Residue-by-residue listing for refined_4 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.6 - - - 2 HIS 2 l - - -65.5 - - - - - - - 178.3 - 30.7 - 3 HIS 3 B 59.8 - - - - - - - - - 186.8 - 33.0 - * * 4 HIS 4 B - 189.0 - - - - - - - - 175.6 - 34.4 - 5 HIS 5 B - - -71.7 - - - - - - - 183.6 - 33.5 - 6 HIS 6 B 63.8 - - - - - - - - - 178.2 - 33.6 - 7 HIS 7 B 60.0 - - - - - - - - - 179.7 - 32.9 - 8 LEU 8 B 57.9 - - 169.8 - - - - - - 178.3 - 30.7 - 9 GLU 9 B - 186.5 - - - - - - - - 182.7 - 35.6 - 10 CYS 10 B 54.0 - - - - - - - - - 175.8 -.5 31.9 - ** ** 11 SER 11 a 54.5 - - - - - - - - - 183.6 -.6 35.1 - +* +* 12 SER 12 A 48.3 - - - - - - - - - 177.2 - 33.9 - * * 13 ASP 13 S b - - -64.0 - - - - - - - 179.1 - 34.2 - 14 SER 14 B - 186.4 - - - - - - - - 179.0 - 34.2 - 15 LEU 15 B - - -69.5 - - - - - - - 178.9 -1.0 34.4 - * * 16 GLN 16 S p - - -54.9 180.1 - - - - - - 176.3 - 34.2 - 17 LEU 17 S B - - -61.4 177.1 - - - - - - 189.4 - 33.1 - +* +* 18 HIS 18 E B - - -46.7 - - - - - - - 177.4 -3.3 35.9 - * +* +* 19 ASN 19 E B 49.7 - - - - - - - - - 186.0 - 30.3 - * * * 20 VAL 20 E B - 180.1 - - - - - - - - 177.5 -2.2 35.1 - Residue-by-residue listing for refined_4 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 21 PHE 21 E B - 177.6 - - - - - - - - 180.9 -2.8 35.5 - * * 22 VAL 22 E B - - -64.3 - - - - - - - 191.3 -2.8 31.0 - +* * +* 23 TYR 23 A 64.1 - - - - - - - - - 180.9 - 34.6 - 24 GLY 24 t - - - - - - - - - - - 182.0 - - - 25 SER 25 T A 52.6 - - - - - - - - - 178.9 - 35.2 - 26 PHE 26 T a - - -59.6 - - - - - - - 182.7 - 34.6 - 27 GLN 27 t a - 182.7 - 174.3 - - - - - - 178.6 -1.7 33.6 - 28 ASP 28 h B - 180.7 - - - - - - - - 183.2 - 34.8 - 29 PRO 29 H - - - - - -61.5 -61.5 -31.2 - - - 181.8 - 38.0 - * * 30 ASP 30 H A - 178.9 - - - -68.0 -37.9 - - - 177.5 - 34.3 - 31 VAL 31 H A - 180.5 - - - -64.6 -38.9 - - - 176.7 - 34.1 - 32 ILE 32 H A - - -81.6 - - -62.6 -50.5 - - - 186.2 -1.5 36.3 - * * 33 ASN 33 H A - 197.5 - - - -54.0 -43.6 - - - 179.8 -3.0 36.6 - * * 34 VAL 34 H A - 182.4 - - - -81.8 -32.4 - - - 186.2 -1.9 33.8 - * * * 35 MET 35 H A - 199.0 - - - -70.6 -37.5 - - - 179.3 -1.9 34.9 - 36 LEU 36 h a 47.4 - - 160.9 - - - - - - 184.8 -2.4 28.0 - * +* +* 37 ASP 37 S ~b - 178.4 - - - - - - - - 181.6 - 35.0 - ** ** 38 ARG 38 B - - -55.7 180.2 - - - - - - 170.4 - 36.9 - +* +* 39 THR 39 B - - -45.6 - - - - - - - 179.2 - 35.2 - * * 40 PRO 40 - - - - - -58.7 - - - - - 185.6 - 37.3 - 41 GLU 41 E B - 183.7 - 176.9 - - - - - - 186.4 -1.1 33.7 - * * * 42 ILE 42 E B - - -47.6 177.4 - - - - - - 172.9 - 36.6 - * * * 43 VAL 43 E B 62.6 - - - - - - - - - 178.4 -2.5 33.7 - 44 SER 44 E B - - -57.5 - - - - - - - 182.5 - 35.3 - 45 ALA 45 E B - - - - - - - - - - 179.4 -1.9 34.4 - 46 THR 46 E B - - -59.3 - - - - - - - 176.5 -2.7 35.1 - 47 LEU 47 E B - 175.9 - - - - - - - - 179.4 -3.4 34.3 - +* +* 48 PRO 48 E - - - - - -86.0 - - - - - 179.5 - 38.7 - +* * +* 49 GLY 49 E - - - - - - - - - - - 181.1 -2.9 - - * * 50 PHE 50 E B - - -67.6 - - - - - - - 183.0 -.7 34.3 - +* +* 51 GLN 51 E B - 186.1 - - - - - - - - 182.1 -2.7 35.0 - 52 ARG 52 E B 58.8 - - 180.2 - - - - - - 174.7 - 34.1 - 53 PHE 53 e B - - -72.8 - - - - - - - 183.4 -2.9 33.3 - * * 54 ARG 54 B B - - -93.8 - - - - - - - 177.0 -1.9 32.7 - +* +* 55 LEU 55 S b - 192.7 - 172.9 - - - - - - 180.0 - 33.3 - 56 LYS 56 S A - 187.6 - - - - - - - - 175.8 -1.9 34.0 - 57 GLY 57 S - - - - - - - - - - - 176.8 -.5 - - ** ** Residue-by-residue listing for refined_4 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 58 ARG 58 S A 53.9 - - - - - - - - - 182.8 -.8 30.1 - +* * +* 59 LEU 59 S B - 185.5 - - - - - - - - 186.2 -.7 33.3 - * +* +* 60 TYR 60 B - - -49.7 - - - - - - - 173.9 - 37.2 - * * * 61 PRO 61 S - - - - - -73.5 - - - - - 184.6 - 37.6 - * * 62 CYS 62 e b 60.4 - - - - - - - - - 178.2 -1.8 35.2 - 63 ILE 63 E B - - -60.6 - - - - - - - 176.0 - 36.6 - 64 VAL 64 E B - - -60.9 - - - - - - - 176.3 -1.7 34.8 - 65 PRO 65 E - - - - - -61.0 - - - - - 180.6 - 37.9 - * * 66 SER 66 E B - 186.9 - - - - - - - - 174.4 -1.9 34.7 - 67 GLU 67 E A - - -61.5 178.0 - - - - - - 179.2 - 34.7 - 68 LYS 68 E b - - -69.3 - - - - - - - 176.7 - 31.8 - 69 GLY 69 E - - - - - - - - - - - 175.2 - - - 70 GLU 70 E B 55.5 - - - - - - - - - 184.8 - 31.3 - 71 VAL 71 E B - 183.9 - - - - - - - - 176.7 -3.0 35.3 - * * 72 HIS 72 E B - - -65.4 - - - - - - - 183.1 -.6 33.7 - +* +* 73 GLY 73 E - - - - - - - - - - - 184.0 -3.1 - - * * 74 LYS 74 E B - - -58.2 - - - - - - - 173.7 -.7 35.7 - * +* +* 75 VAL 75 E B - 168.2 - - - - - - - - 178.2 -3.3 33.9 - +* +* 76 LEU 76 E B - - -67.7 - - - - - - - 183.1 -3.2 31.8 - * * 77 MET 77 E B - - -55.1 174.8 - - - - - - 178.8 -3.6 37.5 - ** * ** 78 GLY 78 E - - - - - - - - - - - 179.3 -1.3 - - 79 VAL 79 E B - 180.6 - - - - - - - - 176.6 -2.6 36.0 - 80 THR 80 h B 57.2 - - - - - - - - - 180.1 - 33.6 - 81 SER 81 H A - 183.0 - - - -55.3 -45.5 - - - 183.2 - 33.8 - 82 ASP 82 H A - - -62.9 - - -58.3 -42.2 - - - 179.5 - 33.1 - 83 GLU 83 H A - - -57.4 167.8 - -73.3 -40.6 - - - 175.5 - 35.6 - 84 LEU 84 H A - 181.5 - - - -55.9 -50.8 - - - 179.7 -2.7 35.7 - * * 85 GLU 85 H A - - -59.7 177.8 - -64.7 -29.2 - - - 176.8 -3.2 33.8 - +* +* 86 ASN 86 H A - 137.2 - - - -71.3 -44.6 - - - 176.1 -1.2 32.2 - +** * +** 87 LEU 87 H A - - -61.0 175.9 - -62.6 -40.9 - - - 177.8 -2.9 35.0 - * * 88 ASP 88 H A - 178.7 - - - -66.4 -29.3 - - - 178.7 -2.5 34.7 - 89 ALA 89 H A - - - - - -75.1 -45.3 - - - 182.0 -1.0 34.6 - * * 90 VAL 90 H A - 172.6 - - - -72.2 -58.3 - - - 181.9 -2.7 33.4 - +* +* 91 GLU 91 h A - - -61.0 - - - - - - - 183.7 -2.8 32.6 - 92 GLY 92 T - - - - - - - - - - - 180.9 -.7 - - +* +* 93 ASN 93 T A - 181.1 - - - - - - - - 176.5 -.7 31.6 - +* +* 94 GLU 94 e A - - -63.3 180.5 - - - - - - 180.9 -1.5 32.5 - Residue-by-residue listing for refined_4 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 95 TYR 95 E B - - -65.3 - - - - - - - 176.0 -1.6 34.9 - 96 GLU 96 E B 61.7 - - 179.5 - - - - - - 181.6 -1.3 32.2 - 97 ARG 97 E B - 188.7 - 187.3 - - - - - - 178.0 - 36.4 - 98 VAL 98 E B - - -69.9 - - - - - - - 182.9 -2.9 30.8 - * * 99 THR 99 E B - 191.1 - - - - - - - - 186.4 - 32.0 - * * 100 VAL 100 E B - - -63.5 - - - - - - - 177.7 -3.3 34.7 - +* +* 101 GLY 101 E - - - - - - - - - - - 181.3 - - - 102 ILE 102 E B 54.3 - - - - - - - - - 181.3 -2.6 32.2 - 103 VAL 103 E B - 177.8 - - - - - - - - 182.5 -2.8 33.5 - 104 ARG 104 E B - 179.7 - 176.9 - - - - - - 182.8 -3.5 35.1 - +* +* 105 GLU 105 e A - - -61.3 - - - - - - - 180.9 -2.5 34.9 - 106 ASP 106 T A - - -63.4 - - - - - - - 190.2 -.6 34.1 - +* +* +* 107 ASN 107 T a 63.2 - - - - - - - - - 175.8 - 33.5 - 108 SER 108 t l - 183.7 - - - - - - - - 178.2 -2.3 32.0 - 109 GLU 109 e B - - -69.8 - - - - - - - 181.2 - 33.1 - 110 LYS 110 E B 58.7 - - 179.4 - - - - - - 178.5 - 34.1 - 111 MET 111 E B - - -67.5 171.5 - - - - - - 180.4 -3.2 34.4 - +* +* 112 ALA 112 E B - - - - - - - - - - 183.3 - 34.2 - 113 VAL 113 E B - - -57.2 - - - - - - - 176.0 -2.3 34.8 - 114 LYS 114 E B - - -70.8 - - - - - - - 179.0 -2.4 33.3 - 115 THR 115 E B - 191.8 - - - - - - - - 183.8 -2.6 33.0 - 116 TYR 116 E B - - -61.0 - - - - - - - 179.3 - 33.7 - 117 MET 117 E B 66.0 - - 176.8 - - - - - - 179.9 -1.1 33.6 - * * 118 TRP 118 E B - 185.4 - - - - - - - - 189.4 -3.3 34.5 - +* +* +* 119 ILE 119 e A - - -48.6 - - - - - - - 188.7 -.6 36.0 - * +* +* +* 120 ASN 120 A - 177.3 - - - - - - - - 179.6 - 30.5 - 121 LYS 121 ~l 43.4 - - - - - - - - - 176.9 - 25.0 - ** * +** +** 122 ALA 122 A - - - - - - - - - - 184.2 - 34.4 - 123 ASP 123 t B - - -56.3 - - - - - - - 178.7 - 35.5 - 124 PRO 124 T - - - - - -83.8 - - - - - 183.8 - 39.3 - +* +* +* 125 ASP 125 T A 55.2 - - - - - - - - - 175.2 - 33.3 - 126 MET 126 t B 58.3 - - 181.3 - - - - - - 182.5 -.6 33.7 - +* +* 127 PHE 127 B B - - -58.1 - - - - - - - 178.7 -.8 34.2 - +* +* 128 GLY 128 - - - - - - - - - - - 183.3 - - - 129 GLU 129 B - - -60.0 185.9 - - - - - - 176.7 -1.7 32.3 - 130 TRP 130 h B - 197.5 - - - - - - - - 181.6 -.5 36.7 - ** ** 131 ASN 131 H A - 182.3 - - - -51.2 -44.6 - - - 177.7 - 32.5 - * * 132 PHE 132 H A - - -59.8 - - -74.0 -39.0 - - - 178.5 - 32.9 - 133 GLU 133 H A - - -65.3 - - -64.2 -28.3 - - - 176.7 - 33.9 - 134 GLU 134 H A - 179.9 - 180.2 - -63.4 -37.7 - - - 177.4 -2.6 34.1 - 135 TRP 135 H A - 185.2 - - - -74.4 -33.8 - - - 174.4 -.8 32.0 - +* +* Residue-by-residue listing for refined_4 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 136 LYS 136 H A - 180.5 - 189.7 - -57.2 -45.1 - - - 175.3 -1.8 36.3 - 137 ARG 137 H A - 160.9 - 177.7 - -53.5 -51.2 - - - 185.0 -2.7 35.6 - * * * 138 LEU 138 H A - - -58.0 174.1 - -77.8 -26.0 - - - 172.4 -1.9 32.4 - * * * * 139 HIS 139 H A - 178.2 - - - -68.1 -39.7 - - - 176.6 -2.6 34.5 - 140 LYS 140 H A - 180.5 - 182.1 - -69.5 -37.1 - - - 182.2 -2.4 34.3 - 141 LYS 141 H A - 183.4 - - - -52.8 -31.7 - - - 178.1 -2.2 33.4 - * * 142 LYS 142 H A - 187.6 - - - -66.1 -40.3 - - - 182.6 -.8 35.0 - +* +* 143 PHE 143 H A - 199.1 - - - -76.3 -32.2 - - - 178.4 -.9 35.9 - * * 144 ILE 144 H A - - -61.1 - - -59.1 -32.0 - - - 178.6 -2.4 31.4 - 145 GLU 145 H A - - -59.2 186.1 - -52.0 -45.2 - - - 178.6 -1.1 33.0 - * * * 146 THR 146 H A - 188.2 - - - -79.2 -29.9 - - - 186.5 -.8 33.8 - * * +* +* 147 PHE 147 H A - 205.1 - - - -75.6 -30.3 - - - 178.4 -1.7 34.1 - * * 148 LYS 148 H A - 181.9 - - - -58.3 -36.9 - - - 178.0 -3.3 35.3 - +* +* 149 LYS 149 H A - - -63.9 178.6 - -74.4 -38.8 - - - 177.1 -.6 33.1 - +* +* 150 ILE 150 H A - - -59.5 177.1 - -63.6 -39.9 - - - 181.7 -1.4 35.7 - 151 MET 151 H A - 183.9 - 180.1 - -60.2 -31.6 - - - 178.4 -3.1 34.5 - * * 152 GLU 152 H A - - -58.4 - - -64.9 -37.0 - - - 178.7 -.8 35.2 - +* +* 153 CYS 153 H A - 180.3 - - - -71.8 -34.4 - - - 183.2 -.9 34.7 - +* +* 154 LYS 154 H A - - -55.5 - - -81.4 -44.9 - - - 184.5 -1.7 35.4 - * * 155 LYS 155 h b - 178.4 - - - - - - - - 180.7 -3.6 35.1 - ** ** 156 LYS 156 B - - -55.7 180.1 - - - - - - 178.2 - 34.6 - 157 PRO 157 S - - - - - -60.9 - - - - - 180.2 - 37.8 - * * 158 GLN 158 B - - -66.6 175.2 - - - - - - 179.0 -.9 35.0 - * * 159 GLY 159 t - - - - - - - - - - - 180.4 - - - 160 GLN 160 T b - 184.5 - 181.4 - - - - - - 175.8 - 32.2 - 161 GLY 161 T - - - - - - - - - - - 183.5 -2.0 - - 162 ASN 162 t B - - -68.8 - - - - - - - 180.1 -.5 35.0 - ** ** 163 ASP 163 B 59.4 - - - - - - - - - 176.8 - 32.4 - 164 ASP 164 B 62.6 - - - - - - - - - 181.4 - 35.0 - 165 ILE 165 b 55.9 - - 176.9 - - - - - - 178.3 - 30.4 - 166 SER 166 b - 187.8 - - - - - - - - 180.6 -1.0 35.1 - * * 167 HIS 167 B - - -66.0 - - - - - - - 180.5 - 31.8 - 168 VAL 168 B - 182.2 - - - - - - - - 177.2 - 35.7 - 169 LEU 169 b - - -58.9 178.7 - - - - - - 185.3 - 34.4 - 170 ARG 170 B - - -72.9 - - - - - - - 174.7 -.9 32.4 - +* +* 171 GLU 171 B 54.6 - - 180.7 - - - - - - 180.6 -.5 34.0 - ** ** Residue-by-residue listing for refined_4 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 172 ASP 172 B - 186.2 - - - - - - - - 181.9 - 32.0 - 173 GLN 173 - - 188.4 - - - - - - - - - -1.0 35.7 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * +** +* +* * +* +* ** +** +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.0 183.1 -62.2 178.0 -69.3 -66.0 -38.7 - - - 180.0 -1.9 34.1 Standard deviations: 5.4 9.4 7.8 5.2 11.7 8.6 7.2 - - - 3.6 1.0 1.9 Numbers of values: 29 59 62 39 7 41 41 0 0 0 172 100 161 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_4 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 - 1.231 1.502 - 1.456 - 116.36 119.82 - 110.41 - 123.81 2 HIS 2 1.329 1.234 1.521 1.542 1.469 124.24 115.37 121.46 110.86 113.35 113.63 123.17 * +* +* 3 HIS 3 1.303 1.238 1.530 1.564 1.456 123.07 117.61 120.05 112.08 108.41 111.37 122.34 +* +* * +* 4 HIS 4 1.321 1.233 1.536 1.546 1.454 119.99 115.65 121.28 110.55 111.98 109.60 123.07 5 HIS 5 1.308 1.231 1.508 1.547 1.459 123.69 116.38 120.57 109.86 108.37 112.82 123.05 +* * * * +* 6 HIS 6 1.305 1.223 1.525 1.552 1.456 121.83 116.72 120.49 110.46 111.02 111.21 122.79 +* * +* 7 HIS 7 1.316 1.226 1.514 1.559 1.456 121.82 116.80 120.29 111.20 109.77 112.06 122.90 * * 8 LEU 8 1.302 1.236 1.517 1.567 1.440 121.18 114.87 121.31 111.93 111.46 113.74 123.77 +* +* +* +* 9 GLU 9 1.311 1.248 1.536 1.555 1.446 123.69 116.95 120.40 112.55 107.49 107.33 122.63 * * * * * +* +* 10 CYS 10 1.312 1.228 1.533 1.534 1.441 121.24 115.18 121.67 112.13 113.45 110.74 123.11 * * * 11 SER 11 1.306 1.235 1.524 1.531 1.446 123.72 114.66 121.76 110.70 108.07 109.46 123.54 +* * * +* 12 SER 12 1.324 1.237 1.531 1.526 1.441 123.72 116.42 120.67 112.08 112.55 108.40 122.91 * * * * Residue-by-residue listing for refined_4 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 1.318 1.236 1.508 1.539 1.457 121.59 116.78 120.52 109.22 109.17 112.13 122.70 14 SER 14 1.300 1.228 1.534 1.548 1.423 121.24 116.39 120.95 111.71 108.85 109.91 122.55 ** +* ** 15 LEU 15 1.318 1.250 1.507 1.507 1.417 122.41 115.72 120.11 109.39 111.16 110.96 124.16 * ** ** 16 GLN 16 1.344 1.238 1.523 1.543 1.479 124.18 117.01 120.69 109.62 109.73 111.31 122.30 * * * * 17 LEU 17 1.305 1.238 1.506 1.520 1.434 120.26 116.35 120.96 111.06 108.05 112.14 122.68 +* * * +* 18 HIS 18 1.285 1.238 1.490 1.540 1.431 121.03 115.36 120.90 108.56 109.84 110.37 123.74 *** +* * *** 19 ASN 19 1.288 1.240 1.517 1.546 1.422 122.47 115.47 121.34 114.29 110.57 112.24 123.11 +** +* ** * +** 20 VAL 20 1.308 1.232 1.521 1.575 1.448 122.41 116.01 120.53 109.43 110.21 110.73 123.45 +* * +* 21 PHE 21 1.307 1.243 1.518 1.544 1.443 122.66 116.39 120.48 110.89 108.48 108.85 123.13 +* +* 22 VAL 22 1.313 1.233 1.508 1.543 1.447 121.43 115.76 121.05 112.04 110.78 113.30 123.18 * * * * 23 TYR 23 1.309 1.241 1.536 1.522 1.439 120.61 117.74 120.03 110.59 114.92 108.13 122.22 * * * * * 24 GLY 24 1.313 1.228 1.505 - 1.454 119.35 116.13 120.57 - 112.56 - 123.23 * * 25 SER 25 1.309 1.224 1.530 1.524 1.455 123.29 116.05 121.23 110.53 111.71 108.26 122.71 * * * 26 PHE 26 1.309 1.214 1.520 1.527 1.442 121.69 116.42 120.80 110.06 110.55 110.21 122.65 * * 27 GLN 27 1.329 1.239 1.561 1.545 1.469 122.84 115.25 122.02 113.23 110.88 108.13 122.68 +* +* * +* 28 ASP 28 1.310 1.242 1.530 1.529 1.445 123.54 118.09 119.98 110.11 108.29 110.46 121.92 * * * * 29 PRO 29 1.346 1.225 1.525 1.520 1.465 122.82 117.40 120.07 109.67 114.47 104.49 122.52 * * * 30 ASP 30 1.324 1.235 1.515 1.526 1.468 121.14 115.16 121.33 110.06 109.68 110.70 123.48 31 VAL 31 1.318 1.239 1.532 1.550 1.453 122.03 115.88 120.74 109.97 109.41 111.48 123.35 32 ILE 32 1.335 1.229 1.509 1.566 1.454 123.01 113.32 122.11 109.62 109.86 108.87 124.49 * +* +* 33 ASN 33 1.276 1.237 1.531 1.503 1.425 125.77 115.92 121.13 111.94 111.61 104.94 122.93 +*** * +* ** *** +*** 34 VAL 34 1.306 1.234 1.547 1.557 1.447 121.55 117.26 120.44 109.90 111.91 111.20 122.28 +* * +* 35 MET 35 1.333 1.229 1.536 1.543 1.459 121.03 117.48 120.57 110.65 110.74 109.13 121.87 36 LEU 36 1.317 1.231 1.513 1.568 1.450 119.66 117.17 119.56 112.60 113.58 115.38 123.23 +* * * +** +** 37 ASP 37 1.331 1.226 1.506 1.552 1.480 122.25 115.59 121.23 109.01 109.84 110.93 123.17 * * * 38 ARG 38 1.311 1.228 1.503 1.526 1.449 121.75 116.04 120.62 106.60 109.49 110.49 123.33 * * +* +* 39 THR 39 1.304 1.238 1.525 1.534 1.425 122.32 117.55 120.15 108.87 106.61 111.63 122.09 +* +* +* +* 40 PRO 40 1.336 1.236 1.534 1.529 1.466 122.81 116.05 120.32 111.70 111.75 104.07 123.62 * * 41 GLU 41 1.326 1.230 1.523 1.524 1.461 123.52 115.34 121.33 110.92 111.21 110.28 123.33 * * Residue-by-residue listing for refined_4 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 42 ILE 42 1.297 1.241 1.514 1.552 1.436 121.99 114.99 121.25 107.27 110.40 110.43 123.75 ** * ** 43 VAL 43 1.289 1.243 1.523 1.564 1.423 123.13 116.68 120.46 110.29 107.78 112.69 122.82 +** +* * +** 44 SER 44 1.288 1.245 1.526 1.508 1.421 121.58 116.55 120.70 111.33 108.99 108.20 122.73 +** * +* * +** 45 ALA 45 1.309 1.232 1.508 1.505 1.439 121.24 115.02 121.29 109.85 111.80 110.14 123.70 * * * 46 THR 46 1.292 1.225 1.522 1.541 1.426 123.07 116.05 120.60 109.66 110.11 110.24 123.33 +** +* +** 47 LEU 47 1.301 1.229 1.528 1.538 1.435 123.02 117.83 120.39 110.78 109.72 110.23 121.71 +* * +* 48 PRO 48 1.337 1.241 1.523 1.538 