 GLY 387 H - - - - - - -84.4 -41.2 - - - 181.6 -1.0 - - +* * +* 182 LEU 388 H A - - -61.8 175.3 - -65.8 -19.9 - - - 180.3 -2.7 34.4 - +* +* 183 ARG 389 h A 63.4 - - 172.0 - - - - - - 182.0 -1.9 34.3 - 184 ARG 390 t B - - -55.0 179.1 - - - - - - 182.1 -1.7 33.3 - 185 GLU 391 B - 181.1 - - - - - - - - 181.2 -.8 35.5 - +* +* 186 PRO 392 - - - - - -70.8 - - - - - 177.3 - 38.2 - * * 187 GLY 393 - - - - - - - - - - - 179.5 -.8 - - +* +* 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * * ** *** *** * ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.2 180.4 -61.2 177.1 -62.4 -65.9 -38.9 - - - 179.7 -1.9 34.4 Standard deviations: 9.1 8.8 7.6 7.3 8.8 9.5 8.9 - - - 3.0 .9 2.2 Numbers of values: 20 50 62 61 18 123 123 0 0 0 186 127 170 0 Residue-by-residue listing for refined_16 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_16 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 - 1.232 1.493 - 1.455 - 116.98 120.14 - 110.29 - 122.87 * * 2 SER 2 1.307 1.246 1.517 1.529 1.431 121.04 116.21 120.85 111.21 110.75 109.83 122.93 +* * +* 3 ASP 3 1.307 1.237 1.519 1.529 1.443 121.15 118.19 119.93 109.84 107.47 110.53 121.88 +* * +* 4 PRO 4 1.339 1.233 1.533 1.537 1.472 122.81 116.97 120.40 109.73 113.82 103.27 122.60 5 GLY 5 1.316 1.239 1.518 - 1.438 120.23 119.37 119.66 - 109.59 - 120.95 * * * * 6 PRO 6 1.340 1.225 1.530 1.538 1.451 121.30 119.18 119.45 110.14 113.48 103.94 121.25 +* +* 7 GLU 7 1.332 1.221 1.507 1.530 1.442 117.54 116.29 120.54 112.77 111.29 117.25 123.16 ** * +*** +*** 8 ALA 8 1.324 1.227 1.524 1.513 1.447 121.13 115.80 121.03 110.75 108.62 111.01 123.15 9 ALA 9 1.330 1.230 1.524 1.517 1.452 121.91 115.78 120.82 110.64 109.29 110.87 123.39 10 ARG 10 1.338 1.225 1.530 1.531 1.464 122.91 115.67 121.21 108.79 110.42 110.79 123.12 11 LEU 11 1.320 1.218 1.526 1.526 1.407 123.72 116.28 120.29 111.76 110.15 108.11 123.41 +** * * +** 12 ARG 12 1.329 1.231 1.530 1.528 1.474 122.77 114.35 121.62 109.62 109.37 109.55 124.01 13 PHE 13 1.311 1.215 1.542 1.532 1.452 125.15 116.99 120.60 113.06 111.32 106.49 122.39 * +* +* ** ** 14 ARG 14 1.319 1.229 1.533 1.520 1.466 121.78 117.11 120.49 109.40 112.90 111.97 122.40 Residue-by-residue listing for refined_16 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 1.322 1.244 1.522 1.530 1.462 121.62 116.13 120.79 111.02 111.67 111.78 123.08 16 PHE 16 1.315 1.240 1.510 1.535 1.436 121.68 117.34 120.40 109.73 108.58 110.37 122.24 * * * 17 HIS 17 1.309 1.239 1.491 1.575 1.437 118.60 117.48 119.90 109.97 107.76 113.92 122.58 * +* ** * +* * ** ** 18 TYR 18 1.285 1.224 1.490 1.526 1.411 118.39 115.09 120.98 111.26 108.18 114.15 123.85 *** +* ** +* * ** *** 19 GLU 19 1.278 1.240 1.507 1.531 1.403 122.23 115.34 121.12 112.73 109.79 110.48 123.51 +*** +** * +*** 20 GLU 20 1.322 1.230 1.516 