Residue-by-residue listing for refined_1 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 181.9 - - - 2 HIS 2 b - 179.9 - - - - - - - - 173.1 - 31.8 - * * 3 HIS 3 ~b 63.1 - - - - - - - - - 183.2 -1.8 29.6 - ** * ** 4 HIS 4 a - 179.9 - - - - - - - - 179.0 - 33.8 - 5 HIS 5 B 60.1 - - - - - - - - - 183.0 - 32.0 - 6 HIS 6 b 59.6 - - - - - - - - - 175.8 - 32.7 - 7 HIS 7 a - 191.7 - - - - - - - - 181.0 - 34.1 - 8 LEU 8 B 67.0 - - 177.3 - - - - - - 184.1 - 31.9 - 9 GLU 9 b 57.8 - - 179.9 - - - - - - 178.5 - 35.8 - 10 CYS 10 B - - -57.8 - - - - - - - 175.6 - 34.5 - 11 SER 11 a - - -60.1 - - - - - - - 180.9 - 34.3 - 12 SER 12 S A 48.3 - - - - - - - - - 180.1 - 34.5 - * * 13 ASP 13 l - 183.2 - - - - - - - - 181.2 - 32.8 - 14 SER 14 b 52.1 - - - - - - - - - 174.9 - 29.3 - * * 15 LEU 15 S a - - -72.7 - - - - - - - 175.0 -.9 34.0 - +* +* 16 GLN 16 S A 56.1 - - 181.6 - - - - - - 173.9 - 31.5 - * * 17 LEU 17 S B - - -65.4 179.1 - - - - - - 188.3 - 32.8 - * * 18 HIS 18 E B - - -53.6 - - - - - - - 175.8 -2.8 35.4 - 19 ASN 19 E B 51.9 - - - - - - - - - 186.1 - 29.4 - * * * 20 VAL 20 E B - 180.3 - - - - - - - - 177.4 -2.3 35.5 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 PHE 21 E B - 178.1 - - - - - - - - 183.9 -3.2 35.4 - +* +* 22 VAL 22 E B - - -64.7 - - - - - - - 187.9 -3.2 31.5 - * +* +* 23 TYR 23 a 56.9 - - - - - - - - - 184.1 - 33.5 - 24 GLY 24 g - - - - - - - - - - - 186.3 - - - * * 25 SER 25 G A - 180.6 - - - - - - - - 183.3 - 34.5 - 26 PHE 26 G A - - -65.5 - - - - - - - 180.7 - 33.2 - 27 GLN 27 G A - 194.8 - 183.9 - - - - - - 180.4 -1.8 33.7 - 28 ASP 28 h B - 176.1 - - - - - - - - 181.8 -.5 34.7 - +* +* 29 PRO 29 H - - - - - -69.4 -69.4 -25.3 - - - 180.6 - 38.0 - * * * 30 ASP 30 H A - 172.5 - - - -67.6 -41.1 - - - 178.6 - 32.4 - 31 VAL 31 H A 66.9 - - - - -68.5 -28.7 - - - 179.7 - 31.7 - 32 ILE 32 H A - - -59.9 - - -67.0 -47.1 - - - 176.6 -1.0 33.3 - * * 33 ASN 33 H A - - -72.6 - - -57.3 -35.2 - - - 181.8 -2.3 33.7 - 34 VAL 34 H A - 180.9 - - - -81.7 -47.4 - - - 185.5 -1.4 32.9 - * * 35 MET 35 H A - 201.1 - - - -64.9 -35.9 - - - 174.6 -3.4 33.6 - * +* +* 36 LEU 36 h a 47.0 - - 160.1 - - - - - - 184.1 -2.4 28.8 - * * * 37 ASP 37 t ~b - 187.4 - - - - - - - - 183.4 -.8 35.4 - ** +* ** 38 ARG 38 S B - - -60.4 178.1 - - - - - - 176.9 - 36.1 - 39 THR 39 B - - -53.9 - - - - - - - 176.2 - 34.0 - 40 PRO 40 - - - - - -52.3 - - - - - 181.1 - 39.1 - * * * 41 GLU 41 E B - 183.9 - 179.9 - - - - - - 185.6 -1.3 33.8 - * * 42 ILE 42 E B - - -50.0 178.3 - - - - - - 176.8 - 36.0 - * * 43 VAL 43 E B 57.8 - - - - - - - - - 175.0 -2.0 33.6 - 44 SER 44 E B - - -58.0 - - - - - - - 181.5 - 35.1 - 45 ALA 45 E B - - - - - - - - - - 181.1 -3.0 33.8 - * * 46 THR 46 E B - - -56.7 - - - - - - - 176.9 -2.7 35.2 - 47 LEU 47 E B - 175.6 - - - - - - - - 180.2 -3.5 34.6 - +* +* 48 PRO 48 E - - - - - -83.9 - - - - - 179.0 - 38.7 - +* * +* 49 GLY 49 e - - - - - - - - - - - 179.4 -2.7 - - 50 PHE 50 t B - - -70.2 - - - - - - - 181.1 -.7 33.4 - +* +* 51 GLN 51 E B - 176.9 - 174.5 - - - - - - 178.7 -2.9 34.6 - * * 52 ARG 52 E B - 184.6 - 185.0 - - - - - - 176.4 - 35.1 - 53 PHE 53 e B - - -72.7 - - - - - - - 187.1 -1.8 33.5 - * * 54 ARG 54 B 66.0 - - 181.0 - - - - - - 176.9 -.5 34.5 - ** ** 55 LEU 55 b - 186.2 - - - - - - - - 173.7 - 35.0 - * * 56 LYS 56 B - 184.5 - 175.7 - - - - - - 180.1 - 32.6 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 GLY 57 S - - - - - - - - - - - 177.9 - - - 58 ARG 58 S A - 190.2 - - - - - - - - 179.2 - 34.8 - 59 LEU 59 S B - 186.5 - - - - - - - - 189.7 - 31.5 - +* +* 60 TYR 60 B - - -53.6 - - - - - - - 175.0 - 37.2 - 61 PRO 61 - - - - - -58.9 - - - - - 183.7 - 38.6 - * * 62 CYS 62 e B 58.7 - - - - - - - - - 179.3 - 35.8 - 63 ILE 63 E B - - -60.6 - - - - - - - 176.6 - 35.5 - 64 VAL 64 E B - - -63.8 - - - - - - - 178.4 -2.7 32.6 - 65 PRO 65 - - - - - -61.6 - - - - - 178.4 - 38.3 - * * 66 SER 66 t B - 183.3 - - - - - - - - 182.4 - 34.7 - 67 GLU 67 T A - - -51.8 - - - - - - - 