Residue-by-residue listing for refined_10 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 180.1 - - - 2 HIS 2 B - - -65.3 - - - - - - - 176.0 - 33.6 - 3 HIS 3 B 67.2 - - - - - - - - - 185.9 -.8 32.1 - * +* +* 4 HIS 4 B - - -65.4 - - - - - - - 176.4 - 33.8 - 5 HIS 5 B - - -75.4 - - - - - - - 174.8 - 34.0 - 6 HIS 6 B 62.3 - - - - - - - - - 182.3 - 32.7 - 7 HIS 7 B - - -63.7 - - - - - - - 180.4 - 32.8 - 8 LEU 8 B - - -58.4 178.9 - - - - - - 180.1 - 34.6 - 9 GLU 9 B - 179.1 - 179.3 - - - - - - 176.9 -.6 34.1 - +* +* 10 CYS 10 b 55.7 - - - - - - - - - 185.3 -.9 33.8 - +* +* 11 SER 11 b - - -55.5 - - - - - - - 175.7 -.7 32.0 - +* +* 12 SER 12 A - - -55.3 - - - - - - - 184.6 -2.1 35.2 - 13 ASP 13 ~p - 188.0 - - - - - - - - 182.6 - 31.0 - ** ** 14 SER 14 b - - -54.3 - - - - - - - 177.4 - 34.2 - 15 LEU 15 b - - -69.9 - - - - - - - 184.1 -1.1 34.1 - * * 16 GLN 16 B - - -68.2 177.1 - - - - - - 174.3 -1.2 34.5 - * * 17 LEU 17 B - - -61.3 - - - - - - - 186.8 - 34.0 - * * 18 HIS 18 E B - - -52.5 - - - - - - - 177.8 -2.8 36.4 - * * 19 ASN 19 E B - - -54.1 - - - - - - - 183.4 - 34.2 - Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 VAL 20 E B - 180.0 - - - - - - - - 178.1 -2.8 34.5 - * * 21 PHE 21 E B - 180.1 - - - - - - - - 179.3 -2.9 35.2 - * * 22 VAL 22 E B - - -70.0 - - - - - - - 186.1 -3.0 29.5 - * * * * 23 TYR 23 A 59.2 - - - - - - - - - 179.6 -.9 32.6 - +* +* 24 GLY 24 t - - - - - - - - - - - 182.9 - - - 25 SER 25 T A - - -52.8 - - - - - - - 183.4 - 36.3 - 26 PHE 26 T a - - -61.2 - - - - - - - 184.4 - 35.4 - 27 GLN 27 t A - 190.8 - 178.9 - - - - - - 178.6 -1.1 34.6 - * * 28 ASP 28 h B - 186.0 - - - - - - - - 182.4 - 34.2 - 29 PRO 29 H - - - - - -56.9 -56.9 -31.6 - - - 180.7 - 37.7 - * * 30 ASP 30 H A - 177.7 - - - -68.0 -33.7 - - - 175.1 - 33.0 - 31 VAL 31 H A - 176.6 - - - -67.3 -39.1 - - - 179.2 -.8 35.0 - +* +* 32 ILE 32 H A - - -63.0 - - -62.5 -37.5 - - - 177.0 -1.6 34.8 - 33 ASN 33 H A - - -75.1 - - -53.8 -50.2 - - - 186.7 -2.0 36.1 - * * 34 VAL 34 H A 60.6 - - - - -82.8 -44.9 - - - 186.8 -1.4 30.8 - * * * 35 MET 35 H A - 203.1 - - - -62.3 -36.7 - - - 178.3 -3.2 34.9 - * +* +* 36 LEU 36 h a 44.6 - - 164.5 - - - - - - 184.9 -1.5 29.0 - * * * 37 ASP 37 t ~b - 173.8 - - - - - - - - 185.8 -1.0 35.3 - ** * * ** 38 ARG 38 B 58.5 - - 181.8 - - - - - - 181.8 - 34.8 - 39 THR 39 B - - -51.1 - - - - - - - 177.4 - 34.3 - * * 40 PRO 40 - - - - - -63.5 - - - - - 179.6 - 38.7 - * * 41 GLU 41 E B - 182.2 - 177.4 - - - - - - 189.1 -1.0 33.7 - +* * +* 42 ILE 42 E B - - -49.9 178.0 - - - - - - 175.0 - 36.1 - * * 43 VAL 43 E B 64.4 - - - - - - - - - 176.6 -1.9 33.7 - 44 SER 44 E B - - -58.5 - - - - - - - 180.5 - 35.3 - 45 ALA 45 E B - - - - - - - - - - 179.3 -3.1 34.2 - * * 46 THR 46 E B - - -62.3 - - - - - - - 176.1 -2.7 34.5 - 47 LEU 47 E B - 174.3 - - - - - - - - 178.9 -3.3 34.6 - +* +* 48 PRO 48 E - - - - - -86.2 - - - - - 180.1 - 38.8 - +* * +* 49 GLY 49 E - - - - - - - - - - - 179.1 -2.9 - - * * 50 PHE 50 E B - - -67.9 - - - - - - - 184.2 -.7 33.9 - +* +* 51 GLN 51 E B - 188.4 - 176.7 - - - - - - 181.0 -2.6 35.5 - 52 ARG 52 E B - 185.1 - 168.1 - - - - - - 181.4 - 32.7 - 53 PHE 53 E B - - -68.0 - - - - - - - 184.6 -2.7 34.6 - 54 ARG 54 B 53.4 - - 173.0 - - - - - - 177.8 -2.9 33.5 - * * Residue-by-residue listing for refined_10 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 55 LEU 55 a - 175.4 - - - - - - - - 179.3 - 35.3 - 56 LYS 56 l - 197.3 - - - - - - - - 183.1 - 33.0 - 57 GLY 57 S - - - - - - - - - - - 179.8 -1.8 - - 58 ARG 58 S A 74.1 - - - - - - - - - 179.9 - 32.4 - 59 LEU 59 S B - 183.9 - - - - - - - - 188.4 - 33.2 - * * 60 TYR 60 B - - -42.4 - - - - - - - 171.4 - 38.1 - +* * * +* 61 PRO 61 - - - - - -72.3 - - - - - 188.0 - 37.8 - * * * 62 CYS 62 E B 60.4 - - - - - - - - - 179.8 -1.5 34.5 - 63 ILE 63 E B - - -59.6 - - - - - - - 176.6 - 35.2 - 64 VAL 64 E B - - -61.9 - - - - - - - 175.7 -2.0 33.6 - 65 PRO 65 E - - - - - -60.3 - - - - - 177.7 - 38.2 - * * 66 SER 66 E B - 179.8 - - - - - - - - 182.7 -.7 