Residue-by-residue listing for refined_19 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.5 - - - 2 SER 2 B - - -60.7 - - - - - - - 173.1 - 34.8 - * * 3 ASP 3 B - - -66.4 - - - - - - - 181.8 - 33.5 - 4 PRO 4 - - - - - -56.6 - - - - - 181.1 - 38.0 - * * 5 GLY 5 h - - - - - - - - - - - 180.6 - - - 6 PRO 6 H - - - - - -56.4 -56.4 -30.3 - - - 179.4 - 38.6 - * * 7 GLU 7 H A 57.1 - - 175.7 - -59.7 -42.1 - - - 181.8 - 33.9 - 8 ALA 8 H A - - - - - -66.0 -44.1 - - - 179.6 -1.0 34.3 - * * 9 ALA 9 H A - - - - - -65.5 -43.1 - - - 179.7 -1.4 34.6 - 10 ARG 10 H A - 187.4 - 188.9 - -64.3 -36.8 - - - 181.2 -2.9 34.6 - * * 11 LEU 11 H A - 175.5 - - - -62.3 -46.3 - - - 178.4 -2.3 34.4 - 12 ARG 12 H A - - -59.7 180.3 - -63.5 -43.8 - - - 179.8 -2.0 35.0 - 13 PHE 13 H A - 170.4 - - - -63.9 -49.3 - - - 187.4 -2.4 35.2 - * * 14 ARG 14 H A - 218.3 - - - -78.3 -22.3 - - - 181.4 -3.7 34.4 - ** * +* ** ** 15 CYS 15 h A - 186.1 - - - - - - - - 179.8 -1.8 33.8 - 16 PHE 16 t B - 181.6 - - - - - - - - 179.4 -.8 35.2 - +* +* 17 HIS 17 B 75.1 - - - - - - - - - 174.6 - 34.2 - 18 TYR 18 B - 170.6 - - - - - - - - 180.5 -1.7 32.0 - 19 GLU 19 t B 41.4 - - 186.2 - - - - - - 181.4 - 32.5 - * * Residue-by-residue listing for refined_19 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 - - -51.5 - - - - - - - 178.0 -.6 34.3 - * +* +* 21 ALA 21 T A - - - - - - - - - - 182.6 - 36.6 - 22 THR 22 T A - - -73.3 - - - - - - - 181.3 -1.8 36.0 - 23 GLY 23 h - - - - - - - - - - - 181.9 -.8 - - +* +* 24 PRO 24 H - - - - - -61.7 -61.7 -30.6 - - - 180.3 - 37.7 - * * 25 GLN 25 H A - - -83.5 - - -73.0 -41.5 - - - 178.5 - 31.7 - * * 26 GLU 26 H A - 188.1 - 178.6 - -68.8 -33.5 - - - 174.3 - 32.6 - 27 ALA 27 H A - - - - - -58.8 -41.3 - - - 177.0 -2.2 33.9 - 28 LEU 28 H A - - -61.4 179.3 - -59.5 -41.5 - - - 179.5 -1.7 34.7 - 29 ALA 29 H A - - - - - -58.7 -43.1 - - - 178.7 -1.6 34.2 - 30 GLN 30 H A - - -70.4 165.1 - -67.6 -49.1 - - - 177.4 -1.8 34.3 - 31 LEU 31 H A - - -72.9 170.3 - -57.8 -46.3 - - - 181.4 -3.1 34.3 - * * 32 ARG 32 H A - 181.7 - 172.4 - -60.1 -42.3 - - - 177.1 -3.4 33.5 - +* +* 33 GLU 33 H A - 176.0 - - - -61.0 -50.3 - - - 181.0 -1.7 36.1 - 34 LEU 34 H A - - -59.8 174.2 - -65.4 -39.3 - - - 175.9 -2.3 34.1 - 35 CYS 35 H A - 181.9 - - - -62.1 -39.6 - - - 180.5 -3.3 35.8 - +* +* 36 ARG 36 H A - 183.5 - - - -70.7 -30.9 - - - 175.8 -2.3 32.7 - 37 GLN 37 H A - - -60.4 - - -68.0 -32.6 - - - 180.3 -1.8 35.2 - 38 TRP 38 H A - 171.5 - - - -74.0 -58.2 - - - 183.1 -1.6 32.9 - +* +* 39 LEU 39 H A - - -54.3 - - -85.5 -40.9 - - - 179.5 -2.9 30.6 - +* * +* 40 ARG 40 h l - - -63.4 180.6 - - - - - - 177.3 -1.0 32.1 - * * 41 PRO 41 T - - - - - -64.4 - - - - - 179.4 - 38.3 - * * 42 GLU 42 T A - 183.3 - - - - - - - - 183.3 - 35.2 - 43 VAL 43 T A - - -55.0 - - - - - - - 178.3 -.6 32.1 - +* +* 44 ARG 44 t B - - -64.5 187.8 - - - - - - 179.7 -3.2 32.5 - +* +* 45 SER 45 h B - - -60.1 - - - - - - - 182.6 - 34.5 - 46 LYS 46 H A 58.7 - - 189.3 - -53.8 -38.7 - - - 180.7 - 34.1 - 47 GLU 47 H A - - -46.0 - - -55.9 -48.8 - - - 180.5 - 35.5 - * * 48 GLN 48 H A - - -61.2 - - -62.5 -34.9 - - - 180.8 -.5 35.3 - ** ** 49 MET 49 H A - - -58.4 181.4 - -66.6 -42.1 - - - 175.5 -1.3 32.3 - 50 LEU 50 H A - - -80.3 - - -55.8 -48.7 - - - 180.8 -2.0 32.5 - 51 GLU 51 H A - 183.7 - 179.6 - -57.4 -49.3 - - - 180.2 -1.8 34.4 - 52 LEU 52 H A - - -59.3 179.3 - -64.8 -34.5 - - - 181.9 -2.3 34.7 - 53 LEU 53 H A - 181.6 - - - -77.3 -33.0 - - - 172.8 -2.4 32.3 - * * * 54 VAL 54 H A - 174.9 - - - -61.2 -42.9 - - - 176.9 -2.7 34.1 - 55 LEU 55 H A - 177.8 - - - -54.9 -49.7 - - - 182.7 -2.1 35.8 - 56 GLU 56 H A - 188.7 - - - -58.1 -42.6 - - - 181.0 -1.9 33.6 - 57 GLN 57 H A - 197.5 - - - -73.6 -47.4 - - - 181.8 -1.9 35.5 - 58 PHE 58 H A - 176.5 - - - -53.6 -46.3 - - - 180.1 -3.4 34.3 - +* +* Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 LEU 59 H A - - -61.2 181.9 - -64.1 -40.8 - - - 179.7 -3.2 32.2 - +* +* 60 GLY 60 H - - - - - - -80.4 -13.8 - - - 176.1 -1.5 - - * ** ** 61 ALA 61 H A - - - - - -76.4 -32.4 - - - 176.6 -1.7 34.3 - 62 LEU 62 h B - - -65.5 171.1 - - - - - - 177.1 -1.5 37.2 - 63 PRO 63 h - - - - - -70.6 - - - - - 181.9 - 39.0 - * * 64 PRO 64 H - - - - - -39.7 -39.7 -45.3 - - - 181.4 - 38.0 - ** ** * ** 65 GLU 65 H A 64.7 - - 176.1 - -65.5 -47.7 - - - 181.2 - 32.3 - 66 ILE 