182.9 - 34.8 - 68 LYS 68 T A - - -62.1 176.1 - - - - - - 183.5 - 35.2 - 69 GLY 69 e - - - - - - - - - - - 175.7 -1.6 - - 70 GLU 70 E B 61.0 - - - - - - - - - 182.1 - 32.7 - 71 VAL 71 E B - 183.6 - - - - - - - - 173.9 -2.9 35.5 - * * * 72 HIS 72 E B - - -66.8 - - - - - - - 182.7 -.6 33.6 - +* +* 73 GLY 73 E - - - - - - - - - - - 182.3 -3.3 - - +* +* 74 LYS 74 E B - - -84.2 - - - - - - - 176.6 -.7 33.0 - * +* +* 75 VAL 75 E B - 169.2 - - - - - - - - 174.9 -3.1 34.7 - * * 76 LEU 76 E B - - -57.6 182.1 - - - - - - 179.9 -3.3 36.1 - +* +* 77 MET 77 E B 55.0 - - 175.8 - - - - - - 179.7 -3.0 31.8 - * * 78 GLY 78 E - - - - - - - - - - - 179.9 -2.3 - - 79 VAL 79 E B 66.0 - - - - - - - - - 179.6 -2.4 33.1 - 80 THR 80 h B 36.0 - - - - - - - - - 186.8 - 33.3 - +* * +* 81 SER 81 H A - - -58.0 - - -68.8 -35.4 - - - 180.2 - 32.0 - 82 ASP 82 H A - - -62.8 - - -63.6 -43.7 - - - 178.4 - 33.7 - 83 GLU 83 H A - - -67.7 - - -69.8 -36.4 - - - 177.8 - 34.9 - 84 LEU 84 H A - 183.6 - - - -60.5 -43.7 - - - 175.5 -2.0 33.2 - 85 GLU 85 H A - - -67.9 - - -71.9 -32.3 - - - 177.1 -2.5 33.0 - 86 ASN 86 H A - 129.6 - - - -65.6 -38.2 - - - 175.3 -1.9 31.7 - *** *** 87 LEU 87 H A - - -61.7 177.1 - -62.2 -42.1 - - - 178.4 -2.8 34.8 - * * 88 ASP 88 H A - 178.2 - - - -64.1 -36.1 - - - 177.5 -1.6 34.5 - 89 ALA 89 H A - - - - - -68.7 -45.3 - - - 181.4 -2.0 34.4 - 90 VAL 90 H A - 175.0 - - - -69.8 -51.4 - - - 182.4 -2.7 33.0 - * * 91 GLU 91 H A - - -61.8 - - -77.0 -29.2 - - - 184.5 -3.3 35.2 - +* +* 92 GLY 92 h - - - - - - - - - - - 179.8 -1.4 - - 93 ASN 93 T A - - -63.0 - - - - - - - 182.3 -.7 34.3 - +* +* 94 GLU 94 e a 52.3 - - 187.5 - - - - - - 180.4 -2.1 33.0 - 95 TYR 95 E B - - -67.8 - - - - - - - 177.1 -1.5 34.0 - 96 GLU 96 E B - 183.2 - - - - - - - - 182.3 -1.9 34.4 - 97 ARG 97 E B - 188.9 - 176.0 - - - - - - 182.5 - 34.4 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 VAL 98 E B - - -60.5 - - - - - - - 179.7 -3.1 32.7 - * * 99 THR 99 E B - 179.4 - - - - - - - - 182.4 - 32.6 - 100 VAL 100 E B - - -64.9 - - - - - - - 177.1 -3.3 34.6 - +* +* 101 GLY 101 E - - - - - - - - - - - 180.8 - - - 102 ILE 102 E B 55.5 - - - - - - - - - 181.6 -2.7 31.4 - 103 VAL 103 E B - 178.6 - - - - - - - - 177.6 -2.7 33.9 - 104 ARG 104 E B - - -61.8 - - - - - - - 175.5 -3.3 37.0 - +* +* 105 GLU 105 e A - - -63.8 184.8 - - - - - - 175.1 -2.8 32.8 - * * 106 ASP 106 S a - - -46.3 - - - - - - - 183.7 - 36.7 - * * 107 ASN 107 S ~a - - -49.4 - - - - - - - 175.3 - 35.3 - ** * ** 108 SER 108 S a - - -60.7 - - - - - - - 183.5 - 35.0 - 109 GLU 109 e B - - -60.7 187.4 - - - - - - 179.6 - 35.5 - 110 LYS 110 E B 69.5 - - - - - - - - - 180.9 - 33.5 - 111 MET 111 E B - - -66.8 173.9 - - - - - - 177.4 -3.3 35.6 - +* +* 112 ALA 112 E B - - - - - - - - - - 182.2 - 33.7 - 113 VAL 113 E B - - -58.8 - - - - - - - 174.4 -2.5 34.4 - 114 LYS 114 E B - - -69.1 - - - - - - - 174.4 -2.0 33.8 - 115 THR 115 E B - 191.7 - - - - - - - - 180.4 -2.4 33.7 - 116 TYR 116 E B - - -61.1 - - - - - - - 186.4 -.5 32.0 - * ** ** 117 MET 117 E B - 175.6 - 178.1 - - - - - - 179.1 -2.5 35.2 - 118 TRP 118 E B - 185.4 - - - - - - - - 188.6 -3.1 33.7 - * * * 119 ILE 119 e A - - -52.0 173.6 - - - - - - 181.2 -.6 34.1 - +* +* 120 ASN 120 B - 185.5 - - - - - - - - 186.3 - 34.1 - * * 121 LYS 121 S A - - -55.7 - - - - - - - 177.1 -1.0 33.7 - * * 122 ALA 122 S b - - - - - - - - - - 184.5 - 33.5 - 123 ASP 123 B - 186.6 - - - - - - - - 180.6 -.8 34.7 - +* +* 124 PRO 124 S - - - - - -87.7 - - - - - 183.8 - 39.3 - +* +* +* 125 ASP 125 S A - - -65.4 - - - - - - - 181.2 - 33.3 - 126 MET 126 S A 60.8 - - 183.0 - - - - - - 185.3 - 34.6 - 127 PHE 127 b - 183.6 - - - - - - - - 176.7 - 32.3 - 128 GLY 128 - - - - - - - - - - - 180.6 - - - 129 GLU 129 B 57.6 - - - - - - - - - 181.4 - 31.6 - 130 TRP 130 h B - 193.4 - - - - - - - - 181.6 - 33.7 - 131 ASN 131 H A - - -51.6 - - -49.8 -46.6 - - - 181.7 - 36.0 - * * * 132 PHE 132 H A - - -69.0 - - -64.2 -31.7 - - - 176.7 - 30.7 - 133 GLU 