Residue-by-residue listing for refined_5 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 - - - - - - - - - - - 177.3 - - - 2 SER 2 B - 179.1 - - - - - - - - 179.4 - 34.8 - 3 ASP 3 B - 188.6 - - - - - - - - 175.1 - 35.3 - 4 PRO 4 h - - - - - -57.6 - - - - - 178.1 - 39.0 - * * 5 GLY 5 H - - - - - - 75.4 165.1 - - - 176.9 - - - *11.8**18.1* *18.1* 6 PRO 6 H - - - - - -69.2 -69.2 -22.2 - - - 182.6 - 38.9 - +* * +* 7 GLU 7 H A - - -57.3 172.2 - -63.7 -55.7 - - - 184.0 - 36.7 - * * 8 ALA 8 H A - - - - - -74.6 -41.2 - - - 182.5 -1.2 33.6 - * * 9 ALA 9 H A - - - - - -63.1 -44.8 - - - 178.9 -1.7 32.6 - 10 ARG 10 H A - 186.9 - 189.8 - -67.3 -33.2 - - - 180.7 -1.9 33.8 - 11 LEU 11 H A - 176.0 - - - -63.4 -41.2 - - - 177.2 -1.3 34.8 - 12 ARG 12 H A - - -58.2 177.0 - -68.8 -44.2 - - - 179.4 -2.2 35.2 - 13 PHE 13 H A - 179.9 - - - -59.5 -39.5 - - - 177.4 -2.6 34.7 - 14 ARG 14 H A - - -70.2 - - -87.4 -8.9 - - - 177.3 -2.8 33.0 - +* +** * +** 15 CYS 15 H A - 180.7 - - - -85.4 -19.9 - - - 179.7 -.6 34.6 - +* +* +* +* 16 PHE 16 h B - 184.5 - - - - - - - - 176.7 -1.1 35.4 - * * 17 HIS 17 B 75.2 - - - - - - - - - 174.2 - 34.6 - 18 TYR 18 B - 165.8 - - - - - - - - 177.7 -1.1 32.2 - * * * Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 19 GLU 19 t B 45.2 - - 178.4 - - - - - - 183.5 -.5 33.0 - * ** ** 20 GLU 20 T A - - -49.2 - - - - - - - 180.0 -.5 34.3 - * ** ** 21 ALA 21 T A - - - - - - - - - - 181.4 - 33.5 - 22 THR 22 T A - 202.2 - - - - - - - - 180.6 -1.6 34.2 - * * 23 GLY 23 h - - - - - - - - - - - 183.4 -1.0 - - * * 24 PRO 24 H - - - - - -67.5 -67.5 -39.1 - - - 182.4 - 37.7 - * * 25 GLN 25 H A - - -90.0 158.0 - -76.8 -29.6 - - - 174.3 - 30.6 - +* * +* 26 GLU 26 H A - 177.1 - 165.5 - -72.0 -34.0 - - - 175.5 - 32.5 - 27 ALA 27 H A - - - - - -66.1 -41.8 - - - 178.9 -1.7 34.4 - 28 LEU 28 H A - - -63.4 178.5 - -57.7 -43.4 - - - 179.7 -2.2 34.1 - 29 ALA 29 H A - - - - - -61.3 -41.4 - - - 178.2 -1.8 33.7 - 30 GLN 30 H A - - -71.5 168.6 - -67.6 -41.9 - - - 178.2 -1.5 33.7 - 31 LEU 31 H A - - -73.5 168.6 - -66.8 -40.0 - - - 182.8 -2.8 33.5 - * * 32 ARG 32 H A - 178.7 - 179.7 - -59.5 -50.4 - - - 180.5 -3.1 30.6 - * * 33 GLU 33 H A 72.0 - - 182.9 - -66.2 -35.5 - - - 176.2 -1.4 30.0 - * * 34 LEU 34 H A - - -67.6 176.1 - -60.6 -45.0 - - - 177.1 -1.4 34.0 - 35 CYS 35 H A - 182.2 - - - -63.0 -40.5 - - - 179.9 -3.1 35.2 - * * 36 ARG 36 H A - 178.4 - - - -68.2 -30.3 - - - 175.6 -2.8 30.6 - 37 GLN 37 H A - - -50.5 - - -66.3 -36.5 - - - 182.4 -2.0 36.1 - * * 38 TRP 38 H A - 170.6 - - - -71.1 -52.2 - - - 181.5 -1.6 32.2 - * * 39 LEU 39 H A - - -55.2 - - -90.4 -43.0 - - - 181.2 -2.6 31.1 - ** ** 40 ARG 40 h l - - -61.7 183.9 - - - - - - 179.2 -1.1 30.1 - * * * 41 PRO 41 T - - - - - -68.3 - - - - - 181.8 - 39.3 - +* +* 42 GLU 42 T A - 190.1 - - - - - - - - 184.1 - 35.5 - 43 VAL 43 T A - - -61.6 - - - - - - - 179.5 - 32.8 - 44 ARG 44 t B - - -62.6 180.3 - - - - - - 178.5 -2.0 33.5 - 45 SER 45 h B - - -56.4 - - - - - - - 184.4 - 35.5 - 46 LYS 46 H A - - -47.0 179.1 - -60.3 -36.0 - - - 180.6 - 37.4 - * * * 47 GLU 47 H A - 176.9 - 179.2 - -52.9 -39.6 - - - 179.4 - 35.6 - * * 48 GLN 48 H A - - -60.3 - - -72.7 -34.3 - - - 181.3 -1.1 34.5 - * * 49 MET 49 H A - - -55.5 181.9 - -66.6 -42.0 - - - 173.7 -1.1 32.8 - * * * 50 LEU 50 H A - - -79.8 - - -53.0 -52.6 - - - 181.0 -2.3 33.8 - * * * 51 GLU 51 H A - - -62.6 - - -59.5 -46.1 - - - 180.1 -1.6 33.5 - 52 LEU 52 H A - - -63.2 178.8 - -63.3 -41.5 - - - 179.5 -2.6 33.5 - 53 LEU 53 H A - 182.7 - - - -74.3 -30.8 - - - 172.2 -2.9 31.3 - * * * 54 VAL 54 H A - 175.1 - - - -62.2 -44.6 - - - 177.4 -2.7 33.8 - Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 LEU 55 H A - 178.0 - - - -56.2 -48.8 - - - 182.5 -2.6 36.3 - 56 GLU 56 H A - 182.2 - - - -52.8 -52.8 - - - 182.9 -2.2 35.3 - * * * 57 GLN 57 H A - 204.5 - - - -72.9 -42.6 - - - 181.8 -1.9 35.2 - * * 58 PHE 58 H A - 178.1 - - - -53.9 -45.7 - - - 181.3 -2.8 33.6 - * * 59 LEU 59 H A - - -60.0 184.7 - -64.9 -34.5 - - - 179.0 -3.0 31.4 - * * 60 GLY 60 H - - - - - - -81.7 -20.5 - - - 177.7 -1.2 - - * +* * +* 61 ALA 61 H A - - - - - -74.2 -23.5 - - - 175.1 -1.9 33.6 - * * 62 LEU 62 h B - - -66.5 170.4 - - - - - - 176.1 -1.1 36.9 - * * 63 PRO 63 h - - - - - -72.8 - - - - - 180.7 - 38.4 - * * 64 PRO 64 H - - - - - -35.5 -35.5 -50.9 - - - 181.1 - 38.9 - +** +** * * +** 65 GLU 65 H A 57.0 - - 176.1 - -59.4 -47.6 - - - 181.0 - 32.3 - 66 ILE 66 H A - - -57.7 180.3 - -73.1 -41.8 - - - 180.9 -.7 34.7 - +* +* 67 GLN 67 H A - 180.2 - 177.2 - -62.0 -43.0 - - - 179.4 -3.3 33.8 - +* +* 68 ALA 68 H A - - - - - -60.7 -36.3 - - - 179.9 -3.0 33.6 - * * 69 ARG 69 H A - - -59.8 - - -66.8 -40.5 - - - 176.2 -1.2 32.8 - * * 70 VAL 70 H A - 174.3 - - - -64.1 -48.8 - - - 180.9 -1.8 35.0 - 71 GLN 71 H A - - -97.5 - - -57.7 -26.7 - - - 174.4 -2.9 27.2 - ** * * +* ** 72 GLY 72 H - - - - - - -78.0 -21.1 - - - 183.2 -1.2 - - * +* * +* 73 GLN 73 H a - - -60.8 183.3 - -104.5 -60.0 - - - 190.0 -1.6 35.7 - *** +* +* *** 74 ARG 74 h l - - -66.0 - - - - - - - 176.4 -2.5 28.3 - +* +* 75 PRO 75 - - - - - -61.3 - - - - - 177.9 - 39.5 - +* +* 76 GLY 76 S - - - - - - - - - - - 177.9 - - - 77 SER 77 h B 54.5 - - - - - - - - - 182.8 - 33.5 - 78 PRO 78 H - - - - - -61.2 -61.2 -44.4 - - - 180.6 - 37.5 - * * 79 GLU 79 H A - - -63.9 175.9 - -67.7 -29.4 - - - 177.1 - 31.8 - 80 GLU 80 H A - 188.4 - - - -74.2 -40.7 - - - 175.3 - 35.3 - 81 ALA 81 H A - - - - - -60.1 -39.8 - - - 179.2 -2.3 34.2 - 82 ALA 82 H A - - - - - -52.8 -38.2 - - - 180.8 -2.5 34.3 - * * 83 ALA 83 H A - - - - - -63.8 -49.6 - - - 179.1 -.9 32.8 - * * 84 LEU 84 H A 46.3 - - 153.0 - -69.5 -42.7 - - - 182.8 -1.1 29.2 - * * * * * 85 VAL 85 H A - - -58.0 - - -68.2 -31.9 - - - 178.1 -2.8 31.1 - 86 ASP 86 H A - 186.0 - - - -59.5 -38.8 - - - 180.2 -2.2 35.6 - 87 GLY 87 H - - - - - - -81.3 -16.1 - - - 180.2 -1.1 - - * ** * ** Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 88 LEU 88 h A - - -62.0 176.3 - - - - - - 178.3 -.8 33.9 - +* +* 89 ARG 89 t B - - -60.5 183.2 - - - - - - 178.3 -.7 34.7 - +* +* 90 ARG 90 S A - - -61.0 180.7 - - - - - - 174.5 -.6 33.6 - +* +* 91 GLU 91 b - 179.1 - - - - - - - - 179.2 - 32.3 - 92 PRO 92 S - - - - - -101.9 - - - - - 182.5 - 40.5 - *** +* *** 93 GLY 93 - - - - - - - - - - - 181.3 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 181.3 - - - 96 SER 302 b - 184.4 - - - - - - - - 180.6 - 34.8 - 97 ASP 303 B - - -63.7 - - - - - - - 177.0 - 35.0 - 98 PRO 304 h - - - - - -61.0 - - - - - 178.1 - 38.0 - * * 99 GLY 305 H - - - - - - 91.1 145.7 - - - 180.9 - - - *13.1**16.4* *16.4* 100 PRO 306 H - - - - - -58.7 -58.7 -22.9 - - - 180.2 - 39.0 - * * * 101 GLU 307 H A - - -60.2 174.3 - -75.2 -56.2 - - - 182.5 - 35.1 - * * 102 ALA 308 H A - - - - - -71.0 -40.5 - - - 181.6 -.6 33.9 - +* +* 103 ALA 309 H A - - - - - -63.2 -44.9 - - - 180.0 -3.1 33.7 - * * 104 ARG 310 H A - 186.2 - 184.3 - -64.9 -36.9 - - - 181.7 -1.1 33.7 - * * 105 LEU 311 H A - 176.8 - - - -61.6 -45.6 - - - 175.8 -1.7 34.4 - 106 ARG 312 H A - - -60.4 177.1 - -56.0 -47.3 - - - 182.0 -2.3 36.5 - 107 PHE 313 H A - 175.4 - - - -61.8 -43.1 - - - 183.0 -2.2 34.7 - 108 ARG 314 H A - - -50.8 180.0 - -80.3 -34.1 - - - 182.5 -2.8 35.4 - * * * 109 CYS 315 h A - 187.2 - - - - - - - - 176.9 -2.7 33.5 - 110 PHE 316 B - 179.4 - - - - - - - - 177.6 - 35.1 - 111 HIS 317 B 72.2 - - - - - - - - - 175.2 -.6 34.5 - +* +* 112 TYR 318 B - 167.6 - - - - - - - - 178.1 -1.2 32.0 - * * 113 GLU 319 t B 43.4 - - 176.1 - - - - - - 181.7 -.7 32.9 - * +* +* 114 GLU 320 T A - - -50.3 - - - - - - - 179.2 -.7 34.2 - * +* +* 115 ALA 321 T A - - - - - - - - - - 181.7 - 34.8 - 116 THR 322 T A - 198.6 - - - - - - - - 184.0 -2.1 34.4 - 117 GLY 323 h - - - - - - - - - - - 186.0 -.9 - - * * * 118 PRO 324 H - - - - - -78.1 -78.1 -32.7 - - - 184.9 - 38.6 - * * * * 119 GLN 325 H A - 196.8 - 170.8 - -78.2 -31.2 - - - 174.5 - 34.9 - * * 120 GLU 326 H A - 180.1 - 167.2 - -75.1 -33.3 - - - 172.5 - 32.7 - * * 121 ALA 327 H A - - - - - -62.8 -40.6 - - - 176.6 -1.5 34.2 - 122 LEU 328 H A - - -63.5 179.7 - -59.4 -39.9 - - - 179.6 -2.1 34.1 - 123 ALA 329 H A - - - - - -60.6 -47.4 - - - 177.3 -1.4 33.9 - 124 GLN 330 H A - - -67.8 171.1 - -60.2 -50.4 - - - 177.9 -1.9 34.5 - Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 125 LEU 331 H A - - -71.5 170.9 - -61.3 -38.2 - - - 181.7 -3.0 33.8 - * * 126 ARG 332 H A - 178.6 - 177.9 - -60.3 -49.1 - - - 180.3 -3.0 32.8 - * * 127 GLU 333 H A 70.7 - - 184.1 - -68.4 -40.5 - - - 178.6 -1.9 31.3 - 128 LEU 334 H A - - -63.5 176.1 - -60.4 -43.8 - - - 177.0 -2.1 34.1 - 129 CYS 335 H A - 186.0 - - - -60.5 -41.5 - - - 178.0 -3.2 35.5 - +* +* 130 ARG 336 H A - 182.7 - - - -67.1 -38.3 - - - 179.7 -2.2 33.4 - 131 GLN 337 H A - - -52.1 