Residue-by-residue listing for refined_2 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 - - - - - - - - - - - 184.0 - - - 2 HIS 2 l - - -60.5 - - - - - - - 186.5 - 32.4 - * * 3 HIS 3 a 60.2 - - - - - - - - - 186.0 - 24.9 - * +** +** 4 HIS 4 l - - -64.8 - - - - - - - 178.0 - 31.7 - 5 HIS 5 B - - -62.1 - - - - - - - 179.6 - 32.7 - 6 HIS 6 A - 183.7 - - - - - - - - 176.8 - 34.0 - 7 HIS 7 b - 177.6 - - - - - - - - 181.0 - 34.1 - 8 LEU 8 B - - -65.7 174.3 - - - - - - 177.4 -1.0 35.6 - * * 9 GLU 9 B - - -78.3 - - - - - - - 181.7 - 32.4 - 10 CYS 10 B - 182.9 - - - - - - - - 179.2 -1.0 34.9 - * * 11 SER 11 B - 185.6 - - - - - - - - 180.5 - 34.0 - 12 SER 12 A - - -55.0 - - - - - - - 178.4 -.6 34.5 - +* +* 13 ASP 13 ~l - - -68.2 - - - - - - - 178.1 - 28.8 - ** * ** 14 SER 14 t B - - -59.5 - - - - - - - 184.7 - 34.4 - 15 LEU 15 T A - - -72.1 - - - - - - - 179.1 - 30.9 - 16 GLN 16 T A 68.2 - - 178.4 - - - - - - 180.4 - 32.5 - 17 LEU 17 t B - - -60.9 179.2 - - - - - - 186.6 -1.5 32.2 - * * 18 HIS 18 E B - - -56.4 - - - - - - - 178.8 -3.0 35.5 - * * 19 ASN 19 E B - - -54.4 - - - - - - - 183.6 - 34.7 - 20 VAL 20 E B - 180.0 - - - - - - - - 176.9 -2.6 35.0 - Residue-by-residue listing for refined_2 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 - 178.1 - - - - - - - - 184.2 -3.0 34.9 - * * 22 VAL 22 E B - - -63.9 - - - - - - - 182.8 -3.3 31.7 - +* +* 23 TYR 23 S A 57.4 - - - - - - - - - 182.6 -.6 32.4 - +* +* 24 GLY 24 t - - - - - - - - - - - 183.1 - - - 25 SER 25 T A - - -52.5 - - - - - - - 183.7 - 35.6 - 26 PHE 26 T a - - -54.3 - - - - - - - 184.9 - 36.3 - 27 GLN 27 t A 63.7 - - - - - - - - - 184.6 -1.3 31.3 - 28 ASP 28 h B - 187.5 - - - - - - - - 184.3 - 34.5 - 29 PRO 29 H - - - - - -61.9 -61.9 -25.5 - - - 181.3 - 37.8 - * * * 30 ASP 30 H A - 178.3 - - - -65.1 -43.2 - - - 180.9 - 33.8 - 31 VAL 31 H A - - -57.4 - - -71.3 -28.0 - - - 182.2 -.6 31.2 - * +* +* 32 ILE 32 H A - - -60.0 - - -63.0 -51.7 - - - 177.9 -1.1 33.8 - * * * 33 ASN 33 H A - - -73.1 - - -57.7 -32.6 - - - 180.9 -1.8 34.2 - 34 VAL 34 H A - 182.4 - - - -82.1 -43.7 - - - 186.3 -1.0 33.6 - * * * * 35 MET 35 H A - 201.4 - - - -71.0 -37.4 - - - 176.8 -3.3 34.5 - * +* +* 36 LEU 36 h a 49.5 - - 163.6 - - - - - - 182.9 -2.6 28.2 - +* +* 37 ASP 37 t ~b - 186.1 - - - - - - - - 183.1 -.9 34.8 - ** +* ** 38 ARG 38 S B - - -59.5 179.8 - - - - - - 174.9 - 36.0 - 39 THR 39 B - - -53.2 - - - - - - - 174.1 - 34.0 - * * 40 PRO 40 - - - - - -59.6 - - - - - 181.5 - 39.6 - +* +* 41 GLU 41 E B - 178.3 - 174.2 - - - - - - 184.4 -1.3 32.2 - 42 ILE 42 E B - - -49.3 178.0 - - - - - - 179.9 - 35.5 - * * 43 VAL 43 E B 63.5 - - - - - - - - - 176.7 -2.1 34.0 - 44 SER 44 E B - - -54.0 - - - - - - - 181.2 - 36.6 - 45 ALA 45 E B - - - - - - - - - - 178.1 -2.8 34.1 - 46 THR 46 E B - - -55.0 - - - - - - - 176.7 -2.4 35.6 - 47 LEU 47 E B - 175.8 - - - - - - - - 179.3 -3.5 34.5 - +* +* 48 PRO 48 E - - - - - -82.1 - - - - - 179.0 - 38.8 - * * * 49 GLY 49 E - - - - - - - - - - - 181.5 -2.7 - - 50 PHE 50 E B - - -66.2 - - - - - - - 180.2 -.7 34.3 - +* +* 51 GLN 51 E B - 180.2 - 174.0 - - - - - - 180.6 -3.1 33.6 - * * 52 ARG 52 E B - 187.2 - 178.6 - - - - - - 178.6 - 34.3 - 53 PHE 53 e B - - -73.9 - - - - - - - 181.5 -2.7 35.9 - 54 ARG 54 B 64.4 - - 179.8 - - - - - - 179.5 -1.8 30.5 - 55 LEU 55 b - 189.1 - - - - - - - - 181.6 -.5 35.9 - +* +* 56 LYS 56 B - 185.8 - 180.7 - - - - - - 178.0 - 32.6 - 57 GLY 57 S - - - - - - - - - - - 174.7 -2.8 - - 58 ARG 58 S A 64.5 - - - - - - - - - 178.0 - 32.5 - 59 LEU 59 S B - 180.2 - - - - - - - - 185.0 - 33.0 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 60 TYR 60 B - - -52.7 - - - - - - - 174.7 - 37.7 - * * 61 PRO 61 S - - - - - -63.7 - - - - - 186.9 - 37.6 - * * * 62 CYS 62 e B 53.2 - - - - - - - - - 180.0 -1.3 35.1 - 63 ILE 63 E B - - -58.7 - - - - - - - 174.1 - 36.7 - * * 64 VAL 64 E B - - -64.1 - - - - - - - 176.8 -2.3 34.1 - 65 PRO 65 E - - - - - -65.5 - - - - - 181.2 - 37.8 - * * 66 SER 66 E B - 181.1 - - - - - - - - 183.0 -1.2 35.4 - * * 67 