1.444 122.53 116.06 120.88 110.31 111.84 103.86 123.06 * * 49 GLY 49 1.315 1.234 1.504 - 1.437 121.04 115.89 120.90 - 111.25 - 123.21 * * 50 PHE 50 1.318 1.208 1.503 1.551 1.449 123.32 117.84 119.84 110.26 108.13 111.45 122.30 * * * * * 51 GLN 51 1.296 1.236 1.506 1.534 1.443 120.50 114.95 121.01 109.91 109.19 110.24 124.01 ** ** 52 ARG 52 1.309 1.235 1.516 1.543 1.430 122.85 115.13 121.44 110.58 111.92 110.24 123.43 * * * 53 PHE 53 1.296 1.206 1.500 1.538 1.431 122.74 117.93 119.75 112.12 107.18 111.30 122.16 ** * * * * * ** 54 ARG 54 1.300 1.240 1.493 1.536 1.468 121.90 115.96 120.60 109.92 111.89 112.52 123.44 ** +* * ** 55 LEU 55 1.325 1.235 1.522 1.561 1.433 121.08 114.39 121.77 112.67 106.99 111.09 123.50 +* * * +* +* 56 LYS 56 1.299 1.231 1.536 1.564 1.436 123.19 113.93 122.57 115.08 107.64 107.34 123.44 ** +* * * * +** * +* +** 57 GLY 57 1.315 1.231 1.504 - 1.435 123.10 118.03 119.44 - 108.04 - 122.51 * * +* +* 58 ARG 58 1.310 1.232 1.526 1.567 1.462 120.00 116.89 120.76 112.50 112.38 113.34 122.29 * +* * +* +* 59 LEU 59 1.313 1.229 1.526 1.549 1.441 120.42 115.32 120.61 111.10 110.18 111.36 124.06 * * 60 TYR 60 1.320 1.237 1.529 1.543 1.457 124.34 118.55 120.13 107.70 109.86 109.02 121.32 * * * * * 61 PRO 61 1.354 1.224 1.534 1.546 1.439 121.65 115.84 121.12 111.13 110.71 104.83 122.99 +* +* +* 62 CYS 62 1.304 1.253 1.548 1.527 1.435 122.90 115.52 121.11 110.78 112.10 107.99 123.36 +* * * * * +* 63 ILE 63 1.330 1.220 1.508 1.568 1.464 124.59 117.93 119.37 107.14 107.12 111.39 122.68 * +* * +* 64 VAL 64 1.302 1.242 1.530 1.573 1.459 121.52 118.25 119.49 108.38 108.45 112.43 122.22 +* * * +* 65 PRO 65 1.349 1.239 1.537 1.539 1.472 122.44 116.16 121.20 110.76 112.12 104.10 122.61 * * 66 SER 66 1.307 1.233 1.521 1.536 1.433 121.93 116.40 120.37 110.06 110.04 110.28 123.22 +* * +* 67 GLU 67 1.317 1.224 1.512 1.524 1.448 121.44 115.19 121.60 109.57 108.49 111.13 123.21 68 LYS 68 1.312 1.236 1.498 1.543 1.434 122.28 114.87 121.44 111.42 110.82 113.01 123.45 * * * * * 69 GLY 69 1.299 1.243 1.496 - 1.413 120.86 115.16 120.88 - 111.91 - 123.94 ** * ** ** Residue-by-residue listing for refined_4 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 70 GLU 70 1.295 1.237 1.518 1.558 1.426 124.38 116.62 120.60 112.58 108.48 113.51 122.76 ** * +* * * +* ** 71 VAL 71 1.304 1.216 1.511 1.557 1.445 121.91 116.57 120.71 108.52 110.56 111.11 122.71 +* +* 72 HIS 72 1.304 1.243 1.517 1.546 1.449 121.11 116.47 120.58 110.91 108.50 111.48 122.94 +* +* 73 GLY 73 1.311 1.238 1.505 - 1.434 120.56 116.47 120.69 - 112.39 - 122.83 * * * 74 LYS 74 1.311 1.235 1.516 1.535 1.445 121.44 115.89 120.72 108.16 111.00 110.46 123.38 * * * 75 VAL 75 1.306 1.221 1.504 1.541 1.437 122.83 115.57 120.79 109.53 110.40 112.02 123.64 +* * * +* 76 LEU 76 1.301 1.232 1.490 1.516 1.426 122.25 114.29 121.50 111.55 110.96 112.54 124.19 +* +* +* * +* 77 MET 77 1.287 1.222 1.509 1.499 1.424 124.39 116.37 120.62 108.29 110.44 107.64 123.01 *** +* +* * +* *** 78 GLY 78 1.298 1.230 1.501 - 1.442 120.20 115.87 120.80 - 111.97 - 123.33 ** ** 79 VAL 79 1.318 1.230 1.511 1.555 1.449 122.29 117.02 120.23 107.87 109.07 111.08 122.75 80 THR 80 1.290 1.245 1.528 1.543 1.428 120.50 117.49 119.88 110.97 108.39 111.59 122.62 +** +* * +** 81 SER 81 1.316 1.222 1.529 1.538 1.463 121.50 116.44 120.30 109.91 110.96 111.26 123.19 82 ASP 82 1.326 1.224 1.520 1.535 1.471 122.31 116.23 120.64 110.40 112.09 111.33 123.12 83 GLU 83 1.310 1.209 1.540 1.522 1.466 122.94 117.02 120.47 110.76 109.46 107.96 122.50 * * * * 84 LEU 84 1.338 1.232 1.529 1.535 1.477 122.21 115.11 121.28 107.84 109.92 110.72 123.61 * * 85 GLU 85 1.325 1.221 1.524 1.531 1.451 123.19 115.60 120.90 111.43 110.26 110.02 123.50 86 ASN 86 1.318 1.231 1.528 1.541 1.461 123.74 116.63 120.49 112.86 112.15 110.15 122.87 * * * 87 LEU 87 1.317 1.236 1.516 1.536 1.460 122.13 114.45 121.64 109.82 108.23 110.44 123.87 * * 88 ASP 88 1.321 1.213 1.525 1.530 1.451 123.51 116.45 121.10 110.37 110.84 109.55 122.44 * * 89 ALA 89 1.303 1.228 