186.6 - -60.5 -31.0 - - - 180.7 -2.5 35.9 - 132 TRP 338 H a - 164.1 - - - -83.5 -60.9 - - - 182.9 -1.4 34.3 - * +* +* +* 133 LEU 339 H A - - -61.6 162.1 - -71.7 -45.3 - - - 181.5 -3.3 34.6 - +* +* 134 ARG 340 h l - - -59.0 182.3 - - - - - - 179.6 -1.8 31.2 - 135 PRO 341 T - - - - - -62.1 - - - - - 178.6 - 38.2 - * * 136 GLU 342 T A - - -62.7 - - - - - - - 186.4 - 36.3 - * * 137 VAL 343 T A - - -56.1 - - - - - - - 180.1 -1.2 32.9 - * * 138 ARG 344 t B - - -69.6 187.4 - - - - - - 176.8 -3.5 31.2 - +* +* 139 SER 345 h B - - -55.5 - - - - - - - 180.1 - 36.1 - 140 LYS 346 H A - - -64.1 170.7 - -52.6 -40.9 - - - 181.6 - 35.8 - * * 141 GLU 347 H A - 176.8 - 176.2 - -55.3 -42.7 - - - 179.4 - 34.3 - 142 GLN 348 H A - - -67.3 - - -66.2 -27.7 - - - 178.5 -.8 33.4 - * +* +* 143 MET 349 H A - - -60.3 180.0 - -70.3 -41.2 - - - 174.6 -.9 32.9 - * * 144 LEU 350 H A - - -74.0 - - -58.1 -48.1 - - - 178.6 -1.6 32.8 - 145 GLU 351 H A - - -66.6 - - -54.1 -53.9 - - - 180.2 -2.1 35.4 - * * 146 LEU 352 H A - - -64.2 176.8 - -60.3 -36.8 - - - 182.1 -2.5 34.7 - 147 LEU 353 H A - 183.5 - - - -77.8 -32.2 - - - 173.5 -2.3 32.1 - * * * 148 VAL 354 H A - 176.3 - - - -63.1 -41.2 - - - 175.7 -2.7 33.6 - 149 LEU 355 H A - 180.3 - - - -56.9 -47.2 - - - 180.3 -2.2 35.7 - 150 GLU 356 H A - 181.2 - - - -56.6 -48.0 - - - 181.2 -1.8 33.5 - 151 GLN 357 H A - 206.8 - - - -72.2 -46.5 - - - 183.6 -2.2 35.5 - * * 152 PHE 358 H A - 179.1 - - - -53.8 -46.3 - - - 180.9 -3.2 33.4 - +* +* 153 LEU 359 H A - - -59.9 187.7 - -64.3 -33.2 - - - 177.5 -2.9 30.8 - * * 154 GLY 360 H - - - - - - -81.8 -22.7 - - - 177.6 -1.1 - - * * * * 155 ALA 361 H A - - - - - -73.3 -21.4 - - - 173.8 -2.1 33.2 - +* * +* 156 LEU 362 h B - - -66.2 172.2 - - - - - - 175.6 -1.1 36.8 - * * 157 PRO 363 h - - - - - -67.5 - - - - - 182.3 - 39.4 - +* +* 158 PRO 364 H - - - - - -42.7 -42.7 -43.0 - - - 179.1 - 38.0 - ** +* * ** 159 GLU 365 H A 53.7 - - 179.0 - -64.0 -47.9 - - - 179.4 - 32.0 - Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 160 ILE 366 H A - - -59.4 180.1 - -70.8 -39.4 - - - 179.6 - 34.5 - 161 GLN 367 H A - 178.7 - 177.4 - -61.7 -39.3 - - - 178.6 -3.5 34.6 - +* +* 162 ALA 368 H A - - - - - -63.7 -35.5 - - - 179.0 -2.4 33.9 - 163 ARG 369 H A - - -61.9 - - -65.1 -42.4 - - - 176.6 -1.2 34.0 - * * 164 VAL 370 H A - 178.7 - - - -70.7 -35.8 - - - 183.4 -1.7 35.7 - 165 GLN 371 H A - 217.9 - - - -60.0 -27.4 - - - 175.5 -2.4 33.4 - ** * ** 166 GLY 372 h - - - - - - - - - - - 183.7 -1.0 - - * * 167 GLN 373 T a - - -61.9 184.2 - - - - - - 188.3 -1.5 35.3 - * * 168 ARG 374 t l - - -57.9 - - - - - - - 176.3 -2.2 30.3 - * * 169 PRO 375 - - - - - -60.0 - - - - - 178.8 - 39.7 - +* +* 170 GLY 376 S - - - - - - - - - - - 176.3 - - - 171 SER 377 h B 47.6 - - - - - - - - - 183.6 - 32.5 - * * 172 PRO 378 H - - - - - -49.1 -49.1 -45.3 - - - 183.6 - 39.4 - * * +* +* 173 GLU 379 H A - - -62.8 172.8 - -72.2 -29.4 - - - 176.6 - 31.5 - 174 GLU 380 H A - 188.6 - - - -70.4 -41.8 - - - 176.5 -.5 35.6 - ** ** 175 ALA 381 H A - - - - - -62.7 -40.8 - - - 178.4 -2.3 34.3 - 176 ALA 382 H A - - - - - -53.2 -42.1 - - - 180.0 -2.5 34.7 - * * 177 ALA 383 H A - - - - - -61.6 -48.2 - - - 178.7 -1.4 32.5 - 178 LEU 384 H A 49.5 - - 153.0 - -69.6 -38.4 - - - 182.2 -1.4 28.6 - * +* +* 179 VAL 385 H A - - -58.5 - - -71.1 -31.3 - - - 178.8 -2.7 30.6 - 180 ASP 386 H A - 180.7 - - - -51.0 -41.7 - - - 180.2 -2.4 34.5 - * * 181 GLY 387 H - - - - - - -83.8 -15.7 - - - 182.4 -.8 - - +* ** +* ** 182 LEU 388 h A - - -60.4 173.8 - - - - - - 182.8 -.6 35.2 - +* +* 183 ARG 389 t B - - -63.6 184.2 - - - - - - 172.9 -.6 34.6 - * +* +* 184 ARG 390 S A - - -65.0 184.2 - - - - - - 179.1 - 34.4 - 185 GLU 391 B - 186.0 - - - - - - - - 176.1 - 33.1 - 186 PRO 392 S - - - - - -97.7 - - - - - 182.2 - 39.7 - +** +* +** 187 GLY 393 - - - - - - - - - - - 178.6 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * ** ** * ****13.1**18.1* +* ** +* *18.1* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.3 182.7 -62.6 176.7 -65.1 -63.2 -36.3 - - - 179.5 -1.9 34.3 Standard deviations: 12.0 9.7 8.2 7.6 16.3 21.2 26.4 - - - 3.0 .8 2.3 Numbers of values: 12 54 66 61 18 123 123 0 0 0 186 126 170 0 Residue-by-residue listing for refined_5 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_5 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 - 1.242 1.514 - 1.477 - 