Residue-by-residue listing for refined_4 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 181.9 - - - 2 SER 2 B 54.9 - - - - - - - - - 179.2 - 34.5 - 3 ASP 3 B - 183.5 - - - - - - - - 179.3 - 34.9 - 4 PRO 4 - - - - - -51.5 - - - - - 182.5 - 38.4 - * * * 5 GLY 5 h - - - - - - - - - - - 181.7 - - - 6 PRO 6 H - - - - - -63.4 -63.4 -35.6 - - - 181.8 - 38.3 - * * 7 GLU 7 H A 64.4 - - - - -74.5 -34.2 - - - 176.6 - 31.6 - 8 ALA 8 H A - - - - - -70.4 -35.1 - - - 176.1 - 33.5 - 9 ALA 9 H A - - - - - -67.8 -40.6 - - - 177.4 -2.3 34.0 - 10 ARG 10 H A - 186.8 - 187.2 - -62.9 -33.8 - - - 179.4 -2.4 34.8 - 11 LEU 11 H A - 175.0 - - - -66.4 -38.0 - - - 175.6 -1.6 33.9 - 12 ARG 12 H A - - -62.2 177.3 - -62.8 -42.9 - - - 179.6 -1.5 35.6 - 13 PHE 13 H A - 180.5 - - - -64.3 -45.7 - - - 175.9 -2.1 35.0 - 14 ARG 14 H A - - -80.0 - - -69.4 -29.6 - - - 180.4 -3.1 33.8 - * * 15 CYS 15 H A - 180.0 - - - -71.6 -24.9 - - - 182.8 -2.0 34.9 - * * 16 PHE 16 h B - 182.9 - - - - - - - - 178.9 -1.0 33.3 - * * 17 HIS 17 B 69.9 - - - - - - - - - 174.4 - 34.5 - 18 TYR 18 B - 171.4 - - - - - - - - 180.5 -1.2 32.8 - * * 19 GLU 19 t B 57.0 - - 171.4 - - - - - - 179.4 -.8 33.0 - +* +* 20 GLU 20 T A - - -61.7 177.8 - - - - - - 179.2 - 35.3 - 21 ALA 21 T A - - - - - - - - - - 180.6 - 34.0 - Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 THR 22 T A - 200.8 - - - - - - - - 182.4 -.9 34.6 - * +* +* 23 GLY 23 h - - - - - - - - - - - 184.5 -1.0 - - * * 24 PRO 24 H - - - - - -70.6 -70.6 -31.0 - - - 182.8 - 38.2 - * * 25 GLN 25 H A - - -52.3 - - -69.9 -39.3 - - - 180.1 - 35.4 - 26 GLU 26 H A - 180.1 - 167.3 - -75.4 -38.2 - - - 176.7 - 32.5 - 27 ALA 27 H A - - - - - -55.8 -35.8 - - - 177.6 -2.4 34.6 - 28 LEU 28 H A - - -66.6 180.1 - -60.7 -35.4 - - - 180.7 -1.6 33.9 - 29 ALA 29 H A - - - - - -67.0 -41.8 - - - 177.2 -1.0 33.7 - * * 30 GLN 30 H A - - -78.8 - - -65.3 -47.8 - - - 177.5 -1.4 33.3 - 31 LEU 31 H A - - -72.1 169.1 - -61.6 -43.8 - - - 179.9 -2.9 33.3 - * * 32 ARG 32 H A - 179.4 - 173.8 - -59.1 -45.3 - - - 177.7 -3.2 32.6 - +* +* 33 GLU 33 H A - 179.9 - - - -61.4 -50.2 - - - 181.9 -2.0 36.2 - 34 LEU 34 H A - - -62.9 174.3 - -64.6 -41.4 - - - 178.4 -2.5 32.8 - 35 CYS 35 H A 68.2 - - - - -68.2 -33.0 - - - 178.7 -3.3 33.5 - +* +* 36 ARG 36 H A - 185.0 - - - -66.9 -36.4 - - - 177.6 -2.0 33.7 - 37 GLN 37 H A - - -61.9 186.2 - -63.6 -27.9 - - - 181.2 -1.9 35.4 - * * 38 TRP 38 H A - 165.7 - - - -86.0 -55.3 - - - 183.3 -1.0 35.1 - * +* * * +* 39 LEU 39 H A - - -62.8 156.9 - -75.5 -47.1 - - - 178.0 -3.5 34.0 - * +* +* 40 ARG 40 h l - - -64.9 180.5 - - - - - - 177.3 -1.9 30.9 - 41 PRO 41 T - - - - - -65.3 - - - - - 179.9 - 38.7 - * * 42 GLU 42 T A 60.4 - - 191.5 - - - - - - 182.5 - 34.8 - 43 VAL 43 T a - 177.5 - - - - - - - - 184.3 -1.5 36.4 - 44 ARG 44 t B - - -65.0 183.9 - - - - - - 179.0 -3.7 33.4 - ** ** 45 SER 45 h B - - -54.1 - - - - - - - 178.7 - 36.2 - 46 LYS 46 H A - - -64.8 169.0 - -51.6 -43.5 - - - 182.7 - 36.2 - * * 47 GLU 47 H A 53.7 - - 174.9 - -59.3 -29.0 - - - 176.1 - 30.1 - * * 48 GLN 48 H A - - -73.0 - - -73.7 -32.9 - - - 182.1 -1.3 33.7 - 49 MET 49 H A - - -60.9 179.4 - -64.7 -38.3 - - - 175.4 -1.1 33.0 - * * 50 LEU 50 H A - - -74.0 - - -54.1 -53.9 - - - 183.1 -1.5 33.7 - * * 51 GLU 51 H A - - -61.0 185.4 - -59.6 -44.0 - - - 180.6 -1.1 33.4 - * * 52 LEU 52 H A - - -60.8 180.3 - -61.4 -42.2 - - - 180.1 -2.1 34.3 - 53 LEU 53 H A - 180.5 - - - -75.8 -30.6 - - - 173.9 -2.4 32.0 - * * 54 VAL 54 H A - 183.8 - - - -60.6 -45.4 - - - 178.1 -2.6 34.2 - 55 LEU 55 H A - 177.6 - - - -56.1 -45.7 - - - 183.2 -2.5 35.3 - 56 GLU 56 H A - 190.6 - - - -56.0 -51.3 - - - 178.0 -1.7 33.2 - * * 57 GLN 57 H A - 173.3 - - - -74.1 -36.4 - - - 179.4 -1.9 31.9 - 58 PHE 58 H A - 178.7 - - - -55.6 -46.4 - - - 179.2 -3.1 33.4 - * * Residue-by-residue listing for refined_4 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 - - -62.5 188.9 - -64.2 -37.7 - - - 179.0 -3.0 30.9 - * * 60 GLY 60 H - - - - - - -80.8 -17.9 - - - 177.9 -1.3 - - * +* * +* 61 ALA 61 H A - - - - - -75.0 -27.6 - - - 175.6 -2.0 33.7 - * * 62 LEU 62 h B - - -67.9 170.1 - - - - - - 178.5 -1.2 36.4 - * * 63 PRO 63 h - - - - - -72.6 - - - - - 182.1 - 37.7 - * * 64 PRO 64 H - - - - - -38.0 -38.0 -45.5 - - - 181.5 - 38.1 - ** ** * ** 65 GLU 65 H A 52.8 - - - - -67.6 -47.3 - - - 179.9 - 30.0 - * * 66 ILE 66 H A - - -57.7 179.1 - -67.8 -45.9 - - - 181.5 - 34.4 - 67 GLN 67 H A - 181.8 - 178.0 - -60.6 -41.3 - - - 179.6 -3.3 33.9 - +* +* 68 ALA 68 H A - - - - - -63.1 -37.8 - - - 178.3 -2.2 33.6 - 69 ARG 69 H A - - -65.5 - - -67.5 -48.9 - - - 179.1 -1.5 33.4 - 70 VAL 70 H A - 176.6 - - - -58.0 -33.9 - - - 182.2 -2.7 35.0 - 71 GLN 71 H A - 210.1 - - - -60.9 -26.0 - - - 175.8 -2.1 32.4 - +* * +* 72 GLY 72 H - - - - - - -64.1 -35.4 - - - 182.1 -1.8 - - 73 GLN 73 H a 47.2 - - - - -103.5 -51.8 - - - 192.5 -1.3 31.0 - * *** * ** *** 74 ARG 74 h l - - -76.6 - - - - - - - 178.2 -2.6 28.8 - * * 75 PRO 75 - - - - - -53.9 - - - - - 177.5 - 39.6 - * +* +* 76 GLY 76 S - - - - - - - - - - - 177.9 - - - 77 SER 77 h B 48.2 - - - - - - - - - 186.7 - 32.8 - * * * 78 PRO 78 H - - - - - -57.7 -57.7 -45.1 - - - 182.3 - 37.5 - * * 79 GLU 79 H A - - -63.5 173.9 - -71.6 -32.9 - - - 178.5 - 34.2 - 80 GLU 80 H A - 190.1 - - - -65.0 -44.0 - - - 175.2 - 35.5 - 81 ALA 81 H A - - - - - -60.5 -46.2 - - - 179.1 -2.4 34.2 - 82 ALA 82 H A - - - - - -55.4 -30.6 - - - 178.7 -2.7 33.8 - 83 ALA 83 H A - - - - - -71.4 -51.1 - - - 180.4 -1.4 33.2 - * * 84 LEU 84 H A 49.6 - - 144.0 - -69.2 -36.5 - - - 180.9 -1.7 29.6 - +* * +* 85 VAL 85 H A - - -58.6 - - -66.0 -31.2 - - - 176.9 -2.9 30.3 - * * * 86 ASP 86 H A - 189.2 - - - -62.3 -28.6 - - - 174.0 -1.1 31.7 - * * * 87 GLY 87 H - - - - - - -84.2 -35.1 - - - 183.3 -1.0 - - +* * +* 88 LEU 88 H A - - -61.6 174.8 - -80.5 -7.3 - - - 180.8 -2.1 35.0 - * +** +** 89 ARG 89 h b 53.9 - - 185.1 - - - - - - 181.5 -1.2 32.5 - * * 90 ARG 90 S XX - - -60.1 176.9 - - - - - - 174.7 -2.6 32.0 - **** **** 91 GLU 91 S B - - -61.5 - - - - - - - 181.5 -2.1 34.3 - 92 PRO 92 - - - - - -52.3 - - - - - 180.2 - 38.8 - * * * Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 GLY 93 - - - - - - - - - - - 177.0 -3.0 - - * * 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 180.2 - - - 96 SER 302 B 54.2 - - - - - - - - - 176.8 - 35.4 - 97 ASP 303 B - 178.7 - - - - - - - - 181.3 - 33.1 - 98 PRO 304 - - - - - -74.6 - - - - - 177.9 - 38.7 - * * 99 GLY 305 h - - - - - - - - - - - 178.5 - - - 100 PRO 306 H - - - - - -61.4 -61.4 -26.5 - - - 177.8 - 38.7 - * * * 101 GLU 307 H A 58.8 - - 179.8 - -63.0 -36.3 - - - 179.5 - 33.7 - 102 ALA 308 H A - - - - - -75.2 -37.3 - - - 177.4 -.9 34.0 - * * 103 ALA 309 H A - - - - - -65.9 -40.2 - - - 177.3 -1.6 34.0 - 104 ARG 310 H A - 184.4 - 178.8 - -65.6 -33.4 - - - 179.0 -2.8 33.8 - * * 105 LEU 311 H A - 174.5 - - - -64.8 -38.8 - - - 176.5 -1.3 34.7 - 106 ARG 312 H A - - -57.7 175.3 - -61.1 -45.6 - - - 181.1 -1.7 36.3 - 107 PHE 313 H A - 180.4 - - - -65.1 -45.6 - - - 177.7 -1.9 34.8 - 108 ARG 314 H A - - -82.6 - - -71.6 -34.3 - - - 181.4 -3.2 32.9 - * +* +* 109 CYS 315 H A - 181.9 - - - -78.3 -15.9 - - - 179.3 -2.6 33.4 - * ** ** 110 PHE 316 h B - 182.5 - - - - - - - - 177.6 -1.0 34.1 - * * 111 HIS 317 B 72.5 - - - - - - - - - 172.6 - 34.2 - * * 112 TYR 318 B - 166.2 - - - - - - - - 178.8 -1.5 31.9 - * * 113 GLU 319 t B 50.4 - - 179.5 - - - - - - 181.6 -.8 31.8 - +* +* 114 GLU 320 T A - - -60.5 172.9 - - - - - - 180.2 -.6 35.4 - +* +* 115 ALA 321 T A - - - - - - - - - - 181.9 - 33.7 - 116 THR 322 T A - 200.9 - - - - - - - - 181.2 -1.5 34.8 - * * 117 GLY 323 h - - - - - - - - - - - 183.7 -1.0 - - * * 118 PRO 324 H - - - - - -71.4 -71.4 -35.2 - - - 182.4 - 38.3 - * * 119 GLN 325 H A - - -51.4 - - -66.4 -35.2 - - - 180.5 - 35.4 - * * 120 GLU 326 H A - 177.1 - 165.1 - -75.2 -46.3 - - - 178.5 - 32.7 - 121 ALA 327 H A - - - - - -55.6 -33.7 - - - 175.9 -2.5 34.2 - 122 LEU 328 H A - - -66.7 180.9 - -60.2 -34.3 - - - 178.9 -1.9 33.6 - 123 ALA 329 H A - - - - - -64.9 -44.0 - - - 177.6 -1.4 34.0 - 124 GLN 330 H A - - -78.0 - - -63.8 -51.4 - - - 178.8 -1.4 33.9 - * * 125 LEU 331 H A - - -71.7 170.6 - -59.2 -44.7 - - - 180.0 -3.2 32.9 - +* +* 126 ARG 332 H A - 178.8 - 173.2 - -62.3 -43.2 - - - 175.5 -2.9 32.5 - * * 127 GLU 333 H A - 176.8 - - - -58.8 -50.6 - - - 181.5 -2.0 37.2 - 128 LEU 334 H A - - -63.0 175.4 - -63.7 -44.5 - - - 179.5 -2.8 33.5 - * * Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 129 CYS 335 H A 69.2 - - - - -66.6 -31.8 - - - 179.4 -3.3 33.2 - +* +* 130 ARG 336 H A - 184.5 - - - -69.9 -33.5 - - - 177.7 -2.0 33.5 - 131 GLN 337 H A - - -61.8 181.7 - -67.7 -22.9 - - - 181.1 -1.8 35.5 - * * 132 TRP 338 H a - 163.6 - - - -92.7 -56.8 - - - 181.6 -.9 35.0 - * ** +* +* ** 133 LEU 339 H A - - -62.9 157.3 - -71.4 -46.8 - - - 177.7 -3.6 34.1 - * ** ** 134 ARG 340 h l - - -59.0 180.7 - - - - - - 178.3 -1.6 32.3 - 135 PRO 341 T - - - - - -64.3 - - - - - 179.5 - 39.0 - * * 136 GLU 342 T A 55.0 - - 189.5 - - - - - - 182.4 - 33.8 - 137 VAL 343 T a - 178.2 - - - - - - - - 182.6 -1.5 35.9 - 138 ARG 344 t B - - -69.1 177.5 - - - - - - 179.0 -3.7 34.0 - ** ** 139 SER 345 h B - - -56.1 - - - - - - - 183.7 - 35.1 - 140 LYS 346 H A - - -66.9 169.8 - -53.2 -44.1 - - - 186.6 - 34.5 - * * * 141 GLU 347 H A 58.7 - - - - -67.3 -28.3 - - - 174.9 - 26.1 - ** ** 142 GLN 348 H A - - -65.9 - - -65.4 -38.5 - - - 181.1 -.9 33.3 - +* +* 143 MET 349 H A - - -60.6 180.2 - -61.5 -41.3 - - - 175.4 -1.1 33.3 - * * 144 LEU 350 H A - - -76.9 - - -53.9 -53.3 - - - 182.6 -1.6 33.8 - * * 145 GLU 351 H A - - -63.3 187.1 - -61.2 -43.1 - - - 180.0 -1.6 33.0 - 146 LEU 352 H A - - -57.7 178.1 - -59.7 -42.4 - - - 180.7 -2.4 35.5 - 147 LEU 353 H A - 182.4 - - - -77.1 -30.5 - - - 173.2 -2.4 31.8 - * * 148 VAL 354 H A - 182.6 - - - -59.0 -46.6 - - - 178.7 -2.5 34.8 - 149 LEU 355 H A - 177.2 - - - -57.3 -45.9 - - - 183.6 -2.6 35.6 - 150 GLU 356 H A - 191.8 - - - -58.4 -46.1 - - - 177.0 -1.7 33.5 - 151 GLN 357 H A - 174.6 - - - -74.3 -39.4 - - - 179.9 -2.0 33.0 - 152 PHE 358 H A - 177.7 - - - -54.3 -44.9 - - - 180.0 -3.1 33.6 - * * 153 LEU 359 H A - - -59.7 187.4 - -67.2 -37.3 - - - 179.8 -2.9 31.7 - * * 154 GLY 360 H - - - - - - -80.4 -21.1 - - - 177.1 -1.2 - - * +* * +* 155 ALA 361 H A - - - - - -70.8 -30.7 - - - 176.1 -2.3 33.9 - 156 LEU 362 h b - - -63.3 168.6 - - - - - - 176.4 -1.2 37.5 - * * * 157 PRO 363 h - - - - - -69.6 - - - - - 180.5 - 39.0 - * * 158 PRO 364 H - - - - - -40.6 -40.6 -42.4 - - - 180.3 - 38.7 - ** ** * ** 159 GLU 365 H A 55.6 - - 182.9 - -62.6 -47.9 - - - 179.6 - 32.4 - 160 ILE 366 H A - - -58.2 179.2 - -73.1 -37.7 - - - 180.7 -.6 34.9 - +* +* 161 GLN 367 H A - 181.3 - 176.9 - -65.4 -40.2 - - - 178.4 -3.2 34.2 - +* +* 162 ALA 368 H A - - - - - -63.2 -31.3 - - - 177.3 -2.8 33.8 - * * 163 ARG 369 H A - - -60.6 - - -67.2 -50.7 - - - 180.0 -1.0 35.3 - * * Residue-by-residue listing for refined_4 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 - 174.6 - - - -56.7 -39.3 - - - 183.2 -2.0 35.7 - 165 GLN 371 H A - 230.4 - - - -53.7 -28.5 - - - 180.9 -2.3 34.4 - +** +** 166 GLY 372 H - - - - - - -73.8 -41.5 - - - 179.3 -1.6 - - 167 GLN 373 H A 51.4 - - - - -91.5 -39.0 - - - 180.9 -.7 30.8 - ** +* ** 168 ARG 374 h l - 197.6 - - - - - - - - 181.6 -3.3 34.1 - +* +* 169 PRO 375 - - - - - -57.3 - - - - - 178.5 - 38.6 - * * 170 GLY 376 - - - - - - - - - - - 175.0 - - - 171 SER 377 h B 45.5 - - - - - - - - - 188.1 - 32.7 - * * * 172 PRO 378 H - - - - - -58.5 -58.5 -45.4 - - - 182.4 - 37.1 - 173 GLU 379 H A - - -64.9 176.4 - -73.5 -31.0 - - - 175.7 - 31.9 - 174 GLU 380 H A - 185.4 - - - -61.2 -50.8 - - - 178.3 - 36.1 - * * 175 ALA 381 H A - - - - - -58.4 -46.8 - - - 180.0 -2.5 34.4 - 176 ALA 382 H A - - - - - -55.4 -37.4 - - - 178.4 -2.7 33.6 - 177 ALA 383 H A - - - - - -66.7 -50.1 - - - 179.2 -1.8 32.9 - 178 LEU 384 H A 47.3 - - 135.4 - -65.7 -43.1 - - - 181.8 -2.0 29.3 - * ** * ** 179 VAL 385 H A - - -61.6 - - -63.3 -32.2 - - - 180.0 -3.1 30.4 - * * * 180 ASP 386 H A - 188.9 - - - -64.6 -30.8 - - - 176.0 -1.6 32.3 - 181 GLY 387 H - - - - - - -84.4 -21.4 - - - 180.6 -.9 - - +* +* * +* 182 LEU 388 H A - - -61.6 177.8 - -78.3 -39.4 - - - 179.3 -1.2 35.0 - * * * 183 ARG 389 h b 51.3 - - 171.5 - - - - - - 178.5 -2.5 33.9 - 184 ARG 390 S p - - -64.0 174.1 - - - - - - 177.1 -.8 34.0 - +* +* 185 GLU 391 S B - - -62.1 - - - - - - - 186.4 - 33.0 - * * 186 PRO 392 - - - - - -63.0 - - - - - 177.5 - 38.4 - * * 187 GLY 393 - - - - - - - - - - - 180.8 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +** * ** ** *** +** ** ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.3 182.6 -64.3 175.8 -60.3 -65.9 -38.9 - - - 179.5 -2.0 34.2 Standard deviations: 7.7 10.9 6.7 9.9 10.3 9.2 8.6 - - - 2.8 .8 2.2 Numbers of values: 24 51 57 57 18 126 126 0 0 0 186 127 170 0 Residue-by-residue listing for refined_4 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_4 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 1.497 - 1.463 - 117.11 120.10 - 110.27 - 122.78 * * 2 SER 2 1.296 1.236 1.512 