1.517 1.513 1.444 121.78 115.81 121.03 110.05 110.34 110.01 123.15 +* +* 90 VAL 90 1.317 1.238 1.552 1.569 1.446 122.09 117.10 120.40 111.41 112.24 110.22 122.45 * * * * 91 GLU 91 1.324 1.225 1.519 1.523 1.469 121.77 115.84 121.07 111.28 112.85 110.70 123.08 92 GLY 92 1.312 1.237 1.516 - 1.461 122.73 116.85 120.48 - 114.44 - 122.66 * * * 93 ASN 93 1.312 1.230 1.546 1.543 1.449 121.34 117.43 120.53 112.86 111.73 111.08 122.04 * * * * 94 GLU 94 1.332 1.235 1.542 1.544 1.476 120.99 116.29 120.87 111.02 112.06 111.47 122.83 95 TYR 95 1.322 1.228 1.517 1.537 1.469 123.18 116.82 120.52 108.58 110.35 111.26 122.65 96 GLU 96 1.314 1.242 1.501 1.538 1.441 120.86 115.88 120.77 111.29 109.54 112.90 123.32 * * * * 97 ARG 97 1.302 1.232 1.509 1.524 1.426 121.38 116.33 120.69 109.01 108.64 109.26 122.98 +* +* +* 98 VAL 98 1.292 1.236 1.476 1.530 1.434 121.37 115.61 120.76 110.47 111.77 114.80 123.63 +** ** * +* +** 99 THR 99 1.284 1.235 1.529 1.578 1.421 120.57 116.10 121.25 113.64 108.16 111.75 122.60 *** * +* ** * *** 100 VAL 100 1.298 1.243 1.518 1.555 1.444 122.00 115.71 120.94 109.10 111.26 111.03 123.35 ** ** Residue-by-residue listing for refined_4 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 101 GLY 101 1.300 1.235 1.506 - 1.423 121.24 116.28 120.75 - 111.04 - 122.96 ** +* ** 102 ILE 102 1.299 1.218 1.505 1.578 1.444 122.14 117.02 120.10 111.83 110.06 112.55 122.87 ** * * ** 103 VAL 103 1.292 1.227 1.509 1.547 1.435 121.72 115.19 120.92 110.90 109.52 111.58 123.87 +** * +** 104 ARG 104 1.302 1.234 1.528 1.526 1.435 123.81 115.81 120.67 111.28 110.69 108.13 123.51 +* * * * +* 105 GLU 105 1.327 1.234 1.530 1.539 1.478 123.70 116.25 120.84 109.49 111.87 109.75 122.91 * * * 106 ASP 106 1.323 1.226 1.513 1.538 1.462 121.66 116.62 120.81 107.80 112.31 112.56 122.53 * * * 107 ASN 107 1.309 1.235 1.522 1.546 1.468 120.64 116.15 120.42 110.92 113.14 109.96 123.44 * * 108 SER 108 1.325 1.231 1.544 1.561 1.469 124.04 117.10 120.72 112.14 112.31 111.11 122.15 +* * * +* 109 GLU 109 1.316 1.230 1.496 1.509 1.446 120.89 115.42 121.13 110.47 111.24 111.59 123.45 * * * 110 LYS 110 1.291 1.237 1.517 1.535 1.435 121.91 115.44 121.18 110.09 110.13 111.12 123.37 +** * +** 111 MET 111 1.285 1.233 1.480 1.523 1.450 123.52 115.53 120.80 109.08 109.54 111.80 123.67 *** ** * *** 112 ALA 112 1.274 1.234 1.502 1.508 1.439 121.24 116.11 120.49 110.14 109.63 110.77 123.39 +*** * +*** 113 VAL 113 1.307 1.232 1.514 1.562 1.442 121.49 116.04 120.97 108.39 110.16 112.11 122.98 +* +* 114 LYS 114 1.299 1.226 1.524 1.555 1.441 122.01 117.21 120.16 110.89 109.06 112.00 122.60 ** * ** 115 THR 115 1.306 1.246 1.531 1.561 1.443 121.50 116.65 120.24 110.74 109.04 112.64 123.11 +* +* 116 TYR 116 1.312 1.235 1.513 1.536 1.440 122.24 115.24 121.22 111.18 110.68 110.47 123.53 * * 117 MET 117 1.305 1.245 1.511 1.548 1.456 122.60 115.88 120.51 109.22 108.73 113.18 123.59 +* +* +* 118 TRP 118 1.302 1.227 1.533 1.522 1.432 122.64 116.42 120.51 111.65 109.17 109.04 123.07 +* * +* 119 ILE 119 1.319 1.234 1.534 1.548 1.465 121.92 116.97 121.00 106.53 113.53 110.91 122.03 * * 120 ASN 120 1.302 1.220 1.526 1.538 1.454 120.00 116.83 120.13 113.54 114.02 110.85 123.02 +* +* * +* 121 LYS 121 1.326 1.236 1.547 1.566 1.498 124.66 117.89 120.06 112.20 117.56 116.47 122.01 * +* ** +* * ** +*** +*** 122 ALA 122 1.307 1.233 1.521 1.526 1.460 121.58 114.58 121.59 110.54 109.01 110.24 123.83 +* +* 123 ASP 123 1.312 1.233 1.514 1.536 1.462 124.72 117.53 120.60 109.36 111.43 109.28 121.87 * +* +* 124 PRO 124 1.333 1.231 1.536 1.528 1.458 122.36 115.75 120.94 110.18 112.14 102.72 123.31 125 ASP 125 1.315 1.234 1.525 1.525 1.461 123.18 117.23 120.58 110.81 113.26 110.12 122.19 * * 126 MET 126 1.309 1.241 1.510 1.522 1.447 120.17 116.87 120.41 110.89 108.68 111.24 122.71 * * 127 PHE 127 1.304 1.243 1.502 1.540 1.439 120.95 116.09 120.86 110.18 110.07 111.10 123.05 +* * +* 128 GLY 128 1.311 1.236 1.499 - 1.444 121.27 116.09 120.87 - 111.31 - 123.04 * * Residue-by-residue listing for refined_4 