GLU 67 E A - - -59.5 188.6 - - - - - - 183.6 - 33.7 - 68 LYS 68 E A - - -58.9 180.4 - - - - - - 185.9 - 36.0 - * * 69 GLY 69 E - - - - - - - - - - - 175.1 - - - 70 GLU 70 E B 63.5 - - - - - - - - - 180.8 - 33.2 - 71 VAL 71 E B - 182.1 - - - - - - - - 176.4 -2.8 35.0 - * * 72 HIS 72 E B - - -65.9 - - - - - - - 183.1 - 33.6 - 73 GLY 73 E - - - - - - - - - - - 181.3 -2.7 - - 74 LYS 74 E B - - -85.1 - - - - - - - 175.8 -1.5 31.6 - * * 75 VAL 75 E B - 167.6 - - - - - - - - 175.1 -2.8 33.9 - 76 LEU 76 E B - - -56.7 180.4 - - - - - - 180.4 -3.2 36.1 - +* +* 77 MET 77 E B 55.0 - - 178.5 - - - - - - 182.3 -3.2 30.9 - +* +* 78 GLY 78 E - - - - - - - - - - - 179.7 -2.4 - - 79 VAL 79 E B 65.4 - - - - - - - - - 181.9 -2.4 32.8 - 80 THR 80 h B - - -52.6 - - - - - - - 183.7 - 36.1 - 81 SER 81 H A - - -54.8 - - -62.1 -35.4 - - - 179.1 - 33.1 - 82 ASP 82 H A - - -62.8 - - -64.8 -36.4 - - - 179.8 - 33.8 - 83 GLU 83 H A - - -49.5 - - -77.5 -30.5 - - - 175.8 - 36.3 - * * * 84 LEU 84 H A - 182.8 - - - -64.8 -41.8 - - - 175.7 -2.1 34.6 - 85 GLU 85 H A - - -64.6 180.2 - -66.2 -29.7 - - - 177.2 -2.4 33.9 - 86 ASN 86 H A - 131.0 - - - -72.3 -42.1 - - - 174.1 -1.0 31.2 - *** * * *** 87 LEU 87 H A - - -61.1 174.8 - -61.6 -42.0 - - - 178.7 -2.7 35.6 - 88 ASP 88 H A - 178.9 - - - -65.7 -30.9 - - - 177.8 -2.4 34.8 - 89 ALA 89 H A - - - - - -75.7 -41.7 - - - 181.7 -1.2 34.4 - * * 90 VAL 90 H A - 173.6 - - - -72.9 -58.4 - - - 182.0 -2.5 32.5 - +* +* 91 GLU 91 h A - - -62.5 - - - - - - - 183.5 -2.8 33.3 - * * 92 GLY 92 T - - - - - - - - - - - 180.7 -.6 - - +* +* 93 ASN 93 T A - - -69.3 - - - - - - - 180.0 -.8 33.9 - +* +* 94 GLU 94 e a - - -61.4 183.0 - - - - - - 179.4 -1.5 32.7 - 95 TYR 95 E B - - -61.1 - - - - - - - 175.9 -1.8 35.5 - 96 GLU 96 E B - 181.9 - - - - - - - - 181.2 -1.1 33.4 - * * 97 ARG 97 E B - 184.5 - 185.2 - - - - - - 179.9 - 35.7 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 VAL 98 E B - - -63.6 - - - - - - - 181.3 -2.8 33.6 - * * 99 THR 99 E B - 181.8 - - - - - - - - 183.9 - 32.2 - 100 VAL 100 E B - - -63.8 - - - - - - - 177.6 -3.6 34.0 - ** ** 101 GLY 101 E - - - - - - - - - - - 182.0 - - - 102 ILE 102 E B 55.5 - - - - - - - - - 177.5 -3.0 32.4 - * * 103 VAL 103 E B - 180.9 - - - - - - - - 180.1 -2.4 33.6 - 104 ARG 104 E B - - -64.0 175.6 - - - - - - 176.4 -3.6 35.8 - ** ** 105 GLU 105 e A - - -58.0 194.9 - - - - - - 173.1 -2.3 33.2 - * * 106 ASP 106 T A - 179.2 - - - - - - - - 176.5 -.8 36.3 - +* +* 107 ASN 107 T ~a - - -46.9 - - - - - - - 178.6 -1.5 33.3 - ** * ** 108 SER 108 T ~a - - -61.8 - - - - - - - 189.2 - 36.0 - ** +* ** 109 GLU 109 E B - - -60.5 186.7 - - - - - - 184.0 -.8 34.5 - +* +* 110 LYS 110 E B 62.5 - - 180.8 - - - - - - 179.0 - 33.7 - 111 MET 111 E B - - -68.0 180.1 - - - - - - 176.6 -3.4 34.6 - +* +* 112 ALA 112 E B - - - - - - - - - - 182.7 - 33.8 - 113 VAL 113 E B - - -60.9 - - - - - - - 176.2 -3.0 34.8 - * * 114 LYS 114 E B - - -57.8 186.6 - - - - - - 180.8 -1.8 32.8 - 115 THR 115 E B - 193.4 - - - - - - - - 182.4 -2.6 33.2 - 116 TYR 116 E B - - -62.8 - - - - - - - 180.2 - 33.9 - 117 MET 117 E B 64.0 - - 175.4 - - - - - - 178.0 -1.0 33.2 - * * 118 TRP 118 E B - 190.5 - - - - - - - - 188.4 -3.5 35.1 - * +* +* 119 ILE 119 e A - - -57.7 - - - - - - - 179.7 -.6 31.7 - +* +* 120 ASN 120 S A - 185.2 - - - - - - - - 177.4 - 34.6 - 121 LYS 121 XX 65.2 - - 183.3 - - - - - - 179.8 - 28.2 - **** +* **** 122 ALA 122 b - - - - - - - - - - 175.7 -3.0 32.8 - * * 123 ASP 123 t B - - -83.7 - - - - - - - 177.1 -1.3 32.4 - * * 124 PRO 124 T - - - - - -62.4 - - - - - 179.1 - 38.8 - * * 125 ASP 125 T A - 180.1 - - - - - - - - 177.9 - 33.7 - 126 MET 126 t B 55.6 - - - - - - - - - 177.5 -1.4 30.1 - * * 127 PHE 127 b - 185.0 - - - - - - - - 179.3 - 33.9 - 128 GLY 128 - - - - - - - - - - - 182.9 - - - 129 GLU 129 B B - 184.7 - 182.4 - - - - - - 178.7 - 35.2 - 130 TRP 130 B - 190.3 - - - - - - - - 182.6 -.9 32.9 - +* +* 131 ASN 131 h b - - -60.2 - - - - - - - 176.5 - 31.1 - 132 PHE 132 H A - - -56.9 - - -73.5 -32.4 - - - 