66 H A - - -58.9 184.7 - -70.3 -39.5 - - - 180.4 - 34.0 - 67 GLN 67 H A - 179.9 - 176.6 - -63.7 -42.4 - - - 181.4 -3.4 34.4 - +* +* 68 ALA 68 H A - - - - - -65.1 -30.8 - - - 177.8 -2.5 33.1 - 69 ARG 69 H A - - -59.1 - - -64.3 -32.2 - - - 175.1 -1.1 33.3 - * * 70 VAL 70 H A - 167.7 - - - -73.0 -45.3 - - - 185.1 -1.0 35.4 - * * 71 GLN 71 H A - - -57.6 - - -56.6 -29.3 - - - 177.8 -2.1 33.5 - 72 GLY 72 h - - - - - - - - - - - 184.5 -1.4 - - 73 GLN 73 T a - 182.7 - 179.6 - - - - - - 185.3 -2.8 35.2 - * * 74 ARG 74 t l - - -63.6 - - - - - - - 178.5 -3.0 30.3 - * * * 75 PRO 75 - - - - - -57.7 - - - - - 179.3 - 39.0 - * * 76 GLY 76 S - - - - - - - - - - - 176.4 - - - 77 SER 77 h B 53.1 - - - - - - - - - 182.7 - 32.7 - 78 PRO 78 H - - - - - -58.2 -58.2 -43.6 - - - 181.6 - 37.5 - * * 79 GLU 79 H A - - -61.6 171.4 - -67.1 -30.3 - - - 175.9 - 33.0 - 80 GLU 80 H A - 184.0 - - - -73.0 -43.6 - - - 175.7 - 33.9 - 81 ALA 81 H A - - - - - -58.0 -43.2 - - - 178.3 -2.5 34.2 - 82 ALA 82 H A - - - - - -58.3 -29.9 - - - 179.4 -3.0 34.4 - * * 83 ALA 83 H A - - - - - -74.5 -50.0 - - - 179.1 -.8 32.5 - +* +* 84 LEU 84 H A 54.9 - - 158.4 - -67.8 -34.5 - - - 178.1 -1.9 27.5 - * +* +* 85 VAL 85 H A - - -57.7 - - -71.2 -32.2 - - - 174.7 -2.6 30.6 - 86 ASP 86 H A - 179.3 - - - -66.0 -35.5 - - - 178.8 -1.2 34.4 - * * 87 GLY 87 H - - - - - - -76.6 -17.2 - - - 179.1 -1.9 - - +* +* 88 LEU 88 H A - 169.4 - - - -90.4 -41.0 - - - 175.2 -.8 34.4 - ** +* ** 89 ARG 89 h B 65.2 - - 175.8 - - - - - - 184.0 -2.7 32.8 - 90 ARG 90 a - 183.6 - - - - - - - - 189.0 - 33.5 - +* +* 91 GLU 91 l - 181.6 - - - - - - - - 184.8 - 32.2 - 92 PRO 92 S - - - - - -66.9 - - - - - 178.8 - 37.4 - * * 93 GLY 93 - - - - - - - - - - - 180.0 -.5 - - ** ** 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 179.0 - - - Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 96 SER 302 b - - -58.8 - - - - - - - 181.6 - 33.5 - 97 ASP 303 B - 183.5 - - - - - - - - 179.2 -1.2 35.3 - * * 98 PRO 304 - - - - - -53.7 - - - - - 177.1 - 38.0 - * * * 99 GLY 305 h - - - - - - - - - - - 175.9 - - - 100 PRO 306 H - - - - - -56.8 -56.8 -26.4 - - - 178.4 - 39.4 - * +* +* 101 GLU 307 H A 57.9 - - 180.6 - -67.3 -32.8 - - - 178.0 - 33.8 - 102 ALA 308 H A - - - - - -75.2 -37.9 - - - 176.1 -1.3 33.8 - 103 ALA 309 H A - - - - - -62.9 -43.8 - - - 178.4 -1.7 34.3 - 104 ARG 310 H A - 186.8 - 193.8 - -62.7 -36.5 - - - 181.1 -2.8 34.7 - 105 LEU 311 H A - 173.8 - - - -63.3 -37.1 - - - 178.8 -1.6 34.7 - 106 ARG 312 H A - - -59.5 178.4 - -76.1 -45.5 - - - 180.5 -1.5 34.9 - 107 PHE 313 H A - 163.1 - - - -66.3 -49.0 - - - 189.0 -2.8 34.5 - * +* * +* 108 ARG 314 H A - 209.6 - - - -78.0 -13.1 - - - 179.6 -3.6 34.0 - +* * ** ** ** 109 CYS 315 h A - 182.2 - - - - - - - - 179.2 -.5 34.0 - ** ** 110 PHE 316 t B - 179.6 - - - - - - - - 179.3 -1.3 34.9 - * * 111 HIS 317 B 72.6 - - - - - - - - - 173.7 - 34.4 - * * 112 TYR 318 B - 169.6 - - - - - - - - 179.2 -1.6 32.2 - 113 GLU 319 t B 51.3 - - 175.3 - - - - - - 179.4 -.7 33.5 - +* +* 114 GLU 320 T A - - -49.9 - - - - - - - 179.6 -.6 34.5 - * +* +* 115 ALA 321 T A - - - - - - - - - - 180.1 - 33.9 - 116 THR 322 T A - 201.2 - - - - - - - - 181.7 -1.8 34.1 - * * 117 GLY 323 h - - - - - - - - - - - 182.4 -1.0 - - * * 118 PRO 324 H - - - - - -61.4 -61.4 -35.9 - - - 180.2 - 38.1 - * * 119 GLN 325 H A - - -84.7 - - -68.4 -40.3 - - - 179.7 - 33.2 - * * 120 GLU 326 H A - 181.9 - 171.6 - -70.1 -35.2 - - - 175.1 - 33.2 - 121 ALA 327 H A - - - - - -60.8 -43.6 - - - 177.5 -2.4 34.3 - 122 LEU 328 H A - - -62.8 180.3 - -58.0 -39.9 - - - 179.6 -2.1 33.9 - 123 ALA 329 H A - - - - - -61.0 -36.6 - - - 177.6 -1.4 33.9 - 124 GLN 330 H A - - -68.1 169.2 - -75.6 -49.5 - - - 180.1 -1.4 34.5 - 125 LEU 331 H A - - -68.9 173.6 - -59.2 -45.6 - - - 180.7 -3.4 33.5 - +* +* 126 ARG 332 H A - 179.2 - 176.6 - -59.1 -43.4 - - - 178.7 -3.4 33.2 - +* +* 127 GLU 333 H A - 179.1 - - - -63.2 -51.3 - - - 182.3 -1.0 37.0 - * * * 128 LEU 334 H A - - -58.8 177.1 - -65.6 -36.4 - - - 177.2 -2.6 33.4 - 129 CYS 335 H A - 184.1 - - - -69.1 -34.4 - - - 179.3 -3.1 34.8 - * * 130 ARG 336 H A - 183.0 - - - -70.2 -36.5 - - - 176.1 -2.0 33.3 - 131 GLN 337 H A - - -63.5 180.4 - -69.1 -16.1 - - - 177.5 -2.3 33.6 - ** ** 132 TRP 338 H A - 170.1 - - - -88.3 -56.7 - - - 181.3 - 33.2 - +* +* +* Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 133 LEU 339 H A - - -57.4 - - -83.8 -36.6 - - - 176.5 -2.9 30.2 - +* * * +* 134 ARG 340 h l - - -54.1 174.7 - - - - - - 179.9 -2.0 32.3 - 135 PRO 341 T - - - - - -67.2 - - - - - 177.0 - 37.5 - * * 136 GLU 342 T A - - -59.3 - - - - - - - 187.8 - 35.8 - * * 137 VAL 343 T A - - -58.1 - - - - - - - 179.8 -.9 33.2 - +* +* 138 ARG 344 t B - - -68.9 180.9 - - - - - - 179.1 -3.3 32.2 - +* +* 139 SER 345 h B - - -56.5 - - - - - - - 178.6 - 35.8 - 140 LYS 346 H A 55.4 - - 186.5 - -57.9 -40.3 - - - 183.5 - 35.5 - 141 GLU 347 H A 45.2 - - - - -55.8 -39.5 - - - 177.7 - 28.1 - * +* +* 142 GLN 348 H A - - -65.0 - - -76.2 -27.6 - - - 179.3 -.6 31.8 - * +* +* 143 MET 349 H A - - -58.8 184.3 - -59.8 -37.8 - - - 175.8 -.9 32.5 - * * 144 LEU 350 H A - - -75.0 - - -58.5 -50.8 - - - 183.9 -1.2 33.4 - * * * 145 GLU 351 H A - 190.1 - 178.8 - -62.4 -41.3 - - - 178.0 -1.0 34.1 - * * 146 LEU 352 H A - - -61.9 177.5 - -60.5 -40.7 - - - 181.3 -2.5 35.4 - 147 LEU 353 H A - 177.7 - - - -73.1 -29.8 - - - 175.2 -2.0 32.7 - 148 VAL 354 H A - 179.1 - - - -58.2 -39.8 - - - 177.4 -1.8 34.0 - 149 LEU 355 H A - 178.9 - - - -55.8 -46.7 - - - 180.1 -1.4 34.8 - 150 GLU 356 H A - - -74.1 - - -55.3 -45.4 - - - 181.1 -1.0 32.4 - * * 151 GLN 357 H A - 203.7 - - - -74.8 -46.0 - - - 184.4 -1.5 34.7 - * * 152 PHE 358 H A - 181.8 - - - -53.4 -47.3 - - - 179.5 -3.1 33.7 - * * * 153 LEU 359 H A - - -63.3 186.9 - -62.6 -36.3 - - - 178.5 -3.0 31.2 - * * 154 GLY 360 H - - - - - - -81.1 -23.1 - - - 177.8 -1.0 - - * * * * 155 ALA 361 H A - - - - - -69.8 -28.4 - - - 174.6 -2.3 34.0 - 156 LEU 362 h B - - -66.8 172.4 - - - - - - 176.0 -1.4 36.9 - 157 PRO 363 h - - - - - -70.0 - - - - - 183.9 - 38.4 - * * 158 PRO 364 H - - - - - -41.6 -41.6 -46.3 - - - 179.1 - 37.5 - ** +* * ** 159 GLU 365 H A 55.9 - - 176.5 - -59.1 -48.8 - - - 180.5 - 33.7 - 160 ILE 366 H A - - -60.1 184.0 - -71.7 -38.7 - - - 179.0 -.6 34.3 - +* +* 161 GLN 367 H A - 177.9 - 176.0 - -60.7 -42.1 - - - 179.1 -3.3 34.2 - +* +* 162 ALA 368 H A - - - - - -63.0 -32.1 - - - 179.4 -2.8 33.7 - * * 163 ARG 369 H A - - -50.3 - - -64.8 -36.5 - - - 176.2 -1.1 34.9 - * * * 164 VAL 370 H A - 166.4 - - - -68.4 -43.0 - - - 185.2 -1.3 35.7 - * * 165 GLN 371 H A - - -57.3 - - -55.8 -27.9 - - - 177.1 -2.0 32.0 - * * Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 166 GLY 372 h - - - - - - - - - - - 182.6 -1.0 - - * * 167 GLN 373 T a - 176.8 - 181.4 - - - - - - 188.6 -3.0 35.5 - * * * 168 ARG 374 t l - - -62.9 - - - - - - - 177.9 -2.8 29.7 - * * * 169 PRO 375 - - - - - -57.6 - - - - - 178.4 - 39.0 - * * 170 GLY 376 S - - - - - - - - - - - 176.0 - - - 171 SER 377 h B 53.8 - - - - - - - - - 185.9 - 33.3 - * * 172 PRO 378 H - - - - - -60.3 -60.3 -43.5 - - - 184.0 - 38.4 - * * 173 GLU 379 H A - - -58.6 175.1 - -71.4 -31.0 - - - 175.6 - 33.2 - 174 GLU 380 H A - 181.4 - - - -66.9 -47.9 - - - 176.4 - 34.1 - 175 ALA 381 H A - - - - - -56.1 -46.2 - - - 179.6 -2.4 34.7 - 176 ALA 382 H A - - - - - -58.5 -29.5 - - - 180.1 -2.8 34.1 - * * 177 ALA 383 H A - - - - - -74.1 -50.2 - - - 178.0 -1.1 32.7 - * * 178 LEU 384 H A 52.6 - - 159.8 - -64.3 -44.8 - - - 182.4 -1.9 27.9 - +* +* 179 VAL 385 H A - - -58.6 - - -64.1 -32.4 - - - 177.6 -2.6 31.0 - 180 ASP 386 H A - 180.7 - - - -62.1 -36.7 - - - 180.7 -1.3 34.7 - * * 181 GLY 387 H - - - - - - -85.4 -44.5 - - - 185.0 -1.3 - - +* * +* 182 LEU 388 H A 56.5 - - - - -74.7 -18.2 - - - 173.2 -3.2 28.1 - +* * +* +* +* 183 ARG 389 h B 57.3 - - 174.7 - - - - - - 177.4 -1.5 34.4 - 184 ARG 390 A - 194.2 - - - - - - - - 176.1 - 34.1 - 185 GLU 391 ~l - 182.1 - - - - - - - - 177.3 - 31.9 - ** ** 186 PRO 392 S - - - - - -77.6 - - - - - 182.6 - 38.8 - * * * 187 GLY 393 - - - - - - - - - - - 179.1 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * ** * * ** ** ** +* ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.1 181.8 -62.3 177.9 -59.9 -65.3 -39.2 - - - 179.6 -1.9 34.2 Standard deviations: 8.3 9.9 7.6 6.8 9.3 8.6 8.5 - - - 3.0 .9 2.1 Numbers of values: 18 57 57 51 18 120 120 0 0 0 186 125 170 0 Residue-by-residue listing for refined_19 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_19 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 - 1.236 1.503 - 1.464 - 117.35 120.07 - 110.81 - 122.58 2 SER 2 1.310 1.232 1.516 1.532 1.444 121.24 116.44 