Residue-by-residue listing for refined_3 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 - - - - - - - - - - - 181.4 - - - 2 HIS 2 B - 186.5 - - - - - - - - 181.7 - 35.0 - 3 HIS 3 B 62.3 - - - - - - - - - 175.2 -.9 33.0 - * * 4 HIS 4 b 54.8 - - - - - - - - - 178.0 - 29.8 - * * 5 HIS 5 b - 180.7 - - - - - - - - 177.4 - 33.7 - 6 HIS 6 b - - -65.1 - - - - - - - 178.9 - 32.7 - 7 HIS 7 B - 188.6 - - - - - - - - 182.4 -.6 34.8 - +* +* 8 LEU 8 a 68.2 - - 173.7 - - - - - - 181.9 -.8 34.3 - +* +* 9 GLU 9 ~p - - -65.4 - - - - - - - 177.3 - 31.3 - ** ** 10 CYS 10 B 54.1 - - - - - - - - - 180.8 - 34.2 - 11 SER 11 B - - -57.6 - - - - - - - 181.2 - 33.4 - 12 SER 12 A - - -55.0 - - - - - - - 179.3 -1.0 34.8 - * * 13 ASP 13 l - 178.7 - - - - - - - - 184.0 - 31.6 - 14 SER 14 S b - 185.3 - - - - - - - - 181.2 - 35.5 - 15 LEU 15 S B - 197.3 - 157.1 - - - - - - 181.0 - 34.2 - * * 16 GLN 16 b - - -59.4 175.6 - - - - - - 173.7 -.8 37.2 - * +* +* 17 LEU 17 B - - -63.0 180.4 - - - - - - 188.9 - 32.1 - +* +* 18 HIS 18 E B - - -59.2 - - - - - - - 174.2 -3.1 35.3 - * * Residue-by-residue listing for refined_3 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 ASN 19 E B 50.9 - - - - - - - - - 185.1 - 29.7 - * * 20 VAL 20 E B - 179.8 - - - - - - - - 177.7 -2.1 35.6 - 21 PHE 21 E B - 181.0 - - - - - - - - 179.4 -3.2 35.1 - +* +* 22 VAL 22 E B - - -61.6 - - - - - - - 183.7 -3.4 32.7 - +* +* 23 TYR 23 A 54.4 - - - - - - - - - 180.6 - 33.2 - 24 GLY 24 t - - - - - - - - - - - 181.1 - - - 25 SER 25 T A 50.3 - - - - - - - - - 182.5 - 34.6 - 26 PHE 26 T a - - -62.8 - - - - - - - 180.0 - 35.0 - 27 GLN 27 t A 64.1 - - 180.4 - - - - - - 180.2 -1.3 33.9 - 28 ASP 28 h B - 179.1 - - - - - - - - 183.3 - 34.5 - 29 PRO 29 H - - - - - -64.0 -64.0 -28.8 - - - 179.4 - 37.7 - * * 30 ASP 30 H A - 175.5 - - - -69.1 -38.2 - - - 174.8 - 32.4 - 31 VAL 31 H A - 175.4 - - - -59.8 -38.9 - - - 179.6 - 34.5 - 32 ILE 32 H A - - -66.5 - - -58.5 -51.8 - - - 176.9 -1.4 34.4 - * * 33 ASN 33 H A - - -78.0 - - -54.2 -34.2 - - - 181.6 -2.0 34.3 - 34 VAL 34 H A - 183.0 - - - -81.1 -45.3 - - - 186.1 -1.4 33.6 - * * * 35 MET 35 H A - 199.7 - - - -67.2 -37.4 - - - 176.8 -3.4 34.8 - +* +* 36 LEU 36 h a 52.4 - - 164.3 - - - - - - 183.9 -2.7 27.8 - +* +* 37 ASP 37 t ~b - 181.8 - - - - - - - - 182.7 -.7 34.4 - ** +* ** 38 ARG 38 S B - - -55.0 - - - - - - - 179.8 - 35.2 - 39 THR 39 B - - -49.7 - - - - - - - 170.2 - 35.2 - * +* +* 40 PRO 40 - - - - - -68.7 - - - - - 181.0 - 39.2 - +* +* 41 GLU 41 E B - 181.5 - 177.6 - - - - - - 184.5 -.9 33.8 - +* +* 42 ILE 42 E B - - -51.6 178.2 - - - - - - 174.8 - 35.8 - * * 43 VAL 43 E B 62.0 - - - - - - - - - 173.8 -2.0 34.0 - * * 44 SER 44 E B - - -60.3 - - - - - - - 182.2 - 35.0 - 45 ALA 45 E B - - - - - - - - - - 179.4 -2.8 34.3 - * * 46 THR 46 E B - - -59.8 - - - - - - - 175.3 -3.1 35.4 - * * 47 LEU 47 E B - 173.8 - - - - - - - - 178.9 -3.7 34.7 - ** ** 48 PRO 48 E - - - - - -81.9 - - - - - 178.7 - 38.5 - * * * 49 GLY 49 E - - - - - - - - - - - 181.2 -3.0 - - * * 50 PHE 50 E B - - -66.8 - - - - - - - 176.9 -.8 34.1 - +* +* 51 GLN 51 E B - 179.4 - - - - - - - - 179.9 -2.9 32.6 - * * 52 ARG 52 E B 64.1 - - 180.0 - - - - - - 177.5 - 31.6 - 53 PHE 53 E B - - -74.2 - - - - - - - 192.1 -2.0 33.2 - ** ** Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 54 ARG 54 B 45.9 - - - - - - - - - 167.7 -3.7 33.3 - * ** ** ** 55 LEU 55 a - - -67.8 180.0 - - - - - - 171.9 -.6 32.3 - * +* +* 56 LYS 56 S ~b - 179.3 - 173.1 - - - - - - 182.9 -3.0 32.1 - ** * ** 57 GLY 57 S - - - - - - - - - - - 178.7 - - - 58 ARG 58 S A - 191.2 - - - - - - - - 173.7 - 35.3 - * * 59 LEU 59 S B - 190.2 - - - - - - - - 190.3 - 31.4 - +* +* 60 TYR 60 B - - -56.4 - - - - - - - 175.6 - 36.3 - 61 PRO 61 - - - - - -66.1 - - - - - 185.1 - 37.3 - 62 CYS 62 E B 54.6 - - - - - - - - - 180.7 -2.2 33.9 - 63 ILE 63 E B - - -59.0 - - - - - - - 176.5 - 35.3 - 64 VAL 64 E B - - -63.5 - - - - - - - 179.1 -2.8 32.5 - * * 65 PRO 65 E - - - - - -61.0 - - - - - 176.3 - 38.1 - * * 66 SER 66 E B - 183.6 - - - - - - - - 183.6 -2.0 35.6 - 67 GLU 67 E A - - -58.7 183.6 - - - - - - 171.3 - 31.4 - * * 68 LYS 68 E b - - -66.6 184.7 - - - - - - 176.4 - 30.4 - 69 GLY 69 E - - - - - - - - - - - 181.2 -.9 - - * * 70 GLU 70 E B 61.4 - - 185.3 - - - - - - 179.1 - 34.0 - 71 VAL 71 E B - 180.7 - - - - - - - - 175.3 -2.7 35.4 - 72 HIS 72 E B - - -62.5 - - - - - - - 183.9 - 33.2 - 73 GLY 73 E - - - - - - - - - - - 184.1 -2.9 - - * * 74 LYS 74 E B - - -80.2 - - - - - - - 173.4 -1.4 34.2 - * * 75 VAL 75 E B - 168.1 - - - - - - - - 177.1 -3.3 34.2 - +* +* 76 LEU 76 E B - - -54.8 179.9 - - - - - - 179.7 -3.1 36.8 - * * 77 MET 77 E B 55.4 - - 175.0 - - - - - - 180.9 -3.3 32.0 - +* +* 78 GLY 78 E - - - - - - - - - - - 179.3 -2.0 - - 79 VAL 79 E B 65.4 - - - - - - - - - 183.3 -1.8 33.7 - 80 THR 80 h B 60.8 - - - - - - - - - 182.3 - 32.7 - 81 SER 81 H A 50.0 - - - - -61.4 -45.2 - - - 180.9 - 33.0 - 82 ASP 82 H A - 181.1 - - - -63.1 -36.6 - - - 180.4 - 34.2 - 83 GLU 83 H A - - -52.7 175.4 - -78.5 -28.5 - - - 176.2 - 35.2 - * * 84 LEU 84 H A - 177.9 - - - -67.7 -41.6 - - - 176.2 -1.8 33.6 - 85 GLU 85 H A 64.2 - - 187.2 - -74.4 -29.4 - - - 175.1 -2.4 31.6 - 86 ASN 86 H A - 168.3 - - - -56.5 -47.5 - - - 180.7 -1.5 36.0 - 87 LEU 87 H A - - -61.1 177.3 - -60.8 -33.8 - - - 177.4 -2.0 33.7 - 88 ASP 88 H A - 177.4 - - - -73.0 -36.9 - - - 178.4 -.9 34.4 - +* +* 89 ALA 89 H A - - - - - -66.8 -47.3 - - - 182.3 -2.1 34.7 - 90 VAL 90 H A 62.1 - - - - -72.7 -56.5 - - - 182.4 -3.2 31.0 - +* +* +* 91 GLU 91 H A - - -63.6 - - -77.5 -23.0 - - - 183.9 -2.2 33.9 - * * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 92 GLY 92 h - - - - - - - - - - - 178.7 -1.0 - - * * 93 ASN 93 T A - - -72.7 - - - - - - - 180.7 -.8 31.9 - +* +* 94 GLU 94 e A - - -68.0 - - - - - - - 185.6 -1.3 34.1 - 95 TYR 95 E B - - -63.7 - - - - - - - 178.5 -3.1 34.5 - * * 96 GLU 96 E B - 180.9 - 176.4 - - - - - - 184.1 -2.1 34.5 - 97 ARG 97 E B - 197.6 - 202.2 - - - - - - 177.7 - 36.1 - * * 98 VAL 98 E B - - -64.4 - - - - - - - 184.3 -3.3 31.1 - +* +* 99 THR 99 E B - 190.8 - - - - - - - - 185.0 - 32.8 - 100 VAL 100 E B - - -64.8 - - - - - - - 176.1 -3.3 34.8 - +* +* 101 GLY 101 E - - - - - - - - - - - 181.8 - - - 102 ILE 102 E B 57.2 - - - - - - - - - 177.9 -3.3 32.5 - +* +* 103 VAL 103 E B - 180.2 - - - - - - - - 184.4 -1.8 34.5 - 104 ARG 104 E B - - -43.1 197.9 - - - - - - 180.5 -3.4 33.9 - +* * +* +* 105 GLU 105 e A - - -61.9 - - - - - - - 182.9 -3.6 35.1 - ** ** 106 ASP 106 T A 68.0 - - - - - - - - - 177.1 -.6 32.1 - +* +* 107 ASN 107 T a 56.5 - - - - - - - - - 170.1 - 30.3 - +* * +* 108 SER 108 t l - - -57.8 - - - - - - - 173.7 -1.0 32.8 - * * * 109 GLU 109 e B - - -61.8 - - - - - - - 179.2 - 34.3 - 110 LYS 110 E B 61.5 - - 182.1 - - - - - - 183.2 - 33.3 - 111 MET 111 E B - - -58.7 187.8 - - - - - - 178.4 -3.3 33.9 - +* +* 112 ALA 112 E B - - - - - - - - - - 184.8 - 34.1 - 113 VAL 113 E B - - -60.0 - - - - - - - 175.5 -2.4 34.7 - 114 LYS 114 E B - - -66.0 - - - - - - - 178.3 -1.3 34.2 - 115 THR 115 E B - 191.7 - - - - - - - - 180.4 -2.8 33.7 - 116 TYR 116 E B - - -61.7 - - - - - - - 187.1 -.6 31.8 - * +* +* 117 MET 117 E B - 171.3 - - - - - - - - 185.2 -2.3 32.5 - 118 TRP 118 E B - 185.1 - - - - - - - - 187.1 -2.9 33.6 - * * * 119 ILE 119 e A - - -55.4 172.0 - - - - - - 178.6 -.6 33.9 - +* +* 120 ASN 120 b - - -64.5 - - - - - - - 180.8 - 32.1 - 121 LYS 121 S A - - -59.5 177.9 - - - - - - 175.0 -1.4 33.9 - 122 ALA 122 S b - - - - - - - - - - 180.6 - 32.8 - 123 ASP 123 B - 181.8 - - - - - - - - 184.5 -.8 34.4 - +* +* 124 PRO 124 S - - - - - -84.3 - - - - - 185.3 - 40.0 - +* +* +* 125 ASP 125 S A - 183.3 - - - - - - - - 179.7 - 32.8 - 126 MET 126 A 60.7 - - 181.6 - - - - - - 180.8 - 34.6 - 127 PHE 127 B - - -74.0 - - - - - - - 185.2 - 28.3 - +* +* 128 GLY 128 - - - - - - - - - - - 189.1 - - - +* +* Residue-by-residue listing for refined_3 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 129 GLU 129 B B - 187.5 - 