176.6 -2.1 33.8 - 133 GLU 133 H A - 193.0 - - - -58.7 -37.8 - - - 181.4 - 38.2 - * * Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 134 GLU 134 H A - 189.9 - - - -66.4 -40.4 - - - 176.6 - 33.8 - 135 TRP 135 H A - 177.1 - - - -73.1 -35.8 - - - 178.0 -1.0 31.5 - * * 136 LYS 136 H A - 184.8 - 182.5 - -59.8 -31.7 - - - 176.4 -2.8 33.9 - 137 ARG 137 H A - 178.9 - - - -62.5 -53.4 - - - 181.8 -1.8 38.3 - * * * 138 LEU 138 H A - - -79.4 - - -74.3 -16.4 - - - 181.7 -1.6 35.8 - ** ** 139 HIS 139 h A - 190.6 - - - - - - - - 172.8 -1.7 33.6 - * * 140 LYS 140 H A - 177.3 - 181.8 - -57.0 -34.6 - - - 182.6 -1.2 35.5 - * * 141 LYS 141 H A - 182.8 - 176.1 - -59.6 -35.5 - - - 176.1 -2.0 31.8 - 142 LYS 142 H A - 180.5 - 190.7 - -55.6 -47.9 - - - 185.0 -.8 37.0 - +* +* 143 PHE 143 H A - 195.7 - - - -66.6 -39.6 - - - 180.0 -1.0 35.5 - * * 144 ILE 144 H A - - -48.4 - - -72.6 -41.0 - - - 178.9 -2.5 33.2 - * * 145 GLU 145 H A - - -62.0 - - -61.8 -34.1 - - - 176.4 -3.6 33.5 - ** ** 146 THR 146 H A - - -58.2 - - -65.4 -48.2 - - - 178.1 -2.1 34.5 - 147 PHE 147 H A - - -76.4 - - -70.8 -30.2 - - - 175.2 -2.1 29.4 - * * 148 LYS 148 H A - 182.4 - 188.6 - -55.6 -45.8 - - - 182.1 -3.2 37.0 - +* +* 149 LYS 149 H A - 182.6 - 182.5 - -71.6 -34.9 - - - 178.1 -1.9 35.3 - 150 ILE 150 H A - - -59.4 174.4 - -67.4 -37.2 - - - 176.4 -1.6 32.4 - 151 MET 151 H A - - -63.5 - - -66.2 -33.1 - - - 177.2 -2.7 33.2 - 152 GLU 152 H A - - -59.2 - - -73.2 -31.1 - - - 178.1 -1.3 33.5 - 153 CYS 153 H A - 181.8 - - - -69.0 -31.8 - - - 177.0 -1.7 34.4 - 154 LYS 154 H A - - -57.3 - - -74.9 -39.0 - - - 177.6 -1.6 34.5 - 155 LYS 155 H A - 181.1 - 191.0 - -58.7 -59.5 - - - 181.8 -1.8 36.8 - +* +* 156 LYS 156 h B - 174.5 - - - - - - - - 186.7 -3.2 32.5 - * * * 157 PRO 157 - - - - - -73.8 - - - - - 172.2 - 37.5 - * * * 158 GLN 158 b - - -69.2 180.0 - - - - - - 181.0 -.9 32.4 - * * 159 GLY 159 - - - - - - - - - - - 179.2 - - - 160 GLN 160 B - 179.4 - 180.2 - - - - - - 179.9 -.8 33.6 - +* +* 161 GLY 161 - - - - - - - - - - - 180.4 -1.1 - - * * 162 ASN 162 b - - -63.0 - - - - - - - 181.4 - 32.7 - 163 ASP 163 a - 171.6 - - - - - - - - 182.5 -1.7 34.1 - 164 ASP 164 B 63.9 - - - - - - - - - 177.0 - 32.0 - 165 ILE 165 b - 177.7 - - - - - - - - 184.0 - 31.4 - 166 SER 166 b 53.8 - - - - - - - - - 178.2 - 35.5 - 167 HIS 167 B - - -66.5 - - - - - - - 180.5 - 34.1 - 168 VAL 168 B - - -63.2 - - - - - - - 185.5 - 32.4 - 169 LEU 169 B - 181.4 - - - - - - - - 171.2 - 33.0 - +* +* 170 ARG 170 B - 187.6 - - - - - - - - 186.1 -.6 33.9 - * +* +* 171 GLU 171 B - 181.1 - 178.7 - - - - - - 177.6 - 34.5 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 172 ASP 172 a - 182.9 - - - - - - - - 178.3 -.5 35.3 - ** ** 173 GLN 173 - - 181.4 - 179.4 - - - - - - - - 34.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** *** * * * ** +* ** +** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.5 181.8 -61.7 180.6 -67.0 -66.7 -38.1 - - - 179.9 -1.9 34.0 Standard deviations: 5.3 8.8 7.7 5.7 8.1 6.5 8.7 - - - 3.4 .9 2.1 Numbers of values: 19 60 71 40 7 40 40 0 0 0 172 102 161 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_2 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 - 1.461 - 116.27 119.57 - 110.70 - 124.14 * * 2 HIS 2 1.337 1.227 1.513 1.552 1.470 124.04 117.06 120.38 110.52 109.28 113.45 122.54 * * +* +* 3 HIS 3 1.328 1.227 1.538 1.571 1.455 119.91 118.17 119.16 114.61 115.67 115.53 122.63 ** ** +* +** +** 4 HIS 4 1.331 1.239 1.534 1.548 1.484 122.18 116.63 120.91 109.60 111.94 113.98 122.32 * ** ** 5 HIS 5 1.316 1.234 1.508 1.553 1.457 121.36 115.68 120.97 109.99 110.07 113.28 123.34 * +* +* 6 HIS 6 1.315 1.225 1.537 1.551 1.456 122.18 115.60 121.17 111.35 109.32 110.20 123.23 * * * 7 HIS 7 1.329 1.228 1.522 1.545 1.461 122.67 115.32 120.78 110.41 110.26 110.75 123.85 8 LEU 8 1.303 1.238 1.504 1.549 1.441 124.17 116.48 120.20 108.78 108.11 111.06 123.31 +* * * * +* 9 GLU 9 1.300 1.233 1.504 1.537 1.442 121.73 115.32 121.44 111.85 110.03 111.82 123.21 ** * ** 10 CYS 10 1.292 1.243 