120.77 109.35 111.07 110.52 122.77 * * 3 ASP 3 1.304 1.242 1.516 1.541 1.442 121.03 118.56 119.60 110.57 108.05 112.18 121.82 +* * * +* 4 PRO 4 1.347 1.232 1.530 1.541 1.474 122.78 116.16 121.01 110.65 112.48 104.05 122.79 5 GLY 5 1.307 1.240 1.504 - 1.422 121.03 118.37 119.55 - 110.18 - 122.08 +* +* +* 6 PRO 6 1.349 1.230 1.531 1.536 1.473 122.84 115.79 120.96 110.21 111.71 103.76 123.23 7 GLU 7 1.331 1.226 1.535 1.527 1.452 123.10 116.74 120.10 110.02 112.16 110.54 123.13 8 ALA 8 1.335 1.236 1.506 1.521 1.456 122.30 115.03 121.33 110.31 110.16 110.43 123.62 9 ALA 9 1.309 1.237 1.518 1.500 1.434 122.32 116.00 120.76 110.54 110.26 109.51 123.21 * * * 10 ARG 10 1.333 1.207 1.512 1.522 1.446 121.52 116.64 120.42 107.98 110.24 112.28 122.94 * * * * 11 LEU 11 1.321 1.222 1.524 1.521 1.410 122.79 116.59 120.40 111.75 110.51 108.97 122.97 +** +** 12 ARG 12 1.326 1.235 1.521 1.517 1.468 121.61 114.58 121.34 108.80 110.16 110.59 124.07 13 PHE 13 1.315 1.205 1.521 1.541 1.448 124.23 116.81 120.67 110.53 112.47 108.41 122.50 * * * * * 14 ARG 14 1.303 1.227 1.535 1.538 1.445 121.48 116.59 120.87 110.54 111.13 109.84 122.53 +* +* Residue-by-residue listing for refined_19 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 1.323 1.241 1.539 1.541 1.457 121.48 115.97 120.80 111.26 110.63 110.05 123.23 16 PHE 16 1.332 1.234 1.533 1.543 1.464 123.38 116.73 120.75 110.67 109.87 108.82 122.50 17 HIS 17 1.311 1.233 1.503 1.568 1.449 120.68 117.30 120.19 109.29 108.26 112.66 122.51 * * +* * * +* 18 TYR 18 1.284 1.230 1.521 1.521 1.422 119.56 114.65 121.44 112.63 110.04 111.55 123.82 *** +* * * *** 19 GLU 19 1.294 1.232 1.530 1.554 1.428 123.78 115.54 121.19 114.01 110.48 109.50 123.22 ** * +* * ** ** 20 GLU 20 1.338 1.230 1.523 1.542 1.475 123.77 115.18 120.99 108.23 110.77 112.31 123.82 * * * 21 ALA 21 1.319 1.228 1.521 1.516 1.469 124.50 114.29 121.88 108.58 110.83 108.32 123.83 +* * * +* 22 THR 22 1.282 1.235 1.546 1.510 1.412 124.31 115.98 121.45 112.91 111.91 104.81 122.43 *** * * ** * +* +*** +*** 23 GLY 23 1.311 1.240 1.511 - 1.428 121.25 118.65 120.13 - 111.19 - 121.22 * * * * * 24 PRO 24 1.342 1.223 1.533 1.517 1.460 122.28 117.52 120.23 110.97 113.85 103.64 122.23 25 GLN 25 1.332 1.230 1.504 1.538 1.461 120.19 116.20 120.87 109.60 110.75 114.61 122.92 ** ** 26 GLU 26 1.315 1.241 1.526 1.517 1.450 120.15 115.85 121.39 110.59 109.74 112.55 122.75 * * 27 ALA 27 1.322 1.226 1.530 1.520 1.454 121.74 116.05 120.62 110.81 109.32 110.54 123.29 28 LEU 28 1.335 1.214 1.513 1.525 1.466 122.57 116.60 120.23 108.00 111.09 111.79 123.17 * * 29 ALA 29 1.328 1.241 1.528 1.518 1.465 122.12 115.06 121.18 110.29 110.52 110.24 123.74 30 GLN 30 1.319 1.234 1.517 1.505 1.442 123.36 115.37 120.92 111.85 110.96 108.48 123.68 * * * 31 LEU 31 1.324 1.208 1.510 1.529 1.458 123.55 116.47 120.48 110.02 111.99 110.10 123.04 * * * 32 ARG 32 1.311 1.214 1.510 1.513 1.452 122.52 115.77 120.55 111.25 111.54 110.01 123.67 * * 33 GLU 33 1.301 1.218 1.529 1.523 1.449 123.07 116.20 120.59 110.64 109.83 107.45 123.15 +* +* +* 34 LEU 34 1.314 1.229 1.522 1.511 1.459 122.56 115.71 120.88 111.26 111.26 109.16 123.40 * * 35 CYS 35 1.315 1.227 1.527 1.542 1.449 123.14 115.49 121.85 110.32 108.55 108.83 122.61 * * 36 ARG 36 1.313 1.212 1.525 1.538 1.409 122.71 116.96 120.15 114.35 110.66 108.82 122.88 * +** ** +** 37 GLN 37 1.315 1.236 1.532 1.541 1.463 122.06 114.75 121.31 109.52 108.86 110.23 123.94 38 TRP 38 1.327 1.234 1.536 1.553 1.447 124.23 118.49 119.72 112.83 112.62 109.28 121.79 * * * * * 39 LEU 39 1.330 1.230 1.518 1.559 1.461 118.63 116.34 119.96 111.05 111.14 114.73 123.67 * +* ** ** 40 ARG 40 1.344 1.221 1.524 1.533 1.469 123.73 117.99 120.43 109.35 113.26 113.22 121.57 * * +* +* 41 PRO 41 1.338 1.238 1.534 1.535 1.472 122.42 115.31 121.31 110.57 111.86 103.80 123.38 * * 42 GLU 42 1.320 1.237 1.537 1.537 1.441 122.82 117.02 120.76 110.43 110.62 108.97 122.19 43 VAL 43 1.326 1.236 1.528 1.559 1.460 120.10 117.00 120.57 110.41 112.14 112.93 122.43 44 ARG 44 1.316 1.234 1.510 1.537 1.445 120.93 114.98 121.44 109.91 111.16 113.15 123.58 +* +* 45 SER 45 1.288 1.241 1.526 1.511 1.426 123.36 115.19 120.88 111.40 111.33 108.59 123.93 +** +* * +** Residue-by-residue listing for refined_19 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 