Residue-by-residue listing for refined_11 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 - - - - - - - - - - - 180.6 - - - 2 HIS 2 b - - -71.2 - - - - - - - 172.8 - 31.9 - * * 3 HIS 3 b - 183.0 - - - - - - - - 192.4 -1.3 34.0 - ** ** 4 HIS 4 B 57.5 - - - - - - - - - 173.4 -1.4 31.6 - * * 5 HIS 5 B - - -69.5 - - - - - - - 181.2 - 33.8 - 6 HIS 6 S ~l - 190.4 - - - - - - - - 191.9 - 31.8 - ** ** ** 7 HIS 7 S ~l - - -68.4 - - - - - - - 181.3 - 30.0 - ** * ** 8 LEU 8 B - - -64.0 175.4 - - - - - - 173.8 - 35.9 - * * 9 GLU 9 S XX - 183.1 - 177.4 - - - - - - 185.8 - 32.1 - **** **** 10 CYS 10 B - 186.2 - - - - - - - - 174.9 -2.6 36.4 - 11 SER 11 b - 183.1 - - - - - - - - 177.2 -.9 35.7 - +* +* 12 SER 12 S A 57.2 - - - - - - - - - 175.8 - 34.6 - 13 ASP 13 S B 57.8 - - - - - - - - - 176.3 - 36.3 - 14 SER 14 S b - 189.9 - - - - - - - - 187.6 - 33.8 - * * 15 LEU 15 S l - 195.2 - 155.9 - - - - - - 180.2 -1.3 31.2 - * * * 16 GLN 16 B 60.6 - - 177.6 - - - - - - 173.9 - 34.1 - * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 17 LEU 17 B - - -60.7 - - - - - - - 185.9 - 33.0 - * * 18 HIS 18 E B - - -56.0 - - - - - - - 180.9 -2.7 34.6 - 19 ASN 19 E B 49.2 - - - - - - - - - 185.1 - 30.4 - * * 20 VAL 20 E B - 178.7 - - - - - - - - 177.6 -2.5 35.7 - 21 PHE 21 E B - 178.1 - - - - - - - - 183.5 -2.8 35.1 - * * 22 VAL 22 E B 62.4 - - - - - - - - - 185.2 -3.0 31.0 - * * 23 TYR 23 a 56.0 - - - - - - - - - 185.6 - 33.2 - 24 GLY 24 t - - - - - - - - - - - 185.4 - - - 25 SER 25 T A - - -48.0 - - - - - - - 183.3 - 35.7 - * * 26 PHE 26 T a - - -60.9 - - - - - - - 181.7 - 35.2 - 27 GLN 27 t a - 189.2 - 181.5 - - - - - - 182.8 -1.6 35.6 - 28 ASP 28 h B - 175.8 - - - - - - - - 181.0 - 35.2 - 29 PRO 29 H - - - - - -73.2 -73.2 -24.5 - - - 182.1 - 38.2 - * * * 30 ASP 30 H A - 176.5 - - - -67.9 -38.5 - - - 175.9 - 32.6 - 31 VAL 31 H A 64.1 - - - - -69.3 -28.9 - - - 178.3 - 31.5 - 32 ILE 32 H A - - -65.6 - - -58.9 -37.8 - - - 179.7 -.9 34.8 - +* +* 33 ASN 33 H A - - -69.7 - - -53.8 -44.6 - - - 185.8 -1.3 36.3 - * * 34 VAL 34 H A - 181.5 - - - -82.5 -41.9 - - - 188.3 -.8 33.6 - * * +* +* 35 MET 35 H A - 199.3 - - - -65.9 -37.5 - - - 176.9 -2.6 33.9 - 36 LEU 36 h a 52.5 - - 164.7 - - - - - - 182.4 -1.9 29.3 - * * 37 ASP 37 t ~b - 182.8 - - - - - - - - 185.6 -.9 35.3 - ** +* ** 38 ARG 38 S B 70.2 - - 187.7 - - - - - - 175.6 - 36.0 - 39 THR 39 B - - -47.5 - - - - - - - 177.2 - 34.6 - * * 40 PRO 40 - - - - - -54.9 - - - - - 177.1 - 39.0 - * * 41 GLU 41 E B - 179.3 - 174.4 - - - - - - 187.8 -1.9 33.9 - * * 42 ILE 42 E B - - -50.1 177.3 - - - - - - 177.2 - 36.0 - * * 43 VAL 43 E B 61.2 - - - - - - - - - 176.4 -2.0 34.0 - 44 SER 44 E B - - -60.3 - - - - - - - 181.0 - 35.2 - 45 ALA 45 E B - - - - - - - - - - 179.1 -3.0 34.3 - * * 46 THR 46 E B - - -55.7 - - - - - - - 177.5 -3.2 35.4 - +* +* 47 LEU 47 E B - 175.1 - - - - - - - - 179.4 -3.4 34.5 - +* +* 48 PRO 48 E - - - - - -86.9 - - - - - 180.0 - 38.6 - +* * +* 49 GLY 49 e - - - - - - - - - - - 181.9 -2.8 - - * * 50 PHE 50 t B - - -67.6 - - - - - - - 181.6 -.6 34.4 - +* +* 51 GLN 51 E B - 180.4 - 176.6 - - - - - - 179.2 -2.9 34.3 - * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 52 ARG 52 E B 54.9 - - 177.8 - - - - - - 177.7 - 32.8 - 53 PHE 53 E B - - -80.0 - - - - - - - 192.9 -3.5 32.9 - ** +* ** 54 ARG 54 B 40.8 - - 182.6 - - - - - - 187.6 -.5 32.9 - * * ** ** 55 LEU 55 B B 59.2 - - - - - - - - - 169.2 - 29.5 - +* * +* 56 LYS 56 S a - 192.0 - 177.8 - - - - - - 181.8 -2.3 34.0 - 57 GLY 57 S - - - - - - - - - - - 182.0 -.6 - - +* +* 58 ARG 58 S A 56.2 - - - - - - - - - 182.4 - 31.0 - 59 LEU 59 B - 183.3 - - - - - - - - 187.0 - 32.8 - * * 60 TYR 60 B - - -53.0 - - - - - - - 175.3 - 36.0 - 61 PRO 61 - - - - - -61.8 - - - - - 183.6 - 38.0 - * * 62 CYS 62 E B 52.8 - - - - - - - - - 180.5 -2.4 34.8 - 63 ILE 63 E B - - -58.3 - - - - - - - 171.9 -.6 35.8 - * +* +* 64 VAL 64 E B - - -62.1 - - - - - - - 178.0 -2.1 33.8 - 65 PRO 65 - - - - - -66.8 - - - - - 176.5 - 37.7 - * * 66 SER 66 