Residue-by-residue listing for analyzed_7 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 180.2 - - - 2 SER 2 b - - -102.5 - - - - - - - 180.0 - 34.5 - ** ** 3 ASP 3 b - - -60.0 - - - - - - - 180.0 - 34.4 - 4 PRO 4 - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 5 GLY 5 h - - - - - - - - - - - 180.1 - - - 6 PRO 6 H - - - - - -69.8 -69.8 -34.5 - - - 180.0 - 38.6 - * * 7 GLU 7 H A - - -46.1 - - -62.0 -33.2 - - - 179.9 - 34.4 - * * 8 ALA 8 H A - - - - - -68.9 -49.3 - - - 180.0 - 34.0 - 9 ALA 9 H A - - - - - -62.3 -48.8 - - - 180.1 -1.3 34.1 - 10 ARG 10 H A - 197.6 - 188.2 - -56.2 -33.5 - - - 180.0 -2.7 34.5 - 11 LEU 11 H A - 141.9 - - - -62.5 -48.8 - - - 179.9 -1.2 34.5 - ** * ** 12 ARG 12 H A - - -52.6 187.1 - -71.7 -39.3 - - - 180.1 -1.5 34.4 - 13 PHE 13 H A - 159.1 - - - -65.0 -38.5 - - - 180.1 -3.1 34.5 - * * * 14 ARG 14 H A - - -78.5 - - -80.3 -26.5 - - - 180.1 -2.6 34.5 - * * * 15 CYS 15 H A - - -90.9 - - -77.7 -13.8 - - - 180.1 -1.5 34.4 - +* * ** ** 16 PHE 16 h B - 180.2 - - - - - - - - 180.0 -.8 34.5 - +* +* 17 HIS 17 B 92.9 - - - - - - - - - 180.2 - 34.4 - +* +* Residue-by-residue listing for analyzed_7 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 18 TYR 18 B - 174.5 - - - - - - - - 180.0 -.6 34.4 - +* +* 19 GLU 19 t B 29.7 - - 169.8 - - - - - - 180.1 - 34.4 - ** ** 20 GLU 20 T A - - -62.1 158.2 - - - - - - 179.9 - 34.4 - * * 21 ALA 21 T A - - - - - - - - - - 180.1 - 34.0 - 22 THR 22 h A - 189.3 - - - - - - - - 180.0 -1.6 34.4 - 23 GLY 23 H - - - - - - 73.0 160.4 - - - 180.1 -.6 - - *11.6**17.7* +* *17.7* 24 PRO 24 H - - - - - -69.8 -69.8 -38.2 - - - 180.0 - 38.6 - * * 25 GLN 25 H A - - -116.7 - - -55.8 -43.4 - - - 180.0 - 34.4 - *** *** 26 GLU 26 H A - 207.5 - 141.6 - -68.0 -46.4 - - - 179.9 -.6 34.4 - * +* +* +* 27 ALA 27 H A - - - - - -55.1 -44.0 - - - 180.1 -1.6 34.0 - 28 LEU 28 H A - - -73.9 184.1 - -52.8 -47.3 - - - 179.8 -2.6 34.5 - * * 29 ALA 29 H A - - - - - -54.9 -38.0 - - - 180.1 -1.2 34.0 - * * 30 GLN 30 H A - - -84.5 144.7 - -78.8 -30.1 - - - 180.1 -1.3 34.4 - * +* * * +* 31 LEU 31 H A - - -86.0 164.8 - -70.4 -49.2 - - - 180.0 -2.4 34.4 - * * 32 ARG 32 H A 54.1 - - 187.2 - -55.2 -45.7 - - - 180.1 -3.2 34.5 - +* +* 33 GLU 33 H A - 130.1 - 174.1 - -60.5 -43.3 - - - 180.0 -1.2 34.4 - *** * *** 34 LEU 34 H A - - -69.4 170.5 - -67.8 -44.6 - - - 179.9 -1.6 34.5 - 35 CYS 35 H A - 212.0 - - - -59.5 -42.9 - - - 180.2 -3.3 34.4 - +* +* +* 36 ARG 36 H A - 160.1 - - - -56.1 -35.0 - - - 180.1 -2.5 34.5 - * * 37 GLN 37 H A - - -38.9 224.1 - -75.3 -16.9 - - - 180.0 -1.0 34.5 - +* +** +* * +** 38 TRP 38 H A - 158.6 - - - -87.6 -52.7 - - - 180.0 -1.5 34.4 - * +* * +* 39 LEU 39 H A - - -57.3 125.8 - -80.4 -39.3 - - - 179.9 -2.6 34.5 - +** * +** 40 ARG 40 h l - - -59.1 230.0 - - - - - - 180.0 -1.9 34.5 - +** +** 41 PRO 41 T - - - - - -69.7 - - - - - 180.0 - 38.6 - * * 42 GLU 42 T A 59.0 - - 221.0 - - - - - - 180.0 - 34.5 - ** ** 43 VAL 43 T A - - -60.5 - - - - - - - 180.1 -1.2 34.3 - * * 44 ARG 44 t B - - -58.1 211.2 - - - - - - 180.2 -3.2 34.5 - +* * +* 45 SER 45 h B - - -65.8 - - - - - - - 180.0 - 34.5 - 46 LYS 46 H A 75.9 - - - - -54.1 -31.6 - - - 180.0 - 34.5 - 47 GLU 47 H A 57.5 - - 182.4 - -67.8 -29.4 - - - 180.0 - 34.4 - 48 GLN 48 H A - - -119.1 - - -73.2 -47.2 - - - 180.0 -1.6 34.4 - *** *** 49 MET 49 H A - - -74.3 124.1 - -54.6 -38.2 - - - 180.0 -1.7 34.4 - +** +** Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 50 LEU 50 H A - - -103.2 - - -54.1 -50.6 - - - 179.9 -1.4 34.5 - ** ** 51 GLU 51 H A - 150.2 - 154.9 - -65.7 -53.6 - - - 180.1 -1.0 34.4 - +* * * * +* 52 LEU 52 H A - - -58.2 151.8 - -53.9 -35.4 - - - 179.9 -2.5 34.5 - * * 53 LEU 53 H A - 190.2 - - - -71.4 -30.5 - - - 179.9 -2.8 34.5 - * * 54 VAL 54 H A - 176.4 - - - -61.9 -36.6 - - - 180.0 -1.2 34.3 - * * 55 LEU 55 H A - 170.4 - - - -60.7 -45.9 - - - 180.0 -1.3 34.5 - * * 56 GLU 56 H A - 219.2 - - - -52.0 -45.4 - - - 180.1 -1.0 34.4 - ** * * ** 57 GLN 57 H A - 169.1 - - - -74.9 -46.0 - - - 180.1 -1.3 34.5 - 58 PHE 58 H A - 174.4 - - - -53.7 -56.2 - - - 180.0 -3.3 34.5 - * +* +* 59 LEU 59 H A - - -63.4 187.9 - -55.3 -31.8 - - - 179.9 -3.2 34.5 - +* +* 60 GLY 60 H - - - - - - -73.4 -18.7 - - - 180.0 -.8 - - +* +* +* 61 ALA 61 H A - - - - - -83.0 -32.2 - - - 180.1 -1.9 34.0 - * * 62 LEU 62 h b - - -76.0 164.9 - - - - - - 179.8 -1.4 34.4 - 63 PRO 63 t - - - - - -69.7 - - - - - 180.0 - 38.6 - * * 64 PRO 64 T - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 65 GLU 65 h A 46.7 - - 178.6 - - - - - - 179.9 - 34.5 - * * 66 ILE 66 H A - - -61.1 171.5 - -75.1 -41.8 - - - 180.0 - 34.3 - 67 GLN 67 H A - 189.1 - 172.7 - -56.9 -40.6 - - - 179.9 -2.6 34.4 - 68 ALA 68 H A - - - - - -60.1 -33.4 - - - 180.1 - 34.0 - 69 ARG 69 H A - - -65.1 - - -74.0 -38.1 - - - 180.0 -.7 34.4 - +* +* 70 VAL 70 H A - 153.8 - - - -56.9 -47.7 - - - 180.0 -1.8 34.4 - +* +* 71 GLN 71 H A - - -44.5 - - -55.9 -30.3 - - - 180.0 -1.8 34.5 - * * 72 GLY 72 h - - - - - - - - - - - 180.1 -.6 - - +* +* 73 GLN 73 T a - - -82.6 215.3 - - - - - - 180.1 -2.5 34.4 - * ** ** 74 ARG 74 t l - - -70.6 - - - - - - - 180.0 -3.3 34.5 - +* +* 75 PRO 75 - - - - - -69.8 - - - - - 179.9 - 38.6 - * * 76 GLY 76 S - - - - - - - - - - - 180.3 - - - 77 SER 77 h B - - -5.6 - - - - - - - 179.9 - 34.5 - **** **** 78 PRO 78 H - - - - - -69.7 -69.7 -45.2 - - - 180.0 - 38.6 - * * 79 GLU 79 H A - - -82.2 158.4 - -60.4 -38.8 - - - 180.1 - 34.4 - * * * 80 GLU 80 H A - 184.5 - - - -66.0 -52.6 - - - 179.9 - 34.4 - * * Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 81 ALA 81 H A - - - - - -54.9 -26.9 - - - 179.9 -2.0 34.0 - * * 82 ALA 82 H A - - - - - -68.2 -27.4 - - - 179.9 -1.4 34.1 - * * 83 ALA 83 H A - - - - - -74.4 -53.7 - - - 180.0 -2.0 34.1 - * * 84 LEU 84 H A 27.0 - - 139.3 - -60.0 -49.2 - - - 179.9 -1.4 34.5 - ** ** ** 85 VAL 85 H A - - -55.8 - - -62.8 -32.6 - - - 179.9 -2.3 34.3 - 86 ASP 86 H A - 165.8 - - - -62.0 -36.9 - - - 180.1 -1.0 34.4 - * * * 87 GLY 87 H - - - - - - -83.7 -27.7 - - - 180.1 -1.4 - - +* * +* 88 LEU 88 H A - - -91.2 159.6 - -72.1 -12.5 - - - 180.0 -1.8 34.5 - +* ** ** 89 ARG 89 h A - - -98.0 144.1 - - - - - - 180.1 -.8 34.5 - ** +* +* ** 90 ARG 90 T b 58.3 - - 234.1 - - - - - - 180.1 -1.2 34.5 - *** * *** 91 GLU 91 t b - 179.0 - - - - - - - - 180.0 -.9 34.4 - +* +* 92 PRO 92 - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 93 GLY 93 - - - - - - - - - - - 180.1 - - - 94 GLY 94 - - - - - - - - - - - - - - - 95 GLY 301 - - - - - - - - - - - 180.2 - - - 96 SER 302 b - - -102.6 - - - - - - - 180.0 - 34.5 - ** ** 97 ASP 303 b - - -60.1 - - - - - - - 180.0 - 34.5 - 98 PRO 304 - - - - - -69.7 - - - - - 180.0 - 38.6 - * * 99 GLY 305 h - - - - - - - - - - - 180.0 - - - 100 PRO 306 H - - - - - -69.7 -69.7 -34.7 - - - 180.0 - 38.6 - * * 101 GLU 307 H A - - -46.1 - - -61.8 -33.1 - - - 179.9 - 34.4 - * * 102 ALA 308 H A - - - - - -68.8 -49.3 - - - 179.9 - 34.0 - 103 ALA 309 H A - - - - - -62.4 -49.1 - - - 180.2 -1.3 34.0 - 104 ARG 310 H A - 198.2 - 187.4 - -56.0 -33.3 - - - 180.0 -2.7 34.5 - 105 LEU 311 H A - 141.9 - - - -62.6 -49.0 - - - 179.9 -1.2 34.5 - ** * ** 106 ARG 312 H A - - -53.2 186.3 - -71.9 -39.5 - - - 180.1 -1.5 34.4 - 107 PHE 313 H A - 159.4 - - - -64.5 -37.8 - - - 180.1 -3.1 34.4 - * * * 108 ARG 314 H A - - -77.8 - - -81.4 -26.4 - - - 180.1 -2.5 34.4 - * * * 109 CYS 315 H A - - -91.4 - - -77.4 -14.1 - - - 180.1 -1.5 34.5 - +* * ** ** 110 PHE 316 h B - 180.9 - - - - - - - - 180.0 -.9 34.5 - +* +* 111 HIS 317 B 111.0 - - - - - - - - - 180.1 - 34.4 - +** +** 112 TYR 318 B - 177.0 - - - - - - - - 180.1 -.6 34.4 - +* +* 113 GLU 319 t B 22.3 - - 178.5 - - - - - - 180.1 - 34.4 - +** +** Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 114 GLU 320 T A - - -61.8 157.1 - - - - - - 180.0 - 34.4 - * * 115 ALA 321 T A - - - - - - - - - - 180.1 - 34.0 - 116 THR 322 h A - 189.5 - - - - - - - - 179.9 -1.7 34.4 - 117 GLY 323 H - - - - - - 74.6 160.4 - - - 180.1 -.6 - - *11.8**17.7* +* *17.7* 118 PRO 324 H - - - - - -69.7 -69.7 -38.3 - - - 180.0 - 38.6 - * * 119 GLN 325 H A - - -117.5 - - -56.0 -44.0 - - - 180.1 - 34.4 - *** *** 120 GLU 326 H A - 207.8 - 139.8 - -66.7 -48.4 - - - 179.9 -.6 34.4 - * ** +* ** 121 ALA 327 H A - - - - - -54.0 -41.2 - - - 180.0 -1.7 34.0 - 122 LEU 328 H A - - -76.0 185.7 - -55.2 -48.3 - - - 179.8 -2.4 34.5 - 123 ALA 329 H A - - - - - -55.0 -37.4 - - - 180.1 -1.3 34.0 - 124 GLN 330 H A - - -77.4 143.0 - -78.7 -30.4 - - - 180.0 -1.4 34.4 - +* * +* 125 LEU 331 H A - - -85.7 163.4 - -70.2 -49.4 - - - 180.0 -2.3 34.5 - * * 126 ARG 332 