1.538 1.466 123.40 114.72 121.14 108.42 110.72 111.72 124.13 21 ALA 21 1.312 1.233 1.538 1.514 1.450 124.35 118.01 119.91 110.15 113.17 109.44 122.08 * * * 22 THR 22 1.332 1.226 1.543 1.577 1.452 119.60 115.85 121.38 110.66 109.05 110.85 122.69 * * * 23 GLY 23 1.327 1.231 1.507 - 1.448 120.84 119.14 119.88 - 111.65 - 120.96 * * * 24 PRO 24 1.342 1.222 1.513 1.520 1.450 121.47 115.13 121.51 110.10 112.13 102.61 123.33 * * * 25 GLN 25 1.293 1.227 1.509 1.492 1.402 123.44 115.98 120.94 113.45 109.76 106.33 123.05 +** +* +** +* ** +** 26 GLU 26 1.319 1.223 1.511 1.520 1.432 121.05 116.03 120.83 112.60 109.16 110.81 123.10 * * * 27 ALA 27 1.324 1.227 1.521 1.517 1.454 122.09 116.06 120.61 110.23 109.43 110.08 123.30 28 LEU 28 1.335 1.207 1.520 1.535 1.459 122.34 117.22 119.82 109.26 111.25 112.16 122.95 * * 29 ALA 29 1.337 1.235 1.526 1.520 1.473 122.22 115.40 121.17 110.08 110.70 110.67 123.42 30 GLN 30 1.313 1.228 1.526 1.549 1.443 123.18 116.23 120.67 111.95 110.66 109.94 123.08 * * 31 LEU 31 1.316 1.219 1.517 1.524 1.459 122.40 117.49 119.79 111.52 112.60 111.14 122.72 32 ARG 32 1.333 1.214 1.515 1.536 1.465 120.92 116.10 120.94 111.51 111.11 113.32 122.95 +* +* 33 GLU 33 1.309 1.231 1.527 1.526 1.439 121.95 115.62 121.01 110.97 109.82 109.34 123.34 * * 34 LEU 34 1.312 1.232 1.523 1.524 1.446 122.55 117.18 120.17 111.36 111.94 110.00 122.63 * * 35 CYS 35 1.328 1.218 1.535 1.543 1.449 120.73 116.77 120.74 111.43 109.59 111.40 122.49 36 ARG 36 1.337 1.214 1.536 1.548 1.435 122.71 117.86 119.94 113.77 112.44 109.66 122.18 * +* +* 37 GLN 37 1.323 1.239 1.529 1.510 1.470 120.94 114.25 121.79 110.01 110.66 110.24 123.95 38 TRP 38 1.305 1.232 1.549 1.549 1.439 125.07 116.00 120.83 112.62 111.35 107.03 123.16 +* * * +* * ** ** 39 LEU 39 1.312 1.227 1.520 1.524 1.462 123.61 115.64 120.45 111.92 111.07 108.18 123.91 * * * * 40 ARG 40 1.334 1.220 1.535 1.536 1.465 124.22 118.51 120.45 110.28 113.19 111.05 121.03 * * * * 41 PRO 41 1.344 1.220 1.521 1.536 1.471 122.37 116.01 121.12 110.05 112.22 103.61 122.86 42 GLU 42 1.304 1.235 1.529 1.514 1.437 122.08 116.92 120.58 110.95 111.47 108.82 122.48 +* * +* 43 VAL 43 1.322 1.231 1.525 1.554 1.461 120.55 117.25 120.19 109.81 113.14 112.25 122.56 44 ARG 44 1.314 1.226 1.507 1.523 1.457 121.03 115.03 121.11 110.13 112.96 112.80 123.86 * * * 45 SER 45 1.312 1.245 1.533 1.529 1.434 123.57 114.99 121.41 110.12 111.30 108.10 123.57 * * * * * 46 LYS 46 1.321 1.232 1.523 1.519 1.462 124.28 114.29 121.97 108.90 109.20 107.59 123.73 * +* +* Residue-by-residue listing for refined_16 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 1.312 1.227 1.518 1.524 1.446 123.88 115.09 121.38 110.30 109.45 108.71 123.50 * * * * 48 GLN 48 1.320 1.228 1.517 1.526 1.452 122.36 116.17 120.69 110.41 110.85 110.48 123.14 