Residue-by-residue listing for refined_19 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 - - - - - - - - - - - 180.7 - - - 2 HIS 2 b - 178.1 - - - - - - - - 174.4 - 33.7 - 3 HIS 3 B - - -65.7 - - - - - - - 185.2 - 33.1 - 4 HIS 4 B 49.1 - - - - - - - - - 182.5 - 33.1 - 5 HIS 5 b - 180.2 - - - - - - - - 173.6 - 33.2 - * * 6 HIS 6 S b 63.0 - - - - - - - - - 186.1 - 30.9 - * * 7 HIS 7 b 58.8 - - - - - - - - - 169.5 - 27.9 - +* +* +* 8 LEU 8 A - - -64.1 179.2 - - - - - - 172.4 -1.7 34.8 - * * 9 GLU 9 S b - 179.9 - 182.5 - - - - - - 183.2 - 36.6 - 10 CYS 10 B 52.2 - - - - - - - - - 178.7 -.8 32.7 - +* +* 11 SER 11 a - - -57.1 - - - - - - - 181.8 - 35.3 - 12 SER 12 A - - -50.8 - - - - - - - 181.9 - 36.7 - * * 13 ASP 13 l - 179.4 - - - - - - - - 181.0 - 31.1 - 14 SER 14 S b - - -60.0 - - - - - - - 177.1 - 35.8 - 15 LEU 15 S a - - -67.7 - - - - - - - 176.2 - 33.0 - 16 GLN 16 S ~p - - -54.2 178.0 - - - - - - 172.1 - 35.6 - ** * ** 17 LEU 17 B - - -58.3 - - - - - - - 183.4 - 33.7 - 18 HIS 18 E B - - -57.5 - - - - - - - 176.4 -3.0 35.8 - * * 19 ASN 19 E B - - -52.3 - - - - - - - 182.9 - 34.4 - 20 VAL 20 E B - 178.9 - - - - - - - - 177.4 -2.6 35.1 - Residue-by-residue listing for refined_19 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 21 PHE 21 E B - 178.0 - - - - - - - - 183.1 -3.0 34.6 - * * 22 VAL 22 E B 63.8 - - - - - - - - - 183.8 -3.3 32.6 - +* +* 23 TYR 23 a 57.2 - - - - - - - - - 185.4 - 32.8 - 24 GLY 24 t - - - - - - - - - - - 187.6 - - - * * 25 SER 25 T A - - -49.3 - - - - - - - 183.0 - 35.9 - * * 26 PHE 26 T a - - -50.9 - - - - - - - 186.4 - 36.4 - * * * 27 GLN 27 t A - 182.7 - 183.1 - - - - - - 183.6 -2.0 35.2 - 28 ASP 28 h B - 176.8 - - - - - - - - 181.2 - 33.9 - 29 PRO 29 H - - - - - -60.2 -60.2 -28.3 - - - 179.6 - 37.9 - * * 30 ASP 30 H A - 175.9 - - - -70.6 -41.7 - - - 177.2 - 32.2 - 31 VAL 31 H A 67.8 - - - - -66.0 -28.5 - - - 175.1 - 30.4 - * * 32 ILE 32 H A - - -65.6 - - -61.6 -46.7 - - - 177.6 -1.5 34.5 - 33 ASN 33 H A - - -73.8 - - -61.0 -32.1 - - - 179.2 -1.9 33.0 - 34 VAL 34 H A - 181.4 - - - -81.7 -39.0 - - - 186.4 -1.5 33.4 - * * * 35 MET 35 H A - 204.7 - - - -74.7 -36.8 - - - 176.8 -3.1 34.3 - * * * 36 LEU 36 h a 45.5 - - 166.7 - - - - - - 177.0 -2.7 27.9 - * +* +* 37 ASP 37 t ~b - 179.2 - - - - - - - - 183.7 -1.1 33.1 - ** * ** 38 ARG 38 S B - - -64.5 - - - - - - - 180.1 - 34.3 - 39 THR 39 B - - -43.1 - - - - - - - 172.1 - 36.2 - +* * +* 40 PRO 40 - - - - - -67.5 - - - - - 178.7 - 39.1 - * * 41 GLU 41 E B - 182.4 - 181.2 - - - - - - 183.5 -.9 32.5 - * * 42 ILE 42 E B - - -53.9 178.0 - - - - - - 177.2 - 35.8 - 43 VAL 43 E B 63.0 - - - - - - - - - 178.6 -2.3 33.2 - 44 SER 44 E B - - -56.1 - - - - - - - 181.3 - 35.1 - 45 ALA 45 E B - - - - - - - - - - 180.5 -2.0 34.2 - 46 THR 46 E B - - -60.5 - - - - - - - 177.7 -3.1 34.7 - * * 47 LEU 47 E B - 173.0 - - - - - - - - 179.4 -3.4 35.1 - +* +* 48 PRO 48 E - - - - - -78.3 - - - - - 178.5 - 38.3 - * * * 49 GLY 49 E - - - - - - - - - - - 181.9 -3.4 - - +* +* 50 PHE 50 E B - - -67.7 - - - - - - - 179.2 -.8 33.6 - +* +* 51 GLN 51 E B 57.9 - - 188.5 - - - - - - 187.4 -2.9 33.6 - * * * 52 ARG 52 E B - 176.6 - 179.1 - - - - - - 177.6 - 35.3 - 53 PHE 53 E B - - -71.3 - - - - - - - 180.8 -2.5 33.0 - 54 ARG 54 B 43.3 - - 131.6 - - - - - - 180.8 -2.8 33.6 - * ** * ** 55 LEU 55 B - 183.4 - - - - - - - - 180.2 - 35.1 - 56 LYS 56 B 58.5 - - 182.5 - - - - - - 180.3 - 34.0 - Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 GLY 57 S - - - - - - - - - - - 178.1 - - - 58 ARG 58 S A 71.9 - - - - - - - - - 178.2 -.5 32.8 - +* +* 59 LEU 59 S B - 184.3 - - - - - - - - 191.8 - 31.9 - ** ** 60 TYR 60 B - - -44.7 - - - - - - - 166.7 - 39.4 - * ** +* ** 61 PRO 61 S - - - - - -59.6 - - - - - 185.9 - 38.6 - * * * 62 CYS 62 E B 57.8 - - - - - - - - - 178.9 -.8 34.4 - +* +* 63 ILE 63 E B - - -58.7 - - - - - - - 175.1 - 35.9 - 64 VAL 64 E B - - -65.5 - - - - - - - 177.4 -2.0 34.1 - 65 PRO 65 E - - - - - -58.5 - - - - - 182.2 - 37.8 - * * 66 SER 66 E B - 185.3 - - - - - - - - 181.8 -2.1 35.0 - 