H A 53.9 - - 186.9 - -55.0 -45.6 - - - 180.1 -3.1 34.5 - * * 127 GLU 333 H A - 129.9 - 174.2 - -60.6 -43.2 - - - 180.0 -1.2 34.5 - *** * *** 128 LEU 334 H A - - -69.4 170.5 - -67.8 -43.8 - - - 179.9 -1.6 34.5 - 129 CYS 335 H A - 211.7 - - - -60.3 -43.1 - - - 180.1 -3.3 34.4 - +* +* +* 130 ARG 336 H A - 159.8 - - - -56.0 -34.4 - - - 180.1 -2.6 34.5 - * * 131 GLN 337 H A - - -39.1 224.4 - -75.5 -18.6 - - - 180.1 -1.0 34.4 - +* +** +* * +** 132 TRP 338 H A - 157.6 - - - -86.9 -51.8 - - - 179.9 -1.4 34.5 - +* +* * +* 133 LEU 339 H A - - -57.2 131.4 - -80.2 -40.1 - - - 179.9 -2.7 34.5 - ** * ** 134 ARG 340 h l - - -59.1 229.8 - - - - - - 179.9 -1.8 34.5 - +** +** 135 PRO 341 T - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 136 GLU 342 T A 59.0 - - 221.1 - - - - - - 180.0 - 34.4 - ** ** 137 VAL 343 T A - - -60.5 - - - - - - - 180.0 -1.2 34.4 - * * 138 ARG 344 t B - - -57.6 211.7 - - - - - - 180.2 -3.2 34.5 - +* * +* 139 SER 345 h B - - -65.8 - - - - - - - 180.0 - 34.5 - 140 LYS 346 H A 76.0 - - - - -54.1 -31.6 - - - 180.0 - 34.5 - 141 GLU 347 H A 57.5 - - 182.3 - -67.4 -29.7 - - - 180.1 - 34.4 - 142 GLN 348 H A - - -119.0 - - -74.0 -46.1 - - - 180.0 -1.6 34.4 - *** *** 143 MET 349 H A - - -76.2 126.7 - -54.5 -39.0 - - - 180.0 -1.7 34.4 - +** +** 144 LEU 350 H A - - -104.5 - - -54.2 -49.6 - - - 179.9 -1.5 34.5 - +** +** 145 GLU 351 H A - 150.2 - 154.7 - -65.7 -54.1 - - - 180.0 -1.0 34.5 - +* * * * +* 146 LEU 352 H A - - -59.3 151.8 - -54.0 -35.0 - - - 179.9 -2.5 34.4 - * * Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 147 LEU 353 H A - 190.5 - - - -71.7 -30.3 - - - 179.8 -2.8 34.5 - * * 148 VAL 354 H A - 176.1 - - - -62.2 -36.3 - - - 180.0 -1.2 34.3 - * * 149 LEU 355 H A - 170.3 - - - -61.0 -44.9 - - - 179.9 -1.3 34.4 - * * 150 GLU 356 H A - 219.3 - - - -52.1 -47.2 - - - 180.1 -.9 34.4 - ** * * ** 151 GLN 357 H A - 170.3 - - - -74.7 -43.2 - - - 180.1 -1.3 34.4 - 152 PHE 358 H A - 175.2 - - - -53.8 -56.2 - - - 180.0 -3.2 34.5 - * +* +* 153 LEU 359 H A - - -61.0 189.6 - -58.4 -29.0 - - - 179.9 -3.2 34.4 - * * 154 GLY 360 H - - - - - - -74.3 -17.4 - - - 179.9 -.8 - - +* +* +* 155 ALA 361 H A - - - - - -86.0 -32.2 - - - 180.0 -1.8 34.0 - +* +* 156 LEU 362 h b - - -75.1 161.6 - - - - - - 179.9 -1.3 34.5 - 157 PRO 363 t - - - - - -69.7 - - - - - 180.0 - 38.6 - * * 158 PRO 364 T - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 159 GLU 365 h A 47.2 - - 178.2 - - - - - - 180.0 - 34.4 - * * 160 ILE 366 H A - - -61.3 171.6 - -75.0 -42.0 - - - 180.0 - 34.3 - 161 GLN 367 H A - 189.2 - 173.9 - -56.7 -40.3 - - - 179.9 -2.6 34.5 - 162 ALA 368 H A - - - - - -60.1 -32.9 - - - 180.1 - 34.1 - 163 ARG 369 H A - - -65.0 - - -73.9 -38.9 - - - 180.0 -.7 34.4 - +* +* 164 VAL 370 H A - 155.6 - - - -56.7 -46.8 - - - 180.0 -1.8 34.4 - +* +* 165 GLN 371 H A - - -45.8 - - -55.2 -32.1 - - - 180.0 -1.8 34.4 - * * 166 GLY 372 h - - - - - - - - - - - 180.1 -.7 - - +* +* 167 GLN 373 T a - - -107.5 160.1 - - - - - - 180.1 -2.3 34.4 - +** +** 168 ARG 374 t l - - -69.9 - - - - - - - 180.0 -3.2 34.5 - +* +* 169 PRO 375 - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 170 GLY 376 S - - - - - - - - - - - 180.2 - - - 171 SER 377 h B - - -5.6 - - - - - - - 180.0 - 34.5 - **** **** 172 PRO 378 H - - - - - -69.7 -69.7 -45.4 - - - 180.0 - 38.6 - * * 173 GLU 379 H A - - -81.3 158.1 - -60.5 -39.7 - - - 180.1 - 34.4 - * * 174 GLU 380 H A - 184.7 - - - -65.4 -52.4 - - - 179.9 - 34.5 - * * 175 ALA 381 H A - - - - - -55.2 -26.9 - - - 180.0 -2.0 34.0 - * * 176 ALA 382 H A - - - - - -68.3 -27.1 - - - 179.9 -1.4 34.0 - * * 177 ALA 383 H A - - - - - -74.3 -53.7 - - - 180.1 -2.0 34.0 - * * Residue-by-residue listing for analyzed_7 Page 7 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 178 LEU 384 H A 26.8 - - 140.3 - -60.2 -49.1 - - - 179.8 -1.4 34.5 - ** ** ** 179 VAL 385 H A - - -55.9 - - -62.8 -32.6 - - - 179.9 -2.3 34.3 - 180 ASP 386 H A - 166.0 - - - -61.9 -37.7 - - - 180.1 -1.0 34.4 - * * * 181 GLY 387 H - - - - - - -82.6 -27.4 - - - 180.1 -1.4 - - * * * 182 LEU 388 H A - - -91.2 159.7 - -72.2 -12.4 - - - 180.0 -1.7 34.5 - +* ** ** 183 ARG 389 h A - - -98.2 144.5 - - - - - - 180.1 -.7 34.4 - ** +* +* ** 184 ARG 390 T b 58.2 - - 234.1 - - - - - - 180.0 -1.2 34.5 - *** * *** 185 GLU 