34.8 - +* +* 67 GLU 67 E A 59.6 - - 174.3 - - - - - - 180.5 - 33.6 - 68 LYS 68 E A - - -61.2 183.7 - - - - - - 181.9 - 34.3 - 69 GLY 69 E - - - - - - - - - - - 180.9 -2.1 - - 70 GLU 70 E B 60.1 - - 181.6 - - - - - - 180.4 - 34.4 - 71 VAL 71 E B - 180.5 - - - - - - - - 177.7 -2.7 34.4 - 72 HIS 72 E B - - -62.6 - - - - - - - 182.2 -.5 34.5 - +* +* 73 GLY 73 E - - - - - - - - - - - 181.8 -3.4 - - +* +* 74 LYS 74 E B - - -87.3 - - - - - - - 178.0 -1.1 31.5 - * * * 75 VAL 75 E B - 167.2 - - - - - - - - 175.2 -3.2 34.7 - +* +* 76 LEU 76 E B - - -58.3 180.0 - - - - - - 180.6 -3.3 36.4 - +* +* 77 MET 77 E B 53.6 - - 175.3 - - - - - - 183.2 -3.4 32.2 - +* +* 78 GLY 78 E - - - - - - - - - - - 179.5 -1.0 - - * * 79 VAL 79 E B 68.1 - - - - - - - - - 181.1 -2.0 32.8 - 80 THR 80 h B - - -36.6 - - - - - - - 181.4 - 36.8 - ** ** 81 SER 81 H A - - -57.0 - - -59.3 -26.7 - - - 180.7 - 33.7 - * * 82 ASP 82 H A - - -56.3 - - -70.8 -47.3 - - - 176.5 - 33.9 - 83 GLU 83 H A - - -56.8 - - -68.7 -28.7 - - - 176.7 - 33.8 - 84 LEU 84 H A - 179.6 - - - -62.8 -50.8 - - - 179.5 -2.0 34.9 - * * 85 GLU 85 H A 59.1 - - 177.8 - -65.8 -29.8 - - - 175.6 -2.5 32.6 - 86 ASN 86 H A - 168.9 - - - -59.2 -47.9 - - - 179.3 -1.7 35.6 - 87 LEU 87 H A - - -62.6 175.8 - -64.6 -37.1 - - - 178.0 -2.2 33.4 - 88 ASP 88 H A - 184.1 - - - -73.5 -30.7 - - - 177.3 -1.8 33.4 - 89 ALA 89 H A - - - - - -70.3 -46.6 - - - 181.2 -2.3 34.5 - 90 VAL 90 H A 62.9 - - - - -72.3 -50.6 - - - 180.2 -3.0 30.9 - * * 91 GLU 91 H A - - -66.0 - - -77.8 -30.2 - - - 184.5 -2.8 33.4 - * * * 92 GLY 92 h - - - - - - - - - - - 177.9 -1.2 - - * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 ASN 93 T A - - -61.9 - - - - - - - 183.4 -.6 34.4 - +* +* 94 GLU 94 e a - - -55.5 176.6 - - - - - - 180.5 -2.2 34.4 - 95 TYR 95 E B - - -67.4 - - - - - - - 178.6 -2.7 33.3 - 96 GLU 96 E B - 181.3 - 180.8 - - - - - - 180.2 -1.9 35.3 - 97 ARG 97 E B - 182.7 - 195.0 - - - - - - 173.6 - 35.4 - * * 98 VAL 98 E B - - -72.1 - - - - - - - 181.3 -2.8 31.1 - * * 99 THR 99 E B - 189.6 - - - - - - - - 186.3 - 31.7 - * * 100 VAL 100 E B - - -64.2 - - - - - - - 178.7 -3.0 34.7 - * * 101 GLY 101 E - - - - - - - - - - - 180.0 - - - 102 ILE 102 E B 55.6 - - - - - - - - - 180.1 -3.0 31.9 - * * 103 VAL 103 E B - 179.1 - - - - - - - - 181.5 -2.4 33.7 - 104 ARG 104 E B - - -67.6 173.8 - - - - - - 180.6 -3.7 34.9 - ** ** 105 GLU 105 e A - - -62.5 - - - - - - - 186.1 -2.8 36.3 - * * * 106 ASP 106 T A 73.2 - - - - - - - - - 180.3 -.7 32.9 - +* +* 107 ASN 107 T a 66.8 - - - - - - - - - 175.0 - 30.8 - 108 SER 108 t l - - -57.0 - - - - - - - 177.0 -1.9 32.5 - 109 GLU 109 e B - - -67.4 - - - - - - - 182.4 - 33.5 - 110 LYS 110 E B 60.7 - - 178.8 - - - - - - 178.4 - 34.8 - 111 MET 111 E B - - -59.9 186.7 - - - - - - 180.7 -2.9 33.3 - * * 112 ALA 112 E B - - - - - - - - - - 183.4 - 34.3 - 113 VAL 113 E B - - -60.5 - - - - - - - 176.2 -2.9 34.5 - * * 114 LYS 114 E B - - -52.9 - - - - - - - 178.6 -2.6 35.6 - 115 THR 115 E B - 187.6 - - - - - - - - 179.5 -3.0 34.2 - * * 116 TYR 116 E B - - -60.4 - - - - - - - 183.4 - 33.8 - 117 MET 117 E B 81.7 - - - - - - - - - 184.0 -2.1 32.1 - * * 118 TRP 118 E B - 190.0 - - - - - - - - 187.7 -2.7 35.2 - * * 119 ILE 119 e A - - -56.8 - - - - - - - 181.8 -.5 32.9 - ** ** 120 ASN 120 S A - 182.2 - - - - - - - - 177.5 - 33.8 - 121 LYS 121 l 63.8 - - 184.1 - - - - - - 181.6 - 30.5 - 122 ALA 122 a - - - - - - - - - - 180.4 - 34.0 - 123 ASP 123 t B - - -67.1 - - - - - - - 179.1 - 33.9 - 124 PRO 124 T - - - - - -67.3 - - - - - 177.5 - 38.5 - * * 125 ASP 125 T A - - -67.3 - - - - - - - 181.0 - 35.6 - 126 MET 126 t b 50.1 - - - - - - - - - 175.0 -1.1 26.8 - * ** ** 127 PHE 127 b - 187.3 - - - - - - - - 183.2 -1.3 32.1 - * * 128 GLY 128 S - - - - - - - - - - - 186.6 - - - * * 129 GLU 129 B B - - -59.1 - - - - - - - 175.8 - 33.8 - Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 130 TRP 130 t B - 202.0 - - - - - - - - 187.1 -1.9 33.9 - * * * 131 ASN 131 h a 61.6 - - - - - - - - - 175.9 - 31.0 - 132 PHE 