1.537 1.434 121.43 116.87 120.22 111.40 109.65 109.50 122.91 ** * ** 3 ASP 3 1.306 1.240 1.516 1.532 1.442 121.17 118.50 119.42 110.25 108.02 110.30 121.99 +* * * +* 4 PRO 4 1.348 1.236 1.538 1.543 1.469 122.89 116.56 120.52 110.07 113.18 104.00 122.89 5 GLY 5 1.317 1.241 1.509 - 1.431 121.03 118.53 119.72 - 110.57 - 121.76 * * * 6 PRO 6 1.342 1.222 1.531 1.538 1.461 122.33 116.86 120.83 110.59 112.06 103.83 122.22 7 GLU 7 1.319 1.234 1.521 1.557 1.446 120.88 116.08 120.80 111.84 110.22 112.94 123.09 * * * 8 ALA 8 1.325 1.234 1.526 1.517 1.454 121.60 115.90 121.28 110.81 109.77 110.94 122.81 9 ALA 9 1.323 1.232 1.515 1.507 1.449 121.79 115.77 121.05 110.28 109.72 110.75 123.16 10 ARG 10 1.329 1.218 1.521 1.519 1.448 121.86 116.14 121.00 108.48 109.65 111.53 122.86 11 LEU 11 1.323 1.210 1.528 1.521 1.405 122.60 116.83 120.12 112.38 110.12 109.11 123.02 * +** * +** 12 ARG 12 1.332 1.235 1.528 1.525 1.475 122.11 114.30 121.79 108.41 109.44 110.39 123.91 13 PHE 13 1.311 1.222 1.548 1.535 1.454 124.88 116.42 120.74 113.03 110.63 106.51 122.82 * * +* +* ** ** 14 ARG 14 1.326 1.233 1.530 1.541 1.474 122.90 116.09 120.79 109.75 112.10 111.07 123.11 15 CYS 15 1.317 1.240 1.520 1.541 1.455 122.94 116.10 120.50 110.23 110.61 109.59 123.39 Residue-by-residue listing for refined_4 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 16 PHE 16 1.329 1.235 1.520 1.536 1.443 122.02 115.45 121.26 110.97 110.92 111.06 123.29 17 HIS 17 1.308 1.232 1.510 1.573 1.445 122.06 118.04 119.85 109.99 108.64 111.54 122.10 * ** ** 18 TYR 18 1.293 1.235 1.498 1.527 1.425 118.53 115.24 121.43 111.38 108.31 112.47 123.32 +** * +* +* * * +** 19 GLU 19 1.284 1.240 1.502 1.537 1.405 121.34 115.28 121.36 111.77 109.91 111.39 123.35 *** * +** *** 20 GLU 20 1.296 1.229 1.513 1.503 1.439 122.54 115.23 121.04 109.62 109.94 109.46 123.73 ** * * ** 21 ALA 21 1.322 1.228 1.526 1.515 1.447 123.50 117.15 120.35 110.34 112.09 110.02 122.50 22 THR 22 1.321 1.227 1.552 1.580 1.439 119.85 116.19 121.12 111.20 108.89 110.02 122.57 * * * * 23 GLY 23 1.340 1.235 1.529 - 1.458 121.43 119.83 119.70 - 110.96 - 120.47 +* +* +* 24 PRO 24 1.348 1.227 1.523 1.511 1.460 121.24 116.84 120.27 110.38 113.85 103.53 122.87 25 GLN 25 1.321 1.231 1.520 1.529 1.446 121.37 115.35 121.52 108.44 108.62 111.11 123.13 26 GLU 26 1.322 1.224 1.518 1.528 1.436 122.07 116.35 120.49 113.18 110.48 110.05 123.10 * +* +* 27 ALA 27 1.331 1.233 1.525 1.522 1.470 122.56 115.61 120.86 110.10 110.29 109.93 123.51 28 LEU 28 1.323 1.212 1.516 1.522 1.456 122.81 117.30 119.98 109.24 112.36 111.29 122.72 29 ALA 29 1.322 1.242 1.521 1.522 1.460 121.30 115.10 121.30 110.91 109.86 110.62 123.58 30 GLN 30 1.322 1.230 1.525 1.553 1.450 122.85 115.96 120.96 111.95 110.30 110.41 123.05 * * 31 LEU 31 1.319 1.222 1.519 1.525 1.457 122.31 116.84 120.13 110.93 112.13 110.51 123.02 32 ARG 32 1.326 1.217 1.520 1.530 1.456 122.02 116.15 120.63 111.22 111.41 111.45 123.20 33 GLU 33 1.298 1.228 1.536 1.526 1.461 123.02 116.17 120.71 110.39 109.93 107.45 123.09 ** +* ** 34 LEU 34 1.314 1.231 1.525 1.518 1.456 122.36 117.11 120.33 111.68 112.48 110.18 122.55 * * 35 CYS 35 1.323 1.218 1.526 1.548 1.455 120.52 115.86 121.27 110.75 109.11 111.69 122.86 36 ARG 36 1.330 1.205 1.533 1.545 1.414 123.27 117.76 119.42 113.77 110.45 108.14 122.82 * ** +* * ** 37 GLN 37 1.334 1.229 1.526 1.511 1.479 122.01 114.07 121.89 108.27 110.82 110.25 124.05 * * * 38 TRP 38 1.305 1.234 1.541 1.545 1.442 125.08 116.18 120.94 112.85 111.90 106.35 122.88 +* +* * ** ** 39 LEU 39 1.308 1.232 1.522 1.527 1.451 122.66 116.22 120.17 112.48 111.10 108.41 123.60 +* * * +* 40 ARG 40 1.344 1.219 1.512 1.534 1.460 123.55 117.92 120.54 110.89 114.31 112.88 121.54 * * * * * 41 PRO 41 1.337 1.229 1.533 1.537 1.473 122.38 114.41 121.78 110.69 110.88 103.34 123.80 +* * +* 42 GLU 42 1.316 1.235 1.531 1.538 1.430 124.21 116.47 120.77 111.48 110.35 108.61 122.75 * * * * 43 VAL 43 1.339 1.232 1.536 1.562 1.444 121.73 116.78 120.95 107.75 111.30 110.02 122.23 44 ARG 44 1.306 1.234 1.496 1.533 1.439 121.00 114.70 121.26 109.91 112.14 111.70 124.04 +* * * +* 45 SER 45 1.297 1.250 1.521 1.527 1.423 123.53 115.79 120.40 110.34 109.09 108.14 123.81 ** +* * * ** 46 LYS 46 1.324 1.212 1.512 1.515 1.466 123.82 115.83 120.90 108.59 110.94 108.91 123.22 * * 47 GLU 47 1.318 1.233 