133 H A - - -64.1 183.4 - -67.7 -45.8 - - - 179.3 -.9 34.4 - +* +* 134 GLU 134 H A - 186.1 - - - -64.3 -43.2 - - - 178.5 -2.0 35.1 - 135 TRP 135 H A - 178.4 - - - -67.2 -37.7 - - - 179.1 -3.0 32.0 - * * 136 LYS 136 H A - 182.1 - 176.0 - -55.9 -32.0 - - - 176.9 -2.5 35.0 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 137 ARG 137 H A - 168.5 - 181.5 - -65.7 -52.0 - - - 180.9 -1.2 36.0 - * * * 138 LEU 138 H A - - -66.9 - - -79.3 -19.6 - - - 178.2 -1.2 32.9 - * +* * +* 139 HIS 139 H A - 180.2 - - - -68.9 -24.5 - - - 175.4 -2.7 33.9 - * * 140 LYS 140 H A - 175.5 - 179.1 - -60.1 -42.0 - - - 181.9 -.7 35.1 - +* +* 141 LYS 141 H A - 180.1 - 176.5 - -57.3 -31.2 - - - 179.1 -.5 32.9 - ** ** 142 LYS 142 H A - - -57.8 - - -61.5 -37.2 - - - 175.2 -.6 33.3 - +* +* 143 PHE 143 H A - - -61.5 - - -76.8 -39.2 - - - 181.5 -1.3 35.3 - 144 ILE 144 H A - - -55.3 - - -60.1 -33.1 - - - 177.6 -2.4 32.4 - 145 GLU 145 H A - - -70.8 - - -51.3 -39.3 - - - 179.8 -2.4 33.5 - * * 146 THR 146 H A - 187.9 - - - -74.9 -29.0 - - - 176.4 -1.1 32.3 - * * 147 PHE 147 H A - - -84.9 - - -76.5 -35.1 - - - 180.4 -.9 32.0 - * * * 148 LYS 148 H A - - -69.7 172.2 - -55.6 -31.1 - - - 177.4 -3.1 32.8 - * * 149 LYS 149 H A 72.0 - - 177.4 - -75.1 -34.5 - - - 183.6 -.8 31.3 - +* +* 150 ILE 150 H A - - -61.7 180.0 - -55.5 -29.7 - - - 177.0 -.8 30.3 - +* * +* 151 MET 151 H A - - -69.4 - - -54.8 -26.0 - - - 179.7 -.9 32.3 - * * * 152 GLU 152 H A 64.0 - - 185.1 - -57.1 -40.9 - - - 180.5 -2.3 33.8 - 153 CYS 153 H A - 182.0 - - - -71.8 -31.9 - - - 184.5 -1.4 35.2 - 154 LYS 154 H A - - -53.6 - - -75.7 -44.4 - - - 181.7 -1.1 34.3 - * * 155 LYS 155 h ~a - 181.3 - 179.5 - - - - - - 188.8 -3.0 35.1 - ** +* * ** 156 LYS 156 t B - 182.2 - 180.1 - - - - - - 177.5 -1.3 35.8 - 157 PRO 157 - - - - - -64.3 - - - - - 182.2 - 38.9 - * * 158 GLN 158 a - - -58.2 - - - - - - - 183.6 -.9 34.0 - +* +* 159 GLY 159 - - - - - - - - - - - 182.1 -2.8 - - * * 160 GLN 160 B - 176.8 - 177.6 - - - - - - 179.6 - 35.1 - 161 GLY 161 S - - - - - - - - - - - 179.2 - - - 162 ASN 162 B - 177.0 - - - - - - - - 179.9 - 34.2 - 163 ASP 163 B 62.6 - - - - - - - - - 175.2 - 32.2 - 164 ASP 164 b - 177.3 - - - - - - - - 183.4 - 32.1 - 165 ILE 165 S b - 183.0 - 179.2 - - - - - - 176.6 - 35.2 - 166 SER 166 B - 180.9 - - - - - - - - 178.0 - 35.0 - 167 HIS 167 B 62.7 - - - - - - - - - 181.7 - 33.2 - 168 VAL 168 B - - -66.1 - - - - - - - 180.8 - 33.8 - 169 LEU 169 B - 190.8 - 172.9 - - - - - - 177.8 - 34.6 - 170 ARG 170 B - 196.0 - - - - - - - - 183.4 -.6 35.5 - +* +* 171 GLU 171 b - - -57.4 186.4 - - - - - - 175.5 - 31.7 - 172 ASP 172 B 63.9 - - - - - - - - - 182.8 -1.5 33.0 - 173 GLN 173 - - 182.9 - 176.8 - - - - - - - - 32.8 - ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* *** * +* * +* +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.9 181.7 -62.2 178.9 -68.3 -65.8 -37.0 - - - 180.0 -2.0 34.0 Standard deviations: 7.5 9.4 7.4 4.9 13.1 7.8 7.5 - - - 3.5 .9 1.8 Numbers of values: 29 58 63 41 7 42 42 0 0 0 172 92 161 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_1 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 - 1.237 1.491 - 1.454 - 117.24 119.99 - 110.31 - 122.76 * * 2 HIS 2 1.308 1.223 1.529 1.548 1.441 120.72 115.03 120.68 111.92 111.79 111.95 124.10 +* +* 3 HIS 3 1.326 1.236 1.518 1.571 1.467 124.78 114.73 122.07 112.50 109.71 115.32 123.08 ** +* * +** +** 4 HIS 4 1.301 1.213 1.525 1.534 1.440 122.60 117.62 119.92 111.69 110.40 109.80 122.46 ** ** 5 HIS 5 1.331 1.228 1.525 1.565 1.473 120.75 117.07 120.32 111.46 110.39 112.72 122.60 +* * +* 6 HIS 6 1.318 1.233 1.518 1.546 1.451 120.65 116.10 121.48 111.08 112.93 111.18 122.42 7 HIS 7 1.305 1.223 1.533 1.549 1.442 120.62 116.30 121.42 111.29 109.10 110.27 122.25 +* +* 8 LEU 8 1.315 1.242 1.514 1.554 1.446 121.25 115.50 120.72 111.26 110.66 112.95 123.77 * * * * 9 GLU 9 1.310 1.237 1.526 1.531 1.442 123.37 116.99 120.05 109.88 108.73 109.09 122.96 * * 10 CYS 10 1.315 1.235 1.524 