49 MET 49 1.320 1.233 1.496 1.498 1.448 121.58 116.47 119.96 111.83 111.15 110.90 123.57 * +* +* 50 LEU 50 1.341 1.214 1.519 1.550 1.453 120.95 116.08 120.19 108.37 108.94 112.99 123.66 * * * 51 GLU 51 1.337 1.244 1.538 1.540 1.474 122.97 116.29 120.64 109.15 111.27 110.60 123.06 52 LEU 52 1.331 1.227 1.514 1.526 1.451 122.46 116.63 120.63 109.56 111.81 110.53 122.73 53 LEU 53 1.312 1.236 1.543 1.519 1.427 121.10 117.92 119.99 115.11 112.82 109.37 122.07 * +* +** +** 54 VAL 54 1.336 1.219 1.527 1.564 1.468 119.82 115.03 121.20 108.75 107.65 113.63 123.72 * * * * 55 LEU 55 1.333 1.234 1.524 1.529 1.462 123.50 115.39 120.78 108.33 110.49 109.25 123.83 56 GLU 56 1.324 1.244 1.531 1.550 1.454 123.26 116.49 120.75 110.75 111.58 110.59 122.75 * * 57 GLN 57 1.318 1.222 1.513 1.543 1.443 120.42 116.35 119.88 112.27 109.73 110.73 123.73 * * 58 PHE 58 1.331 1.238 1.519 1.535 1.463 122.89 116.64 120.60 110.31 111.92 110.46 122.75 59 LEU 59 1.320 1.223 1.519 1.527 1.447 120.46 116.94 120.36 111.78 112.45 112.14 122.69 60 GLY 60 1.316 1.232 1.513 - 1.445 119.76 116.01 120.82 - 112.02 - 123.16 61 ALA 61 1.326 1.233 1.517 1.528 1.449 122.67 115.60 120.70 110.71 109.92 110.68 123.68 62 LEU 62 1.332 1.240 1.528 1.525 1.455 123.69 118.44 120.00 107.45 109.71 108.77 121.55 * * * * * 63 PRO 63 1.341 1.235 1.522 1.533 1.446 121.35 118.46 119.01 110.58 108.88 104.79 122.53 * * * * +* +* 64 PRO 64 1.356 1.226 1.533 1.524 1.483 123.81 116.11 120.53 110.27 113.67 102.85 123.32 * * 65 GLU 65 1.324 1.229 1.554 1.541 1.458 122.58 117.32 120.51 112.82 112.60 109.54 122.13 * * * 66 ILE 66 1.328 1.240 1.531 1.549 1.456 121.81 115.15 121.29 109.89 110.23 110.39 123.54 67 GLN 67 1.322 1.235 1.528 1.531 1.454 123.48 116.07 120.59 111.03 111.33 109.16 123.33 68 ALA 68 1.325 1.236 1.529 1.519 1.462 122.67 116.73 120.44 110.24 112.08 110.60 122.82 69 ARG 69 1.325 1.231 1.526 1.528 1.463 121.38 115.62 120.99 110.03 109.83 110.96 123.37 70 VAL 70 1.324 1.236 1.510 1.540 1.466 123.07 115.35 120.82 106.97 111.46 110.82 123.82 71 GLN 71 1.313 1.230 1.539 1.518 1.450 122.65 116.07 121.16 109.27 110.67 109.68 122.77 * * 72 GLY 72 1.320 1.232 1.530 - 1.450 121.30 117.28 120.37 - 113.45 - 122.34 73 GLN 73 1.326 1.239 1.517 1.526 1.455 121.37 114.74 121.15 109.78 110.16 109.92 124.09 74 ARG 74 1.325 1.238 1.532 1.528 1.459 124.64 116.43 121.25 112.27 113.09 112.61 122.28 +* * * +* 75 PRO 75 1.343 1.230 1.537 1.533 1.472 123.15 116.14 120.89 109.37 113.59 103.63 122.97 76 GLY 76 1.311 1.226 1.517 - 1.443 121.54 116.93 120.73 - 112.73 - 122.33 * * 77 SER 77 1.318 1.241 1.553 1.532 1.452 122.04 118.15 119.88 111.59 109.71 109.49 121.97 * * 78 PRO 78 1.365 1.222 1.528 1.537 1.485 123.39 117.16 120.43 109.56 114.79 104.43 122.40 +* * * * +* 79 GLU 79 1.307 1.235 1.509 1.531 1.457 