Residue-by-residue listing for refined_12 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 - - - - - - - - - - - 180.3 - - - 2 HIS 2 B - - -63.1 - - - - - - - 178.9 - 33.9 - 3 HIS 3 B - - -62.8 - - - - - - - 183.0 -.6 34.5 - +* +* 4 HIS 4 B - 187.4 - - - - - - - - 180.4 -.9 34.3 - * * 5 HIS 5 B - - -59.6 - - - - - - - 178.2 -.6 35.4 - +* +* 6 HIS 6 B 64.8 - - - - - - - - - 178.3 - 32.8 - 7 HIS 7 B - - -62.6 - - - - - - - 180.8 - 33.2 - 8 LEU 8 B - - -61.1 - - - - - - - 175.7 - 34.9 - 9 GLU 9 B - 191.4 - - - - - - - - 184.0 - 35.2 - 10 CYS 10 B - 184.3 - - - - - - - - 175.6 -.8 35.1 - +* +* 11 SER 11 b 55.1 - - - - - - - - - 179.1 - 34.9 - 12 SER 12 A - 182.1 - - - - - - - - 179.5 - 34.6 - 13 ASP 13 XX - 181.9 - - - - - - - - 180.3 - 30.7 - **** **** 14 SER 14 B 56.3 - - - - - - - - - 178.3 - 35.5 - 15 LEU 15 S A - - -71.4 - - - - - - - 177.0 -.6 33.1 - +* +* 16 GLN 16 S b - - -72.1 - - - - - - - 182.3 - 29.5 - * * 17 LEU 17 B - - -60.2 174.8 - - - - - - 185.7 -1.3 33.5 - * * 18 HIS 18 E B - - -46.8 - - - - - - - 173.0 -2.6 37.0 - * * * Residue-by-residue listing for refined_12 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 48.0 - - - - - - - - - 185.4 - 28.9 - * * * 20 VAL 20 E B - 180.6 - - - - - - - - 176.3 -1.5 35.9 - 21 PHE 21 E B - 180.3 - - - - - - - - 179.2 -2.9 35.1 - * * 22 VAL 22 E B - - -66.9 - - - - - - - 187.1 -3.4 30.4 - * +* +* 23 TYR 23 a 56.1 - - - - - - - - - 181.9 -.7 30.6 - +* +* 24 GLY 24 t - - - - - - - - - - - 180.4 - - - 25 SER 25 T A 48.1 - - - - - - - - - 182.4 - 34.7 - * * 26 PHE 26 T a - - -62.6 - - - - - - - 182.9 - 34.0 - 27 GLN 27 t A 58.9 - - 177.9 - - - - - - 182.3 -.6 34.2 - +* +* 28 ASP 28 h B - 183.5 - - - - - - - - 182.1 - 34.9 - 29 PRO 29 H - - - - - -60.3 -60.3 -33.0 - - - 183.9 - 38.4 - * * 30 ASP 30 H A - 175.4 - - - -66.8 -36.0 - - - 178.4 - 33.0 - 31 VAL 31 H A 61.9 - - - - -70.6 -29.9 - - - 174.4 -.5 30.6 - ** ** 32 ILE 32 H A - - -79.1 - - -70.8 -43.6 - - - 183.0 -1.1 35.2 - * * 33 ASN 33 H A - 200.2 - - - -54.2 -51.7 - - - 182.7 -3.0 38.0 - * * * * 34 VAL 34 H A 62.9 - - - - -78.1 -35.3 - - - 184.1 -2.5 33.1 - * * 35 MET 35 H A - 193.0 - - - -67.6 -37.0 - - - 180.8 -1.7 33.9 - 36 LEU 36 h a 51.7 - - - - - - - - - 180.1 -2.5 25.0 - +** +** 37 ASP 37 t ~b - 180.1 - - - - - - - - 184.5 -.7 35.0 - ** +* ** 38 ARG 38 S b - - -59.0 178.9 - - - - - - 174.6 - 36.8 - 39 THR 39 b - - -53.9 - - - - - - - 178.0 - 34.4 - 40 PRO 40 - - - - - -59.3 - - - - - 181.4 - 38.8 - * * 41 GLU 41 E B - 182.8 - 175.5 - - - - - - 187.0 -.6 33.9 - * +* +* 42 ILE 42 E B - - -55.2 179.8 - - - - - - 175.2 - 35.9 - 43 VAL 43 E B 64.1 - - - - - - - - - 179.0 -2.3 33.8 - 44 SER 44 E B - - -53.4 - - - - - - - 179.6 - 36.2 - 45 ALA 45 E B - - - - - - - - - - 178.9 -2.1 33.7 - 46 THR 46 E B - - -55.8 - - - - - - - 177.8 -2.8 36.0 - * * 47 LEU 47 E B - 175.1 - - - - - - - - 180.5 -3.6 34.4 - ** ** 48 PRO 48 E - - - - - -83.9 - - - - - 177.4 - 38.6 - +* * +* 49 GLY 49 E - - - - - - - - - - - 181.9 -2.7 - - 50 PHE 50 E B - - -67.8 - - - - - - - 180.6 -.7 34.1 - +* +* 51 GLN 51 E B - 182.8 - - - - - - - - 176.9 -2.8 34.5 - * * 52 ARG 52 E B 68.4 - - 166.6 - - - - - - 175.7 - 34.0 - 53 PHE 53 e B - - -72.3 - - - - - - - 182.7 -2.4 33.9 - 54 ARG 54 B 65.1 - - 178.2 - - - - - - 180.7 -1.2 32.3 - * * Residue-by-residue listing for refined_12 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 b - 195.5 - - - - - - - - 176.4 -.6 35.7 - +* +* 56 LYS 56 B 63.5 - - - - - - - - - 182.1 - 31.1 - 57 GLY 57 S - - - - - - - - - - - 178.0 - - - 58 ARG 58 S A - 181.0 - - - - - - - - 179.5 - 33.3 - 59 LEU 59 S B - 181.4 - - - - - - - - 186.8 - 31.8 - * * 60 TYR 60 B - - -53.6 - - - - - - - 173.2 - 37.2 - * * 61 PRO 61 - - - - - -67.3 - - - - - 186.6 - 37.6 - * * * 62 CYS 62 e B 52.4 - - - - - - - - - 180.1 -1.2 33.8 - * * 63 ILE 63 E B - - -62.7 - - - - - - - 171.8 - 36.9 - * * 64 VAL 64 E B - - -64.5 - - - - - - - 176.4 -1.9 33.9 - 65 PRO 65 E - - - - - -60.5 - - - - - 182.7 - 37.9 - * * 66 SER 66 E B - 185.4 - - - - - - - - 