46 LYS 46 1.324 1.217 1.520 1.520 1.457 124.63 116.24 120.34 111.47 112.97 108.47 123.39 +* * +* 47 GLU 47 1.319 1.234 1.517 1.541 1.487 122.54 113.81 122.15 106.48 109.56 112.47 124.03 +* * +* * +* 48 GLN 48 1.311 1.232 1.522 1.521 1.453 123.43 116.44 120.59 108.81 111.23 110.11 122.96 * * 49 MET 49 1.328 1.229 1.493 1.504 1.452 121.23 116.34 120.00 111.09 111.67 111.73 123.65 +* * +* 50 LEU 50 1.331 1.210 1.505 1.553 1.453 121.16 116.38 120.16 110.52 110.36 112.95 123.37 * * * * 51 GLU 51 1.323 1.241 1.552 1.517 1.426 122.88 116.88 120.62 111.06 111.84 108.82 122.49 * +* +* 52 LEU 52 1.332 1.232 1.523 1.528 1.457 121.92 115.92 121.27 109.35 111.08 110.46 122.80 53 LEU 53 1.306 1.252 1.532 1.513 1.427 121.70 116.54 120.42 113.60 111.95 109.19 123.04 +* * +* +* +* 54 VAL 54 1.329 1.223 1.519 1.564 1.457 121.61 115.29 120.80 109.78 108.17 112.20 123.87 * * 55 LEU 55 1.332 1.222 1.521 1.531 1.461 123.37 115.91 120.53 108.71 110.67 109.65 123.55 56 GLU 56 1.327 1.237 1.534 1.540 1.455 122.34 116.60 120.75 110.77 111.48 110.58 122.64 57 GLN 57 1.325 1.205 1.508 1.532 1.454 120.47 115.79 120.25 109.56 107.93 110.05 123.86 * * * 58 PHE 58 1.325 1.236 1.517 1.536 1.453 123.08 116.12 120.69 110.31 111.32 110.09 123.17 59 LEU 59 1.317 1.212 1.519 1.529 1.437 121.09 117.05 120.23 111.69 111.62 111.57 122.69 * * 60 GLY 60 1.321 1.235 1.522 - 1.454 120.29 116.44 120.73 - 112.80 - 122.80 61 ALA 61 1.316 1.237 1.512 1.527 1.447 122.34 114.98 120.89 110.44 109.14 110.67 124.13 62 LEU 62 1.334 1.241 1.533 1.535 1.462 124.22 118.46 119.91 107.69 109.99 108.75 121.62 * * * * * 63 PRO 63 1.346 1.237 1.521 1.536 1.455 121.67 118.29 119.10 110.17 108.89 103.96 122.60 * * 64 PRO 64 1.349 1.224 1.538 1.521 1.471 123.86 117.82 119.63 110.77 114.62 103.20 122.53 * * 65 GLU 65 1.340 1.228 1.540 1.544 1.464 120.56 116.89 120.55 110.58 111.74 112.34 122.53 * * 66 ILE 66 1.335 1.234 1.536 1.556 1.439 121.79 115.71 121.09 110.81 110.43 110.52 123.16 67 GLN 67 1.317 1.234 1.526 1.526 1.449 122.71 116.04 120.86 110.38 111.10 109.93 123.08 68 ALA 68 1.318 1.240 1.529 1.513 1.460 122.16 116.76 120.41 110.53 112.07 110.97 122.83 69 ARG 69 1.334 1.229 1.519 1.533 1.469 121.48 115.28 121.64 110.54 109.60 111.80 123.09 70 VAL 70 1.311 1.230 1.501 1.530 1.435 121.88 115.68 120.48 107.26 110.70 111.86 123.83 * * * * 71 GLN 71 1.314 1.217 1.522 1.513 1.450 122.50 116.64 120.49 109.81 111.91 111.30 122.86 * * 72 GLY 72 1.313 1.235 1.536 - 1.442 120.82 117.76 119.85 - 114.03 - 122.39 * * * 73 GLN 73 1.333 1.221 1.528 1.527 1.465 121.22 115.75 120.81 109.46 112.26 109.23 123.42 74 ARG 74 1.329 1.223 1.526 1.559 1.471 124.25 117.48 120.55 110.41 111.74 115.38 121.93 * * +** +** 75 PRO 75 1.352 1.219 1.532 1.538 1.474 122.87 115.26 121.27 110.02 111.87 103.31 123.44 * * * 76 GLY 76 1.315 1.235 1.514 - 1.453 122.08 116.53 120.44 - 113.26 - 123.02 * * 77 SER 77 1.309 1.243 1.544 1.541 1.441 122.14 117.92 120.11 112.86 109.87 110.35 121.90 * * * 78 PRO 78 1.357 1.222 1.518 1.533 1.473 123.10 116.83 120.28 110.33 113.52 104.87 122.88 * +* +* Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 79 GLU 79 1.316 1.235 1.515 1.516 1.459 122.03 115.95 120.75 112.30 110.90 109.81 123.28 * * 80 GLU 80 1.323 1.217 1.531 1.527 1.439 121.41 116.71 120.62 111.00 108.89 110.71 122.66 81 ALA 81 1.347 1.228 1.514 1.512 1.459 121.78 115.21 120.88 110.21 110.17 110.40 123.88 * * 82 ALA 82 1.328 1.214 1.530 1.528 1.449 123.64 115.79 120.96 110.69 110.92 109.59 123.25 * * 83 ALA 83 1.295 1.237 1.534 1.513 1.443 123.26 118.47 119.57 111.41 112.01 110.99 121.95 ** * ** 84 LEU 84 1.353 1.226 1.508 1.561 1.470 118.65 117.01 120.54 110.89 112.76 117.91 122.45 +* +* +* **** **** 85 VAL 85 1.320 1.233 1.528 1.546 1.446 119.92 115.89 120.98 112.27 110.54 113.60 123.12 * * * 86 ASP 86 1.332 1.223 1.522 1.530 1.464 122.24 115.76 121.08 109.55 109.90 111.02 123.16 87 GLY 87 1.321 1.237 1.520 - 1.446 121.32 116.78 120.76 - 112.25 - 122.45 88 LEU 88 1.318 1.234 1.531 1.508 1.381 122.70 117.22 120.06 112.44 110.49 108.23 122.72 * **** * * **** 89 ARG 89 1.339 1.232 1.514 1.552 1.439 120.44 115.86 121.44 110.97 107.38 113.14 122.64 * * +* +* 90 ARG 90 1.267 1.230 1.504 1.539 1.431 119.84 116.18 119.54 110.55 112.40 110.90 124.26 **** * * **** 91 GLU 91 1.334 1.238 1.535 1.546 