Residue-by-residue listing for refined_8 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 180.7 - - - 2 HIS 2 B - - -65.5 - - - - - - - 171.3 - 34.8 - +* +* 3 HIS 3 b - 191.1 - - - - - - - - 193.4 -.5 33.8 - ** ** ** 4 HIS 4 B - 182.2 - - - - - - - - 173.4 -1.1 34.9 - * * * 5 HIS 5 b 58.8 - - - - - - - - - 178.5 -.7 30.2 - +* * +* 6 HIS 6 b - - -70.8 - - - - - - - 177.2 - 32.9 - 7 HIS 7 B - - -67.9 - - - - - - - 174.1 - 33.5 - * * 8 LEU 8 A - - -62.7 178.1 - - - - - - 183.9 - 34.9 - 9 GLU 9 B - 184.8 - 176.0 - - - - - - 182.2 - 35.3 - 10 CYS 10 b - - -55.9 - - - - - - - 178.1 -.6 33.5 - +* +* 11 SER 11 B - 182.5 - - - - - - - - 177.4 -1.3 35.3 - 12 SER 12 A - - -56.5 - - - - - - - 181.5 - 34.8 - 13 ASP 13 l - 185.5 - - - - - - - - 180.5 - 30.0 - * * 14 SER 14 a - - -57.3 - - - - - - - 182.6 - 36.0 - 15 LEU 15 b - - -64.9 - - - - - - - 171.3 - 31.9 - * * 16 GLN 16 B 59.3 - - 174.7 - - - - - - 182.0 -1.7 34.2 - 17 LEU 17 B - - -56.4 - - - - - - - 184.2 - 31.9 - 18 HIS 18 E B - - -59.4 - - - - - - - 175.0 -2.3 35.9 - 19 ASN 19 E B 48.5 - - - - - - - - - 184.4 - 30.1 - * * Residue-by-residue listing for refined_8 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 - 180.8 - - - - - - - - 177.6 -1.9 35.6 - 21 PHE 21 E B - 179.7 - - - - - - - - 182.9 -3.0 35.1 - * * 22 VAL 22 E B - - -67.7 - - - - - - - 189.6 -2.8 31.7 - +* * +* 23 TYR 23 a 56.8 - - - - - - - - - 184.2 - 35.7 - 24 GLY 24 t - - - - - - - - - - - 186.1 - - - * * 25 SER 25 T A - - -56.2 - - - - - - - 185.4 - 34.7 - 26 PHE 26 T a - - -60.1 - - - - - - - 179.3 - 33.2 - 27 GLN 27 t A - 186.6 - 178.4 - - - - - - 179.9 -1.5 33.1 - 28 ASP 28 h B - 181.7 - - - - - - - - 181.9 - 34.6 - 29 PRO 29 H - - - - - -67.4 -67.4 -31.0 - - - 184.0 - 38.9 - * * 30 ASP 30 H A - 176.6 - - - -62.8 -38.2 - - - 178.2 - 32.7 - 31 VAL 31 H A - - -58.6 - - -73.3 -28.3 - - - 181.2 - 31.6 - 32 ILE 32 H A - - -60.4 - - -61.5 -38.7 - - - 176.7 -.9 34.3 - +* +* 33 ASN 33 H A - - -68.3 - - -59.5 -35.2 - - - 182.2 -1.4 35.2 - 34 VAL 34 H A - 180.0 - - - -82.0 -51.2 - - - 185.9 -.7 33.8 - * * * +* +* 35 MET 35 H A - 197.1 - - - -63.6 -36.7 - - - 179.2 -3.4 33.6 - +* +* 36 LEU 36 h a 52.2 - - - - - - - - - 183.2 -2.3 25.4 - ** ** 37 ASP 37 t ~b - 191.0 - - - - - - - - 183.6 -1.3 35.4 - ** ** 38 ARG 38 S B - - -64.4 - - - - - - - 182.6 - 33.9 - 39 THR 39 B - - -48.8 - - - - - - - 173.9 - 34.7 - * * * 40 PRO 40 - - - - - -61.6 - - - - - 176.8 - 39.2 - +* +* 41 GLU 41 E B - 180.2 - - - - - - - - 185.3 -.9 34.6 - * * 42 ILE 42 E B - - -53.9 177.7 - - - - - - 175.4 - 35.7 - 43 VAL 43 E B 61.2 - - - - - - - - - 176.9 -2.3 33.6 - 44 SER 44 E B - - -58.8 - - - - - - - 181.8 - 35.0 - 45 ALA 45 E B - - - - - - - - - - 179.9 -2.1 34.6 - 46 THR 46 E B - - -60.7 - - - - - - - 177.1 -2.7 34.8 - 47 LEU 47 E B - 177.0 - - - - - - - - 179.6 -3.4 34.0 - +* +* 48 PRO 48 E - - - - - -88.1 - - - - - 181.5 - 38.9 - ** * ** 49 GLY 49 E - - - - - - - - - - - 180.5 -3.0 - - * * 50 PHE 50 E