1.516 1.448 121.80 115.76 121.27 109.71 111.15 110.29 122.90 11 SER 11 1.301 1.229 1.532 1.532 1.449 123.30 114.78 121.83 111.56 108.79 109.63 123.36 +* +* 12 SER 12 1.321 1.233 1.527 1.527 1.441 123.29 115.87 120.29 111.45 111.55 108.53 123.83 * * Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 ASP 13 1.348 1.231 1.528 1.556 1.474 123.62 116.31 121.50 111.87 110.22 111.12 122.10 * * * * 14 SER 14 1.311 1.231 1.522 1.544 1.433 120.48 114.58 121.91 113.69 113.61 112.57 123.28 * * +* * +* 15 LEU 15 1.308 1.227 1.489 1.499 1.408 123.63 114.50 121.75 110.81 109.56 110.61 123.73 +* +* +* +** * +** 16 GLN 16 1.294 1.228 1.513 1.535 1.459 122.60 113.56 122.47 112.95 109.30 112.18 123.97 ** * +* ** 17 LEU 17 1.287 1.236 1.494 1.524 1.434 123.23 116.31 120.58 110.69 107.91 113.15 123.11 *** * * * +* *** 18 HIS 18 1.286 1.247 1.503 1.530 1.439 121.27 115.56 120.59 109.49 111.08 109.66 123.82 *** * * *** 19 ASN 19 1.308 1.241 1.523 1.549 1.440 122.65 115.39 121.57 113.89 111.46 113.36 123.01 +* +* +* +* 20 VAL 20 1.317 1.223 1.525 1.576 1.452 122.80 116.42 120.35 108.91 110.04 110.62 123.23 * * 21 PHE 21 1.308 1.239 1.519 1.544 1.444 122.86 116.30 120.68 111.29 107.77 108.74 123.02 +* * * +* 22 VAL 22 1.308 1.242 1.510 1.544 1.441 121.65 115.63 121.22 111.25 112.35 112.85 123.15 +* +* 23 TYR 23 1.312 1.226 1.539 1.554 1.435 121.15 117.22 120.49 111.98 113.13 109.22 122.29 * * * * 24 GLY 24 1.313 1.230 1.502 - 1.435 119.98 115.23 120.76 - 113.43 - 123.95 * * * 25 SER 25 1.310 1.230 1.543 1.545 1.450 123.87 117.08 120.62 111.28 112.59 108.53 122.24 * * * * 26 PHE 26 1.316 1.220 1.523 1.532 1.462 120.91 118.39 119.87 109.69 113.66 111.31 121.70 * * 27 GLN 27 1.323 1.234 1.549 1.531 1.454 119.64 115.85 121.82 110.81 110.00 110.67 122.33 * * * 28 ASP 28 1.305 1.211 1.526 1.531 1.451 122.61 118.65 120.04 110.34 109.85 109.86 121.31 +* * * * +* 29 PRO 29 1.341 1.228 1.536 1.524 1.469 122.15 117.28 120.83 110.53 113.54 103.81 121.87 30 ASP 30 1.312 1.233 1.508 1.523 1.455 120.48 116.39 120.57 111.02 110.81 112.18 122.98 * * 31 VAL 31 1.321 1.223 1.530 1.572 1.448 120.41 116.28 120.89 111.27 109.40 113.81 122.81 * * * 32 ILE 32 1.332 1.236 1.541 1.548 1.438 122.02 116.99 120.53 111.68 110.41 110.56 122.43 * * * 33 ASN 33 1.333 1.228 1.519 1.533 1.471 121.41 116.30 121.04 108.19 111.74 112.78 122.65 * * * 34 VAL 34 1.304 1.236 1.533 1.555 1.445 120.78 116.66 120.45 110.33 112.07 111.91 122.87 +* +* 35 MET 35 1.332 1.220 1.533 1.548 1.459 121.75 117.33 120.47 112.19 110.27 109.64 122.16 * * 36 LEU 36 1.324 1.240 1.515 1.564 1.443 120.10 117.21 119.84 112.42 112.05 115.37 122.84 +* * +** +** 37 ASP 37 1.331 1.233 1.511 1.538 1.474 121.49 115.27 121.38 108.61 109.86 110.69 123.33 38 ARG 38 1.312 1.227 1.493 1.528 1.453 122.55 116.42 119.98 107.61 109.16 110.91 123.60 * +* * +* 39 THR 39 1.311 1.247 1.534 1.535 1.432 121.41 116.48 120.65 110.31 110.30 110.98 122.83 * * * 40 PRO 40 1.349 1.238 1.532 1.527 1.480 124.23 116.97 119.84 110.02 111.65 103.05 123.16 41 GLU 41 1.335 1.236 1.519 1.538 1.461 122.24 115.59 121.08 110.25 109.37 111.50 123.30 Residue-by-residue listing for refined_1 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 1.296 1.240 1.513 1.548 1.427 121.66 115.66 121.02 108.15 109.70 110.59 123.33 ** +* ** 43 VAL 43 1.289 1.225 1.522 1.558 1.434 122.13 116.97 120.22 110.30 110.14 111.90 122.77 +** * +** 44 SER 44 1.309 1.249 1.530 1.523 1.434 121.22 116.45 120.53 110.32 108.06 109.77 123.00 * * * * 45 ALA 45 1.304 1.233 1.506 1.508 1.430 121.81 115.23 121.41 110.53 111.09 110.58 123.36 +* * +* 46 THR 46 1.287 1.218 1.515 1.540 1.427 122.56 116.04 120.56 109.25 110.15 110.50 123.39 *** +* *** 47 LEU 47 1.294 1.229 1.532 1.535 1.431 122.88 118.07 120.30 110.95 109.60 109.71 121.57 +** * +** 48 PRO 48 1.337 1.244 1.528 1.543 1.447 122.56 116.27 120.99 110.23 111.84 103.92 122.74 * * 49 GLY 49 1.315 1.233 1.505 - 1.443 120.49 115.85 120.94 - 111.81 - 123.20 * * 50 PHE 50 