Residue-by-residue listing for refined_18 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.7 - - - 2 HIS 2 ~p - - -66.4 - - - - - - - 187.2 - 30.4 - ** * * ** 3 HIS 3 l - 181.7 - - - - - - - - 183.9 - 32.0 - 4 HIS 4 B 65.5 - - - - - - - - - 175.1 - 31.3 - 5 HIS 5 b - 189.1 - - - - - - - - 180.4 - 33.6 - 6 HIS 6 B - 188.4 - - - - - - - - 180.2 - 34.3 - 7 HIS 7 B - 174.8 - - - - - - - - 175.9 -.6 33.0 - +* +* 8 LEU 8 B 63.0 - - 169.8 - - - - - - 179.6 - 34.2 - 9 GLU 9 B - 189.3 - - - - - - - - 180.6 - 33.8 - 10 CYS 10 B - 181.9 - - - - - - - - 177.9 -1.0 34.6 - * * 11 SER 11 b - - -58.7 - - - - - - - 180.8 -.6 33.6 - +* +* 12 SER 12 A - - -56.7 - - - - - - - 180.5 -1.3 34.5 - * * 13 ASP 13 S XX - - -68.2 - - - - - - - 178.9 - 30.1 - **** * **** 14 SER 14 S b 50.2 - - - - - - - - - 178.1 -1.1 34.5 - * * 15 LEU 15 S B - 192.9 - - - - - - - - 186.3 - 35.7 - * * 16 GLN 16 b 61.8 - - 178.1 - - - - - - 175.2 -.6 36.7 - +* +* 17 LEU 17 B - - -59.9 177.3 - - - - - - 187.6 - 33.6 - * * Residue-by-residue listing for refined_18 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 HIS 18 E B - - -48.5 - - - - - - - 176.9 -2.7 35.5 - * * 19 ASN 19 E B - - -54.1 - - - - - - - 182.8 - 35.7 - 20 VAL 20 E B - 182.1 - - - - - - - - 174.9 -3.2 35.4 - +* +* 21 PHE 21 E B - 177.6 - - - - - - - - 183.7 -3.5 35.0 - ** ** 22 VAL 22 E B 53.0 - - - - - - - - - 185.0 -2.1 32.8 - 23 TYR 23 A 59.4 - - - - - - - - - 181.6 - 29.0 - * * 24 GLY 24 g - - - - - - - - - - - 189.2 - - - +* +* 25 SER 25 G A - 185.1 - - - - - - - - 184.8 - 33.5 - 26 PHE 26 G a - - -54.7 - - - - - - - 176.1 - 32.0 - 27 GLN 27 G A - - -68.1 181.0 - - - - - - 183.5 -1.9 34.5 - 28 ASP 28 h B - 177.2 - - - - - - - - 180.2 -.6 33.9 - +* +* 29 PRO 29 H - - - - - -62.9 -62.9 -37.1 - - - 181.3 - 38.4 - * * 30 ASP 30 H A - - -69.9 - - -65.6 -33.8 - - - 173.9 - 31.6 - * * 31 VAL 31 H A - 175.1 - - - -65.4 -40.9 - - - 180.9 - 34.4 - 32 ILE 32 H A - - -63.4 - - -65.9 -42.1 - - - 176.0 -1.6 33.5 - 33 ASN 33 H A - - -74.0 - - -58.8 -34.5 - - - 179.1 -2.8 33.2 - * * 34 VAL 34 H A - 178.1 - - - -77.6 -46.7 - - - 182.7 -1.3 33.3 - * * 35 MET 35 H A - 181.4 - 181.9 - -63.6 -36.8 - - - 181.5 -3.2 34.4 - +* +* 36 LEU 36 h a 51.3 - - - - - - - - - 182.9 -2.9 25.8 - * ** ** 37 ASP 37 t ~b - 182.2 - - - - - - - - 182.3 -.9 35.1 - ** * ** 38 ARG 38 S b - - -62.8 176.4 - - - - - - 171.8 - 36.5 - * * 39 THR 39 B - - -57.0 - - - - - - - 173.1 - 33.9 - * * 40 PRO 40 - - - - - -58.3 - - - - - 179.1 - 39.0 - * * 41 GLU 41 E B - 176.3 - 178.9 - - - - - - 184.4 -.9 35.1 - +* +* 42 ILE 42 E B - - -55.9 179.7 - - - - - - 176.3 - 35.5 - 43 VAL 43 E B 62.1 - - - - - - - - - 176.8 -2.2 33.7 - 44 SER 44 E B - - -57.0 - - - - - - - 184.0 - 36.1 - 45 ALA 45 E B - - - - - - - - - - 177.8 -2.5 34.2 - 46 THR 46 E B - - -55.5 - - - - - - - 176.9 -2.9 35.8 - * * 47 LEU 47 E B - 176.2 - - - - - - - - 180.5 -3.4 34.7 - +* +* 48 PRO 48 E - - - - - -82.6 - - - - - 178.7 - 38.6 - +* * +* 49 GLY 49 E - - - - - - - - - - - 180.2 -2.3 - - 50 PHE 50 E B - - -70.9 - - - - - - - 176.2 -.7 35.0 - +* +* 51 GLN 51 E B 63.3 - - 176.7 - - - - - - 183.6 -2.4 31.2 - 52 ARG 52 E B 40.7 - - - - - - - - - 181.7 - 30.1 - * * * Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 53 PHE 53 e B - - -70.1 - - - - - - - 174.8 -2.1 35.6 - 54 ARG 54 B B - - -80.9 - - - - - - - 179.7 -2.9 31.2 - * * 55 LEU 55 b - 190.2 - - - - - - - - 177.2 - 35.0 - 56 LYS 56 B - - -61.5 183.5 - - - - - - 180.5 - 32.8 - 57 GLY 57 S - - - - - - - - - - - 177.0 -1.3 - - * * 58 ARG 58 S A 57.6 - - - - - - - - - 180.5 - 31.2 - 59 LEU 59 S B - 183.7 - - - - - - - - 187.5 - 32.3 - * * 60 TYR 60 B - - -43.2 - - - - - - - 172.2 - 38.5 - +* * * +* 61 PRO 61 S - - - - - -68.3 - - - - - 184.6 - 38.4 - * * 62 CYS 62 e B 55.0 - - - - - - - - - 180.9 -1.6 33.3 - 63 ILE 63 E B - - -56.3 - - - - - - - 176.3 - 36.4 - 64 VAL 64 E B - - -58.7 - - - - - - - 177.1 -1.5 34.8 - 65 PRO 65 E - - - - - -57.0 - - - - - 182.7 - 37.3 - 66 SER 66 E B - 184.4 - - - - - - - - 176.1 -2.4 36.2 - 67 GLU 67 E A - - -59.2 178.0 - - - - - - 176.7 - 33.7 - 68 LYS 68 E