1.457 123.19 116.87 121.25 111.76 107.91 112.90 121.74 * * * 92 PRO 92 1.335 1.243 1.525 1.530 1.451 122.17 115.64 121.30 111.29 113.08 104.21 123.05 * * * 93 GLY 93 1.307 1.240 1.501 - 1.431 120.84 115.90 120.42 - 111.97 - 123.68 +* * +* 94 GLY 94 1.305 1.245 1.508 - 1.442 122.03 - 119.52 - 110.92 - - +* +* 95 GLY 301 - 1.234 1.508 - 1.449 - 116.05 121.07 - 111.85 - 122.88 96 SER 302 1.306 1.228 1.516 1.529 1.433 121.06 115.62 121.12 111.49 109.33 110.74 123.19 +* * +* 97 ASP 303 1.305 1.229 1.527 1.535 1.451 122.43 118.45 119.51 110.05 109.46 109.53 122.03 +* * +* 98 PRO 304 1.361 1.238 1.540 1.542 1.481 123.21 116.50 120.74 110.42 113.33 103.99 122.76 * * 99 GLY 305 1.317 1.235 1.507 - 1.424 121.28 118.27 119.97 - 112.37 - 121.76 +* +* 100 PRO 306 1.356 1.220 1.523 1.529 1.476 123.10 115.22 121.51 109.57 110.74 103.30 123.26 * * 101 GLU 307 1.322 1.233 1.539 1.530 1.445 123.21 116.73 120.49 111.19 111.15 109.83 122.78 102 ALA 308 1.330 1.234 1.514 1.524 1.452 121.78 115.21 121.28 110.92 108.82 110.87 123.50 103 ALA 309 1.328 1.235 1.521 1.522 1.450 122.23 115.64 121.21 110.48 109.29 110.40 123.12 104 ARG 310 1.334 1.205 1.523 1.526 1.451 122.17 117.03 120.33 108.17 110.25 111.88 122.63 * * * 105 LEU 311 1.325 1.222 1.534 1.527 1.421 122.64 116.19 120.95 111.63 110.62 108.47 122.84 +* * +* 106 ARG 312 1.312 1.231 1.525 1.518 1.454 121.78 115.03 121.35 110.20 110.12 109.47 123.61 * * 107 PHE 313 1.311 1.207 1.525 1.536 1.454 124.06 117.23 120.71 110.51 113.76 108.91 122.05 * * * * 108 ARG 314 1.304 1.241 1.536 1.536 1.451 120.73 115.93 121.05 110.68 111.12 110.22 123.02 +* +* 109 CYS 315 1.316 1.244 1.534 1.536 1.447 122.14 115.96 120.51 111.01 110.24 110.22 123.54 110 PHE 316 1.339 1.241 1.519 1.545 1.460 122.87 116.16 120.99 110.54 109.57 109.68 122.83 Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 111 HIS 317 1.301 1.230 1.502 1.573 1.435 120.47 117.95 120.00 110.03 108.28 111.87 122.02 +* * ** * * ** 112 TYR 318 1.293 1.233 1.489 1.517 1.418 118.04 114.57 121.32 111.52 108.55 112.99 124.07 +** +* ** ** * +** 113 GLU 319 1.276 1.241 1.511 1.546 1.401 122.64 115.80 120.99 112.61 109.08 110.28 123.17 +*** +** * +*** 114 GLU 320 1.323 1.217 1.516 1.548 1.461 122.50 114.82 121.14 108.34 109.14 112.49 124.02 * * 115 ALA 321 1.314 1.232 1.544 1.516 1.445 123.97 118.28 119.77 110.41 113.26 109.69 121.94 * * * * 116 THR 322 1.334 1.223 1.538 1.585 1.458 119.10 116.06 121.08 110.34 108.73 111.57 122.81 +* * +* 117 GLY 323 1.329 1.237 1.520 - 1.441 120.96 118.95 119.97 - 110.98 - 121.08 * * * 118 PRO 324 1.342 1.226 1.533 1.514 1.462 122.27 117.41 120.22 110.62 113.88 103.43 122.35 119 GLN 325 1.336 1.232 1.512 1.548 1.465 120.47 115.24 121.49 109.10 109.62 113.56 123.26 +* +* 120 GLU 326 1.307 1.240 1.533 1.517 1.449 121.79 115.95 121.24 111.99 110.71 109.97 122.81 +* +* 121 ALA 327 1.318 1.217 1.524 1.521 1.454 122.01 116.19 120.47 110.59 109.66 110.16 123.32 122 LEU 328 1.327 1.222 1.523 1.524 1.471 122.66 117.01 120.03 108.70 112.24 111.76 122.96 123 ALA 329 1.330 1.234 1.528 1.523 1.468 121.57 115.13 121.57 110.64 110.15 110.50 123.29 124 GLN 330 1.307 1.231 1.523 1.508 1.441 123.15 115.54 120.98 111.73 110.92 108.35 123.44 +* * * +* 125 LEU 331 1.319 1.214 1.506 1.520 1.459 123.49 117.21 119.82 110.16 113.19 110.70 122.96 126 ARG 332 1.321 1.215 1.510 1.526 1.454 121.38 115.52 120.77 110.73 110.99 111.35 123.69 127 GLU 333 1.298 1.223 1.528 1.518 1.450 123.36 116.43 120.48 109.43 110.31 107.15 123.03 ** +* ** 128 LEU 334 1.317 1.229 1.525 1.524 1.457 121.59 115.90 121.02 111.17 111.07 110.42 123.06 129 CYS 335 1.317 1.227 1.526 1.535 1.446 122.30 116.13 121.20 110.28 109.28 110.03 122.65 130 ARG 336 1.316 1.212 1.518 1.540 1.414 122.43 116.29 120.49 113.98 109.54 108.83 123.19 ** ** ** 131 GLN 337 1.313 1.226 1.529 1.506 1.451 122.42 115.09 121.53 111.42 110.80 109.79 123.37 * * * 132 TRP 338 1.315 1.228 1.552 1.546 1.442 123.93 118.54 120.00 113.20 111.60 108.71 121.45 * * * * +* * +* 133 LEU 339 1.332 1.222 1.511 1.547 1.475 118.87 116.66 119.77 110.49 112.27 115.16 123.57 +* +** +** 134 ARG 340 1.336 1.230 1.522 1.531 1.467 123.53 117.10 121.09 111.44 112.47 111.18 121.80 * * 135 PRO 341 1.341 1.234 1.527 1.534 1.456 122.56 116.07 120.99 110.93 112.21 104.64 122.94 * * 136 GLU 342 1.320 