1.314 1.219 1.489 1.541 1.441 123.19 116.47 120.27 110.14 108.84 112.66 123.26 * +* * +* 51 GLN 51 1.285 1.238 1.500 1.519 1.421 122.04 115.54 120.66 111.27 109.77 109.39 123.76 *** * +* *** 52 ARG 52 1.306 1.224 1.499 1.537 1.420 121.68 115.88 120.50 109.16 108.22 111.39 123.61 +* * +* * +* 53 PHE 53 1.278 1.230 1.507 1.526 1.428 122.21 118.50 119.32 112.44 107.55 110.51 122.17 +*** +* * * * +*** 54 ARG 54 1.304 1.239 1.519 1.538 1.447 119.44 115.53 120.36 110.40 111.94 109.62 124.10 +* * +* 55 LEU 55 1.333 1.236 1.525 1.552 1.459 124.50 117.50 119.71 109.15 107.54 111.42 122.75 * +* * +* 56 LYS 56 1.315 1.242 1.521 1.538 1.445 121.53 116.13 120.58 111.37 109.49 112.08 123.24 57 GLY 57 1.314 1.224 1.502 - 1.440 121.31 116.19 120.78 - 110.66 - 123.02 * * 58 ARG 58 1.309 1.227 1.503 1.561 1.444 121.87 115.70 121.09 112.45 106.46 109.11 123.19 * * +* * +* +* 59 LEU 59 1.304 1.229 1.520 1.532 1.426 121.44 116.74 119.67 113.65 109.01 111.72 123.57 +* +* +* +* 60 TYR 60 1.307 1.230 1.531 1.545 1.445 123.20 119.37 118.92 109.69 108.62 107.31 121.69 +* +* * +* +* 61 PRO 61 1.368 1.233 1.527 1.537 1.465 122.01 116.10 120.57 110.39 110.85 103.80 123.32 +* +* 62 CYS 62 1.308 1.234 1.536 1.522 1.444 122.54 116.80 120.32 110.35 110.69 107.99 122.89 +* * +* 63 ILE 63 1.333 1.231 1.524 1.566 1.467 122.74 116.99 120.12 107.76 109.66 111.66 122.89 64 VAL 64 1.312 1.231 1.524 1.563 1.461 121.84 117.59 120.29 109.62 110.43 113.68 122.07 * * * 65 PRO 65 1.340 1.230 1.537 1.536 1.470 123.06 115.90 120.99 110.56 112.92 103.65 123.06 66 SER 66 1.310 1.233 1.530 1.533 1.440 123.03 116.94 120.18 111.22 108.62 109.47 122.88 * * 67 GLU 67 1.318 1.236 1.530 1.545 1.468 123.07 115.77 121.39 107.84 111.35 111.74 122.84 * * 68 LYS 68 1.304 1.234 1.522 1.515 1.446 122.52 116.75 120.75 110.18 111.99 108.64 122.48 +* * +* 69 GLY 69 1.314 1.252 1.510 - 1.429 119.57 114.30 121.54 - 114.05 - 124.14 * * * * 70 GLU 70 1.303 1.241 1.522 1.558 1.430 125.14 116.77 120.66 110.78 107.76 113.49 122.57 +* * * +* * +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.295 1.216 1.493 1.559 1.432 121.26 116.57 120.69 107.77 109.41 112.08 122.73 ** +* * ** 72 HIS 72 1.288 1.227 1.503 1.541 1.430 120.16 116.31 120.52 111.26 106.84 111.94 123.12 +** * * +* +** 73 GLY 73 1.293 1.226 1.480 - 1.418 120.68 116.75 120.21 - 110.68 - 123.04 +** +* ** +** 74 LYS 74 1.288 1.227 1.498 1.537 1.433 121.48 114.58 121.38 110.20 111.96 111.99 124.02 +** * * +** 75 VAL 75 1.284 1.223 1.520 1.553 1.444 123.53 115.68 120.51 108.91 111.28 111.28 123.80 *** * *** 76 LEU 76 1.316 1.233 1.515 1.541 1.443 123.20 117.45 119.99 107.98 107.42 111.02 122.53 * * * 77 MET 77 1.300 1.229 1.496 1.524 1.450 120.49 114.96 121.34 110.59 112.44 112.83 123.69 ** * * ** 78 GLY 78 1.300 1.225 1.505 - 1.427 121.16 116.49 120.45 - 111.59 - 123.06 ** * ** 79 VAL 79 1.327 1.245 1.536 1.577 1.453 120.94 116.09 120.54 110.70 110.18 112.19 123.35 * * 80 THR 80 1.303 1.240 1.552 1.531 1.439 123.82 116.58 120.91 112.46 112.34 108.97 122.51 +* * * * +* * +* 81 SER 81 1.326 1.235 1.542 1.526 1.458 122.56 117.82 119.75 111.77 114.42 110.35 122.41 * * 82 ASP 82 1.333 1.235 1.505 1.537 1.482 120.85 114.71 121.57 109.18 110.03 112.42 123.72 * * * 83 GLU 83 1.302 1.200 1.522 1.536 1.444 123.92 116.48 120.77 110.59 109.83 109.57 122.73 +* +* * +* 84 LEU 84 1.317 1.239 1.548 1.559 1.457 122.33 116.49 120.89 113.75 109.80 108.77 122.60 * * +* * +* 85 GLU 85 1.324 1.221 1.519 1.520 1.456 121.25 116.11 120.97 111.01 110.84 111.27 122.91 86 ASN 86 1.313 1.221 1.529 1.548 1.456 122.14 116.36 120.70 113.34 110.95 110.88 122.92 * +* +* 87 LEU 87 1.322 1.223 1.520 1.541 1.457 122.48 115.40 121.12 109.48 109.12 110.95 123.47 88 ASP 88 1.324 1.224 1.523 1.536 1.468 122.94 115.62 121.47 110.57 110.39 109.76 122.91 89 ALA 89 1.307 1.231 1.533 1.522 1.447 122.53 115.93 120.90 110.60 110.81 109.66 123.17 +* +* 90 VAL 90 1.321 1.232 1.550 1.571 1.464 123.03 116.93 120.59 111.04 112.40 