B - - -69.7 - - - - - - - 180.9 -.7 33.4 - +* +* 51 GLN 51 E B - 185.4 - - - - - - - - 179.6 -3.0 34.4 - * * 52 ARG 52 E B - 176.3 - 182.6 - - - - - - 182.8 - 35.6 - 53 PHE 53 e B - - -71.5 - - - - - - - 184.8 -2.8 30.1 - * * * 54 ARG 54 B - 177.9 - - - - - - - - 173.8 -.5 37.8 - * +* * +* 55 LEU 55 b 45.1 - - - - - - - - - 187.6 - 28.8 - * * * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 LYS 56 t B - 193.1 - - - - - - - - 175.2 -1.1 35.5 - * * 57 GLY 57 T - - - - - - - - - - - 187.3 -.9 - - * +* +* 58 ARG 58 T A 73.9 - - - - - - - - - 187.2 -1.5 35.2 - * * 59 LEU 59 t B - 188.0 - - - - - - - - 184.0 -1.1 32.1 - * * 60 TYR 60 B - - -49.4 - - - - - - - 172.5 - 38.0 - * * * * 61 PRO 61 - - - - - -75.3 - - - - - 186.7 - 38.5 - * * * 62 CYS 62 e B 56.1 - - - - - - - - - 180.7 -1.2 34.2 - * * 63 ILE 63 E B - - -59.9 - - - - - - - 172.2 - 36.9 - * * 64 VAL 64 E B - - -61.9 - - - - - - - 179.1 -2.1 33.7 - 65 PRO 65 E - - - - - -65.0 - - - - - 177.3 - 37.7 - * * 66 SER 66 E B - 180.2 - - - - - - - - 185.2 -.5 34.6 - ** ** 67 GLU 67 E A - - -56.2 183.8 - - - - - - 180.9 - 34.7 - 68 LYS 68 E A - - -67.0 - - - - - - - 181.8 - 32.9 - 69 GLY 69 E - - - - - - - - - - - 178.7 -1.8 - - 70 GLU 70 E B 62.9 - - - - - - - - - 180.8 - 32.9 - 71 VAL 71 E B - 183.2 - - - - - - - - 173.8 -2.6 35.6 - * * 72 HIS 72 E B - - -62.7 - - - - - - - 184.1 -.5 33.9 - ** ** 73 GLY 73 E - - - - - - - - - - - 184.4 -3.3 - - +* +* 74 LYS 74 E B - - -52.2 - - - - - - - 175.7 -.9 35.3 - * * 75 VAL 75 E B - 170.4 - - - - - - - - 177.6 -3.4 35.0 - +* +* 76 LEU 76 E B - - -56.8 183.4 - - - - - - 177.3 -3.2 35.7 - +* +* 77 MET 77 E B - - -53.6 182.0 - - - - - - 179.3 -3.8 37.1 - ** ** 78 GLY 78 E - - - - - - - - - - - 178.3 - - - 79 VAL 79 E B 67.2 - - - - - - - - - 183.6 -1.8 33.3 - 80 THR 80 h B 60.2 - - - - - - - - - 179.4 - 32.5 - 81 SER 81 H A - - -57.9 - - -62.9 -33.5 - - - 178.6 - 33.5 - 82 ASP 82 H A - 175.9 - - - -64.7 -39.2 - - - 178.5 - 34.5 - 83 GLU 83 H A - - -57.6 172.3 - -78.3 -28.4 - - - 175.9 - 35.4 - * * 84 LEU 84 H A - 179.1 - - - -66.2 -50.2 - - - 178.3 -1.9 33.7 - 85 GLU 85 H A 63.9 - - 177.3 - -62.0 -28.9 - - - 176.1 -3.0 32.3 - * * 86 ASN 86 H A - 166.6 - - - -65.4 -49.2 - - - 177.9 -1.0 35.2 - * * * 87 LEU 87 H A - - -60.9 177.4 - -65.0 -38.9 - - - 179.1 -2.5 34.6 - 88 ASP 88 H A - 186.0 - - - -65.2 -31.6 - - - 174.5 -3.0 35.3 - * * 89 ALA 89 H A - - - - - -77.2 -48.4 - - - 186.6 -1.3 34.5 - * * Residue-by-residue listing for refined_8 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 90 VAL 90 H A 57.6 - - - - -72.3 -59.1 - - - 175.6 -3.2 30.3 - +* +* * +* 91 GLU 91 h A - - -65.0 187.8 - - - - - - 183.5 -2.0 30.5 - 92 GLY 92 T - - - - - - - - - - - 176.8 -1.6 - - 93 ASN 93 T A - - -66.0 - - - - - - - 182.3 -.5 31.8 - ** ** 94 GLU 94 T A - - -54.5 177.3 - - - - - - 186.6 -2.3 36.0 - * * 95 TYR 95 t B - - -61.4 - - - - - - - 177.7 -1.6 35.2 - 96 GLU 96 E B - 181.1 - 178.9 - - - - - - 183.2 -1.8 34.4 - 