391 t b - 179.0 - - - - - - - - 180.0 -.9 34.4 - +* +* 186 PRO 392 - - - - - -69.8 - - - - - 180.0 - 38.6 - * * 187 GLY 393 - - - - - - - - - - - 180.0 - - - 188 GLY 394 - - - - - - - - - - - - - - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +** *** **** *** *11.8**17.7* +* * *17.7* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.3 175.5 -71.3 174.2 -69.8 -62.9 -35.4 - - - 180.0 -1.7 34.8 Standard deviations: 22.9 21.8 23.0 28.7 .0 20.1 27.4 - - - .1 .8 1.3 Numbers of values: 18 46 68 62 18 120 120 0 0 0 186 122 170 0 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 analyzed_7 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 - 1.231 1.516 - 1.452 - 116.34 120.64 - 112.46 - 123.02 2 SER 2 1.329 1.231 1.525 1.529 1.458 121.59 116.15 120.87 109.93 110.88 110.30 122.98 3 ASP 3 1.329 1.231 1.525 1.530 1.459 121.61 116.17 121.59 110.00 110.86 110.29 122.23 4 PRO 4 1.341 1.230 1.525 1.531 1.466 122.66 116.20 120.84 110.44 112.38 103.40 122.96 5 GLY 5 1.330 1.231 1.516 - 1.451 120.75 116.37 121.41 - 112.52 - 122.21 6 PRO 6 1.341 1.230 1.526 1.531 1.466 122.67 116.21 120.74 110.43 112.34 103.37 123.05 7 GLU 7 1.329 1.231 1.526 1.529 1.458 121.58 116.14 120.88 109.89 110.88 110.39 122.98 8 ALA 8 1.329 1.230 1.525 1.521 1.458 121.59 116.20 120.79 110.37 111.10 110.28 123.01 9 ALA 9 1.330 1.232 1.524 1.522 1.457 121.56 116.25 120.79 110.36 111.12 110.28 122.96 10 ARG 10 1.329 1.232 1.526 1.530 1.458 121.62 116.22 120.85 109.87 110.89 110.31 122.93 11 LEU 11 1.329 1.232 1.525 1.530 1.458 121.66 116.20 120.80 109.96 110.93 110.25 123.00 12 ARG 12 1.329 1.231 1.526 1.530 1.457 121.63 116.16 120.88 109.88 110.91 110.37 122.97 13 PHE 13 1.329 1.232 1.526 1.531 1.458 121.61 116.17 120.82 109.89 110.86 110.32 123.01 14 ARG 14 1.329 1.232 1.526 1.530 1.458 121.61 116.22 120.84 109.89 110.85 110.33 122.94 15 CYS 15 1.329 1.231 1.526 1.529 1.458 121.65 116.20 120.86 109.96 110.85 110.32 122.95 16 PHE 16 1.328 1.231 1.525 1.531 1.459 121.63 116.14 120.90 109.94 110.87 110.30 122.96 17 HIS 17 1.329 1.232 1.526 1.528 1.459 121.62 116.21 120.81 109.96 110.86 110.32 122.98 18 TYR 18 1.328 1.230 1.526 1.529 1.458 121.63 116.10 120.88 109.91 110.90 110.32 123.02 19 GLU 19 1.330 1.231 1.526 1.530 1.458 121.52 116.15 120.80 109.90 110.88 110.35 123.05 20 GLU 20 1.328 1.231 1.526 1.530 1.459 121.56 116.16 120.87 109.91 110.87 110.35 122.96 21 ALA 21 1.330 1.231 1.525 1.522 1.457 121.59 116.19 120.85 110.38 111.13 110.27 122.96 22 THR 22 1.330 1.229 1.525 1.541 1.457 121.58 116.18 120.83 109.02 111.16 111.36 122.98 Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 23 GLY 23 1.330 1.231 1.516 - 1.451 120.72 116.36 121.39 - 112.49 - 122.25 24 PRO 24 1.341 1.231 1.525 1.531 1.466 122.67 116.23 120.78 110.45 112.33 103.41 123.00 25 GLN 25 1.329 1.230 1.525 1.529 1.458 121.61 116.20 120.79 109.94 110.93 110.35 123.01 26 GLU 26 1.329 1.230 1.526 1.531 1.458 121.56 116.15 120.85 109.89 110.90 110.37 123.00 27 ALA 27 1.329 1.231 1.525 1.521 1.458 121.65 116.21 120.85 110.43 111.07 110.34 122.94 28 LEU 28 1.328 1.230 1.526 1.530 1.459 121.66 116.19 120.80 109.94 110.88 110.26 123.01 29 ALA 29 1.329 1.231 1.525 1.522 1.458 121.61 116.23 120.76 110.36 111.06 110.33 123.01 30 GLN 30 1.329 1.232 1.525 1.529 1.459 121.58 116.19 120.85 109.94 110.91 110.31 122.96 31 LEU 31 1.329 1.231 1.526 1.530 1.459 121.65 116.16 120.80 109.96 110.88 110.29 123.04 32 ARG 32 1.329 1.231 1.526 1.530 1.458 121.59 116.20 120.79 109.91 110.89 110.33 123.01 33 GLU 33 1.330 1.232 1.526 1.530 1.457 121.58 116.17 120.86 109.88 110.90 110.37 122.96 34 LEU 34 1.329 1.233 1.525 1.530 1.459 121.65 116.24 120.77 109.94 110.88 110.23 122.99 35 CYS 35 1.328 1.232 1.524 1.529 1.459 121.64 116.21 120.84 109.99 110.91 110.32 122.95 36 ARG 36 1.329 1.231 1.526 1.530 1.458 121.66 116.15 120.76 109.91 110.83 110.32 123.09 37 GLN 37 1.329 1.232 1.525 1.530 1.459 121.52 116.25 120.75 109.96 110.87 110.28 122.99 38 TRP 38 1.327 1.232 1.524 1.530 1.459 121.60 116.25 120.79 109.97 110.91 110.29 122.96 39 LEU 39 1.328 1.231 1.526 1.530 1.459 121.63 116.15 120.83 109.90 110.91 110.27 123.02 40 ARG 40 1.329 1.232 1.525 1.530 1.459 121.56 116.18 121.66 109.92 110.89 110.29 122.16 41 PRO 41 1.341 1.231 1.525 1.531 1.466 