121.71 115.92 120.79 114.12 111.20 111.80 123.29 +* ** ** 80 GLU 80 1.323 1.219 1.533 1.528 1.428 122.02 115.52 121.13 110.32 106.77 109.17 123.30 +* +* +* 81 ALA 81 1.348 1.223 1.518 1.508 1.454 122.86 115.76 120.75 109.76 110.64 110.14 123.48 * * 82 ALA 82 1.326 1.221 1.527 1.523 1.454 122.91 115.72 121.21 110.60 110.93 110.05 123.07 Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 83 ALA 83 1.292 1.235 1.531 1.521 1.446 122.52 116.99 120.38 110.96 111.08 110.49 122.62 +** +** 84 LEU 84 1.342 1.237 1.512 1.540 1.463 120.78 114.18 121.93 104.58 107.97 112.03 123.85 * +** * +** 85 VAL 85 1.323 1.219 1.503 1.536 1.438 122.93 116.70 120.02 112.23 112.94 113.96 123.25 * * * * * 86 ASP 86 1.324 1.227 1.523 1.530 1.472 121.97 116.36 120.56 109.53 111.49 112.05 123.06 87 GLY 87 1.315 1.230 1.512 - 1.437 120.33 115.70 120.84 - 111.84 - 123.44 88 LEU 88 1.321 1.222 1.530 1.527 1.469 123.25 116.71 120.48 109.32 112.18 109.97 122.80 89 ARG 89 1.332 1.222 1.520 1.543 1.471 121.96 116.77 120.49 108.58 111.53 111.72 122.74 90 ARG 90 1.306 1.237 1.502 1.520 1.434 120.75 116.00 120.74 110.86 108.95 110.38 123.24 +* * * +* 91 GLU 91 1.296 1.239 1.535 1.532 1.425 121.64 118.59 119.59 110.16 107.41 108.79 121.75 ** +* * * * ** 92 PRO 92 1.346 1.240 1.528 1.534 1.472 122.88 115.90 120.93 110.10 112.22 103.81 123.16 93 GLY 93 1.317 1.229 1.510 - 1.437 120.93 116.08 120.89 - 111.61 - 123.03 94 GLY 94 1.312 1.241 1.508 - 1.446 121.26 - 120.08 - 111.98 - - * * 95 GLY 301 - 1.234 1.511 - 1.447 - 115.83 120.90 - 111.99 - 123.27 96 SER 302 1.309 1.234 1.525 1.535 1.446 122.18 116.90 120.20 110.67 110.35 109.25 122.91 * * 97 ASP 303 1.312 1.234 1.523 1.534 1.448 121.24 118.19 119.86 109.73 108.69 111.10 121.95 * * 98 PRO 304 1.338 1.242 1.538 1.536 1.475 122.97 116.64 120.66 109.97 113.70 103.79 122.66 99 GLY 305 1.312 1.232 1.517 - 1.434 120.47 118.47 119.88 - 111.23 - 121.65 * * * 100 PRO 306 1.352 1.235 1.530 1.530 1.481 123.10 115.60 121.35 110.03 111.87 103.26 123.04 * * 101 GLU 307 1.320 1.240 1.543 1.531 1.444 122.60 116.17 120.62 110.90 110.78 109.86 123.18 102 ALA 308 1.339 1.233 1.515 1.526 1.456 122.78 115.50 121.33 110.72 109.72 110.67 123.17 103 ALA 309 1.319 1.241 1.510 1.502 1.449 122.10 115.67 120.98 109.46 109.43 110.23 123.33 104 ARG 310 1.336 1.209 1.516 1.518 1.447 121.51 115.96 120.98 107.72 109.58 112.19 123.06 * * * 105 LEU 311 1.316 1.222 1.533 1.515 1.406 123.41 116.90 120.27 112.84 110.80 107.63 122.80 +** * +* +** 106 ARG 312 1.327 1.229 1.529 1.528 1.463 120.93 114.23 121.84 106.67 109.07 110.68 123.87 +* +* 107 PHE 313 1.314 1.214 1.528 1.539 1.457 124.74 116.79 120.83 111.16 113.45 107.77 122.36 * +* +* +* 108 ARG 314 1.298 1.225 1.534 1.537 1.444 121.58 117.19 120.50 112.21 111.76 109.15 122.30 ** * ** 109 CYS 315 1.318 1.243 