97 ARG 97 E B - 191.3 - 191.9 - - - - - - 178.3 - 36.5 - 98 VAL 98 E B - - -67.9 - - - - - - - 180.6 -2.8 30.9 - * * 99 THR 99 E B - 180.2 - - - - - - - - 183.9 - 33.1 - 100 VAL 100 E B - - -62.3 - - - - - - - 178.4 -3.0 34.0 - * * 101 GLY 101 E - - - - - - - - - - - 180.4 - - - 102 ILE 102 E B 55.5 - - - - - - - - - 181.1 -2.8 32.2 - * * 103 VAL 103 E B - 180.3 - - - - - - - - 182.9 -3.0 32.9 - * * 104 ARG 104 E B - 177.5 - 179.0 - - - - - - 181.8 -3.1 35.3 - * * 105 GLU 105 e A - - -63.8 - - - - - - - 183.4 -2.7 35.1 - 106 ASP 106 T A - - -60.3 - - - - - - - 192.6 -.6 36.0 - ** +* ** 107 ASN 107 T a - 167.1 - - - - - - - - 174.5 - 32.5 - 108 SER 108 t l - 185.9 - - - - - - - - 179.6 -1.9 33.0 - 109 GLU 109 e B 61.3 - - 184.2 - - - - - - 180.4 - 34.9 - 110 LYS 110 E B 62.0 - - 181.0 - - - - - - 178.2 - 33.7 - 111 MET 111 E B - - -61.9 189.7 - - - - - - 180.6 -3.3 32.8 - +* +* 112 ALA 112 E B - - - - - - - - - - 183.0 - 33.8 - 113 VAL 113 E B - - -59.1 - - - - - - - 175.9 -2.8 34.4 - * * 114 LYS 114 E B - - -57.2 - - - - - - - 175.2 -2.1 36.3 - 115 THR 115 E B - 192.3 - - - - - - - - 181.7 -2.0 33.1 - 116 TYR 116 E B - - -57.5 - - - - - - - 179.8 -.5 34.4 - ** ** 117 MET 117 E B 64.0 - - 175.5 - - - - - - 180.6 -2.0 32.1 - 118 TRP 118 B - 187.3 - - - - - - - - 187.2 -3.4 34.2 - * +* +* 119 ILE 119 S A - - -50.0 174.4 - - - - - - 177.1 - 34.1 - * * 120 ASN 120 t b - 181.4 - - - - - - - - 184.9 - 32.0 - 121 LYS 121 T A 51.2 - - 184.9 - - - - - - 176.1 -1.9 31.5 - 122 ALA 122 T A - - - - - - - - - - 179.3 - 34.2 - 123 ASP 123 t B - 180.6 - - - - - - - - 178.1 -1.6 35.2 - 124 PRO 124 S - - - - - -99.6 - - - - - 186.3 - 40.3 - *** * +* *** 125 ASP 125 S A - - -67.8 - - - - - - - 175.4 - 32.0 - 126 MET 126 S A 65.2 - - - - - - - - - 178.8 - 31.8 - 127 PHE 127 b - - -64.0 - - - - - - - 177.4 - 31.7 - 128 GLY 128 - - - - - - - - - - - 184.9 -1.4 - - 129 GLU 129 B - - -49.6 - - - - - - - 179.4 - 35.6 - * * Residue-by-residue listing for refined_8 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 130 TRP 130 t B - 204.0 - - - - - - - - 180.8 -.5 32.5 - * ** ** 131 ASN 131 h a - - -61.7 - - - - - - - 174.5 - 33.8 - 132 PHE 132 H A - - -63.9 - - -67.8 -34.3 - - - 179.1 - 34.0 - 133 GLU 133 H A - - -58.3 178.9 - -71.6 -28.7 - - - 174.7 -2.4 34.3 - 134 GLU 134 H A - 173.0 - 176.5 - -62.7 -40.7 - - - 176.1 - 34.0 - 135 TRP 135 H A - 178.3 - - - -71.4 -43.4 - - - 175.8 -1.5 32.5 - 136 LYS 136 H A - - -68.0 - - -55.2 -31.0 - - - 176.2 -2.6 32.7 - 137 ARG 137 H A - 172.4 - 172.6 - -59.1 -48.7 - - - 180.4 -1.7 34.2 - 138 LEU 138 H A - - -68.1 - - -80.5 -21.9 - - - 178.1 -1.0 33.2 - * +* * +* 139 HIS 139 h A - 182.3 - - - - - - - - 188.9 -2.1 34.8 - +* +* 140 LYS 140 H A - 184.0 - 179.0 - -48.7 -41.0 - - - 181.6 -.5 33.0 - * +* +* 141 LYS 141 H A - - -70.7 182.3 - -55.8 -35.1 - - - 179.8 - 32.4 - 142 LYS 142 H A - 184.6 - - - -66.8 -36.6 - - - 184.9 -1.9 36.5 - 143 PHE 143 H A - 194.9 - - - -77.0 -36.0 - - - 