185.9 - - - - - - 180.8 - 34.9 - 130 TRP 130 B - 195.0 - - - - - - - - 182.1 -1.8 34.3 - 131 ASN 131 h b - - -70.4 - - - - - - - 184.3 - 31.4 - 132 PHE 132 H A - 193.2 - - - -73.4 -35.3 - - - 183.9 -1.5 36.9 - 133 GLU 133 H A - - -61.4 - - -62.2 -31.7 - - - 176.4 - 31.9 - 134 GLU 134 H A - 178.9 - 179.8 - -66.9 -37.0 - - - 177.6 - 33.2 - 135 TRP 135 H A - 177.6 - - - -73.2 -36.8 - - - 177.2 -.7 32.4 - +* +* 136 LYS 136 H A - 182.7 - 174.4 - -60.2 -31.3 - - - 174.4 -2.7 33.7 - 137 ARG 137 H A - 165.0 - - - -55.7 -51.3 - - - 180.3 -1.5 35.4 - * * * 138 LEU 138 H A - - -62.7 - - -83.8 -16.5 - - - 181.2 -1.0 33.2 - +* ** * ** 139 HIS 139 H A - 183.9 - - - -64.7 -16.0 - - - 177.6 -1.9 33.4 - ** ** 140 LYS 140 H A - 180.0 - 180.7 - -55.6 -35.2 - - - 184.4 -.7 35.0 - +* +* 141 LYS 141 H A - 198.2 - - - -53.2 -36.2 - - - 180.8 -1.6 35.0 - * * 142 LYS 142 H A - 182.4 - 184.3 - -63.5 -42.5 - - - 179.9 -1.2 34.2 - * * 143 PHE 143 H A - - -58.5 - - -73.8 -31.7 - - - 178.7 -.9 34.5 - +* +* 144 ILE 144 H A - - -56.8 - - -59.8 -32.6 - - - 175.5 -2.1 31.5 - 145 GLU 145 H A - - -61.5 - - -61.5 -36.2 - - - 177.9 -1.3 34.2 - 146 THR 146 H A - - -54.9 - - -72.5 -47.8 - - - 179.2 -.6 35.5 - +* +* 147 PHE 147 H A - - -73.0 - - -66.6 -28.8 - - - 178.5 -2.8 29.4 - * * 148 LYS 148 H A - 175.6 - 184.3 - -52.5 -47.7 - - - 181.7 -2.8 36.9 - * * 149 LYS 149 H A - 187.8 - - - -70.8 -39.3 - - - 181.4 -.9 34.4 - * * 150 ILE 150 H A - - -58.2 176.5 - -67.7 -52.3 - - - 185.2 -1.4 34.1 - * * 151 MET 151 H A 62.7 - - 185.6 - -76.4 -40.5 - - - 180.4 -3.8 30.4 - ** * ** 152 GLU 152 H A - - -73.1 - - -62.8 -30.3 - - - 177.9 -2.1 30.5 - 153 CYS 153 H A - - -60.0 - - -71.3 -30.0 - - - 175.5 -.9 31.7 - * * 154 LYS 154 H A - - -58.2 183.2 - -77.5 -39.9 - - - 178.7 -.7 35.4 - * +* +* 155 LYS 155 H A - 178.4 - - - -64.0 -47.9 - - - 175.4 -2.7 34.9 - 156 LYS 156 h B - 181.5 - 177.7 - - - - - - 184.6 -3.3 34.0 - +* +* 157 PRO 157 S - - - - - -53.5 - - - - - 179.9 - 38.2 - * * * 158 GLN 158 S B 63.4 - - 177.9 - - - - - - 178.4 - 33.3 - 159 GLY 159 S - - - - - - - - - - - 175.3 - - - 160 GLN 160 B 62.2 - - 170.7 - - - - - - 172.2 - 33.1 - * * 161 GLY 161 - - - - - - - - - - - 185.6 - - - 162 ASN 162 B - 181.1 - - - - - - - - 176.6 -.8 34.8 - +* +* 163 ASP 163 b 66.4 - - - - - - - - - 177.6 - 31.3 - 164 ASP 164 b - 187.6 - - - - - - - - 187.1 -1.3 34.6 - * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 165 ILE 165 B - 183.4 - - - - - - - - 179.9 - 33.0 - 166 SER 166 B - - -55.0 - - - - - - - 176.2 - 35.0 - 167 HIS 167 B - - -69.7 - - - - - - - 173.5 - 34.5 - * * 168 VAL 168 B - - -67.0 - - - - - - - 183.4 - 31.5 - 169 LEU 169 B - 182.9 - - - - - - - - 179.5 -1.0 33.8 - * * 170 ARG 170 b - 177.8 - 181.4 - - - - - - 180.5 - 34.5 - 171 GLU 171 b 55.2 - - 182.4 - - - - - - 180.0 - 31.0 - 172 ASP 172 B 66.1 - - - - - - - - - 180.5 -.5 35.0 - ** ** 173 GLN 173 - - 189.6 - - - - - - - - - - 33.8 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +* * +* +* ** ** ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.3 182.8 -62.2 179.8 -68.5 -66.6 -37.5 - - - 179.9 -2.0 33.8 Standard deviations: 5.9 7.3 6.8 7.5 11.1 7.9 9.1 - - - 4.0 1.0 1.9 Numbers of values: 31 57 62 41 7 42 42 0 0 0 172 99 161 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_3 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 - 1.237 1.500 - 1.468 - 116.07 121.02 - 111.66 - 122.90 * * 2 HIS 2 1.308 1.235 1.524 1.533 1.439 121.70 116.46 120.70 111.08 108.54 109.29 122.79 +* * +* 3 HIS 3 1.310 1.239 1.509 1.562 1.447 121.29 115.60 120.73 110.49 110.82 112.35 123.64 * +* * +* 4 HIS 4 1.304 1.230 1.516 1.556 1.440 122.76 114.90 122.10 113.17 111.06 113.74 122.84 +* * +* +* +* 5 HIS 5 1.298 1.228 1.509 1.548 1.436 122.36 116.16 120.88 110.30 109.20 112.01 122.89 ** * ** 6 HIS 6 1.290 1.228 1.502 1.542 1.435 121.62 115.55 121.07 110.86 109.61 112.71 123.28 +** * * * +** 7 HIS 7 1.306 1.231 1.510 1.538 1.438 121.91 116.15 120.50 110.84 107.56 110.14 123.28 +* * * +* 