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 129 GLU 129 1.314 1.224 1.496 1.538 1.421 121.18 113.21 121.97 110.91 111.16 112.66 124.76 * * +* * * * +* 130 TRP 130 1.270 1.228 1.512 1.531 1.418 126.17 120.36 117.21 111.77 101.98 107.50 122.43 **** ** ** ** ** *** +* **** 131 ASN 131 1.312 1.235 1.545 1.542 1.490 120.71 116.51 120.90 110.84 111.53 111.68 122.57 * +* +* 132 PHE 132 1.328 1.238 1.541 1.523 1.466 121.81 116.34 120.79 111.02 111.80 110.88 122.86 133 GLU 133 1.338 1.213 1.527 1.529 1.477 122.49 116.41 120.84 109.59 110.72 111.29 122.74 134 GLU 134 1.317 1.229 1.525 1.522 1.448 122.25 116.71 120.91 110.69 109.92 110.28 122.37 135 TRP 135 1.321 1.219 1.523 1.529 1.437 119.72 115.90 120.71 111.97 109.39 112.36 123.36 * * * * 136 LYS 136 1.333 1.235 1.533 1.528 1.470 122.88 114.44 121.59 109.29 108.14 108.76 123.96 * * * 137 ARG 137 1.325 1.224 1.522 1.542 1.448 124.73 116.09 120.88 109.64 112.04 108.90 123.02 +* +* 138 LEU 138 1.301 1.236 1.519 1.509 1.447 121.85 115.54 121.13 113.88 111.91 108.73 123.31 +* * +* * +* 139 HIS 139 1.309 1.238 1.526 1.553 1.465 122.21 115.65 121.20 110.49 108.31 110.72 123.15 * * * * 140 LYS 140 1.324 1.206 1.515 1.539 1.447 122.11 116.00 120.43 109.61 109.71 111.43 123.57 * * 141 LYS 141 1.331 1.233 1.538 1.541 1.470 124.03 117.10 120.38 110.99 112.25 110.30 122.51 * * 142 LYS 142 1.332 1.227 1.515 1.533 1.462 120.80 114.53 121.86 108.37 109.38 111.55 123.59 143 PHE 143 1.296 1.224 1.526 1.523 1.428 123.10 114.76 121.79 110.82 108.30 108.19 123.45 ** +* * * ** 144 ILE 144 1.317 1.201 1.526 1.569 1.444 123.52 118.12 119.56 111.96 111.80 112.67 122.32 +* * * * +* 145 GLU 145 1.336 1.235 1.547 1.523 1.473 120.89 117.26 120.52 109.36 111.81 112.33 122.20 * * * 146 THR 146 1.327 1.243 1.530 1.577 1.455 120.48 115.45 121.49 109.45 109.80 112.59 122.99 * * 147 PHE 147 1.318 1.208 1.518 1.521 1.434 122.18 115.66 120.95 111.09 110.54 109.89 123.39 * * * 148 LYS 148 1.310 1.224 1.531 1.546 1.454 124.63 116.19 120.84 111.21 109.85 108.22 122.96 * +* * +* 149 LYS 149 1.323 1.225 1.527 1.534 1.455 121.69 115.66 121.05 111.81 110.00 110.67 123.26 150 ILE 150 1.327 1.232 1.529 1.557 1.465 122.70 115.03 121.47 108.39 109.42 110.68 123.49 151 MET 151 1.320 1.209 1.524 1.527 1.431 124.28 117.00 120.07 110.74 111.48 109.37 122.91 * * * * 152 GLU 152 1.327 1.229 1.516 1.525 1.467 121.78 115.22 121.48 108.82 109.75 110.51 123.29 153 CYS 153 1.312 1.232 1.540 1.540 1.440 122.72 115.93 121.08 111.32 110.25 108.97 122.96 * * 154 LYS 154 1.328 1.230 1.529 1.540 1.463 122.24 116.22 120.67 108.54 111.87 110.12 123.11 155 LYS 155 1.306 1.237 1.512 1.551 1.439 123.08 115.72 120.88 110.64 108.79 109.71 123.35 +* * * +* 156 LYS 156 1.303 1.242 1.531 1.534 1.446 121.82 118.18 119.77 110.51 109.40 110.03 121.99 +* +* 157 PRO 157 1.350 1.249 1.532 1.536 1.463 122.50 115.01 121.53 110.92 112.01 104.20 123.35 * * * 158 GLN 158 1.308 1.233 1.511 1.544 1.438 123.98 116.68 120.14 109.75 108.51 110.69 123.16 +* * * +* 159 GLY 159 1.305 1.240 1.503 - 1.438 120.93 116.07 120.81 - 111.46 - 123.12 +* +* Residue-by-residue listing for refined_4 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 160 GLN 160 1.323 1.244 1.528 1.527 1.441 121.48 114.09 122.04 111.53 110.91 111.87 123.66 * * 161 GLY 161 1.294 1.231 1.495 - 1.437 123.24 114.25 121.65 - 108.50 - 124.11 +** * +* * * +** 162 ASN 162 1.320 1.242 1.499 1.553 1.444 124.39 116.76 120.06 109.13 108.06 111.70 123.18 * * * * * 163 ASP 163 1.298 1.246 1.508 1.549 1.439 121.48 114.66 121.73 111.21 111.18 112.21 123.57 ** * ** 164 ASP 164 1.299 1.243 1.515 1.539 1.443 122.82 117.25 119.81 110.32 108.25 110.12 122.94 ** * ** 165 ILE 165 1.316 1.234 1.530 1.559 1.452 121.04 114.91 122.22 111.49 112.71 113.79 122.83 * * * 166 SER 166 1.297 1.235 1.527 1.540 1.423 122.72 118.00 119.98 111.46 106.86 109.32 122.02 ** +* +* ** 167 HIS 167 1.301 1.248 1.507 1.535 1.441 120.43 115.16 121.07 111.51 111.90 112.33 123.77 +* * +* 168 VAL 168 1.306 1.236 1.514 1.564 1.438 123.22 116.64 120.01 109.17 