182.6 -.9 36.0 - * * 144 ILE 144 H A - - -58.5 - - -61.4 -32.7 - - - 185.0 -2.6 32.3 - 145 GLU 145 H A - - -58.8 189.6 - -51.6 -42.4 - - - 180.6 -1.0 32.7 - * * * 146 THR 146 H A - 190.8 - - - -70.7 -33.6 - - - 176.4 -.8 31.9 - +* +* 147 PHE 147 H A - - -74.4 - - -71.8 -30.3 - - - 174.1 -.8 30.6 - * +* +* 148 LYS 148 H A - - -60.7 180.0 - -59.8 -36.8 - - - 176.1 -2.5 33.6 - 149 LYS 149 H A - - -87.6 - - -74.6 -36.7 - - - 176.4 -1.3 30.7 - * * 150 ILE 150 H A - - -62.8 173.7 - -63.3 -41.4 - - - 176.7 -1.9 32.5 - 151 MET 151 H A - - -61.3 176.2 - -66.6 -40.7 - - - 178.9 -3.1 35.0 - * * 152 GLU 152 H A - 198.8 - - - -62.2 -34.3 - - - 176.3 -1.9 35.9 - 153 CYS 153 H A - - -61.4 - - -71.2 -34.0 - - - 179.6 -2.0 34.0 - 154 LYS 154 H A - - -57.1 - - -73.3 -45.2 - - - 179.3 -1.5 35.1 - 155 LYS 155 h ~a - 188.8 - 175.7 - - - - - - 178.7 -3.2 33.7 - ** +* ** 156 LYS 156 b - - -78.4 180.1 - - - - - - 171.1 - 34.2 - +* +* 157 PRO 157 - - - - - -99.8 - - - - - 172.1 - 41.1 - *** * ** *** 158 GLN 158 S B - - -64.0 - - - - - - - 184.8 - 32.7 - 159 GLY 159 S - - - - - - - - - - - 176.6 -1.1 - - * * 160 GLN 160 b - 184.8 - 181.5 - - - - - - 177.4 - 33.5 - 161 GLY 161 - - - - - - - - - - - 184.4 - - - 162 ASN 162 B - - -62.5 - - - - - - - 178.8 - 31.8 - 163 ASP 163 B - 177.4 - - - - - - - - 181.3 -.5 35.2 - ** ** 164 ASP 164 S A - - -67.3 - - - - - - - 181.1 - 33.1 - 165 ILE 165 S B - 178.5 - 179.9 - - - - - - 182.8 - 33.0 - 166 SER 166 b 54.0 - - - - - - - - - 178.1 - 34.5 - 167 HIS 167 A 64.7 - - - - - - - - - 174.6 - 32.2 - 168 VAL 168 B - - -67.7 - - - - - - - 181.4 - 32.6 - 169 LEU 169 B - - -63.9 174.4 - - - - - - 177.4 - 35.2 - 170 ARG 170 B - - -63.2 173.8 - - - - - - 179.9 - 35.3 - 171 GLU 171 B - 182.6 - - - - - - - - 178.4 - 34.1 - Residue-by-residue listing for refined_8 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 b - - -68.2 - - - - - - - 180.1 - 31.4 - 173 GLN 173 - - 181.4 - 186.1 - - - - - - - -1.9 35.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * *** * +* ** ** ** *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.2 183.0 -62.0 179.7 -79.5 -66.5 -37.7 - - - 180.0 -1.9 34.0 * * Standard deviations: 6.6 7.4 6.6 4.9 16.2 7.6 7.6 - - - 4.1 .9 2.1 Numbers of values: 22 54 74 39 7 39 39 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_8 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 - 1.238 1.497 - 1.457 - 116.83 120.11 - 110.60 - 123.06 * * 2 HIS 2 1.312 1.240 1.504 1.540 1.451 121.69 116.49 120.63 107.95 110.95 111.97 122.87 * * * * 3 HIS 3 1.302 1.229 1.523 1.543 1.436 120.56 115.69 121.26 112.60 104.10 111.02 122.92 +* * * +** +** 4 HIS 4 1.303 1.225 1.530 1.551 1.445 121.99 115.87 121.11 111.72 113.23 107.45 123.00 +* * +* +* 5 HIS 5 1.320 1.216 1.524 1.571 1.453 122.10 116.18 121.57 112.60 110.99 113.92 122.11 ** * ** ** 6 HIS 6 1.310 1.224 1.498 1.549 1.462 121.85 116.21 120.67 109.51 110.62 113.27 123.06 * * +* +* 7 HIS 7 1.303 1.224 1.506 1.543 1.442 122.08 115.69 