116.04 121.06 - 111.79 - 122.90 +* +* 2 SER 2 1.303 1.237 1.504 1.544 1.431 122.63 117.19 119.91 110.70 107.34 110.47 122.87 +* * * * +* 3 ASP 3 1.295 1.233 1.503 1.544 1.434 120.63 118.11 119.62 109.28 107.73 111.04 122.23 ** * * * ** 4 PRO 4 1.350 1.236 1.525 1.533 1.467 122.36 115.09 121.51 110.18 110.36 103.44 123.38 * * 5 GLY 5 1.316 1.239 1.500 - 1.416 122.09 117.54 121.03 - 112.86 - 121.43 ** ** 6 PRO 6 1.326 1.231 1.531 1.547 1.451 122.03 114.73 121.70 110.28 109.79 103.92 123.55 * * * * 7 GLU 7 1.323 1.238 1.533 1.521 1.442 123.70 116.13 120.64 108.21 111.28 108.68 123.20 * * * 8 ALA 8 1.327 1.230 1.510 1.523 1.453 121.83 116.39 120.61 110.54 111.69 110.71 122.98 9 ALA 9 1.316 1.233 1.522 1.497 1.446 121.19 117.32 120.09 111.15 112.08 111.06 122.57 10 ARG 10 1.337 1.219 1.521 1.523 1.457 120.18 116.42 120.82 108.69 109.62 112.80 122.76 * * 11 LEU 11 1.329 1.213 1.528 1.522 1.412 122.53 116.27 120.43 111.64 109.95 108.68 123.27 ** * ** 12 ARG 12 1.326 1.222 1.528 1.523 1.464 122.27 114.91 121.44 109.71 109.51 109.65 123.62 Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 PHE 13 1.316 1.219 1.547 1.536 1.461 124.45 116.76 120.62 112.57 111.32 107.09 122.61 * +* * ** ** 14 ARG 14 1.326 1.230 1.527 1.540 1.471 122.45 116.72 120.66 110.47 112.07 111.35 122.62 15 CYS 15 1.315 1.242 1.515 1.538 1.455 121.79 114.89 121.36 110.34 108.64 110.48 123.74 * * 16 PHE 16 1.320 1.242 1.512 1.535 1.424 122.38 116.12 121.00 109.49 109.55 110.14 122.87 +* +* 17 HIS 17 1.295 1.247 1.504 1.565 1.425 120.25 117.45 120.02 109.63 107.01 112.27 122.52 ** * +* +* * * ** 18 TYR 18 1.289 1.217 1.499 1.526 1.422 119.29 115.35 120.96 111.72 109.43 112.55 123.62 +** * +* * * +** 19 GLU 19 1.283 1.228 1.509 1.535 1.421 122.85 115.69 120.89 112.99 109.25 110.27 123.39 *** +* +* *** 20 GLU 20 1.310 1.231 1.515 1.536 1.451 123.75 115.49 120.73 108.80 111.12 111.69 123.77 * * * 21 ALA 21 1.319 1.226 1.532 1.519 1.447 123.06 117.81 120.23 110.66 112.39 110.35 121.95 22 THR 22 1.335 1.217 1.538 1.583 1.448 119.44 116.31 121.13 110.50 108.84 111.32 122.51 +* * +* 23 GLY 23 1.323 1.238 1.519 - 1.444 120.54 118.77 120.04 - 111.23 - 121.19 * * * 24 PRO 24 1.335 1.221 1.519 1.514 1.455 121.88 116.47 120.79 111.07 113.62 103.77 122.70 25 GLN 25 1.299 1.236 1.503 1.503 1.441 122.10 116.29 120.79 114.19 113.25 110.26 122.89 ** * * ** ** 26 GLU 26 1.301 1.238 1.519 1.524 1.439 120.16 115.27 121.44 112.64 108.89 111.16 123.27 +* * * +* 27 ALA 27 1.319 1.225 1.526 1.519 1.441 122.20 116.21 120.43 110.50 109.72 110.14 123.35 28 LEU 28 1.334 1.222 1.514 1.526 1.469 122.78 116.60 120.34 109.04 111.87 111.36 123.06 29 ALA 29 1.322 1.234 1.527 1.514 1.458 121.49 115.75 121.11 110.87 110.67 110.36 123.11 30 GLN 30 1.317 1.232 1.523 1.505 1.441 122.52 115.37 121.34 112.00 111.26 108.97 123.27 * * * 31 LEU 31 1.318 1.226 1.517 1.530 1.453 123.13 117.50 119.80 110.50 112.78 110.51 122.69 32 ARG 32 1.328 1.229 1.512 1.530 1.453 120.54 118.21 119.62 110.68 113.17 113.93 122.16 * ** ** 33 GLU 33 1.329 1.197 1.521 1.540 1.451 118.30 117.46 119.56 111.92 110.75 114.69 122.95 +* +* ** ** 34 LEU 34 1.343 1.229 1.516 1.531 1.476 122.03 115.55 121.04 109.83 110.50 111.17 123.40 * * 35 CYS 35 1.312 1.227 1.526 1.535 1.442 122.75 115.88 121.44 110.50 109.20 109.27 122.63 * * 36 ARG 36 1.316 1.207 1.531 1.552 1.410 122.57 117.57 119.58 115.70 111.53 110.03 122.84 * * +** +** +** 37 GLN 37 1.339 1.230 1.536 1.550 1.475 121.43 114.42 121.74 106.51 108.34 111.96 123.84 +* * +* 38 TRP 38 1.326 1.238 1.540 1.560 1.451 124.31 118.48 119.71 113.73 113.07 109.07 121.81 * * * +* +* 39 LEU 39 1.330 1.216 1.513 1.554 1.467 119.11 116.28 119.93 110.06 111.78 114.70 123.77 * * ** ** 40 ARG 40 1.319 1.227 1.533 1.533 1.468 124.25 117.22 121.05 111.45 114.08 113.33 121.73 * * +* +* 41 PRO 41 1.346 1.222 1.526 1.536 1.470 123.19 116.65 120.71 109.53 112.58 103.39 122.64 42 GLU 42 1.314 1.232 1.529 1.533 1.446 121.28 116.07 121.48 109.60 109.38 109.64 122.41 * * 43 VAL 43 1.312 1.233 1.517 1.545 1.449 120.74 117.13 120.39 110.27 112.80 111.87 122.48 * * Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ARG 44 1.309 1.228 1.506 1.520 1.457 120.47 114.63 121.39 109.14 112.19 111.94 123.98 * * 45 SER 45 1.302 1.248 1.528 1.529 1.431 123.92 115.08 121.11 110.59 109.32 108.68 123.79 +* * * * +* 46 LYS 46 1.309 1.213 