176.8 -2.5 35.1 - 67 GLU 67 E A - - -62.4 - - - - - - - 174.6 - 32.5 - 68 LYS 68 E b - - -58.2 - - - - - - - 177.3 - 32.3 - 69 GLY 69 E - - - - - - - - - - - 175.7 -.5 - - ** ** 70 GLU 70 E B 60.5 - - - - - - - - - 184.2 - 31.4 - 71 VAL 71 E B - 182.3 - - - - - - - - 174.4 -3.0 35.2 - * * 72 HIS 72 E B - - -65.5 - - - - - - - 181.7 -.6 33.6 - +* +* 73 GLY 73 E - - - - - - - - - - - 183.3 -3.1 - - * * 74 LYS 74 E B - - -59.4 - - - - - - - 176.0 -1.3 35.3 - 75 VAL 75 E B - 167.2 - - - - - - - - 176.7 -3.3 34.3 - +* +* 76 LEU 76 E B - - -59.1 180.6 - - - - - - 178.8 -3.2 36.4 - +* +* 77 MET 77 E B - - -65.5 - - - - - - - 177.4 -3.7 36.0 - ** ** 78 GLY 78 E - - - - - - - - - - - 179.7 - - - 79 VAL 79 E B - 184.7 - - - - - - - - 177.5 -2.8 35.4 - * * 80 THR 80 h B 58.6 - - - - - - - - - 180.3 - 33.7 - 81 SER 81 H A - 183.2 - - - -55.3 -48.1 - - - 185.4 - 34.5 - 82 ASP 82 H A - - -59.0 - - -58.5 -37.4 - - - 183.4 - 35.2 - 83 GLU 83 H A - - -55.8 172.4 - -76.6 -46.2 - - - 178.5 - 33.9 - 84 LEU 84 H A - 180.0 - 161.4 - -69.0 -41.2 - - - 180.0 -2.1 30.4 - * * 85 GLU 85 H A 60.6 - - 186.2 - -62.8 -29.7 - - - 177.5 -3.3 32.7 - +* +* 86 ASN 86 H A - 184.5 - - - -75.0 -42.7 - - - 177.3 -1.0 35.9 - * * 87 LEU 87 H A - - -64.6 177.2 - -60.3 -42.5 - - - 176.9 -2.2 34.0 - 88 ASP 88 H A - 178.2 - - - -62.0 -36.3 - - - 180.2 -3.1 35.4 - * * 89 ALA 89 H A - - - - - -75.4 -48.7 - - - 184.1 -1.2 34.3 - * * 90 VAL 90 H A 64.5 - - - - -63.9 -48.0 - - - 178.9 -3.7 31.5 - ** ** Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 91 GLU 91 H A - - -58.1 - - -78.3 -19.8 - - - 186.9 -2.3 34.5 - * +* * +* 92 GLY 92 h - - - - - - - - - - - 181.1 -.5 - - ** ** 93 ASN 93 T A - - -65.4 - - - - - - - 177.9 -.6 31.8 - +* +* 94 GLU 94 e a 51.8 - - - - - - - - - 179.3 -1.3 30.6 - 95 TYR 95 E B - - -58.4 - - - - - - - 176.4 -2.0 35.3 - 96 GLU 96 E B - 186.2 - 182.3 - - - - - - 183.4 -1.0 33.7 - * * 97 ARG 97 E B - 188.5 - 203.9 - - - - - - 178.4 - 37.4 - * * * 98 VAL 98 E B - - -61.1 - - - - - - - 180.0 -2.9 33.3 - * * 99 THR 99 E B - 180.1 - - - - - - - - 182.6 - 32.7 - 100 VAL 100 E B - - -64.4 - - - - - - - 177.6 -3.2 34.2 - +* +* 101 GLY 101 E - - - - - - - - - - - 180.2 - - - 102 ILE 102 E B 54.8 - - - - - - - - - 181.8 -3.1 32.0 - * * 103 VAL 103 E B - 178.6 - - - - - - - - 180.6 -3.1 33.9 - * * 104 ARG 104 E B - - -64.3 180.1 - - - - - - 179.7 -2.6 34.3 - 105 GLU 105 e A - - -58.2 185.2 - - - - - - 176.6 -2.9 33.2 - * * 106 ASP 106 T A - - -57.1 - - - - - - - 186.8 -.6 37.4 - * +* * +* 107 ASN 107 T a 59.0 - - - - - - - - - 183.3 - 36.4 - 108 SER 108 t l - - -59.2 - - - - - - - 175.5 -1.2 30.2 - * * * 109 GLU 109 e B 57.8 - - 172.8 - - - - - - 181.1 - 34.9 - 110 LYS 110 E B 68.4 - - 178.3 - - - - - - 176.9 - 34.2 - 111 MET 111 E B - 187.7 - 172.8 - - - - - - 184.3 -2.8 34.8 - * * 112 ALA 112 E B - - - - - - - - - - 182.8 - 33.9 - 113 VAL 113 E B - - -60.1 - - - - - - - 175.1 -2.6 34.7 - 114 LYS 114 E B - - -67.0 - - - - - - - 175.7 -2.0 34.5 - 115 THR 115 E B - 188.9 - - - - - - - - 181.3 -2.8 33.5 - 116 TYR 116 E B - - -55.0 - - - - - - - 180.6 - 34.6 - 117 MET 117 E B 62.9 - - 174.5 - - - - - - 181.1 -1.1 31.7 - * * 118 TRP 118 E B - 191.5 - - - - - - - - 189.7 -3.2 35.2 - +* +* +* 119 ILE 119 e A - - -55.1 - - - - - - - 181.5 -.8 32.6 - +* +* 120 ASN 120 S A - 183.7 - - - - - - - - 173.5 - 31.9 - * * 121 LYS 121 ~l 61.0 - - 182.3 - - - - - - 177.2 - 27.8 - ** +* ** 122 ALA 122 b - - - - - - - - - - 179.6 -1.5 32.5 - 123 ASP 123 g B - - -65.1 - - - - - - - 176.5 -.6 34.7 - +* +* 124 PRO 124 G - - - - - -66.0 - - - - - 180.5 - 38.9 - * * 125 ASP 125 G A - - -59.6 - - - - - - - 182.9 - 35.2 - 126 MET 126 G A 59.4 - - 181.2 - - - - - - 185.0 -1.2 35.7 - * * Residue-by-residue listing for refined_12 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 g b - 185.6 - - - - - - - - 176.1 -1.5 31.0 - 128 GLY 128 - - - - - - - - - - - 184.0 -.7 - - +* +* 129 GLU 129 B 45.2 - - - - - - - - - 190.8 - 30.4 - * +* +* 130 TRP 130 B - 173.1 - - - - - - - - 176.4 -.5 35.8 - ** ** 131 ASN 131 h XX - 178.2 - - - - - - - - 181.5 - 32.6 - **** **** 132 PHE 132 H A - - -69.4 - - -52.5 -29.9 - - - 176.2 -3.2 31.5 - * +* +* 133 GLU 133 H A 63.7 - - 172.9 - -56.2 -32.1 - - - 181.3 - 35.3 - 134 GLU 134 H A - 182.1 - 181.9 - -63.5 -48.6 - - - 178.2 -2.4 35.0 - 135 TRP 135 H A - 176.8 - - - -64.1 -37.7 - - - 178.4 -.6 32.1 - +* +* 136 LYS 136 H A - - -64.0 182.3 - -59.1 -31.8 - - - 176.0 -2.0 32.4 - 137 ARG 137 H A - 171.2 - 174.4 - -68.6 -52.0 - - - 181.5 -1.4 35.1 - * * 138 LEU 138 H A - - -74.1 - - -68.9 -24.6 - - - 177.3 -2.0 31.6 - * * 139 HIS 139 H A - 187.9 - - - -76.1 -38.7 - - - 177.6 -2.6 33.7 - 140 LYS 140 H A - 177.6 - 176.5 - -65.4 -34.1 - - - 180.2 -1.8 34.3 - 141 LYS 141 H A - 184.4 - - - -52.2 -31.6 - - - 176.7 -2.0 34.1 - * * 142 LYS 142 H A - 184.0 - 177.3 - -67.5 -44.0 - - - 186.0 -.9 36.5 - * * * 143 PHE 143 H A - 193.4 - - - -71.7 -36.4 - - - 179.8 -.8 36.6 - +* +* 144 ILE 144 H A - - -60.3 - - -55.1 -32.7 - - - 180.4 -2.7 32.4 - 145 GLU 145 H A - - -61.7 - - -56.1 -38.4 - - - 179.4 -.7 32.6 - +* +* 146 THR 146 H A - 193.7 - - - -78.0 -32.8 - - - 186.4 -1.3 33.7 - * * * 147 PHE 147 H A - 199.4 - - - -77.5 -33.6 - - - 176.9 -1.4 33.2 - * * 148 LYS 148 H A - 170.8 - 176.6 - -56.4 -42.3 - - - 181.2 -3.5 34.6 - +* +* 149 LYS 149 H A - - -56.3 177.9 - -66.9 -30.9 - - - 178.0 -.9 34.8 - * * 150 ILE 150 H A - - -59.6 176.7 - -73.3 -47.4 - - - 180.5 -.9 34.9 - +* +* 151 MET 151 H A - 183.0 - 177.4 - -64.2 -40.5 - - - 177.2 -3.0 34.4 - * * 152 GLU 152 H A - - -65.8 184.2 - -64.1 -29.8 - - - 177.7 -3.1 32.3 - * * 153 CYS 153 H A - 180.3 - - - -70.8 -31.8 - - - 181.6 -.9 34.1 - +* +* 154 LYS 154 H A - - -60.5 179.1 - -82.8 -45.8 - - - 186.2 -1.3 35.8 - * * * * 155 LYS 155 H A - 183.8 - 178.9 - -94.4 -27.9 - - - 182.9 -3.1 34.6 - ** * * ** 156 LYS 156 h ~l 64.2 - - 181.3 - - - - - - 176.7 -1.4 27.7 - ** +* ** 157 PRO 157 - - - - - -65.9 - - - - - 181.2 - 38.7 - * * 158 GLN 158 S A - 177.4 - - - - - - - - 179.9 - 33.3 - 159 GLY 159 S - - - - - - - - - - - 182.8 - - - Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 160 GLN 160 B - 187.3 - 185.8 - - - - - - 172.1 - 35.5 - * * 161 GLY 161 - - - - - - - - - - - 177.2 - - - 162 ASN 162 b - 186.7 - - - - - - - - 176.6 - 35.3 - 163 ASP 163 b - 181.1 - - - - - - - - 179.8 - 31.9 - 164 ASP 164 B - - -65.4 - - - - - - - 170.8 -1.7 35.5 - +* +* 165 ILE 165 b 52.0 - - 177.4 - - - - - - 188.6 - 32.2 - * * 166 SER 166 B - - -54.0 - - - - - - - 176.2 -.9 34.1 - +* +* 167 HIS 167 B - 173.1 - - - - - - - - 176.3 -.9 32.5 - * * 168 VAL 168 b 50.8 - - - - - - - - - 182.2 -.6 34.4 - +* +* 169 LEU 169 B - 182.6 - - - - - - - - 179.3 - 35.2 - 170 ARG 170 B 76.2 - - - - - - - - - 173.4 - 34.6 - * * 171 GLU 171 B - 183.9 - - - - - - - - 182.2 - 33.9 - 172 ASP 172 B - - -66.5 - - - - - - - 177.8 - 32.6 - 173 GLN 173 - - 187.5 - - - - - - - - - -.9 34.4 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * +* ** +* +* ** +** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.1 183.3 -61.7 178.5 -66.2 -66.9 -37.7 - - - 179.8 -1.8 34.0 Standard deviations: 6.8 6.5 5.8 6.5 8.5 9.2 7.6 - - - 3.6 1.0 2.2 Numbers of values: 33 59 58 38 7 42 42 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_12 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 - 1.233 1.500 - 1.455 - 116.97 120.34 - 110.52 - 122.69 2 HIS 2 1.307 1.237 1.508 1.534 1.446 121.02 115.89 120.49 109.85 110.06 111.70 123.61 +* +* 3 HIS 3 1.311 1.235 1.507 1.541 1.447 122.53 116.25 120.87 109.68 108.78 111.46 122.85 * * 4 HIS 4 1.294 1.229 1.511 1.533 1.434 121.18 115.75 120.82 111.34 109.44 109.86 123.43 ** * ** 5 HIS 5 1.298 1.234 1.512 1.537 1.454 122.37 117.17 120.11 109.29 109.19 110.26 122.73 ** ** 6 HIS 6 1.309 1.237 1.516 1.559 1.453 120.77 116.75 120.46 110.52 109.63 112.85 122.79 * * * * 7 HIS 7 1.301 1.238 1.511 1.538 1.448 120.89 116.56 120.31 110.46 109.34 112.21 123.12 +* * +* 8 LEU 8 1.303 1.237 1.516 1.558 1.448 121.98 116.92 119.97 109.20 108.85 111.39 123.11 +* * +* 9 GLU 9 