8 LEU 8 1.300 1.236 1.511 1.555 1.455 121.78 114.69 121.23 109.65 109.35 111.60 124.07 ** * ** 9 GLU 9 1.316 1.244 1.526 1.549 1.445 124.42 115.01 122.05 110.50 112.35 113.73 122.92 +* +* +* 10 CYS 10 1.291 1.242 1.510 1.537 1.428 122.84 116.88 119.98 111.55 108.24 110.25 123.11 +** +* * +** 11 SER 11 1.306 1.235 1.516 1.525 1.433 121.67 115.04 121.37 111.81 110.23 110.25 123.53 +* * +* Residue-by-residue listing for refined_3 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 SER 12 1.312 1.225 1.516 1.516 1.434 122.85 115.72 120.14 111.01 110.93 108.78 124.14 * * * * 13 ASP 13 1.341 1.230 1.523 1.537 1.461 123.59 114.89 121.88 112.60 111.31 111.52 123.15 * * * 14 SER 14 1.303 1.234 1.525 1.549 1.428 122.75 117.70 119.19 111.37 106.97 108.78 123.10 +* +* +* * +* 15 LEU 15 1.323 1.240 1.511 1.510 1.413 122.75 114.71 121.32 111.70 109.61 109.42 123.90 ** ** 16 GLN 16 1.292 1.249 1.520 1.544 1.437 124.49 117.95 119.76 108.71 105.99 108.89 122.28 +** * +* +* +** 17 LEU 17 1.312 1.239 1.505 1.523 1.436 119.59 116.51 120.84 111.24 108.20 113.44 122.65 * * * * +* +* 18 HIS 18 1.287 1.246 1.487 1.524 1.440 120.68 114.31 121.12 108.35 112.15 110.53 124.56 *** +* *** 19 ASN 19 1.305 1.238 1.521 1.549 1.426 123.33 115.23 121.70 113.73 110.58 113.49 123.01 +* +* +* +* +* 20 VAL 20 1.311 1.226 1.523 1.566 1.454 122.76 116.63 120.20 108.95 110.17 110.26 123.17 * * 21 PHE 21 1.315 1.236 1.516 1.543 1.445 122.29 116.24 120.78 110.38 108.71 109.86 122.97 22 VAL 22 1.296 1.234 1.509 1.559 1.432 121.67 115.78 120.93 110.65 109.90 113.00 123.29 ** * ** 23 TYR 23 1.306 1.234 1.519 1.527 1.457 122.20 116.32 120.70 110.89 112.93 110.47 122.98 +* +* 24 GLY 24 1.308 1.225 1.500 - 1.438 120.08 116.28 120.40 - 112.17 - 123.29 * * 25 SER 25 1.325 1.229 1.525 1.531 1.460 122.51 115.70 121.14 110.56 112.10 109.11 123.13 26 PHE 26 1.309 1.218 1.521 1.528 1.440 122.12 116.49 120.87 110.54 110.89 109.08 122.60 * * 27 GLN 27 1.329 1.234 1.531 1.536 1.471 120.72 115.73 121.06 109.65 110.78 111.35 123.21 28 ASP 28 1.318 1.234 1.519 1.532 1.449 122.52 117.46 120.39 110.33 109.38 110.45 122.15 29 PRO 29 1.339 1.231 1.534 1.522 1.466 122.79 117.30 120.57 110.76 114.08 103.91 122.11 30 ASP 30 1.317 1.236 1.513 1.525 1.457 120.49 115.58 120.79 111.62 110.07 111.77 123.60 31 VAL 31 1.329 1.228 1.522 1.556 1.459 122.49 115.64 121.05 109.08 109.41 111.79 123.27 32 ILE 32 1.320 1.237 1.539 1.535 1.446 122.90 116.40 120.73 111.11 110.90 109.29 122.85 * * 33 ASN 33 1.320 1.228 1.509 1.520 1.476 122.56 116.28 120.93 109.15 112.26 110.80 122.78 34 VAL 34 1.305 1.232 1.527 1.553 1.439 120.95 116.54 120.31 109.82 111.29 111.85 123.12 +* * +* 35 MET 35 1.328 1.225 1.526 1.542 1.451 121.71 117.48 120.30 110.88 110.26 109.27 122.16 36 LEU 36 1.327 1.237 1.508 1.567 1.438 119.18 117.42 119.19 113.03 112.71 115.71 123.33 +* * * +* *** *** 37 ASP 37 1.339 1.239 1.524 1.545 1.479 121.67 116.12 120.85 109.14 111.38 111.00 123.03 * * 38 ARG 38 1.324 1.230 1.503 1.540 1.468 122.24 116.43 120.31 108.25 109.27 111.59 123.26 * * 39 THR 39 1.314 1.231 1.540 1.543 1.438 121.60 117.65 120.22 108.56 111.48 110.70 122.03 * * * 40 PRO 40 1.347 1.241 1.525 1.537 1.465 123.18 116.82 119.77 109.90 109.34 103.71 123.37 41 GLU 41 1.316 1.238 1.534 1.531 1.462 122.21 116.20 121.03 110.81 110.36 110.53 122.76 42 ILE 42 1.310 1.237 1.516 1.557 1.442 121.52 115.96 121.13 107.99 109.59 111.06 122.89 * * 43 VAL 43 1.288 1.226 1.521 1.564 1.439 121.86 117.27 120.12 109.99 108.90 112.07 122.57 +** * +** 44 SER 44 1.298 1.233 1.538 1.527 1.426 120.92 117.02 120.23 111.17 107.43 109.31 122.71 ** +* * ** Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 ALA 45 1.304 1.228 1.514 1.510 1.452 122.22 115.31 121.06 109.85 111.73 110.13 123.63 +* +* 46 THR 46 1.299 1.229 1.521 1.542 1.436 123.31 115.63 120.53 108.62 110.78 110.58 123.84 ** * ** 47 LEU 47 1.305 1.233 1.528 1.536 1.432 123.53 117.59 120.41 110.68 109.34 109.90 121.95 +* * * +* 48 PRO 48 1.334 1.245 1.530 