1.510 1.502 1.461 124.82 114.81 121.28 108.33 110.34 107.44 123.90 * * +* +* +* 47 GLU 47 1.311 1.241 1.533 1.517 1.457 124.52 115.68 121.27 110.11 111.66 108.14 123.04 * +* * +* 48 GLN 48 1.315 1.224 1.509 1.525 1.446 121.62 115.79 120.93 109.80 109.95 110.75 123.26 * * 49 MET 49 1.320 1.227 1.503 1.507 1.451 121.79 116.16 120.11 111.28 111.26 111.07 123.72 * * * 50 LEU 50 1.336 1.215 1.515 1.556 1.464 121.81 116.71 119.84 109.47 109.91 112.25 123.35 * * * 51 GLU 51 1.335 1.235 1.526 1.531 1.469 122.16 116.59 120.52 109.76 111.93 111.45 122.89 52 LEU 52 1.326 1.228 1.521 1.528 1.444 121.89 116.80 120.65 110.69 111.55 110.76 122.55 53 LEU 53 1.315 1.236 1.554 1.519 1.420 120.98 117.34 120.50 115.77 111.82 108.46 122.13 * ** +** * +** 54 VAL 54 1.338 1.228 1.530 1.571 1.471 120.86 115.28 120.95 109.61 108.56 112.70 123.74 * * 55 LEU 55 1.336 1.226 1.520 1.532 1.464 123.87 115.46 120.51 108.43 110.58 109.16 124.02 * * 56 GLU 56 1.325 1.237 1.537 1.534 1.457 123.55 116.52 120.98 109.29 111.87 109.43 122.47 * * 57 GLN 57 1.327 1.220 1.520 1.532 1.453 120.30 116.20 120.50 109.35 108.21 110.68 123.28 * * 58 PHE 58 1.337 1.236 1.514 1.539 1.456 121.97 116.42 120.44 109.70 111.40 111.71 123.13 59 LEU 59 1.315 1.221 1.521 1.529 1.439 120.82 117.23 120.01 112.06 112.34 112.01 122.74 * * 60 GLY 60 1.325 1.232 1.513 - 1.449 119.94 116.11 120.87 - 112.02 - 123.01 61 ALA 61 1.326 1.240 1.525 1.533 1.452 122.26 115.28 121.01 111.22 109.68 110.72 123.70 62 LEU 62 1.331 1.239 1.530 1.534 1.451 123.54 118.33 119.98 107.91 109.93 109.12 121.69 * * * * 63 PRO 63 1.345 1.238 1.526 1.540 1.443 121.58 117.51 119.43 109.94 109.23 105.12 123.05 +* * +* +* 64 PRO 64 1.351 1.219 1.534 1.516 1.474 124.88 117.41 119.83 110.33 114.64 102.31 122.75 * * 65 GLU 65 1.336 1.227 1.540 1.538 1.468 121.26 117.06 120.38 110.84 112.65 111.70 122.53 66 ILE 66 1.327 1.239 1.535 1.549 1.443 121.56 115.58 121.20 109.68 110.19 110.66 123.20 67 GLN 67 1.321 1.237 1.527 1.525 1.451 122.69 116.38 120.72 110.95 111.06 110.10 122.88 68 ALA 68 1.320 1.236 1.523 1.517 1.457 121.85 116.52 120.59 110.34 111.23 110.90 122.87 69 ARG 69 1.329 1.238 1.528 1.532 1.458 121.26 116.55 120.64 111.00 110.58 111.74 122.80 70 VAL 70 1.337 1.223 1.499 1.531 1.464 121.27 115.20 120.94 106.43 110.15 113.24 123.85 * * * * 71 GLN 71 1.306 1.200 1.512 1.530 1.437 122.73 117.17 119.99 114.90 113.82 113.68 122.83 +* +* * +** +* +** 72 GLY 72 1.314 1.233 1.550 - 1.447 120.30 117.36 120.25 - 112.80 - 122.37 * +* +* 73 GLN 73 1.342 1.224 1.527 1.541 1.477 122.02 114.60 121.31 106.76 112.36 111.27 124.07 * +* +* 74 ARG 74 1.328 1.217 1.523 1.544 1.467 125.37 116.86 121.25 111.25 112.28 116.74 121.79 ** +*** +*** 75 PRO 75 1.342 1.225 1.539 1.528 1.477 123.04 115.47 121.28 109.62 112.17 102.76 123.25 76 GLY 76 1.317 1.231 1.520 - 1.458 121.97 116.68 120.78 - 113.44 - 122.54 Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 77 SER 77 1.308 1.246 1.535 1.531 1.439 121.69 118.04 120.08 112.13 110.01 109.87 121.86 +* * +* 78 PRO 78 1.357 1.223 1.526 1.538 1.467 122.78 116.81 120.56 111.05 113.21 104.34 122.62 * * * 79 GLU 79 1.316 1.232 1.521 1.516 1.461 122.04 116.26 120.80 112.69 111.99 110.66 122.93 * * 80 GLU 80 1.316 1.234 1.539 1.518 1.437 121.80 116.16 120.94 110.50 107.93 109.24 122.90 * * * 81 ALA 81 1.355 1.231 1.508 1.520 1.460 122.18 115.38 120.44 110.05 110.19 110.79 124.15 +* +* 82 ALA 82 1.334 1.208 1.517 1.523 1.456 123.72 116.14 120.52 110.28 111.21 110.01 123.29 * * * 83 ALA 83 1.309 1.238 1.529 1.510 1.454 122.54 117.68 120.10 111.03 112.19 110.88 122.23 * * 84 LEU 84 1.340 1.227 1.512 1.560 1.457 119.14 116.43 120.71 110.85 112.34 116.11 122.81 * * *** *** 85 VAL 85 1.319 1.230 1.527 1.540 1.456 121.14 116.30 120.47 111.14 112.42 113.26 123.23 * * 86 ASP 86 1.332 1.237 1.520 1.534 1.468 122.90 115.42 121.17 108.88 109.68 110.05 123.40 87 GLY 87 1.321 1.220 1.518 - 1.446 121.63 116.68 120.73 - 112.69 - 122.59 88 LEU 88 1.317 1.242 1.526 1.530 1.462 121.91 115.78 121.17 110.52 111.02 110.43 123.05 89 ARG 89 1.316 1.233 1.503 1.536 1.432 122.45 115.82 120.53 109.64 108.92 111.24 123.63 * * * 90 ARG 90 1.314 1.225 1.513 1.529 1.464 122.15 115.77 121.17 110.19 109.74 111.70 123.06 * * 91 GLU 91 1.314 1.238 1.528 1.538 1.432 121.67 116.67 121.04 112.08 109.54 111.96 122.09 * * * * 92 PRO 92 1.341 