Residue-by-residue listing for refined_6 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 - - - - - - - - - - - 183.6 - - - 2 HIS 2 ~l - - -60.4 - - - - - - - 179.1 - 31.6 - ** ** 3 HIS 3 B - 181.1 - - - - - - - - 182.3 - 34.7 - 4 HIS 4 B - - -59.3 - - - - - - - 175.6 - 34.4 - 5 HIS 5 B - - -71.7 - - - - - - - 174.1 - 34.4 - * * 6 HIS 6 B 53.7 - - - - - - - - - 185.2 - 30.5 - 7 HIS 7 B - - -62.2 - - - - - - - 172.7 - 34.9 - * * 8 LEU 8 b - - -62.4 181.0 - - - - - - 185.2 - 33.0 - 9 GLU 9 B - 189.4 - 179.0 - - - - - - 178.5 -.8 35.2 - +* +* 10 CYS 10 B - 179.2 - - - - - - - - 177.8 - 34.5 - 11 SER 11 B - - -57.9 - - - - - - - 179.8 - 34.8 - 12 SER 12 S A - 184.1 - - - - - - - - 176.0 - 34.0 - 13 ASP 13 S B - - -69.7 - - - - - - - 178.4 - 32.7 - 14 SER 14 B - 180.5 - - - - - - - - 177.3 -1.1 35.3 - * * 15 LEU 15 B - - -71.4 - - - - - - - 180.7 - 33.3 - 16 GLN 16 e B 59.7 - - 176.6 - - - - - - 180.1 -.8 34.0 - +* +* 17 LEU 17 E B - - -59.5 179.1 - - - - - - 187.8 - 32.2 - * * 18 HIS 18 E B - - -55.4 - - - - - - - 174.5 -2.3 35.6 - 19 ASN 19 E B 44.4 - - - - - - - - - 183.3 - 30.3 - * * * Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 VAL 20 E B - 179.7 - - - - - - - - 178.6 -1.3 35.3 - * * 21 PHE 21 E B - 178.4 - - - - - - - - 177.6 -3.1 35.6 - * * 22 VAL 22 E B - - -70.6 - - - - - - - 190.6 -2.9 31.3 - +* * +* 23 TYR 23 a 52.4 - - - - - - - - - 181.4 - 30.6 - 24 GLY 24 t - - - - - - - - - - - 185.3 - - - 25 SER 25 T A - 182.2 - - - - - - - - 183.4 - 34.5 - 26 PHE 26 T a - - -56.8 - - - - - - - 180.6 - 34.5 - 27 GLN 27 t A - 190.3 - - - - - - - - 184.1 -1.7 36.4 - 28 ASP 28 h B - 169.8 - - - - - - - - 179.2 - 36.0 - 29 PRO 29 H - - - - - -72.3 -72.3 -25.0 - - - 180.5 - 38.5 - * * * 30 ASP 30 H A - 175.0 - - - -64.1 -43.2 - - - 178.6 - 32.7 - 31 VAL 31 H A 64.2 - - - - -69.3 -29.6 - - - 177.4 - 31.4 - 32 ILE 32 H A - - -67.6 - - -65.7 -47.5 - - - 175.9 -.9 32.0 - * * 33 ASN 33 H A - - -74.7 - - -55.8 -32.7 - - - 180.0 -2.6 33.0 - 34 VAL 34 H A - 180.8 - - - -81.6 -37.0 - - - 182.1 -1.3 32.9 - * * * 35 MET 35 H A - 190.7 - 187.5 - -63.8 -36.5 - - - 176.3 -2.7 34.6 - 36 LEU 36 h a 54.4 - - 161.1 - - - - - - 189.8 -2.2 30.2 - +* * +* 37 ASP 37 S a - - -62.9 - - - - - - - 184.4 - 36.8 - 38 ARG 38 b - - -62.7 178.6 - - - - - - 175.7 - 36.5 - 39 THR 39 B - - -58.4 - - - - - - - 176.1 - 34.8 - 40 PRO 40 - - - - - -58.8 - - - - - 182.1 - 38.9 - * * 41 GLU 41 E b - 186.7 - 184.0 - - - - - - 185.9 -1.3 34.9 - * * * 42 ILE 42 E B - - -55.3 180.6 - - - - - - 172.8 - 36.5 - * * 43 VAL 43 E B 61.1 - - - - - - - - - 177.0 -1.7 33.5 - 44 SER 44 E B - - -59.9 - - - - - - - 181.7 - 35.4 - 45 ALA 45 E B - - - - - - - - - - 178.9 -1.9 34.1 - 46 THR 46 E B - - -57.2 - - - - - - - 176.9 -3.2 36.0 - +* +* 47 LEU 47 E b - 175.0 - - - - - - - - 179.6 -3.5 34.6 - +* +* 48 PRO 48 E - - - - - -84.7 - - - - - 178.9 - 38.5 - +* * +* 49 GLY 49 E - - - - - - - - - - - 180.0 -2.6 - - 50 PHE 50 E B - - -69.7 - - - - - - - 181.7 -.6 33.9 - +* +* 51 GLN 51 E B - 187.2 - - - - - - - - 176.8 -3.2 35.0 - +* +* 52 ARG 52 E B - 177.0 - 182.9 - - - - - - 177.7 -.5 35.7 - ** ** 53 PHE 53 e B - - -72.7 - - - - - - - 185.9 -1.9 32.1 - * * 54 ARG 54 B - - -78.2 - - - - - - - 175.8 -1.6 32.4 - 55 LEU 55 B 68.7 - - 179.9 - - - - - - 178.4 - 34.2 - 56 LYS 56 S a - - -72.4 182.5 - - - - - - 174.8 -.7 31.7 - +* +* 57 GLY 57 S - - - - - - - - - - - 185.3 -.7 - - +* +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 ARG 58 S A - 187.5 - - - - - - - - 182.4 - 32.9 - 59 LEU 59 S B - 186.3 - - - - - - - - 184.6 - 32.1 - 60 TYR 60 B - - -61.2 - - - - - - - 179.7 - 35.9 - 61 PRO 61 - - - - - -69.3 - - - - - 181.1 - 39.0 - * * 62 CYS 62 e B 54.6 - - - - - - - - - 178.1 -.6 34.0 - +* +* 63 ILE 63 E B - - -58.7 - - - - - - - 173.4 -.7 36.7 - * +* +* 64 VAL 64 E B - - -56.8 - - - - - - - 177.1 -1.5 34.7 - 65 PRO 65 E - - - - - -65.0 - - - - - 181.5 - 37.7 - * * 66 SER 66 E B - 181.8 - - - - - - - - 182.1 -1.7 34.7 - 67 GLU 67 E A - - -57.0 179.2 - - - - - - 181.2 - 33.0 - 68 LYS 68 E a - - -66.7 184.8 - - - - - - 179.9 - 33.0 - 69 GLY 69 E - - - - - - - - - - - 179.5 - - - 70 GLU 70 E B 67.9 - - 185.1 - - - - - - 179.1 - 34.3 - 71 VAL 71 E B - 184.8 - - - - - - - - 174.1 -2.2 35.9 - * * 72 HIS 72 E B - - -67.0 - - - - - - - 183.7 - 32.8 - 73 GLY 73 E - - - - - - - - - - - 185.5 -2.9 - - * * 74 LYS 74 E B - - -53.7 - - - - - - - 174.8 -1.3 37.4 - * * 75 VAL 75 E B - 169.1 - - - - - - - - 179.7 -2.8 34.3 - * * 76 LEU 76 E B - - -57.1 181.1 - - - - - - 176.7 -3.3 36.1 - +* +* 77 MET 77 E B - - -81.9 - - - - - - - 179.2 -2.9 32.2 - * * * 78 GLY 78 E - - - - - - - - - - - 177.9 -1.5 - - 79 VAL 79 E B 66.4 - - - - - - - - - 183.4 -2.4 32.4 - 80 THR 80 E B - - -28.7 - - - - - - - 183.4 -.5 35.9 - +** ** +** 81 SER 81 H A - - -57.1 - - -58.5 -36.8 - - - 180.5 -.6 33.0 - +* +* 82 ASP 82 H A - 188.0 - - - -66.8 -44.7 - - - 176.0 - 33.1 - 83 GLU 83 H A - - -64.6 - - -68.6 -30.6 - - - 174.7 - 33.7 - 84 LEU 84 H A - 177.9 - - - -60.3 -50.3 - - - 177.4 -2.3 35.7 - 85 GLU 85 H A - - -64.9 180.6 - -65.0 -28.6 - - - 174.4 -2.7 32.1 - 86 ASN 86 H A - 162.0 - - - -62.1 -49.4 - - - 178.7 -1.4 34.8 - * * 87 LEU 87 H A - - -60.7 176.2 - -64.4 -38.8 - - - 178.2 -2.5 35.2 - 88 ASP 88 H A - 179.9 - - - -64.9 -35.5 - - - 176.9 -2.3 34.7 - 89 ALA 89 H A - - - - - -75.6 -48.3 - - - 181.7 -1.9 35.3 - 90 VAL 90 H A - 163.9 - - - -63.1 -57.0 - - - 177.5 -3.6 31.8 - * +* ** ** 91 GLU 91 h A - - -65.4 - - - - - - - 184.7 -3.2 32.2 - +* +* 92 GLY 92 T - - - - - - - - - - - 182.3 -.7 - - +* +* 93 ASN 93 T A - - -60.4 - - - - - - - 179.6 -.5 33.2 - ** ** 94 GLU 94 e a - - -62.1 183.3 - - - - - - 181.1 -1.5 33.2 - 95 TYR 95 E B - - -58.7 - - - - - - - 177.6 -1.1 35.5 - * * Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 96 GLU 96 E B - 184.7 - 178.0 - - - - - - 183.7 -1.0 34.0 - * * 97 ARG 97 E B - 187.2 - 186.2 - - - - - - 179.0 - 37.0 - 98 VAL 98 E B - - -62.7 - - - - - - - 180.8 -3.1 32.6 - * * 99 THR 99 E B - 183.4 - - - - - - - - 181.1 - 33.8 - 100 VAL 100 E B - - -64.3 - - - - - - - 176.7 -3.4 34.4 - +* +* 101 GLY 101 E - - - - - - - - - - - 180.7 - - - 102 ILE 102 E B 56.7 - - - - - - - - - 179.4 -3.1 32.0 - * * 103 VAL 103 E B - 181.9 - - - - - - - - 180.6 -3.0 34.2 - * * 104 ARG 104 E B - - -66.3 171.9 - - - - - - 176.6 -3.6 35.6 - ** ** 105 GLU 105 e A - - -63.3 181.8 - - - - - - 178.4 -2.7 34.5 - 106 ASP 106 T A - 175.6 - - - - - - - - 183.4 -1.1 35.7 - * * 107 ASN 107 T a 66.1 - - - - - - - - - 177.1 -.7 33.7 - +* +* 108 SER 108 t l - 186.1 - - - - - - - - 179.6 -2.4 31.8 - 109 GLU 109 e B - - -65.4 - - - - - - - 184.1 - 32.6 - 110 LYS 110 E B 58.7 - - - - - - - - - 180.0 - 30.6 - 111 MET 111 E B - - -68.6 174.8 - - - - - - 177.9 -3.3 34.2 - +* +* 112 ALA 112 E B - - - - - - - - - - 182.3 - 34.0 - 113 VAL 113 E B - - -61.9 - - - - - - - 175.5 -3.0 34.5 - * * 114 LYS 114 E B - - -64.4 - - - - - - - 176.7 -1.7 34.5 - 115 THR 115 E B - 193.4 - - - - - - - - 183.0 -2.7 32.7 - 116 TYR 116 E B - - -59.6 - - - - - - - 179.7 - 34.2 - 117 MET 117 E B 61.7 - - 176.6 - - - - - - 179.5 -1.2 31.9 - * * 118 TRP 118 E B - 190.9 - - - - - - - - 189.9 -3.3 35.2 - +* +* +* 119 ILE 119 e A - - -51.8 - - - - - - - 182.0 -.8 33.3 - +* +* 120 ASN 120 S A - 182.2 - - - - - - - - 186.8 - 34.4 - * * 121 LYS 121 ~l 55.3 - - - - - - - - - 182.4 - 26.4 - ** ** ** 122 ALA 122 ~a - - - - - - - - - - 180.4 - 34.2 - ** ** 123 ASP 123 t B - - -61.5 - - - - - - - 176.7 - 35.1 - 124 PRO 124 T - - - - - -80.1 - - - - - 178.6 - 38.8 - * * * 125 ASP 125 T A - - -66.8 - - - - - - - 181.9 - 33.2 - 126 MET 126 t A 59.8 - - 183.7 - - - - - - 183.6 -.5 34.8 - ** ** 127 PHE 127 b - 183.6 - - - - - - - - 179.9 - 33.3 - 128 GLY 128 - - - - - - - - - - - 179.8 - - - 129 GLU 129 B 53.3 - - 177.0 - - - - - - 177.1 - 32.9 - 130 TRP 130 h B - - -81.0 - - - - - - - 183.0 - 33.2 - 131 ASN 131 H A - 180.1 - - - -57.9 -30.9 - - - 179.0 - 33.5 - 132 PHE 132 H A - - -60.9 - - -62.4 -47.6 - - - 178.6 - 33.3 - 133 GLU 133 H A - - -60.8 - - -74.2 -32.2 - - - 177.9 -.5 35.2 - ** ** Residue-by-residue listing for refined_6 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 - 176.3 - 177.2 - -58.9 -54.1 - - - 179.1 -2.4 33.7 - * * 135 TRP 135 H A - 177.2 - - - -65.5 -40.8 - - - 177.7 -2.9 31.2 - * * 136 LYS 136 H A - 177.9 - - - -55.8 -41.5 - - - 177.4 -2.0 33.6 - 137 ARG 137 H A - 171.6 - 176.8 - -60.1 -52.1 - - - 180.4 -2.6 34.9 - * * 138 LEU 138 H A - - -75.3 - - -70.8 -20.4 - - - 178.0 -2.2 32.1 - +* +* 139 HIS 139 H A - 183.9 - - - -80.8 -40.2 - - - 176.8 -2.2 34.4 - * * 140 LYS 140 H A - 178.3 - 182.3 - -69.4 -39.8 - - - 182.6 -2.8 34.1 - * * 141 LYS 141 H A - 186.8 - 177.4 - -53.7 -31.0 - - - 179.2 -2.9 34.2 - * * 142 LYS 142 H A - 188.4 - - - -65.3 -39.3 - - - 177.4 -.6 34.2 - +* +* 143 PHE 143 H A - - -58.8 - - -76.7 -32.9 - - - 180.5 -1.3 35.0 - * * 144 ILE 144 H A - - -58.9 - - -58.5 -31.2 - - - 181.0 -2.3 31.5 - 145 GLU 145 H A - - -59.7 185.6 - -50.6 -44.7 - - - 179.7 -1.3 34.6 - * * * 146 THR 146 H A - 185.2 - - - -68.8 -40.6 - - - 178.4 -1.0 31.3 - * * 147 PHE 147 H A - - -75.2 - - -69.6 -30.0 - - - 175.2 -1.0 30.1 - * * * 148 LYS 148 H A - 181.3 - 183.0 - -59.7 -43.1 - - - 180.6 -3.1 35.2 - * * 149 LYS 149 H A - - -60.1 178.5 - -72.6 -28.5 - - - 177.2 -1.5 33.8 - 150 ILE 150 H A - - -61.0 175.0 - -73.7 -43.2 - - - 180.4 -1.4 33.2 - 151 MET 151 H A 63.8 - - 179.4 - -70.8 -29.9 - - - 176.8 -3.2 31.8 - +* +* 152 GLU 152 H A - - -66.3 - - -66.1 -33.4 - - - 177.8 -1.9 33.6 - 153 CYS 153 H A - 183.6 - - - -71.9 -33.8 - - - 179.3 -.9 33.6 - +* +* 154 LYS 154 H A - - -63.3 183.4 - -76.4 -44.8 - - - 180.2 -1.4 35.8 - 155 LYS 155 h b - 174.1 - - - - - - - - 179.3 -3.3 32.8 - +* +* 156 LYS 156 B 58.9 - - 178.1 - - - - - - 170.7 -1.0 35.2 - +* * +* 157 PRO 157 - - - - - -65.2 - - - - - 183.4 - 39.2 - +* +* 158 GLN 158 B 60.2 - - 179.5 - - - - - - 177.1 - 34.4 - 159 GLY 159 - - - - - - - - - - - 181.9 - - - 160 GLN 160 B - 179.6 - 182.6 - - - - - - 176.0 - 35.8 - 161 GLY 161 - - - - - - - - - - - 184.1 - - - 162 ASN 162 B - 190.6 - - - - - - - - 180.3 -1.2 34.2 - * * 163 ASP 163 B - 176.3 - - - - - - - - 177.6 - 33.3 - 164 ASP 164 B - 178.1 - - - - - - - - 178.3 -.6 34.8 - +* +* 165 ILE 165 b - 179.5 - 178.4 - - - - - - 179.5 - 31.0 - 166 SER 166 B - - -62.3 - - - - - - - 180.9 - 33.9 - 167 HIS 167 A - - -54.4 - - - - - - - 174.7 -.8 35.7 - +* +* 168 VAL 168 l - 187.5 - - - - - - - - 178.3 - 32.7 - 169 LEU 169 B - 181.1 - - - - - - - - 180.4 - 34.6 - Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 170 ARG 170 B - - -58.1 - - - - - - - 179.9 -.6 34.9 - +* +* 171 GLU 171 b - - -65.2 183.0 - - - - - - 175.8 - 32.5 - 172 ASP 172 b 54.3 - - - - - - - - - 183.8 -1.4 31.0 - 173 GLN 173 - - 184.2 - - - - - - - - - -1.9 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +** +* * +* +* ** ** +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.9 181.4 -63.0 179.8 -70.8 -66.1 -38.5 - - - 179.7 -1.9 34.0 Standard deviations: 5.9 6.4 7.6 4.5 9.1 7.2 8.4 - - - 3.4 1.0 1.9 Numbers of values: 22 58 70 42 7 41 41 0 0 0 172 100 161 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_6 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 - 1.245 1.513 - 1.462 - 115.79 120.38 - 112.54 - 123.81 2 HIS 2 1.333 1.229 1.515 1.553 1.470 124.48 115.79 120.96 110.29 110.69 114.16 123.20 * +* ** ** 3 HIS 3 1.310 1.231 1.518 1.540 1.455 122.50 117.50 120.01 110.89 108.64 109.83 122.48 * * 4 HIS 4 1.316 1.230 1.513 1.538 1.454 120.45 115.96 120.66 109.35 111.02 111.07 123.36 5 HIS 5 1.312 1.229 1.500 1.534 1.454 123.06 115.78 120.70 107.61 110.51 113.04 123.51 * * * * * 6 HIS 6 1.298 1.228 1.506 1.561 1.437 122.58 115.70 120.99 113.66 109.06 113.38 123.28 ** +* * +* +* ** 7 HIS 7 1.304 1.231 1.503 1.544 1.448 121.76 116.03 120.54 108.52 111.07 111.34 123.43 +* * +* 8 LEU 8 1.304 1.230 1.506 1.537 1.439 121.54 115.32 121.27 