1.530 1.448 122.23 116.03 121.01 110.87 111.61 103.33 122.95 * * 49 GLY 49 1.308 1.231 1.510 - 1.437 121.47 117.13 120.68 - 112.61 - 122.18 * * 50 PHE 50 1.307 1.214 1.496 1.548 1.451 121.31 116.73 119.97 109.85 109.73 111.65 123.29 +* * +* 51 GLN 51 1.305 1.237 1.504 1.538 1.438 121.66 116.04 120.50 111.77 109.75 111.78 123.41 +* * * +* 52 ARG 52 1.318 1.251 1.515 1.554 1.426 120.91 114.89 121.64 111.60 111.29 112.85 123.47 * +* * +* 53 PHE 53 1.292 1.204 1.491 1.529 1.434 123.00 117.51 119.93 112.17 107.57 111.21 122.55 +** * +* * * * +** 54 ARG 54 1.285 1.231 1.494 1.559 1.429 120.40 114.05 121.18 112.00 114.89 108.97 124.73 *** * * +* * * * *** 55 LEU 55 1.300 1.229 1.518 1.550 1.441 125.08 115.57 119.88 111.80 105.87 113.50 124.50 ** +* +* +* ** 56 LYS 56 1.351 1.234 1.519 1.546 1.483 125.76 115.88 120.80 109.26 110.34 114.53 123.32 +* * ** ** ** 57 GLY 57 1.317 1.226 1.499 - 1.440 120.93 116.43 120.40 - 112.45 - 123.17 58 ARG 58 1.329 1.225 1.494 1.561 1.446 121.92 115.50 121.50 112.53 104.32 108.85 122.91 * +* * ** ** 59 LEU 59 1.293 1.239 1.512 1.524 1.401 120.06 116.09 120.37 113.24 108.39 112.55 123.53 +** +** +* * * +** 60 TYR 60 1.286 1.226 1.508 1.543 1.439 122.91 119.82 118.28 110.73 107.80 108.04 121.88 *** +* * * * *** 61 PRO 61 1.362 1.224 1.523 1.533 1.453 121.55 115.22 121.56 111.28 110.88 104.88 123.18 * * +* +* 62 CYS 62 1.285 1.233 1.521 1.522 1.415 122.86 115.70 121.16 112.44 111.20 108.70 123.11 *** ** * * *** 63 ILE 63 1.312 1.231 1.504 1.555 1.445 122.13 116.26 120.61 108.45 109.62 111.40 123.12 * * * 64 VAL 64 1.289 1.239 1.511 1.560 1.438 121.28 117.26 120.45 110.21 109.75 113.66 122.20 +** * * +** 65 PRO 65 1.328 1.242 1.528 1.536 1.458 122.47 114.97 121.41 110.76 112.73 103.87 123.60 * * * 66 SER 66 1.304 1.233 1.504 1.536 1.429 123.65 117.45 119.44 109.85 106.09 110.38 123.11 +* +* * +* +* 67 GLU 67 1.322 1.236 1.522 1.514 1.463 121.24 116.19 120.62 112.55 112.09 111.35 123.19 * * 68 LYS 68 1.324 1.231 1.519 1.535 1.439 122.24 115.13 121.64 111.96 111.04 113.96 123.01 ** ** 69 GLY 69 1.306 1.233 1.497 - 1.436 122.01 117.71 119.29 - 109.29 - 123.00 +* * * +* 70 GLU 70 1.303 1.231 1.530 1.537 1.444 121.40 116.39 120.82 111.16 110.52 109.94 122.78 +* +* 71 VAL 71 1.313 1.209 1.499 1.562 1.452 122.00 117.09 120.59 107.71 109.00 112.26 122.30 * * * * 72 HIS 72 1.292 1.231 1.490 1.542 1.438 120.06 115.47 120.66 111.43 107.21 112.34 123.85 +** +* * * * +** Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 GLY 73 1.283 1.227 1.484 - 1.417 121.42 116.77 120.27 - 110.89 - 122.96 *** +* ** *** 74 LYS 74 1.300 1.222 1.498 1.540 1.451 121.67 114.58 121.28 108.66 112.53 111.64 124.14 ** * ** 75 VAL 75 1.290 1.235 1.518 1.548 1.433 123.73 114.91 120.93 109.19 110.51 111.94 124.16 +** * * +** 76 LEU 76 1.309 1.229 1.513 1.535 1.439 123.45 117.34 119.91 107.70 107.58 110.10 122.71 * * * * 77 MET 77 1.296 1.225 1.496 1.528 1.450 120.80 115.33 121.24 110.75 111.77 112.71 123.42 ** * * ** 78 GLY 78 1.301 1.233 1.506 - 1.433 120.78 115.85 121.16 - 111.19 - 122.99 ** * ** 79 VAL 79 1.318 1.246 1.542 1.573 1.446 121.58 117.71 119.98 111.69 108.58 110.91 122.29 * * * 80 THR 80 1.323 1.230 1.532 1.545 1.455 120.44 116.49 120.62 110.34 111.58 112.22 122.89 81 SER 81 1.317 1.233 1.551 1.522 1.454 123.03 117.34 120.12 112.10 113.74 109.01 122.51 * * * 82 ASP 82 1.337 1.221 1.516 1.537 1.485 121.67 115.24 121.70 109.33 110.83 111.30 123.05 * * 83 GLU 83 1.288 1.220 1.543 1.503 1.444 122.79 115.83 121.49 111.80 109.47 107.47 122.67 +** * +* +** 84 LEU 84 1.318 1.243 1.536 1.565 1.459 122.96 116.26 120.93 113.32 109.65 108.90 122.82 +* +* +* 85 GLU 85 1.324 1.224 1.540 1.543 1.452 121.15 115.69 120.93 113.12 109.80 111.63 123.35 +* +* 86 ASN 86 1.341 1.217 1.509 1.534 1.477 123.77 115.37 121.15 108.87 110.29 109.26 123.47 * * * 87 LEU 87 1.314 1.229 1.527 1.527 1.451 122.74 115.99 121.01 110.91 111.03 110.29 122.99 * * 88 ASP 88 1.320 1.217 1.508 1.523 1.460 121.73 115.74 121.31 109.95 