t B - 183.5 - - - - - - - - 185.8 -.8 35.0 - +* +* 67 GLU 67 T A - - -64.7 - - - - - - - 181.8 - 33.4 - 68 LYS 68 T A - - -59.7 181.6 - - - - - - 180.3 - 34.1 - 69 GLY 69 e - - - - - - - - - - - 178.3 -2.4 - - 70 GLU 70 E B 64.4 - - - - - - - - - 181.9 - 33.2 - 71 VAL 71 E B - 183.9 - - - - - - - - 173.8 -2.3 35.9 - * * 72 HIS 72 E B - - -65.0 - - - - - - - 182.7 - 33.7 - 73 GLY 73 E - - - - - - - - - - - 181.4 -3.2 - - +* +* 74 LYS 74 E B - - -80.4 - - - - - - - 177.5 -.9 32.0 - +* +* 75 VAL 75 E B - 168.1 - - - - - - - - 177.2 -3.2 34.4 - +* +* 76 LEU 76 E B - - -55.6 179.6 - - - - - - 179.6 -3.5 36.8 - +* +* 77 MET 77 E B 55.8 - - 177.9 - - - - - - 184.3 -3.1 32.3 - * * 78 GLY 78 E - - - - - - - - - - - 179.0 -1.2 - - * * 79 VAL 79 E B 67.7 - - - - - - - - - 182.5 -1.9 33.2 - 80 THR 80 h B - - -44.5 - - - - - - - 181.4 - 36.2 - * * 81 SER 81 H A - - -58.1 - - -59.0 -38.3 - - - 178.6 - 33.1 - 82 ASP 82 H A - - -58.2 - - -60.2 -48.8 - - - 179.8 - 35.4 - 83 GLU 83 H A - - -52.6 173.5 - -69.2 -31.6 - - - 176.4 - 36.4 - 84 LEU 84 H A - 180.0 - - - -62.7 -40.1 - - - 176.6 -2.4 33.7 - 85 GLU 85 H A - - -60.2 184.0 - -72.6 -29.5 - - - 176.4 -2.1 33.1 - 86 ASN 86 H A - 133.9 - - - -67.6 -42.1 - - - 174.8 -1.4 32.4 - +** +** 87 LEU 87 H A - - -62.8 175.6 - -61.3 -43.7 - - - 178.6 -2.7 35.0 - 88 ASP 88 H A - 178.3 - - - -65.0 -34.0 - - - 178.4 -2.0 34.0 - 89 ALA 89 H A - - - - - -70.5 -44.0 - - - 181.7 -1.9 34.6 - Residue-by-residue listing for refined_11 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 - 175.3 - - - -72.8 -57.3 - - - 183.4 -2.7 33.0 - +* +* 91 GLU 91 H A - - -62.2 - - -77.4 -22.8 - - - 182.7 -2.9 34.4 - * * * * 92 GLY 92 h - - - - - - - - - - - 182.5 -.8 - - +* +* 93 ASN 93 T A - - -61.9 - - - - - - - 182.7 -.9 32.3 - +* +* 94 GLU 94 e A - - -57.7 179.7 - - - - - - 179.8 -.8 33.7 - +* +* 95 TYR 95 E B - - -61.4 - - - - - - - 176.9 -2.0 35.1 - 96 GLU 96 E B - 184.6 - 181.3 - - - - - - 181.5 -1.8 34.4 - 97 ARG 97 E B - 187.8 - 188.4 - - - - - - 177.1 - 36.1 - 98 VAL 98 E B - - -66.5 - - - - - - - 183.5 -3.0 31.8 - * * 99 THR 99 E B - 190.7 - - - - - - - - 186.9 - 31.9 - * * 100 VAL 100 E B - - -62.4 - - - - - - - 178.5 -3.3 34.5 - +* +* 101 GLY 101 E - - - - - - - - - - - 180.0 - - - 102 ILE 102 E B 54.5 - - - - - - - - - 177.8 -3.3 32.7 - +* +* 103 VAL 103 E B - 182.3 - - - - - - - - 184.2 -2.7 34.9 - 104 ARG 104 E B - - -48.9 197.6 - - - - - - 177.3 -3.2 33.3 - * * +* +* 105 GLU 105 e A - - -59.3 173.6 - - - - - - 179.0 -2.8 35.5 - * * 106 ASP 106 T A - 172.6 - - - - - - - - 185.0 - 36.8 - 107 ASN 107 T a 63.4 - - - - - - - - - 176.4 - 34.5 - 108 SER 108 t l - 181.1 - - - - - - - - 177.7 -1.8 32.0 - 109 GLU 109 e B - - -66.1 - - - - - - - 178.7 - 34.1 - 110 LYS 110 E B 63.2 - - 183.7 - - - - - - 184.6 - 31.8 - 111 MET 111 E B - - -67.9 177.0 - - - - - - 177.1 -3.4 35.3 - +* +* 112 ALA 112 E B - - - - - - - - - - 180.2 - 34.0 - 113 VAL 113 E B - - -59.8 - - - - - - - 176.0 -2.6 34.6 - 114 LYS 114 E B - - -61.6 - - - - - - - 176.9 -2.2 33.0 - 115 THR 115 E B - 188.5 - - - - - - - - 179.0 -2.7 34.0 - 116 TYR 116 E B - - -57.4 - - - - - - - 181.1 - 34.5 - 117 MET 117 E B 63.9 - - 178.1 - - - - - - 181.5 -1.9 32.1 - 118 TRP 118 E B - 191.4 - - - - - - - - 187.2 -3.1 35.1 - * * * 119 ILE 119 e A - - -56.1 - - - - - - - 184.5 -.7 31.6 - +* +* 120 ASN 120 S A - 184.3 - - - - - - - - 176.6 - 33.2 - 121 LYS 121 ~l - - -57.3 173.8 - - - - - - 188.2 - 34.5 - ** * ** 122 ALA 122 a - - - - - - - - - - 180.1 - 33.8 - 123 ASP 123 t B - - -62.6 - - - - - - - 182.4 - 33.3 - 124 PRO 124 T - - - - - -74.3 - - - - - 175.8 - 38.5 - * * 125 ASP 125 T A - - -70.7 - - - - - - - 177.5 - 32.5 - 126 MET 126 B B 54.4 - - - - - - - - - 179.0 -1.5 32.2 - 127 PHE 127 S a - - -59.2 - - - - - - - 186.6 -1.2 35.5 - * * * 128 GLY 128 S - - - - - - - - - - - 180.9 -.8 - - +* +* Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 129 GLU 129 B - - -66.8 174.8 - - - - - - 179.3 - 36.5 - 130 TRP 130 B - 198.9 - - - - - - - - 