1.515 1.536 1.421 122.42 116.04 121.12 110.80 109.25 109.66 122.83 +** +* +** 11 SER 11 1.291 1.234 1.522 1.531 1.404 121.47 115.92 120.70 111.87 108.51 110.15 123.30 +** +** +** 12 SER 12 1.316 1.234 1.535 1.527 1.442 122.15 115.43 120.56 111.33 110.53 108.95 123.99 Residue-by-residue listing for refined_2 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 13 ASP 13 1.336 1.235 1.508 1.535 1.473 124.64 114.69 122.14 112.10 114.97 113.86 123.16 +* * * +* +* 14 SER 14 1.299 1.237 1.525 1.535 1.436 123.94 117.71 119.61 111.43 107.36 110.12 122.68 ** * * * ** 15 LEU 15 1.317 1.244 1.514 1.498 1.436 121.75 116.86 120.55 111.41 115.22 111.80 122.58 +* * * +* 16 GLN 16 1.312 1.226 1.514 1.529 1.465 120.70 115.49 121.40 110.24 110.91 112.72 123.10 * * * 17 LEU 17 1.289 1.239 1.506 1.518 1.438 121.33 115.28 121.16 111.33 110.27 112.38 123.55 +** * * +** 18 HIS 18 1.297 1.250 1.495 1.522 1.448 123.09 115.37 120.77 108.58 110.67 110.37 123.85 ** * ** 19 ASN 19 1.308 1.244 1.525 1.532 1.442 122.33 116.85 120.48 110.06 108.46 110.59 122.66 +* +* 20 VAL 20 1.308 1.221 1.528 1.570 1.462 121.79 116.73 120.36 109.34 110.67 110.62 122.91 +* * +* 21 PHE 21 1.318 1.240 1.507 1.543 1.449 121.94 116.03 120.92 110.80 107.67 110.03 123.05 * * 22 VAL 22 1.293 1.235 1.515 1.554 1.424 121.63 114.87 121.77 112.18 111.64 112.03 123.36 +** +* * +** 23 TYR 23 1.308 1.221 1.522 1.535 1.442 122.16 117.42 120.18 111.49 113.43 110.81 122.40 * * 24 GLY 24 1.319 1.229 1.503 - 1.446 118.81 116.60 120.17 - 113.49 - 123.20 * * 25 SER 25 1.323 1.224 1.541 1.522 1.459 122.67 116.99 120.52 109.20 112.68 108.77 122.49 * * 26 PHE 26 1.321 1.215 1.532 1.543 1.455 121.20 117.34 120.67 108.57 110.06 109.30 121.97 27 GLN 27 1.324 1.237 1.538 1.566 1.473 120.07 116.55 120.54 112.45 113.05 111.47 122.89 +* * +* 28 ASP 28 1.316 1.219 1.528 1.529 1.459 121.49 118.24 120.17 110.44 110.19 109.87 121.58 * * 29 PRO 29 1.343 1.236 1.538 1.523 1.471 122.91 117.35 120.39 110.32 114.73 103.92 122.24 * * 30 ASP 30 1.327 1.229 1.507 1.527 1.472 121.07 115.73 121.04 109.94 110.59 111.24 123.17 31 VAL 31 1.316 1.215 1.521 1.569 1.441 121.00 116.40 120.64 111.48 110.74 113.80 122.94 * * * * 32 ILE 32 1.326 1.238 1.538 1.541 1.449 122.67 116.53 120.73 111.22 111.62 109.81 122.71 33 ASN 33 1.316 1.223 1.512 1.527 1.473 122.28 115.99 121.08 109.98 111.56 110.30 122.93 34 VAL 34 1.305 1.237 1.536 1.551 1.440 121.41 116.65 120.78 109.68 112.00 111.64 122.56 +* +* 35 MET 35 1.316 1.228 1.532 1.541 1.450 121.50 117.18 120.51 111.42 110.54 108.97 122.21 36 LEU 36 1.322 1.238 1.513 1.568 1.442 119.94 117.40 119.27 113.11 112.40 115.27 123.23 +* +* +** +** 37 ASP 37 1.338 1.225 1.513 1.547 1.487 122.43 115.95 121.08 108.27 109.89 111.80 122.96 +* +* 38 ARG 38 1.317 1.228 1.502 1.530 1.465 122.07 116.66 119.98 107.36 109.68 111.01 123.36 * * * 39 THR 39 1.323 1.242 1.536 1.545 1.437 121.42 117.03 120.40 109.45 110.44 111.77 122.50 * * 40 PRO 40 1.347 1.237 1.524 1.532 1.471 123.38 117.20 119.60 109.77 110.18 102.99 123.19 41 GLU 41 1.332 1.229 1.515 1.544 1.461 121.29 115.77 121.09 111.15 110.18 112.65 123.11 * * 42 ILE 42 1.297 1.234 1.512 1.543 1.427 121.18 116.05 120.70 109.15 109.19 110.57 123.24 ** +* ** Residue-by-residue listing for refined_2 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 1.295 1.238 1.534 1.564 1.441 121.99 116.58 120.40 110.23 110.32 111.33 122.99 ** ** 44 SER 44 1.318 1.242 1.527 1.523 1.444 122.20 117.11 120.25 109.00 108.38 108.67 122.61 * * * 45 ALA 45 1.308 1.231 1.518 1.511 1.439 120.94 115.15 121.65 110.12 112.34 110.06 123.20 +* * +* 46 THR 46 1.297 1.228 1.518 1.536 1.428 122.82 115.99 120.44 108.42 109.39 110.82 123.56 ** +* ** 47 LEU 47 1.297 1.232 1.531 1.536 1.429 123.21 117.73 120.31 111.07 109.37 109.80 121.87 ** +* ** 48 PRO 48 1.337 1.239 1.531 1.544 1.454 122.70 116.16 121.02 110.12 111.80 103.87 122.82 49 GLY 49 1.312 1.227 1.505 - 1.442 120.96 116.15 121.07 - 111.70 - 122.77 * * 50 PHE 50 1.311 1.210 1.494 1.547 1.443 122.44 117.11 120.01 