111.17 107.57 112.57 123.32 +* * * * +* 9 GLU 9 1.298 1.242 1.526 1.529 1.436 122.18 116.10 120.75 111.03 110.33 108.50 123.14 ** * * ** 10 CYS 10 1.306 1.235 1.516 1.541 1.436 122.13 116.50 120.15 110.36 109.10 110.62 123.34 +* * +* 11 SER 11 1.312 1.250 1.537 1.528 1.442 122.50 116.18 120.63 110.66 110.78 109.13 123.18 * * 12 SER 12 1.325 1.232 1.529 1.544 1.441 122.29 116.00 120.96 111.46 109.06 110.25 123.02 Residue-by-residue listing for refined_6 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 1.320 1.234 1.502 1.541 1.446 121.49 115.43 121.19 110.18 109.76 113.22 123.32 * +* +* 14 SER 14 1.296 1.241 1.510 1.551 1.427 122.58 116.95 120.13 110.59 107.64 109.97 122.87 ** * +* * ** 15 LEU 15 1.310 1.237 1.515 1.538 1.421 121.29 115.89 121.00 111.12 109.57 111.50 123.05 * +* +* 16 GLN 16 1.299 1.239 1.504 1.538 1.436 121.92 116.27 120.48 110.61 109.52 111.08 123.25 ** * ** 17 LEU 17 1.298 1.232 1.514 1.511 1.429 121.39 115.72 121.05 112.12 110.23 111.47 123.19 ** +* * ** 18 HIS 18 1.303 1.246 1.512 1.534 1.448 122.47 115.47 120.59 108.71 110.99 110.08 123.87 +* +* 19 ASN 19 1.315 1.239 1.523 1.540 1.453 123.28 115.32 121.64 112.83 112.01 112.81 123.02 * * * * 20 VAL 20 1.314 1.228 1.517 1.572 1.454 123.05 116.76 120.19 108.97 108.98 111.14 123.04 * * * 21 PHE 21 1.303 1.240 1.516 1.544 1.437 121.98 116.08 120.73 111.01 108.85 108.57 123.18 +* * * +* 22 VAL 22 1.307 1.242 1.497 1.552 1.439 121.67 115.79 120.99 111.17 109.82 114.38 123.20 +* * +* +* 23 TYR 23 1.292 1.232 1.530 1.536 1.425 120.68 118.58 119.41 113.79 115.87 109.78 122.01 +** +* * +* +* +** 24 GLY 24 1.322 1.225 1.513 - 1.450 118.64 116.15 120.36 - 114.40 - 123.47 * * 25 SER 25 1.318 1.221 1.539 1.549 1.465 123.63 116.88 120.87 110.90 112.54 108.79 122.22 * * * 26 PHE 26 1.318 1.214 1.519 1.523 1.457 120.86 116.12 121.16 110.26 111.12 109.76 122.66 27 GLN 27 1.323 1.246 1.550 1.536 1.466 123.08 114.37 121.69 109.83 109.62 107.84 123.92 * +* +* 28 ASP 28 1.304 1.224 1.543 1.529 1.438 124.88 118.14 120.36 110.64 111.02 107.43 121.49 +* * +* +* +* 29 PRO 29 1.344 1.233 1.533 1.525 1.472 122.49 117.06 120.77 110.14 112.93 103.56 122.15 30 ASP 30 1.318 1.239 1.512 1.531 1.458 121.08 116.18 120.54 110.93 110.54 111.92 123.22 31 VAL 31 1.324 1.222 1.532 1.572 1.447 120.91 116.86 120.62 111.77 110.10 113.47 122.47 * * * * 32 ILE 32 1.333 1.233 1.533 1.549 1.444 121.36 117.10 120.20 112.04 110.75 111.87 122.66 * * 33 ASN 33 1.334 1.226 1.522 1.540 1.475 121.23 116.49 120.84 108.93 111.47 113.11 122.67 +* +* 34 VAL 34 1.314 1.232 1.537 1.559 1.452 121.37 116.82 120.51 110.41 111.44 112.05 122.67 * * 35 MET 35 1.335 1.239 1.524 1.531 1.452 121.74 116.38 120.74 109.39 110.25 110.90 122.87 36 LEU 36 1.321 1.227 1.525 1.566 1.442 120.60 116.47 120.24 111.17 112.85 114.49 123.19 +* ** ** 37 ASP 37 1.328 1.228 1.500 1.568 1.476 123.63 114.13 122.00 105.35 108.56 112.51 123.87 * +* * * +** * +** 38 ARG 38 1.315 1.228 1.504 1.528 1.448 123.13 115.71 120.79 107.65 110.09 110.05 123.50 * * * 39 THR 39 1.305 1.233 1.525 1.536 1.431 122.94 117.51 120.14 110.17 109.62 110.21 122.27 +* * +* 40 PRO 40 1.346 1.233 1.524 1.531 1.465 122.74 116.21 120.14 110.08 111.03 103.56 123.65 * * 41 GLU 41 1.321 1.237 1.531 1.522 1.457 123.10 115.72 121.09 110.05 109.98 109.68 123.19 42 ILE 42 1.296 1.238 1.514 1.557 1.445 122.50 115.48 121.00 107.45 110.88 110.32 123.52 ** ** Residue-by-residue listing for refined_6 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 1.299 1.243 1.530 1.564 1.428 122.36 116.71 120.44 110.54 108.47 112.32 122.81 ** +* ** 44 SER 44 1.306 1.241 1.517 1.516 1.434 121.65 116.27 120.93 110.23 108.84 109.25 122.79 +* * +* 45 ALA 45 1.299 1.234 1.503 1.507 1.431 121.50 114.35 121.64 110.21 111.67 110.35 124.01 ** * * ** 46 THR 46 1.283 1.217 1.511 1.543 1.415 123.98 116.26 120.39 108.99 108.39 110.20 123.33 *** ** * * *** 47 LEU 47 1.283 1.223 1.524 1.536 1.426 122.79 117.90 120.34 111.08 108.91 109.77 