1.321 1.237 1.521 1.552 1.450 121.41 116.76 120.64 111.19 105.96 109.66 122.57 * +* +* 10 CYS 10 1.295 1.239 1.507 1.539 1.428 120.94 115.84 120.72 110.41 110.11 109.53 123.43 ** +* ** 11 SER 11 1.305 1.246 1.533 1.534 1.428 122.09 117.67 119.88 111.49 108.50 109.01 122.45 +* +* +* Residue-by-residue listing for refined_12 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 SER 12 1.312 1.228 1.528 1.541 1.432 120.09 115.73 120.24 111.18 108.68 109.76 123.86 * * * 13 ASP 13 1.335 1.239 1.549 1.536 1.476 124.44 115.50 122.13 111.68 113.94 112.26 122.37 * +* * +* 14 SER 14 1.305 1.239 1.522 1.526 1.431 122.23 116.62 120.32 110.19 110.36 108.91 123.06 +* * +* 15 LEU 15 1.317 1.231 1.500 1.532 1.433 122.16 115.38 121.47 110.80 110.59 111.73 123.15 * * * 16 GLN 16 1.296 1.238 1.478 1.510 1.429 121.30 112.93 122.61 113.69 111.94 113.10 124.44 ** ** +* +* * +* +* ** 17 LEU 17 1.277 1.232 1.502 1.514 1.428 122.93 115.84 120.95 111.09 110.24 110.92 123.21 +*** * +* +*** 18 HIS 18 1.294 1.230 1.500 1.530 1.448 122.67 116.69 120.03 106.67 108.61 110.56 123.25 ** * +* ** 19 ASN 19 1.294 1.240 1.522 1.542 1.443 121.61 115.44 121.44 113.93 111.77 113.72 123.08 ** ** +* ** 20 VAL 20 1.317 1.223 1.523 1.572 1.462 122.79 116.97 119.99 108.50 110.04 110.37 123.04 * * 21 PHE 21 1.314 1.232 1.512 1.554 1.450 121.78 116.26 120.87 110.87 107.75 109.75 122.85 * * * * 22 VAL 22 1.298 1.237 1.500 1.549 1.423 121.05 114.40 121.85 112.64 110.02 114.04 123.72 ** * +* +* * ** 23 TYR 23 1.288 1.214 1.526 1.530 1.416 121.90 117.69 120.21 113.74 114.58 110.45 122.10 +** ** +* * +** 24 GLY 24 1.304 1.224 1.492 - 1.437 119.64 115.87 120.71 - 112.04 - 123.41 +* * +* 25 SER 25 1.309 1.227 1.540 1.518 1.441 122.75 116.73 120.87 111.47 112.37 107.84 122.36 * +* +* 26 PHE 26 1.321 1.214 1.517 1.526 1.453 121.01 117.00 120.08 109.74 112.57 110.64 122.77 27 GLN 27 1.327 1.241 1.541 1.521 1.490 122.33 116.56 120.53 108.95 113.21 110.54 122.91 +* +* 28 ASP 28 1.305 1.226 1.524 1.532 1.437 122.16 118.67 119.97 110.59 108.75 109.74 121.35 +* * * * +* 29 PRO 29 1.337 1.217 1.525 1.518 1.461 122.34 117.77 119.82 109.44 114.08 104.19 122.38 * * 30 ASP 30 1.328 1.230 1.525 1.531 1.470 121.05 117.26 120.57 110.37 111.65 111.58 122.14 31 VAL 31 1.322 1.223 1.540 1.563 1.452 119.77 116.56 120.89 112.60 110.21 113.54 122.47 * +* * +* 32 ILE 32 1.336 1.244 1.515 1.563 1.461 121.50 112.99 122.12 109.89 108.91 110.23 124.84 +* * +* 33 ASN 33 1.292 1.229 1.517 1.511 1.434 126.24 115.59 121.30 109.08 110.59 106.06 123.09 +** * +** +** +** 34 VAL 34 1.309 1.232 1.535 1.557 1.439 121.90 116.81 120.60 110.81 112.01 111.24 122.56 * * 35 MET 35 1.330 1.233 1.526 1.544 1.446 121.23 118.02 120.13 111.64 111.19 109.57 121.76 36 LEU 36 1.322 1.230 1.524 1.565 1.438 118.75 117.62 118.58 116.35 115.41 113.94 123.77 +* * +* * *** +* ** *** 37 ASP 37 1.344 1.234 1.510 1.547 1.497 124.08 114.49 121.87 107.28 109.63 112.58 123.63 * ** * * * ** 38 ARG 38 1.306 1.230 1.515 1.524 1.449 123.10 116.05 120.92 107.73 109.89 109.40 123.02 +* * +* 39 THR 39 1.309 1.234 1.535 1.549 1.436 122.69 117.60 120.21 109.66 108.85 111.52 122.10 * * * 40 PRO 40 1.347 1.234 1.527 1.529 1.471 122.90 115.99 120.39 109.81 111.74 103.74 123.62 * * Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 GLU 41 1.323 1.221 1.525 1.526 1.457 123.08 115.76 121.24 111.28 110.42 109.86 123.00 42 ILE 42 1.288 1.237 1.531 1.557 1.441 122.54 115.68 121.30 109.38 111.10 109.21 123.01 +** * +** 43 VAL 43 1.304 1.238 1.539 1.563 1.439 123.02 116.77 120.50 110.27 108.57 112.09 122.69 +* +* 44 SER 44 1.301 1.238 1.531 1.513 1.440 122.30 117.11 120.39 109.44 109.38 108.61 122.49 +* * +* 45 ALA 45 1.312 1.226 1.516 1.507 1.449 121.04 114.85 121.82 110.14 112.28 110.51 123.33 * * 46 THR 46 1.292 1.216 1.526 1.544 1.427 123.74 116.56 120.26 109.19 108.93 109.74 123.15 +** +* * * +** 47 LEU 47 1.298 1.231 1.530 1.541 1.441 122.79 117.53 120.50 111.04 109.71 109.85 121.91 ** ** 48 PRO 48 1.334 1.243 1.534 1.526 1.445 122.50 115.80 121.29 110.74 