121.02 109.19 110.54 112.82 123.26 +* * +* 8 LEU 8 1.301 1.238 1.509 1.536 1.455 122.84 113.41 122.47 110.42 106.72 110.52 124.11 ** * +* ** 9 GLU 9 1.309 1.238 1.510 1.523 1.425 124.48 115.91 121.00 111.75 109.33 108.00 123.05 * +* +* * +* 10 CYS 10 1.302 1.240 1.516 1.528 1.425 121.04 115.60 121.31 111.51 110.27 110.48 122.99 +* +* +* 11 SER 11 1.300 1.239 1.517 1.541 1.425 122.26 116.97 120.37 110.77 107.92 109.54 122.62 ** +* * ** Residue-by-residue listing for refined_8 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 1.306 1.234 1.520 1.521 1.438 121.05 114.75 120.56 110.64 109.53 109.61 124.67 +* * * +* 13 ASP 13 1.346 1.235 1.508 1.532 1.467 125.14 114.53 122.19 112.02 112.09 113.85 123.05 * +* * +* +* 14 SER 14 1.281 1.233 1.508 1.529 1.423 123.12 115.14 121.41 111.06 107.74 108.03 123.41 *** +* * * *** 15 LEU 15 1.333 1.236 1.515 1.542 1.413 122.32 114.06 122.02 111.18 111.98 112.65 123.72 ** * * ** 16 GLN 16 1.282 1.242 1.491 1.548 1.416 124.22 117.41 120.10 110.91 104.63 112.32 122.35 *** +* ** * ** * *** 17 LEU 17 1.271 1.225 1.476 1.501 1.395 119.67 114.72 121.47 111.50 110.94 112.58 123.77 **** ** * *** * * **** 18 HIS 18 1.271 1.239 1.481 1.526 1.415 122.55 115.06 120.88 108.87 109.46 110.18 124.06 **** ** ** **** 19 ASN 19 1.281 1.242 1.522 1.542 1.419 122.75 115.45 121.67 114.15 110.36 112.61 122.79 *** ** ** * *** 20 VAL 20 1.303 1.221 1.515 1.573 1.450 122.58 117.06 120.13 109.07 109.47 110.49 122.81 +* * +* 21 PHE 21 1.306 1.239 1.500 1.546 1.443 121.08 115.72 120.75 110.81 107.17 110.00 123.52 +* * * +* 22 VAL 22 1.297 1.234 1.508 1.548 1.433 121.95 115.84 120.84 112.05 110.85 112.51 123.32 ** * * ** 23 TYR 23 1.300 1.226 1.523 1.540 1.445 121.35 117.48 120.23 109.66 112.98 108.39 122.29 ** * ** 24 GLY 24 1.319 1.233 1.495 - 1.433 118.89 115.79 120.56 - 113.52 - 123.60 * * * * 25 SER 25 1.317 1.230 1.536 1.532 1.454 123.31 117.36 120.56 110.20 113.20 108.98 122.06 26 PHE 26 1.318 1.223 1.511 1.523 1.455 120.12 117.31 120.31 111.11 113.67 109.93 122.30 27 GLN 27 1.322 1.237 1.548 1.535 1.451 120.13 115.44 121.91 112.08 110.11 110.36 122.64 * * * 28 ASP 28 1.311 1.217 1.530 1.526 1.445 122.29 118.18 120.25 110.28 109.55 110.12 121.57 * * 29 PRO 29 1.336 1.233 1.533 1.528 1.475 122.68 116.83 120.72 109.82 113.55 103.27 122.41 30 ASP 30 1.316 1.246 1.523 1.526 1.458 121.91 116.16 120.68 111.59 111.57 110.82 123.10 31 VAL 31 1.322 1.225 1.529 1.566 1.456 121.41 116.49 120.73 110.48 110.78 114.06 122.77 +* +* 32 ILE 32 1.338 1.248 1.538 1.541 1.455 122.63 115.71 121.06 110.36 110.86 110.12 123.21 33 ASN 33 1.328 1.230 1.514 1.536 1.468 122.53 115.35 121.22 108.39 110.35 110.96 123.42 34 VAL 34 1.311 1.233 1.522 1.550 1.440 122.06 116.53 120.44 109.48 111.69 111.74 123.02 * * 35 MET 35 1.323 1.230 1.525 1.542 1.442 121.55 118.13 120.19 111.74 110.95 109.93 121.58 36 LEU 36 1.325 1.238 1.517 1.561 1.423 118.37 118.25 118.91 116.30 114.69 114.08 122.74 +* +* +* * * *** * ** *** 