178.8 - 35.3 - 131 ASN 131 h b - 187.8 - - - - - - - - 183.7 -1.1 31.5 - * * 132 PHE 132 H A - 199.5 - - - -59.4 -43.3 - - - 184.4 -2.3 37.2 - 133 GLU 133 H A 58.8 - - 176.1 - -58.6 -37.9 - - - 180.1 - 33.0 - 134 GLU 134 H A - 189.4 - - - -66.1 -47.5 - - - 179.4 - 34.0 - 135 TRP 135 H A - 176.4 - - - -68.6 -39.3 - - - 178.6 -1.3 32.3 - * * 136 LYS 136 H A - 185.4 - - - -59.0 -33.8 - - - 175.2 -3.3 34.5 - +* +* 137 ARG 137 H A - 167.7 - 180.2 - -62.6 -50.0 - - - 179.3 -1.7 35.2 - 138 LEU 138 H A - - -78.9 - - -68.2 -30.2 - - - 177.9 -1.6 33.2 - 139 HIS 139 H A - 184.5 - - - -68.8 -39.3 - - - 177.0 -2.7 34.4 - 140 LYS 140 H A - 178.1 - 182.6 - -67.3 -45.5 - - - 181.5 -2.1 36.0 - 141 LYS 141 H A - 177.9 - - - -48.5 -39.6 - - - 180.0 -3.0 36.0 - * * * 142 LYS 142 H A - 182.9 - 177.5 - -64.2 -40.1 - - - 178.8 -1.3 33.5 - 143 PHE 143 H A - - -56.6 - - -76.2 -32.2 - - - 180.7 -1.0 34.1 - * * 144 ILE 144 H A - - -58.4 - - -56.5 -33.5 - - - 175.2 -2.4 31.0 - 145 GLU 145 H A - - -72.1 - - -57.3 -31.3 - - - 176.6 -1.2 32.1 - * * 146 THR 146 H A - - -54.8 - - -80.6 -41.9 - - - 181.5 -1.6 35.0 - * * 147 PHE 147 H A - - -72.6 - - -70.9 -30.1 - - - 176.9 -2.1 29.0 - * * 148 LYS 148 H A - - -68.5 175.0 - -55.5 -38.7 - - - 180.3 -3.4 33.6 - +* +* 149 LYS 149 H A - - -55.0 176.8 - -67.3 -38.8 - - - 179.3 -.5 35.9 - ** ** 150 ILE 150 H A - - -58.2 177.6 - -69.9 -41.4 - - - 178.5 -1.0 33.9 - * * 151 MET 151 H A - - -63.8 178.4 - -67.9 -48.5 - - - 181.0 -3.3 34.2 - +* +* 152 GLU 152 H A - - -61.8 191.2 - -62.2 -30.4 - - - 179.0 -3.4 31.8 - +* +* 153 CYS 153 H A - 184.4 - - - -61.6 -42.5 - - - 179.4 -1.4 34.0 - 154 LYS 154 H A - - -61.1 - - -82.7 -45.0 - - - 181.6 -1.1 34.4 - * * * 155 LYS 155 H b - 181.0 - 178.3 - 179.1 110.3 - - - 182.9 -3.4 34.6 - *20.5**13.2* +* *20.5* 156 LYS 156 h B 63.5 - - 175.3 - - - - - - 169.9 -.6 34.4 - +* +* +* 157 PRO 157 - - - - - -64.1 - - - - - 181.7 - 39.0 - * * 158 GLN 158 B 59.6 - - - - - - - - - 183.5 - 30.0 - * * 159 GLY 159 - - - - - - - - - - - 176.9 - - - 160 GLN 160 b 56.6 - - 177.0 - - - - - - 178.7 -2.1 32.3 - 161 GLY 161 - - - - - - - - - - - 177.6 -1.3 - - 162 ASN 162 B - 175.9 - - - - - - - - 179.4 - 34.0 - 163 ASP 163 b - - -65.6 - - - - - - - 178.3 -.6 32.6 - +* +* 164 ASP 164 B - 179.9 - - - - - - - - 177.6 -1.0 34.1 - * * 165 ILE 165 b - 179.9 - 177.5 - - - - - - 181.6 - 33.0 - Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 166 SER 166 B 53.3 - - - - - - - - - 177.8 - 32.6 - 167 HIS 167 B - - -78.1 - - - - - - - 170.2 -.5 34.8 - +* ** ** 168 VAL 168 B 50.8 - - - - - - - - - 183.5 - 31.8 - 169 LEU 169 b - 180.6 - - - - - - - - 181.3 -.8 34.0 - +* +* 170 ARG 170 b - 188.1 - - - - - - - - 177.1 - 33.7 - 171 GLU 171 b - - -70.0 - - - - - - - 180.6 - 33.1 - 172 ASP 172 ~l - - -61.4 - - - - - - - 176.8 - 31.4 - ** ** 173 GLN 173 - - 180.6 - 178.1 - - - - - - - - 33.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +** * * +**20.5**13.2* ** ** * *20.5* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.1 182.3 -62.0 178.3 -68.9 -60.3 -35.2 - - - 180.1 -2.0 34.0 Standard deviations: 6.0 9.5 7.6 6.4 10.4 38.6 24.1 - - - 4.0 .9 1.9 Numbers of values: 30 55 65 43 7 42 42 0 0 0 172 101 161 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_11 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 1.493 - 1.454 - 117.17 120.16 - 110.34 - 122.67 * * 2 HIS 2 1.309 1.231 1.503 1.538 1.445 120.98 115.71 121.19 110.38 112.54 113.02 123.06 * * * * 3 HIS 3 1.305 1.233 1.514 1.536 1.436 121.41 115.14 121.39 112.05 105.45 110.76 123.37 +* * * ** ** 4 HIS 4 1.301 1.223 1.508 1.550 1.441 121.86 113.69 121.87 111.18 115.16 111.67 124.43 +* * * +* 5 HIS 5 1.299 1.234 1.498 1.546 1.445 126.24 117.14 118.74 109.21 105.76 113.89 124.11 ** * +** * +* +* +** 6 HIS 6 1.324 1.230 1.542 1.551 1.471 123.71 115.32 121.20 113.45 109.23 111.13 123.45 * * +* +* 7 HIS 7 1.329 1.236 1.504 1.561 1.484 124.75 114.85 121.27 110.17 109.39 117.05 123.77 * +* * +* +*** +*** 8 LEU 8 1.309 1.241 