122.67 116.22 120.72 110.46 112.37 103.39 123.06 42 GLU 42 1.328 1.231 1.526 1.530 1.458 121.57 116.18 120.87 109.89 110.88 110.33 122.95 43 VAL 43 1.329 1.231 1.525 1.541 1.457 121.65 116.16 120.80 109.05 111.12 111.40 123.04 44 ARG 44 1.329 1.231 1.526 1.530 1.458 121.57 116.22 120.83 109.90 110.87 110.32 122.95 45 SER 45 1.330 1.230 1.526 1.530 1.458 121.64 116.09 120.92 109.92 110.86 110.30 123.00 46 LYS 46 1.329 1.231 1.525 1.530 1.458 121.61 116.20 120.76 109.88 110.93 110.26 123.04 47 GLU 47 1.329 1.231 1.526 1.530 1.458 121.57 116.20 120.78 109.87 110.87 110.38 123.02 48 GLN 48 1.329 1.230 1.525 1.529 1.458 121.64 116.17 120.81 109.97 110.91 110.33 123.03 49 MET 49 1.329 1.232 1.525 1.530 1.459 121.57 116.21 120.87 109.96 110.90 110.30 122.92 50 LEU 50 1.329 1.230 1.525 1.530 1.458 121.61 116.17 120.80 109.90 110.97 110.25 123.04 51 GLU 51 1.329 1.232 1.526 1.530 1.459 121.55 116.15 120.89 109.91 110.92 110.36 122.96 52 LEU 52 1.329 1.232 1.526 1.530 1.458 121.63 116.20 120.79 109.92 110.89 110.23 123.00 53 LEU 53 1.328 1.231 1.526 1.530 1.459 121.62 116.17 120.85 109.98 110.90 110.24 122.98 54 VAL 54 1.328 1.232 1.525 1.539 1.459 121.64 116.14 120.86 109.09 111.12 111.39 123.00 55 LEU 55 1.328 1.231 1.525 1.530 1.459 121.59 116.16 120.78 109.96 110.95 110.24 123.05 56 GLU 56 1.329 1.230 1.526 1.530 1.459 121.58 116.12 120.78 109.93 110.85 110.35 123.10 57 GLN 57 1.329 1.232 1.525 1.530 1.459 121.52 116.21 120.82 109.94 110.91 110.28 122.96 58 PHE 58 1.329 1.232 1.526 1.531 1.459 121.61 116.12 120.91 109.92 110.89 110.30 122.98 59 LEU 59 1.329 1.230 1.526 1.530 1.458 121.60 116.16 120.89 109.88 110.95 110.28 122.96 60 GLY 60 1.330 1.230 1.516 - 1.452 120.72 116.39 120.64 - 112.48 - 122.96 61 ALA 61 1.329 1.232 1.526 1.521 1.457 121.65 116.26 120.78 110.37 111.05 110.33 122.96 62 LEU 62 1.328 1.231 1.526 1.529 1.459 121.66 116.17 121.64 109.96 110.86 110.28 122.19 63 PRO 63 1.342 1.231 1.525 1.530 1.466 122.69 116.22 121.55 110.45 112.37 103.39 122.23 64 PRO 64 1.341 1.231 1.525 1.531 1.466 122.68 116.22 120.76 110.42 112.35 103.41 123.03 65 GLU 65 1.330 1.231 1.527 1.531 1.458 121.55 116.16 120.78 109.85 110.90 110.35 123.06 66 ILE 66 1.328 1.231 1.525 1.540 1.458 121.62 116.18 120.76 109.06 111.12 111.47 123.06 67 GLN 67 1.329 1.230 1.525 1.530 1.457 121.56 116.19 120.83 109.92 110.92 110.32 122.98 68 ALA 68 1.328 1.232 1.524 1.522 1.458 121.61 116.23 120.79 110.38 111.12 110.29 122.98 69 ARG 69 1.329 1.231 1.526 1.529 1.458 121.63 116.21 120.81 109.91 110.84 110.33 122.97 70 VAL 70 1.329 1.232 1.525 1.540 1.458 121.61 116.21 120.75 108.99 111.12 111.38 123.04 71 GLN 71 1.329 1.230 1.525 1.530 1.458 121.57 116.20 120.81 109.95 110.91 110.28 122.99 72 GLY 72 1.330 1.231 1.515 - 1.451 120.72 116.34 120.61 - 112.53 - 123.05 73 GLN 73 1.329 1.230 1.525 1.530 1.458 121.56 116.19 120.84 109.93 110.92 110.33 122.96 74 ARG 74 1.329 1.231 1.526 1.529 1.458 121.61 116.19 121.56 109.91 110.89 110.29 122.25 75 PRO 75 1.342 1.230 1.525 1.530 1.465 122.67 116.21 120.85 110.43 112.33 103.43 122.94 76 GLY 76 1.330 1.230 1.516 - 1.451 120.73 116.37 120.69 - 112.47 - 122.94 77 SER 77 1.329 1.231 1.526 1.530 1.458 121.63 116.16 121.71 109.89 110.85 110.32 122.13 Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 78 PRO 78 1.341 1.230 1.525 1.531 1.466 122.74 116.20 120.72 110.47 112.35 103.40 123.08 79 GLU 79 1.329 1.230 1.526 1.530 1.458 121.54 116.16 120.79 109.91 110.87 110.34 123.04 80 GLU 80 1.329 1.231 1.526 1.530 1.458 121.56 116.19 120.87 109.90 110.85 110.34 122.94 81 ALA 81 1.329 1.231 1.524 1.522 1.457 121.63 116.24 120.82 110.37 111.09 110.31 122.94 82 ALA 82 1.329 1.231 1.524 1.522 1.458 121.61 116.22 120.78 110.35 111.11 110.28 123.00 83 ALA 83 1.329 1.232 1.524 1.522 1.458 121.58 116.23 120.80 110.36 111.10 110.26 122.97 84 LEU 84 1.329 1.231 1.525 1.530 1.459 121.63 116.20 120.88 109.91 110.89 110.25 122.92 85 VAL 85 1.329 1.231 1.524 1.540 1.459 121.63 116.21 120.83 109.07 111.11 111.35 122.96 86 ASP 86 1.329 1.231 1.525 1.530 1.458 121.66 116.24 120.87 109.97 110.84 110.36 122.90 87 GLY 87 1.329 1.231 1.516 - 1.451 120.80 116.32 120.69 - 112.51 - 122.99 88 LEU 88 1.328 1.232 1.526 1.530 1.458 121.62 116.17 120.76 109.90 110.88 110.29 123.07 89 