111.03 122.46 * * * 91 GLU 91 1.318 1.237 1.528 1.527 1.472 121.98 115.83 120.92 109.04 111.56 109.77 123.21 92 GLY 92 1.329 1.227 1.520 - 1.469 123.03 116.68 120.34 - 114.70 - 122.98 * * * 93 ASN 93 1.322 1.233 1.523 1.537 1.468 122.50 116.70 120.80 109.15 111.52 111.08 122.49 94 GLU 94 1.316 1.229 1.531 1.534 1.455 121.35 116.18 121.07 112.41 112.39 109.32 122.73 * * 95 TYR 95 1.316 1.234 1.508 1.527 1.454 122.56 115.76 120.74 109.07 110.90 111.84 123.49 96 GLU 96 1.310 1.246 1.521 1.535 1.436 122.15 116.72 120.13 110.76 108.61 110.41 123.15 * * * 97 ARG 97 1.321 1.231 1.512 1.538 1.441 121.39 116.04 121.17 110.58 108.87 110.59 122.79 98 VAL 98 1.300 1.232 1.502 1.543 1.436 121.68 115.87 120.82 110.06 111.43 112.86 123.29 ** * * ** 99 THR 99 1.296 1.234 1.523 1.570 1.437 121.31 116.39 120.82 111.79 109.17 112.27 122.73 ** * * * ** 100 VAL 100 1.308 1.235 1.514 1.555 1.446 122.40 116.04 120.62 108.59 110.69 111.88 123.33 * * 101 GLY 101 1.304 1.225 1.503 - 1.430 121.43 116.43 120.38 - 110.74 - 123.19 +* * +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 102 ILE 102 1.305 1.218 1.512 1.580 1.442 122.35 116.87 120.56 112.46 110.70 112.73 122.55 +* * +* +* 103 VAL 103 1.292 1.226 1.514 1.561 1.438 121.56 115.51 120.50 110.37 110.12 111.39 123.96 +** * +** 104 ARG 104 1.318 1.236 1.508 1.547 1.456 123.71 116.88 119.99 107.12 109.33 110.18 123.12 * +* +* 105 GLU 105 1.319 1.226 1.514 1.510 1.452 120.90 114.52 121.98 110.84 109.89 111.93 123.49 106 ASP 106 1.297 1.229 1.506 1.538 1.434 123.23 115.56 121.33 107.43 106.77 110.85 123.04 ** * * +* ** 107 ASN 107 1.340 1.229 1.533 1.566 1.441 121.02 114.61 121.53 108.58 108.69 111.52 123.85 +* +* 108 SER 108 1.312 1.232 1.539 1.553 1.443 126.36 114.82 121.70 110.22 106.30 110.76 123.45 * * +** +* +** 109 GLU 109 1.348 1.215 1.509 1.531 1.457 123.00 116.37 120.55 108.20 110.48 110.70 123.06 * * * 110 LYS 110 1.291 1.231 1.524 1.557 1.453 121.65 116.64 120.27 109.82 108.90 112.70 123.08 +** * * +** 111 MET 111 1.295 1.223 1.481 1.515 1.454 123.62 115.25 120.97 107.17 110.32 111.62 123.78 ** ** * +* ** 112 ALA 112 1.274 1.228 1.506 1.515 1.441 121.88 116.51 120.68 110.50 109.38 111.31 122.81 +*** +*** 113 VAL 113 1.301 1.239 1.517 1.562 1.450 121.49 116.57 120.59 108.59 110.04 112.41 122.83 +* +* 114 LYS 114 1.308 1.223 1.504 1.553 1.444 121.03 116.31 120.72 108.67 109.19 113.43 122.95 +* * +* +* 115 THR 115 1.281 1.248 1.509 1.564 1.421 122.22 116.85 120.05 110.65 106.48 112.75 123.09 *** +* +* *** 116 TYR 116 1.283 1.230 1.499 1.523 1.414 121.22 114.99 121.45 113.80 108.96 110.91 123.55 *** * ** +* *** 117 MET 117 1.293 1.241 1.500 1.538 1.432 122.45 115.45 120.69 110.67 110.21 109.09 123.85 +** * * +** 118 TRP 118 1.313 1.249 1.513 1.524 1.425 122.42 114.81 121.54 113.11 107.88 109.37 123.61 * +* +* * +* 119 ILE 119 1.290 1.234 1.527 1.540 1.427 122.92 116.75 120.17 111.04 111.62 109.72 123.02 +** +* * +** 120 ASN 120 1.314 1.206 1.530 1.533 1.462 121.50 116.84 121.16 110.61 109.94 110.34 121.99 * * * 121 LYS 121 1.306 1.234 1.523 1.520 1.461 121.60 116.61 120.79 110.39 112.34 110.36 122.58 +* +* 122 ALA 122 1.299 1.227 1.506 1.525 1.435 121.21 116.58 120.56 111.08 108.58 111.46 122.82 ** * ** 123 ASP 123 1.309 1.236 1.523 1.531 1.453 120.95 117.75 120.50 109.91 110.76 110.04 121.74 * * 124 PRO 124 1.339 1.232 1.541 1.526 1.456 122.51 117.74 120.02 110.14 113.78 102.34 122.22 125 ASP 125 1.331 1.231 1.492 1.540 1.466 121.04 116.09 120.91 109.02 111.02 113.08 122.99 +* +* +* 126 MET 126 1.312 1.215 1.523 1.527 1.450 120.81 116.65 120.16 109.88 111.51 110.05 123.19 * * 127 PHE 127 1.333 1.238 1.539 1.541 1.459 122.40 114.61 121.61 111.23 112.91 111.27 123.77 128 GLY 128 1.308 1.236 1.493 - 1.435 123.88 117.86 119.09 - 108.03 - 123.02 * * * +* +* +* 129 GLU 129 1.309 1.238 1.508 1.562 1.441 120.82 115.93 120.98 111.52 110.27 113.42 123.07 * +* +* +* 130 TRP 130 1.302 1.239 1.537 1.534 1.421 121.42 116.38 120.13 111.92 