b - - -63.5 179.3 - - - - - - 176.1 - 33.2 - 69 GLY 69 E - - - - - - - - - - - 176.0 - - - 70 GLU 70 E B 67.0 - - - - - - - - - 180.9 - 32.8 - 71 VAL 71 E B - 183.4 - - - - - - - - 177.7 -2.7 35.0 - 72 HIS 72 E B - - -67.4 - - - - - - - 179.5 -.5 33.4 - ** ** 73 GLY 73 E - - - - - - - - - - - 179.5 -2.7 - - 74 LYS 74 E B - - -85.9 - - - - - - - 177.2 -.6 32.3 - * +* +* 75 VAL 75 E B - 171.7 - - - - - - - - 175.9 -3.0 34.8 - * * 76 LEU 76 E B - - -54.3 179.7 - - - - - - 181.7 -3.5 36.9 - ** ** 77 MET 77 E B 56.6 - - 176.9 - - - - - - 184.5 -3.7 31.7 - ** ** 78 GLY 78 E - - - - - - - - - - - 181.4 -1.4 - - 79 VAL 79 E B - 182.1 - - - - - - - - 174.4 -2.3 37.1 - 80 THR 80 h B 56.1 - - - - - - - - - 183.0 - 33.2 - 81 SER 81 H A - - -57.2 - - -61.2 -26.8 - - - 176.9 - 31.6 - * * 82 ASP 82 H A - - -63.4 - - -65.5 -40.7 - - - 180.6 - 35.5 - 83 GLU 83 H A - - -55.6 172.4 - -78.0 -35.1 - - - 175.3 -.6 35.4 - * +* +* 84 LEU 84 H A - 181.3 - - - -62.2 -51.3 - - - 179.4 -2.6 33.8 - * * 85 GLU 85 H A 64.2 - - 173.2 - -64.1 -29.4 - - - 177.2 -3.2 32.6 - +* +* 86 ASN 86 H A - 175.0 - - - -59.7 -46.6 - - - 181.0 -1.1 35.0 - * * 87 LEU 87 H A - - -60.9 177.5 - -72.3 -36.9 - - - 177.0 -1.9 33.6 - 88 ASP 88 H A - 180.8 - - - -64.3 -31.5 - - - 174.1 -2.5 34.0 - * * 89 ALA 89 H A - - - - - -76.9 -47.2 - - - 183.8 -1.9 34.0 - 90 VAL 90 H a - 175.4 - - - -72.2 -60.1 - - - 177.7 -3.0 34.1 - +* * +* 91 GLU 91 h A - - -55.6 183.8 - - - - - - 188.6 -2.3 32.1 - * * Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 92 GLY 92 T - - - - - - - - - - - 180.4 -2.2 - - 93 ASN 93 T A - - -67.9 - - - - - - - 181.6 -.5 30.7 - ** ** 94 GLU 94 T A - - -58.9 178.4 - - - - - - 181.9 -.9 33.8 - +* +* 95 TYR 95 t B - - -68.5 - - - - - - - 176.9 -1.0 34.2 - * * 96 GLU 96 E B - 185.5 - 177.8 - - - - - - 182.1 -1.9 33.4 - 97 ARG 97 E B - 172.7 - 175.8 - - - - - - 182.5 - 34.3 - 98 VAL 98 E B - - -64.1 - - - - - - - 180.6 -2.6 33.2 - 99 THR 99 E B - 181.6 - - - - - - - - 183.1 - 32.8 - 100 VAL 100 E B - - -63.7 - - - - - - - 177.7 -3.1 34.3 - * * 101 GLY 101 E - - - - - - - - - - - 180.0 - - - 102 ILE 102 E B 53.2 - - - - - - - - - 180.4 -3.0 32.4 - * * 103 VAL 103 E B - 179.1 - - - - - - - - 182.8 -3.1 33.8 - * * 104 ARG 104 E B - - -58.8 183.8 - - - - - - 177.8 -3.4 34.9 - +* +* 105 GLU 105 e A - - -59.2 182.7 - - - - - - 176.6 -3.0 32.9 - * * 106 ASP 106 T A - - -57.6 - - - - - - - 190.2 -.5 37.2 - +* ** ** 107 ASN 107 T a 62.9 - - - - - - - - - 175.4 - 35.6 - 108 SER 108 t l - 185.8 - - - - - - - - 176.7 -1.5 32.3 - 109 GLU 109 e B - - -65.9 - - - - - - - 183.3 - 33.1 - 110 LYS 110 E B 64.1 - - 180.9 - - - - - - 179.8 - 33.9 - 111 MET 111 E B - - -65.5 176.2 - - - - - - 181.0 -3.3 34.4 - +* +* 112 ALA 112 E B - - - - - - - - - - 182.2 - 33.1 - 113 VAL 113 E B - - -58.7 - - - - - - - 175.0 -2.9 34.7 - * * 114 LYS 114 E B - - -51.1 - - - - - - - 175.0 -2.9 37.3 - * * * 115 THR 115 E B - 194.5 - - - - - - - - 184.1 -2.4 32.4 - 116 TYR 116 E B - - -58.3 - - - - - - - 179.6 -.6 34.7 - +* +* 117 MET 117 E B 63.0 - - 175.1 - - - - - - 180.2 -1.9 32.5 - 118 TRP 118 B - 191.0 - - - - - - - - 188.6 -2.9 34.3 - * * * 119 ILE 119 S A - - -54.1 - - - - - - - 182.4 - 33.7 - 120 ASN 120 S A - 185.4 - - - - - - - - 175.9 - 34.0 - 121 LYS 121 ~l 63.6 - - 188.9 - - - - - - 183.8 - 31.2 - ** ** 122 ALA 122 a - - - - - - - - - - 177.0 - 34.3 - 123 ASP 123 t B - - -72.5 - - - - - - - 181.4 - 33.5 - 124 PRO 124 T - - - - - -72.3 - - - - - 179.9 - 38.7 - * * 125 ASP 125 T A - - -60.5 - - - - - - - 184.7 - 35.5 - 126 MET 126 t B 56.0 - - 181.1 - - - - - - 174.1 -.6 34.9 - * +* +* 127 PHE 127 B B 53.6 - - - - - - - - - 185.7 -1.4 31.6 - 128 GLY 128 S - - - - - - - - - - - 182.1 - - - 129 GLU 129 B - - -61.8 186.8 - - - - - - 177.6 - 31.6 - 130 TRP 130 t B - 196.3 - - - - - - - - 181.1 - 34.0 - Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 131 ASN 131 h a - - -60.8 - - - - - - - 170.5 - 32.7 - +* +* 132 PHE 132 H A - - -56.7 - - -61.2 -31.3 - - - 177.6 - 35.3 - 133 GLU 133 H A 48.5 - - - - -56.3 -34.6 - - - 173.1 -2.2 30.2 - * * * 134 GLU 134 H A - 