109.59 110.79 122.94 89 ALA 89 1.302 1.233 1.530 1.519 1.439 122.27 116.29 120.84 110.47 110.62 109.52 122.87 +* * +* 90 VAL 90 1.321 1.230 1.565 1.583 1.455 121.94 117.82 120.14 112.58 113.06 111.94 121.96 +* +* +* +* 91 GLU 91 1.331 1.232 1.526 1.538 1.479 121.87 115.71 121.00 109.85 111.59 110.85 123.27 * * 92 GLY 92 1.324 1.222 1.515 - 1.460 122.98 117.54 120.20 - 115.11 - 122.25 * * 93 ASN 93 1.317 1.231 1.523 1.542 1.461 120.33 116.73 120.62 110.95 111.20 112.89 122.62 * * 94 GLU 94 1.316 1.237 1.540 1.549 1.461 121.42 116.10 121.00 109.31 111.77 111.22 122.89 95 TYR 95 1.319 1.221 1.511 1.522 1.462 123.39 116.22 120.77 109.07 111.72 110.82 123.00 96 GLU 96 1.313 1.239 1.528 1.536 1.448 122.10 116.95 120.09 111.20 108.83 109.71 122.96 * * 97 ARG 97 1.330 1.231 1.515 1.541 1.454 121.14 116.87 120.54 106.88 108.85 111.61 122.59 +* +* 98 VAL 98 1.295 1.238 1.489 1.530 1.443 121.54 115.34 120.97 110.33 111.59 114.51 123.69 ** +* +* ** 99 THR 99 1.286 1.232 1.539 1.575 1.444 121.15 117.05 120.69 112.66 108.88 111.12 122.21 *** * +* *** 100 VAL 100 1.321 1.236 1.526 1.556 1.460 121.75 115.77 121.07 108.22 112.05 111.49 123.16 101 GLY 101 1.304 1.232 1.509 - 1.435 121.63 117.12 119.85 - 109.80 - 123.03 +* * +* 102 ILE 102 1.315 1.227 1.521 1.590 1.452 122.25 116.56 120.55 111.16 111.07 112.46 122.88 +* +* Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 103 VAL 103 1.306 1.220 1.514 1.561 1.452 122.53 117.57 119.67 109.83 107.41 111.83 122.75 +* * +* 104 ARG 104 1.317 1.237 1.532 1.534 1.453 120.80 116.04 120.95 108.93 110.62 112.20 123.00 * * 105 GLU 105 1.308 1.222 1.516 1.530 1.455 122.72 116.62 120.49 109.05 111.33 110.17 122.89 +* +* 106 ASP 106 1.309 1.232 1.527 1.545 1.454 121.22 117.10 120.39 111.88 111.27 111.71 122.51 * * 107 ASN 107 1.321 1.228 1.526 1.554 1.473 120.86 115.78 120.90 112.19 112.74 113.15 123.31 * * +* +* 108 SER 108 1.331 1.234 1.549 1.536 1.475 123.45 118.37 119.85 111.20 115.88 109.36 121.75 * * +* +* 109 GLU 109 1.324 1.233 1.513 1.520 1.466 119.49 116.85 120.31 108.55 108.97 112.34 122.83 * * * 110 LYS 110 1.294 1.239 1.522 1.531 1.449 121.01 115.98 120.99 110.85 109.69 111.46 123.03 +** +** 111 MET 111 1.296 1.226 1.473 1.512 1.454 122.80 113.92 121.81 106.71 111.39 114.21 124.28 ** ** * +* ** ** 112 ALA 112 1.267 1.237 1.506 1.513 1.433 122.79 116.63 120.46 110.65 107.99 111.01 122.91 **** * * **** 113 VAL 113 1.305 1.233 1.519 1.563 1.445 121.36 115.67 121.38 108.15 110.88 112.13 122.95 +* +* 114 LYS 114 1.298 1.229 1.509 1.554 1.439 121.90 117.25 120.03 109.73 107.97 112.29 122.71 ** * * * * ** 115 THR 115 1.291 1.242 1.516 1.562 1.433 121.08 116.52 120.32 110.29 108.42 112.38 123.15 +** * +** 116 TYR 116 1.298 1.231 1.499 1.525 1.424 121.85 114.37 121.67 113.93 109.75 110.79 123.96 ** * +* ** ** 117 MET 117 1.295 1.246 1.512 1.559 1.434 123.16 115.27 120.82 115.14 110.85 108.41 123.87 ** * * +** * +** 118 TRP 118 1.321 1.227 1.503 1.521 1.434 123.14 113.80 121.61 112.33 110.32 109.45 124.58 * * * * * 119 ILE 119 1.305 1.237 1.532 1.537 1.443 124.54 117.27 120.45 111.37 112.97 109.07 122.27 +* +* * * +* 120 ASN 120 1.312 1.219 1.497 1.535 1.447 119.89 115.63 121.10 110.51 110.41 113.41 123.25 * * * +* +* 121 LYS 121 1.313 1.232 1.516 1.520 1.451 122.16 115.57 121.03 111.05 110.43 110.10 123.40 * * 122 ALA 122 1.312 1.246 1.520 1.525 1.425 121.84 115.29 121.56 111.62 108.89 111.76 123.03 * +* +* 123 ASP 123 1.300 1.231 1.511 1.533 1.445 122.44 117.53 120.43 110.20 108.75 110.94 122.04 ** ** 124 PRO 124 1.327 1.237 1.532 1.521 1.460 122.83 117.63 120.20 109.63 113.99 101.88 122.17 * * 125 ASP 125 1.314 1.231 1.519 1.524 1.450 119.98 116.80 120.84 111.42 112.31 110.71 122.32 * * 126 MET 126 1.317 1.222 1.533 1.521 1.467 121.36 117.42 120.16 108.94 112.09 110.50 122.42 127 PHE 127 1.334 1.241 1.517 1.529 1.455 120.78 113.09 122.57 113.48 113.44 113.86 124.34 +* * +* +* +* 128 GLY 128 1.285 1.220 1.480 - 1.411 124.35 116.29 120.60 - 106.06 - 123.09 *** ** ** ** ** *** 129 GLU 129 1.283 1.233 1.503 1.526 1.427 121.54 116.64 120.25 110.58 109.00 109.79 123.10 *** * +* *** 130 TRP 130 1.314 1.235 1.520 1.537 1.436 120.75 116.87 119.47 111.27 108.22 110.30 123.62 * * * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 131 ASN 131 1.328 1.244 1.512 1.523 1.469 122.87 113.87 122.05 111.52 112.42 112.26 124.03 * * * 132 PHE 132 1.305 1.234 1.523 1.506 1.384 125.38 116.98 120.14 110.18 112.50 106.47 122.88 +* * +*** ** ** +*** 133 GLU 133 1.328 1.235 1.524 1.531 1.460 121.06 116.61 120.42 111.55 111.67 111.97 122.96 134 GLU 134 1.326 1.219 1.532 1.528 1.452 121.68 117.15 120.86 110.39 110.82 111.55 121.98 135 TRP 135 1.315 1.223 1.514 1.536 1.450 119.93 115.24 121.23 111.90 109.32 111.93 123.48 136 LYS 136 1.316 1.227 1.546 1.532 1.451 123.42 115.42 121.17 112.61 109.84 109.04 123.40 * * 137 ARG 137 1.325 1.232 1.542 1.536 1.465 124.06 116.93 120.75 110.44 111.33 108.23 122.32 * * * 138 LEU 138 1.322 1.228 1.517 1.550 1.464 120.99 115.35 121.42 109.92 110.66 112.41 123.21 * * 139 HIS 139 1.313 1.240 1.539 1.540 1.468 123.17 116.73 120.23 110.87 112.09 110.42 123.03 * * 140 LYS 140 1.340 1.229 1.520 1.545 1.471 122.32 114.93 120.78 108.66 110.08 111.11 124.21 141 LYS 141 1.331 1.227 1.551 1.556 1.459 124.87 116.72 120.42 112.06 110.52 107.64 122.79 * * +* * +* +* 142 LYS 142 1.339 1.232 1.539 1.540 1.469 121.85 115.95 121.13 109.66 110.62 110.98 122.91 143 PHE 143 1.325 1.234 1.504 1.525 1.460 121.94 115.30 121.30 109.28 109.57 111.33 123.39 * * 144 ILE 144 1.319 1.193 1.526 1.560 1.440 122.31 117.59 120.02 111.74 110.57 113.10 122.39 +* * +* 145 GLU 145 1.328 1.242 1.534 1.516 1.472 121.32 115.96 121.20 109.34 111.00 110.95 122.85 146 THR 146 1.318 1.238 1.532 1.543 1.435 121.84 115.49 121.43 109.82 108.91 109.69 123.00 * * * 147 PHE 147 1.325 1.200 1.496 1.524 1.450 122.12 116.57 119.84 112.59 113.50 113.42 123.58 +* * * +* +* 148 LYS 148 1.308 1.224 1.519 1.535 1.457 123.94 115.61 120.87 108.46 109.91 108.61 123.45 +* * * +* 149 LYS 149 1.316 1.213 1.534 1.555 1.440 121.99 116.18 120.88 112.72 108.86 108.56 122.90 * * * * 150 ILE 150 1.309 1.236 1.552 1.566 1.456 122.16 116.61 120.91 110.17 111.92 110.54 122.46 * * * 151 MET 151 1.320 1.226 1.524 1.542 1.458 121.80 118.19 119.35 112.13 113.91 112.53 122.45 * * * 152 GLU 152 1.339 1.210 1.508 1.524 1.469 120.45 116.72 120.37 111.37 112.95 113.39 122.91 * +* +* 153 CYS 153 1.303 1.222 1.535 1.504 1.448 121.75 116.73 120.91 112.81 112.14 110.57 122.33 +* * * +* 154 LYS 154 1.319 1.232 1.527 1.515 1.459 121.39 113.97 122.00 109.49 108.79 109.72 124.03 * * 155 LYS 155 1.318 1.236 1.546 1.556 1.455 125.49 116.26 120.88 114.32 110.07 105.70 122.85 * * ** ** +** +** 156 LYS 156 1.310 1.235 1.528 1.544 1.445 123.27 117.02 120.30 110.72 107.86 111.25 122.64 * * * 157 PRO 157 1.351 1.238 1.523 1.528 1.483 123.70 116.57 120.73 110.47 113.99 103.49 122.70 * * 158 GLN 158 1.314 1.239 1.528 1.536 1.438 120.76 116.48 120.98 110.82 110.34 111.45 122.54 * * * 159 GLY 159 1.305 1.243 1.511 - 1.437 120.25 116.83 120.27 - 113.67 - 122.88 +* +* 160 GLN 160 1.323 1.239 1.514 1.545 1.446 120.96 115.52 121.22 108.87 111.47 113.28 123.26 +* +* Residue-by-residue listing for refined_3 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 1.300 1.235 1.501 - 1.432 121.27 114.75 121.13 - 107.78 - 124.09 ** * +* ** 162 ASN 162 1.325 1.235 1.511 1.533 1.457 123.71 116.21 120.77 109.04 111.98 110.42 123.02 * * 163 ASP 163 1.311 1.235 1.520 1.560 1.434 120.62 114.51 122.33 112.39 109.58 113.24 122.93 * * * * +* +* 164 ASP 164 1.294 1.235 1.507 1.542 1.439 122.96 116.38 120.61 110.76 106.20 110.95 122.94 +** * +* +** 165 ILE 165 1.298 1.243 1.532 1.567 1.442 121.21 115.98 121.09 111.22 111.58 111.22 122.92 ** * ** 166 SER 166 1.311 1.231 1.535 1.532 1.434 122.07 116.57 121.06 109.92 110.46 109.74 122.30 * * * 167 HIS 167 1.312 1.230 1.492 1.530 1.455 121.29 115.88 120.74 107.83 110.41 112.58 123.38 * +* * * +* 168 VAL 