1.508 1.544 1.443 123.43 115.48 120.03 108.17 109.50 110.75 124.47 * * * 9 GLU 9 1.327 1.242 1.537 1.544 1.470 125.02 117.24 120.52 111.49 113.92 110.92 122.24 +* +* 10 CYS 10 1.311 1.237 1.525 1.543 1.431 120.90 115.96 120.72 110.23 110.28 107.72 123.31 * * +* +* 11 SER 11 1.316 1.248 1.542 1.544 1.442 122.86 117.76 119.65 111.12 107.02 108.49 122.59 * * * Residue-by-residue listing for refined_11 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 1.330 1.234 1.526 1.539 1.454 121.71 114.17 121.82 111.01 108.53 109.87 123.99 * * 13 ASP 13 1.314 1.235 1.494 1.534 1.434 123.90 116.61 120.36 108.21 108.64 110.33 123.03 * * * * * 14 SER 14 1.292 1.234 1.524 1.541 1.418 120.77 114.11 121.38 112.49 106.25 110.51 124.39 +** ** * * +* +** 15 LEU 15 1.336 1.238 1.534 1.498 1.413 125.38 115.50 121.77 113.98 110.54 110.80 122.57 +* ** ** ** ** 16 GLN 16 1.314 1.246 1.511 1.543 1.453 121.75 115.62 121.24 109.11 111.48 111.69 123.14 * * 17 LEU 17 1.305 1.246 1.494 1.518 1.410 121.70 115.80 121.14 110.17 108.40 113.24 123.06 +* * +** * +* +** 18 HIS 18 1.274 1.247 1.493 1.524 1.426 120.71 114.94 121.01 110.01 110.07 110.59 124.03 +*** * +* +*** 19 ASN 19 1.291 1.239 1.515 1.543 1.419 123.17 114.76 121.89 114.13 111.50 111.89 123.31 +** ** ** +** 20 VAL 20 1.303 1.225 1.520 1.572 1.443 123.32 116.59 120.35 109.23 109.50 110.21 123.06 +* * +* 21 PHE 21 1.298 1.232 1.517 1.541 1.440 122.23 116.65 120.66 111.52 107.54 108.97 122.66 ** * ** 22 VAL 22 1.306 1.234 1.522 1.559 1.431 120.51 115.18 121.32 112.05 111.55 113.08 123.50 +* * * +* 23 TYR 23 1.309 1.239 1.541 1.540 1.437 122.39 118.07 120.13 111.56 113.88 109.58 121.79 * * * 24 GLY 24 1.330 1.227 1.508 - 1.446 118.11 117.60 119.63 - 115.39 - 122.76 * * 25 SER 25 1.327 1.227 1.526 1.515 1.470 121.74 115.83 121.22 108.49 111.60 109.56 122.91 26 PHE 26 1.306 1.221 1.508 1.520 1.442 121.79 116.03 120.91 110.04 110.81 109.18 122.98 +* +* 27 GLN 27 1.318 1.237 1.575 1.541 1.468 123.33 116.17 121.63 111.04 110.76 107.44 122.14 ** +* ** 28 ASP 28 1.307 1.217 1.526 1.528 1.439 123.71 118.55 120.00 110.20 109.31 109.45 121.44 +* * * * +* 29 PRO 29 1.343 1.228 1.530 1.519 1.465 122.22 116.83 120.69 110.41 113.19 103.62 122.47 30 ASP 30 1.319 1.234 1.528 1.530 1.454 121.40 116.55 120.83 111.78 111.00 111.04 122.60 31 VAL 31 1.328 1.242 1.548 1.574 1.463 120.83 115.94 121.16 111.58 110.04 113.46 122.86 * * * * * 32 ILE 32 1.344 1.238 1.536 1.559 1.459 123.12 115.77 120.76 110.09 110.31 110.14 123.39 * * 33 ASN 33 1.337 1.229 1.511 1.551 1.474 122.88 114.70 121.66 106.34 110.28 111.50 123.64 * +* +* 34 VAL 34 1.305 1.241 1.533 1.557 1.440 122.77 117.09 120.21 110.29 113.25 110.73 122.70 +* +* 35 MET 35 1.334 1.227 1.536 1.539 1.456 120.91 117.38 120.50 111.50 111.10 109.52 122.04 36 LEU 36 1.316 1.240 1.508 1.566 1.443 119.66 116.55 119.61 112.50 111.36 115.00 123.74 +* * * +** +** 37 ASP 37 1.336 1.228 1.501 1.540 1.474 123.11 115.21 121.26 107.31 109.51 112.20 123.52 * * * * 38 ARG 38 1.309 1.228 1.505 1.536 1.444 121.77 116.51 120.11 109.09 109.67 109.57 123.37 * * 39 THR 39 1.304 1.244 1.523 1.535 1.427 121.17 117.02 120.47 109.58 108.46 111.37 122.39 +* +* +* 40 PRO 40 1.340 1.243 1.531 1.533 1.463 123.36 115.93 120.73 110.16 111.92 103.22 123.28 41 GLU 41 1.314 1.235 1.527 1.531 1.440 122.45 116.04 121.00 112.17 108.25 109.83 122.95 * * * * Residue-by-residue listing for refined_11 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 42 ILE 42 1.296 1.236 1.517 1.553 1.436 121.63 116.01 120.89 108.63 110.10 110.05 123.09 ** * ** 43 VAL 43 1.299 1.229 1.528 1.564 1.445 122.35 117.17 120.20 110.00 109.72 111.63 122.62 ** ** 44 SER 44 1.309 1.242 1.530 1.522 1.437 121.40 116.50 120.68 110.34 108.80 109.44 122.79 * * * 45 ALA 45 1.301 1.224 1.508 1.508 1.436 122.20 115.29 121.63 110.03 111.14 110.26 123.08 ** * ** 46 THR 46 1.279 1.221 1.516 1.538 1.419 122.65 116.23 120.36 109.51 109.00 110.36 123.38 +*** ** +*** 47 LEU 47 1.294 1.222 1.525 1.541 1.435 122.80 117.95 