67 GLU 67 E A - - -54.4 176.2 - - - - - - 173.6 - 34.2 - * * 68 LYS 68 E b - - -61.4 190.5 - - - - - - 179.5 - 32.4 - 69 GLY 69 E - - - - - - - - - - - 178.5 -.5 - - +* +* 70 GLU 70 E B 55.6 - - 180.6 - - - - - - 182.6 - 33.8 - 71 VAL 71 E B - 182.2 - - - - - - - - 177.2 -2.9 35.4 - * * 72 HIS 72 E B - - -62.6 - - - - - - - 183.1 -.6 34.1 - +* +* 73 GLY 73 E - - - - - - - - - - - 183.9 -3.3 - - +* +* 74 LYS 74 E B - - -61.2 - - - - - - - 174.1 -1.6 35.3 - * * 75 VAL 75 E B - 166.1 - - - - - - - - 177.4 -3.3 34.1 - * +* +* 76 LEU 76 E B - - -55.8 179.3 - - - - - - 178.4 -3.5 36.4 - +* +* 77 MET 77 E B 56.5 - - 173.6 - - - - - - 184.9 -3.1 31.8 - * * 78 GLY 78 E - - - - - - - - - - - 178.5 -1.6 - - 79 VAL 79 E B 66.7 - - - - - - - - - 183.4 -1.9 32.5 - 80 THR 80 h B - - -45.3 - - - - - - - 181.5 - 36.0 - * * 81 SER 81 H A - - -53.9 - - -56.5 -42.3 - - - 177.0 - 33.4 - 82 ASP 82 H A - 174.6 - - - -62.8 -41.5 - - - 180.4 - 34.0 - 83 GLU 83 H A - - -54.3 177.5 - -70.5 -28.3 - - - 173.4 - 34.4 - * * 84 LEU 84 H A - 178.7 - - - -63.3 -47.1 - - - 176.9 -2.0 35.3 - 85 GLU 85 H A - - -62.3 180.7 - -68.5 -29.1 - - - 175.5 -2.1 33.4 - 86 ASN 86 H A - 174.5 - - - -63.2 -45.9 - - - 176.6 -1.8 36.2 - 87 LEU 87 H A - - -61.5 176.6 - -64.2 -38.8 - - - 173.7 -2.4 34.2 - * * 88 ASP 88 H A - 169.1 - - - -58.9 -47.2 - - - 179.6 -1.9 35.1 - 89 ALA 89 H A - - - - - -60.6 -48.1 - - - 182.1 -2.8 34.9 - 90 VAL 90 H A - 180.3 - - - -73.5 -58.0 - - - 185.6 -2.7 33.0 - +* +* 91 GLU 91 H A - 201.3 - - - -79.9 -36.4 - - - 186.9 -3.0 34.9 - * * * * * 92 GLY 92 h - - - - - - - - - - - 178.3 -1.1 - - * * Residue-by-residue listing for refined_19 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 93 ASN 93 T A - - -67.1 - - - - - - - 180.7 - 33.6 - 94 GLU 94 e a - - -59.9 178.8 - - - - - - 183.8 -2.2 33.6 - 95 TYR 95 E B - - -71.8 - - - - - - - 178.8 -1.3 34.4 - 96 GLU 96 E B - 178.0 - - - - - - - - 181.2 -2.0 34.2 - 97 ARG 97 E B - 183.2 - 181.5 - - - - - - 180.4 - 34.5 - 98 VAL 98 E B - - -66.8 - - - - - - - 182.1 -2.5 31.3 - 99 THR 99 E B 45.7 - - - - - - - - - 183.6 - 35.4 - * * 100 VAL 100 E B - - -62.8 - - - - - - - 177.4 -2.8 33.5 - * * 101 GLY 101 E - - - - - - - - - - - 181.5 - - - 102 ILE 102 E B 56.4 - - - - - - - - - 182.1 -2.7 31.2 - 103 VAL 103 E B - 181.7 - - - - - - - - 182.1 -2.7 34.8 - 104 ARG 104 E B - - -62.8 200.1 - - - - - - 177.4 -3.0 32.8 - * * * 105 GLU 105 e A - - -65.5 - - - - - - - 180.0 -2.7 35.6 - 106 ASP 106 T A - - -65.3 - - - - - - - 182.8 - 34.2 - 107 ASN 107 T a 72.6 - - - - - - - - - 186.2 - 35.1 - * * 108 SER 108 t l - 186.8 - - - - - - - - 175.0 -1.2 30.9 - * * 109 GLU 109 e B 65.9 - - 176.6 - - - - - - 190.2 - 33.5 - +* +* 110 LYS 110 E B 81.2 - - 186.7 - - - - - - 174.6 - 33.1 - * * 111 MET 111 E B - - -60.0 189.9 - - - - - - 181.5 -3.1 33.1 - * * 112 ALA 112 E B - - - - - - - - - - 183.0 - 33.3 - 113 VAL 113 E B - - -59.1 - - - - - - - 175.8 -2.0 34.5 - 114 LYS 114 E B - - -54.9 183.7 - - - - - - 178.8 -1.3 34.7 - * * 115 THR 115 E B - 192.6 - - - - - - - - 181.9 -2.1 33.4 - 116 TYR 116 E B - - -63.2 - - - - - - - 181.3 -.5 33.5 - ** ** 117 MET 117 E B 66.7 - - 174.1 - - - - - - 180.8 -2.2 32.0 - 118 TRP 118 E B - 187.4 - - - - - - - - 194.4 -3.1 35.1 - ** * ** 119 ILE 119 e A - - -48.9 177.1 - - - - - - 181.6 -.6 34.4 - * +* +* 120 ASN 120 S A 67.5 - - - - - - - - - 173.8 - 31.4 - * * 121 LYS 121 ~l 61.5 - - 187.4 - - - - - - 182.6 - 29.1 - ** * ** 122 ALA 122 b - - - - - - - - - - 174.8 -2.5 32.3 - 123 ASP 123 t B - - -80.8 - - - - - - - 175.2 -.8 32.6 - +* +* 124 PRO 124 T - - - - - -67.8 - - - - - 178.6 - 39.1 - * * 125 ASP 125 T A - - -68.9 - - - - - - - 183.6 - 35.4 - 126 MET 126 t b 53.7 - - 186.0 - - - - - - 174.2 -.9 28.6 - * * +* +* 127 PHE 127 B - 185.1 - - - - - - - - 187.9 -2.1 35.2 - * * 128 GLY 128 - - - - - - - - - - - 186.7 -.8 - - * +* +* 129 GLU 129 B B - - -64.6 - - - - - - - 181.1 - 34.4 - Residue-by-residue listing for refined_19 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 130 TRP 130 h B - 191.6 - - - - - - - - 180.2 -1.0 32.6 - * * 131 ASN 131 H A - - -59.3 - - -37.8 -47.9 - - - 180.2 - 35.3 - ** ** 132 PHE 132 H A - 163.8 - - - -72.9 -47.4 - - - 179.3 - 32.5 - * * 133 GLU 133 H A - - -63.4 - - -56.5 -31.4 - - - 176.9 - 34.0 - 134 GLU 134 H A - 184.6 - - - -66.0 -53.6 - - - 178.5 -2.7 34.7 - * * 135 TRP 135 H A - 177.1 - - - -64.9 -36.6 - - - 177.3 -1.8 33.0 - 136 LYS 136 H A - 179.0 - 182.0 - -52.8 -50.3 - - - 179.8 -3.5 36.5 - * +* +* 137 ARG 137 H A 61.2 - - 181.3 - -71.2 -30.6 - - - 177.2 -2.2 30.5 - 138 LEU 138 H A - - -59.9 180.0 - -69.7 -32.8 - - - 176.9 -1.7 33.6 - 139 HIS 139 H A - 182.0 - - - -75.7 -36.8 - - - 176.6 -2.6 34.7 - 140 LYS 140 H A - 175.5 - 178.2 - -61.8 -34.2 - - - 182.0 -2.2 35.4 - 141 LYS 141 H A - - -67.2 - - -48.9 -31.4 - - - 178.9 -1.6 31.8 - * * 142 LYS 142 H A - 175.4 - 177.0 - -54.6 -46.4 - - - 179.7 -1.0 34.3 - * * 143 PHE 143 H A - - -57.4 - - -76.4 -36.1 - - - 182.6 -1.6 35.1 - 144 ILE 144 H A - - -57.5 - - -62.0 -33.2 - - - 177.0 -1.9 32.1 - 145 GLU 145 H A - - -58.8 - - -54.3 -36.2 - - - 176.8 -2.4 33.6 - 146 THR 146 H A - - -57.9 - - -74.4 -42.8 - - - 180.2 -1.1 35.3 - * * 147 PHE 147 H A - - -73.4 - - -67.7 -29.4 - - - 176.8 -1.7 29.6 - * * 148 LYS 148 H A - - -67.2 178.7 - -53.4 -49.0 - - - 184.1 -3.1 35.8 - * * 149 LYS 149 H A - - -56.9 179.3 - -68.1 -36.2 - - - 177.2 -.8 34.2 - +* +* 150 ILE 150 H A - - -60.8 175.3 - -64.3 -39.8 - - - 179.0 -1.3 33.7 - 151 MET 151 H A - 181.1 - 178.4 - -73.5 -38.5 - - - 177.6 -2.8 34.5 - * * 152 GLU 152 H A - - -63.4 177.8 - -62.9 -34.6 - - - 178.3 -2.8 34.7 - * * 153 CYS 153 H A - 182.8 - - - -65.9 -36.2 - - - 180.7 -1.9 35.1 - 154 LYS 154 H A - - -60.9 182.9 - -82.5 -44.5 - - - 181.9 -1.0 34.3 - * * * 155 LYS 155 h a - - -58.5 178.2 - - - - - - 180.7 -3.5 33.5 - +* +* 156 LYS 156 B - - -64.9 180.1 - - - - - - 175.9 - 35.9 - 157 PRO 157 - - - - - -70.3 - - - - - 179.8 - 38.3 - * * 158 GLN 158 b 58.2 - - 176.2 - - - - - - 178.0 - 34.5 - 159 GLY 159 - - - - - - - - - - - 180.6 - - - 160 GLN 160 B 60.9 - - - - - - - - - 182.5 - 32.6 - 161 GLY 161 - - - - - - - - - - - 180.9 - - - 162 ASN 162 B - 179.0 - - - - - - - - 175.6 - 34.4 - 163 ASP 163 B - 176.9 - - - - - - - - 183.5 -.6 33.4 - +* +* 164 ASP 164 B - 185.6 - - - - - - - - 176.7 -.8 35.1 - +* +* 165 ILE 165 a 45.2 - - - - - - - - - 180.6 -.6 31.1 - * +* +* 166 SER 166 b - 179.1 - - - - - - - - 182.1 - 34.7 - 167 HIS 167 B - - -64.3 - - - - - - - 181.0 - 33.9 - Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 168 VAL 168 B - 187.2 - - - - - - - - 180.1 - 35.3 - 169 LEU 169 B - 177.8 - - - - - - - - 178.9 - 34.2 - 170 ARG 170 B - - -66.4 - - - - - - - 176.2 - 34.4 - 171 GLU 171 B - - -62.1 183.2 - - - - - - 177.0 - 33.0 - 172 ASP 172 b 58.6 - - - - - - - - - 185.1 -.6 32.0 - +* +* 173 GLN 173 - - 186.1 - 182.4 - - - - - - - -1.2 35.6 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +* ** * ** +* ** ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.5 180.9 -60.7 179.5 -66.0 -65.1 -39.3 - - - 179.9 -2.0 34.1 Standard deviations: 8.6 7.1 7.0 8.9 7.1 9.1 7.5 - - - 4.0 .9 1.9 Numbers of values: 31 50 69 46 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_19 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 - 1.235 1.498 - 1.459 - 117.35 119.83 - 110.31 - 122.83 2 HIS 2 1.314 1.227 1.504 1.544 1.444 121.10 115.60 120.95 109.89 111.35 111.63 123.45 * * 3 HIS 3 1.304 1.232 1.505 1.530 1.435 121.15 115.83 121.04 111.13 108.63 112.05 123.13 +* * +* 4 HIS 4 1.282 1.233 1.509 1.553 1.439 122.64 116.61 120.60 112.15 110.55 110.60 122.77 *** * * * *** 5 HIS 5 1.306 1.223 1.521 1.549 1.438 121.00 115.57 120.38 110.81 111.66 111.29 123.97 +* * +* 6 HIS 6 1.317 1.235 1.513 1.572 1.471 124.81 117.05 120.51 111.96 108.47 114.58 122.42 ** +* ** ** 7 HIS 7 1.308 1.228 1.521 1.564 1.447 119.94 115.39 121.71 112.96 114.80 114.43 122.82 * +* +* * ** ** 8 LEU 8 1.320 1.239 1.500 1.518 1.457 121.26 113.00 122.30 109.71 106.60 111.13 124.70 * +* +* * +* 9 GLU 9 1.309 1.234 1.521 1.531 1.419 124.23 116.82 