1.238 1.536 1.531 1.440 123.36 117.02 120.44 109.67 112.76 101.59 122.54 +* * +* 93 GLY 93 1.321 1.228 1.498 - 1.440 120.31 116.07 120.81 - 112.36 - 123.12 94 GLY 94 1.301 1.248 1.507 - 1.444 121.02 - 120.61 - 112.37 - - ** ** 95 GLY 301 - 1.235 1.505 - 1.452 - 115.43 121.26 - 111.62 - 123.30 96 SER 302 1.300 1.237 1.534 1.545 1.436 122.39 116.98 120.06 111.64 108.54 109.06 122.95 ** * ** 97 ASP 303 1.317 1.247 1.502 1.541 1.459 122.81 118.17 119.67 108.11 109.46 111.98 122.16 * * * 98 PRO 304 1.354 1.220 1.515 1.539 1.461 122.38 115.72 120.88 110.75 110.78 104.44 123.39 * * 99 GLY 305 1.317 1.231 1.500 - 1.426 121.09 118.14 119.81 - 111.95 - 122.04 +* +* 100 PRO 306 1.347 1.227 1.526 1.537 1.472 123.26 116.25 121.12 109.73 112.38 103.58 122.63 101 GLU 307 1.309 1.242 1.530 1.512 1.435 121.59 116.06 120.74 110.17 110.57 109.11 123.08 * * * 102 ALA 308 1.321 1.231 1.511 1.515 1.455 121.80 116.03 120.82 110.22 111.25 110.58 123.13 103 ALA 309 1.318 1.236 1.513 1.500 1.447 121.75 116.77 120.40 110.23 111.41 110.76 122.81 104 ARG 310 1.337 1.215 1.517 1.525 1.446 120.13 116.33 120.63 108.59 109.94 112.98 123.00 * * 105 LEU 311 1.326 1.225 1.533 1.519 1.409 122.73 116.28 120.25 112.42 110.03 108.26 123.42 +** * * +** 106 ARG 312 1.335 1.237 1.530 1.529 1.473 122.66 114.16 121.75 107.58 109.59 109.88 124.08 * * * 107 PHE 313 1.314 1.223 1.541 1.537 1.453 125.04 117.19 120.40 111.71 113.03 107.53 122.41 * +* +* +* 108 ARG 314 1.319 1.234 1.520 1.516 1.471 121.31 115.71 121.05 108.25 110.61 110.44 123.22 Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 109 CYS 315 1.327 1.239 1.537 1.543 1.459 122.90 116.01 121.14 111.63 110.81 110.01 122.84 110 PHE 316 1.317 1.243 1.520 1.539 1.437 122.41 116.37 120.69 109.79 109.35 110.19 122.94 * * 111 HIS 317 1.308 1.229 1.500 1.564 1.443 120.85 118.00 119.76 109.21 107.43 112.61 122.23 * * +* * * +* 112 TYR 318 1.293 1.230 1.506 1.526 1.421 118.46 114.37 121.57 111.96 109.76 112.41 124.05 +** +* +* * +** 113 GLU 319 1.284 1.236 1.512 1.548 1.414 123.45 115.61 121.09 113.16 109.41 110.35 123.26 *** ** +* *** 114 GLU 320 1.326 1.232 1.522 1.542 1.465 123.19 114.75 120.91 108.70 110.80 112.05 124.34 115 ALA 321 1.312 1.225 1.528 1.513 1.446 124.87 117.88 120.17 109.50 112.89 109.49 121.95 * +* +* 116 THR 322 1.321 1.223 1.534 1.582 1.448 119.86 115.63 121.24 110.82 108.73 110.75 123.05 +* * +* 117 GLY 323 1.327 1.232 1.515 - 1.450 120.99 120.42 119.43 - 109.47 - 120.14 +* * +* +* 118 PRO 324 1.333 1.218 1.503 1.509 1.447 120.64 115.43 121.29 110.58 112.63 103.17 123.24 * * * * 119 GLN 325 1.291 1.230 1.521 1.484 1.401 122.87 115.74 121.23 113.24 109.82 106.57 123.01 +** ** +** +* ** +** 120 GLU 326 1.319 1.236 1.523 1.521 1.439 121.76 115.75 121.57 112.80 108.87 110.58 122.68 * * 121 ALA 327 1.323 1.223 1.528 1.519 1.447 121.59 115.90 120.69 110.66 108.93 110.49 123.39 122 LEU 328 1.339 1.199 1.506 1.528 1.464 122.65 117.21 119.77 108.24 111.51 112.26 123.02 +* * +* 123 ALA 329 1.330 1.237 1.523 1.519 1.466 121.40 114.94 121.30 110.56 109.99 110.54 123.74 124 GLN 330 1.319 1.230 1.520 1.500 1.441 123.01 115.46 121.31 111.56 110.99 108.42 123.20 * * * 125 LEU 331 1.320 1.211 1.520 1.532 1.454 122.91 116.83 120.22 110.40 112.19 110.34 122.94 * * 126 ARG 332 1.314 1.236 1.513 1.530 1.453 122.46 117.32 120.01 110.96 112.16 111.28 122.66 * * 127 GLU 333 1.328 1.198 1.516 1.536 1.444 119.13 117.29 119.43 111.80 110.09 113.37 123.21 +* * +* +* 128 LEU 334 1.342 1.231 1.521 1.532 1.474 122.49 115.33 121.10 109.98 110.77 110.69 123.56 129 CYS 335 1.317 1.230 1.538 1.542 1.445 123.56 115.78 121.35 111.16 108.85 108.36 122.85 * * * 130 ARG 336 1.329 1.203 1.541 1.549 1.420 123.22 118.11 119.33 113.46 111.50 108.38 122.56 * +* +* * +* 131 GLN 337 1.337 1.231 1.524 1.518 1.484 122.34 113.63 122.16 107.98 109.85 110.09 124.21 * * * * 132 TRP 338 1.313 1.237 1.545 1.550 1.440 125.31 116.80 120.38 113.20 112.54 107.00 122.81 * * ** +* ** ** 133 LEU 339 1.319 1.227 1.524 1.533 1.464 122.15 115.79 120.36 110.43 111.06 109.49 123.84 134 ARG 340 1.337 1.234 1.532 1.542 1.462 124.37 117.64 120.73 111.08 112.54 113.10 121.62 * +* +* 135 PRO 341 1.350 1.232 1.525 1.537 1.474 123.06 114.94 121.45 110.68 111.84 103.86 123.60 * * * 136 GLU 342 1.314 1.233 1.517 1.538 1.443 123.59 116.18 121.00 107.10 110.35 110.82 122.82 * * +* +* 137 