120.17 110.95 109.52 109.89 121.81 ** * ** 48 PRO 48 1.336 1.245 1.533 1.531 1.449 122.34 116.31 120.75 111.12 111.82 102.88 122.93 * * 49 GLY 49 1.314 1.236 1.505 - 1.446 120.90 115.47 121.34 - 111.23 - 123.17 * * 50 PHE 50 1.310 1.213 1.481 1.542 1.432 123.56 116.89 120.01 109.93 107.63 111.94 123.09 * ** * * * ** 51 GLN 51 1.279 1.242 1.488 1.535 1.422 121.05 115.63 120.60 111.23 108.63 110.41 123.71 +*** +* +* +*** 52 ARG 52 1.298 1.240 1.494 1.547 1.413 121.05 115.36 121.43 111.43 109.54 112.28 123.21 ** * ** * ** 53 PHE 53 1.275 1.214 1.475 1.528 1.400 121.35 114.28 121.69 112.73 107.40 111.57 124.03 +*** ** *** * * +*** 54 ARG 54 1.272 1.243 1.502 1.529 1.419 122.68 113.95 120.89 113.59 113.27 108.36 125.16 **** * ** * +* * * **** 55 LEU 55 1.317 1.230 1.510 1.579 1.441 124.56 113.43 122.26 111.99 116.39 113.00 124.28 ** +* * +* * ** 56 LYS 56 1.302 1.231 1.535 1.542 1.436 124.34 112.89 123.04 112.20 104.43 110.84 124.06 +* * * +* * * ** ** 57 GLY 57 1.329 1.235 1.518 - 1.437 124.55 117.74 119.51 - 108.98 - 122.69 ** * ** 58 ARG 58 1.322 1.226 1.540 1.567 1.466 121.20 117.96 120.37 112.28 113.80 111.74 121.51 +* * +* 59 LEU 59 1.311 1.230 1.523 1.551 1.455 119.55 116.00 120.77 111.79 109.75 111.40 123.23 * * * * 60 TYR 60 1.300 1.240 1.525 1.540 1.443 123.26 118.32 119.55 110.37 109.72 108.16 122.08 ** * * ** 61 PRO 61 1.360 1.225 1.523 1.534 1.459 122.19 115.36 120.98 110.88 110.76 104.33 123.62 * * * * * 62 CYS 62 1.297 1.226 1.525 1.533 1.429 123.41 116.84 120.59 111.71 110.49 108.34 122.55 ** +* * ** 63 ILE 63 1.312 1.217 1.513 1.567 1.455 121.63 117.09 119.87 108.22 109.40 111.02 122.98 * * 64 VAL 64 1.308 1.242 1.528 1.577 1.457 122.31 118.18 119.89 108.81 107.96 113.76 121.88 +* * * * +* 65 PRO 65 1.332 1.236 1.528 1.528 1.460 122.54 115.02 121.67 110.99 112.54 104.15 123.21 * * * 66 SER 66 1.292 1.228 1.508 1.538 1.420 123.70 116.31 120.26 111.30 106.11 109.91 123.39 +** +* * +* +** 67 GLU 67 1.313 1.237 1.524 1.535 1.469 123.22 115.83 121.01 109.81 112.72 111.29 123.14 * * 68 LYS 68 1.312 1.231 1.529 1.524 1.441 122.25 117.04 120.79 110.69 111.73 109.87 122.16 * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 69 GLY 69 1.313 1.244 1.515 - 1.436 120.23 114.95 121.09 - 113.37 - 123.96 * * 70 GLU 70 1.308 1.236 1.522 1.553 1.438 124.82 117.04 120.37 110.57 108.00 112.85 122.57 * * * +* * * +* 71 VAL 71 1.300 1.223 1.503 1.551 1.445 121.69 117.25 120.27 107.43 110.01 111.35 122.47 ** * ** 72 HIS 72 1.296 1.233 1.502 1.540 1.438 120.03 115.86 120.96 110.62 107.64 112.05 123.18 ** * * * ** 73 GLY 73 1.290 1.232 1.475 - 1.415 121.06 117.09 120.09 - 109.80 - 122.82 +** ** ** +** 74 LYS 74 1.285 1.230 1.490 1.540 1.432 120.69 113.86 121.81 110.00 112.55 113.39 124.33 *** +* * * +* *** 75 VAL 75 1.287 1.230 1.517 1.551 1.434 123.48 114.63 120.99 109.36 111.13 111.32 124.38 +** * +** 76 LEU 76 1.310 1.229 1.520 1.542 1.436 124.34 117.26 120.05 108.17 107.72 109.70 122.65 * * * * * * 77 MET 77 1.299 1.222 1.508 1.534 1.458 121.26 116.93 120.54 111.67 111.05 111.63 122.53 ** ** 78 GLY 78 1.307 1.229 1.514 - 1.430 119.64 116.52 120.68 - 111.50 - 122.80 +* * +* 79 VAL 79 1.325 1.253 1.543 1.578 1.453 120.85 117.13 120.29 111.24 109.02 111.84 122.56 * * * 80 THR 80 1.320 1.228 1.550 1.536 1.422 122.26 117.69 120.07 110.17 109.29 108.19 122.24 * +* +* +* 81 SER 81 1.329 1.230 1.546 1.521 1.460 122.06 116.66 120.38 111.52 112.58 109.87 122.93 82 ASP 82 1.327 1.233 1.526 1.537 1.474 122.79 114.96 121.51 109.39 110.19 109.72 123.51 83 GLU 83 1.314 1.205 1.544 1.521 1.459 124.15 116.42 121.21 110.16 109.23 107.39 122.36 * * * +* +* 84 LEU 84 1.327 1.238 1.535 1.569 1.469 122.67 116.12 121.04 113.00 109.44 109.17 122.84 +* +* +* 85 GLU 85 1.324 1.209 1.516 1.520 1.450 121.29 115.80 120.91 110.90 109.90 111.60 123.28 * * 86 ASN 86 1.316 1.224 1.526 1.542 1.454 122.80 116.33 120.56 113.10 110.97 110.17 123.09 +* +* 87 LEU 87 1.317 1.238 1.518 1.537 1.459 122.45 114.96 121.34 109.65 108.99 110.46 123.66 