37 ASP 37 1.341 1.235 1.526 1.545 1.484 121.09 115.75 121.14 108.26 110.84 110.69 123.10 * * 38 ARG 38 1.325 1.215 1.506 1.551 1.484 122.29 117.15 120.31 108.87 110.25 112.55 122.54 * * * * 39 THR 39 1.304 1.239 1.547 1.528 1.435 120.77 117.12 120.66 109.55 112.09 109.93 122.20 +* * * +* 40 PRO 40 1.354 1.242 1.524 1.532 1.470 124.01 116.51 120.25 109.42 111.40 103.75 123.15 41 GLU 41 1.321 1.222 1.532 1.530 1.453 121.79 116.54 120.99 109.75 109.18 110.81 122.47 42 ILE 42 1.288 1.237 1.501 1.558 1.441 121.24 115.60 120.95 108.13 109.30 111.37 123.44 +** * +** 43 VAL 43 1.283 1.233 1.512 1.558 1.420 121.72 116.73 120.68 110.47 108.53 112.37 122.55 *** ** *** Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 SER 44 1.287 1.245 1.518 1.500 1.416 121.01 116.34 120.76 111.09 108.81 108.97 122.88 *** +* ** *** 45 ALA 45 1.298 1.226 1.501 1.505 1.429 121.35 115.21 121.15 110.01 110.87 110.00 123.63 ** * +* ** 46 THR 46 1.279 1.221 1.508 1.541 1.421 123.02 115.88 120.55 110.20 110.01 110.24 123.54 +*** +* +*** 47 LEU 47 1.298 1.233 1.529 1.537 1.428 122.67 117.36 120.58 111.35 109.40 110.20 121.97 ** +* ** 48 PRO 48 1.334 1.247 1.526 1.522 1.444 122.70 116.08 121.21 110.87 111.63 102.78 122.71 * * 49 GLY 49 1.305 1.234 1.504 - 1.431 120.42 115.99 120.93 - 111.11 - 123.07 +* * +* 50 PHE 50 1.323 1.224 1.494 1.546 1.448 123.12 116.74 120.02 110.53 108.91 112.32 123.24 * * * 51 GLN 51 1.298 1.239 1.505 1.534 1.427 121.23 114.81 120.98 110.26 109.62 110.84 124.19 ** +* ** 52 ARG 52 1.301 1.230 1.498 1.526 1.431 123.75 116.22 120.73 110.69 107.80 109.09 123.05 ** * * * * ** 53 PHE 53 1.279 1.230 1.495 1.529 1.416 120.93 114.23 121.70 113.26 113.34 112.23 124.06 +*** * ** +* * +*** 54 ARG 54 1.288 1.233 1.506 1.538 1.428 124.26 116.51 120.06 109.32 109.18 106.83 123.40 +** +* * ** +** 55 LEU 55 1.326 1.224 1.527 1.561 1.437 120.68 114.80 122.58 115.82 110.57 112.71 122.49 +* * * *** * *** 56 LYS 56 1.295 1.244 1.521 1.530 1.421 121.56 115.58 120.75 110.60 110.31 108.57 123.58 ** +* * ** 57 GLY 57 1.318 1.232 1.520 - 1.445 122.52 115.94 120.95 - 114.67 - 123.09 * * 58 ARG 58 1.312 1.232 1.528 1.556 1.462 122.20 117.50 120.35 108.81 112.23 110.28 122.15 * * * 59 LEU 59 1.306 1.232 1.537 1.537 1.440 119.31 115.49 120.78 113.32 112.42 109.71 123.71 +* * +* +* 60 TYR 60 1.324 1.240 1.538 1.543 1.459 124.33 118.55 119.84 106.41 109.04 109.07 121.60 * * +* +* 61 PRO 61 1.359 1.231 1.526 1.545 1.451 121.89 116.20 120.73 110.26 108.96 104.66 123.01 * * * +* +* 62 CYS 62 1.300 1.241 1.540 1.528 1.438 121.87 115.93 120.69 112.16 112.20 108.10 123.37 ** * * * ** 63 ILE 63 1.331 1.210 1.524 1.576 1.467 123.60 117.52 119.65 107.15 109.29 110.38 122.80 * * * * 64 VAL 64 1.318 1.236 1.539 1.582 1.476 122.65 118.78 119.48 108.79 107.81 113.77 121.71 +* * * * +* 65 PRO 65 1.346 1.233 1.547 1.535 1.475 122.61 115.46 121.44 110.78 113.93 103.93 123.09 * * 66 SER 66 1.315 1.225 1.526 1.533 1.442 123.67 116.88 120.38 110.71 