1.539 1.524 1.456 122.51 117.67 120.25 112.48 114.02 112.31 122.08 * * * * 48 GLN 48 1.332 1.232 1.518 1.541 1.464 120.43 115.66 120.99 108.38 109.92 113.29 123.34 +* +* Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 49 MET 49 1.325 1.233 1.500 1.509 1.453 122.53 116.34 119.89 111.28 111.67 110.70 123.76 * * * 50 LEU 50 1.347 1.206 1.518 1.572 1.461 121.14 117.02 119.70 109.34 109.71 112.86 123.01 * * ** * ** 51 GLU 51 1.346 1.235 1.519 1.525 1.477 121.81 116.47 120.52 108.81 112.34 112.26 123.02 * * * * 52 LEU 52 1.323 1.234 1.519 1.525 1.445 121.81 115.83 121.20 110.34 110.84 110.15 122.95 53 LEU 53 1.310 1.236 1.548 1.520 1.416 121.64 117.48 120.22 115.27 111.75 108.16 122.28 * * ** +** * +** 54 VAL 54 1.341 1.223 1.532 1.567 1.470 120.94 115.24 121.04 108.25 108.32 113.40 123.70 * * * * 55 LEU 55 1.334 1.236 1.518 1.558 1.469 123.99 115.44 120.56 111.00 110.56 108.36 123.99 * * * * 56 GLU 56 1.320 1.248 1.543 1.543 1.444 122.69 116.55 120.97 111.90 111.22 110.18 122.46 57 GLN 57 1.320 1.214 1.514 1.528 1.452 120.62 117.20 119.89 111.90 111.45 111.77 122.89 58 PHE 58 1.328 1.236 1.522 1.540 1.459 121.59 116.31 120.69 110.34 110.79 111.54 122.97 59 LEU 59 1.325 1.219 1.516 1.527 1.450 120.83 117.23 120.12 112.22 112.82 112.25 122.63 * * * 60 GLY 60 1.320 1.234 1.520 - 1.455 119.72 116.46 120.61 - 112.95 - 122.92 61 ALA 61 1.323 1.242 1.516 1.530 1.455 122.29 115.34 120.80 110.84 109.93 110.91 123.85 62 LEU 62 1.334 1.245 1.526 1.529 1.446 123.58 118.06 120.18 108.62 110.34 109.02 121.76 * * 63 PRO 63 1.339 1.248 1.521 1.536 1.433 121.60 117.12 119.89 110.96 109.61 105.14 122.97 ** +* ** 64 PRO 64 1.347 1.222 1.538 1.514 1.467 124.51 118.42 119.55 110.66 115.35 102.99 122.03 * * * 65 GLU 65 1.332 1.239 1.528 1.555 1.458 120.32 117.00 120.20 111.48 112.80 114.27 122.78 * ** ** 66 ILE 66 1.325 1.232 1.530 1.552 1.444 121.50 115.98 120.71 109.86 110.04 111.07 123.26 67 GLN 67 1.333 1.232 1.523 1.524 1.456 122.31 116.31 120.59 109.95 111.27 110.88 123.10 68 ALA 68 1.322 1.233 1.517 1.511 1.460 121.81 116.38 120.55 110.28 111.10 110.88 123.06 69 ARG 69 1.329 1.232 1.512 1.530 1.458 121.09 115.67 120.36 109.94 110.21 112.11 123.95 70 VAL 70 1.336 1.248 1.509 1.543 1.473 123.17 114.58 121.71 108.04 110.90 111.49 123.70 71 GLN 71 1.301 1.220 1.537 1.514 1.419 123.42 116.41 120.88 112.34 110.89 110.85 122.62 ** ** * ** 72 GLY 72 1.320 1.233 1.538 - 1.442 120.65 117.43 120.20 - 112.36 - 122.35 * * 73 GLN 73 1.336 1.217 1.532 1.569 1.464 120.74 117.20 119.83 109.78 114.53 113.97 122.94 +* * ** ** 74 ARG 74 1.329 1.226 1.532 1.551 1.474 122.32 117.04 121.09 110.52 112.10 116.93 121.80 * +*** +*** 75 PRO 75 1.350 1.229 1.540 1.535 1.489 123.61 115.43 121.11 109.68 112.99 102.40 123.45 +* * +* 76 GLY 76 1.318 1.233 1.523 - 1.463 122.38 116.44 120.72 - 113.46 - 122.83 * * 77 SER 77 1.299 1.250 1.543 1.535 1.436 122.31 117.77 120.09 113.69 109.63 109.39 122.10 ** * +* ** 78 PRO 78 1.359 1.234 1.528 1.537 1.475 123.15 117.14 120.24 110.50 114.57 104.41 122.60 * * * * 79 GLU 79 1.318 1.234 1.498 1.494 1.460 121.45 115.34 120.95 109.78 111.19 110.46 123.71 * +* +* 80 GLU 80 1.312 1.233 1.527 1.518 1.431 122.22 115.58 121.06 110.67 107.78 108.96 123.35 * * * * 81 ALA 81 1.347 1.229 1.508 1.510 1.449 122.45 115.85 120.30 110.30 110.36 110.45 123.81 * * Residue-by-residue listing for refined_4 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 82 ALA 82 1.335 1.225 1.534 1.534 1.458 123.23 115.87 121.23 110.99 111.11 110.10 122.88 83 ALA 83 1.307 1.230 1.536 1.517 1.444 122.23 118.36 119.65 110.95 111.67 110.67 121.95 +* * +* 84 LEU 84 1.349 1.227 1.514 1.552 1.473 119.26 116.66 120.61 110.84 112.39 115.48 122.70 * * * +** +** 85 VAL 85 1.324 1.215 1.515 1.536 1.456 120.94 116.49 120.46 111.27 112.16 114.29 123.05 +* +* 86 ASP 86 1.323 1.232 1.542 1.527 1.462 121.85 116.06 121.54 111.93 110.33 112.28 122.35 * * 87 GLY 87 1.316 1.230 1.539 - 1.445 120.52 115.97 121.13 - 111.44 - 122.87 * * 88 LEU 88 1.329 1.231 1.534 1.526 1.481 123.50 117.04 120.28 108.77 113.59 109.73 122.67 * * 89 ARG 89 1.314 1.236 1.536 1.540 1.474 122.75 115.30 121.03 111.93 112.38 110.40 123.66 * * 90 ARG 90 1.343 1.233 1.522 1.542 1.473 124.67 116.25 120.84 112.20 110.06 111.80 122.85 +* * +* 91 GLU 91 1.299 1.240 1.515 1.524 1.424 122.22 117.86 119.54 110.24 107.43 