88 ASP 88 1.328 1.219 1.523 1.538 1.459 122.80 116.07 121.19 111.06 110.56 110.09 122.73 89 ALA 89 1.308 1.224 1.523 1.520 1.444 122.63 116.28 120.58 110.00 111.02 109.96 123.13 * * 90 VAL 90 1.316 1.242 1.546 1.558 1.455 122.60 116.70 120.67 110.83 112.86 110.97 122.60 91 GLU 91 1.322 1.232 1.525 1.529 1.472 122.28 115.20 121.31 110.30 111.41 109.79 123.47 92 GLY 92 1.315 1.234 1.519 - 1.452 123.08 117.59 120.16 - 115.00 - 122.20 * * 93 ASN 93 1.322 1.236 1.516 1.540 1.462 120.37 117.00 120.53 109.86 112.25 112.96 122.46 * * 94 GLU 94 1.311 1.231 1.518 1.521 1.455 120.34 116.13 120.87 110.88 111.80 110.12 123.00 * * 95 TYR 95 1.309 1.225 1.513 1.533 1.448 122.49 117.62 120.02 109.30 108.61 110.80 122.34 * * 96 GLU 96 1.304 1.243 1.511 1.533 1.444 120.12 116.17 120.33 110.07 109.21 110.94 123.50 +* +* 97 ARG 97 1.318 1.237 1.510 1.531 1.431 122.02 116.12 120.92 108.58 108.84 110.14 122.95 * * 98 VAL 98 1.288 1.243 1.492 1.541 1.429 121.72 116.25 120.61 110.96 110.14 113.70 123.14 +** +* +* * +** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 THR 99 1.288 1.236 1.536 1.578 1.433 120.31 116.23 121.06 113.65 108.50 111.73 122.65 +** * * ** +** 100 VAL 100 1.310 1.236 1.515 1.552 1.450 122.12 115.87 120.90 108.96 111.48 111.33 123.22 * * 101 GLY 101 1.301 1.232 1.506 - 1.427 121.27 116.18 120.47 - 111.53 - 123.35 +* +* +* 102 ILE 102 1.301 1.208 1.503 1.579 1.445 123.14 117.17 120.17 111.53 110.17 112.16 122.65 ** * * * * ** 103 VAL 103 1.288 1.227 1.493 1.551 1.441 122.07 117.71 119.74 109.55 106.76 111.78 122.54 +** +* +* +** 104 ARG 104 1.311 1.229 1.502 1.533 1.433 119.03 115.35 121.00 108.77 110.36 113.53 123.57 * * * * +* +* 105 GLU 105 1.307 1.223 1.543 1.525 1.460 123.61 113.03 122.92 111.22 108.16 108.00 124.05 +* * +* * * * +* 106 ASP 106 1.300 1.233 1.529 1.535 1.450 126.56 116.17 121.05 109.25 111.23 107.63 122.78 ** +** +* +** 107 ASN 107 1.319 1.229 1.523 1.538 1.464 121.36 115.79 120.68 110.16 112.03 109.75 123.52 108 SER 108 1.331 1.226 1.541 1.554 1.463 124.18 117.14 120.59 112.49 112.54 110.74 122.26 * * * * 109 GLU 109 1.318 1.247 1.492 1.518 1.445 120.73 115.79 120.79 109.20 110.25 111.90 123.42 +* +* 110 LYS 110 1.293 1.235 1.511 1.529 1.410 120.94 115.18 121.43 112.68 109.76 112.00 123.37 +** +** * +** 111 MET 111 1.286 1.218 1.468 1.513 1.441 123.48 114.68 121.30 107.51 111.27 111.68 124.02 *** +** * *** 112 ALA 112 1.270 1.245 1.509 1.511 1.426 121.75 115.81 120.52 110.56 109.08 111.00 123.67 **** +* **** 113 VAL 113 1.310 1.233 1.513 1.566 1.453 123.32 117.33 120.34 108.34 108.44 112.90 122.33 * * 114 LYS 114 1.297 1.226 1.510 1.553 1.442 120.23 116.90 120.29 110.23 109.24 113.10 122.78 ** * +* ** 115 THR 115 1.298 1.241 1.512 1.571 1.435 121.31 116.16 120.58 109.65 108.20 112.77 123.27 ** * * * ** 116 TYR 116 1.293 1.236 1.502 1.523 1.423 122.11 116.24 120.60 110.89 108.48 110.32 123.12 +** * +* +** 117 MET 117 1.299 1.245 1.509 1.543 1.440 121.07 115.26 120.60 111.19 110.52 112.73 124.12 ** * ** 118 TRP 118 1.309 1.234 1.520 1.527 1.437 123.50 116.50 120.41 111.14 108.70 108.97 123.09 * * * * 119 ILE 119 1.315 1.240 1.537 1.587 1.460 121.13 116.88 120.43 109.48 112.59 114.42 122.68 +* +* +* 120 ASN 120 1.327 1.223 1.530 1.525 1.479 121.06 116.10 120.58 110.05 111.69 111.46 123.33 * * 121 LYS 121 1.333 1.232 1.559 1.552 1.491 124.22 119.03 119.58 108.34 114.15 110.69 121.38 +* * +* * * * * +* 122 ALA 122 1.333 1.233 1.538 1.521 1.473 119.46 117.76 119.86 110.13 115.03 109.33 122.36 * * * 123 ASP 123 1.321 1.227 1.520 1.531 1.483 121.14 117.73 120.30 109.93 111.30 111.61 121.97 * * 124 PRO 124 1.348 1.233 1.541 1.525 1.478 123.50 117.04 121.04 110.33 113.92 103.10 121.92 125 ASP 125 1.309 1.240 1.500 1.521 1.457 120.94 115.20 121.40 110.54 110.52 112.56 123.41 * * * * 126 MET 126 1.305 1.223 1.511 1.556 1.423 122.76 116.95 120.56 113.22 109.24 111.37 122.34 +* * +* +* +* Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 127 PHE 127 1.302 1.218 1.500 1.530 1.470 120.61 