Residue-by-residue listing for refined_17 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 179.7 - - - 2 HIS 2 B - - -60.2 - - - - - - - 175.1 - 35.0 - 3 HIS 3 S A - - -66.7 - - - - - - - 178.0 - 33.7 - 4 HIS 4 B - 189.6 - - - - - - - - 186.8 - 34.6 - * * 5 HIS 5 A - - -56.8 - - - - - - - 185.3 -.9 34.8 - * * 6 HIS 6 S B - - -57.0 - - - - - - - 175.0 - 35.2 - 7 HIS 7 S B 57.3 - - - - - - - - - 185.9 - 32.0 - * * 8 LEU 8 S l - 194.4 - 174.0 - - - - - - 184.1 - 32.2 - 9 GLU 9 B - 187.6 - 183.2 - - - - - - 180.2 - 35.0 - 10 CYS 10 S XX - - -59.5 - - - - - - - 180.8 - 31.6 - **** **** 11 SER 11 B - - -53.7 - - - - - - - 180.6 - 35.0 - 12 SER 12 A - - -54.1 - - - - - - - 179.4 - 34.1 - 13 ASP 13 t ~l - 177.8 - - - - - - - - 179.4 - 31.6 - ** ** 14 SER 14 T ~p - 183.7 - - - - - - - - 179.6 - 33.7 - ** ** 15 LEU 15 T A - - -65.1 - - - - - - - 175.9 - 33.9 - 16 GLN 16 t ~p - - -62.7 183.8 - - - - - - 173.2 -.6 33.4 - ** * +* ** 17 LEU 17 B - - -61.9 - - - - - - - 186.3 - 33.9 - * * 18 HIS 18 E B - - -55.6 - - - - - - - 180.1 -3.2 36.6 - +* +* Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 19 ASN 19 E B 50.9 - - - - - - - - - 184.2 - 29.7 - * * 20 VAL 20 E B 45.9 - - - - - - - - - 179.7 -2.0 32.8 - * * 21 PHE 21 E B - 178.1 - - - - - - - - 179.9 -3.4 35.8 - +* +* 22 VAL 22 E B - - -67.4 - - - - - - - 191.4 -2.6 31.3 - +* +* 23 TYR 23 a 54.7 - - - - - - - - - 186.9 -1.0 31.9 - * * * 24 GLY 24 S - - - - - - - - - - - 179.6 - - - 25 SER 25 S A - - -52.8 - - - - - - - 178.2 - 35.1 - 26 PHE 26 S B - - -68.8 - - - - - - - 173.3 - 34.8 - * * 27 GLN 27 a 48.2 - - - - - - - - - 183.6 -.9 29.8 - * +* * +* 28 ASP 28 h B - 187.2 - - - - - - - - 182.6 - 35.2 - 29 PRO 29 H - - - - - -63.3 -63.3 -30.8 - - - 181.6 - 38.1 - * * 30 ASP 30 H A - 176.2 - - - -70.3 -35.3 - - - 175.7 - 34.0 - 31 VAL 31 H A - 178.2 - - - -62.4 -42.5 - - - 178.9 - 35.0 - 32 ILE 32 H A - - -69.4 - - -66.1 -43.6 - - - 183.3 -1.6 36.0 - 33 ASN 33 H A - 206.8 - - - -55.4 -43.9 - - - 181.1 -3.0 37.4 - * * * * 34 VAL 34 H A - 180.8 - - - -81.0 -39.4 - - - 185.4 -2.0 33.9 - * * 35 MET 35 H A - 201.6 - - - -64.9 -36.5 - - - 174.3 -2.4 33.3 - * * 36 LEU 36 h a 44.7 - - 159.9 - - - - - - 183.5 -2.5 28.1 - * +* +* 37 ASP 37 S ~b - 179.5 - - - - - - - - 182.4 - 35.8 - ** ** 38 ARG 38 S B - - -61.6 181.5 - - - - - - 177.0 - 35.0 - 39 THR 39 B - - -51.6 - - - - - - - 177.1 - 34.9 - * * 40 PRO 40 - - - - - -56.2 - - - - - 180.7 - 39.4 - +* +* 41 GLU 41 E B - - -68.4 173.2 - - - - - - 183.9 -1.2 31.6 - * * 42 ILE 42 E B - - -51.9 178.0 - - - - - - 174.7 - 35.6 - 43 VAL 43 E B 62.9 - - - - - - - - - 176.1 -1.9 33.5 - 44 SER 44 E B - - -57.4 - - - - - - - 181.7 - 35.0 - 45 ALA 45 E B - - - - - - - - - - 180.2 -2.4 34.3 - 46 THR 46 E B - - -59.9 - - - - - - - 175.6 -3.0 35.0 - * * 47 LEU 47 E b - 174.8 - - - - - - - - 178.9 -3.4 34.2 - +* +* 48 PRO 48 E - - - - - -84.0 - - - - - 180.5 - 38.6 - +* * +* 49 GLY 49 E - - - - - - - - - - - 180.4 -3.2 - - +* +* 50 PHE 50 E B - - -66.6 - - - - - - - 177.9 -.8 34.5 - +* +* 51 GLN 51 E B - 178.3 - - - - - - - - 177.0 -2.3 34.0 - 52 ARG 52 E B 77.7 - - - - - - - - - 184.0 - 30.6 - 53 PHE 53 e B - - -74.8 - - - - - - - 186.8 -2.0 32.0 - * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 54 ARG 54 B - - -83.1 - - - - - - - 181.4 -1.1 31.1 - * * * 55 LEU 55 t A - 182.8 - 167.0 - - - - - - 180.1 - 35.0 - 56 LYS 56 T XX - - -66.9 - - - - - - - 184.4 - 30.1 - **** * **** 57 GLY 57 T - - - - - - - - - - - 183.2 -2.6 - - 58 ARG 58 T A 48.0 - - - - - - - - - 181.8 - 30.6 - * * 59 LEU 59 t B - 185.2 - - - - - - - - 184.3 -.8 32.3 - +* +* 60 TYR 60 B - - -48.3 - - - - - - - 171.8 - 37.7 - * * * * 61 PRO 61 S - - - - - -68.8 - - - - - 185.8 - 38.2 - * * * 62 CYS 62 e B 55.7 - - - - - - - - - 177.8 -1.5 34.3 - 63 ILE 63 E B - - -65.8 - - - - - - - 174.0 - 35.5 - * * 64 VAL 64 E B - - -63.5 - - - - - - - 177.4 -2.2 32.4 - 65 PRO 65 E - - - - - -56.0 - - - - - 176.0 - 37.9 - * * 66 SER 66 E B - 184.3 - - - - - - - - 187.6 -.8 34.7 - * +* +* 67 GLU 67 E A - 185.7 - - - - - - - - 183.9 - 33.6 - 68 LYS 68 E A - 203.9 - - - - - - - - 183.9 - 35.2 - * * 69 GLY 69 E - - - - - - - - - - - 179.7 - - - 70 GLU 70 E b 58.8 - - 184.4 - - - - - - 178.9 - 34.0 - 71 VAL 71 E B - 180.4 - - - - - - - - 174.1 -2.5 35.0 - * * 72 HIS 72 E B - - -60.8 - - - - - - - 184.9 -.6 34.9 - +* +* 73 GLY 73 E - - - - - - - - - - - 186.1 -3.5 - - * +* +* 74 LYS 74 E B - - -56.7 - - - - - - - 172.9 -.5 36.3 - * ** ** 75 VAL 75 E B - 166.7 - - - - - - - - 176.6 -2.9 34.4 - * * * 76 LEU 76 E B - - -57.0 180.5 - - - - - - 177.9 -3.3 36.4 - +* +* 77 MET 77 E B 55.4 - - 178.1 - - - - - - 185.6 -3.3 31.9 - +* +* 78 GLY 78 E - - - - - - - - - - - 178.4 -1.6 - - 79 VAL 79 E B 67.8 - - - - - - - - - 181.2 -2.1 32.7 - 80 THR 80 h B 54.6 - - - - - - - - - 180.0 - 34.6 - 81 SER 81 H A - - -58.4 - - -58.6 -32.1 - - - 181.0 - 33.5 - 82 ASP 82 H A - - -55.1 - - -67.5 -41.0 - - - 176.2 - 34.3 - 83 GLU 83 H A - - -63.5 - - -80.2 -28.7 - - - 176.1 - 29.4 - * * * 84 LEU 84 H A - 181.3 - - - -60.8 -45.2 - - - 178.0 -2.6 33.6 - 85 GLU 85 H A 61.8 - - 175.9 - -67.9 -29.9 - - - 179.2 -2.7 33.2 - 86 ASN 86 H A - 182.9 - - - -72.9 -40.3 - - - 177.1 -.9 34.1 - * * 87 LEU 87 H A - - -64.8 176.6 - -60.2 -40.5 - - - 177.9 -3.0 34.3 - * * 88 ASP 88 H A - 175.9 - - - -71.4 -29.5 - - - 177.3 -1.9 34.3 - 89 ALA 89 H A - - - - - -75.7 -48.2 - - - 183.1 -1.2 34.2 - * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 90 VAL 90 H A 64.9 - - - - -65.3 -53.4 - - - 179.3 -3.7 31.6 - * ** ** 91 GLU 91 H A - - -69.4 - - -78.0 -27.8 - - - 184.8 -2.5 33.2 - * * * 92 GLY 92 H - - - - - - -60.0 -17.8 - - - 178.4 -.6 - - +* +* +* 93 ASN 93 h A - - -62.3 - - - - - - - 181.9 -.6 33.7 - +* +* 94 GLU 94 e a - - -58.3 182.4 - - - - - - 182.5 -2.0 33.6 - 95 TYR 95 E B - - -64.5 - - - - - - - 179.4 -1.3 33.2 - 96 GLU 96 E B - 176.1 - 173.9 - - - - - - 183.3 -1.7 34.6 - 97 ARG 97 E B - 192.6 - 200.3 - - - - - - 176.2 - 37.0 - * * 98 VAL 98 E B - - -66.8 - - - - - - - 180.9 -2.7 30.1 - * * 99 THR 99 E B 52.3 - - - - - - - - - 182.1 - 35.8 - 100 VAL 100 E B - - -64.9 - - - - - - - 179.8 -3.2 33.7 - +* +* 101 GLY 101 E - - - - - - - - - - - 181.1 - - - 102 ILE 102 E B 56.5 - - - - - - - - - 179.5 -2.4 32.7 - 103 VAL 103 E B - 183.3 - - - - - - - - 180.3 -2.5 34.4 - 104 ARG 104 E B - - -66.0 177.7 - - - - - - 175.5 -3.2 34.2 - +* +* 105 GLU 105 e A - - -57.3 - - - - - - - 176.6 -3.4 35.4 - +* +* 106 ASP 106 T A - 179.5 - - - - - - - - 180.3 -.6 35.8 - +* +* 107 ASN 107 T a 68.8 - - - - - - - - - 186.1 - 35.0 - * * 108 SER 108 T l - - -60.5 - - - - - - - 173.8 -1.6 30.6 - * * 109 GLU 109 E B 58.6 - - 171.8 - - - - - - 183.6 -.5 33.5 - ** ** 110 LYS 110 E B 61.9 - - 186.2 - - - - - - 184.6 - 31.5 - 111 MET 111 E B - - -63.6 175.4 - - - - - - 176.6 -3.5 35.5 - +* +* 112 ALA 112 E B - - - - - - - - - - 181.8 - 33.4 - 113 VAL 113 E B - - -58.3 - - - - - - - 177.4 -2.7 34.5 - 114 LYS 114 E B - - -67.5 - - - - - - - 173.3 -2.3 33.4 - * * 115 THR 115 E B - 194.2 - - - - - - - - 182.1 -1.8 32.6 - 116 TYR 116 E B - - -56.4 - - - - - - - 182.8 - 34.5 - 117 MET 117 E B 78.0 - - - - - - - - - 182.1 -1.5 31.2 - 118 TRP 118 E B - 191.2 - - - - - - - - 186.6 -2.8 35.7 - * * 119 ILE 119 e A - - -59.0 - - - - - - - 181.3 -.5 32.7 - ** ** 120 ASN 120 S A - 177.3 - - - - - - - - 175.9 - 33.3 - 121 LYS 121 XX - - -55.7 180.1 - - - - - - 178.9 - 31.3 - **** **** 122 ALA 122 b - - - - - - - - - - 180.2 -2.1 32.4 - 123 ASP 123 B - 184.5 - - - - - - - - 183.0 -.6 34.3 - +* +* 124 PRO 124 S - - - - - -71.2 - - - - - 184.1 - 38.3 - * * 125 ASP 125 S A - - -70.2 - - - - - - - 181.0 - 31.7 - 126 MET 126 S A 61.4 - - 178.3 - - - - - - 176.9 - 34.3 - Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 127 PHE 127 b - 186.0 - - - - - - - - 183.9 - 33.6 - 128 GLY 128 S - - - - - - - - - - - 176.0 -1.9 - - 129 GLU 129 B - 184.5 - 181.6 - - - - - - 182.6 - 34.7 - 130 TRP 130 B - - -37.3 - - - - - - - 174.5 -.6 36.1 - +* +* +* 131 ASN 131 h b - - -61.5 - - - - - - - 183.4 - 34.0 - 132 PHE 132 H A - 201.8 - - - -61.2 -33.2 - - - 178.3 -1.3 34.7 - * * * 133 GLU 133 H A - - -57.9 184.4 - -64.9 -28.3 - - - 175.2 - 33.2 - 134 GLU 134 H A - 173.4 - 184.0 - -79.2 -54.3 - - - 183.4 -.8 35.9 - * * +* +* 135 TRP 135 H A - 176.6 - - - -58.6 -40.3 - - - 178.6 -3.0 32.0 - * * 136 LYS 136 H A - 177.9 - - - -53.2 -34.1 - - - 177.6 -3.2 33.2 - * +* +* 137 ARG 137 H A - 167.1 - 182.1 - -63.3 -51.7 - - - 182.9 -1.1 34.7 - * * * 138 LEU 138 H A - - -59.9 - - -76.9 -25.5 - - - 177.5 -1.1 32.7 - * * * 139 HIS 139 H A - 176.7 - - - -67.8 -24.6 - - - 178.5 -3.0 33.7 - * * * 140 LYS 140 H A - 179.2 - 182.2 - -56.3 -35.9 - - - 180.8 -1.0 34.0 - * * 141 LYS 141 H A - 182.0 - 188.0 - -54.7 -41.9 - - - 179.2 -.9 35.7 - +* +* 142 LYS 142 H A - 185.4 - - - -61.7 -44.4 - - - 184.0 -.8 37.7 - +* * +* 143 PHE 143 H A - 192.7 - - - -67.5 -38.2 - - - 179.9 -1.5 36.4 - 144 ILE 144 H A - - -52.6 - - -67.0 -35.6 - - - 180.1 -2.8 33.9 - 145 GLU 145 H A - - -58.7 182.1 - -59.8 -30.9 - - - 176.8 -1.8 33.3 - 146 THR 146 H A - - -53.5 - - -73.7 -48.4 - - - 181.8 -.8 35.4 - +* +* 147 PHE 147 H A - - -76.9 - - -71.6 -36.3 - - - 177.4 -1.9 29.0 - * * 148 LYS 148 H A - 183.2 - 176.7 - -62.0 -34.3 - - - 180.3 -4.0 34.8 - +** +** 149 LYS 149 H A - 186.6 - 173.3 - -75.2 -37.8 - - - 175.7 -.9 34.8 - +* +* 150 ILE 150 H A - - -63.2 174.9 - -64.5 -33.6 - - - 176.8 -1.9 33.2 - 151 MET 151 H A - - -59.8 - - -72.7 -28.0 - - - 173.9 -2.3 32.0 - * * * 152 GLU 152 H A - - -60.5 183.6 - -68.7 -30.7 - - - 177.1 -1.0 34.1 - * * 153 CYS 153 H A - 180.0 - - - -70.4 -32.9 - - - 178.2 -1.4 34.3 - 154 LYS 154 H A - - -55.7 - - -72.5 -38.1 - - - 179.5 -1.2 34.8 - * * 155 LYS 155 h XX - - -66.4 183.2 - - - - - - 173.5 -2.0 30.5 - **** * **** 156 LYS 156 B - - -65.7 - - - - - - - 183.8 - 34.4 - 157 PRO 157 S - - - - - -61.7 - - - - - 179.8 - 36.9 - 158 GLN 158 b 58.2 - - 181.4 - - - - - - 180.2 -1.3 33.8 - * * 159 GLY 159 - - - - - - - - - - - 181.3 - - - 160 GLN 160 l - - -59.5 - - - - - - - 178.7 - 30.4 - * * 161 GLY 161 - - - - - - - - - - - 182.6 - - - 162 ASN 162 t B - 181.5 - - - - - - - - 180.9 - 34.4 - Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 163 ASP 163 T B - - -67.3 - - - - - - - 180.5 -.7 32.2 - +* +* 164 ASP 164 T l - - -72.1 - - - - - - - 168.4 - 27.0 - ** +* ** 165 ILE 165 t A - 178.1 - - - - - - - - 173.3 -.5 32.9 - * ** ** 166 SER 166 S B - 183.6 - - - - - - - - 184.3 - 35.3 - 167 HIS 167 B 66.7 - - - - - - - - - 184.3 -.6 31.8 - +* +* 168 VAL 168 S A - - -61.6 - - - - - - - 181.4 - 33.0 - 169 LEU 169 B 55.7 - - - - - - - - - 175.5 - 31.0 - 170 ARG 170 b - 173.8 - 179.8 - - - - - - 174.6 - 33.3 - 171 GLU 171 ~p - - -60.1 174.9 - - - - - - 177.4 - 34.0 - ** ** 172 ASP 172 B - 186.8 - - - - - - - - 180.7 - 35.0 - 173 GLN 173 - 52.7 - - 182.1 - - - - - - - - 31.3 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * +* * +* * +* ** +** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.5 183.4 -61.4 179.4 -65.9 -66.8 -36.8 - - - 179.9 -1.9 33.9 Standard deviations: 8.5 8.3 6.9 6.5 9.8 7.3 8.0 - - - 3.7 1.0 2.0 Numbers of values: 27 53 70 38 7 42 42 0 0 0 172 97 161 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_17 Page 7 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - 1.232 1.498 - 1.457 - 117.15 120.34 - 110.48 - 122.50 2 HIS 2 1.308 1.229 1.506 1.547 1.453 121.95 116.62 120.31 108.51 109.06 111.72 123.07 +* +* 3 HIS 3 1.301 1.226 1.514 1.536 1.451 121.69 115.83 121.25 110.61 108.83 111.58 122.90 ** ** 4 HIS 4 1.309 1.236 1.522 1.539 1.441 121.75 116.39 120.60 111.37 106.93 110.09 122.94 * +* +* 5 HIS 5 1.313 1.234 1.506 1.538 1.462 121.34 116.21 120.76 108.38 111.69 111.22 123.04 * * 6 HIS 6 1.310 1.222 1.501 1.539 1.449 121.06 116.81 120.20 108.57 109.99 111.08 122.98 * * * 7 HIS 7 1.308 1.236 1.522 1.553 1.452 120.80 115.87 120.08 112.46 108.86 112.20 124.05 +* * * +* 8 LEU 8 1.324 1.238 1.533 1.565 1.457 124.04 115.26 121.62 113.31 107.51 111.64 122.93 +* * +* * +* 9 GLU 9 1.302 1.246 1.522 1.540 1.435 121.98 115.64 120.04 110.97 109.26 109.28 124.31 +* * +* 10 CYS 10 