ARG 89 1.329 1.232 1.526 1.530 1.458 121.56 116.23 120.79 109.87 110.88 110.31 122.98 90 ARG 90 1.329 1.230 1.525 1.530 1.457 121.66 116.19 120.82 109.89 110.91 110.32 122.99 91 GLU 91 1.329 1.232 1.526 1.529 1.459 121.60 116.21 121.64 109.92 110.88 110.38 122.15 92 PRO 92 1.341 1.230 1.525 1.530 1.465 122.76 116.19 120.88 110.43 112.30 103.46 122.93 93 GLY 93 1.331 1.230 1.516 - 1.451 120.70 116.34 120.66 - 112.46 - 123.00 94 GLY 94 1.330 1.230 1.516 - 1.451 120.70 - 119.11 - 112.44 - - 95 GLY 301 - 1.231 1.515 - 1.451 - 116.35 120.68 - 112.48 - 122.97 96 SER 302 1.329 1.232 1.526 1.530 1.458 121.59 116.15 120.83 109.93 110.87 110.30 123.02 97 ASP 303 1.328 1.231 1.526 1.530 1.459 121.59 116.15 121.62 109.95 110.86 110.29 122.23 98 PRO 304 1.342 1.230 1.524 1.530 1.465 122.69 116.19 120.84 110.47 112.35 103.41 122.97 99 GLY 305 1.330 1.231 1.516 - 1.451 120.70 116.38 121.42 - 112.48 - 122.21 100 PRO 306 1.342 1.230 1.525 1.530 1.465 122.67 116.18 120.75 110.47 112.38 103.41 123.07 101 GLU 307 1.329 1.230 1.526 1.530 1.459 121.57 116.17 120.83 109.92 110.88 110.35 123.01 102 ALA 308 1.329 1.231 1.525 1.522 1.457 121.62 116.22 120.79 110.39 111.11 110.31 122.98 103 ALA 309 1.329 1.231 1.525 1.521 1.458 121.62 116.20 120.81 110.41 111.11 110.27 122.99 104 ARG 310 1.329 1.232 1.526 1.529 1.458 121.60 116.24 120.88 109.86 110.83 110.32 122.87 105 LEU 311 1.329 1.232 1.525 1.530 1.459 121.66 116.22 120.77 109.92 110.94 110.25 123.01 106 ARG 312 1.328 1.231 1.526 1.530 1.458 121.63 116.16 120.86 109.91 110.85 110.35 122.98 107 PHE 313 1.329 1.230 1.525 1.530 1.459 121.59 116.15 120.88 109.94 110.93 110.30 122.97 108 ARG 314 1.330 1.232 1.526 1.529 1.457 121.65 116.21 120.82 109.92 110.84 110.35 122.96 109 CYS 315 1.329 1.231 1.525 1.530 1.458 121.61 116.14 120.85 109.93 110.91 110.29 123.01 110 PHE 316 1.329 1.232 1.526 1.530 1.459 121.57 116.15 120.88 109.92 110.86 110.29 122.98 111 HIS 317 1.330 1.231 1.525 1.529 1.459 121.61 116.23 120.81 109.95 110.86 110.31 122.96 112 TYR 318 1.328 1.231 1.526 1.529 1.458 121.66 116.14 120.83 109.91 110.96 110.34 123.03 113 GLU 319 1.329 1.230 1.526 1.530 1.458 121.57 116.17 120.83 109.92 110.87 110.36 123.00 114 GLU 320 1.330 1.230 1.526 1.530 1.458 121.58 116.14 120.82 109.98 110.87 110.32 123.03 115 ALA 321 1.328 1.232 1.525 1.521 1.458 121.62 116.26 120.85 110.39 111.03 110.31 122.90 116 THR 322 1.330 1.231 1.525 1.540 1.457 121.63 116.23 120.80 109.01 111.13 111.36 122.97 117 GLY 323 1.329 1.232 1.516 - 1.451 120.75 116.40 121.40 - 112.47 - 122.20 118 PRO 324 1.341 1.230 1.525 1.531 1.466 122.71 116.22 120.72 110.46 112.33 103.38 123.06 119 GLN 325 1.329 1.230 1.526 1.529 1.457 121.55 116.18 120.77 109.97 110.95 110.33 123.05 120 GLU 326 1.329 1.230 1.526 1.530 1.458 121.60 116.16 120.87 109.90 110.85 110.40 122.96 121 ALA 327 1.329 1.231 1.525 1.522 1.458 121.62 116.21 120.86 110.35 111.12 110.29 122.93 122 LEU 328 1.329 1.231 1.524 1.530 1.459 121.65 116.19 120.85 109.94 110.92 110.27 122.95 123 ALA 329 1.329 1.230 1.525 1.522 1.458 121.62 116.21 120.78 110.39 111.10 110.28 123.01 124 GLN 330 1.330 1.231 1.526 1.530 1.458 121.56 116.20 120.85 109.94 110.90 110.31 122.95 125 LEU 331 1.329 1.231 1.525 1.530 1.458 121.66 116.18 120.83 109.89 110.92 110.28 122.98 126 ARG 332 1.329 1.230 1.526 1.530 1.459 121.58 116.18 120.75 109.90 110.86 110.30 123.07 127 GLU 333 1.330 1.232 1.526 1.530 1.458 121.52 116.16 120.86 109.85 110.89 110.34 122.98 128 LEU 334 1.328 1.231 1.526 1.529 1.459 121.64 116.19 120.79 109.93 110.89 110.29 123.03 129 CYS 335 1.328 1.230 1.526 1.530 1.459 121.61 116.16 120.82 109.94 110.91 110.29 123.03 130 ARG 336 1.329 1.231 1.526 1.530 1.458 121.57 116.22 120.71 109.93 110.86 110.27 123.07 131 GLN 337 1.329 1.230 1.525 1.529 1.458 121.57 116.19 120.82 109.98 110.91 110.32 122.98 132 TRP 338 1.328 1.233 1.525 1.530 1.458 121.59 116.26 120.77 109.93 110.91 110.31 122.97 Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 133 LEU 339 1.328 1.231 1.525 1.530 1.458 121.62 116.20 120.85 109.89 110.97 110.24 122.95 134 ARG 340 1.330 1.231 1.525 1.530 1.458 121.61 116.19 121.59 109.92 110.85 110.32 122.22 135 PRO 341 1.342 1.230 1.525 1.531 1.465 122.64 116.21 120.74 110.41 112.39 103.38 123.05 136 GLU 342 