112.68 103.14 122.90 * * 49 GLY 49 1.313 1.225 1.503 - 1.436 121.08 116.82 120.53 - 112.74 - 122.65 * * 50 PHE 50 1.309 1.214 1.499 1.545 1.451 122.49 117.30 119.86 110.31 108.99 111.44 122.84 * * * 51 GLN 51 1.300 1.239 1.511 1.536 1.441 121.17 116.18 120.23 110.06 109.78 110.69 123.56 ** ** 52 ARG 52 1.325 1.241 1.503 1.554 1.431 120.98 115.96 121.24 108.43 108.26 113.83 122.79 * * * * +* +* 53 PHE 53 1.265 1.220 1.497 1.525 1.416 121.63 117.57 119.87 112.38 107.94 109.96 122.51 *4.6* * ** * * *4.6* 54 ARG 54 1.313 1.230 1.504 1.544 1.445 119.56 115.89 120.86 111.11 110.43 112.65 123.25 * * * * * 55 LEU 55 1.300 1.217 1.514 1.564 1.425 121.60 117.04 120.39 111.18 106.73 109.06 122.51 ** +* +* +* ** 56 LYS 56 1.299 1.243 1.504 1.564 1.441 120.82 115.52 120.60 111.65 109.92 114.08 123.86 ** * +* ** ** 57 GLY 57 1.303 1.223 1.502 - 1.429 121.96 116.02 120.77 - 109.74 - 123.19 +* * +* 58 ARG 58 1.309 1.227 1.526 1.562 1.457 122.26 116.24 121.05 112.90 109.58 109.77 122.70 * +* * +* 59 LEU 59 1.311 1.235 1.528 1.559 1.446 121.65 116.63 120.11 113.27 109.00 111.80 123.22 * * +* +* 60 TYR 60 1.306 1.227 1.516 1.540 1.447 123.04 118.27 119.47 108.09 109.09 108.87 122.24 +* * * +* 61 PRO 61 1.349 1.239 1.532 1.539 1.449 121.64 115.58 121.06 111.38 109.92 104.58 123.27 * * * 62 CYS 62 1.308 1.241 1.537 1.531 1.435 122.97 115.03 121.36 112.05 113.29 108.42 123.60 * * * * * 63 ILE 63 1.330 1.218 1.505 1.570 1.461 124.06 116.72 119.98 107.43 109.30 110.26 123.29 * * * 64 VAL 64 1.301 1.244 1.523 1.574 1.451 122.67 118.16 119.70 108.86 107.80 113.63 122.09 ** * * * ** 65 PRO 65 1.338 1.234 1.535 1.538 1.462 122.18 116.29 120.85 111.38 111.22 103.80 122.84 66 SER 66 1.310 1.245 1.523 1.538 1.437 122.10 116.67 120.49 110.00 109.94 109.79 122.84 * * * 67 GLU 67 1.323 1.232 1.515 1.528 1.453 120.93 116.33 120.97 111.35 110.35 111.91 122.70 68 LYS 68 1.314 1.233 1.501 1.552 1.439 121.17 116.09 120.86 109.23 109.25 115.02 122.86 * * * * +** +** 69 GLY 69 1.296 1.236 1.495 - 1.426 119.76 115.68 120.71 - 112.44 - 123.61 ** * +* ** Residue-by-residue listing for refined_12 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 1.301 1.230 1.516 1.559 1.433 123.45 116.57 120.69 112.31 108.89 113.48 122.72 +* * * * +* +* 71 VAL 71 1.303 1.217 1.498 1.559 1.442 121.75 116.55 120.80 108.16 110.78 111.61 122.64 +* * +* 72 HIS 72 1.291 1.224 1.503 1.535 1.439 120.22 116.34 120.37 111.14 107.74 111.61 123.23 +** * * +** 73 GLY 73 1.305 1.240 1.489 - 1.421 120.90 116.77 120.48 - 110.89 - 122.74 +* +* +* +* 74 LYS 74 1.289 1.217 1.523 1.537 1.433 121.18 116.95 120.35 109.99 110.09 109.59 122.66 +** * +** 75 VAL 75 1.303 1.223 1.525 1.548 1.445 122.31 115.70 120.53 109.61 111.24 111.07 123.77 +* +* 76 LEU 76 1.316 1.232 1.522 1.536 1.443 123.50 116.46 120.24 107.93 108.44 110.29 123.25 * * * 77 MET 77 1.305 1.239 1.501 1.511 1.423 123.47 114.82 121.25 108.52 111.20 109.62 123.93 +* * +* +* 78 GLY 78 1.308 1.225 1.509 - 1.441 122.14 116.84 120.31 - 113.44 - 122.85 * * 79 VAL 79 1.319 1.239 1.505 1.551 1.452 121.19 116.99 120.13 107.55 108.78 112.25 122.89 80 THR 80 1.300 1.250 1.521 1.535 1.427 120.25 116.69 120.34 110.28 109.14 111.89 122.96 ** +* ** 81 SER 81 1.314 1.224 1.527 1.542 1.448 121.70 116.03 119.88 110.10 110.59 110.42 123.88 * * 82 ASP 82 1.337 1.225 1.508 1.527 1.484 123.85 116.07 121.27 107.66 112.78 110.84 122.66 * * * * 83 GLU 83 1.289 1.224 1.534 1.528 1.440 121.77 117.70 120.03 113.00 110.19 108.25 122.22 +** +* * +** 84 LEU 84 1.338 1.226 1.526 1.562 1.468 120.37 117.58 119.87 112.78 112.06 112.81 122.54 +* * * +* 85 GLU 85 1.335 1.232 1.517 1.544 1.471 121.06 115.04 121.38 111.60 109.84 111.53 123.55 86 ASN 86 1.318 1.205 1.517 1.495 1.440 122.74 116.54 120.54 108.40 109.56 109.84 122.92 * +* +* 87 LEU 87 1.332 1.232 1.518 1.540 1.470 122.12 114.77 121.45 109.96 109.69 111.40 123.77 88 ASP 88 1.315 1.228 1.516 1.531 1.453 123.44 115.42 121.19 109.95 110.06 109.26 123.39 89 ALA 89 1.316 1.219 1.530 1.518 1.444 122.88 116.77 120.40 