121.66 *** +* *** 48 PRO 48 1.331 1.240 1.526 1.528 1.444 122.01 116.49 120.62 111.04 111.20 103.23 122.86 * * 49 GLY 49 1.312 1.232 1.507 - 1.441 120.30 115.91 121.28 - 111.72 - 122.80 * * 50 PHE 50 1.301 1.209 1.482 1.547 1.437 123.24 117.83 119.60 110.50 107.51 112.14 122.57 ** * ** * * ** 51 GLN 51 1.288 1.226 1.497 1.535 1.423 120.04 114.72 121.31 110.31 109.62 109.99 123.92 +** * +* +** 52 ARG 52 1.297 1.241 1.496 1.530 1.424 122.94 115.99 120.39 109.50 108.43 110.05 123.62 ** * +* ** 53 PHE 53 1.277 1.218 1.515 1.517 1.428 122.41 117.69 119.47 113.49 109.57 110.63 122.76 +*** +* +* +*** 54 ARG 54 1.316 1.230 1.497 1.512 1.457 120.90 113.57 122.10 107.42 115.08 114.03 124.32 * * * * ** ** 55 LEU 55 1.313 1.241 1.523 1.561 1.425 123.75 116.49 120.71 110.59 108.57 111.25 122.72 * +* +* * +* 56 LYS 56 1.301 1.241 1.515 1.543 1.448 121.68 116.46 120.92 111.71 111.93 112.21 122.60 ** * ** 57 GLY 57 1.317 1.230 1.495 - 1.431 119.30 116.86 120.43 - 114.53 - 122.71 * * * 58 ARG 58 1.304 1.229 1.510 1.556 1.433 120.44 116.99 120.55 112.88 110.25 110.32 122.45 +* * * * +* 59 LEU 59 1.298 1.229 1.523 1.539 1.428 119.61 115.28 120.81 112.69 110.82 111.19 123.90 ** +* * * ** 60 TYR 60 1.307 1.232 1.529 1.540 1.441 124.43 119.17 119.37 110.72 109.38 108.05 121.45 +* +* * * +* 61 PRO 61 1.365 1.228 1.510 1.545 1.453 121.79 116.38 120.18 109.98 110.64 104.06 123.41 * * * 62 CYS 62 1.305 1.244 1.528 1.530 1.434 122.12 115.81 120.69 111.57 111.64 109.25 123.48 +* * +* 63 ILE 63 1.326 1.222 1.509 1.571 1.459 123.30 117.36 119.69 107.37 108.25 110.83 122.91 * * * 64 VAL 64 1.306 1.228 1.532 1.578 1.455 122.22 119.05 119.29 108.54 107.27 112.83 121.62 +* * * * +* 65 PRO 65 1.332 1.243 1.537 1.535 1.475 122.19 115.62 121.16 111.15 112.29 103.87 123.22 66 SER 66 1.316 1.230 1.531 1.539 1.441 122.83 117.10 120.62 111.14 109.21 109.50 122.28 67 GLU 67 1.307 1.222 1.534 1.516 1.448 121.05 117.19 120.54 111.18 112.45 110.42 122.25 +* +* 68 LYS 68 1.323 1.237 1.527 1.534 1.467 121.01 116.46 120.89 110.59 112.68 110.99 122.62 69 GLY 69 1.313 1.247 1.519 - 1.450 120.54 116.02 120.62 - 112.38 - 123.36 * * 70 GLU 70 1.320 1.240 1.525 1.533 1.446 122.86 116.54 120.49 109.92 108.65 111.29 122.96 71 VAL 71 1.300 1.215 1.502 1.549 1.439 121.93 117.01 120.44 107.60 109.16 111.54 122.52 ** * ** Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 HIS 72 1.284 1.228 1.477 1.520 1.433 120.66 115.68 120.69 111.83 108.48 111.81 123.62 *** ** * *** 73 GLY 73 1.293 1.243 1.479 - 1.404 119.98 115.34 120.93 - 112.16 - 123.69 +** ** +** +** 74 LYS 74 1.294 1.230 1.519 1.542 1.428 122.15 117.02 119.97 108.24 108.73 108.58 123.00 ** +* * ** 75 VAL 75 1.305 1.226 1.518 1.549 1.443 121.81 115.63 120.62 109.48 110.31 111.44 123.76 +* +* 76 LEU 76 1.315 1.229 1.517 1.541 1.441 123.14 116.50 120.46 108.21 109.46 110.34 122.99 * * 77 MET 77 1.304 1.229 1.478 1.515 1.433 122.42 114.46 121.76 111.11 112.10 112.02 123.78 +* ** * ** 78 GLY 78 1.279 1.228 1.510 - 1.425 120.53 117.31 120.26 - 112.83 - 122.43 +*** +* +*** 79 VAL 79 1.322 1.232 1.538 1.583 1.449 120.09 117.18 120.50 112.19 108.42 112.35 122.26 +* * +* 80 THR 80 1.311 1.238 1.543 1.530 1.432 121.82 117.14 120.20 109.82 109.37 108.84 122.66 * * +* +* 81 SER 81 1.322 1.230 1.546 1.531 1.460 122.32 117.42 120.18 111.38 112.83 110.11 122.37 82 ASP 82 1.327 1.232 1.531 1.533 1.466 121.22 116.39 120.65 110.80 110.48 111.46 122.95 83 GLU 83 1.334 1.217 1.540 1.543 1.469 122.19 116.79 120.79 109.09 110.21 112.43 122.41 * * 84 LEU 84 1.331 1.228 1.515 1.535 1.467 121.88 114.65 121.74 108.60 108.29 110.50 123.60 * * 85 GLU 85 1.317 1.217 1.521 1.513 1.435 123.07 115.87 120.64 112.63 111.30 110.78 123.48 * * * 86 ASN 86 1.316 1.208 1.507 1.526 1.457 123.37 115.92 120.61 110.50 110.53 109.39 123.43 * * 87 LEU 87 1.307 1.228 1.507 1.527 1.457 122.77 114.54 121.66 109.81 109.20 109.93 123.78 +* +* 88 ASP 88 1.307 1.212 1.526 1.518 1.446 123.29 116.03 121.22 110.69 