115.72 121.13 107.93 110.41 111.02 123.14 +* * * +* 128 GLY 128 1.306 1.216 1.505 - 1.444 119.89 114.73 121.83 - 109.53 - 123.38 +* * +* 129 GLU 129 1.304 1.226 1.477 1.516 1.435 124.39 116.95 119.67 108.02 107.28 110.42 123.37 +* ** * * * * ** 130 TRP 130 1.282 1.249 1.507 1.533 1.417 120.37 117.68 119.72 110.98 106.46 109.65 122.54 *** ** +* *** 131 ASN 131 1.309 1.236 1.528 1.539 1.446 120.40 113.49 122.38 112.69 109.69 112.33 123.92 * * * * * 132 PHE 132 1.319 1.221 1.513 1.515 1.413 126.05 116.15 120.37 109.62 111.89 106.67 123.48 ** ** ** ** 133 GLU 133 1.326 1.229 1.525 1.522 1.464 122.45 116.60 120.50 110.41 112.82 111.04 122.90 134 GLU 134 1.313 1.217 1.527 1.528 1.454 121.15 116.77 120.86 110.07 109.63 111.18 122.34 * * 135 TRP 135 1.322 1.222 1.520 1.528 1.452 120.65 116.50 120.53 111.49 111.03 111.68 122.94 136 LYS 136 1.326 1.233 1.535 1.536 1.460 122.43 115.01 121.35 110.82 109.37 109.86 123.62 137 ARG 137 1.320 1.219 1.524 1.512 1.451 123.97 116.66 120.51 109.93 111.37 109.01 122.83 * * 138 LEU 138 1.322 1.232 1.512 1.537 1.466 121.63 115.28 121.24 110.29 110.62 111.84 123.45 139 HIS 139 1.306 1.224 1.527 1.540 1.451 121.87 115.14 121.18 110.81 108.71 110.26 123.66 +* +* 140 LYS 140 1.320 1.221 1.520 1.531 1.451 123.85 114.76 120.94 109.70 109.37 108.72 124.26 * * * 141 LYS 141 1.329 1.241 1.530 1.546 1.471 125.77 115.88 120.69 109.83 111.67 108.03 123.42 ** * ** 142 LYS 142 1.318 1.233 1.535 1.526 1.442 122.18 116.62 120.66 111.44 111.17 110.08 122.70 143 PHE 143 1.323 1.235 1.514 1.533 1.458 121.64 115.41 121.03 109.21 109.50 112.00 123.56 144 ILE 144 1.327 1.196 1.533 1.570 1.452 122.81 118.27 119.68 112.15 111.82 112.87 122.01 +* * * * +* 145 GLU 145 1.333 1.227 1.534 1.529 1.483 120.57 116.33 121.02 110.71 111.95 112.23 122.64 * * * 146 THR 146 1.309 1.235 1.549 1.542 1.432 121.66 115.59 121.57 110.55 108.97 109.58 122.80 * * * * * 147 PHE 147 1.327 1.209 1.509 1.520 1.452 122.46 117.95 119.37 112.39 115.28 113.13 122.68 * * * +* +* 148 LYS 148 1.319 1.208 1.511 1.529 1.464 121.75 115.88 120.69 109.85 110.68 111.63 123.36 * * 149 LYS 149 1.318 1.233 1.524 1.525 1.459 122.70 114.78 121.75 109.75 109.33 108.79 123.46 * * 150 ILE 150 1.312 1.238 1.544 1.571 1.443 123.11 115.85 121.17 111.89 109.68 109.97 122.92 * * * * 151 MET 151 1.320 1.230 1.516 1.536 1.457 122.62 116.77 120.14 109.30 111.04 111.33 123.07 152 GLU 152 1.338 1.223 1.509 1.541 1.460 121.87 116.41 120.31 110.36 111.93 113.29 123.28 +* +* 153 CYS 153 1.319 1.235 1.540 1.535 1.444 121.85 116.67 120.79 110.87 110.33 110.24 122.54 154 LYS 154 1.325 1.229 1.523 1.533 1.458 120.99 115.64 120.56 109.47 110.87 110.89 123.79 155 LYS 155 1.325 1.236 1.525 1.544 1.462 123.99 116.58 120.72 110.03 108.58 110.78 122.68 * * 156 LYS 156 1.307 1.241 1.518 1.543 1.452 121.29 117.16 120.65 108.55 111.91 111.70 122.16 +* +* 157 PRO 157 1.345 1.254 1.526 1.539 1.454 121.94 117.07 119.85 110.21 108.88 103.86 123.06 * * * 158 GLN 158 1.317 1.243 1.527 1.561 1.447 120.52 115.52 120.77 114.51 111.38 111.96 123.67 +* ** ** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 159 GLY 159 1.318 1.240 1.506 - 1.439 122.33 115.88 120.87 - 113.23 - 123.25 * * 160 GLN 160 1.305 1.236 1.530 1.544 1.433 122.06 115.57 121.75 112.09 110.45 111.56 122.58 +* * * +* 161 GLY 161 1.302 1.240 1.498 - 1.430 120.48 116.69 120.12 - 110.83 - 123.17 +* * +* 162 ASN 162 1.297 1.241 1.517 1.536 1.443 121.76 116.49 120.85 110.66 109.86 110.77 122.63 ** ** 163 ASP 163 1.311 1.233 1.499 1.543 1.448 121.03 115.87 120.80 110.02 110.43 113.30 123.28 * * +* +* 164 ASP 164 1.306 1.231 1.504 1.534 1.449 122.01 115.66 120.42 109.74 109.92 111.46 123.88 +* * +* 165 ILE 165 1.307 1.238 1.524 1.574 1.441 123.96 117.01 120.31 111.15 108.00 112.78 122.63 +* * * * +* 166 SER 166 1.305 1.236 1.536 1.530 1.434 121.42 115.42 121.62 112.46 112.01 110.05 122.91 +* * * +* 167 HIS 167 1.308 1.234 1.479 1.539 1.446 123.07 115.78 120.60 106.86 110.74 113.31 123.62 * ** +* +* ** 168 