1.237 1.516 1.551 1.453 121.80 115.60 121.25 106.22 109.80 112.61 123.13 * ** * ** 137 VAL 343 1.318 1.230 1.524 1.557 1.446 121.33 117.24 120.34 110.21 112.83 111.40 122.41 138 ARG 344 1.311 1.246 1.504 1.533 1.446 120.81 114.38 121.75 110.44 112.18 112.59 123.86 * * * 139 SER 345 1.292 1.243 1.527 1.531 1.417 123.44 114.85 121.25 109.90 109.90 109.02 123.90 +** ** +** 140 LYS 346 1.310 1.215 1.526 1.515 1.449 124.21 115.53 120.93 110.60 112.21 107.64 123.50 * * +* +* 141 GLU 347 1.304 1.239 1.544 1.552 1.460 123.34 117.61 120.12 114.63 115.65 111.91 122.26 +* * ** +* ** 142 GLN 348 1.317 1.234 1.510 1.529 1.457 120.77 116.60 120.35 111.49 112.08 112.02 123.04 Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 143 MET 349 1.330 1.235 1.511 1.509 1.454 121.37 116.00 120.44 111.38 111.59 111.24 123.53 * * 144 LEU 350 1.332 1.227 1.508 1.554 1.457 121.64 115.93 120.27 109.11 110.79 112.91 123.76 * * * 145 GLU 351 1.330 1.236 1.541 1.524 1.426 123.12 116.73 120.40 111.58 111.32 109.07 122.85 +* +* 146 LEU 352 1.333 1.229 1.523 1.528 1.459 122.30 115.22 121.41 109.10 110.48 109.85 123.35 147 LEU 353 1.308 1.251 1.540 1.516 1.435 122.98 116.52 120.69 113.72 112.30 108.43 122.80 * * * +* * +* 148 VAL 354 1.326 1.229 1.536 1.559 1.465 121.80 115.47 120.86 110.02 109.31 111.55 123.61 149 LEU 355 1.335 1.235 1.528 1.558 1.471 123.76 115.78 120.68 111.81 110.13 108.37 123.53 * * * * 150 GLU 356 1.328 1.229 1.506 1.528 1.453 122.39 117.11 120.11 110.17 113.60 112.05 122.78 151 GLN 357 1.313 1.205 1.507 1.526 1.443 119.42 115.76 120.39 109.62 107.78 111.33 123.76 * * * * * 152 PHE 358 1.327 1.236 1.524 1.527 1.448 122.68 116.99 120.10 110.11 112.07 110.84 122.90 153 LEU 359 1.329 1.222 1.522 1.533 1.456 120.19 116.81 120.50 111.60 112.31 112.67 122.67 * * 154 GLY 360 1.315 1.235 1.523 - 1.444 120.28 116.38 120.56 - 112.57 - 123.04 * * 155 ALA 361 1.326 1.238 1.511 1.525 1.456 122.75 115.13 121.01 110.43 109.63 110.82 123.84 156 LEU 362 1.324 1.242 1.521 1.530 1.444 123.36 118.27 120.00 108.04 109.57 109.01 121.73 * * * 157 PRO 363 1.338 1.236 1.524 1.537 1.448 121.18 118.74 118.82 110.68 107.99 104.57 122.44 * * * +* * +* 158 PRO 364 1.351 1.220 1.538 1.517 1.477 123.56 117.09 119.97 111.27 114.01 103.39 122.92 159 GLU 365 1.332 1.223 1.548 1.536 1.466 121.94 117.35 120.30 110.22 112.62 110.48 122.29 * * 160 ILE 366 1.339 1.235 1.519 1.547 1.450 121.84 115.22 121.30 109.93 110.02 111.04 123.45 161 GLN 367 1.314 1.225 1.524 1.524 1.440 122.65 115.96 120.74 111.13 110.22 109.70 123.27 * * 162 ALA 368 1.319 1.228 1.525 1.517 1.457 122.82 116.76 120.48 110.11 111.53 110.79 122.75 163 ARG 369 1.331 1.228 1.519 1.529 1.469 121.29 114.66 121.76 108.91 108.56 111.34 123.58 164 VAL 370 1.316 1.228 1.502 1.536 1.442 123.12 115.56 120.64 107.61 111.11 111.05 123.79 * * 165 GLN 371 1.308 1.211 1.530 1.513 1.450 123.06 117.07 120.54 111.24 112.75 111.55 122.38 * * * 166 GLY 372 1.315 1.234 1.541 - 1.455 120.74 117.01 120.36 - 113.14 - 122.62 * * 167 GLN 373 1.332 1.229 1.535 1.532 1.459 122.38 115.26 121.02 108.79 112.30 109.54 123.71 168 ARG 374 1.329 1.229 1.530 1.550 1.468 124.85 117.28 120.84 110.12 111.62 116.35 121.81 +* *** *** 169 PRO 375 1.343 1.221 1.539 1.537 1.476 123.15 115.75 121.13 110.18 112.29 103.00 123.12 170 GLY 376 1.320 1.227 1.520 - 1.462 122.06 116.34 120.88 - 112.87 - 122.77 171 SER 377 1.302 1.250 1.528 1.533 1.432 122.10 117.86 120.03 112.55 108.50 110.27 122.10 +* * * +* 172 PRO 378 1.347 1.226 1.520 1.534 1.467 122.79 116.23 120.72 110.08 113.16 104.00 123.03 173 GLU 379 1.312 1.227 1.515 1.504 1.444 122.05 116.62 120.26 111.99 111.54 109.69 123.11 * * * 174 GLU 380 1.326 1.220 1.527 1.533 1.449 120.99 116.20 120.57 111.24 108.10 110.41 123.18 * * 175 ALA 381 1.350 1.230 1.516 1.515 1.464 122.31 115.34 120.82 109.79 110.69 110.06 123.83 +* +* 176 ALA 382 1.325 1.218 1.533 1.522 1.453 123.56 115.81 121.18 110.97 111.39 109.45 123.01 * * Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 177 ALA 383 1.293 1.242 1.527 1.513 1.443 122.72 118.10 119.73 111.41 111.55 110.99 122.16 +** +** 178 LEU 384 1.351 1.225 1.498 1.563 1.464 118.68 116.75 120.16 110.59 112.51 117.95 123.03 +* * +* +* **** **** 179 VAL 385 1.325 1.226 1.519 1.540 1.456 120.95 116.31 120.34 111.17 112.17 113.44 123.34 * * 180 