132 H A - - -65.1 - - -56.7 -30.5 - - - 181.5 -.5 33.5 - ** ** 133 GLU 133 H A - - -62.8 - - -51.9 -33.5 - - - 181.4 -1.2 36.2 - * * * 134 GLU 134 H A - 182.6 - 173.8 - -71.4 -45.5 - - - 179.1 -1.6 32.8 - 135 TRP 135 H A - 183.8 - - - -74.1 -30.4 - - - 175.6 -.7 32.0 - +* +* 136 LYS 136 H A - 184.4 - - - -57.8 -40.2 - - - 176.9 -3.0 34.8 - * * 137 ARG 137 H A - 172.8 - - - -55.8 -51.0 - - - 180.7 -1.6 35.9 - * * 138 LEU 138 H A - - -72.7 - - -74.7 -20.3 - - - 178.1 -1.2 32.7 - +* * +* 139 HIS 139 H A - 185.6 - - - -69.6 -34.0 - - - 176.1 -1.7 32.9 - 140 LYS 140 H A - 178.0 - 174.9 - -62.7 -35.2 - - - 182.5 -1.5 34.8 - 141 LYS 141 H A - - -73.0 - - -54.7 -40.2 - - - 180.9 -.8 31.6 - +* +* 142 LYS 142 H A - 186.5 - 185.6 - -55.5 -43.5 - - - 184.3 -.8 36.6 - +* +* 143 PHE 143 H A - 196.2 - - - -73.8 -35.3 - - - 181.1 -.7 35.5 - +* +* 144 ILE 144 H A - - -51.3 - - -72.3 -38.5 - - - 179.4 -2.0 33.3 - * * 145 GLU 145 H A - - -60.1 - - -59.8 -32.4 - - - 177.8 -3.2 33.7 - +* +* 146 THR 146 H A - - -52.6 - - -70.3 -47.2 - - - 177.9 -1.1 35.4 - * * 147 PHE 147 H A - - -81.2 - - -71.1 -28.6 - - - 178.1 -1.8 29.7 - * * 148 LYS 148 H A - 194.1 - - - -57.8 -38.1 - - - 179.1 -3.0 35.5 - * * 149 LYS 149 H A - - -63.1 176.6 - -71.4 -28.9 - - - 177.9 -1.0 34.5 - * * 150 ILE 150 H A - - -58.2 177.3 - -72.7 -31.2 - - - 174.1 -.7 32.0 - * +* +* 151 MET 151 H A - - -60.8 175.7 - -63.4 -41.2 - - - 177.7 -1.9 35.0 - 152 GLU 152 H A - - -57.3 - - -61.7 -35.9 - - - 180.3 -1.5 35.7 - 153 CYS 153 H A - - -59.8 - - -67.4 -31.3 - - - 177.9 -1.3 34.0 - 154 LYS 154 H A - - -55.4 - - -71.2 -27.6 - - - 174.8 -1.2 34.6 - * * * 155 LYS 155 h XX - 178.6 - 177.0 - - - - - - 183.7 -1.0 31.1 - **** * **** 156 LYS 156 XX - - -60.5 181.1 - - - - - - 173.1 -2.2 33.0 - **** * **** 157 PRO 157 S - - - - - -75.8 - - - - - 182.9 - 38.2 - * * 158 GLN 158 S B 54.3 - - 176.4 - - - - - - 175.2 -1.3 35.4 - 159 GLY 159 S - - - - - - - - - - - 186.9 - - - * * 160 GLN 160 b 55.0 - - 181.3 - - - - - - 176.9 - 36.1 - 161 GLY 161 - - - - - - - - - - - 179.9 - - - 162 ASN 162 B - - -68.8 - - - - - - - 178.8 - 32.7 - 163 ASP 163 B - 180.9 - - - - - - - - 184.0 -.6 35.2 - +* +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 164 ASP 164 B 69.7 - - - - - - - - - 172.4 - 36.5 - * * 165 ILE 165 B 63.5 - - - - - - - - - 178.2 - 32.5 - 166 SER 166 B - - -58.0 - - - - - - - 178.4 - 35.0 - 167 HIS 167 B 65.8 - - - - - - - - - 184.4 -.6 31.6 - +* +* 168 VAL 168 B - 184.6 - - - - - - - - 175.0 - 34.3 - 169 LEU 169 B - - -60.6 178.1 - - - - - - 188.1 - 34.8 - * * 170 ARG 170 B 61.5 - - 174.0 - - - - - - 165.2 -.6 32.4 - +** +* +** 171 GLU 171 b 53.3 - - 180.4 - - - - - - 191.9 - 31.3 - ** ** 172 ASP 172 b - 189.5 - - - - - - - - 177.6 -.6 33.2 - +* +* 173 GLN 173 - - 192.7 - - - - - - - - - - 34.5 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * ** +* * +* +** ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.3 183.8 -61.5 178.2 -68.9 -65.8 -37.1 - - - 180.1 -1.8 34.0 Standard deviations: 7.4 7.6 7.9 5.1 10.1 7.4 7.8 - - - 3.8 .9 1.9 Numbers of values: 32 46 72 38 7 41 41 0 0 0 172 105 161 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_10 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 - 1.239 1.505 - 1.459 - 116.78 120.20 - 110.91 - 123.01 2 HIS 2 1.319 1.234 1.523 1.547 1.457 121.60 115.98 120.69 109.50 111.12 112.11 123.31 3 HIS 3 1.324 1.225 1.522 1.564 1.464 123.49 117.64 119.57 111.95 107.94 113.05 122.79 +* * +* +* 4 HIS 4 1.316 1.226 1.514 1.533 1.462 121.54 115.73 120.73 109.61 112.89 111.02 123.54 5 HIS 5 1.320 1.236 1.505 1.549 1.465 124.14 115.84 120.85 108.02 110.08 113.31 123.31 * * +* +* 6 HIS 6 1.300 1.234 1.505 1.562 1.439 122.43 117.32 119.69 111.96 107.52 112.50 122.97 ** +* * * * ** 7 HIS 7 1.313 1.230 1.501 1.535 1.456 120.42 116.03 120.72 110.25 110.36 112.72 123.23 * * * * 8 LEU 8 1.300 1.238 1.508 1.532 1.430 121.50 116.45 120.57 110.71 108.98 110.25 122.96 ** * ** 9 GLU 9 1.301 1.246 1.509 1.531 1.434 121.26 115.93 120.61 