VAL 168 1.295 1.230 1.503 1.548 1.420 120.50 115.09 121.52 112.01 108.21 113.52 123.34 ** * ** * * * ** 169 LEU 169 1.268 1.231 1.503 1.541 1.427 122.13 115.08 120.91 111.52 109.35 110.25 123.94 **** * +* **** 170 ARG 170 1.310 1.232 1.497 1.567 1.439 123.85 115.33 120.95 111.37 106.99 111.89 123.55 * * +* * +* +* 171 GLU 171 1.291 1.241 1.515 1.548 1.429 121.43 116.57 119.57 111.54 108.75 111.75 123.85 +** +* +** 172 ASP 172 1.322 1.241 1.507 1.555 1.474 124.25 115.50 121.37 109.96 111.56 114.44 123.10 * * ** ** 173 GLN 173 1.301 - 1.517 1.531 1.430 121.68 - - 111.41 108.61 110.83 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* +** ** *** +** +* * ** ** +*** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 1.268 1.344 1.310 .015 **** * * C-N (Pro) 1.341 .016 7 1.332 1.360 1.343 .008 * C-O C-O 1.231 .020 172 1.196 1.254 1.232 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.468 1.575 1.519 .017 +** ** CH2G*-C (Gly) 1.516 .018 12 1.475 1.519 1.505 .012 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.508 1.521 1.515 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.535 1.587 1.561 .014 +* CH1E-CH2E (the rest) 1.530 .020 128 1.498 1.579 1.536 .013 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.400 1.491 1.446 .017 *** +* NH1-CH2G* (Gly) 1.451 .016 12 1.415 1.454 1.438 .011 ** N-CH1E (Pro) 1.466 .015 7 1.449 1.478 1.461 .008 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 2.0 153 112.89 119.03 116.12 1.11 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.73 117.74 116.47 .99 CH1E-C-N (Pro) 116.9 1.5 7 115.02 117.07 116.22 .76 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.38 125.16 123.08 .65 * * O-C-N (Pro) 122.0 1.4 7 121.92 123.62 122.93 .52 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.03 126.56 122.24 1.41 * +** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.11 124.55 121.05 1.68 * ** C-N-CH1E (Pro) 122.6 5.0 7 121.94 123.50 122.58 .56 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.74 123.04 120.77 .65 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.51 121.83 120.50 .66 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.00 110.56 110.18 .23 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.43 113.65 110.24 1.40 ** CH2E-CH1E-C (the rest) 110.1 1.9 128 106.34 114.51 110.62 1.46 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.43 116.39 110.15 1.96 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 108.98 115.39 111.73 2.01 * N-CH1E-C (Pro) 111.8 2.5 7 108.88 113.92 111.86 1.54 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.33 111.00 110.14 .60 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.19 114.42 111.69 1.45 +* +* N-CH1E-CH2E (Pro) 103.0 1.1 7 102.88 104.33 103.59 .51 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.67 117.05 110.88 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_11 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] 125 81.7% Residues in additional allowed regions [a,b,l,p] 22 14.4% Residues in generously allowed regions [~a,~b,~l,~p] 5 3.3% Residues in disallowed regions [XX] 1 .7% ---- ------ 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 81.7 83.8 10.0 -.2 Inside b. Omega angle st dev 172 4.0 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 101 .9 .8 .2 .6 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 30 6.0 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 55 9.5 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 65 7.6 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 150 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 43 6.4 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% 81.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_11 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.57 Chi1-chi2 distribution -.29 Chi1 only -.19 Chi3 & chi4 .47 Omega -.11 ------ -.22 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .36 ------ .18 ===== OVERALL AVERAGE -.08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.