180.4 - 183.5 - -68.3 -39.7 - - - 179.5 -.7 33.6 - +* +* 135 TRP 135 H A - 180.9 - - - -63.5 -30.0 - - - 177.1 -1.1 32.4 - * * 136 LYS 136 H A - 177.6 - - - -52.3 -39.1 - - - 176.9 -1.7 34.6 - * * 137 ARG 137 H A - 167.0 - 182.6 - -57.1 -48.2 - - - 183.6 -1.0 35.3 - * * 138 LEU 138 H A - - -61.2 - - -83.0 -26.9 - - - 182.8 -.8 33.4 - * * +* +* 139 HIS 139 H A - 180.9 - - - -82.0 -27.4 - - - 179.7 -3.1 33.0 - * * * * 140 LYS 140 H A 69.8 - - 182.9 - -66.5 -32.5 - - - 184.4 -2.4 33.0 - 141 LYS 141 H A - - -60.0 183.9 - -48.6 -35.1 - - - 177.8 -.6 33.4 - * +* +* 142 LYS 142 H A - 180.3 - - - -59.0 -45.3 - - - 180.2 -.8 34.6 - +* +* 143 PHE 143 H A - - -56.1 - - -76.2 -34.8 - - - 179.3 -1.3 35.2 - 144 ILE 144 H A - - -54.9 - - -61.4 -34.0 - - - 178.7 -2.6 33.2 - 145 GLU 145 H A - - -60.8 183.4 - -54.1 -35.9 - - - 179.8 -2.1 34.0 - 146 THR 146 H A - - -53.7 - - -70.6 -47.4 - - - 178.7 -.9 34.6 - * * 147 PHE 147 H A - - -75.2 - - -71.8 -30.5 - - - 174.7 -1.4 29.6 - * * 148 LYS 148 H A - 176.4 - 179.3 - -57.0 -42.8 - - - 182.3 -3.5 35.7 - ** ** 149 LYS 149 H A - 190.2 - - - -71.0 -38.4 - - - 177.1 -1.5 34.6 - 150 ILE 150 H A - - -61.7 174.7 - -65.6 -41.0 - - - 177.8 -1.7 33.0 - 151 MET 151 H A - - -64.7 182.6 - -67.8 -37.7 - - - 176.1 -3.0 32.5 - * * 152 GLU 152 H A - - -67.3 179.0 - -67.8 -31.3 - - - 178.0 -2.3 32.0 - 153 CYS 153 H A - 184.2 - - - -71.9 -47.0 - - - 183.8 -1.8 34.1 - 154 LYS 154 H A - - -61.9 - - -80.6 -45.1 - - - 184.1 -2.7 34.7 - * * 155 LYS 155 h a - - -62.7 179.5 - - - - - - 185.6 -2.7 34.7 - 156 LYS 156 t l - 181.2 - 181.9 - - - - - - 173.8 -2.3 30.7 - * * 157 PRO 157 - - - - - -101.4 - - - - - 175.6 - 40.0 - *** +* *** 158 GLN 158 B 59.5 - - 181.5 - - - - - - 180.8 - 32.0 - 159 GLY 159 - - - - - - - - - - - 179.8 -.7 - - +* +* 160 GLN 160 B - 182.7 - 180.0 - - - - - - 178.7 - 33.7 - 161 GLY 161 - - - - - - - - - - - 181.3 -1.0 - - * * 162 ASN 162 B 62.8 - - - - - - - - - 173.9 - 33.8 - * * 163 ASP 163 b - - -70.5 - - - - - - - 183.8 - 33.5 - 164 ASP 164 b - 184.0 - - - - - - - - 173.1 - 31.6 - * * 165 ILE 165 a - 185.1 - 178.3 - - - - - - 186.2 -.7 34.3 - * +* +* Residue-by-residue listing for refined_18 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 166 SER 166 b 52.6 - - - - - - - - - 176.9 - 34.6 - 167 HIS 167 B - - -67.5 - - - - - - - 183.9 - 32.5 - 168 VAL 168 B 56.0 - - - - - - - - - 177.4 - 34.3 - 169 LEU 169 b - 181.0 - - - - - - - - 183.2 - 33.6 - 170 ARG 170 b 64.5 - - 179.3 - - - - - - 175.4 - 36.3 - 171 GLU 171 b - 179.3 - 180.5 - - - - - - 177.6 - 32.7 - 172 ASP 172 B 52.4 - - - - - - - - - 182.9 -.6 29.5 - +* * +* 173 GLN 173 - - 185.7 - - - - - - - - - -1.2 35.5 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* *** * +* +* ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.4 182.0 -61.8 179.7 -71.8 -66.2 -38.3 - - - 179.7 -1.9 33.9 Standard deviations: 6.4 5.8 7.2 3.7 15.7 8.2 7.4 - - - 3.8 .9 2.0 Numbers of values: 31 52 67 45 7 40 40 0 0 0 172 101 161 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 refined_18 Page 7 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.232 1.506 - 1.466 - 116.60 119.89 - 111.23 - 123.51 2 HIS 2 1.337 1.238 1.527 1.543 1.477 123.83 116.39 120.06 112.45 112.51 112.71 123.54 * * * * 3 HIS 3 1.342 1.242 1.512 1.566 1.465 123.34 115.73 121.33 111.96 108.04 113.10 122.80 +* * +* +* 4 HIS 4 1.308 1.238 1.506 1.560 1.441 120.47 114.84 121.40 111.44 111.79 113.30 123.74 * * +* +* 5 HIS 5 1.291 1.232 1.505 1.543 1.424 122.88 115.74 121.11 110.60 107.39 112.39 122.97 +** +* * * +** 6 HIS 6 1.294 1.229 1.496 1.539 1.432 121.26 116.14 120.66 110.73 107.87 111.04 123.15 +** * * * +** 7 HIS 7 1.289 1.232 1.520 1.542 1.428 121.11 114.92 121.17 111.24 110.99 111.32 123.90 +** +* +** 8 LEU 8 1.297 1.230 1.504 1.557 1.427 123.49 117.32 119.75 109.93 106.85 112.52 122.93 ** * +* +* * ** 9 GLU 9 1.291 1.230 1.518 1.546 1.435 120.82 115.86 120.99 112.61 107.88 109.88 123.07 +** * * * +** 10 CYS 10 1.296 1.236 1.510 1.538 1.428 121.60 116.48 120.66 110.53 109.31 110.40 122.84 ** +* ** 11 SER 11 1.307 1.235 1.530 1.524 1.432 