1.530 1.528 1.458 120.72 115.72 121.01 110.59 110.35 111.07 123.26 110 PHE 316 1.331 1.240 1.520 1.543 1.450 122.70 116.44 120.84 110.51 109.77 109.98 122.70 111 HIS 317 1.306 1.232 1.502 1.574 1.443 120.43 117.59 119.88 109.33 108.24 112.35 122.52 +* * ** * * ** 112 TYR 318 1.295 1.221 1.497 1.524 1.425 118.94 115.31 120.97 111.58 108.34 112.10 123.65 ** * +* +* * ** 113 GLU 319 1.279 1.230 1.514 1.539 1.414 122.34 115.27 121.07 113.59 110.29 110.49 123.63 +*** ** +* +*** 114 GLU 320 1.327 1.221 1.510 1.543 1.469 123.64 115.48 120.63 107.86 110.71 112.38 123.89 * * * * 115 ALA 321 1.318 1.235 1.528 1.511 1.449 123.30 117.35 120.11 110.21 112.44 109.92 122.50 116 THR 322 1.332 1.212 1.535 1.587 1.446 120.14 116.24 121.06 110.46 108.40 110.67 122.58 +* +* Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 117 GLY 323 1.336 1.229 1.516 - 1.438 120.67 118.98 120.19 - 110.38 - 120.84 * * * 118 PRO 324 1.331 1.226 1.531 1.502 1.466 122.09 117.57 120.10 110.44 114.33 103.25 122.32 * * * 119 GLN 325 1.332 1.231 1.513 1.542 1.462 120.23 115.02 121.48 109.34 109.60 113.25 123.48 +* +* 120 GLU 326 1.307 1.228 1.527 1.524 1.441 122.21 116.42 120.67 112.20 110.23 110.05 122.90 +* * +* 121 ALA 327 1.328 1.227 1.524 1.520 1.463 122.11 116.17 120.82 110.47 109.74 110.58 122.99 122 LEU 328 1.326 1.210 1.502 1.513 1.455 121.60 116.65 120.28 109.03 111.05 111.88 123.07 * * * 123 ALA 329 1.321 1.231 1.526 1.521 1.453 121.62 116.05 120.84 111.07 110.26 110.80 123.11 124 GLN 330 1.325 1.229 1.526 1.544 1.457 121.87 113.92 121.84 107.13 107.81 110.09 124.18 * +* * +* 125 LEU 331 1.317 1.226 1.517 1.528 1.456 124.88 116.93 120.14 109.28 114.16 108.87 122.93 +* * +* 126 ARG 332 1.313 1.228 1.526 1.535 1.451 121.35 118.48 119.98 113.89 114.32 112.95 121.53 * * +* * * +* 127 GLU 333 1.331 1.212 1.529 1.553 1.450 117.31 116.19 120.63 111.04 108.42 114.09 123.10 * ** ** ** 128 LEU 334 1.338 1.231 1.512 1.532 1.465 122.95 116.48 120.36 109.74 111.74 111.07 123.15 129 CYS 335 1.322 1.219 1.527 1.533 1.448 121.42 116.08 121.15 110.80 109.66 110.49 122.75 130 ARG 336 1.324 1.209 1.536 1.548 1.425 122.47 117.75 119.90 115.33 112.39 110.76 122.31 * +* +** +** 131 GLN 337 1.333 1.231 1.547 1.536 1.485 120.99 114.72 121.77 106.28 108.39 111.53 123.48 * * ** * ** 132 TRP 338 1.313 1.233 1.541 1.555 1.453 124.97 115.94 120.96 112.69 111.73 106.90 123.09 * * +* * ** ** 133 LEU 339 1.302 1.227 1.530 1.523 1.457 123.24 115.18 120.79 112.58 110.75 107.25 124.02 +* * +* +* 134 ARG 340 1.326 1.218 1.546 1.536 1.470 125.17 119.65 119.66 109.27 115.25 111.61 120.68 +* +* * * +* 135 PRO 341 1.350 1.239 1.535 1.532 1.482 122.66 116.67 120.61 108.96 113.36 103.43 122.72 * * 136 GLU 342 1.321 1.229 1.536 1.535 1.448 121.37 116.56 121.10 109.57 109.86 110.09 122.33 137 VAL 343 