110.06 109.89 123.49 +* +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 131 ASN 131 1.345 1.226 1.506 1.548 1.480 123.97 114.97 121.30 106.41 110.08 111.96 123.73 * * * +* +* 132 PHE 132 1.321 1.202 1.502 1.521 1.446 122.96 117.91 119.28 112.05 113.42 112.37 122.80 * * * * * 133 GLU 133 1.327 1.239 1.514 1.517 1.462 120.95 115.36 120.98 108.41 109.85 112.09 123.66 134 GLU 134 1.325 1.223 1.525 1.531 1.450 122.15 115.90 121.35 109.91 108.94 110.05 122.73 135 TRP 135 1.322 1.197 1.526 1.541 1.438 121.25 116.98 119.98 111.92 111.16 111.90 123.00 +* * +* 136 LYS 136 1.324 1.238 1.536 1.535 1.480 124.05 114.96 121.38 111.26 110.39 108.21 123.62 * * * * 137 ARG 137 1.310 1.234 1.533 1.511 1.445 123.83 116.63 120.84 110.12 111.31 107.54 122.52 * * +* +* 138 LEU 138 1.321 1.226 1.517 1.545 1.465 121.51 115.18 121.51 110.47 110.64 112.24 123.30 * * 139 HIS 139 1.313 1.224 1.513 1.548 1.457 123.37 115.56 120.69 111.82 109.25 110.00 123.74 * * 140 LYS 140 1.331 1.224 1.513 1.534 1.450 122.50 115.62 120.73 109.46 109.56 110.39 123.60 141 LYS 141 1.335 1.216 1.522 1.535 1.455 122.99 116.52 120.74 111.06 111.44 111.26 122.72 142 LYS 142 1.321 1.236 1.532 1.533 1.453 121.45 115.85 120.76 111.07 110.38 111.01 123.39 143 PHE 143 1.332 1.222 1.509 1.535 1.460 122.52 115.25 121.43 108.26 109.03 111.36 123.32 144 ILE 144 1.318 1.194 1.528 1.565 1.449 122.67 117.34 119.87 111.29 110.99 112.17 122.77 +* +* 145 GLU 145 1.330 1.235 1.538 1.525 1.479 123.01 117.70 120.04 109.96 113.26 110.60 122.23 * * 146 THR 146 1.330 1.225 1.538 1.566 1.449 119.72 116.14 120.84 111.02 109.48 113.13 123.02 * * 147 PHE 147 1.330 1.204 1.479 1.520 1.450 122.20 116.17 119.88 110.08 112.19 113.27 123.95 * ** +* ** 148 LYS 148 1.320 1.237 1.508 1.529 1.443 122.93 117.30 120.38 111.00 112.16 111.26 122.33 149 LYS 149 1.332 1.205 1.533 1.541 1.438 118.18 115.96 120.34 111.09 109.74 114.19 123.57 * * +* ** ** 150 ILE 150 1.339 1.248 1.550 1.591 1.476 124.84 116.95 120.59 113.35 112.89 112.09 122.44 * +* +* +* +* 151 MET 151 1.343 1.235 1.539 1.550 1.480 122.01 117.39 119.81 109.00 112.47 113.69 122.80 * +* +* 152 GLU 152 1.344 1.227 1.530 1.547 1.476 122.31 115.70 121.12 109.97 110.92 111.27 123.17 * * 153 CYS 153 1.322 1.230 1.516 1.537 1.446 122.95 115.16 121.48 110.28 109.70 109.53 123.33 154 LYS 154 1.311 1.233 1.518 1.529 1.437 122.07 117.11 120.03 110.27 111.32 110.16 122.86 * * * 155 LYS 155 1.336 1.240 1.526 1.547 1.462 120.80 116.98 120.71 108.94 112.46 110.03 122.31 156 LYS 156 1.309 1.226 1.522 1.528 1.446 120.38 117.60 120.08 110.48 111.48 107.68 122.31 * +* +* 157 PRO 157 1.345 1.238 1.524 1.541 1.468 122.76 116.86 120.61 110.00 111.04 103.85 122.53 158 GLN 158 1.313 1.240 1.525 1.544 1.451 121.16 116.19 120.63 109.82 111.05 111.23 123.17 * * 159 GLY 159 1.311 1.238 1.499 - 1.441 121.02 115.50 120.87 - 113.02 - 123.62 * * 160 GLN 160 1.301 1.233 1.515 1.532 1.439 123.17 116.48 120.37 110.57 109.39 109.45 123.14 ** * ** 161 GLY 161 1.308 1.234 1.497 - 1.434 120.98 116.67 120.05 - 110.96 - 123.28 +* * * +* 162 ASN 162 1.303 1.236 1.515 1.541 1.454 122.07 116.53 120.36 110.47 110.06 110.56 123.11 +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 163 ASP 163 1.312 1.235 1.518 1.566 1.452 121.22 116.10 121.15 110.70 111.36 112.96 122.71 * +* * +* 164 ASP 164 1.311 1.237 1.494 1.543 1.451 121.94 114.79 121.44 111.28 108.95 113.30 123.60 * * +* +* 165 ILE 165 1.307 1.245 1.527 1.577 1.433 122.51 116.71 120.10 110.22 108.39 110.37 123.16 +* * * * +* 166 SER 166 1.311 1.242 1.542 1.551 1.443 122.55 116.81 120.66 110.99 108.99 109.34 122.52 * * * 167 HIS 167 1.315 1.232 1.519 1.540 1.449 121.21 116.84 120.43 110.36 109.90 112.09 122.73 * * 168 VAL 168 1.297 1.237 1.507 1.547 1.446 121.68 116.01 120.71 109.76 110.68 111.76 123.29 ** ** 169 LEU 169 1.299 1.234 1.517 1.562 1.426 121.39 116.11 120.91 112.03 107.73 109.64 122.94 ** +* +* * * ** 170 ARG 170 1.289 1.229 1.509 1.545 1.432 122.49 117.23 120.21 