121.02 115.52 121.17 111.17 109.54 110.86 123.13 +* * +* Residue-by-residue listing for refined_18 Page 8 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 SER 12 1.306 1.232 1.544 1.527 1.443 123.10 116.04 120.66 111.08 111.64 108.89 123.28 +* +* 13 ASP 13 1.347 1.242 1.516 1.551 1.502 124.76 116.38 120.49 110.57 113.41 114.58 123.14 * * ** +* ** ** 14 SER 14 1.306 1.252 1.550 1.533 1.442 123.02 117.06 120.47 112.18 111.24 107.93 122.45 +* * * * +* +* 15 LEU 15 1.336 1.237 1.526 1.533 1.428 122.04 116.04 120.72 112.09 107.08 107.58 123.22 +* * * +* +* 16 GLN 16 1.303 1.241 1.523 1.530 1.447 122.24 116.34 120.47 108.98 109.79 108.36 123.18 +* * +* 17 LEU 17 1.319 1.231 1.518 1.515 1.436 121.83 116.58 120.78 110.77 108.86 111.28 122.64 * * 18 HIS 18 1.300 1.247 1.509 1.536 1.450 121.01 115.97 120.34 108.86 110.59 110.23 123.69 ** ** 19 ASN 19 1.317 1.225 1.507 1.530 1.449 122.40 117.63 119.96 107.50 107.55 111.98 122.41 * * * 20 VAL 20 1.301 1.217 1.527 1.559 1.450 121.40 116.91 120.39 108.31 110.78 111.01 122.69 +* +* 21 PHE 21 1.308 1.240 1.509 1.544 1.440 121.58 115.58 120.72 111.01 107.21 109.92 123.69 +* * +* 22 VAL 22 1.296 1.247 1.527 1.558 1.440 122.33 116.37 120.93 112.02 110.70 111.07 122.70 ** * ** 23 TYR 23 1.324 1.233 1.528 1.539 1.436 120.59 119.10 119.43 112.63 115.13 113.22 121.46 * * * * +* +* 24 GLY 24 1.320 1.225 1.511 - 1.450 117.62 116.13 120.46 - 115.79 - 123.39 +* * +* 25 SER 25 1.307 1.229 1.544 1.542 1.455 123.07 118.06 120.32 110.96 113.73 109.65 121.58 +* +* 26 PHE 26 1.306 1.222 1.540 1.536 1.454 119.23 116.70 120.75 112.47 112.57 110.53 122.49 +* * * +* 27 GLN 27 1.347 1.235 1.524 1.538 1.486 121.52 116.38 120.66 107.65 111.30 112.33 122.95 * * * * * 28 ASP 28 1.307 1.231 1.525 1.525 1.444 121.74 117.20 120.54 110.27 111.39 110.57 122.26 +* +* 29 PRO 29 1.345 1.220 1.532 1.533 1.467 123.00 117.52 120.79 109.98 113.13 104.00 121.68 30 ASP 30 1.313 1.228 1.503 1.526 1.459 120.67 115.70 120.76 111.91 110.80 112.46 123.52 * * * * 31 VAL 31 1.317 1.231 1.533 1.557 1.454 122.27 115.91 121.12 109.44 109.62 111.57 122.93 32 ILE 32 1.321 1.244 1.541 1.544 1.450 122.60 116.47 120.55 111.32 111.04 110.35 122.96 * * 33 ASN 33 1.337 1.230 1.515 1.543 1.473 121.76 116.10 120.86 109.28 110.76 112.82 123.04 * * 34 VAL 34 1.317 1.238 1.530 1.563 1.445 121.45 116.57 120.35 109.89 110.83 112.37 123.08 35 MET 35 1.333 1.230 1.523 1.541 1.452 122.25 117.53 120.22 109.36 112.02 110.82 122.22 36 LEU 36 1.319 1.235 1.526 1.560 1.428 119.28 118.44 118.59 116.46 115.38 113.05 122.85 * +* * * * *** * * *** 37 ASP 37 1.343 1.232 1.519 1.548 1.496 122.05 115.22 121.34 108.01 110.61 111.40 123.44 * +* * +* 38 ARG 38 1.309 1.216 1.508 1.536 1.470 123.15 117.04 120.21 107.31 108.53 110.55 122.70 * * * 39 THR 39 1.307 1.240 1.525 1.525 1.431 121.55 116.74 120.51 109.22 111.16 111.76 122.69 +* * +* 40 PRO 40 1.343 1.247 1.529 1.532 1.466 123.61 116.34 120.32 109.89 110.79 103.68 123.30 41 GLU 41 1.316 1.223 1.534 1.526 1.455 122.27 116.07 121.32 110.10 110.22 109.37 122.61 Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 ILE 42 1.298 1.238 1.515 1.558 1.436 121.87 116.01 120.85 108.58 109.75 110.94 123.13 ** * ** 43 VAL 43 1.295 1.240 1.530 1.558 1.429 121.68 116.38 120.55 110.37 109.43 111.87 123.04 ** +* ** 44 SER 44 1.303 1.239 1.533 1.514 1.437 122.11 117.07 120.50 110.46 108.34 107.98 122.42 +* * * * +* 45 ALA 45 1.310 1.229 1.504 1.511 1.441 120.96 114.82 121.92 109.97 112.33 110.13 123.25 * * 46 THR 46 1.281 1.220 1.517 1.536 1.414 123.10 116.44 120.34 109.13 108.62 110.19 123.20 *** ** *** 47 LEU 47 1.291 1.231 1.527 1.539 1.431 122.42 117.98 120.24 111.12 108.83 109.65 121.69 +** * +** 48 PRO 48 1.339 1.235 1.523 1.541 1.447 122.46 116.12 120.77 110.20 111.52 104.07 123.10 * * 49 GLY 49 1.316 1.225 1.505 - 1.441 120.88 116.19 120.87 - 112.25 - 122.94 50 PHE 50 1.308 1.208 1.489 1.548 1.452 122.88 118.14 119.45 109.11 107.96 111.61 122.41 +* * +* * +* 51 GLN 51 1.299 1.239 1.482 1.526 1.439 119.30 113.85 121.46 109.95 111.33 114.85 124.69 ** ** * * * +** * +** 52 ARG 52 1.284 1.232 