110.10 112.04 109.89 122.82 90 VAL 90 1.325 1.226 1.559 1.597 1.462 122.35 116.71 120.53 112.36 111.67 112.09 122.72 +* ** * ** 91 GLU 91 1.328 1.230 1.541 1.536 1.477 123.50 114.98 121.83 110.00 110.67 110.17 123.18 92 GLY 92 1.321 1.225 1.518 - 1.466 124.10 118.15 119.24 - 116.92 - 122.61 ** +* ** 93 ASN 93 1.319 1.240 1.536 1.536 1.466 120.92 117.39 120.29 111.04 112.46 112.23 122.32 * * 94 GLU 94 1.323 1.237 1.537 1.553 1.465 121.11 117.40 120.31 111.19 114.01 113.09 122.29 * * +* +* 95 TYR 95 1.316 1.242 1.512 1.532 1.462 121.01 117.18 120.15 108.62 109.58 110.77 122.66 96 GLU 96 1.314 1.245 1.513 1.546 1.438 120.64 116.31 120.29 111.20 107.31 111.64 123.40 * * * * 97 ARG 97 1.299 1.237 1.507 1.522 1.434 122.29 116.69 120.53 107.52 108.11 109.15 122.77 ** * * * ** 98 VAL 98 1.286 1.240 1.517 1.544 1.428 120.88 116.57 120.43 111.11 110.18 111.41 122.98 *** +* *** 99 THR 99 1.301 1.238 1.522 1.565 1.435 121.14 116.35 120.82 111.40 109.23 112.41 122.81 +* * * +* 100 VAL 100 1.307 1.242 1.517 1.557 1.444 121.83 115.57 120.94 108.86 111.12 112.02 123.49 +* +* Residue-by-residue listing for refined_12 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 1.305 1.227 1.501 - 1.425 121.42 116.44 120.36 - 110.38 - 123.19 +* +* +* 102 ILE 102 1.305 1.215 1.499 1.576 1.442 122.12 116.98 120.21 111.96 110.09 112.63 122.81 +* * * * +* 103 VAL 103 1.292 1.222 1.512 1.555 1.430 121.63 116.15 120.45 110.81 109.52 111.22 123.38 +** * +** 104 ARG 104 1.316 1.229 1.502 1.522 1.459 122.35 116.33 120.65 109.24 111.20 111.09 123.02 * * 105 GLU 105 1.305 1.232 1.532 1.528 1.448 121.54 114.77 121.55 111.50 110.03 110.79 123.67 +* +* 106 ASP 106 1.318 1.226 1.511 1.544 1.465 124.38 114.42 121.77 105.99 110.48 110.24 123.81 * ** ** 107 ASN 107 1.312 1.234 1.516 1.538 1.458 123.43 115.83 120.64 108.95 111.31 108.54 123.53 * * * 108 SER 108 1.314 1.237 1.539 1.539 1.448 123.47 114.84 122.04 113.15 112.65 112.32 122.99 * +* * +* 109 GLU 109 1.317 1.238 1.500 1.522 1.435 123.80 117.12 119.78 109.02 107.63 111.66 123.10 * * * * * 110 LYS 110 1.294 1.243 1.527 1.536 1.438 120.22 116.15 120.92 109.59 109.37 111.72 122.91 ** * ** 111 MET 111 1.286 1.225 1.523 1.523 1.415 123.04 117.81 119.70 111.06 107.57 109.90 122.49 *** ** * *** 112 ALA 112 1.306 1.230 1.496 1.512 1.449 120.91 116.30 120.58 110.06 110.56 111.04 123.12 +* * +* 113 VAL 113 1.292 1.240 1.512 1.555 1.437 121.18 115.64 120.98 108.55 110.30 112.00 123.38 +** * +** 114 LYS 114 1.298 1.228 1.516 1.553 1.436 121.86 116.93 120.20 109.24 108.63 112.13 122.85 ** * * ** 115 THR 115 1.296 1.246 1.514 1.566 1.433 121.26 116.21 120.63 110.07 108.12 113.09 123.16 ** * * ** 116 TYR 116 1.293 1.234 1.496 1.527 1.422 122.02 115.77 120.94 111.31 108.32 109.90 123.22 +** * +* * +** 117 MET 117 1.291 1.237 1.507 1.542 1.451 120.94 115.29 120.61 110.79 110.81 113.55 124.08 +** +* +** 118 TRP 118 1.308 1.238 1.523 1.521 1.436 123.75 116.03 120.83 111.49 108.55 108.44 123.14 +* * * * +* 119 ILE 119 1.313 1.242 1.518 1.552 1.455 121.74 117.12 120.04 110.84 113.12 111.49 122.78 * * 120 ASN 120 1.325 1.228 1.525 1.535 1.468 120.24 114.85 121.03 112.26 110.42 111.76 124.11 * * 121 LYS 121 1.339 1.234 1.549 1.554 1.494 127.20 118.26 119.76 112.58 117.65 113.04 121.98 * * +* *** * * ** * *** 122 ALA 122 1.301 1.241 1.510 1.524 1.441 121.35 115.17 121.45 111.59 110.01 111.81 123.21 +* +* 123 ASP 123 1.307 1.229 1.502 1.546 1.449 122.28 118.30 120.10 108.36 109.79 112.18 121.59 +* * * +* 124 PRO 124 1.337 1.236 1.533 1.536 1.473 122.57 115.14 121.41 110.01 111.13 103.66 123.45 * * * 125 ASP 125 1.326 1.222 1.516 1.531 1.462 124.13 116.49 120.56 108.32 111.92 110.52 122.95 * * 126 MET 126 1.319 1.213 1.510 1.536 1.464 121.54 117.82 119.81 108.12 111.41 110.28 122.37 * * 127 PHE 127 1.324 1.235 1.521 1.531 1.445 119.67 114.45 121.62 111.10 112.27 113.45 123.91 * +* +* Residue-by-residue listing for refined_12 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 128 GLY 128 1.297 1.244 1.492 - 1.416 122.63 116.49 120.14 - 108.88 - 123.37 ** * ** * * ** 129 GLU 129 1.297 1.193 1.502 1.553 1.434 121.68 116.48 120.91 115.29 110.51 111.13 122.60 ** +* * * * +** +** 130 TRP 130 1.289 1.219 1.522 1.539 1.441 121.24 116.22 119.78 111.32 111.97 106.98 124.00 +** ** +** 131 ASN 131 1.356 1.211 1.511 1.539 1.505 125.61 115.56 121.00 109.83 113.00 112.16 123.44 +* ** ** ** 132 PHE 132 1.294 1.236 1.536 1.523 1.439 125.61 116.70 120.38 113.37 113.38 109.97 122.90 +** * ** +* +** 133 GLU 133 1.337 1.234 1.542 1.530 1.471 122.40 115.22 121.11 108.36 110.72 110.43 123.67 134 GLU 134 1.325 1.230 1.515 1.523 1.450 124.06 116.47 120.59 110.61 110.00 109.14 122.92 * * 135 TRP 135 1.327 1.227 1.514 1.537 1.442 120.43 116.55 120.45 111.02 110.57 112.82 122.97 * * 136 LYS 136 1.328 1.233 1.528 1.530 1.459 121.28 116.25 120.55 111.13 110.94 111.94 123.18 137 ARG 137 1.327 1.227 1.519 1.511 1.437 122.50 116.71 120.68 109.43 111.49 109.61 122.59 * * 138 LEU 138 1.316 1.232 1.517 1.538 1.459 120.90 116.12 120.97 111.46 111.84 112.44 122.90 * * 139 HIS 139 1.306 1.229 1.530 1.545 1.449 121.29 115.63 121.13 110.86 108.53 111.39 123.22 +* +* 140 LYS 140 1.331 1.211 1.513 1.536 1.463 122.95 115.93 120.64 110.28 110.26 110.52 123.42 141 LYS 141 1.320 1.226 1.556 1.541 1.462 123.79 116.87 120.40 111.66 111.44 108.87 122.71 * * * 142 LYS 142 1.338 1.233 1.515 1.537 1.474 121.96 113.81 122.00 107.16 109.37 110.46 124.17 * +* +* 143 PHE 143 1.301 1.235 1.519 1.522 1.436 124.50 115.24 121.27 109.98 110.18 107.45 123.49 +* * +* +* +* 144 ILE 144 1.317 1.202 1.524 1.560 1.448 123.30 117.16 120.15 111.10 111.58 112.10 122.66 * * 145 GLU 145 1.315 1.230 1.536 1.514 1.458 121.83 117.70 120.15 110.89 113.20 110.87 122.13 * * 146 THR 146 1.329 1.236 1.525 1.588 1.448 119.75 115.24 121.46 109.74 108.63 113.07 123.25 +* * +* 147 PHE 147 1.322 1.227 1.515 1.514 1.421 121.95 115.38 121.05 111.52 111.15 110.52 123.57 +* +* 148 LYS 148 1.310 1.212 1.514 1.537 1.439 123.79 115.86 120.76 111.12 110.21 109.34 123.26 * * * 149 LYS 149 1.321 1.238 1.533 1.524 1.463 122.33 115.25 121.82 110.56 110.30 109.18 122.91 150 ILE 150 1.311 1.234 1.525 1.552 1.444 122.82 115.36 121.32 109.99 109.33 110.38 123.28 * * 151 MET 151 1.313 1.234 1.534 1.521 1.427 123.36 116.49 120.67 111.47 110.73 108.93 122.82 * +* +* 152 GLU 152 1.329 1.216 1.516 1.519 1.456 121.80 117.03 120.47 110.11 111.91 112.62 122.49 * * 153 CYS 153 1.308 1.229 1.538 1.538 1.449 121.20 115.97 121.19 110.91 109.98 110.22 122.84 +* +* 154 LYS 154 1.323 1.241 1.527 1.510 1.451 121.96 115.97 121.03 108.43 112.64 109.21 122.98 155 LYS 155 1.314 1.224 1.535 1.540 1.459 121.95 115.70 120.36 110.92 112.24 108.78 123.92 * * * 156 LYS 156 1.327 1.240 1.539 1.554 1.480 125.51 116.77 121.72 112.82 114.80 114.58 121.49 * * ** * * ** ** 157 PRO 157 1.336 1.237 1.536 1.535 1.465 122.96 116.32 120.62 110.24 111.50 103.66 123.06 Residue-by-residue listing for refined_12 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 158 GLN 158 1.319 1.239 1.523 1.564 1.460 122.78 115.61 120.77 113.06 110.61 109.26 123.61 +* +* +* 159 GLY 159 1.309 1.230 1.494 - 1.433 121.51 115.69 121.15 - 110.03 - 123.16 * * * * 160 GLN 160 1.306 1.242 1.510 1.536 1.436 121.65 116.00 121.05 108.69 109.63 110.72 122.92 +* * +* 161 GLY 161 1.289 1.238 1.497 - 1.421 120.46 115.86 120.65 - 108.37 - 123.42 +** * +* * +** 162 ASN 162 1.287 1.244 1.483 1.539 1.440 123.20 117.37 119.65 108.47 106.57 112.18 122.95 +** +* +* +** 163 ASP 163 1.298 1.235 1.499 1.521 1.425 119.49 114.68 121.54 111.29 109.27 113.39 123.59 ** * +* * +* ** 164 ASP 164 1.296 1.247 1.478 1.538 1.428 122.31 116.33 120.16 107.60 109.67 112.00 123.49 ** ** +* * ** 165 ILE 165 1.309 1.236 1.526 1.563 1.434 120.62 115.84 121.53 112.07 107.50 112.99 122.54 * * * * * 166 SER 166 1.290 1.225 1.523 1.527 1.420 121.28 115.71 121.15 111.79 111.85 108.93 123.10 +** ** +** 167 HIS 167 1.311 1.238 1.480 1.541 1.438 122.07 113.65 121.25 111.63 109.32 112.41 125.06 * ** * * * * ** 168 VAL 168 1.286 1.235 1.536 1.529 1.430 124.76 