110.22 108.78 111.42 122.88 * * * * 51 GLN 51 1.292 1.240 1.503 1.538 1.437 121.63 116.13 120.41 111.75 109.00 110.62 123.40 +** * * +** 52 ARG 52 1.309 1.239 1.500 1.533 1.423 121.10 115.45 120.68 110.01 109.21 111.31 123.87 * * +* +* 53 PHE 53 1.292 1.214 1.471 1.538 1.436 122.31 117.00 120.07 108.48 107.17 111.16 122.92 +** +** * * +** 54 ARG 54 1.290 1.239 1.508 1.542 1.431 119.14 114.22 121.61 112.59 112.31 112.79 124.16 +** * * * * +** 55 LEU 55 1.302 1.225 1.511 1.572 1.437 125.09 118.04 119.43 111.16 104.20 109.50 122.46 +* ** * +* ** ** 56 LYS 56 1.304 1.242 1.518 1.533 1.436 119.81 115.00 121.61 111.13 111.16 111.80 123.38 +* * * +* 57 GLY 57 1.293 1.232 1.495 - 1.434 122.24 116.29 120.57 - 109.52 - 123.12 +** * * * +** 58 ARG 58 1.313 1.229 1.520 1.569 1.452 120.91 113.95 122.00 112.98 107.94 111.62 124.04 * +* * +* * +* 59 LEU 59 1.313 1.237 1.523 1.542 1.423 124.29 115.71 120.49 112.34 108.55 111.09 123.78 * +* * * +* 60 TYR 60 1.296 1.239 1.522 1.539 1.428 124.30 119.05 119.20 108.64 107.33 108.03 121.74 ** +* * * * * ** 61 PRO 61 1.353 1.244 1.535 1.529 1.455 121.95 114.98 121.15 111.16 111.54 104.27 123.86 * * * * 62 CYS 62 1.307 1.240 1.541 1.541 1.440 124.63 115.76 121.13 111.86 112.31 107.25 123.10 +* +* +* +* 63 ILE 63 1.325 1.211 1.510 1.571 1.464 123.41 117.59 119.72 107.52 108.64 110.57 122.68 * * * 64 VAL 64 1.302 1.237 1.525 1.578 1.460 121.94 118.21 119.70 108.64 108.47 113.28 122.05 +* * * * +* 65 PRO 65 1.338 1.249 1.534 1.529 1.462 122.40 115.25 121.40 110.91 112.12 104.09 123.35 * * 66 SER 66 1.306 1.224 1.518 1.530 1.434 123.46 117.78 119.95 110.62 108.33 109.19 122.27 +* * * +* 67 GLU 67 1.314 1.232 1.521 1.519 1.452 120.24 116.40 120.96 109.21 111.68 111.74 122.64 * * 68 LYS 68 1.309 1.234 1.510 1.510 1.455 121.24 116.43 120.60 108.29 111.74 109.41 122.96 * * * 69 GLY 69 1.301 1.243 1.506 - 1.434 120.10 114.57 121.48 - 114.38 - 123.94 ** * ** 70 GLU 70 1.301 1.241 1.537 1.555 1.431 124.61 117.09 120.54 110.97 108.10 112.30 122.35 ** * * +* * * ** Residue-by-residue listing for refined_2 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 1.306 1.210 1.502 1.564 1.448 121.72 116.86 120.60 108.17 109.50 112.22 122.53 +* * * +* 72 HIS 72 1.292 1.234 1.494 1.525 1.439 120.65 116.15 120.34 110.57 108.26 111.89 123.50 +** * * * +** 73 GLY 73 1.296 1.238 1.487 - 1.421 120.84 116.49 120.71 - 110.98 - 122.80 ** +* +* ** 74 LYS 74 1.296 1.226 1.478 1.530 1.432 120.95 114.12 121.48 110.02 113.23 113.57 124.39 ** ** * * +* ** 75 VAL 75 1.290 1.229 1.513 1.551 1.440 122.66 115.20 120.73 109.53 111.22 111.77 124.07 +** +** 76 LEU 76 1.311 1.240 1.512 1.537 1.435 123.24 117.14 120.27 108.29 107.11 110.74 122.54 * * * * 77 MET 77 1.297 1.236 1.497 1.525 1.443 120.74 114.67 121.70 111.83 112.32 112.85 123.63 ** * * ** 78 GLY 78 1.293 1.231 1.511 - 1.434 121.17 116.33 120.85 - 111.64 - 122.81 +** * +** 79 VAL 79 1.322 1.240 1.538 1.579 1.447 121.07 116.82 120.65 111.66 109.36 111.90 122.51 * * * 80 THR 80 1.311 1.233 1.558 1.538 1.426 122.55 117.85 120.00 111.56 109.98 106.63 122.15 * +* +* * +** +** 81 SER 81 1.340 1.226 1.534 1.528 1.466 121.99 116.79 120.41 111.04 112.33 110.49 122.77 82 ASP 82 1.326 1.228 1.519 1.531 1.471 121.44 115.30 121.31 110.05 110.72 111.18 123.34 83 GLU 83 1.310 1.206 1.533 1.525 1.452 123.03 116.49 121.24 109.89 108.02 108.27 122.26 * * * * * 84 LEU 84 1.332 1.226 1.522 1.533 1.461 121.77 115.66 121.08 109.28 108.78 111.33 123.26 85 GLU 85 1.334 1.214 1.514 1.524 1.454 122.21 115.78 120.92 109.81 110.09 111.45 123.30 86 ASN 86 1.311 1.223 1.536 1.543 1.451 122.84 116.97 120.35 113.97 111.64 110.57 122.65 * ** ** 87 LEU 87 1.322 1.241 1.523 1.538 1.469 122.18 113.89 121.97 109.02 108.20 110.23 124.11 * * * 88 ASP 88 1.320 1.217 1.524 1.536 1.456 124.47 115.91 121.30 111.27 110.79 108.59 122.79 +* * +* 89 ALA 89 1.308 1.224 1.521 1.522 1.446 122.58 116.03 121.03 110.21 110.50 110.20 122.94 +* +* 90 VAL 90 1.315 1.231 1.554 1.565 1.446 122.16 117.86 120.19 111.77 113.03 