120.51 110.52 106.49 108.00 122.55 * ** * +* * ** 10 CYS 10 1.293 1.233 1.514 1.531 1.429 120.84 115.16 121.48 112.26 111.64 110.42 123.32 +** +* * +** 11 SER 11 1.298 1.237 1.530 1.532 1.437 123.08 113.98 121.69 111.32 108.12 108.60 124.31 ** * * * * ** Residue-by-residue listing for refined_19 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 1.331 1.233 1.528 1.519 1.446 125.08 115.66 120.51 109.40 111.74 107.27 123.83 +* +* +* 13 ASP 13 1.328 1.236 1.521 1.541 1.461 123.82 114.71 121.73 112.09 110.98 112.85 123.41 * * * * 14 SER 14 1.314 1.241 1.525 1.544 1.452 124.71 117.77 119.33 109.15 107.36 110.24 122.90 * +* * +* 15 LEU 15 1.329 1.237 1.488 1.508 1.419 121.15 114.53 120.50 110.62 110.43 112.03 124.94 +* * ** * ** 16 GLN 16 1.328 1.249 1.541 1.536 1.479 124.85 116.50 121.12 109.76 110.85 108.70 122.31 * +* * +* 17 LEU 17 1.315 1.232 1.493 1.513 1.411 120.75 115.52 121.17 109.02 108.39 113.34 123.32 * +* ** * +* ** 18 HIS 18 1.270 1.252 1.497 1.531 1.432 122.05 116.35 120.17 109.24 108.93 109.87 123.45 **** * * * **** 19 ASN 19 1.304 1.239 1.523 1.537 1.435 120.98 116.68 120.54 109.21 107.83 112.19 122.77 +* * * +* 20 VAL 20 1.306 1.217 1.525 1.573 1.458 122.21 117.10 120.28 109.49 109.82 110.65 122.62 +* * +* 21 PHE 21 1.308 1.239 1.506 1.539 1.446 121.51 116.03 120.82 110.91 108.06 110.20 123.15 +* * +* 22 VAL 22 1.295 1.238 1.522 1.553 1.418 121.55 115.20 121.43 111.24 110.62 112.19 123.36 ** ** ** 23 TYR 23 1.303 1.211 1.539 1.542 1.425 122.26 118.42 119.76 112.31 113.02 109.76 121.81 +* * +* * * +* 24 GLY 24 1.336 1.226 1.518 - 1.459 118.69 116.91 119.86 - 115.45 - 123.18 * * * 25 SER 25 1.331 1.230 1.545 1.523 1.477 123.15 116.74 120.76 108.78 113.38 108.43 122.50 * * * 26 PHE 26 1.319 1.217 1.537 1.550 1.458 121.56 116.09 120.93 109.04 108.76 109.05 122.97 27 GLN 27 1.332 1.242 1.532 1.529 1.471 122.66 115.90 121.25 109.38 112.46 109.26 122.86 28 ASP 28 1.298 1.220 1.527 1.527 1.446 121.66 118.16 120.51 111.14 111.34 109.74 121.33 ** * ** 29 PRO 29 1.340 1.234 1.535 1.521 1.467 122.52 117.04 120.71 110.28 113.64 104.19 122.24 * * 30 ASP 30 1.323 1.232 1.509 1.525 1.457 120.56 116.87 120.39 110.89 110.89 112.55 122.71 * * 31 VAL 31 1.335 1.220 1.531 1.578 1.454 119.90 116.49 120.65 111.98 109.29 115.04 122.83 * * * ** ** 32 ILE 32 1.342 1.235 1.537 1.548 1.447 121.91 115.95 121.17 110.52 109.55 110.32 122.84 33 ASN 33 1.316 1.224 1.513 1.531 1.463 122.14 116.76 120.82 110.79 111.95 111.17 122.41 34 VAL 34 1.303 1.242 1.542 1.559 1.447 120.68 116.48 120.76 110.02 111.56 111.80 122.75 +* +* 35 MET 35 1.323 1.230 1.536 1.543 1.452 121.70 117.63 120.27 111.54 110.78 109.03 122.03 36 LEU 36 1.322 1.235 1.515 1.573 1.449 120.12 116.58 119.32 114.01 111.94 115.03 124.07 ** ** +** +** 37 ASP 37 1.342 1.224 1.505 1.542 1.499 124.53 115.96 120.82 107.80 110.20 114.48 123.21 ** +* * ** ** 38 ARG 38 1.317 1.237 1.520 1.547 1.467 122.19 116.64 120.29 109.51 110.63 111.16 123.07 39 THR 39 1.325 1.244 1.546 1.541 1.446 121.63 118.17 120.08 106.92 111.05 110.76 121.74 40 PRO 40 1.345 1.244 1.517 1.534 1.461 122.82 117.45 119.65 109.73 109.32 104.04 122.82 41 GLU 41 1.319 1.239 1.525 1.530 1.460 120.34 115.48 121.22 110.10 109.84 113.23 123.29 +* +* 42 ILE 42 1.296 1.244 1.511 1.546 1.427 122.32 115.81 120.84 108.26 109.26 110.97 123.35 ** +* ** Residue-by-residue listing for refined_19 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 1.289 1.230 1.518 1.561 1.435 121.56 116.92 120.45 110.41 109.04 112.69 122.58 +** * +** 44 SER 44 1.294 1.244 1.528 1.499 1.426 121.15 116.18 121.05 110.70 109.63 108.75 122.77 +** +* +* * +** 45 ALA 45 1.303 1.227 1.503 1.504 1.438 121.92 115.34 121.14 110.09 111.15 110.44 123.52 +* * * +* 46 THR 46 1.282 1.224 1.515 1.534 1.420 122.96 115.31 120.85 110.39 110.81 109.89 123.82 *** +* *** 47 LEU 47 1.298 1.228 1.532 1.540 1.431 124.03 118.17 120.38 110.71 110.02 109.08 121.40 ** * * * ** 48 PRO 48 1.335 1.245 1.530 1.529 1.448 122.09 116.04 120.86 110.92 111.65 103.65 123.09 * * 49 GLY 49 1.313 