115.01 121.80 111.42 112.00 108.61 123.18 *** * +* * +* *** 169 LEU 169 1.285 1.245 1.516 1.539 1.438 122.14 117.04 120.23 110.75 108.84 109.34 122.71 *** * *** 170 ARG 170 1.311 1.230 1.505 1.567 1.443 120.96 116.18 120.36 108.63 108.76 112.64 123.47 * +* * +* 171 GLU 171 1.294 1.227 1.503 1.530 1.423 121.86 116.77 120.38 110.72 107.44 111.72 122.82 ** * +* * ** 172 ASP 172 1.298 1.235 1.488 1.534 1.443 120.86 115.66 120.67 110.43 110.97 112.74 123.65 ** +* * ** 173 GLN 173 1.305 - 1.527 1.544 1.433 122.55 - - 111.16 107.75 110.47 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* +* ** ** ** *** +* * *** ** +** * *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 1.265 1.356 1.310 .014 *4.6* +* * C-N (Pro) 1.341 .016 7 1.334 1.349 1.340 .005 C-O C-O 1.231 .020 172 1.193 1.250 1.231 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 161 1.478 1.559 1.519 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.489 1.518 1.499 .008 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.507 1.524 1.515 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.529 1.597 1.559 .014 ** CH1E-CH2E (the rest) 1.530 .020 128 1.495 1.567 1.536 .013 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.415 1.505 1.446 .016 ** ** NH1-CH2G* (Gly) 1.451 .016 12 1.416 1.466 1.434 .014 ** * N-CH1E (Pro) 1.466 .015 7 1.445 1.473 1.461 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 2.0 153 112.93 118.67 116.24 1.01 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.68 118.15 116.47 .68 CH1E-C-N (Pro) 116.9 1.5 7 115.14 117.77 116.13 .77 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.35 125.06 123.04 .57 * * O-C-N (Pro) 122.0 1.4 7 122.38 123.62 123.07 .38 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 118.75 127.20 122.10 1.35 +* *** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.64 124.10 121.42 1.23 ** C-N-CH1E (Pro) 122.6 5.0 7 121.64 122.96 122.44 .42 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.58 122.61 120.70 .62 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.24 121.15 120.45 .45 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.06 111.59 110.47 .65 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.43 112.64 110.18 1.43 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.99 116.35 110.52 1.69 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 105.96 117.65 110.29 1.79 +* ** NH1-CH2G*-C (Gly) 112.5 2.9 12 108.37 116.92 111.37 2.24 * +* N-CH1E-C (Pro) 111.8 2.5 7 109.92 114.08 111.75 1.22 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.89 111.81 110.81 .71 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.61 114.04 111.66 1.30 +* * N-CH1E-CH2E (Pro) 103.0 1.1 7 103.14 104.58 103.82 .42 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.06 115.02 110.82 1.67 +** +** ------------------------------------------------------------------------------------------------------------- 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_12 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] 18 11.8% Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0% 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 3.6 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 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 105 1.0 .8 .2 1.0 Inside f. Overall G-factor 173 -.1 -.4 .3 1.0 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 33 6.8 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 59 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 58 5.8 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 150 7.4 18.2 4.8 -2.2 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% 85.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 1.02 3 Residue-by-residue listing for refined_12 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.56 Chi1-chi2 distribution -.30 Chi1 only -.31 Chi3 & chi4 .22 Omega -.07 ------ -.24 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .37 ------ .20 ===== OVERALL AVERAGE -.09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.