111.42 122.56 ** +* * ** 92 PRO 92 1.344 1.240 1.522 1.531 1.466 122.74 116.09 120.48 110.10 111.95 103.51 123.42 * * 93 GLY 93 1.325 1.235 1.503 - 1.447 121.11 115.36 121.06 - 110.92 - 123.57 94 GLY 94 1.303 1.244 1.503 - 1.434 121.60 - 119.59 - 110.87 - - +* * +* 95 GLY 301 - 1.233 1.509 - 1.450 - 115.64 121.23 - 111.30 - 123.13 96 SER 302 1.303 1.239 1.527 1.527 1.435 122.42 116.60 120.64 110.65 110.44 108.51 122.76 +* * * +* 97 ASP 303 1.311 1.231 1.515 1.531 1.449 121.41 117.63 120.40 110.69 110.23 111.75 121.97 * * 98 PRO 304 1.339 1.231 1.531 1.528 1.472 122.97 116.34 120.84 110.42 112.70 103.18 122.81 99 GLY 305 1.314 1.238 1.510 - 1.426 120.75 118.10 120.12 - 112.08 - 121.77 * +* +* 100 PRO 306 1.346 1.223 1.526 1.533 1.468 122.70 115.91 121.00 110.06 111.26 103.86 123.08 101 GLU 307 1.329 1.236 1.538 1.540 1.453 122.50 115.92 120.82 110.96 110.41 110.59 123.23 102 ALA 308 1.332 1.230 1.514 1.514 1.447 122.44 115.79 121.08 110.63 109.87 110.53 123.12 103 ALA 309 1.323 1.234 1.518 1.510 1.451 121.81 115.64 121.23 110.46 109.78 110.61 123.12 104 ARG 310 1.324 1.220 1.522 1.522 1.442 121.97 116.32 120.81 109.66 110.33 111.65 122.87 105 LEU 311 1.327 1.215 1.530 1.522 1.412 122.64 116.24 120.46 111.70 109.83 108.77 123.28 ** * ** 106 ARG 312 1.330 1.224 1.525 1.529 1.469 122.45 114.22 121.81 108.21 109.00 109.75 123.95 107 PHE 313 1.314 1.223 1.549 1.534 1.450 124.70 116.65 120.70 112.68 111.39 106.83 122.64 * * +* * ** ** 108 ARG 314 1.324 1.231 1.526 1.532 1.469 122.32 117.25 120.32 109.69 113.33 111.79 122.43 109 CYS 315 1.315 1.242 1.523 1.537 1.455 121.21 116.25 120.58 110.69 110.95 111.11 123.16 110 PHE 316 1.320 1.247 1.523 1.537 1.438 122.00 115.80 121.12 110.54 110.08 110.69 123.05 * * 111 HIS 317 1.307 1.234 1.505 1.577 1.442 121.22 118.13 119.97 109.93 108.12 112.27 121.87 +* ** * * ** 112 TYR 318 1.289 1.228 1.499 1.526 1.418 117.80 114.91 121.44 111.91 108.74 113.04 123.63 +** * ** ** * +** 113 GLU 319 1.285 1.237 1.508 1.544 1.408 121.96 114.90 121.30 113.41 109.98 111.44 123.79 *** +** +* *** 114 GLU 320 1.310 1.218 1.516 1.522 1.450 124.06 115.31 121.00 110.06 110.31 108.95 123.66 * * * 115 ALA 321 1.320 1.230 1.539 1.519 1.453 123.20 117.70 120.11 110.54 112.65 110.04 122.18 Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 116 THR 322 1.330 1.225 1.551 1.579 1.449 119.69 116.02 121.14 110.61 109.18 110.08 122.75 * * * * 117 GLY 323 1.329 1.245 1.526 - 1.453 121.29 119.04 120.12 - 111.49 - 120.84 * * * 118 PRO 324 1.344 1.231 1.517 1.508 1.455 121.78 116.93 120.07 110.49 113.55 103.34 122.98 * * 119 GLN 325 1.330 1.234 1.520 1.531 1.450 121.22 115.27 121.40 107.99 108.11 111.63 123.32 * * * 120 GLU 326 1.330 1.220 1.510 1.523 1.434 121.80 116.49 120.38 112.38 110.87 110.49 123.10 * * * 121 ALA 327 1.322 1.226 1.533 1.516 1.464 122.34 116.41 120.50 110.42 110.94 109.92 123.09 122 LEU 328 1.329 1.223 1.518 1.523 1.466 122.15 117.27 120.00 108.79 112.16 112.07 122.73 123 ALA 329 1.324 1.236 1.515 1.521 1.455 121.23 114.66 121.25 110.73 108.96 110.75 124.05 124 GLN 330 1.316 1.225 1.527 1.542 1.449 123.51 116.09 120.81 111.14 110.91 110.09 123.07 * * 125 LEU 331 1.319 1.219 1.517 1.521 1.462 122.67 117.07 119.98 110.66 112.65 111.01 122.94 126 ARG 332 1.319 1.218 1.525 1.521 1.454 121.49 115.89 120.71 112.13 111.09 110.75 123.38 * * 127 GLU 333 1.298 1.227 1.539 1.526 1.464 123.74 116.11 120.68 110.57 109.43 105.77 123.14 ** * +** +** 128 LEU 334 1.322 1.234 1.515 1.518 1.458 122.69 116.89 120.36 110.55 112.32 110.49 122.74 129 CYS 335 1.325 1.214 1.532 1.548 1.442 120.70 116.28 121.16 111.45 109.36 111.35 122.53 130 ARG 336 1.331 1.215 1.538 1.547 1.421 123.10 117.34 119.85 113.73 110.90 108.17 122.80 +* +* * +* 131 GLN 337 1.328 1.238 1.529 1.505 1.475 122.37 113.97 122.01 109.07 110.75 109.27 124.02 * * * 132 TRP 338 1.303 1.239 1.549 1.545 1.441 125.29 116.28 120.93 112.84 111.87 106.41 122.79 +* * +* * ** ** 133 LEU 339 1.309 1.228 1.523 1.533 1.453 123.00 116.09 120.21 112.36 110.75 108.55 123.68 * * * * 134 ARG 340 1.344 1.212 1.523 1.547 1.463 123.82 118.62 119.98 110.26 113.23 112.23 121.40 * * * * * * 135 PRO 341 1.347 1.235 1.534 1.540 1.489 122.43 114.31 121.91 110.16 111.43 103.22 123.78 +* +* * +* 136 GLU 342 1.306 1.235 1.541 1.536 1.432 124.52 116.26 121.27 112.79 111.29 108.41 122.47 +* * +* * * +* 137 VAL 343 1.333 1.229 1.543 1.556 1.446 122.05 116.19 121.26 108.57 111.02 109.78 122.52 * * 138 ARG 344 1.306 1.233 1.505 1.535 1.440 122.12 114.83 121.32 109.86 111.48 111.08 123.84 +* +* 139 SER 345 1.298 1.250 1.524 1.518 1.423 123.56 115.27 120.82 110.76 109.52 109.00 123.90 ** +* * ** 140 LYS 346 1.310 1.216 1.531 1.512 1.458 124.09 118.12 119.92 109.57 114.36 109.26 121.92 * * * * 141 GLU 347 1.322 1.233 1.511 1.551 1.473 119.83 117.17 120.11 113.19 114.19 116.44 122.72 * * +* * *** *** 142 GLN 348 1.331 1.224 1.519 1.554 1.457 119.92 115.49 120.91 109.09 108.83 113.75 123.57 * +* +* 143 MET 349 1.336 1.234 1.501 1.508 1.459 122.72 116.16 120.03 110.77 111.59 110.72 123.80 * * * 144 LEU 350 1.344 1.206 1.514 1.568 1.461 121.51 116.92 119.86 109.28 109.73 112.67 123.02 * * +* * +* 145 GLU 351 1.339 1.237 1.516 1.516 1.470 121.68 116.29 120.34 109.19 112.71 112.18 123.37 146 LEU 352 1.319 1.232 1.517 1.522 1.445 122.26 115.46 121.37 109.46 110.09 109.53 123.15 Residue-by-residue listing for refined_4 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 147 LEU 353 1.309 1.237 1.552 1.520 1.414 121.75 117.42 120.14 115.53 111.82 108.03 122.42 * * ** +** * +** 148 VAL 354 1.346 1.222 1.526 1.570 1.476 121.10 114.90 121.19 107.45 107.97 113.48 123.90 * * * * * 149 LEU 355 1.328 1.234 1.513 1.554 1.460 124.25 115.39 120.66 110.87 110.66 108.21 123.95 * * * * 150 GLU 356 1.314 1.241 1.539 1.533 1.438 122.59 116.38 121.09 111.96 110.95 109.65 122.52 * * * 151 GLN 357 1.317 1.213 1.506 1.516 1.450 120.80 116.65 120.08 110.92 111.07 111.31 123.27 152 PHE 358 1.322 1.236 1.523 1.539 1.452 122.08 116.19 120.67 110.48 110.96 111.05 123.12 153 LEU 359 1.322 1.223 1.516 1.524 1.450 120.76 117.03 120.32 111.61 112.53 111.92 122.63 154 GLY 360 1.314 1.239 1.512 - 1.445 119.87 116.24 120.34 - 112.79 - 123.41 * * 155 ALA 361 1.324 1.231 1.516 1.530 1.452 122.49 115.69 120.72 110.57 109.88 110.90 123.58 156 LEU 362 1.332 1.245 1.536 1.524 1.453 123.20 118.39 120.22 107.20 109.24 108.76 121.39 * +* * * +* 157 PRO 363 1.334 1.241 1.516 1.535 1.441 121.65 117.89 119.25 109.64 108.63 104.67 122.86 +* * +* +* 158 PRO 364 1.348 1.210 1.536 1.518 1.472 124.00 117.14 120.13 110.69 113.85 102.51 122.70 * * 159 GLU 365 1.329 1.228 1.548 1.535 1.466 121.82 117.29 120.31 111.97 112.71 110.35 122.36 * * 160 ILE 366 1.333 1.233 1.531 1.557 1.450 121.93 115.25 121.54 110.00 109.70 110.31 123.18 161 GLN 367 1.313 1.241 1.540 1.522 1.445 122.84 116.17 120.90 111.15 110.99 109.29 122.92 * * 162 ALA 368 1.323 1.225 1.519 1.521 1.468 122.51 116.23 120.94 110.08 110.92 110.94 122.83 163 ARG 369 1.315 1.235 1.530 1.524 1.450 121.59 115.26 120.98 109.27 108.99 110.23 123.72 * * 164 VAL 370 1.342 1.244 1.506 1.539 1.475 123.76 114.25 121.49 107.13 111.60 111.23 124.26 * * 165 GLN 371 1.301 1.226 1.545 1.523 1.439 124.32 116.96 120.10 111.32 111.62 108.76 122.93 ** * * * ** 166 GLY 372 1.340 1.225 1.537 - 1.453 120.78 118.12 120.32 - 113.69 - 121.55 * * 167 GLN 373 1.327 1.224 1.512 1.562 1.478 119.75 115.33 120.63 110.58 111.70 114.68 124.02 +* * * ** ** 168 ARG 374 1.322 1.221 1.560 1.540 1.457 124.34 118.15 120.26 109.57 110.66 111.18 121.53 +* * +* 169 PRO 375 1.358 1.218 1.543 1.540 1.489 122.93 116.01 121.25 110.15 113.26 103.40 122.73 * +* +* 170 GLY 376 1.321 1.230 1.523 - 1.462 121.41 116.25 120.38 - 113.13 - 123.37 171 SER 377 1.305 1.249 1.547 1.532 1.440 123.08 117.77 120.25 113.78 109.11 109.50 121.94 +* * +* +* 172 PRO 378 1.358 1.235 1.534 1.537 1.473 123.06 117.83 119.89 110.68 115.50 104.57 122.24 * * * * 173 GLU 379 1.317 1.235 1.505 1.518 1.465 120.64 115.65 120.71 111.99 111.53 111.53 123.62 174 GLU 380 1.324 1.241 1.522 1.523 1.446 122.37 115.02 121.17 109.49 107.97 109.06 123.79 * * 175 ALA 381 1.344 1.228 1.507 1.505 1.448 122.95 116.09 120.15 109.80 111.17 110.27 123.76 * * 176 ALA 382 1.334 1.223 1.533 1.531 1.457 122.75 115.72 121.16 111.27 110.96 110.13 123.10 177 ALA 383 1.303 1.234 1.539 1.523 1.453 122.55 117.91 119.92 111.18 111.60 110.89 122.15 +* +* 178 LEU 384 1.353 1.228 1.514 1.549 1.465 119.13 116.76 120.33 111.08 112.48 115.68 122.86 +* * *** *** Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 179 VAL 385 1.332 1.217 1.502 1.542 1.456 121.02 117.03 119.71 110.32 113.05 114.83 123.24 * +* +* 180 ASP 386 