1.508 1.555 1.423 123.39 115.08 121.68 113.74 112.78 112.17 123.24 *** * +* +* *** 53 PHE 53 1.289 1.217 1.497 1.528 1.428 122.37 116.43 120.30 109.27 109.94 109.97 123.24 +** * +* +** 54 ARG 54 1.304 1.231 1.505 1.559 1.446 122.47 116.13 120.20 111.18 110.17 114.30 123.62 +* * ** ** 55 LEU 55 1.324 1.238 1.521 1.571 1.449 122.99 116.87 120.20 111.47 107.22 109.67 122.87 ** * ** 56 LYS 56 1.309 1.237 1.513 1.534 1.441 121.57 115.46 121.09 111.26 110.20 111.72 123.42 * * 57 GLY 57 1.304 1.234 1.497 - 1.435 122.20 117.21 119.81 - 109.41 - 122.95 +* * * * +* 58 ARG 58 1.327 1.226 1.512 1.563 1.455 120.62 115.37 121.43 112.52 110.85 112.69 123.18 +* * * +* 59 LEU 59 1.303 1.238 1.519 1.540 1.415 121.63 115.77 120.57 113.59 109.05 110.80 123.65 +* ** +* ** 60 TYR 60 1.294 1.236 1.525 1.544 1.431 123.75 119.37 119.10 108.31 106.78 107.22 121.53 +** * * +* * +* +* +** 61 PRO 61 1.347 1.226 1.532 1.546 1.455 121.73 116.14 121.04 110.59 109.97 104.21 122.71 * * 62 CYS 62 1.304 1.244 1.524 1.532 1.434 121.90 115.24 121.08 112.16 112.48 109.30 123.67 +* * * +* 63 ILE 63 1.321 1.229 1.513 1.562 1.447 123.28 117.07 119.89 108.20 108.44 110.36 123.00 64 VAL 64 1.312 1.251 1.531 1.576 1.458 122.30 117.91 119.62 108.16 108.04 112.93 122.43 * * * * * 65 PRO 65 1.349 1.247 1.532 1.534 1.463 122.52 115.36 121.54 110.94 112.03 104.84 123.10 * +* +* 66 SER 66 1.299 1.233 1.503 1.525 1.426 122.94 117.09 120.11 109.34 108.91 109.24 122.77 ** * +* ** 67 GLU 67 1.307 1.233 1.509 1.506 1.444 120.54 115.60 121.24 110.41 109.56 111.23 123.16 +* * +* 68 LYS 68 1.307 1.237 1.500 1.523 1.432 122.02 115.82 121.27 110.24 110.25 112.25 122.62 +* * * * +* 69 GLY 69 1.299 1.244 1.497 - 1.440 119.52 115.76 120.48 - 112.80 - 123.76 ** * ** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 70 GLU 70 1.308 1.232 1.522 1.551 1.438 122.87 116.88 120.47 111.07 108.86 112.63 122.64 * * * * * 71 VAL 71 1.297 1.225 1.516 1.553 1.443 121.57 116.82 120.54 108.87 109.48 111.37 122.62 ** ** 72 HIS 72 1.299 1.236 1.501 1.538 1.448 121.09 115.91 120.75 110.12 109.76 112.25 123.33 ** * * ** 73 GLY 73 1.300 1.236 1.486 - 1.418 120.70 116.60 120.57 - 110.31 - 122.83 ** +* ** ** 74 LYS 74 1.286 1.239 1.491 1.537 1.435 121.52 114.19 121.57 109.97 111.88 113.21 124.24 *** +* * * +* *** 75 VAL 75 1.289 1.229 1.512 1.547 1.434 122.92 115.02 120.72 108.66 110.64 111.56 124.26 +** * +** 76 LEU 76 1.302 1.226 1.512 1.540 1.427 123.63 117.21 120.33 108.35 106.00 109.86 122.40 +* +* * +* +* 77 MET 77 1.285 1.220 1.500 1.524 1.440 120.94 116.00 121.07 111.76 112.04 112.02 122.92 *** * *** 78 GLY 78 1.309 1.229 1.497 - 1.431 120.02 114.25 121.64 - 109.16 - 124.10 * * * * * * 79 VAL 79 1.312 1.233 1.511 1.557 1.437 124.10 117.34 119.86 107.62 109.69 109.60 122.80 * * * * * 80 THR 80 1.308 1.240 1.529 1.553 1.440 120.08 117.93 119.92 110.96 107.86 112.38 122.15 * * * 81 SER 81 1.305 1.216 1.539 1.526 1.448 121.05 116.45 120.55 113.20 111.88 110.58 122.93 +* +* +* 82 ASP 82 1.329 1.227 1.520 1.526 1.472 122.62 115.56 121.59 108.06 110.81 110.62 122.85 * * 83 GLU 83 1.301 1.227 1.535 1.526 1.451 122.69 115.49 121.23 111.44 109.03 107.93 123.28 ** +* ** 84 LEU 84 1.325 1.231 1.532 1.564 1.460 123.00 117.13 120.00 112.60 110.16 109.15 122.85 +* * +* 85 GLU 85 1.341 1.221 1.515 1.541 1.462 121.25 115.71 120.93 110.48 109.77 112.86 123.35 * * 86 ASN 86 1.333 1.211 1.517 1.544 1.445 122.52 115.90 121.02 110.42 108.95 109.98 123.01 87 LEU 87 1.314 1.226 1.518 1.519 1.453 122.48 116.27 120.61 110.96 110.97 110.38 123.11 * * 88 ASP 88 1.321 1.221 1.534 1.540 1.470 121.92 115.59 121.92 111.11 109.25 110.27 122.49 89 ALA 89 1.302 1.225 1.549 1.513 1.439 122.45 116.86 120.92 110.75 111.47 109.69 122.21 +* * +* 90 VAL 90 1.336 1.225 1.548 1.576 1.474 121.66 117.65 120.36 109.83 112.77 110.58 121.98 * * * 91 GLU 91 1.311 1.224 1.530 1.533 1.463 121.63 114.39 121.85 112.12 111.80 111.05 123.72 * * * 92 GLY 92 1.313 1.215 1.531 - 1.461 124.22 120.14 118.92 - 118.21 - 120.90 * ** +* +* * ** 93 ASN 93 1.315 1.233 1.522 1.538 1.476 118.24 117.07 120.56 110.57 112.29 114.25 