ASP 386 1.329 1.229 1.520 1.541 1.465 122.28 115.45 120.79 109.76 110.00 110.50 123.75 181 GLY 387 1.320 1.230 1.522 - 1.439 121.44 117.00 120.25 - 114.22 - 122.75 182 LEU 388 1.331 1.239 1.533 1.545 1.462 121.45 117.15 120.15 114.33 115.21 112.36 122.68 ** * * ** 183 ARG 389 1.331 1.237 1.505 1.545 1.432 121.14 115.78 121.21 109.32 108.66 112.13 123.00 * * 184 ARG 390 1.277 1.235 1.526 1.530 1.438 120.68 114.04 121.42 110.73 107.54 111.10 124.54 +*** * * * +*** 185 GLU 391 1.344 1.231 1.533 1.540 1.457 125.28 117.22 121.24 112.10 112.36 111.23 121.50 * +* * +* 186 PRO 392 1.332 1.234 1.541 1.527 1.455 122.38 117.09 120.67 110.24 112.59 103.24 122.24 187 GLY 393 1.320 1.229 1.508 - 1.440 120.41 116.32 120.74 - 112.39 - 122.93 188 GLY 394 1.298 - 1.486 - 1.427 121.63 - - - 109.37 - - ** +* * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** **** ** * * ** +* **** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 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 1.267 1.353 1.320 .014 **** +* C-N (Pro) 1.341 .016 18 1.332 1.361 1.346 .008 * C-O C-O 1.231 .020 187 1.205 1.252 1.230 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 170 1.489 1.552 1.524 .011 +* * CH2G*-C (Gly) 1.516 .018 18 1.486 1.541 1.514 .012 +* * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.500 1.528 1.518 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.510 1.585 1.549 .018 * +* CH1E-CH2E (the rest) 1.530 .020 138 1.504 1.573 1.532 .014 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.381 1.487 1.450 .015 **** +* NH1-CH2G* (Gly) 1.451 .016 18 1.422 1.464 1.442 .012 +* N-CH1E (Pro) 1.466 .015 18 1.448 1.481 1.467 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 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 2.0 152 113.81 118.56 116.23 .98 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.90 118.95 117.13 .95 * CH1E-C-N (Pro) 116.9 1.5 18 115.22 118.74 116.60 1.03 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 121.08 124.54 122.99 .67 * O-C-N (Pro) 122.0 1.4 18 122.23 123.44 122.84 .37 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.04 125.28 122.14 1.35 ** +* C-NH1-CH2G* (Gly) 120.6 1.7 16 120.28 122.08 121.15 .58 C-N-CH1E (Pro) 122.6 5.0 18 121.18 123.86 122.68 .63 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.82 122.15 120.69 .56 * CH2G*-C-O (Gly) 120.8 2.1 17 119.52 121.07 120.31 .44 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 108.58 111.41 110.48 .58 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.26 112.91 110.23 1.55 +* CH2E-CH1E-C (the rest) 110.1 1.9 138 106.22 114.63 110.62 1.43 ** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.38 115.65 110.76 1.47 * +* NH1-CH2G*-C (Gly) 112.5 2.9 18 109.37 114.22 112.06 1.26 * N-CH1E-C (Pro) 111.8 2.5 18 107.99 114.62 112.34 1.68 +* * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 108.32 110.99 110.27 .66 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 104.81 113.60 111.33 2.17 +*** * N-CH1E-CH2E (Pro) 103.0 1.1 18 103.00 104.87 103.80 .52 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 107.15 117.95 110.81 1.96 +* **** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_19 Page 17 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 142 93.4% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 1 .7% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 93.4 83.8 10.0 1.0 Inside 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 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 125 .9 .8 .2 .2 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 8.3 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 57 9.9 19.0 5.3 -1.7 BETTER c. Chi-1 gauche plus st dev 57 7.6 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 132 9.7 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 51 6.8 20.4 5.0 -2.7 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 93.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .86 2 Residue-by-residue listing for refined_19 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .16 Chi1-chi2 distribution -.22 Chi1 only -.05 Chi3 & chi4 .39 Omega .18 ------ .12 ===== Main-chain covalent forces:- Main-chain bond lengths .26 Main-chain bond angles .39 ------ .34 ===== OVERALL AVERAGE .20 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.