1.322 1.234 1.519 1.546 1.461 120.94 117.17 120.53 110.24 113.37 112.47 122.29 138 ARG 344 1.305 1.234 1.491 1.523 1.442 120.66 114.75 121.25 110.67 111.62 112.76 124.00 +* +* * +* 139 SER 345 1.291 1.247 1.518 1.524 1.416 123.12 115.11 121.04 110.09 110.50 107.82 123.84 +** ** +* +** 140 LYS 346 1.322 1.214 1.514 1.521 1.454 123.93 114.83 121.18 109.32 109.67 108.14 123.95 * * * 141 GLU 347 1.319 1.229 1.537 1.516 1.452 124.38 116.58 120.73 111.46 111.53 107.85 122.67 * +* +* 142 GLN 348 1.326 1.228 1.514 1.525 1.460 121.58 116.26 120.66 110.07 111.73 111.46 123.07 143 MET 349 1.312 1.232 1.512 1.505 1.444 121.75 116.63 120.08 112.40 110.91 110.43 123.29 * * * * 144 LEU 350 1.349 1.209 1.518 1.572 1.465 120.83 116.14 120.06 109.46 108.51 114.02 123.58 * * ** ** ** 145 GLU 351 1.343 1.243 1.530 1.536 1.485 123.45 115.64 121.01 107.55 111.42 109.58 123.35 * * * 146 LEU 352 1.319 1.231 1.522 1.527 1.442 122.89 116.15 120.89 110.22 111.68 109.31 122.94 147 LEU 353 1.307 1.235 1.549 1.515 1.423 121.47 117.68 120.12 114.96 112.92 108.42 122.20 +* * +* +** * +** Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 148 VAL 354 1.337 1.229 1.527 1.566 1.473 120.62 115.08 121.07 108.47 108.50 113.23 123.82 * * 149 LEU 355 1.334 1.228 1.519 1.528 1.463 123.48 115.09 120.81 108.09 110.75 109.34 124.10 * * 150 GLU 356 1.321 1.239 1.544 1.538 1.451 123.76 117.09 120.66 111.29 111.69 109.19 122.21 * * 151 GLN 357 1.322 1.235 1.515 1.541 1.456 120.28 116.27 119.77 111.79 109.66 110.86 123.90 152 PHE 358 1.345 1.238 1.512 1.551 1.464 122.60 116.12 120.69 109.52 111.29 111.31 123.18 * * * 153 LEU 359 1.318 1.214 1.513 1.524 1.439 121.02 116.83 120.25 111.51 112.23 111.73 122.88 154 GLY 360 1.311 1.229 1.513 - 1.442 119.87 116.69 120.34 - 112.54 - 122.97 * * 155 ALA 361 1.327 1.237 1.537 1.540 1.459 121.89 115.54 121.08 111.40 109.96 110.90 123.38 156 LEU 362 1.325 1.242 1.540 1.524 1.459 124.01 117.92 120.36 108.07 111.26 108.23 121.72 * * * * 157 PRO 363 1.356 1.236 1.518 1.541 1.459 122.41 118.39 119.08 108.91 108.86 104.11 122.52 * * * * 158 PRO 364 1.353 1.228 1.536 1.525 1.478 123.38 116.56 120.37 110.16 113.43 103.07 123.04 159 GLU 365 1.327 1.228 1.533 1.534 1.454 121.69 117.75 119.99 112.82 113.09 110.89 122.22 * * 160 ILE 366 1.331 1.238 1.534 1.549 1.452 120.48 115.23 121.26 109.58 109.86 111.18 123.47 161 GLN 367 1.322 1.234 1.523 1.526 1.451 123.04 116.58 120.53 110.69 111.77 109.74 122.88 162 ALA 368 1.320 1.241 1.529 1.521 1.456 121.38 116.68 120.37 111.20 111.23 111.32 122.95 163 ARG 369 1.336 1.238 1.505 1.525 1.470 121.35 115.26 120.90 110.19 110.26 111.95 123.83 164 VAL 370 1.321 1.232 1.501 1.539 1.442 122.42 115.65 120.59 107.39 110.68 112.13 123.76 * * 165 GLN 371 1.319 1.229 1.520 1.518 1.442 121.91 116.04 120.57 109.63 111.08 