1.232 1.509 - 1.444 121.59 116.55 120.66 - 112.31 - 122.79 * * 50 PHE 50 1.321 1.212 1.515 1.548 1.459 122.42 116.96 120.20 110.74 110.44 111.11 122.83 51 GLN 51 1.309 1.244 1.499 1.512 1.443 122.69 115.45 120.72 111.27 109.15 110.80 123.83 * * * 52 ARG 52 1.286 1.227 1.502 1.539 1.443 122.31 115.66 120.96 110.42 110.67 109.03 123.38 *** * *** 53 PHE 53 1.290 1.226 1.488 1.530 1.432 122.01 116.15 120.30 111.58 109.75 111.51 123.53 +** +* * +** 54 ARG 54 1.293 1.226 1.513 1.538 1.431 122.11 115.52 121.01 111.49 111.22 110.16 123.45 +** * +** 55 LEU 55 1.307 1.237 1.523 1.552 1.442 123.11 117.19 119.81 110.66 107.60 109.97 123.00 +* * * +* 56 LYS 56 1.307 1.249 1.525 1.538 1.443 122.09 116.16 120.56 111.10 109.85 110.27 123.27 +* +* 57 GLY 57 1.311 1.237 1.502 - 1.435 121.54 116.60 120.36 - 110.96 - 123.03 * * * 58 ARG 58 1.328 1.221 1.509 1.575 1.453 120.53 115.05 121.60 112.30 108.05 111.90 123.34 ** * * ** 59 LEU 59 1.314 1.235 1.517 1.533 1.421 122.06 116.10 120.67 112.91 108.89 111.98 123.23 * +* * +* 60 TYR 60 1.297 1.230 1.505 1.546 1.431 122.92 119.22 119.00 107.23 106.89 107.03 121.74 ** * +* * +* +* ** ** 61 PRO 61 1.349 1.226 1.521 1.543 1.446 120.94 116.93 120.12 110.78 107.77 104.22 122.91 * +* * +* 62 CYS 62 1.300 1.249 1.526 1.539 1.435 121.31 115.74 120.90 111.59 111.22 108.84 123.34 ** * ** 63 ILE 63 1.321 1.223 1.506 1.568 1.449 122.92 116.86 119.92 108.14 108.38 111.26 123.20 * * * 64 VAL 64 1.302 1.233 1.524 1.580 1.456 122.60 118.09 119.68 108.87 108.17 113.31 122.17 +* * * * +* 65 PRO 65 1.334 1.240 1.543 1.536 1.469 122.66 115.94 121.16 110.85 112.60 104.09 122.90 66 SER 66 1.315 1.239 1.513 1.539 1.443 122.57 116.39 120.35 110.33 108.78 110.07 123.26 * * 67 GLU 67 1.313 1.222 1.516 1.513 1.448 121.56 116.17 120.72 111.20 110.32 109.47 123.09 * * 68 LYS 68 1.310 1.231 1.488 1.534 1.440 121.98 115.53 121.21 109.63 108.75 114.60 123.04 * +* ** ** 69 GLY 69 1.287 1.235 1.490 - 1.431 119.53 115.48 120.71 - 112.70 - 123.80 *** * * *** 70 GLU 70 1.301 1.220 1.521 1.535 1.429 123.42 117.27 120.74 111.70 108.66 110.47 121.99 +* +* +* Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.292 1.213 1.491 1.554 1.435 120.53 116.15 120.76 107.98 109.29 111.95 123.09 +** +* * +** 72 HIS 72 1.294 1.236 1.504 1.545 1.435 120.76 116.48 120.34 111.15 106.97 111.17 123.16 ** * +* ** 73 GLY 73 1.298 1.243 1.490 - 1.424 120.73 116.34 120.66 - 111.53 - 122.98 ** * +* ** 74 LYS 74 1.295 1.220 1.518 1.534 1.430 121.12 116.13 120.75 108.96 110.88 110.30 123.10 ** * ** 75 VAL 75 1.300 1.232 1.507 1.547 1.433 122.85 114.80 121.02 109.56 110.61 111.73 124.18 ** * ** 76 LEU 76 1.303 1.235 1.510 1.541 1.422 123.69 116.64 120.56 108.35 107.33 110.38 122.72 +* +* * * +* 77 MET 77 1.289 1.234 1.489 1.532 1.440 120.71 116.15 120.85 111.31 109.87 113.25 123.00 +** +* +* +** 78 GLY 78 1.293 1.235 1.515 - 1.427 119.44 116.78 120.64 - 111.71 - 122.58 +** +* +** 79 VAL 79 1.326 1.237 1.538 1.579 1.448 120.64 116.94 120.64 111.89 108.53 112.47 122.36 * * * 80 THR 80 1.309 1.232 1.549 1.530 1.424 122.22 117.21 120.19 110.65 109.82 107.79 122.60 * * +* ** ** 81 SER 81 1.330 1.232 1.546 1.520 1.463 122.48 116.87 120.57 111.50 112.26 109.55 122.52 * * 82 ASP 82 1.330 1.208 1.512 1.519 1.471 121.32 115.95 120.89 109.30 111.33 111.37 123.15 * * 83 GLU 83 1.309 1.213 1.545 1.521 1.459 122.88 116.52 121.13 111.53 109.30 108.98 122.35 * * 84 LEU 84 1.323 1.237 1.533 1.535 1.463 122.03 115.06 121.49 109.29 108.48 110.28 123.44 85 GLU 85 1.327 1.211 1.529 1.523 1.452 122.94 115.30 121.38 111.43 110.17 110.51 123.32 * * 86 ASN 86 1.304 1.223 1.524 1.526 1.455 124.50 115.59 121.18 110.92 109.08 107.30 123.20 +* +* +* +* 87 LEU 87 1.317 1.222 1.519 1.530 1.456 122.74 115.51 120.78 110.60 109.34 110.48 123.72 88 ASP 88 1.326 1.210 1.518 1.531 1.470 122.94 115.67 121.02 109.32 110.43 110.07 123.31 * * 89 ALA 89 1.309 1.232 1.521 1.521 1.444 123.03 115.80 120.83 110.03 111.30 109.49 123.37 * * 90 VAL 90 1.313 1.234 1.559 1.564 1.444 122.10 117.22 120.49 110.76 113.31 110.88 