108.26 110.28 122.73 * * * 67 GLU 67 1.311 1.226 1.530 1.516 1.463 122.54 116.72 120.71 108.88 112.37 110.28 122.55 * * 68 LYS 68 1.311 1.241 1.526 1.566 1.459 121.32 116.21 120.87 110.68 110.96 112.14 122.87 * +* +* 69 GLY 69 1.320 1.249 1.513 - 1.440 120.67 115.60 120.90 - 112.68 - 123.50 70 GLU 70 1.311 1.240 1.531 1.554 1.437 123.86 116.54 120.82 110.49 109.57 112.70 122.64 * * * * * * 71 VAL 71 1.309 1.219 1.515 1.559 1.449 121.86 117.63 120.19 107.88 110.13 111.36 122.17 * * Residue-by-residue listing for refined_8 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 1.313 1.235 1.508 1.553 1.454 119.70 116.70 120.39 110.27 106.80 112.37 122.91 * * * +* * +* 73 GLY 73 1.294 1.244 1.492 - 1.429 120.61 116.47 120.58 - 111.91 - 122.93 ** * * ** 74 LYS 74 1.307 1.234 1.525 1.545 1.436 120.91 115.98 120.83 109.63 110.30 109.87 123.17 +* * +* 75 VAL 75 1.304 1.227 1.524 1.544 1.437 122.89 115.94 120.43 109.02 110.73 110.75 123.62 +* * +* 76 LEU 76 1.317 1.231 1.518 1.540 1.445 122.93 116.58 120.24 108.19 108.86 111.09 123.10 * * 77 MET 77 1.304 1.219 1.510 1.502 1.420 123.14 117.44 120.23 108.26 108.35 108.67 122.33 +* * +* * * +* 78 GLY 78 1.301 1.238 1.522 - 1.439 119.29 116.74 120.56 - 112.79 - 122.69 +* +* 79 VAL 79 1.321 1.237 1.541 1.578 1.453 121.01 118.12 119.96 111.78 108.31 111.40 121.89 * * * * 80 THR 80 1.322 1.235 1.528 1.554 1.457 119.94 116.19 120.96 109.97 111.73 112.87 122.85 81 SER 81 1.314 1.230 1.541 1.520 1.461 122.29 116.52 120.55 111.07 111.99 109.95 122.90 * * 82 ASP 82 1.328 1.228 1.517 1.534 1.474 122.35 115.01 121.81 109.92 110.48 110.39 123.17 83 GLU 83 1.289 1.213 1.535 1.507 1.438 122.70 117.03 120.61 111.30 109.28 107.78 122.36 +** * * +* +** 84 LEU 84 1.337 1.215 1.510 1.529 1.460 121.02 116.60 120.15 108.46 109.91 113.16 123.25 +* +* 85 GLU 85 1.341 1.208 1.523 1.546 1.462 121.35 115.23 121.40 111.41 109.45 112.50 123.36 * * * 86 ASN 86 1.316 1.216 1.520 1.516 1.446 123.65 116.16 120.64 110.86 110.56 108.40 123.18 * * * 87 LEU 87 1.318 1.246 1.516 1.533 1.462 122.83 114.24 121.84 110.22 109.66 110.26 123.88 88 ASP 88 1.316 1.225 1.524 1.526 1.452 124.08 115.30 121.59 110.79 109.72 108.56 123.09 * * * 89 ALA 89 1.306 1.214 1.536 1.519 1.436 123.02 117.11 120.64 109.98 111.55 109.93 122.24 +* * +* 90 VAL 90 1.330 1.233 1.556 1.583 1.465 120.95 119.02 119.46 113.04 113.98 111.90 121.48 * +* * +* +* 91 GLU 91 1.326 1.224 1.508 1.542 1.473 119.68 114.82 121.54 111.78 110.81 114.10 123.57 * ** ** 92 GLY 92 1.314 1.222 1.530 - 1.458 123.47 118.29 120.02 - 115.57 - 121.60 * +* * +* 93 ASN 93 1.313 1.226 1.519 1.538 1.462 119.73 116.58 120.60 110.51 111.58 113.22 122.81 * * +* +* 94 GLU 94 1.322 1.230 1.538 1.535 1.463 121.88 115.36 121.44 109.28 110.34 108.81 123.19 95 TYR 95 1.315 1.224 1.507 1.524 1.453 123.77 116.58 120.44 108.71 110.42 110.60 122.99 * * * 96 GLU 96 1.310 1.244 1.510 1.536 1.439 121.20 115.60 120.70 110.10 108.37 111.19 123.68 * * * 97 ARG 97 1.311 