111.51 123.38 166 GLY 372 1.318 1.225 1.523 - 1.445 121.30 117.15 120.44 - 113.14 - 122.41 167 GLN 373 1.326 1.225 1.515 1.519 1.457 120.50 115.24 120.62 107.64 111.05 111.56 124.13 * * 168 ARG 374 1.336 1.233 1.540 1.537 1.463 124.24 117.35 120.74 110.49 111.51 114.02 121.85 * ** ** 169 PRO 375 1.354 1.220 1.538 1.536 1.478 122.88 115.99 120.99 110.12 112.63 103.52 123.01 170 GLY 376 1.318 1.228 1.522 - 1.458 121.77 116.67 120.44 - 113.22 - 122.83 171 SER 377 1.318 1.243 1.543 1.535 1.452 122.31 118.14 119.98 110.13 109.25 110.25 121.87 172 PRO 378 1.354 1.232 1.536 1.538 1.477 123.09 116.73 120.55 111.09 113.52 104.56 122.71 * * 173 GLU 379 1.317 1.231 1.516 1.515 1.466 122.50 115.85 120.89 111.88 110.45 109.39 123.25 174 GLU 380 1.324 1.218 1.522 1.522 1.436 121.75 116.22 120.81 110.14 108.32 110.31 122.95 * * * 175 ALA 381 1.345 1.220 1.509 1.515 1.446 121.52 115.58 120.73 110.47 109.52 110.61 123.64 * * 176 ALA 382 1.328 1.212 1.528 1.523 1.453 123.27 116.37 120.38 110.40 111.54 110.10 123.23 177 ALA 383 1.318 1.238 1.527 1.522 1.458 122.80 117.19 120.25 110.91 111.13 111.03 122.56 178 LEU 384 1.334 1.231 1.513 1.557 1.459 120.27 115.95 120.73 110.56 111.52 115.47 123.29 * +** +** 179 VAL 385 1.325 1.222 1.531 1.557 1.459 122.67 116.42 120.56 110.51 111.47 111.61 123.01 180 ASP 386 1.323 1.220 1.536 1.533 1.473 122.65 116.56 120.77 110.40 110.96 110.54 122.66 181 GLY 387 1.321 1.225 1.515 - 1.448 120.81 115.87 121.12 - 111.27 - 122.98 182 LEU 388 1.321 1.233 1.535 1.530 1.471 123.10 116.77 120.64 109.67 112.63 110.00 122.59 183 ARG 389 1.324 1.238 1.523 1.531 1.463 121.77 116.76 120.58 108.53 111.48 111.74 122.66 184 ARG 390 1.304 1.246 1.518 1.522 1.435 120.82 115.10 121.19 112.02 110.06 110.22 123.70 +* * * +* 185 GLU 391 1.308 1.236 1.530 1.544 1.441 123.68 117.92 120.28 110.70 108.10 109.02 121.73 +* * * +* Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 186 PRO 392 1.345 1.246 1.529 1.540 1.456 122.60 115.83 121.23 110.28 112.58 104.31 122.91 * * 187 GLY 393 1.309 1.237 1.509 - 1.447 121.50 115.01 121.61 - 110.57 - 123.37 * * 188 GLY 394 1.299 - 1.482 - 1.417 122.54 - - - 108.48 - - ** +* ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * +* ** +** ** +* * +** +* +*** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 1.278 1.349 1.321 .012 +*** * C-N (Pro) 1.341 .016 18 1.331 1.365 1.347 .008 +* C-O C-O 1.231 .020 187 1.207 1.247 1.230 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.490 1.554 1.524 .012 +* * CH2G*-C (Gly) 1.516 .018 18 1.482 1.530 1.512 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.502 1.540 1.519 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.536 1.587 1.555 .015 +* CH1E-CH2E (the rest) 1.530 .020 138 1.492 1.575 1.531 .012 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.402 