1.332 1.241 1.526 1.533 1.458 124.60 115.46 121.57 111.66 112.04 112.11 122.98 +* +* 11 SER 11 1.316 1.248 1.533 1.525 1.440 122.27 116.07 120.94 110.48 110.49 109.14 122.99 12 SER 12 1.310 1.233 1.537 1.525 1.430 122.16 116.40 119.89 111.67 110.59 109.19 123.65 * * * Residue-by-residue listing for refined_17 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 1.243 1.521 1.544 1.484 123.75 115.31 121.01 111.02 112.32 112.62 123.67 * * * * * 14 SER 14 1.335 1.250 1.558 1.559 1.461 123.43 116.84 120.55 112.32 109.89 109.52 122.59 +* * * +* 15 LEU 15 1.326 1.237 1.529 1.539 1.434 123.31 114.78 121.08 110.61 110.25 110.81 124.14 * * 16 GLN 16 1.328 1.247 1.524 1.540 1.467 125.10 112.54 122.93 107.94 114.73 112.43 124.51 +* +* * * * * +* 17 LEU 17 1.304 1.236 1.494 1.521 1.413 126.32 116.67 120.81 109.62 108.02 112.61 122.52 +* * ** +** * * +** 18 HIS 18 1.272 1.250 1.493 1.530 1.429 120.03 115.17 120.80 107.42 108.69 110.63 123.98 **** +* +* * **** 19 ASN 19 1.300 1.231 1.510 1.540 1.425 122.60 114.54 122.04 113.91 111.99 112.67 123.30 ** +* ** * ** 20 VAL 20 1.289 1.232 1.528 1.566 1.437 123.82 116.03 120.64 113.10 111.01 109.86 123.31 +** * * +* +** 21 PHE 21 1.302 1.244 1.519 1.540 1.436 123.27 115.82 120.66 110.71 108.76 108.53 123.52 +* * * +* 22 VAL 22 1.313 1.234 1.521 1.546 1.446 122.02 117.71 119.94 111.92 110.56 113.12 122.32 * * * 23 TYR 23 1.328 1.235 1.547 1.550 1.448 119.17 118.39 119.65 112.16 116.33 109.61 121.95 * * * * * +* +* 24 GLY 24 1.330 1.216 1.510 - 1.462 119.31 117.47 120.05 - 114.50 - 122.46 25 SER 25 1.314 1.242 1.527 1.520 1.461 121.46 114.56 121.98 110.29 109.20 109.32 123.41 * * 26 PHE 26 1.308 1.217 1.496 1.541 1.401 123.59 115.13 120.47 110.21 108.13 110.99 124.01 * * *** * * *** 27 GLN 27 1.295 1.240 1.519 1.567 1.474 123.18 115.88 121.15 113.50 112.52 112.72 122.91 ** +* +* * ** 28 ASP 28 1.319 1.242 1.519 1.527 1.444 121.59 118.00 119.99 109.92 109.37 109.83 122.01 29 PRO 29 1.345 1.210 1.520 1.518 1.458 122.84 117.80 119.73 109.81 113.99 104.38 122.45 * * * 30 ASP 30 1.323 1.234 1.524 1.530 1.472 121.12 115.39 121.22 110.35 109.62 110.82 123.37 31 VAL 31 1.326 1.238 1.522 1.557 1.463 122.41 114.90 121.58 109.26 108.61 111.11 123.47 32 ILE 32 1.324 1.234 1.511 1.551 1.443 123.00 113.67 122.01 110.15 109.63 108.59 124.26 * +* +* 33 ASN 33 1.285 1.226 1.519 1.502 1.432 125.25 115.89 121.05 108.89 110.72 106.94 123.06 *** * * +* ** *** 34 VAL 34 1.318 1.236 1.533 1.559 1.447 121.75 116.85 120.33 109.57 111.47 111.64 122.81 35 MET 35 1.339 1.233 1.541 1.548 1.459 121.35 117.44 120.47 112.38 110.48 109.72 122.04 * * 36 LEU 36 1.334 1.228 1.512 1.559 1.449 119.92 116.82 119.84 112.40 113.05 115.61 123.31 * * *** *** 37 ASP 37 1.322 1.228 1.495 1.548 1.480 123.05 114.19 122.12 107.83 108.37 111.31 123.68 * * * * * * 38 ARG 38 1.300 1.232 1.496 1.540 1.434 122.40 116.27 120.61 109.20 108.98 111.20 123.11 ** * * ** 39 THR 39 1.288 1.233 1.518 1.537 1.415 121.68 117.16 120.14 109.85 108.65 110.86 122.60 +** ** +** 40 PRO 40 1.345 1.236 1.514 1.530 1.467 122.99 116.65 119.86 109.95 110.34 103.14 123.48 * * 41 GLU 41 1.317 1.234 1.465 1.491 1.444 121.41 113.23 122.18 110.94 112.10 112.76 124.59 +** +* * * +** 42 ILE 42 1.248 1.241 1.497 1.546 1.406 122.19 115.69 121.08 108.60 108.95 111.25 123.20 *5.8* * +** *5.8* Residue-by-residue listing for refined_17 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 1.278 1.239 1.511 1.562 1.419 121.39 116.88 120.26 110.57 108.00 112.63 122.80 +*** ** * +*** 44 SER 44 1.293 1.243 1.519 1.517 1.415 120.71 116.83 120.42 111.31 107.33 109.37 122.70 +** ** * +** 45 ALA 45 1.293 1.225 1.497 1.506 1.433 121.12 115.36 121.04 110.11 110.94 110.30 123.60 +** * * +** 46 THR 46 1.280 1.227 1.510 1.538 1.418 122.73 116.09 120.44 109.77 110.28 110.24 123.45 +*** ** +*** 47 LEU 47 1.305 1.227 1.526 1.536 1.431 122.44 117.88 120.21 110.68 109.88 110.52 121.84 +* * +* 48 PRO 48 1.338 1.245 1.525 1.543 1.445 122.79 116.27 120.99 110.36 111.53 103.95 122.74 * * 49 GLY 49 1.309 1.240 1.509 - 1.434 120.58 116.15 120.81 - 111.70 - 123.04 * * * 50 PHE 50 1.319 1.219 1.504 1.543 1.446 123.31 116.55 120.15 109.52 109.17 111.55 123.29 * * 51 GLN 51 1.304 1.242 1.509 1.546 1.448 122.15 117.11 119.85 110.99 108.66 110.89 123.01 +* +* 52 ARG 52 1.326 1.246 1.502 1.566 1.424 119.57 114.67 121.77 111.74 109.01 115.19 123.55 * +* +* * +** +** 53 PHE 53 1.259 1.227 1.509 1.524 1.434 123.29 116.49 120.24 112.71 111.16 111.08 123.23 *5.0* * * *5.0* 54 ARG 54 1.316 1.229 1.516 1.555 1.451 121.58 113.68 121.18 111.64 113.61 112.43 125.14 * * * * * 55 LEU 55 1.332 1.240 1.533 1.578 1.462 125.83 115.76 120.62 112.57 110.66 107.40 123.61 ** ** * +* ** 56 LYS 56 1.333 1.240 1.546 1.544 1.469 123.99 117.54 120.04 112.19 114.68 112.29 122.41 * * * * * * 57 GLY 57 1.313 1.228 1.510 - 1.443 120.31 116.51 120.64 - 113.68 - 122.85 * * 58 ARG 58 1.325 1.236 1.515 1.554 1.477 121.77 116.89 120.56 111.24 114.63 112.86 122.55 * * * * 59 LEU 59 1.291 1.219 1.516 1.536 1.425 120.52 116.67 120.10 113.63 109.18 110.63 123.17 +** +* +* +** 60 TYR 60 1.296 1.232 1.513 1.540 1.443 123.07 119.51 119.11 108.25 107.30 108.32 121.37 ** +* * * * ** 61 PRO 61 1.347 1.232 1.524 1.543 1.445 121.06 115.63 120.94 110.96 108.20 104.67 123.20 * * +* +* 62 CYS 62 1.303 1.240 1.517 1.532 1.430 122.40 115.08 121.19 111.13 112.44 109.08 123.72 +* * +* 63 ILE 63 1.317 1.234 1.512 1.569 1.445 123.30 116.38 120.57 108.72 109.47 111.06 123.02 * * 64 VAL 64 1.301 1.244 1.513 1.562 1.442 121.64 117.54 120.06 110.18 109.22 113.98 122.28 ** * ** 65 PRO 65 1.339 1.237 1.533 1.541 1.460 122.59 115.10 121.62 110.75 112.92 104.17 123.21 * * * 66 SER 66 1.298 1.220 1.513 1.541 1.422 123.64 116.13 120.28 111.25 106.06 110.43 123.56 ** +* * +* ** 67 GLU 67 1.316 1.230 1.532 1.563 1.464 123.68 116.97 120.64 113.03 112.22 108.27 122.27 +* * +* * +* 68 LYS 68 1.305 1.245 1.527 1.526 1.431 120.58 115.41 121.33 110.49 110.27 109.02 123.21 +* * +* 69 GLY 69 1.313 1.239 1.510 - 1.430 121.32 115.02 121.41 - 113.14 - 123.57 * * * Residue-by-residue listing for refined_17 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 1.299 1.234 1.513 1.540 1.431 123.81 116.91 120.23 111.04 108.31 111.08 122.84 ** * * * ** 71 VAL 71 1.293 1.220 1.497 1.560 1.440 121.14 116.64 120.49 107.89 109.01 112.69 122.85 +** * +** 72 HIS 72 1.292 1.233 1.500 1.543 1.433 120.08 116.85 120.09 109.96 105.54 111.63 123.05 +** * * ** +** 73 GLY 73 1.293 1.235 1.487 - 1.425 120.32 116.30 120.67 - 112.38 - 123.01 +** +* +* +** 74 LYS 74 1.306 1.234 1.523 1.538 1.434 120.86 115.86 120.90 108.56 111.33 109.19 123.24 +* * +* 75 VAL 75 1.312 1.227 1.510 1.550 1.438 122.73 115.70 120.39 109.20 110.36 111.72 123.91 * * * 76 LEU 76 1.313 1.233 1.504 1.531 1.436 122.80 116.92 120.20 107.50 107.87 110.91 122.85 * * * * * 77 MET 77 1.293 1.227 1.501 1.530 1.442 121.22 116.01 121.17 111.94 110.36 112.26 122.82 +** * * +** 78 GLY 78 1.292 1.230 1.508 - 1.422 120.00 116.74 120.58 - 111.18 - 122.67 +** +* +** 79 VAL 79 1.332 1.247 1.526 1.578 1.446 120.35 116.40 120.60 110.98 109.03 112.97 122.98 * * 80 THR 80 1.306 1.235 1.529 1.536 1.434 122.20 116.63 120.50 110.33 110.76 109.91 122.86 +* * +* 81 SER 81 1.320 1.235 1.531 1.525 1.459 122.59 116.53 120.29 110.70 112.36 110.24 123.14 82 ASP 82 1.326 1.225 1.515 1.534 1.468 121.67 116.59 121.35 108.93 109.93 111.81 122.02 83 GLU 83 1.303 1.201 1.511 1.507 1.432 119.63 117.05 120.11 113.18 112.46 113.30 122.83 +* +* * * * +* +* +* 84 LEU 84 1.324 1.235 1.529 1.564 1.465 122.04 116.31 120.82 112.52 109.10 109.83 122.85 +* * +* 85 GLU 85 1.330 1.224 1.530 1.541 1.450 121.04 116.15 120.79 110.54 109.87 111.88 123.05 86 ASN 86 1.332 1.202 1.520 1.522 1.456 122.13 116.94 120.14 109.28 110.17 111.63 122.91 * * 87 LEU 87 1.329 1.237 1.513 1.537 1.469 122.66 114.45 121.93 109.96 109.32 111.04 123.58 88 ASP 88 1.304 1.219 1.521 1.509 1.440 122.69 116.35 120.99 111.13 111.08 109.16 122.66 +* * +* 89 ALA 89 1.304 1.217 1.526 1.521 1.443 121.90 115.87 120.83 110.50 110.35 110.28 123.28 +* +* 90 VAL 90 