1.329 1.231 1.526 1.530 1.459 121.59 116.13 120.90 109.91 110.87 110.38 122.97 137 VAL 343 1.329 1.232 1.524 1.541 1.459 121.60 116.21 120.81 109.03 111.13 111.35 122.98 138 ARG 344 1.328 1.231 1.526 1.531 1.457 121.62 116.20 120.82 109.88 110.91 110.30 122.98 139 SER 345 1.329 1.230 1.527 1.529 1.458 121.60 116.11 120.92 109.88 110.83 110.33 122.97 140 LYS 346 1.329 1.231 1.526 1.530 1.458 121.66 116.23 120.72 109.87 110.87 110.28 123.05 141 GLU 347 1.330 1.231 1.526 1.530 1.458 121.56 116.17 120.81 109.92 110.86 110.37 123.02 142 GLN 348 1.329 1.231 1.524 1.530 1.458 121.58 116.26 120.78 109.96 110.93 110.30 122.97 143 MET 349 1.329 1.231 1.525 1.530 1.458 121.66 116.16 120.87 109.97 110.88 110.36 122.97 144 LEU 350 1.329 1.230 1.525 1.530 1.459 121.59 116.14 120.81 109.95 110.98 110.25 123.05 145 GLU 351 1.330 1.232 1.527 1.530 1.458 121.51 116.17 120.86 109.85 110.91 110.33 122.96 146 LEU 352 1.329 1.232 1.525 1.529 1.458 121.64 116.21 120.86 109.97 110.91 110.27 122.93 147 LEU 353 1.329 1.231 1.525 1.529 1.459 121.65 116.23 120.83 109.91 110.91 110.24 122.95 148 VAL 354 1.330 1.232 1.525 1.540 1.457 121.65 116.16 120.86 109.06 111.12 111.35 122.98 149 LEU 355 1.328 1.230 1.526 1.529 1.459 121.64 116.15 120.81 109.94 110.94 110.29 123.04 150 GLU 356 1.329 1.231 1.526 1.530 1.459 121.56 116.14 120.85 109.92 110.90 110.37 123.01 151 GLN 357 1.329 1.232 1.526 1.530 1.458 121.59 116.19 120.79 109.93 110.88 110.32 123.01 152 PHE 358 1.329 1.232 1.527 1.530 1.458 121.56 116.12 120.88 109.87 110.89 110.31 123.00 153 LEU 359 1.328 1.230 1.525 1.530 1.460 121.61 116.16 120.87 109.97 110.90 110.27 122.98 154 GLY 360 1.329 1.230 1.516 - 1.452 120.69 116.38 120.61 - 112.49 - 123.01 155 ALA 361 1.329 1.231 1.525 1.521 1.458 121.62 116.22 120.80 110.39 111.13 110.30 122.97 156 LEU 362 1.329 1.231 1.525 1.530 1.458 121.63 116.21 121.59 109.89 110.92 110.25 122.20 157 PRO 363 1.342 1.231 1.525 1.531 1.466 122.69 116.26 121.56 110.44 112.36 103.37 122.18 158 PRO 364 1.341 1.231 1.526 1.530 1.465 122.75 116.22 120.71 110.45 112.30 103.43 123.07 159 GLU 365 1.329 1.231 1.526 1.530 1.459 121.56 116.13 120.86 109.94 110.87 110.39 123.00 160 ILE 366 1.328 1.230 1.525 1.540 1.458 121.60 116.14 120.83 109.02 111.14 111.50 123.03 161 GLN 367 1.329 1.231 1.525 1.530 1.458 121.58 116.23 120.79 109.94 110.88 110.30 122.97 162 ALA 368 1.329 1.230 1.525 1.522 1.458 121.59 116.21 120.77 110.34 111.13 110.27 123.02 163 ARG 369 1.329 1.231 1.526 1.529 1.459 121.60 116.16 120.86 109.91 110.86 110.33 122.98 164 VAL 370 1.329 1.230 1.525 1.541 1.458 121.60 116.14 120.78 109.03 111.11 111.37 123.08 165 GLN 371 1.328 1.231 1.524 1.530 1.459 121.54 116.22 120.86 109.96 110.90 110.31 122.92 166 GLY 372 1.330 1.230 1.516 - 1.451 120.73 116.35 120.60 - 112.51 - 123.05 167 GLN 373 1.329 1.231 1.525 1.530 1.458 121.54 116.23 120.80 109.96 110.88 110.29 122.97 168 ARG 374 1.329 1.231 1.527 1.529 1.458 121.63 116.19 121.58 109.92 110.83 110.33 122.23 169 PRO 375 1.341 1.230 1.525 1.530 1.466 122.69 116.23 120.81 110.44 112.33 103.40 122.96 170 GLY 376 1.330 1.230 1.515 - 1.451 120.74 116.31 120.72 - 112.53 - 122.97 171 SER 377 1.330 1.231 1.526 1.530 1.458 121.57 116.14 121.67 109.87 110.86 110.30 122.20 172 PRO 378 1.341 1.230 1.524 1.531 1.466 122.71 116.22 120.74 110.48 112.35 103.41 123.04 173 GLU 379 1.329 1.230 1.526 1.530 1.459 121.56 116.17 120.83 109.90 110.88 110.37 123.00 174 GLU 380 1.330 1.230 1.526 1.530 1.458 121.55 116.13 120.81 109.90 110.89 110.31 123.06 175 ALA 381 1.329 1.231 1.525 1.521 1.458 121.57 116.26 120.73 110.36 111.08 110.31 123.01 176 ALA 382 1.328 1.230 1.525 1.521 1.457 121.63 116.21 120.82 110.35 111.10 110.33 122.97 177 ALA 383 1.329 1.232 1.525 1.521 1.458 121.63 116.27 120.81 110.40 111.05 110.29 122.92 178 LEU 384 1.329 1.230 1.526 1.530 1.458 121.68 116.15 120.88 109.93 110.91 110.28 122.97 179 VAL 385 1.329 1.232 1.524 1.540 1.458 121.60 116.19 120.86 109.03 111.16 111.39 122.95 180 ASP 386 1.329 1.230 1.525 1.529 1.459 121.63 116.20 120.86 109.98 110.89 110.30 122.93 181 GLY 387 1.330 1.232 1.515 - 1.451 120.74 116.38 120.67 - 112.48 - 122.95 182 LEU 388 1.328 1.230 1.526 1.530 1.459 121.66 116.16 120.83 109.90 110.95 110.28 123.01 183 ARG 389 1.329 1.232 