122.29 * +* +* 91 GLU 91 1.330 1.242 1.540 1.530 1.466 121.79 115.15 121.39 109.04 111.83 110.10 123.45 92 GLY 92 1.333 1.232 1.509 - 1.474 124.03 116.63 120.41 - 115.11 - 122.96 * ** ** 93 ASN 93 1.313 1.234 1.520 1.531 1.460 121.98 116.76 120.34 109.68 111.79 111.49 122.90 * * 94 GLU 94 1.330 1.228 1.536 1.542 1.458 121.30 116.52 120.60 110.89 111.64 110.35 122.85 95 TYR 95 1.326 1.223 1.520 1.523 1.466 122.63 116.61 120.45 109.84 112.18 110.02 122.94 96 GLU 96 1.326 1.237 1.516 1.548 1.456 122.11 116.31 120.45 110.80 109.38 110.60 123.24 97 ARG 97 1.313 1.240 1.508 1.522 1.433 121.96 115.64 121.28 110.02 109.54 110.70 123.07 * * * 98 VAL 98 1.288 1.242 1.497 1.532 1.434 121.87 114.94 121.07 110.48 112.07 113.88 123.99 +** * * * +** 99 THR 99 1.295 1.252 1.519 1.535 1.412 123.25 115.86 121.40 110.90 109.93 108.67 122.73 ** * ** +* ** 100 VAL 100 1.308 1.234 1.530 1.563 1.453 120.96 116.13 121.05 109.60 112.08 111.86 122.82 * * Residue-by-residue listing for refined_19 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 1.232 1.500 - 1.435 121.06 117.03 120.20 - 109.99 - 122.75 +* +* 102 ILE 102 1.305 1.220 1.503 1.573 1.445 121.15 116.69 120.30 112.34 111.08 112.95 123.01 +* * * * +* 103 VAL 103 1.296 1.221 1.519 1.562 1.436 122.06 117.28 119.80 110.18 108.65 110.73 122.91 ** * ** 104 ARG 104 1.336 1.233 1.494 1.531 1.464 120.93 114.54 121.11 107.40 112.42 114.63 124.29 * * ** ** 105 GLU 105 1.302 1.239 1.526 1.517 1.443 123.48 115.56 121.16 109.92 110.16 108.76 123.27 +* * +* 106 ASP 106 1.326 1.235 1.504 1.526 1.446 122.44 116.85 120.52 109.28 111.55 111.22 122.64 107 ASN 107 1.321 1.234 1.509 1.543 1.476 119.76 115.79 119.92 108.22 111.41 111.03 124.25 * * 108 SER 108 1.320 1.231 1.544 1.559 1.449 123.65 115.30 121.73 112.52 110.99 112.85 122.82 * * * * * 109 GLU 109 1.324 1.235 1.509 1.512 1.425 123.02 117.68 119.53 111.53 107.16 111.33 122.79 +* * +* 110 LYS 110 1.298 1.235 1.537 1.544 1.456 119.76 115.30 121.42 110.28 112.85 111.23 123.25 ** * ** 111 MET 111 1.312 1.237 1.474 1.511 1.453 123.60 114.85 121.24 107.01 109.37 115.67 123.90 * ** * +* *** *** 112 ALA 112 1.268 1.233 1.503 1.513 1.441 121.34 116.26 121.00 110.85 109.51 111.44 122.74 **** * **** 113 VAL 113 1.294 1.228 1.509 1.557 1.438 121.34 116.58 120.90 108.66 109.73 112.29 122.51 ** * ** 114 LYS 114 1.282 1.230 1.507 1.510 1.425 120.44 117.86 119.72 110.42 108.08 110.42 122.41 *** +* * *** 115 THR 115 1.301 1.240 1.517 1.560 1.437 120.08 116.22 120.19 110.60 109.17 112.24 123.59 +* * +* 116 TYR 116 1.302 1.228 1.517 1.541 1.430 122.61 115.71 121.09 111.68 109.37 110.70 123.17 +* * +* 117 MET 117 1.305 1.250 1.511 1.551 1.449 122.06 115.73 120.43 110.54 109.85 113.80 123.81 +* * +* +* 118 TRP 118 1.314 1.234 1.530 1.526 1.442 122.95 115.55 120.81 111.99 107.81 108.17 123.63 * * * * 119 ILE 119 1.320 1.230 1.526 1.541 1.460 122.71 117.90 120.17 109.07 113.98 110.31 121.89 120 ASN 120 1.317 1.226 1.515 1.543 1.464 119.24 115.08 120.46 111.55 110.65 113.17 124.45 * +* +* 121 LYS 121 1.351 1.232 1.548 1.552 1.504 127.47 118.72 119.71 111.64 118.10 112.26 121.57 +* * * ** *** * ** * *** 122 ALA 122 1.295 1.235 1.514 1.517 1.438 120.70 115.01 121.42 111.51 112.34 111.18 123.50 ** * ** 123 ASP 123 1.302 1.236 1.501 1.548 1.463 122.60 117.59 120.49 109.23 111.35 113.75 121.92 +* * +* +* 124 PRO 124 1.348 1.232 1.526 1.539 1.473 122.59 114.27 121.55 109.69 110.01 103.85 124.18 +* +* +* 125 ASP 125 1.326 1.230 1.490 1.520 1.455 124.97 116.93 119.85 107.79 112.46 110.72 123.22 +* +* * +* 126 MET 126 1.329 1.232 1.520 1.544 1.447 120.80 113.56 122.50 114.07 113.45 113.12 123.75 * * ** +* ** 127 PHE 127 1.305 1.235 1.507 1.541 1.420 124.10 115.65 121.07 111.32 105.21 109.85 123.22 +* ** * ** ** 128 GLY 128 1.282 1.234 1.472 - 1.423 121.59 114.80 121.43 - 108.45 - 123.77 *** ** +* * *** Residue-by-residue listing for refined_19 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 1.278 1.237 1.500 1.545 1.414 122.48 115.57 120.98 111.32 109.53 110.02 123.45 +*** * ** +*** 