110.89 109.09 122.75 +* +* 89 ALA 89 1.305 1.231 1.525 1.515 1.449 122.63 114.86 121.22 109.99 110.09 109.06 123.92 +* +* 90 VAL 90 1.315 1.230 1.561 1.581 1.448 124.71 118.07 120.11 113.49 113.12 109.92 121.83 * +* +* +* +* +* 91 GLU 91 1.318 1.228 1.532 1.526 1.472 121.49 115.52 121.38 111.54 112.56 111.13 123.08 92 GLY 92 1.310 1.233 1.523 - 1.466 123.39 117.53 119.82 - 116.04 - 122.64 * +* * +* 93 ASN 93 1.321 1.234 1.525 1.532 1.468 121.58 117.28 119.93 109.42 112.37 111.96 122.79 94 GLU 94 1.334 1.235 1.525 1.539 1.471 121.12 116.01 120.93 110.48 111.72 111.19 123.04 95 TYR 95 1.316 1.233 1.521 1.536 1.457 122.58 116.90 120.17 108.35 109.04 111.00 122.93 96 GLU 96 1.312 1.241 1.516 1.538 1.448 121.98 116.17 120.36 111.54 108.15 110.49 123.47 * * * 97 ARG 97 1.302 1.227 1.517 1.529 1.439 122.80 116.68 120.67 109.19 109.22 108.00 122.65 +* * +* 98 VAL 98 1.299 1.240 1.515 1.539 1.436 121.26 116.31 120.47 110.86 111.19 112.14 123.21 ** * ** 99 THR 99 1.304 1.235 1.528 1.570 1.442 121.85 116.59 120.85 110.68 109.39 111.58 122.53 +* * +* 100 VAL 100 1.308 1.242 1.521 1.555 1.446 122.07 115.96 120.62 108.69 110.88 112.01 123.42 * * 101 GLY 101 1.307 1.236 1.505 - 1.432 121.39 116.59 120.30 - 110.61 - 123.10 +* * +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 102 ILE 102 1.306 1.222 1.505 1.582 1.444 122.18 116.74 120.47 111.70 110.47 112.83 122.79 +* +* * +* 103 VAL 103 1.293 1.224 1.503 1.554 1.431 121.70 116.17 120.60 109.96 108.33 112.04 123.20 +** * * * +** 104 ARG 104 1.294 1.216 1.507 1.524 1.438 122.73 116.63 120.52 108.79 110.49 110.10 122.83 ** * ** 105 GLU 105 1.308 1.232 1.514 1.520 1.459 122.00 113.26 122.16 110.78 108.83 109.87 124.56 * * * 106 ASP 106 1.307 1.234 1.539 1.525 1.444 125.33 117.36 120.23 110.21 112.64 107.74 122.40 +* ** +* ** 107 ASN 107 1.332 1.226 1.546 1.539 1.474 120.15 116.80 120.07 110.29 113.30 110.13 123.13 * * 108 SER 108 1.338 1.242 1.557 1.563 1.483 124.55 116.91 121.35 112.52 112.32 110.94 121.70 +* +* * +* * +* 109 GLU 109 1.317 1.229 1.516 1.512 1.453 120.83 116.02 120.90 111.33 111.59 111.19 123.08 110 LYS 110 1.307 1.233 1.511 1.547 1.446 122.09 114.82 121.50 112.23 112.84 112.80 123.66 +* * * +* 111 MET 111 1.282 1.226 1.490 1.530 1.457 124.21 115.36 121.13 108.52 110.18 112.40 123.51 *** +* * * *** 112 ALA 112 1.281 1.229 1.507 1.518 1.446 121.82 116.99 120.11 110.52 108.80 111.07 122.89 *** *** 113 VAL 113 1.307 1.235 1.519 1.564 1.458 121.72 116.00 120.87 108.37 110.50 112.34 123.12 +* +* 114 LYS 114 1.308 1.230 1.524 1.557 1.447 121.87 117.49 119.91 109.05 108.46 112.24 122.58 +* * * +* 115 THR 115 1.306 1.243 1.526 1.563 1.443 121.18 116.46 120.32 110.71 108.90 113.19 123.21 +* +* 116 TYR 116 1.306 1.232 1.514 1.536 1.436 122.52 115.86 121.09 111.23 110.03 109.96 123.02 +* * +* 117 MET 117 1.305 1.239 1.508 1.546 1.456 121.48 115.39 120.65 110.40 110.81 113.67 123.93 +* +* +* 118 TRP 118 1.313 1.232 1.520 1.529 1.436 123.08 116.46 120.31 111.15 107.54 109.05 123.23 * * * * 119 ILE 119 1.308 1.234 1.516 1.549 1.464 121.56 116.35 120.97 109.79 112.72 111.66 122.68 * * 120 ASN 120 1.301 1.223 1.526 1.531 1.450 120.67 115.81 120.50 109.90 111.24 110.41 123.61 +* +* 121 LYS 121 1.338 1.232 1.522 1.558 1.472 124.19 115.61 121.15 112.77 114.11 116.60 123.21 * * * * +*** +*** 122 ALA 122 1.321 1.229 1.520 1.524 1.459 121.85 116.17 120.41 109.94 111.26 110.43 123.42 123 ASP 123 1.335 1.241 1.513 1.532 1.474 122.95 117.30 120.72 107.76 112.07 111.14 121.97 * * 124 PRO 124 1.338 1.228 1.531 1.526 1.456 122.64 115.62 121.39 110.52 110.68 103.29 123.00 125 ASP 125 1.331 1.221 1.501 1.535 1.454 122.13 116.30 120.59 109.55 110.91 112.56 123.08 * * * 126 MET 126 1.321 1.222 1.521 1.533 1.462 121.59 116.01 120.74 109.93 110.76 109.91 123.23 127 PHE 127 1.326 1.242 1.524 1.538 1.447 122.26 115.23 121.54 111.41 110.73 110.67 123.19 128 GLY 128 1.301 1.244 1.497 - 1.414 121.47 116.16 120.45 - 111.06 - 123.39 +* * ** ** 129 