1.328 1.240 1.559 1.600 1.451 123.05 117.32 120.29 112.79 111.51 111.77 122.35 +* ** +* ** 91 GLU 91 1.331 1.234 1.520 1.533 1.467 121.95 115.74 120.90 110.50 112.21 111.01 123.31 92 GLY 92 1.325 1.227 1.511 - 1.463 122.83 117.15 120.06 - 114.97 - 122.79 * * 93 ASN 93 1.321 1.230 1.517 1.542 1.466 121.41 116.60 120.94 109.07 111.17 112.33 122.46 * * 94 GLU 94 1.323 1.228 1.538 1.545 1.449 120.60 116.90 120.65 111.25 111.78 110.12 122.44 95 TYR 95 1.326 1.230 1.527 1.532 1.470 122.15 116.30 120.51 110.05 111.80 111.51 123.19 96 GLU 96 1.327 1.229 1.532 1.543 1.450 122.52 115.82 120.85 110.83 110.06 109.58 123.32 97 ARG 97 1.329 1.241 1.524 1.542 1.460 122.67 117.42 119.88 106.80 109.31 110.15 122.70 +* +* 98 VAL 98 1.308 1.237 1.487 1.528 1.463 121.51 114.14 121.47 109.15 113.13 116.15 124.38 * +* * +** +** 99 THR 99 1.290 1.240 1.521 1.521 1.411 123.47 116.61 120.59 110.00 109.98 108.87 122.79 +** ** +* +** 100 VAL 100 1.303 1.241 1.514 1.548 1.442 121.61 115.86 120.78 109.60 111.28 111.87 123.36 +* +* Residue-by-residue listing for refined_17 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 1.308 1.230 1.499 - 1.425 120.91 116.19 120.42 - 111.34 - 123.38 +* +* +* 102 ILE 102 1.301 1.224 1.502 1.580 1.440 122.31 116.84 120.42 111.38 110.15 112.39 122.72 +* * * * +* 103 VAL 103 1.289 1.223 1.507 1.549 1.430 121.17 116.39 120.36 109.67 108.64 111.88 123.23 +** * +** 104 ARG 104 1.313 1.235 1.510 1.543 1.449 121.93 115.75 120.93 109.26 110.99 111.65 123.31 * * 105 GLU 105 1.314 1.230 1.539 1.534 1.460 123.05 113.75 122.01 110.36 107.93 109.31 124.24 * * * * 106 ASP 106 1.333 1.224 1.526 1.541 1.461 125.69 116.76 120.40 109.64 110.99 108.77 122.84 ** * ** 107 ASN 107 1.332 1.229 1.514 1.549 1.480 120.77 115.64 120.74 108.78 110.33 111.03 123.57 * * 108 SER 108 1.319 1.235 1.529 1.537 1.445 122.90 114.69 121.61 112.49 111.64 112.90 123.54 * * * 109 GLU 109 1.324 1.243 1.495 1.537 1.425 122.89 116.46 120.35 110.61 107.40 112.60 123.19 * +* * * +* 110 LYS 110 1.278 1.231 1.514 1.528 1.437 120.39 115.03 121.47 112.54 111.30 111.78 123.49 +*** * * +*** 111 MET 111 1.293 1.228 1.476 1.516 1.445 123.94 114.94 121.25 107.52 110.36 111.50 123.80 +** ** * * +** 112 ALA 112 1.270 1.234 1.509 1.513 1.438 121.61 115.82 120.76 110.75 109.19 111.61 123.43 **** * **** 113 VAL 113 1.301 1.241 1.518 1.561 1.450 122.41 117.61 120.12 108.77 109.11 112.39 122.26 +* +* 114 LYS 114 1.318 1.213 1.506 1.549 1.440 119.59 117.30 120.06 110.28 109.13 112.49 122.56 * * * 115 THR 115 1.290 1.250 1.518 1.563 1.433 121.62 116.62 119.86 111.06 107.69 113.51 123.51 +** * * * +** 116 TYR 116 1.304 1.234 1.517 1.533 1.431 122.39 116.54 120.63 111.35 109.04 109.65 122.81 +* * +* 117 MET 117 1.312 1.244 1.514 1.548 1.447 120.97 115.36 120.94 111.67 110.95 113.36 123.66 * +* +* 118 TRP 118 1.316 1.235 1.532 1.536 1.445 123.13 116.63 120.42 111.05 108.57 108.12 122.95 * * 119 ILE 119 1.325 1.235 1.520 1.588 1.466 121.39 115.77 120.63 109.24 111.11 113.98 123.57 +* * +* 120 ASN 120 1.318 1.237 1.527 1.537 1.463 122.99 115.32 120.90 111.55 111.37 110.21 123.77 121 LYS 121 1.336 1.216 1.541 1.534 1.482 125.41 118.09 119.94 111.18 114.35 111.85 121.96 * ** * ** 122 ALA 122 1.308 1.233 1.515 1.526 1.446 121.31 115.27 121.11 111.50 110.56 111.83 123.46 * * 123 ASP 123 1.312 1.245 1.525 1.548 1.458 122.81 117.65 120.24 110.67 108.54 110.64 122.10 * * 124 PRO 124 1.337 1.235 1.540 1.533 1.463 122.76 117.77 120.03 110.39 114.35 103.45 122.17 * * 125 ASP 125 1.328 1.235 1.493 1.524 1.471 120.72 117.08 120.00 109.50 113.26 113.60 122.91 * +* +* 126 MET 126 1.325 1.247 1.520 1.515 1.465 120.48 115.61 121.44 109.49 109.94 111.03 122.94 127 PHE 127 1.325 1.237 1.523 1.544 1.426 121.75 114.65 122.03 112.35 107.15 110.67 123.06 +* * * +* 128 GLY 128 1.296 1.234 1.464 - 1.415 121.68 115.18 120.99 - 111.36 - 123.82 ** +** ** +** Residue-by-residue listing for refined_17 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 1.281 1.238 1.483 1.521 1.393 120.98 115.49 120.83 110.84 105.29 111.22 