130 TRP 130 1.302 1.219 1.529 1.532 1.425 121.90 116.01 120.04 111.83 110.54 111.28 123.91 +* +* +* 131 ASN 131 1.334 1.239 1.532 1.544 1.481 125.60 117.08 120.47 108.24 112.54 110.30 122.44 * ** ** 132 PHE 132 1.330 1.202 1.523 1.523 1.407 121.30 117.64 119.30 112.61 111.34 110.43 123.06 * +** * +** 133 GLU 133 1.346 1.235 1.534 1.537 1.482 122.33 115.43 121.33 109.56 110.42 111.32 123.23 * * * 134 GLU 134 1.317 1.227 1.539 1.531 1.439 122.87 116.48 120.94 110.77 109.65 109.53 122.55 135 TRP 135 1.327 1.224 1.530 1.538 1.458 121.07 115.04 121.25 111.04 110.37 111.42 123.70 136 LYS 136 1.307 1.228 1.520 1.517 1.450 124.98 116.57 120.49 110.34 110.10 107.13 122.90 +* +* +* +* 137 ARG 137 1.332 1.218 1.525 1.535 1.445 120.57 117.14 120.17 112.28 111.89 113.16 122.67 * +* +* 138 LEU 138 1.327 1.228 1.531 1.535 1.465 121.68 115.52 121.31 110.80 110.36 110.83 123.17 139 HIS 139 1.311 1.241 1.541 1.550 1.465 123.06 114.58 121.59 111.45 108.92 109.14 123.82 * * 140 LYS 140 1.322 1.242 1.532 1.542 1.464 125.13 115.63 120.67 110.81 110.67 108.25 123.69 +* * +* 141 LYS 141 1.344 1.221 1.515 1.523 1.469 123.79 117.23 119.52 109.65 114.39 112.83 123.24 * * * * * 142 LYS 142 1.326 1.235 1.529 1.533 1.460 121.89 115.88 121.10 110.05 110.87 110.36 123.01 143 PHE 143 1.310 1.235 1.515 1.533 1.448 122.15 114.72 121.58 109.76 109.18 110.17 123.67 * * 144 ILE 144 1.319 1.199 1.518 1.552 1.448 123.01 118.11 119.46 111.10 112.31 112.20 122.43 +* +* 145 GLU 145 1.329 1.228 1.541 1.524 1.473 121.04 115.91 121.14 109.90 110.65 111.41 122.92 146 THR 146 1.319 1.241 1.546 1.548 1.438 122.14 115.45 121.24 110.00 109.39 109.64 123.29 * * * * 147 PHE 147 1.330 1.224 1.506 1.525 1.461 122.85 117.23 119.55 112.03 114.60 113.13 123.21 * * +* +* 148 LYS 148 1.330 1.208 1.493 1.530 1.454 121.79 115.21 120.78 107.13 109.24 111.85 123.85 * +* +* +* 149 LYS 149 1.316 1.232 1.516 1.518 1.443 122.81 115.59 121.01 111.52 110.52 109.24 123.37 150 ILE 150 1.322 1.239 1.534 1.567 1.451 122.37 115.53 121.14 110.96 109.65 111.12 123.28 * * 151 MET 151 1.316 1.222 1.536 1.526 1.425 123.28 116.75 120.32 111.33 110.58 109.11 122.92 +* +* 152 GLU 152 1.333 1.224 1.510 1.528 1.475 122.78 115.29 121.18 108.83 110.60 111.02 123.52 153 CYS 153 1.306 1.232 1.533 1.532 1.437 122.75 116.17 120.92 110.88 109.96 108.82 122.90 +* * +* 154 LYS 154 1.326 1.227 1.516 1.510 1.447 121.96 116.40 120.76 109.45 111.96 110.52 122.85 155 LYS 155 1.311 1.233 1.526 1.543 1.450 121.46 115.75 120.65 110.06 111.32 111.49 123.58 * * 156 LYS 156 1.324 1.240 1.512 1.548 1.456 124.58 118.45 119.47 107.57 107.87 111.60 122.07 +* * * * +* 157 PRO 157 1.337 1.248 1.530 1.529 1.458 122.24 115.74 121.22 110.73 111.44 103.70 123.03 158 GLN 158 1.294 1.235 1.517 1.541 1.438 122.85 117.64 119.85 110.80 108.24 110.55 122.50 ** * * ** 159 GLY 159 1.304 1.240 1.493 - 1.430 119.70 115.82 120.77 - 112.19 - 123.41 +* * * +* 160 GLN 160 1.300 1.240 1.512 1.550 1.434 121.97 116.60 120.25 111.24 109.84 112.44 123.15 ** * * * ** Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 161 GLY 161 1.310 1.229 1.502 - 1.436 120.61 116.46 120.82 - 112.59 - 122.72 * * 162 ASN 162 1.298 1.232 1.511 1.540 1.443 121.31 116.42 120.59 110.27 110.84 110.33 122.97 ** ** 163 ASP 163 1.314 1.231 1.508 1.532 1.456 121.46 115.94 120.97 110.92 109.11 111.49 123.04 * * 164 ASP 164 1.302 1.228 1.503 1.522 1.439 121.70 115.97 120.75 109.14 110.56 110.38 123.28 +* * +* 165 ILE 165 1.298 1.230 1.513 1.570 1.446 122.33 114.77 120.89 112.51 111.01 112.79 124.28 ** * +* ** 166 SER 166 1.341 1.237 1.534 1.537 1.458 123.77 115.47 121.13 110.41 110.97 109.57 123.38 * * 167 HIS 167 1.313 1.245 1.503 1.533 1.443 122.25 115.37 121.06 109.92 111.15 111.22 123.56 * * * 168 VAL 168 1.308 1.241 1.522 1.545 1.436 122.30 116.10 120.72 109.05 109.05 110.74 123.17 +* * +* 169 LEU 169 1.301 1.231 1.518 1.531 1.434 122.28 116.05 120.79 110.59 110.12 110.41 123.11 ** * ** 170 ARG 170 1.305 1.231 1.505 1.547 1.449 122.93 116.46 120.42 109.24 109.52 111.83 123.11 +* +* 171 GLU 