110.35 109.76 111.06 123.42 ** * ** 10 CYS 10 1.316 1.239 1.515 1.534 1.434 121.43 116.32 120.92 111.74 108.37 110.52 122.71 * * * 11 SER 11 1.304 1.224 1.520 1.515 1.423 120.61 114.54 121.75 112.78 111.82 110.61 123.39 +* +* * +* 12 SER 12 1.311 1.236 1.530 1.524 1.433 123.22 114.81 120.78 110.73 109.58 108.94 124.41 * * * Residue-by-residue listing for refined_10 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 1.347 1.239 1.538 1.571 1.475 125.69 118.58 119.95 113.44 108.16 112.89 121.46 * ** ** * +* * * ** 14 SER 14 1.294 1.238 1.537 1.533 1.432 120.35 116.75 120.73 111.40 110.33 109.50 122.41 ** * ** 15 LEU 15 1.327 1.229 1.500 1.543 1.436 122.06 116.15 120.93 110.00 108.60 111.89 122.86 * * * 16 GLN 16 1.294 1.237 1.491 1.533 1.429 121.30 114.74 121.40 109.53 111.49 110.91 123.86 +** +* * +** 17 LEU 17 1.296 1.227 1.479 1.516 1.406 122.51 116.54 120.72 109.55 107.73 112.75 122.73 ** ** +** * * +** 18 HIS 18 1.262 1.248 1.491 1.535 1.425 120.13 116.11 120.28 109.04 108.07 109.57 123.57 *4.8* +* +* * *4.8* 19 ASN 19 1.294 1.230 1.520 1.547 1.427 121.08 117.04 120.39 110.25 107.10 112.00 122.54 ** +* * ** 20 VAL 20 1.303 1.229 1.518 1.565 1.458 121.60 116.43 120.53 109.59 110.41 111.16 123.03 +* +* 21 PHE 21 1.308 1.232 1.514 1.542 1.437 121.81 116.32 121.02 111.02 108.41 109.26 122.66 +* * +* 22 VAL 22 1.301 1.240 1.509 1.556 1.429 120.96 114.04 122.23 113.39 111.16 113.92 123.73 ** +* * +* * ** 23 TYR 23 1.307 1.223 1.526 1.530 1.450 123.34 117.32 120.21 111.16 114.27 110.44 122.47 +* * +* 24 GLY 24 1.314 1.222 1.500 - 1.446 119.00 116.22 120.17 - 112.96 - 123.58 * * 25 SER 25 1.327 1.234 1.536 1.522 1.464 122.87 116.15 120.96 108.89 112.19 108.21 122.87 * * 26 PHE 26 1.317 1.216 1.509 1.532 1.453 122.40 115.60 121.46 110.39 109.50 109.07 122.88 27 GLN 27 1.306 1.243 1.545 1.515 1.434 121.76 116.27 121.48 111.50 110.97 108.37 122.25 +* * * +* 28 ASP 28 1.308 1.233 1.532 1.528 1.447 121.31 117.99 120.20 110.75 109.38 110.32 121.80 * * 29 PRO 29 1.355 1.228 1.527 1.530 1.469 123.16 117.49 120.20 110.30 113.90 104.54 122.28 * * 30 ASP 30 1.325 1.241 1.520 1.525 1.464 120.79 115.22 121.41 111.19 109.98 111.41 123.34 31 VAL 31 1.317 1.231 1.522 1.548 1.452 122.35 115.29 121.46 109.31 108.79 110.94 123.21 32 ILE 32 1.316 1.237 1.548 1.541 1.440 122.93 116.34 120.89 110.56 110.36 109.53 122.74 * * * 33 ASN 33 1.336 1.227 1.513 1.549 1.475 122.28 115.08 121.54 106.34 110.31 111.78 123.37 +* +* 34 VAL 34 1.306 1.232 1.532 1.562 1.448 121.76 116.54 120.30 111.71 114.25 112.45 123.15 +* * * +* 35 MET 35 1.327 1.234 1.534 1.541 1.467 122.49 116.56 121.11 110.68 110.66 108.96 122.27 36 LEU 36 1.309 1.233 1.505 1.567 1.426 120.50 117.07 119.44 113.35 111.95 114.36 123.35 * +* +* +* ** ** 37 ASP 37 1.331 1.226 1.505 1.541 1.477 122.08 115.50 121.26 108.30 111.10 110.83 123.22 * * 38 ARG 38 1.300 1.220 1.503 1.531 1.453 121.87 117.19 119.78 110.46 109.76 109.82 123.03 ** * ** 39 THR 39 1.311 1.238 1.529 1.539 1.442 121.68 116.60 120.60 110.63 110.69 110.03 122.74 * * 40 PRO 40 1.345 1.233 1.523 1.533 1.465 123.58 116.09 120.17 110.04 111.79 103.83 123.72 * * 41 GLU 41 1.329 1.238 1.527 1.534 1.458 122.82 116.33 120.75 111.13 109.64 110.57 122.92 42 ILE 42 1.306 1.235 1.524 1.550 1.435 121.14 115.79 120.96 108.41 111.16 109.79 123.25 +* * * +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.308 1.237 1.532 1.568 1.450 122.50 116.87 120.34 109.62 109.07 112.68 122.75 +* * +* 44 SER 44 1.302 1.236 1.536 1.522 1.437 121.83 116.92 120.38 110.46 109.15 108.95 122.67 +* * +* 45 ALA 45 1.313 1.221 1.518 1.500 1.452 122.18 115.55 121.23 109.66 111.98 110.26 123.21 * * 46 THR 46 1.293 1.233 1.515 1.542 1.434 122.74 115.55 120.56 109.71 110.82 110.80 123.87 +** * +** 47 LEU 47 1.306 1.226 1.525 1.537 1.431 123.14 117.80 120.17 110.84 109.46 109.88 121.96 +* * +* 48 PRO 48 1.335 1.243 1.529 1.529 1.447 122.27 116.40 120.95 110.81 111.52 103.05 122.66 * * 49 GLY 49 1.311 1.238 1.501 - 1.442 120.43 115.70 120.87 - 111.57 - 