123.64 *** ** *** ** *** 130 TRP 130 1.262 1.238 1.478 1.524 1.412 122.44 117.26 119.21 108.50 106.10 110.99 123.40 *4.8* ** ** +* *4.8* 131 ASN 131 1.304 1.222 1.519 1.534 1.449 120.32 115.93 120.78 110.10 108.08 111.76 123.13 +* * +* 132 PHE 132 1.317 1.213 1.517 1.509 1.407 123.71 116.98 120.16 111.15 111.60 108.67 122.84 * +** * * +** 133 GLU 133 1.331 1.237 1.533 1.528 1.461 121.36 115.09 121.51 111.15 109.99 111.15 123.40 134 GLU 134 1.315 1.224 1.530 1.527 1.446 123.21 115.77 120.96 109.56 109.49 108.94 123.24 * * 135 TRP 135 1.327 1.221 1.528 1.538 1.454 122.94 116.81 119.89 112.08 112.77 110.91 123.27 * * 136 LYS 136 1.329 1.233 1.537 1.566 1.470 123.52 116.03 120.87 113.24 110.64 109.05 123.06 +* * +* +* 137 ARG 137 1.322 1.233 1.529 1.525 1.449 122.41 116.52 120.95 109.61 111.39 110.09 122.52 138 LEU 138 1.315 1.230 1.519 1.547 1.453 120.95 115.37 121.29 110.87 110.37 112.32 123.32 * * 139 HIS 139 1.316 1.234 1.526 1.552 1.460 123.03 116.27 120.55 111.29 109.98 110.59 123.17 * * 140 LYS 140 1.334 1.199 1.518 1.531 1.456 121.98 116.68 120.18 109.35 110.54 111.68 123.11 +* +* 141 LYS 141 1.321 1.224 1.543 1.533 1.472 122.92 115.86 120.74 109.62 110.26 108.85 123.38 142 LYS 142 1.335 1.232 1.508 1.532 1.469 123.32 113.35 122.19 107.16 108.72 108.81 124.45 * +* +* 143 PHE 143 1.297 1.243 1.536 1.528 1.426 124.75 115.64 121.24 111.21 109.97 106.59 123.10 ** +* +* ** ** 144 ILE 144 1.330 1.201 1.511 1.558 1.448 122.07 117.40 120.03 108.20 110.16 113.47 122.55 +* * +* 145 GLU 145 1.326 1.238 1.519 1.510 1.465 121.03 116.16 120.74 110.07 111.11 111.54 123.09 146 THR 146 1.319 1.224 1.543 1.546 1.429 121.25 116.54 121.03 109.76 108.92 109.98 122.29 +* +* 147 PHE 147 1.327 1.223 1.496 1.514 1.461 121.62 117.10 119.92 112.48 115.26 113.07 122.97 * * * +* +* 148 LYS 148 1.303 1.230 1.531 1.536 1.438 121.80 114.71 121.61 110.53 108.45 110.11 123.61 +* * +* 149 LYS 149 1.330 1.235 1.527 1.520 1.445 123.62 115.83 121.27 111.53 109.82 108.55 122.90 * * * 150 ILE 150 1.323 1.227 1.531 1.566 1.452 122.28 116.27 121.23 111.45 109.48 111.46 122.44 * * 151 MET 151 1.319 1.233 1.525 1.527 1.450 121.37 116.65 120.68 111.79 110.60 112.04 122.66 152 GLU 152 1.335 1.223 1.521 1.535 1.464 121.47 115.30 121.51 109.49 108.71 111.93 123.19 153 CYS 153 1.322 1.237 1.535 1.541 1.445 122.73 116.29 120.82 110.98 109.95 109.93 122.88 154 LYS 154 1.334 1.236 1.521 1.542 1.460 121.83 115.03 120.66 109.18 109.35 111.14 124.31 155 LYS 155 1.341 1.235 1.510 1.546 1.458 124.87 115.18 121.79 110.94 113.07 114.04 122.99 +* ** ** 156 LYS 156 1.299 1.233 1.515 1.556 1.442 121.73 118.45 119.02 109.65 106.75 112.40 122.51 ** * * * +* * ** 157 PRO 157 1.347 1.242 1.536 1.534 1.470 122.92 114.93 121.43 111.26 113.91 104.65 123.61 * * * * 158 GLN 158 1.321 1.244 1.505 1.549 1.448 125.19 116.73 120.08 110.18 108.12 112.25 123.19 +* * * +* 159 GLY 159 1.300 1.235 1.501 - 1.428 120.17 114.76 120.85 - 111.74 - 124.36 ** * ** Residue-by-residue listing for refined_17 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 1.318 1.229 1.515 1.537 1.453 124.57 115.11 121.88 112.20 112.65 113.04 122.98 +* * * +* 161 GLY 161 1.287 1.217 1.476 - 1.426 121.67 114.86 121.35 - 108.95 - 123.78 +** ** +* * +** 162 ASN 162 1.301 1.241 1.510 1.530 1.433 122.23 115.92 120.62 111.06 109.83 109.87 123.42 ** * ** 163 ASP 163 1.312 1.239 1.502 1.538 1.448 121.78 114.40 120.95 110.43 111.45 112.99 124.64 * * * * * 164 ASP 164 1.317 1.237 1.504 1.547 1.456 124.89 115.47 121.40 112.34 115.52 115.55 123.01 * +* * +* +** +** 165 ILE 165 1.306 1.231 1.518 1.580 1.439 121.11 113.70 122.35 111.95 105.21 113.10 123.84 +* * * * * ** ** 166 SER 166 1.308 1.239 1.518 1.538 1.407 123.85 116.66 120.57 111.39 105.32 109.60 122.65 +* +** * ** +** 167 HIS 167 1.314 1.236 1.520 1.556 1.447 120.34 116.29 120.76 112.24 110.35 112.24 122.95 * * * * * 168 VAL 168 1.302 1.228 1.523 1.548 1.447 121.27 117.43 120.28 109.99 112.72 111.94 122.29 +* +* 169 LEU 169 1.320 1.231 1.515 1.567 1.445 119.94 114.93 120.77 113.01 113.07 111.59 124.23 +* +* +* 170 ARG 170 1.320 1.237 1.517 1.548 1.461 125.47 116.08 120.01 108.84 109.81 113.63 123.90 ** +* ** 171 GLU 171 1.333 1.244 1.530 1.529 1.472 123.42 115.32 121.28 110.54 112.77 109.56 123.35 172 ASP 172 1.312 1.242 1.511 1.541 1.449 123.45 117.71 119.74 110.22 106.55 110.73 122.54 * +* +* 173 GLN 173 1.293 - 1.516 1.531 1.438 120.99 - - 113.12 111.42 111.42 - +** * +* +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.8* +* +** ** *** +** +* * ** ** *** * *5.