171 1.302 1.238 1.501 1.530 1.435 121.20 115.65 121.01 110.27 109.70 112.62 123.26 +* * * * +* 172 ASP 172 1.304 1.236 1.523 1.550 1.440 121.94 114.76 122.13 113.03 108.70 111.82 122.98 +* * +* +* 173 GLN 173 1.296 - 1.510 1.535 1.432 122.89 - - 110.82 108.10 108.81 - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** ** +** *** +* * ** ** *** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 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 1.351 1.312 .016 **** +* * C-N (Pro) 1.341 .016 7 1.334 1.349 1.341 .006 C-O C-O 1.231 .020 172 1.199 1.252 1.232 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.474 1.559 1.519 .015 ** +* CH2G*-C (Gly) 1.516 .018 12 1.472 1.518 1.500 .012 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.504 1.521 1.514 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.530 1.580 1.556 .014 * CH1E-CH2E (the rest) 1.530 .020 128 1.499 1.575 1.534 .013 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.407 1.504 1.447 .017 +** ** NH1-CH2G* (Gly) 1.451 .016 12 1.423 1.474 1.440 .015 +* * N-CH1E (Pro) 1.466 .015 7 1.446 1.473 1.460 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 Page 15 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 153 113.00 119.22 116.17 1.01 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.80 117.35 116.40 .68 CH1E-C-N (Pro) 116.9 1.5 7 114.27 117.45 116.20 .99 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.33 124.94 123.09 .60 * * O-C-N (Pro) 122.0 1.4 7 122.24 124.18 123.03 .54 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.24 127.47 122.23 1.29 * *** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.69 124.03 120.77 1.40 * ** C-N-CH1E (Pro) 122.6 5.0 7 120.94 122.82 122.27 .59 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 119.00 122.50 120.72 .60 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.83 121.43 120.53 .42 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.03 111.51 110.62 .60 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 106.92 112.51 110.09 1.33 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 107.01 114.07 110.49 1.34 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 105.21 118.10 110.25 1.78 ** ** NH1-CH2G*-C (Gly) 112.5 2.9 12 108.45 115.45 111.94 1.90 * * N-CH1E-C (Pro) 111.8 2.5 7 107.77 113.64 110.92 1.87 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.49 111.44 110.64 .76 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 107.79 115.04 111.49 1.49 ** ** N-CH1E-CH2E (Pro) 103.0 1.1 7 103.65 104.22 103.96 .21 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.03 115.67 110.85 1.73 ** *** ------------------------------------------------------------------------------------------------------------- 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_19 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] 127 83.0% Residues in additional allowed regions [a,b,l,p] 23 15.0% Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 153 100.0% Number of end-residues (excl. Gly and Pro) 1 Number of glycine residues 12 Number of proline residues 7 ---- Total number of residues 173 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 153 83.0 83.8 10.0 -.1 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 -.7 Inside e. H-bond energy st dev 97 .9 .8 .2 .4 Inside f. Overall G-factor 173 .0 -.4 .3 1.2 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 31 8.6 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 50 7.1 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 69 7.0 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 46 8.9 20.4 5.0 -2.3 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% 83.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_19 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.48 Chi1-chi2 distribution -.16 Chi1 only -.11 Chi3 & chi4 .41 Omega -.07 ------ -.15 ===== Main-chain covalent forces:- Main-chain bond lengths -.02 Main-chain bond angles .39 ------ .22 ===== OVERALL AVERAGE -.02 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.