123.43 * * 50 PHE 50 1.315 1.217 1.481 1.544 1.438 123.64 117.04 119.93 110.08 107.01 112.65 123.03 ** * * * * ** 51 GLN 51 1.283 1.238 1.503 1.525 1.423 120.70 116.90 120.01 112.23 107.71 107.66 123.03 *** * +* * * +* *** 52 ARG 52 1.313 1.246 1.503 1.550 1.427 119.94 114.98 121.11 111.89 109.55 111.85 123.90 * * +* +* 53 PHE 53 1.299 1.222 1.486 1.541 1.440 122.41 115.53 120.80 109.06 108.64 112.13 123.67 ** +* ** 54 ARG 54 1.288 1.237 1.511 1.531 1.425 122.13 114.19 121.82 110.37 112.45 110.91 123.99 +** +* * +** 55 LEU 55 1.298 1.231 1.488 1.528 1.438 124.10 114.33 120.85 108.70 107.73 111.53 124.83 ** +* * * * * ** 56 LYS 56 1.336 1.233 1.537 1.569 1.442 123.88 115.22 121.72 113.77 107.73 110.08 122.84 +* * +* * +* 57 GLY 57 1.314 1.229 1.501 - 1.440 121.03 117.28 119.83 - 111.20 - 122.88 * * 58 ARG 58 1.333 1.232 1.523 1.581 1.464 120.21 114.89 121.66 112.45 109.04 111.80 123.45 +** * +** 59 LEU 59 1.314 1.248 1.526 1.546 1.433 122.71 115.91 120.42 112.52 108.62 110.66 123.66 * * * * 60 TYR 60 1.299 1.237 1.517 1.544 1.441 123.24 118.84 119.46 107.76 107.86 108.15 121.68 ** * * * * ** 61 PRO 61 1.344 1.239 1.528 1.541 1.440 121.52 116.01 121.00 111.38 108.71 104.67 122.96 +* * +* +* 62 CYS 62 1.305 1.241 1.525 1.526 1.436 121.70 115.77 120.89 110.99 112.08 108.95 123.33 +* * +* 63 ILE 63 1.320 1.234 1.510 1.566 1.454 122.84 116.34 120.50 109.12 109.66 110.95 123.13 64 VAL 64 1.304 1.244 1.523 1.563 1.444 121.85 117.79 119.89 109.64 109.58 112.71 122.23 +* +* 65 PRO 65 1.343 1.229 1.533 1.537 1.466 122.66 115.56 121.32 110.53 112.54 103.98 123.05 66 SER 66 1.299 1.228 1.513 1.537 1.430 123.33 117.14 119.97 110.89 107.93 110.02 122.88 ** * * ** 67 GLU 67 1.324 1.232 1.532 1.527 1.467 121.95 116.14 120.94 109.81 111.84 111.16 122.91 68 LYS 68 1.316 1.230 1.525 1.530 1.438 121.90 117.13 120.54 110.33 111.52 110.07 122.33 * * 69 GLY 69 1.321 1.241 1.513 - 1.436 119.77 114.93 121.28 - 114.07 - 123.79 70 GLU 70 1.311 1.240 1.534 1.539 1.436 124.22 116.85 120.69 110.67 108.46 110.60 122.44 * * * * 71 VAL 71 1.300 1.219 1.509 1.558 1.443 121.86 116.40 120.61 109.37 109.80 111.82 122.98 ** ** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 HIS 72 1.304 1.230 1.500 1.541 1.447 121.26 116.71 120.25 109.96 107.92 111.47 123.03 +* * * +* 73 GLY 73 1.288 1.227 1.485 - 1.416 120.24 116.22 120.98 - 111.48 - 122.79 +** +* ** +** 74 LYS 74 1.288 1.237 1.490 1.534 1.426 121.21 114.03 121.54 110.84 112.96 113.03 124.42 +** +* +* * * +** 75 VAL 75 1.293 1.230 1.517 1.552 1.436 123.38 114.80 120.97 109.28 111.58 110.87 124.23 +** * +** 76 LEU 76 1.315 1.235 1.513 1.539 1.437 123.63 116.90 120.32 107.92 107.17 110.76 122.75 * * * * * * 77 MET 77 1.291 1.235 1.492 1.523 1.447 121.15 116.01 121.00 110.98 111.39 112.32 122.99 +** +* * +** 78 GLY 78 1.308 1.233 1.504 - 1.421 119.52 116.49 120.62 - 111.29 - 122.89 +* +* +* 79 VAL 79 1.325 1.252 1.530 1.578 1.441 120.78 116.35 120.74 111.17 109.05 112.65 122.85 * * * 80 THR 80 1.304 1.244 1.540 1.524 1.413 122.49 117.08 120.27 109.75 108.49 107.83 122.65 +* ** ** ** 81 SER 81 1.317 1.235 1.552 1.523 1.455 122.28 117.06 120.42 111.32 112.53 109.28 122.48 * * 82 ASP 82 1.333 1.216 1.523 1.529 1.474 121.83 116.73 121.06 109.33 110.75 111.59 122.20 83 GLU 83 1.309 1.218 1.539 1.546 1.455 121.14 116.44 121.08 109.61 109.18 112.25 122.47 * * * 84 LEU 84 1.330 1.244 1.531 1.522 1.459 121.67 116.23 120.82 108.53 110.37 111.05 122.95 85 GLU 85 1.340 1.207 1.516 1.538 1.460 121.53 115.51 120.80 111.31 109.68 112.09 123.66 * * 86 ASN 86 1.322 1.219 1.505 1.521 1.452 123.59 115.26 121.19 110.67 109.94 108.29 123.51 * * * 87 LEU 87 1.309 1.222 1.521 1.525 1.442 122.65 116.68 120.72 111.51 111.29 110.15 122.58 * * 88 ASP 88 1.320 1.212 1.521 1.526 1.469 120.91 116.33 121.21 110.76 110.11 111.08 122.46 89 ALA 89 1.305 1.235 1.523 1.516 1.447 122.24 115.90 120.98 110.39 110.26 109.84 123.11 +* +* 90 VAL 90 1.317 1.235 1.565 1.584 1.442 121.80 117.71 120.05 113.06 112.31 112.00 122.22 +* +* +* +* 