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 1.248 1.347 1.312 .017 *5.8* * * C-N (Pro) 1.341 .016 7 1.337 1.347 1.343 .004 C-O C-O 1.231 .020 172 1.199 1.250 1.233 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 161 1.465 1.559 1.518 .014 +** +* CH2G*-C (Gly) 1.516 .018 12 1.464 1.511 1.499 .015 +** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.506 1.526 1.517 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.521 1.600 1.557 .017 ** CH1E-CH2E (the rest) 1.530 .020 128 1.491 1.578 1.537 .014 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.393 1.484 1.446 .017 *** * NH1-CH2G* (Gly) 1.451 .016 12 1.415 1.463 1.436 .016 ** N-CH1E (Pro) 1.466 .015 7 1.445 1.470 1.458 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 2.0 153 112.54 119.51 116.09 1.09 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.76 117.47 116.12 .92 CH1E-C-N (Pro) 116.9 1.5 7 114.93 117.80 116.31 1.09 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.37 125.14 123.14 .61 * * O-C-N (Pro) 122.0 1.4 7 122.17 123.61 122.98 .50 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.17 126.32 122.28 1.38 * +** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.31 122.83 120.83 .94 * C-N-CH1E (Pro) 122.6 5.0 7 121.06 122.99 122.56 .63 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 119.02 122.93 120.74 .67 * * CH2G*-C-O (Gly) 120.8 2.1 12 120.05 121.41 120.68 .42 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.11 111.50 110.72 .51 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.89 113.10 110.11 1.27 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 106.80 113.91 110.68 1.47 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 105.21 116.33 110.15 2.03 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 108.95 114.97 112.12 1.64 * N-CH1E-C (Pro) 111.8 2.5 7 108.20 114.35 112.18 2.11 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 110.28 111.83 111.00 .72 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.59 116.15 111.88 1.61 +* +** N-CH1E-CH2E (Pro) 103.0 1.1 7 103.14 104.67 104.06 .54 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.59 115.61 110.97 1.65 ** *** ------------------------------------------------------------------------------------------------------------- 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_17 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] 16 10.5% Residues in generously allowed regions [~a,~b,~l,~p] 5 3.3% Residues in disallowed regions [XX] 4 2.6% ---- ------ 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 3.7 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 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 97 1.0 .8 .2 .8 Inside f. Overall G-factor 173 -.1 -.4 .3 .9 Inside 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 27 8.5 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 53 8.3 19.0 5.3 -2.0 BETTER c. Chi-1 gauche plus st dev 70 6.9 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 150 8.8 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 38 6.5 20.4 5.0 -2.8 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 8.7 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .98 3 Residue-by-residue listing for refined_17 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.62 Chi1-chi2 distribution -.39 Chi1 only -.14 Chi3 & chi4 .39 Omega -.10 ------ -.25 ===== Main-chain covalent forces:- Main-chain bond lengths -.08 Main-chain bond angles .35 ------ .17 ===== OVERALL AVERAGE -.11 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.