122.35 * +* ** ** 94 GLU 94 1.316 1.231 1.529 1.529 1.466 121.10 115.45 121.23 110.57 111.24 110.36 123.31 95 TYR 95 1.300 1.218 1.510 1.530 1.452 123.79 117.44 120.30 110.40 110.04 110.54 122.22 ** * ** 96 GLU 96 1.305 1.247 1.505 1.536 1.433 119.72 114.92 121.06 111.19 108.84 111.60 124.00 +* * * +* 97 ARG 97 1.305 1.235 1.507 1.538 1.425 123.14 114.77 121.48 111.65 109.71 109.61 123.75 +* +* +* 98 VAL 98 1.300 1.241 1.504 1.539 1.437 123.12 116.08 120.52 110.18 110.80 112.23 123.38 ** * ** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 THR 99 1.296 1.234 1.529 1.569 1.434 121.31 116.35 120.95 112.02 108.79 111.78 122.65 ** * * * ** 100 VAL 100 1.306 1.242 1.518 1.561 1.450 121.63 115.43 120.96 108.56 111.14 112.19 123.61 +* +* 101 GLY 101 1.307 1.229 1.506 - 1.425 121.82 116.01 120.60 - 110.98 - 123.38 +* +* +* 102 ILE 102 1.302 1.215 1.500 1.575 1.442 122.91 117.01 120.27 111.68 110.17 112.34 122.71 +* * * * +* 103 VAL 103 1.289 1.227 1.502 1.552 1.429 121.47 116.02 120.48 110.78 108.42 111.80 123.48 +** * +* +** 104 ARG 104 1.306 1.244 1.500 1.520 1.440 122.11 116.10 120.88 108.65 110.72 111.06 123.00 +* * +* 105 GLU 105 1.304 1.227 1.527 1.526 1.442 121.08 115.03 121.21 111.76 109.73 111.08 123.76 +* +* 106 ASP 106 1.326 1.227 1.513 1.547 1.461 123.78 114.61 121.79 105.29 110.53 111.32 123.60 * +** +** 107 ASN 107 1.317 1.230 1.530 1.537 1.453 122.70 116.06 120.77 110.37 112.25 107.96 123.16 * * 108 SER 108 1.326 1.236 1.552 1.561 1.470 123.82 117.87 120.25 111.77 113.15 110.71 121.84 * +* * +* 109 GLU 109 1.321 1.235 1.519 1.511 1.461 120.47 116.34 120.45 110.50 110.87 111.40 123.21 110 LYS 110 1.314 1.237 1.530 1.532 1.454 121.69 115.59 121.17 109.86 111.10 111.09 123.23 * * 111 MET 111 1.303 1.220 1.487 1.518 1.455 123.71 115.59 120.94 108.67 110.39 111.82 123.46 +* +* * +* 112 ALA 112 1.282 1.241 1.515 1.513 1.454 121.60 116.10 120.67 110.66 110.82 111.35 123.23 *** *** 113 VAL 113 1.322 1.236 1.531 1.561 1.459 122.58 116.41 120.46 108.23 110.37 112.09 123.10 114 LYS 114 1.313 1.220 1.524 1.542 1.448 122.81 118.59 119.27 107.27 106.43 109.94 122.13 * * * +* +* 115 THR 115 1.298 1.245 1.520 1.562 1.448 120.09 116.44 120.08 110.83 109.07 113.36 123.48 ** * ** 116 TYR 116 1.310 1.233 1.519 1.539 1.436 122.42 116.13 120.94 110.57 109.89 109.94 122.92 * * * 117 MET 117 1.309 1.244 1.510 1.548 1.452 121.50 115.87 120.45 110.29 109.76 113.36 123.64 * +* +* 118 TRP 118 1.309 1.236 1.537 1.534 1.445 122.47 116.75 120.25 111.95 108.48 109.35 123.00 * * 119 ILE 119 1.325 1.238 1.518 1.580 1.470 121.50 116.30 120.76 107.61 111.81 113.86 122.92 * * * 120 ASN 120 1.318 1.225 1.503 1.528 1.456 120.83 114.66 120.93 110.01 109.17 111.55 124.41 * * 121 LYS 121 1.340 1.226 1.548 1.567 1.490 126.31 117.53 120.20 111.99 114.89 111.18 122.19 * +* +* +** * +** 122 ALA 122 1.325 1.234 1.527 1.523 1.451 121.26 117.14 120.29 110.28 112.39 109.61 122.56 123 ASP 123 1.324 1.225 1.514 1.537 1.470 121.06 118.47 120.02 109.51 110.13 112.30 121.50 * * * 124 PRO 124 1.346 1.231 1.527 1.539 1.470 122.62 116.56 120.22 109.60 112.97 104.04 123.21 125 ASP 125 1.332 1.230 1.506 1.539 1.471 122.53 114.78 121.33 107.54 110.25 111.46 123.85 * * 126 MET 126 1.308 1.237 1.515 1.527 1.444 123.18 115.38 121.19 109.75 112.24 109.51 123.43 +* +* 127 PHE 127 1.301 1.243 1.512 1.554 1.432 122.20 116.33 120.81 113.14 108.50 112.46 122.85 +* * * +* * +* Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 128 GLY 128 1.311 1.229 1.492 - 1.452 121.05 116.59 120.65 - 113.49 - 122.76 * * * 129 GLU 129 1.299 1.232 1.496 1.532 1.411 120.53 114.24 121.83 111.65 111.52 112.68 123.90 ** * ** * ** 130 TRP 130 1.273 1.229 1.505 1.523 1.414 124.06 117.39 118.53 111.12 106.30 111.50 123.97 **** ** * * +* **** 131 ASN 131 1.333 1.234 1.565 1.526 1.505 125.83 118.06 120.01 109.61 116.33 110.54 121.93 +* ** ** +* ** 132 PHE 132 1.326 1.217 1.530 1.534 1.454 122.95 115.32 121.30 108.26 107.58 111.68 123.37 * * 133 GLU 133 1.337 1.225 1.526 1.539 1.453 123.19 116.28 120.91 114.01 113.31 111.15 122.81 ** ** 134 GLU 134 1.305 1.227 1.527 1.528 