VAL 343 1.315 1.228 1.526 1.555 1.446 120.32 117.61 120.28 110.50 112.52 111.60 122.11 138 ARG 344 1.320 1.238 1.502 1.537 1.443 119.91 114.37 121.74 110.39 112.82 113.76 123.89 * +* +* 139 SER 345 1.294 1.246 1.518 1.528 1.420 123.61 115.80 120.36 110.48 108.56 108.21 123.84 ** +* * * ** Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 140 LYS 346 1.318 1.214 1.525 1.515 1.464 123.82 115.80 120.75 109.42 111.26 108.48 123.40 * * * 141 GLU 347 1.320 1.232 1.536 1.519 1.460 123.70 116.32 120.80 111.18 112.06 108.75 122.84 * * * 142 GLN 348 1.322 1.225 1.517 1.524 1.455 121.88 116.48 120.56 110.37 111.36 111.13 122.96 143 MET 349 1.319 1.227 1.500 1.501 1.450 121.50 116.41 119.99 111.41 110.94 110.81 123.59 * * * 144 LEU 350 1.342 1.209 1.510 1.559 1.462 121.04 115.85 120.39 110.16 109.32 113.33 123.65 * * +* +* 145 GLU 351 1.324 1.234 1.539 1.526 1.467 123.04 116.56 120.80 109.56 111.32 108.98 122.62 146 LEU 352 1.323 1.230 1.527 1.530 1.453 122.42 116.05 121.11 109.96 111.65 109.77 122.84 147 LEU 353 1.304 1.241 1.543 1.508 1.426 121.87 117.04 120.51 114.36 112.42 108.43 122.43 +* * +* ** * ** 148 VAL 354 1.330 1.224 1.521 1.561 1.463 121.34 115.03 120.99 110.27 108.29 112.38 123.93 * * 149 LEU 355 1.329 1.234 1.530 1.560 1.463 123.99 115.41 120.93 111.69 109.27 107.58 123.66 +* * +* +* 150 GLU 356 1.323 1.242 1.538 1.544 1.459 123.35 117.19 120.70 111.06 112.06 110.18 122.11 151 GLN 357 1.321 1.221 1.511 1.523 1.451 119.81 115.68 120.57 108.23 108.39 111.22 123.71 * * * 152 PHE 358 1.326 1.234 1.512 1.529 1.448 122.75 116.74 120.31 110.17 112.11 111.30 122.94 153 LEU 359 1.321 1.216 1.522 1.527 1.444 120.05 117.24 120.20 112.16 112.53 112.52 122.55 * * * 154 GLY 360 1.322 1.235 1.516 - 1.452 119.90 116.01 120.79 - 111.93 - 123.19 155 ALA 361 1.329 1.235 1.523 1.534 1.452 122.50 115.58 120.84 111.40 109.78 111.06 123.57 156 LEU 362 1.327 1.238 1.524 1.533 1.442 123.24 118.24 119.93 107.84 109.55 109.45 121.82 * * * 157 PRO 363 1.342 1.235 1.520 1.536 1.452 121.75 118.45 118.90 109.24 108.61 104.34 122.65 * * * * * 158 PRO 364 1.353 1.215 1.537 1.522 1.475 123.67 117.36 120.13 111.00 113.90 103.14 122.49 159 GLU 365 1.331 1.230 1.542 1.530 1.465 121.28 117.56 120.18 111.46 113.02 111.31 122.22 160 ILE 366 1.334 1.239 1.534 1.551 1.455 121.01 115.16 121.51 109.75 109.66 110.99 123.31 161 GLN 367 1.316 1.229 1.526 1.523 1.448 123.22 116.19 120.54 110.78 110.86 109.30 123.27 162 ALA 368 1.326 1.237 1.521 1.516 1.467 122.99 116.13 120.70 109.93 111.32 110.71 123.15 163 ARG 369 1.324 1.233 1.518 1.529 1.459 121.96 115.83 121.22 110.40 109.81 110.88 122.93 164 VAL 370 1.316 1.218 1.505 1.531 1.450 121.55 115.18 121.13 106.74 109.81 112.12 123.69 * * 165 GLN 371 1.303 1.207 1.527 1.516 1.442 123.68 116.42 120.65 111.44 110.57 110.32 122.89 +* * * +* 166 GLY 372 1.319 1.228 1.542 - 1.447 120.81 117.18 120.08 - 113.11 - 122.73 * * 167 GLN 373 1.344 1.225 1.535 1.545 1.476 122.18 114.87 121.30 107.67 112.34 110.90 123.81 * * * 168 ARG 374 1.328 1.212 1.522 1.543 1.471 125.55 117.56 120.60 109.41 111.94 116.10 121.75 ** *** *** 169 PRO 375 1.334 1.236 1.536 1.525 1.482 122.88 115.15 121.69 109.36 112.66 102.55 123.15 * * * 170 GLY 376 1.312 1.229 1.518 - 1.460 121.97 116.08 120.87 - 112.59 - 123.05 * * 171 SER 377 1.306 1.243 1.546 1.541 1.430 122.62 117.30 120.36 113.76 109.73 109.88 122.26 +* * * +* +* 172 PRO 378 1.359 1.228 1.533 1.524 1.484 123.93 116.57 120.63 108.69 114.81 103.35 122.79 * * * * 173 GLU 379 1.310 1.229 1.517 1.524 1.458 122.24 115.85 121.01 113.89 111.69 110.19 123.12 * +* +* Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 174 GLU 380 1.314 1.237 1.531 1.513 1.442 121.78 115.63 121.05 109.85 108.08 109.30 123.32 * * * 175 ALA 381 1.352 1.228 1.509 1.516 1.449 122.10 115.48 120.45 110.28 109.81 110.53 124.05 +* +* 176 ALA 382 1.331 1.218 1.510 1.508 1.452 123.68 115.84 120.77 110.01 111.21 109.69 123.37 * * 177 ALA 383 1.307 1.232 1.540 1.504 1.441 122.27 118.62 119.69 111.64 112.39 110.48 121.68 +* * +* 178 LEU 384 1.347 1.227 1.518 1.557 1.465 118.45 116.72 120.66 110.81 112.49 116.74 122.59 * * +* +*** +*** 179 VAL 385 1.314 1.228 1.527 1.540 1.457 121.24 116.13 120.39 111.32 112.80 113.46 123.48 * * * * 180 ASP 386 1.325 1.237 1.535 1.533 1.475 123.81 116.40 120.62 109.87 111.89 109.87 122.96 * * 181 GLY 387 1.322 