1.325 1.231 1.529 1.526 1.460 121.18 115.81 121.35 111.51 110.45 111.79 122.83 181 GLY 387 1.322 1.227 1.530 - 1.446 120.82 116.34 120.80 - 112.14 - 122.86 182 LEU 388 1.327 1.240 1.514 1.529 1.469 122.65 115.39 120.87 108.63 111.25 110.64 123.72 183 ARG 389 1.310 1.241 1.524 1.535 1.445 123.11 115.51 120.92 110.57 111.04 110.53 123.53 * * 184 ARG 390 1.330 1.237 1.525 1.535 1.460 122.95 116.72 120.58 111.30 110.56 109.70 122.65 185 GLU 391 1.306 1.236 1.520 1.523 1.440 121.09 116.86 120.48 111.97 109.39 110.95 122.66 +* +* 186 PRO 392 1.333 1.241 1.526 1.526 1.462 123.38 114.77 121.67 110.19 114.17 103.50 123.56 * * * 187 GLY 393 1.302 1.233 1.497 - 1.427 122.87 117.94 119.33 - 108.87 - 122.73 +* * * * * +* 188 GLY 394 1.299 - 1.489 - 1.435 120.12 - - - 111.02 - - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** * +* ** +** ** +* +** * +*** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 1.284 1.353 1.321 .013 *** +* C-N (Pro) 1.341 .016 18 1.333 1.359 1.346 .007 * C-O C-O 1.231 .020 187 1.205 1.250 1.231 .009 * CA-C CH1E-C (except Gly) 1.525 .021 170 1.496 1.560 1.524 .012 * +* CH2G*-C (Gly) 1.516 .018 18 1.489 1.539 1.516 .015 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.505 1.534 1.519 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.536 1.580 1.557 .015 * CH1E-CH2E (the rest) 1.530 .020 138 1.494 1.577 1.532 .014 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.405 1.481 1.451 .016 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.426 1.463 1.446 .012 +* N-CH1E (Pro) 1.466 .015 18 1.433 1.489 1.468 .014 ** +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 2.0 152 113.97 118.62 116.28 .97 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.36 119.83 117.18 1.26 +* CH1E-C-N (Pro) 116.9 1.5 18 114.31 118.42 116.45 1.13 +* * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.47 124.26 122.97 .67 +* O-C-N (Pro) 122.0 1.4 18 122.03 123.80 122.94 .50 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 117.80 125.29 122.18 1.26 ** +* C-NH1-CH2G* (Gly) 120.6 1.7 16 119.72 122.87 121.02 .81 * C-N-CH1E (Pro) 122.6 5.0 18 121.24 124.51 122.74 .83 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 119.25 122.01 120.66 .56 CH2G*-C-O (Gly) 120.8 2.1 17 119.33 121.23 120.32 .54 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.80 111.27 110.58 .38 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 107.13 111.27 109.20 1.44 CH2E-CH1E-C (the rest) 110.1 1.9 138 107.20 115.53 110.79 1.44 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.43 114.53 110.76 1.42 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 108.87 113.69 111.68 1.21 * N-CH1E-C (Pro) 111.8 2.5 18 108.63 115.50 112.71 1.80 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.92 110.94 110.51 .36 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 109.78 114.83 111.67 1.76 * +* N-CH1E-CH2E (Pro) 103.0 1.1 18 102.40 105.14 103.63 .70 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 105.77 116.93 110.65 1.97 +** +*** ------------------------------------------------------------------------------------------------------------- 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_4 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] 139 91.4% Residues in additional allowed regions [a,b,l,p] 12 7.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 1 .7% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 91.4 83.8 10.0 .8 Inside b. Omega angle st dev 186 2.8 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 127 .8 .8 .2 -.1 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 24 7.7 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 51 10.9 19.0 5.3 -1.5 BETTER c. Chi-1 gauche plus st dev 57 6.7 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 132 9.3 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 57 9.9 20.4 5.0 -2.1 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% 91.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .79 2 Residue-by-residue listing for refined_4 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .18 Chi1-chi2 distribution -.19 Chi1 only .17 Chi3 & chi4 .29 Omega .20 ------ .13 ===== Main-chain covalent forces:- Main-chain bond lengths .28 Main-chain bond angles .40 ------ .35 ===== OVERALL AVERAGE .21 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.