111.29 105.34 109.39 122.53 +** * ** +** 171 GLU 171 1.302 1.235 1.516 1.525 1.433 120.05 115.08 121.39 111.49 112.09 112.22 123.44 +* * * +* 172 ASP 172 1.294 1.235 1.504 1.550 1.443 123.64 117.69 119.59 111.22 107.28 112.66 122.69 +** * * * +** 173 GLN 173 1.296 - 1.530 1.531 1.438 120.82 - - 111.90 111.24 110.65 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +* ** ** +** +** +* * +* ** +** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 1.274 1.348 1.312 .015 +*** * * C-N (Pro) 1.341 .016 7 1.337 1.368 1.346 .010 +* C-O C-O 1.231 .020 172 1.194 1.252 1.231 .010 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.479 1.552 1.520 .014 ** * CH2G*-C (Gly) 1.516 .018 12 1.480 1.520 1.500 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.508 1.525 1.518 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.531 1.591 1.559 .014 +* CH1E-CH2E (the rest) 1.530 .020 128 1.499 1.571 1.537 .013 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.408 1.482 1.447 .014 +** * NH1-CH2G* (Gly) 1.451 .016 12 1.418 1.469 1.438 .013 ** * N-CH1E (Pro) 1.466 .015 7 1.447 1.480 1.465 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 2.0 153 113.56 119.37 116.25 .93 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.30 117.86 116.27 .91 CH1E-C-N (Pro) 116.9 1.5 7 115.90 117.74 116.73 .62 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.31 124.14 123.03 .54 * O-C-N (Pro) 122.0 1.4 7 121.87 123.32 122.70 .49 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 118.18 126.36 122.07 1.18 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.57 123.88 121.23 1.19 +* C-N-CH1E (Pro) 122.6 5.0 7 122.01 124.23 122.75 .69 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.92 122.47 120.71 .59 * CH2G*-C-O (Gly) 120.8 2.1 12 119.09 121.54 120.45 .58 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.50 111.08 110.68 .24 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.76 113.35 110.31 1.40 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 106.41 113.89 110.57 1.43 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 105.34 114.42 110.23 1.63 ** * NH1-CH2G*-C (Gly) 112.5 2.9 12 108.03 114.70 111.67 1.79 +* N-CH1E-C (Pro) 111.8 2.5 7 110.85 113.78 112.23 1.10 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.66 111.46 110.75 .71 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.97 113.81 111.73 1.12 * * N-CH1E-CH2E (Pro) 103.0 1.1 7 102.34 103.92 103.49 .54 NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.31 115.37 110.94 1.56 +* +** ------------------------------------------------------------------------------------------------------------- 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_1 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] 128 83.7% Residues in additional allowed regions [a,b,l,p] 21 13.7% Residues in generously allowed regions [~a,~b,~l,~p] 4 2.6% Residues in disallowed regions [XX] 0 .0% ---- ------ 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 83.7 83.8 10.0 .0 Inside b. Omega angle st dev 172 3.5 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 161 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 92 .9 .8 .2 .6 Inside f. Overall G-factor 173 .0 -.4 .3 1.2 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 29 7.5 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 58 9.4 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 63 7.4 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 150 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 41 4.9 20.4 5.0 -3.1 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 83.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_1 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.54 Chi1-chi2 distribution -.33 Chi1 only -.11 Chi3 & chi4 .37 Omega -.03 ------ -.20 ===== Main-chain covalent forces:- Main-chain bond lengths .04 Main-chain bond angles .43 ------ .26 ===== OVERALL AVERAGE -.04 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.