1.224 1.524 - 1.456 120.87 116.65 120.81 - 113.11 - 122.53 182 LEU 388 1.315 1.234 1.527 1.525 1.468 122.62 115.73 121.23 109.56 111.00 109.47 123.04 183 ARG 389 1.305 1.234 1.503 1.527 1.428 122.87 115.61 120.71 109.15 111.92 110.79 123.68 +* * +* +* 184 ARG 390 1.317 1.237 1.519 1.530 1.470 121.51 116.13 121.17 107.64 109.79 112.91 122.69 * * * 185 GLU 391 1.316 1.233 1.522 1.533 1.425 120.77 116.99 120.79 111.09 110.68 111.43 122.10 +* +* 186 PRO 392 1.334 1.231 1.542 1.524 1.441 122.88 117.04 120.51 110.36 112.42 101.93 122.45 +* +* 187 GLY 393 1.321 1.240 1.500 - 1.436 120.23 116.12 120.81 - 112.10 - 123.07 188 GLY 394 1.305 - 1.496 - 1.426 120.43 - - - 110.17 - - +* * +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* ** +** ** +* * +** * +*** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 1.283 1.355 1.320 .012 *** +* C-N (Pro) 1.341 .016 18 1.326 1.359 1.344 .009 * C-O C-O 1.231 .020 187 1.197 1.248 1.229 .010 +* CA-C CH1E-C (except Gly) 1.525 .021 170 1.499 1.554 1.523 .011 * * CH2G*-C (Gly) 1.516 .018 18 1.496 1.550 1.514 .014 * +* CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.497 1.534 1.516 .009 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.531 1.583 1.553 .017 +* CH1E-CH2E (the rest) 1.530 .020 138 1.484 1.565 1.531 .013 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.401 1.484 1.450 .016 +** * NH1-CH2G* (Gly) 1.451 .016 18 1.416 1.477 1.446 .014 ** +* N-CH1E (Pro) 1.466 .015 18 1.440 1.484 1.463 .014 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 2.0 152 113.63 118.62 116.29 .97 * * CH2G*-C-NH1 (Gly) 116.4 2.1 16 115.43 120.42 116.95 1.24 +* CH1E-C-N (Pro) 116.9 1.5 18 114.73 118.45 116.34 1.02 * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 120.14 124.34 122.96 .66 +* O-C-N (Pro) 122.0 1.4 18 122.45 123.60 122.94 .38 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 118.30 125.55 122.14 1.41 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 16 119.90 122.09 120.88 .70 C-N-CH1E (Pro) 122.6 5.0 18 120.64 124.88 122.75 .95 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 118.90 122.16 120.68 .57 * CH2G*-C-O (Gly) 120.8 2.1 17 119.43 121.26 120.59 .48 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 109.50 111.64 110.55 .52 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 106.43 111.32 109.75 1.51 * * CH2E-CH1E-C (the rest) 110.1 1.9 138 106.51 115.77 110.51 1.71 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 107.01 114.08 110.73 1.47 * * NH1-CH2G*-C (Gly) 112.5 2.9 18 109.47 113.44 112.09 .98 * N-CH1E-C (Pro) 111.8 2.5 18 108.61 114.81 112.13 1.71 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 109.49 111.06 110.51 .41 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 110.66 113.46 112.03 .95 * N-CH1E-CH2E (Pro) 103.0 1.1 18 101.59 105.12 103.39 .89 * +* NH1-CH1E-CH2E (the rest) 110.5 1.7 120 106.57 116.74 110.73 1.95 ** +*** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_5 Page 17 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 143 94.1% Residues in additional allowed regions [a,b,l,p] 9 5.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 152 100.0% Number of end-residues (excl. Gly and Pro) 0 Number of glycine residues 18 Number of proline residues 18 ---- Total number of residues 188 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 152 94.1 83.8 10.0 1.0 BETTER b. Omega angle st dev 186 3.0 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 2.3 3.1 1.6 -.5 Inside e. H-bond energy st dev 126 .8 .8 .2 .0 Inside f. Overall G-factor 188 .2 -.4 .3 2.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 12 12.0 18.1 6.5 -.9 Inside b. Chi-1 trans st dev 54 9.7 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 66 8.2 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 132 9.8 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 61 7.6 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 94.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .82 2 Residue-by-residue listing for refined_5 Page 18 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution .14 Chi1-chi2 distribution .00 Chi1 only .02 Chi3 & chi4 .39 Omega .15 ------ .15 ===== Main-chain covalent forces:- Main-chain bond lengths .29 Main-chain bond angles .38 ------ .34 ===== OVERALL AVERAGE .22 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.