91 GLU 91 1.338 1.235 1.525 1.539 1.488 121.93 116.09 120.63 109.29 112.81 111.67 123.26 +* +* 92 GLY 92 1.327 1.231 1.510 - 1.474 123.21 116.35 120.56 - 114.76 - 123.08 * +* +* 93 ASN 93 1.316 1.232 1.523 1.539 1.449 122.08 116.87 120.47 109.04 110.58 111.50 122.64 94 GLU 94 1.335 1.222 1.543 1.534 1.466 120.71 117.22 120.49 110.29 112.34 109.52 122.28 95 TYR 95 1.324 1.230 1.523 1.539 1.467 122.07 116.63 120.37 110.34 110.99 111.47 122.96 96 GLU 96 1.322 1.233 1.527 1.531 1.451 122.05 116.55 120.29 110.19 109.41 109.31 123.16 97 ARG 97 1.322 1.238 1.522 1.532 1.452 121.94 115.92 120.76 107.16 110.85 111.78 123.32 +* +* 98 VAL 98 1.302 1.239 1.474 1.528 1.446 122.96 114.94 121.21 109.24 111.36 115.75 123.85 +* ** ** ** 99 THR 99 1.276 1.241 1.538 1.578 1.428 121.16 116.13 121.39 113.55 108.28 112.13 122.41 +*** * +* ** * +*** 100 VAL 100 1.302 1.241 1.521 1.556 1.449 121.87 115.86 120.78 109.16 111.37 111.02 123.36 +* +* 101 GLY 101 1.307 1.231 1.506 - 1.430 121.31 116.20 120.69 - 111.00 - 123.11 +* * +* 102 ILE 102 1.305 1.237 1.509 1.580 1.442 121.98 116.90 120.27 112.13 110.29 112.57 122.81 +* * * +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 103 VAL 103 1.300 1.227 1.519 1.554 1.439 121.39 115.58 120.60 110.48 109.50 111.75 123.82 ** * ** 104 ARG 104 1.308 1.224 1.531 1.531 1.455 124.31 116.06 120.70 110.05 111.85 109.24 123.22 +* * +* 105 GLU 105 1.320 1.236 1.525 1.536 1.474 123.45 116.11 120.93 107.78 110.99 109.71 122.96 * * 106 ASP 106 1.319 1.226 1.534 1.542 1.454 121.66 117.72 120.15 110.92 112.20 111.16 122.13 107 ASN 107 1.332 1.227 1.528 1.559 1.476 119.80 116.35 120.57 110.77 113.16 113.67 123.08 * * +* +* 108 SER 108 1.328 1.228 1.541 1.531 1.480 123.76 117.61 120.27 110.83 114.04 110.85 122.10 * * * * 109 GLU 109 1.318 1.223 1.514 1.514 1.461 120.95 116.16 120.81 109.99 110.87 111.51 123.02 110 LYS 110 1.291 1.228 1.517 1.531 1.446 121.97 116.36 120.57 109.30 109.89 110.93 123.06 +** +** 111 MET 111 1.294 1.233 1.474 1.514 1.456 122.76 114.29 121.23 107.15 110.39 114.89 124.47 +** ** +* +** +** 112 ALA 112 1.274 1.238 1.501 1.512 1.438 122.55 116.57 120.51 110.45 108.44 110.85 122.91 +*** * * +*** 113 VAL 113 1.304 1.239 1.512 1.555 1.443 120.75 115.37 121.17 108.32 111.46 112.04 123.46 +* +* 114 LYS 114 1.301 1.231 1.522 1.539 1.432 122.37 117.31 120.11 109.39 107.69 110.29 122.56 +* * * +* 115 THR 115 1.297 1.236 1.518 1.564 1.437 121.06 116.25 120.30 109.77 108.79 112.05 123.45 ** * ** 116 TYR 116 1.304 1.235 1.519 1.538 1.433 122.44 116.36 120.42 112.36 108.84 109.72 123.17 +* * * +* 117 MET 117 1.316 1.241 1.532 1.555 1.451 122.04 116.24 120.37 111.81 110.08 112.35 123.35 * * * 118 TRP 118 1.320 1.244 1.543 1.530 1.460 123.17 116.49 120.61 111.25 109.93 108.15 122.90 * * 119 ILE 119 1.333 1.232 1.525 1.585 1.466 121.50 117.19 120.14 108.70 112.28 113.75 122.58 +* * +* 120 ASN 120 1.326 1.226 1.507 1.538 1.473 120.61 114.51 121.15 109.89 109.45 111.77 124.34 121 LYS 121 1.337 1.227 1.546 1.569 1.482 126.14 116.79 120.62 112.82 114.02 111.71 122.47 * +* * ** * * ** 122 ALA 122 1.329 1.225 1.534 1.522 1.454 121.52 117.29 120.02 110.32 112.44 109.98 122.69 123 ASP 123 1.335 1.224 1.516 1.543 1.483 121.94 117.61 120.35 108.60 111.68 112.22 122.03 * * * 124 PRO 124 1.350 1.236 1.528 1.534 1.473 122.60 115.16 121.24 110.57 111.40 103.65 123.60 * * * 125 ASP 125 1.331 1.234 1.502 1.526 1.459 123.69 115.95 121.09 107.96 110.78 110.72 122.96 * * * * 126 MET 126 1.308 1.214 1.518 1.570 1.420 120.61 114.73 122.76 115.94 113.13 113.88 122.34 +* ** ** * *** +* *** 127 PHE 127 1.300 1.235 1.505 1.538 1.421 121.73 113.85 122.04 112.03 107.93 112.95 123.95 ** +* * * * * ** 128 GLY 128 1.280 1.230 1.478 - 1.415 123.56 117.36 119.85 - 106.92 - 122.78 +*** ** ** +* +* +*** 129 GLU 129 1.277 1.239 1.489 1.545 1.424 120.26 115.73 121.04 109.47 110.07 112.52 123.22 +*** +* +* * +*** 130 TRP 130 1.298 1.233 1.535 1.530 1.422 120.84 118.09 118.89 112.50 105.80 110.20 123.01 ** +* * * +* ** 131 ASN 131 