110.69 121.92 * * * 91 GLU 91 1.327 1.242 1.521 1.525 1.483 121.49 114.90 121.15 110.30 111.88 110.97 123.92 * * 92 GLY 92 1.319 1.222 1.514 - 1.461 123.92 117.34 119.94 - 115.25 - 122.71 +* +* 93 ASN 93 1.326 1.230 1.521 1.540 1.464 121.73 117.39 120.14 108.97 111.66 111.91 122.46 94 GLU 94 1.330 1.234 1.533 1.526 1.466 120.47 116.48 120.86 110.92 112.78 110.91 122.66 95 TYR 95 1.312 1.228 1.503 1.541 1.455 122.14 117.17 119.83 108.41 108.26 111.28 122.99 * * * * 96 GLU 96 1.301 1.244 1.510 1.541 1.437 120.91 116.43 120.34 111.63 108.36 111.30 123.22 +* * * +* 97 ARG 97 1.305 1.240 1.516 1.527 1.426 121.41 115.86 121.16 109.81 108.79 109.43 122.97 +* +* +* 98 VAL 98 1.296 1.237 1.511 1.545 1.430 122.05 116.77 120.32 110.84 110.00 111.29 122.91 ** * ** 99 THR 99 1.298 1.245 1.524 1.567 1.439 120.76 116.14 120.95 112.00 109.47 112.40 122.87 ** * * ** 100 VAL 100 1.308 1.231 1.534 1.561 1.455 122.17 115.87 121.11 108.96 112.03 111.82 123.02 * * Residue-by-residue listing for refined_2 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 1.306 1.234 1.505 - 1.435 121.57 116.44 120.27 - 110.64 - 123.29 +* * +* 102 ILE 102 1.305 1.221 1.508 1.580 1.445 122.57 116.61 120.62 111.18 111.10 112.47 122.77 +* * +* 103 VAL 103 1.299 1.225 1.507 1.554 1.438 121.33 115.89 120.55 109.93 109.04 112.63 123.54 ** * ** 104 ARG 104 1.304 1.242 1.504 1.535 1.437 122.78 116.26 120.25 108.02 110.26 110.77 123.42 +* * * * +* 105 GLU 105 1.322 1.222 1.521 1.527 1.459 121.99 113.31 122.43 111.22 108.74 111.49 124.24 * * 106 ASP 106 1.310 1.233 1.523 1.522 1.448 125.25 115.78 121.32 110.24 109.19 107.79 122.90 * +* +* +* 107 ASN 107 1.337 1.218 1.531 1.570 1.451 121.15 115.45 120.93 108.82 108.30 114.23 123.52 ** * ** ** 108 SER 108 1.331 1.226 1.530 1.561 1.470 126.70 115.14 121.82 108.48 105.37 111.14 123.01 +* +** ** +** 109 GLU 109 1.327 1.219 1.515 1.516 1.445 122.18 115.92 120.57 110.99 111.70 108.92 123.50 110 LYS 110 1.301 1.242 1.528 1.531 1.463 122.91 115.66 120.93 109.82 111.60 111.19 123.37 ** ** 111 MET 111 1.308 1.224 1.484 1.508 1.458 123.83 114.66 121.45 106.87 111.34 112.92 123.88 +* +* * * +* * +* 112 ALA 112 1.281 1.237 1.509 1.509 1.436 122.09 116.13 120.75 110.45 108.94 111.32 123.11 *** * *** 113 VAL 113 1.302 1.215 1.514 1.561 1.451 123.06 117.53 120.47 108.42 108.84 112.34 121.98 +* +* 114 LYS 114 1.294 1.226 1.508 1.523 1.439 119.95 117.06 120.12 111.83 109.71 111.32 122.80 +** * +** 115 THR 115 1.306 1.246 1.531 1.563 1.438 121.06 116.04 120.53 110.65 109.56 112.27 123.42 +* * +* 116 TYR 116 1.308 1.232 1.515 1.541 1.439 122.94 115.59 121.03 111.26 109.84 110.37 123.36 +* * +* 117 MET 117 1.307 1.243 1.507 1.544 1.455 122.13 115.98 120.29 109.59 109.68 113.11 123.68 +* +* +* 118 TRP 118 1.313 1.237 1.514 1.533 1.432 122.29 115.70 120.93 111.05 107.32 109.61 123.37 * * * * 119 ILE 119 1.297 1.238 1.512 1.543 1.443 121.63 116.55 120.27 112.18 113.01 111.29 123.14 ** * ** 120 ASN 120 1.327 1.229 1.523 1.528 1.468 121.14 114.47 121.03 109.22 109.23 111.19 124.50 121 LYS 121 1.346 1.232 1.543 1.555 1.494 127.70 117.49 120.29 112.81 115.86 113.41 122.23 * * +* *** * +* +* *** 122 ALA 122 1.299 1.237 1.517 1.521 1.430 122.01 115.10 121.53 111.30 111.00 111.38 123.26 ** * ** 123 ASP 123 1.301 1.228 1.485 1.548 1.446 122.85 117.60 120.14 109.61 110.53 114.09 122.25 +* +* ** ** 124 PRO 124 1.344 1.227 1.524 1.538 1.469 122.66 115.06 121.24 110.07 110.72 103.89 123.70 * * * 125 ASP 125 1.332 1.229 1.528 1.532 1.450 123.42 116.89 120.71 111.21 111.16 110.13 122.36 126 MET 126 1.324 1.237 1.515 1.564 1.443 120.41 115.56 121.07 113.28 111.36 113.22 123.26 +* +* +* +* 127 PHE 127 1.317 1.239 1.511 1.546 1.444 122.94 115.86 120.70 110.12 108.76 111.88 123.43 128 GLY 128 1.296 1.229 1.484 - 1.425 121.69 116.97 119.54 - 109.28 - 123.49 ** +* +* * ** 129 GLU 129 1.303 1.235 1.502 1.540 1.442 121.61 116.99 120.20 110.04 108.23 110.30 122.79 +* * * +* Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 130 TRP 130 1.302 1.234 1.528 1.536 