GLU 129 1.303 1.228 1.520 1.543 1.434 122.24 115.59 120.99 111.41 111.07 111.23 123.39 +* * +* 130 TRP 130 1.311 1.240 1.508 1.532 1.447 122.71 115.63 120.49 109.93 110.21 112.54 123.87 * * * 131 ASN 131 1.314 1.233 1.534 1.536 1.465 124.03 116.69 120.59 111.16 112.41 109.87 122.71 * * * Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 132 PHE 132 1.326 1.235 1.533 1.536 1.463 121.79 115.86 120.92 111.04 110.96 110.72 123.18 133 GLU 133 1.324 1.225 1.518 1.521 1.465 122.36 115.80 120.86 109.48 109.81 109.83 123.35 134 GLU 134 1.334 1.232 1.514 1.529 1.451 122.34 116.78 120.27 110.35 110.59 111.09 122.93 135 TRP 135 1.324 1.220 1.511 1.533 1.439 119.83 117.00 119.89 111.42 111.04 113.44 123.08 * * +* +* 136 LYS 136 1.332 1.228 1.532 1.534 1.456 120.98 115.82 120.97 110.19 110.17 111.54 123.20 137 ARG 137 1.316 1.222 1.524 1.507 1.441 123.06 117.01 120.17 110.10 112.00 108.98 122.79 * * 138 LEU 138 1.321 1.235 1.523 1.541 1.462 121.39 115.89 121.13 111.11 111.95 112.15 122.98 139 HIS 139 1.305 1.222 1.525 1.541 1.449 121.74 116.27 120.83 110.67 108.99 110.44 122.88 +* +* 140 LYS 140 1.331 1.222 1.505 1.543 1.453 121.52 114.97 120.88 109.36 109.78 111.95 124.14 141 LYS 141 1.322 1.229 1.532 1.531 1.457 124.40 116.40 120.67 111.19 111.74 109.17 122.92 +* +* 142 LYS 142 1.326 1.230 1.551 1.536 1.446 121.53 116.26 121.11 110.26 109.94 110.61 122.63 * * 143 PHE 143 1.332 1.224 1.518 1.537 1.470 122.19 114.83 121.65 108.38 109.30 111.52 123.52 144 ILE 144 1.318 1.204 1.518 1.566 1.454 123.40 117.38 119.69 111.58 111.76 112.81 122.93 * * * 145 GLU 145 1.334 1.234 1.534 1.513 1.469 121.91 117.46 120.00 107.62 112.34 111.66 122.54 * * 146 THR 146 1.331 1.227 1.544 1.574 1.445 120.21 116.77 120.69 112.41 110.23 112.92 122.41 * +* +* 147 PHE 147 1.335 1.222 1.497 1.520 1.458 121.87 116.10 120.44 112.23 112.95 113.18 123.46 * * +* +* 148 LYS 148 1.309 1.211 1.523 1.534 1.437 122.67 115.85 121.15 110.15 108.50 109.96 122.89 * * * 149 LYS 149 1.322 1.238 1.533 1.531 1.455 122.12 115.73 121.35 111.19 110.30 110.14 122.92 150 ILE 150 1.318 1.233 1.543 1.571 1.452 122.05 116.96 120.71 111.11 110.45 111.45 122.30 * * 151 MET 151 1.330 1.213 1.524 1.546 1.464 121.12 117.23 120.00 110.69 111.58 113.09 122.77 +* +* 152 GLU 152 1.332 1.225 1.516 1.533 1.469 121.36 116.07 121.10 110.19 110.70 111.30 122.83 153 CYS 153 1.316 1.230 1.541 1.537 1.443 121.46 116.13 121.02 111.39 110.10 110.45 122.85 154 LYS 154 1.334 1.241 1.521 1.511 1.462 122.44 115.13 121.56 107.94 111.12 110.12 123.31 * * 155 LYS 155 1.306 1.236 1.504 1.546 1.420 123.18 113.96 122.07 112.08 109.47 111.58 123.81 +* +* * * +* 156 LYS 156 1.283 1.239 1.526 1.533 1.433 122.66 117.40 120.50 109.23 111.10 110.02 122.04 *** * *** 157 PRO 157 1.338 1.254 1.519 1.536 1.454 122.11 116.38 120.54 109.77 108.63 104.02 123.06 * * * 158 GLN 158 1.295 1.245 1.512 1.537 1.436 121.45 115.59 120.77 110.36 110.51 110.36 123.64 ** * ** 159 GLY 159 1.315 1.244 1.503 - 1.428 121.33 116.23 120.48 - 110.56 - 123.28 * * 160 GLN 160 1.290 1.237 1.514 1.532 1.433 122.31 116.58 120.15 110.07 109.26 108.85 123.24 +** * +** 161 GLY 161 1.315 1.234 1.506 - 1.438 120.75 116.22 120.47 - 109.71 - 123.30 * * 162 ASN 162 1.314 1.245 1.538 1.551 1.455 121.82 116.98 120.38 111.43 109.71 109.77 122.62 * * * 163 ASP 163 1.323 1.233 1.512 1.538 1.456 121.93 115.64 121.10 110.45 111.05 111.51 123.22 164 ASP 164 1.307 1.238 1.503 1.541 1.445 122.03 116.68 120.55 109.53 108.77 111.17 122.77 +* * +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 165 ILE 165 1.293 1.235 1.523 1.564 1.417 120.94 114.84 122.36 112.75 110.33 113.09 122.68 +** ** +* +** 166 SER 166 1.294 1.229 1.520 1.527 1.421 121.98 115.56 121.19 111.60 110.03 109.96 123.24 +** +* +** 167 HIS 167 1.312 1.233 1.492 1.550 1.460 122.41 113.58 121.33 108.85 106.25 111.21 125.07 * +* * * +* * +* 168 VAL 168 1.329 1.239 1.513 1.518 1.446 125.53 113.62 122.74 110.43 112.31 111.75 123.57 ** * * ** 169 LEU 169 1.250 1.232 1.507 1.532 1.427 123.00 116.48 120.46 110.75 108.27 110.34 123.04 *5.6* +* * *5.6* 170 ARG 170 1.300 1.234 1.505 1.523 1.444 121.66 117.39 119.88 110.22 108.54 110.19 122.73 ** ** 171 GLU 171 1.306 1.238 1.507 1.526 1.438 120.39 115.99 120.98 110.49 111.41 112.50 122.96 +* * * +* 172 ASP 172 1.309 1.228 1.510 1.550 1.442 121.50 114.44 122.46 112.92 109.84 112.91 122.96 * * * * * 173 GLN 173 1.290 - 1.509 1.532 1.423 122.55 - - 111.86 108.82 108.95 - +** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.6* * ** +* +** ** * * +** +* +*** * *5.