1.330 1.233 1.562 1.538 1.508 123.74 118.46 119.32 109.55 117.40 112.40 122.16 +* +** * * ** * +** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 132 PHE 132 1.332 1.226 1.517 1.532 1.477 123.01 115.51 120.39 108.79 110.96 112.73 124.10 * * 133 GLU 133 1.335 1.236 1.525 1.531 1.466 124.20 116.73 120.62 108.08 111.97 109.30 122.64 * * * 134 GLU 134 1.316 1.223 1.528 1.519 1.440 120.83 116.93 120.75 111.76 111.12 110.62 122.29 135 TRP 135 1.314 1.226 1.533 1.532 1.443 120.63 115.83 121.08 112.88 110.25 111.15 123.08 * * * 136 LYS 136 1.328 1.236 1.535 1.557 1.466 123.36 115.08 121.17 112.18 108.60 108.42 123.72 * * * * 137 ARG 137 1.322 1.239 1.541 1.524 1.454 123.84 116.13 121.18 109.22 111.09 108.75 122.69 * * * 138 LEU 138 1.317 1.229 1.517 1.535 1.456 121.99 116.26 120.86 110.53 111.70 112.04 122.88 139 HIS 139 1.307 1.232 1.529 1.551 1.466 121.32 115.47 120.98 111.77 109.26 111.44 123.53 +* * +* 140 LYS 140 1.328 1.229 1.525 1.549 1.462 122.81 115.70 120.93 110.70 109.80 109.62 123.29 141 LYS 141 1.329 1.210 1.514 1.528 1.461 122.82 118.17 118.85 110.41 114.24 112.51 122.96 * * * * * 142 LYS 142 1.336 1.248 1.519 1.530 1.489 121.52 113.74 122.54 106.62 109.49 110.63 123.70 +* * * +* +* 143 PHE 143 1.298 1.235 1.528 1.526 1.414 122.93 115.78 121.27 111.68 109.18 107.77 122.87 ** ** +* ** 144 ILE 144 1.325 1.190 1.511 1.552 1.450 121.49 117.52 119.70 108.76 110.81 113.42 122.77 ** * ** 145 GLU 145 1.326 1.239 1.520 1.530 1.472 121.78 115.03 121.24 110.19 110.47 111.18 123.70 146 THR 146 1.315 1.229 1.553 1.546 1.431 122.68 115.83 121.42 110.69 108.85 109.03 122.69 * * * * 147 PHE 147 1.323 1.230 1.512 1.520 1.465 122.95 116.34 120.27 112.20 114.43 112.91 123.36 * * * * 148 LYS 148 1.311 1.225 1.545 1.558 1.447 123.50 115.75 121.31 111.13 107.77 108.77 122.87 * * * * * 149 LYS 149 1.336 1.228 1.524 1.520 1.459 122.36 115.68 121.48 109.90 110.47 110.33 122.84 150 ILE 150 1.315 1.231 1.538 1.564 1.446 122.20 115.87 121.23 113.09 109.42 111.50 122.87 * +* +* 151 MET 151 1.331 1.238 1.528 1.538 1.469 122.24 115.13 121.20 109.22 108.61 110.77 123.65 152 GLU 152 1.342 1.232 1.531 1.533 1.465 123.22 115.60 120.95 107.95 110.05 110.61 123.45 * * 153 CYS 153 1.333 1.231 1.523 1.525 1.462 123.02 116.26 120.78 110.18 111.44 110.43 122.96 154 LYS 154 1.330 1.235 1.521 1.535 1.461 121.49 113.98 121.26 110.35 108.37 110.54 124.76 * * * * 155 LYS 155 1.337 1.233 1.510 1.540 1.448 126.00 115.71 119.98 112.57 113.00 111.67 124.28 ** * ** 156 LYS 156 1.323 1.242 1.553 1.548 1.471 124.20 118.29 121.32 110.18 111.67 111.86 120.31 * * * +* +* 157 PRO 157 1.340 1.236 1.526 1.540 1.451 121.71 115.67 121.03 110.75 110.00 104.38 123.18 * * * 158 GLN 158 1.308 1.245 1.513 1.547 1.451 123.61 116.34 119.68 109.32 109.06 110.37 123.97 * * * 159 GLY 159 1.334 1.230 1.507 - 1.447 121.22 116.87 120.36 - 109.67 - 122.77 160 GLN 160 1.292 1.232 1.511 1.524 1.443 121.51 116.01 120.62 109.87 110.78 108.19 123.37 +** * +** 161 GLY 161 1.310 1.244 1.513 - 1.431 120.96 116.76 120.54 - 111.03 - 122.69 * * * 162 ASN 162 1.307 1.228 1.515 1.545 1.451 122.15 115.68 121.05 110.72 111.13 112.18 123.25 +* +* Residue-by-residue listing for refined_10 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 1.242 1.509 1.533 1.459 123.17 116.81 120.30 109.61 108.18 110.39 122.89 * * * 164 ASP 164 1.306 1.242 1.510 1.547 1.454 121.19 115.47 121.02 107.36 110.31 110.30 123.51 +* * +* 165 ILE 165 1.304 1.239 1.513 1.586 1.440 122.74 117.07 120.12 109.37 107.77 115.40 122.78 +* +* * ** ** 166 SER 166 1.291 1.231 1.522 1.529 1.437 121.21 117.28 120.14 110.40 109.09 109.64 122.53 +** * +** 167 HIS 167 1.326 1.234 1.508 1.553 1.454 120.25 116.50 119.97 111.76 109.65 113.29 123.52 * +* +* 168 VAL 168 1.305 1.237 1.516 1.545 1.445 121.81 114.78 121.49 108.63 111.18 111.99 123.71 +* +* 169 LEU 169 1.282 1.241 1.498 1.532 1.427 123.32 116.98 120.36 110.81 106.07 110.75 122.65 *** * +* +* *** 170 ARG 170 1.290 1.237 1.504 1.540 1.422 119.80 114.29 121.94 109.86 