1.428 119.83 117.68 120.03 112.05 108.49 111.45 122.27 +* +* * * +* 131 ASN 131 1.317 1.232 1.512 1.533 1.449 120.28 115.21 121.60 110.90 112.50 113.51 123.13 +* +* 132 PHE 132 1.310 1.223 1.512 1.536 1.442 122.62 115.06 121.06 110.94 108.61 111.13 123.89 * * 133 GLU 133 1.339 1.230 1.536 1.516 1.418 125.25 116.08 120.93 111.10 109.50 104.10 122.96 ** +* +*** +*** 134 GLU 134 1.330 1.219 1.527 1.531 1.445 121.51 116.92 121.00 110.41 109.74 111.25 122.06 135 TRP 135 1.320 1.200 1.510 1.533 1.439 119.50 117.07 119.89 111.70 110.40 113.05 123.00 +* * * +* 136 LYS 136 1.333 1.238 1.536 1.538 1.470 122.02 115.13 121.35 110.21 109.79 111.05 123.52 137 ARG 137 1.318 1.239 1.530 1.516 1.450 123.73 114.39 121.78 107.61 110.04 107.04 123.74 * * ** ** 138 LEU 138 1.312 1.237 1.512 1.525 1.460 124.38 114.53 121.69 109.28 110.77 109.07 123.78 * * * 139 HIS 139 1.297 1.236 1.535 1.528 1.453 124.44 116.26 120.72 111.64 111.54 109.58 123.02 ** +* ** 140 LYS 140 1.341 1.219 1.511 1.541 1.458 122.08 115.55 121.04 108.50 108.80 111.05 123.39 141 LYS 141 1.328 1.197 1.528 1.528 1.433 121.92 118.55 119.02 111.98 112.15 111.63 122.41 +* * * * +* 142 LYS 142 1.350 1.240 1.503 1.538 1.487 121.04 113.28 122.37 105.04 108.65 111.96 124.35 +* * +* * +** +** 143 PHE 143 1.303 1.232 1.523 1.527 1.415 123.71 116.16 120.89 111.72 109.03 107.78 122.88 +* ** * +* ** 144 ILE 144 1.326 1.185 1.519 1.544 1.441 120.79 117.94 119.65 108.21 110.31 114.22 122.41 ** +* ** 145 GLU 145 1.336 1.236 1.514 1.533 1.470 121.64 115.65 120.99 109.80 110.04 112.09 123.35 146 THR 146 1.319 1.230 1.538 1.547 1.434 121.42 116.55 120.65 110.52 109.28 110.45 122.68 * * 147 PHE 147 1.327 1.229 1.498 1.521 1.457 121.55 116.01 120.37 113.01 113.17 113.16 123.62 * +* +* +* 148 LYS 148 1.316 1.229 1.531 1.536 1.436 123.25 114.06 121.93 107.54 107.55 109.88 123.93 * * * * * 149 LYS 149 1.335 1.234 1.528 1.534 1.447 123.89 116.29 120.94 110.41 110.27 108.88 122.77 * * 150 ILE 150 1.322 1.225 1.532 1.562 1.455 121.93 116.68 120.71 111.70 110.28 111.92 122.56 * * 151 MET 151 1.327 1.233 1.525 1.535 1.466 121.25 116.29 121.01 110.21 110.14 112.04 122.69 152 GLU 152 1.326 1.227 1.525 1.530 1.457 121.59 115.59 121.12 110.39 110.04 111.40 123.27 153 CYS 153 1.322 1.229 1.529 1.540 1.452 122.69 116.18 121.02 110.93 109.79 109.88 122.80 154 LYS 154 1.326 1.223 1.519 1.536 1.455 121.36 115.02 120.95 109.84 108.94 111.02 124.03 155 LYS 155 1.330 1.228 1.533 1.528 1.458 123.90 115.06 121.18 108.38 110.26 108.53 123.76 * * * 156 LYS 156 1.322 1.235 1.536 1.563 1.444 123.69 116.82 121.00 114.86 110.33 108.64 122.18 +* * +** * +** 157 PRO 157 1.345 1.236 1.532 1.526 1.454 123.01 114.88 121.50 110.90 115.20 103.94 123.56 * * * * 158 GLN 158 1.309 1.237 1.507 1.547 1.454 124.34 115.51 120.92 110.17 108.33 114.11 123.46 * * * ** ** 159 GLY 159 1.304 1.248 1.498 - 1.431 121.34 116.00 120.65 - 111.32 - 123.33 +* * * +* 160 GLN 160 1.311 1.239 1.516 1.533 1.437 121.66 115.79 120.87 110.65 109.79 111.39 123.30 * * * Residue-by-residue listing for refined_2 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 1.306 1.227 1.507 - 1.438 120.84 116.84 120.64 - 112.34 - 122.52 +* +* 162 ASN 162 1.321 1.234 1.509 1.542 1.453 121.13 115.29 121.48 110.93 110.11 112.33 123.10 * * 163 ASP 163 1.302 1.229 1.506 1.542 1.455 122.43 116.08 120.95 110.34 111.22 110.51 122.97 +* +* 164 ASP 164 1.309 1.238 1.515 1.546 1.447 121.13 114.71 121.66 110.91 111.83 112.71 123.60 * * * 165 ILE 165 1.300 1.230 1.523 1.579 1.438 124.28 115.10 121.89 112.42 108.58 113.56 122.86 ** * * * +* * ** 166 SER 166 1.308 1.244 1.523 1.537 1.439 122.48 116.57 120.28 110.59 109.43 108.72 123.14 +* * * +* 167 HIS 167 1.314 1.233 1.515 1.538 1.450 123.03 117.08 119.81 110.57 109.34 110.89 123.11 * * 168 VAL 168 1.322 1.237 1.521 1.561 1.454 121.65 116.67 121.07 111.28 110.18 112.45 122.26 169 LEU 169 1.299 1.242 1.523 1.535 1.436 120.46 114.90 121.76 110.52 113.38 111.12 123.33 ** * ** 170 ARG 170 1.295 1.230 1.511 1.558 1.430 123.37 116.28 