1.464 121.13 115.91 121.04 109.44 109.81 112.20 123.04 +* * +* 135 TRP 135 1.324 1.214 1.523 1.546 1.455 122.18 116.28 120.33 111.93 110.36 111.60 123.37 136 LYS 136 1.339 1.219 1.532 1.542 1.470 123.17 116.08 120.63 110.59 110.24 109.62 123.25 137 ARG 137 1.318 1.228 1.530 1.527 1.459 123.30 116.26 121.26 109.57 111.76 109.19 122.48 138 LEU 138 1.301 1.223 1.519 1.546 1.441 120.97 115.65 121.18 110.29 110.69 111.79 123.14 ** ** 139 HIS 139 1.301 1.233 1.533 1.544 1.465 122.45 116.83 120.59 111.05 112.09 110.82 122.58 ** ** 140 LYS 140 1.322 1.216 1.513 1.541 1.457 121.39 115.98 120.23 109.93 110.23 112.74 123.78 * * 141 LYS 141 1.351 1.225 1.521 1.528 1.473 123.75 116.63 119.94 109.38 112.62 111.62 123.43 +* * +* 142 LYS 142 1.329 1.239 1.540 1.537 1.459 122.56 115.76 121.25 109.98 110.79 110.05 122.98 143 PHE 143 1.313 1.238 1.514 1.534 1.453 122.51 115.05 121.35 109.66 108.85 110.27 123.58 * * 144 ILE 144 1.332 1.196 1.525 1.564 1.447 122.23 117.73 119.66 109.64 110.18 112.94 122.58 +* +* 145 GLU 145 1.352 1.234 1.528 1.538 1.484 121.75 116.11 120.74 108.43 110.86 112.39 123.15 +* * * +* 146 THR 146 1.319 1.229 1.545 1.545 1.434 121.90 116.80 120.83 110.67 110.01 109.83 122.32 * * 147 PHE 147 1.327 1.223 1.502 1.517 1.460 121.05 116.11 120.39 112.44 113.26 113.29 123.51 * * +* +* 148 LYS 148 1.305 1.225 1.524 1.533 1.441 123.07 114.76 121.36 110.01 109.01 109.16 123.74 +* +* 149 LYS 149 1.324 1.232 1.535 1.556 1.448 123.43 115.83 121.23 113.25 108.87 107.71 122.91 * +* +* +* 150 ILE 150 1.324 1.235 1.545 1.569 1.459 122.42 116.51 121.03 111.62 110.37 111.11 122.41 * * * 151 MET 151 1.327 1.234 1.517 1.535 1.460 121.64 116.66 120.60 110.61 110.82 112.42 122.74 * * 152 GLU 152 1.321 1.224 1.524 1.534 1.450 121.17 116.28 120.79 111.61 111.04 112.15 122.92 153 CYS 153 1.307 1.234 1.538 1.530 1.445 121.85 116.80 120.69 110.22 111.52 110.36 122.51 +* +* 154 LYS 154 1.327 1.228 1.521 1.533 1.467 121.61 116.50 120.81 108.97 112.63 110.33 122.69 155 LYS 155 1.304 1.233 1.508 1.527 1.461 121.09 115.29 120.61 108.82 112.23 110.63 124.11 +* +* 156 LYS 156 1.313 1.237 1.532 1.554 1.464 124.15 117.24 121.12 111.44 111.49 113.91 121.40 * * * ** ** 157 PRO 157 1.335 1.257 1.534 1.533 1.426 122.67 116.55 121.19 110.26 110.55 102.12 122.25 * +** +** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 158 GLN 158 1.298 1.235 1.520 1.543 1.430 120.43 115.95 121.24 112.56 109.29 112.12 122.76 ** * * ** 159 GLY 159 1.302 1.242 1.495 - 1.430 120.39 116.71 120.10 - 111.36 - 123.20 +* * * +* 160 GLN 160 1.309 1.241 1.521 1.535 1.439 121.49 115.58 121.29 110.84 109.42 111.10 123.07 * * 161 GLY 161 1.302 1.231 1.496 - 1.435 121.35 115.54 121.24 - 110.29 - 123.21 +* * * +* 162 ASN 162 1.309 1.238 1.508 1.552 1.433 121.68 115.00 121.20 110.26 110.70 111.45 123.75 * * * * 163 ASP 163 1.294 1.234 1.490 1.546 1.440 123.92 116.53 120.74 109.62 107.79 113.41 122.63 ** +* * * +* ** 164 ASP 164 1.306 1.231 1.506 1.529 1.435 119.74 113.84 121.90 111.23 112.48 112.54 124.15 +* * * * * +* 165 ILE 165 1.290 1.227 1.534 1.572 1.448 125.06 111.56 123.80 112.20 103.52 110.97 124.58 +** * +* ** +* * +** +** 166 SER 166 1.320 1.245 1.521 1.527 1.427 126.68 115.14 121.82 111.43 113.69 107.90 123.04 +* +** +* +** 167 HIS 167 1.302 1.237 1.499 1.524 1.433 121.94 116.88 120.27 112.20 110.07 111.35 122.85 +* * * * +* 168 VAL 168 1.296 1.230 1.514 1.557 1.430 121.05 115.54 120.77 111.23 110.41 109.98 123.63 ** * ** 169 LEU 169 1.301 1.234 1.511 1.535 1.437 122.49 115.69 121.17 110.91 108.30 111.65 123.08 +* * * +* 170 ARG 170 1.300 1.236 1.506 1.533 1.439 121.85 116.86 120.09 108.93 108.56 109.43 123.05 ** * ** 171 GLU 171 1.298 1.233 1.511 1.533 1.423 121.16 115.43 121.46 111.43 109.20 112.21 122.97 ** +* * ** 172 ASP 172 1.299 1.236 1.507 1.556 1.439 121.52 113.78 122.67 114.01 110.62 113.53 123.45 ** * * * ** +* ** 173 GLN 173 1.292 - 1.511 1.560 1.428 124.31 - - 112.10 106.07 108.56 - +** +* +* * * +* * +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** ** +** +** ** +* *** +** +** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 