113.67 112.62 123.68 +** +* * * +** 171 GLU 171 1.289 1.235 1.511 1.541 1.418 122.84 114.33 121.65 114.55 104.72 112.89 123.73 +** ** ** ** * +** 172 ASP 172 1.308 1.237 1.517 1.527 1.454 123.42 115.15 121.47 110.79 113.12 110.49 123.36 +* +* 173 GLN 173 1.310 - 1.509 1.553 1.433 123.14 - - 111.26 106.06 110.83 - * * * +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.8* ** ** +** +** ** * * *** ** +** +* *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 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 1.262 1.347 1.312 .015 *4.8* * * C-N (Pro) 1.341 .016 7 1.335 1.355 1.345 .006 C-O C-O 1.231 .020 172 1.190 1.252 1.232 .008 ** * CA-C CH1E-C (except Gly) 1.525 .021 161 1.474 1.565 1.520 .016 ** +* CH2G*-C (Gly) 1.516 .018 12 1.478 1.513 1.502 .010 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.500 1.522 1.512 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.524 1.586 1.558 .016 +* CH1E-CH2E (the rest) 1.530 .020 128 1.514 1.581 1.537 .013 +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.406 1.508 1.449 .017 +** +** NH1-CH2G* (Gly) 1.451 .016 12 1.415 1.474 1.438 .017 ** * N-CH1E (Pro) 1.466 .015 7 1.440 1.473 1.459 .012 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 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 2.0 153 113.74 118.84 116.18 1.01 * * CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.93 117.36 116.43 .64 CH1E-C-N (Pro) 116.9 1.5 7 115.16 117.49 116.05 .70 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 120.31 124.83 123.06 .62 +* * O-C-N (Pro) 122.0 1.4 7 122.28 123.72 123.06 .47 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.80 126.14 122.17 1.17 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.00 123.56 120.93 1.35 +* C-N-CH1E (Pro) 122.6 5.0 7 121.52 123.58 122.50 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.85 122.76 120.74 .62 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.83 121.28 120.50 .42 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.66 110.45 110.20 .32 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 108.32 113.55 110.21 1.52 ** CH2E-CH1E-C (the rest) 110.1 1.9 128 106.34 115.94 110.45 1.55 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.72 117.40 110.21 1.92 ** ** NH1-CH2G*-C (Gly) 112.5 2.9 12 106.92 114.76 111.40 1.92 +* N-CH1E-C (Pro) 111.8 2.5 7 108.71 113.90 111.41 1.55 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.84 110.85 110.23 .39 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 107.83 115.75 111.81 1.70 ** ** N-CH1E-CH2E (Pro) 103.0 1.1 7 103.05 104.67 104.01 .52 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.66 114.89 110.92 1.48 +* +** ------------------------------------------------------------------------------------------------------------- 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_10 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] 130 85.0% Residues in additional allowed regions [a,b,l,p] 19 12.4% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% Residues in disallowed regions [XX] 2 1.3% ---- ------ 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 85.0 83.8 10.0 .1 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 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 105 .9 .8 .2 .5 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 32 7.4 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 46 7.6 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 72 7.9 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 150 8.6 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 38 5.1 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% 85.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_10 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.48 Chi1-chi2 distribution -.41 Chi1 only -.08 Chi3 & chi4 .32 Omega -.09 ------ -.22 ===== Main-chain covalent forces:- Main-chain bond lengths .00 Main-chain bond angles .39 ------ .23 ===== OVERALL AVERAGE -.06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.