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 1.250 1.338 1.311 .014 *5.6* * C-N (Pro) 1.341 .016 7 1.331 1.365 1.342 .011 * C-O C-O 1.231 .020 172 1.204 1.254 1.232 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 161 1.477 1.561 1.519 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.479 1.523 1.506 .011 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.507 1.524 1.516 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.518 1.583 1.559 .016 +* CH1E-CH2E (the rest) 1.530 .020 128 1.507 1.568 1.535 .012 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.415 1.483 1.447 .014 ** * NH1-CH2G* (Gly) 1.451 .016 12 1.404 1.466 1.437 .018 +** N-CH1E (Pro) 1.466 .015 7 1.444 1.475 1.460 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 2.0 153 113.26 119.17 116.20 1.01 * * CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.34 117.53 116.34 .60 CH1E-C-N (Pro) 116.9 1.5 7 115.62 117.06 116.25 .47 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.45 125.07 123.05 .57 * O-C-N (Pro) 122.0 1.4 7 122.15 123.65 123.05 .44 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.61 125.53 122.16 1.08 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.64 123.39 120.69 1.19 * +* C-N-CH1E (Pro) 122.6 5.0 7 121.79 122.74 122.28 .32 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 119.29 122.74 120.73 .59 * CH2G*-C-O (Gly) 120.8 2.1 12 119.82 121.28 120.48 .34 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.94 110.52 110.17 .23 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.37 113.49 110.31 1.59 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.35 113.79 110.45 1.37 +** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 106.25 115.87 110.34 1.56 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 12 109.71 116.04 112.38 1.78 * N-CH1E-C (Pro) 111.8 2.5 7 108.63 112.93 111.06 1.27 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.06 111.07 110.23 .73 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 108.84 114.38 111.85 1.17 +* +* N-CH1E-CH2E (Pro) 103.0 1.1 7 103.23 104.06 103.66 .31 NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.43 116.60 110.87 1.54 +* +*** ------------------------------------------------------------------------------------------------------------- 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_6 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] 19 12.4% 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 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 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 100 1.0 .8 .2 .7 Inside f. Overall G-factor 173 .0 -.4 .3 1.4 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 22 5.9 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 58 6.4 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 70 7.6 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 150 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 42 4.5 20.4 5.0 -3.2 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 8.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for refined_6 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.43 Chi1-chi2 distribution -.10 Chi1 only -.09 Chi3 & chi4 .38 Omega .05 ------ -.09 ===== Main-chain covalent forces:- Main-chain bond lengths .04 Main-chain bond angles .44 ------ .27 ===== OVERALL AVERAGE .03 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.