14 ---------------------------------------- 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 .014 165 1.273 1.352 1.311 .015 **** +* * C-N (Pro) 1.341 .016 7 1.335 1.349 1.344 .005 C-O C-O 1.231 .020 172 1.196 1.257 1.232 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.482 1.565 1.520 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.486 1.531 1.502 .011 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.511 1.523 1.515 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.525 1.580 1.558 .012 * CH1E-CH2E (the rest) 1.530 .020 128 1.506 1.571 1.537 .012 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.411 1.505 1.448 .017 ** ** NH1-CH2G* (Gly) 1.451 .016 12 1.418 1.466 1.440 .014 ** N-CH1E (Pro) 1.466 .015 7 1.426 1.470 1.456 .014 +** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 15 ---------------------------------------- +-----------------+ | 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 2.0 153 111.56 119.37 116.21 1.08 ** +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.25 120.14 116.48 1.32 * +* CH1E-C-N (Pro) 116.9 1.5 7 115.36 117.52 116.37 .60 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 120.90 124.69 123.03 .62 * * O-C-N (Pro) 122.0 1.4 7 121.68 123.30 122.76 .56 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 118.24 126.68 122.13 1.28 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 11 117.62 124.22 120.89 1.58 +* ** C-N-CH1E (Pro) 122.6 5.0 7 121.73 123.61 122.66 .53 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.53 123.80 120.74 .66 * +* CH2G*-C-O (Gly) 120.8 2.1 12 118.92 121.64 120.44 .68 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.97 110.75 110.42 .31 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.61 112.20 109.86 1.40 * CH2E-CH1E-C (the rest) 110.1 1.9 128 105.29 116.46 110.63 1.59 +** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 103.52 116.33 110.26 1.93 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 109.16 118.21 112.11 2.56 * +* N-CH1E-C (Pro) 111.8 2.5 7 109.97 113.13 111.56 1.12 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.61 111.35 110.20 .69 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.60 113.86 111.53 1.05 * * N-CH1E-CH2E (Pro) 103.0 1.1 7 102.12 104.84 103.85 .78 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.22 114.85 111.09 1.60 +* +** ------------------------------------------------------------------------------------------------------------- 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_18 Page 16 ---------------------------------------- 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] 125 81.7% Residues in additional allowed regions [a,b,l,p] 24 15.7% Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0% Residues in disallowed regions [XX] 1 .7% ---- ------ Number of non-glycine and non-proline residues 153 100.0% Number of end-residues (excl. Gly and Pro) 1 Number of glycine residues 12 Number of proline residues 7 ---- Total number of residues 173 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 153 81.7 83.8 10.0 -.2 Inside b. Omega angle st dev 172 3.8 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 161 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 101 .9 .8 .2 .7 Inside f. Overall G-factor 173 -.1 -.4 .3 1.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 31 6.4 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 52 5.8 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 67 7.2 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 150 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 45 3.7 20.4 5.0 -3.3 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% 81.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .95 3 Residue-by-residue listing for refined_18 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.55 Chi1-chi2 distribution -.24 Chi1 only -.06 Chi3 & chi4 .39 Omega -.12 ------ -.20 ===== Main-chain covalent forces:- Main-chain bond lengths -.01 Main-chain bond angles .37 ------ .21 ===== OVERALL AVERAGE -.06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.