120.76 112.53 104.71 111.04 122.91 ** * * * ** ** 171 GLU 171 1.295 1.232 1.514 1.527 1.430 121.14 115.42 120.92 110.94 111.14 109.44 123.65 ** * ** 172 ASP 172 1.298 1.232 1.487 1.538 1.454 123.53 112.88 121.96 109.35 107.05 111.05 125.13 ** +* * +* * * ** 173 GLN 173 1.299 - 1.523 1.533 1.436 125.50 - - 110.98 107.37 111.07 - ** * ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** ** +** ** +** *** +* * +** ** +*** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 1.281 1.350 1.313 .014 *** +* * C-N (Pro) 1.341 .016 7 1.337 1.353 1.344 .005 C-O C-O 1.231 .020 172 1.185 1.250 1.231 .010 ** CA-C CH1E-C (except Gly) 1.525 .021 161 1.471 1.558 1.519 .014 +** +* CH2G*-C (Gly) 1.516 .018 12 1.484 1.514 1.501 .009 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.509 1.522 1.516 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.536 1.580 1.558 .013 * CH1E-CH2E (the rest) 1.530 .020 128 1.498 1.572 1.536 .013 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.404 1.494 1.448 .015 +** +* NH1-CH2G* (Gly) 1.451 .016 12 1.421 1.461 1.438 .012 +* N-CH1E (Pro) 1.466 .015 7 1.454 1.471 1.462 .007 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 2.0 153 112.88 119.05 116.14 1.08 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.57 117.34 116.36 .65 CH1E-C-N (Pro) 116.9 1.5 7 114.88 117.35 115.84 .99 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.58 125.13 123.07 .59 * O-C-N (Pro) 122.0 1.4 7 122.24 123.86 123.25 .52 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.14 127.70 122.22 1.39 * *** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.81 123.92 121.23 1.21 * +* C-N-CH1E (Pro) 122.6 5.0 7 121.95 123.38 122.72 .42 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 119.02 122.43 120.78 .63 * CH2G*-C-O (Gly) 120.8 2.1 12 119.54 121.48 120.46 .56 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.12 111.30 110.52 .47 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.52 112.42 110.29 1.42 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.04 114.86 110.47 1.49 +** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.20 115.86 110.09 1.88 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 109.28 115.25 111.77 1.75 * N-CH1E-C (Pro) 111.8 2.5 7 110.18 115.20 112.33 1.78 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 110.06 111.38 110.74 .61 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 106.63 114.22 111.68 1.41 +** +* N-CH1E-CH2E (Pro) 103.0 1.1 7 102.99 104.27 103.85 .37 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 104.10 115.53 110.97 1.75 +*** +** ------------------------------------------------------------------------------------------------------------- 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_2 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] 131 85.6% Residues in additional allowed regions [a,b,l,p] 17 11.1% Residues in generously allowed regions [~a,~b,~l,~p] 4 2.6% 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 85.6 83.8 10.0 .2 Inside b. Omega angle st dev 172 3.4 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 161 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 102 .9 .8 .2 .5 Inside f. Overall G-factor 173 .0 -.4 .3 1.3 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 19 5.3 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 60 8.8 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 71 7.7 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 150 8.7 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 40 5.7 20.4 5.0 -2.9 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% 85.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .91 3 Residue-by-residue listing for refined_2 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.53 Chi1-chi2 distribution -.14 Chi1 only -.01 Chi3 & chi4 .37 Omega -.01 ------ -.14 ===== Main-chain covalent forces:- Main-chain bond lengths .07 Main-chain bond angles .36 ------ .24 ===== OVERALL AVERAGE -.01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.