1.485 1.451 .015 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.417 1.458 1.443 .009 ** N-CH1E (Pro) 1.466 .015 18 1.446 1.485 1.470 .012 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 2.0 152 113.92 119.65 116.28 1.03 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.01 119.37 117.01 1.29 * CH1E-C-N (Pro) 116.9 1.5 18 115.13 119.18 116.72 1.05 * +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.68 124.18 122.97 .70 * O-C-N (Pro) 122.0 1.4 18 121.25 123.33 122.74 .46 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.31 125.17 122.12 1.41 ** +* C-NH1-CH2G* (Gly) 120.6 1.7 16 119.76 122.54 120.94 .71 * C-N-CH1E (Pro) 122.6 5.0 18 121.30 123.81 122.65 .69 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.01 121.97 120.66 .52 * CH2G*-C-O (Gly) 120.8 2.1 17 119.66 121.61 120.49 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.46 111.40 110.52 .47 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.97 112.23 109.58 1.41 * CH2E-CH1E-C (the rest) 110.1 1.9 138 104.58 115.33 110.49 1.72 +** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 106.77 115.25 110.66 1.54 +* * NH1-CH2G*-C (Gly) 112.5 2.9 18 108.48 113.45 111.55 1.28 * N-CH1E-C (Pro) 111.8 2.5 18 108.86 114.79 112.73 1.57 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.44 111.32 110.51 .44 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.39 113.96 111.93 1.16 * N-CH1E-CH2E (Pro) 103.0 1.1 18 102.61 104.79 103.68 .58 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.33 117.25 110.51 1.84 ** +*** ------------------------------------------------------------------------------------------------------------- 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_16 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] 144 94.7% Residues in additional allowed regions [a,b,l,p] 8 5.3% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 94.7 83.8 10.0 1.1 BETTER b. Omega angle st dev 186 3.0 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 127 .9 .8 .2 .3 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 20 9.1 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 50 8.8 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 62 7.6 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 132 9.4 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 61 7.3 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 94.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 3 Residue-by-residue listing for refined_16 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .18 Chi1-chi2 distribution -.01 Chi1 only .05 Chi3 & chi4 .38 Omega .13 ------ .16 ===== Main-chain covalent forces:- Main-chain bond lengths .33 Main-chain bond angles .39 ------ .36 ===== OVERALL AVERAGE .23 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.