1.527 1.529 1.458 121.63 116.21 120.78 109.92 110.82 110.35 123.01 184 ARG 390 1.328 1.230 1.526 1.530 1.458 121.60 116.17 120.81 109.86 110.85 110.31 123.02 185 GLU 391 1.329 1.231 1.526 1.531 1.459 121.59 116.19 121.63 109.93 110.90 110.35 122.18 186 PRO 392 1.342 1.230 1.525 1.531 1.465 122.72 116.20 120.85 110.47 112.34 103.41 122.95 187 GLY 393 1.330 1.230 1.515 - 1.451 120.73 116.39 120.68 - 112.46 - 122.93 Residue-by-residue listing for analyzed_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 188 GLY 394 1.330 - 1.516 - 1.451 120.74 - - - 112.49 - - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for analyzed_7 Page 13 ---------------------------------------- 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 1.327 1.331 1.329 .001 C-N (Pro) 1.341 .016 18 1.341 1.342 1.341 .000 C-O C-O 1.231 .020 187 1.229 1.233 1.231 .001 CA-C CH1E-C (except Gly) 1.525 .021 170 1.524 1.527 1.525 .001 CH2G*-C (Gly) 1.516 .018 18 1.515 1.516 1.516 .000 CA-CB CH1E-CH3E (Ala) 1.521 .033 20 1.521 1.522 1.522 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 12 1.539 1.541 1.540 .000 CH1E-CH2E (the rest) 1.530 .020 138 1.528 1.531 1.530 .001 N-CA NH1-CH1E (except Gly,Pro)1.458 .019 152 1.457 1.460 1.458 .001 NH1-CH2G* (Gly) 1.451 .016 18 1.451 1.452 1.451 .000 N-CH1E (Pro) 1.466 .015 18 1.465 1.466 1.466 .000 ------------------------------------------------------------------------------------------------------------- +-----------------+ | 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 2.0 152 116.09 116.27 116.19 .04 CH2G*-C-NH1 (Gly) 116.4 2.1 16 116.31 116.40 116.36 .03 CH1E-C-N (Pro) 116.9 1.5 18 116.18 116.26 116.21 .02 O-C-N O-C-NH1 (except Pro) 123.0 1.6 168 122.13 123.10 122.91 .23 O-C-N (Pro) 122.0 1.4 18 122.18 123.08 122.92 .26 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 152 121.51 121.68 121.60 .04 C-NH1-CH2G* (Gly) 120.6 1.7 16 120.69 120.80 120.73 .02 C-N-CH1E (Pro) 122.6 5.0 18 122.64 122.76 122.69 .03 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 170 120.71 121.71 120.88 .22 CH2G*-C-O (Gly) 120.8 2.1 17 119.11 121.42 120.74 .52 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 20 110.34 110.43 110.38 .02 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 12 108.99 109.09 109.04 .03 CH2E-CH1E-C (the rest) 110.1 1.9 138 109.85 110.48 109.99 .18 N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 152 110.82 111.16 110.94 .09 NH1-CH2G*-C (Gly) 112.5 2.9 18 112.44 112.53 112.49 .03 N-CH1E-C (Pro) 111.8 2.5 18 112.30 112.39 112.35 .03 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 20 110.26 110.34 110.30 .02 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 12 111.35 111.50 111.39 .05 N-CH1E-CH2E (Pro) 103.0 1.1 18 103.37 103.46 103.40 .02 NH1-CH1E-CH2E (the rest) 110.5 1.7 120 110.23 110.40 110.31 .04 ------------------------------------------------------------------------------------------------------------- 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 analyzed_7 Page 14 ---------------------------------------- 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] 136 89.5% Residues in additional allowed regions [a,b,l,p] 16 10.5% 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 89.5 83.8 10.0 .6 Inside b. Omega angle st dev 186 .1 6.0 3.0 -2.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 170 1.3 3.1 1.6 -1.1 BETTER e. H-bond energy st dev 122 .8 .8 .2 -.1 Inside f. Overall G-factor 188 .3 -.4 .3 2.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 22.9 18.1 6.5 .7 Inside b. Chi-1 trans st dev 46 21.8 19.0 5.3 .5 Inside c. Chi-1 gauche plus st dev 68 23.0 17.5 4.9 1.1 WORSE d. Chi-1 pooled st dev 132 23.5 18.2 4.8 1.1 WORSE e. Chi-2 trans st dev 62 28.7 20.4 5.0 1.7 WORSE 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% 89.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 23.4 3 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for analyzed_7 Page 15 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.08 Chi1-chi2 distribution -1.19 Chi1 only -.15 Chi3 & chi4 .47 Omega .71 ------ .04 ===== Main-chain covalent forces:- Main-chain bond lengths .71 Main-chain bond angles .69 ------ .70 ===== OVERALL AVERAGE .30 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.