168 1.296 1.242 1.529 1.569 1.428 121.56 115.28 122.00 112.79 108.67 113.07 122.55 ** * +* +* ** 169 LEU 169 1.305 1.239 1.514 1.542 1.436 121.32 115.22 121.23 111.08 110.61 110.53 123.54 +* * +* 170 ARG 170 1.302 1.235 1.521 1.534 1.431 123.34 116.28 121.12 110.58 108.81 110.40 122.56 +* * +* 171 GLU 171 1.299 1.236 1.520 1.535 1.433 121.32 114.53 122.21 113.32 111.27 111.71 123.16 ** * +* ** 172 ASP 172 1.301 1.240 1.503 1.541 1.436 122.52 116.79 120.26 109.93 108.17 110.73 122.94 ** * * * ** 173 GLN 173 1.296 - 1.517 1.538 1.430 120.98 - - 111.52 108.95 110.53 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** +* +*** ** +* * +** ** *** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 1.267 1.351 1.311 .014 **** +* * C-N (Pro) 1.341 .016 7 1.327 1.362 1.341 .012 * C-O C-O 1.231 .020 172 1.193 1.251 1.232 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 161 1.473 1.565 1.520 .014 ** +* CH2G*-C (Gly) 1.516 .018 12 1.480 1.515 1.501 .010 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.510 1.525 1.517 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.530 1.590 1.558 .014 +* CH1E-CH2E (the rest) 1.530 .020 128 1.503 1.567 1.535 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.384 1.485 1.447 .015 +*** * NH1-CH2G* (Gly) 1.451 .016 12 1.411 1.468 1.437 .015 ** * N-CH1E (Pro) 1.466 .015 7 1.448 1.483 1.462 .010 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 2.0 153 113.09 119.82 116.14 1.02 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.75 117.71 116.56 .78 CH1E-C-N (Pro) 116.9 1.5 7 114.97 117.63 116.36 .93 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.75 124.73 123.05 .57 * O-C-N (Pro) 122.0 1.4 7 122.11 123.60 122.87 .53 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.18 125.76 122.06 1.20 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 120.08 124.35 121.56 1.17 ** C-N-CH1E (Pro) 122.6 5.0 7 121.55 123.70 122.68 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.28 122.57 120.77 .65 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.29 121.16 120.44 .52 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.85 111.62 110.65 .64 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.71 112.79 110.09 1.42 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 106.71 115.14 110.82 1.51 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.32 115.88 110.27 1.80 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 106.06 115.11 111.06 2.41 ** N-CH1E-C (Pro) 111.8 2.5 7 109.34 114.08 112.38 1.70 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.52 111.76 110.60 .85 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.07 114.51 111.64 1.22 * +* N-CH1E-CH2E (Pro) 103.0 1.1 7 101.88 104.88 103.58 .83 * +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 105.70 115.71 110.93 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_3 Page 16 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 130 85.0% Residues in additional allowed regions [a,b,l,p] 20 13.1% 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 85.0 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 -.8 Inside e. H-bond energy st dev 99 1.0 .8 .2 .9 Inside f. Overall G-factor 173 -.1 -.4 .3 1.1 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 5.9 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 57 7.3 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 62 6.8 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 150 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 41 7.5 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 85.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .99 3 Residue-by-residue listing for refined_3 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.50 Chi1-chi2 distribution -.28 Chi1 only -.14 Chi3 & chi4 .27 Omega -.11 ------ -.22 ===== Main-chain covalent forces:- Main-chain bond lengths .01 Main-chain bond angles .38 ------ .23 ===== OVERALL AVERAGE -.06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.