108.53 110.53 123.31 +* * +* 169 LEU 169 1.315 1.231 1.522 1.534 1.449 122.10 116.15 120.87 110.61 108.51 110.56 122.92 170 ARG 170 1.309 1.241 1.490 1.519 1.434 121.80 113.91 121.71 110.71 114.07 111.41 124.38 * +* * * * +* 171 GLU 171 1.295 1.244 1.518 1.535 1.421 123.86 117.17 120.67 111.57 107.90 110.52 122.09 ** +* * * ** 172 ASP 172 1.303 1.240 1.501 1.523 1.442 119.37 114.65 121.37 111.11 109.82 113.04 123.93 +* * * * +* 173 GLN 173 1.294 - 1.499 1.553 1.428 123.66 - - 111.51 105.43 109.06 - +** * * +* * ** +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** +* ** ** ** ** +** *** +*** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 1.270 1.344 1.310 .013 **** * * C-N (Pro) 1.341 .016 7 1.333 1.354 1.344 .007 C-O C-O 1.231 .020 172 1.201 1.253 1.232 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.476 1.561 1.521 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.495 1.516 1.503 .005 * CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.505 1.526 1.513 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.530 1.578 1.558 .013 * CH1E-CH2E (the rest) 1.530 .020 128 1.499 1.568 1.536 .014 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.417 1.498 1.448 .016 ** ** NH1-CH2G* (Gly) 1.451 .016 12 1.413 1.461 1.439 .013 ** N-CH1E (Pro) 1.466 .015 7 1.439 1.472 1.458 .011 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 2.0 153 113.21 120.36 116.16 1.09 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.25 118.03 116.12 .86 * CH1E-C-N (Pro) 116.9 1.5 7 115.01 117.40 116.04 .66 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.32 124.76 123.04 .59 * * O-C-N (Pro) 122.0 1.4 7 122.52 123.62 123.07 .37 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.37 126.17 122.26 1.27 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.35 123.24 121.32 1.17 +* C-N-CH1E (Pro) 122.6 5.0 7 121.65 122.82 122.45 .36 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 117.21 122.57 120.79 .64 ** * CH2G*-C-O (Gly) 120.8 2.1 12 119.44 121.65 120.64 .53 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.85 110.54 110.15 .25 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 106.53 113.64 109.76 1.62 * ** CH2E-CH1E-C (the rest) 110.1 1.9 128 106.60 115.08 110.71 1.34 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 101.98 117.56 110.22 1.91 *** ** NH1-CH2G*-C (Gly) 112.5 2.9 12 108.04 114.44 111.27 1.65 +* N-CH1E-C (Pro) 111.8 2.5 7 110.71 114.47 112.15 1.05 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 110.01 110.77 110.29 .29 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.87 114.80 111.66 1.19 +* +* N-CH1E-CH2E (Pro) 103.0 1.1 7 102.72 104.83 104.04 .61 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 104.94 116.47 110.62 1.70 *** +*** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_4 Page 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] 134 87.6% Residues in additional allowed regions [a,b,l,p] 17 11.1% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% 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 87.6 83.8 10.0 .4 Inside b. Omega angle st dev 172 3.6 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 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 100 1.0 .8 .2 .8 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 5.4 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 59 9.4 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 62 7.8 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 150 9.2 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 39 5.2 20.4 5.0 -3.0 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% 87.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .97 3 Residue-by-residue listing for refined_4 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.49 Chi1-chi2 distribution -.34 Chi1 only -.04 Chi3 & chi4 .38 Omega -.08 ------ -.19 ===== Main-chain covalent forces:- Main-chain bond lengths .02 Main-chain bond angles .39 ------ .23 ===== OVERALL AVERAGE -.04 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.