1.231 1.506 1.517 1.433 122.33 116.67 120.56 108.25 108.79 109.66 122.76 * * * 98 VAL 98 1.290 1.244 1.498 1.535 1.431 121.11 115.01 121.10 110.79 112.40 114.03 123.88 +** * * * +** 99 THR 99 1.298 1.237 1.531 1.571 1.438 122.32 116.31 121.25 111.80 108.98 111.58 122.41 ** * * * ** 100 VAL 100 1.300 1.241 1.516 1.553 1.446 121.18 115.53 121.10 109.16 111.60 111.91 123.37 ** ** Residue-by-residue listing for refined_8 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 1.308 1.234 1.504 - 1.431 121.19 116.23 120.40 - 111.02 - 123.37 +* * +* 102 ILE 102 1.306 1.223 1.508 1.576 1.446 122.27 116.95 120.40 111.71 110.46 112.44 122.65 +* * * +* 103 VAL 103 1.295 1.225 1.513 1.547 1.432 121.34 114.77 121.19 111.12 109.81 112.07 124.03 ** * ** 104 ARG 104 1.299 1.227 1.525 1.520 1.438 124.56 115.58 120.73 110.63 111.39 108.20 123.67 ** * +* * ** 105 GLU 105 1.314 1.226 1.525 1.531 1.466 123.77 116.01 120.81 109.54 112.16 109.33 123.18 * * * 106 ASP 106 1.318 1.228 1.509 1.530 1.475 122.22 115.71 121.41 105.99 113.05 111.39 122.88 ** ** 107 ASN 107 1.303 1.226 1.555 1.551 1.420 121.03 115.86 121.69 116.10 113.43 106.12 122.42 +* * * ** *** +** *** 108 SER 108 1.337 1.231 1.555 1.556 1.481 123.45 116.64 121.38 112.06 112.45 109.64 121.94 * * * * * 109 GLU 109 1.311 1.232 1.506 1.518 1.445 121.44 116.78 120.68 109.90 109.24 110.22 122.55 * * 110 LYS 110 1.278 1.238 1.517 1.525 1.427 120.29 115.85 120.80 110.72 109.78 111.19 123.32 +*** +* +*** 111 MET 111 1.290 1.228 1.465 1.515 1.445 122.99 114.60 121.41 107.68 110.18 115.36 123.98 +** +** * +** +** 112 ALA 112 1.262 1.232 1.491 1.511 1.432 122.05 116.05 120.70 110.43 108.52 111.63 123.24 *4.8* +* * *4.8* 113 VAL 113 1.293 1.242 1.509 1.558 1.433 121.37 115.85 120.66 108.99 110.23 112.12 123.48 +** * +** 114 LYS 114 1.296 1.228 1.519 1.538 1.439 122.26 117.92 119.70 108.95 107.19 109.84 122.34 ** * * ** 115 THR 115 1.299 1.238 1.516 1.564 1.444 120.32 116.51 120.13 110.48 108.61 112.89 123.36 ** ** 116 TYR 116 1.300 1.224 1.510 1.535 1.429 122.44 116.06 121.09 111.01 109.06 110.21 122.81 ** +* ** 117 MET 117 1.297 1.248 1.503 1.543 1.444 121.32 115.65 120.52 110.74 109.79 113.57 123.79 ** * +* ** 118 TRP 118 1.307 1.233 1.518 1.526 1.425 122.54 115.10 121.15 111.43 108.63 110.07 123.74 +* +* +* 119 ILE 119 1.310 1.241 1.526 1.534 1.449 122.67 117.17 120.64 110.27 112.02 110.19 122.17 * * 120 ASN 120 1.323 1.216 1.500 1.543 1.453 119.74 114.98 121.96 111.39 108.63 113.41 123.01 * * +* +* 121 LYS 121 1.296 1.222 1.520 1.537 1.442 122.44 116.16 120.75 113.31 112.81 110.44 123.09 ** +* ** 122 ALA 122 1.316 1.229 1.533 1.520 1.446 122.22 115.84 120.80 110.63 109.82 110.15 123.35 123 ASP 123 1.326 1.214 1.536 1.542 1.472 123.23 118.95 120.29 110.30 109.97 109.17 120.67 * * * 124 PRO 124 1.338 1.234 1.543 1.527 1.448 122.23 117.83 120.13 109.75 113.31 101.42 122.02 * * * 125 ASP 125 1.327 1.229 1.517 1.537 1.460 120.77 118.70 119.36 110.11 114.23 112.32 121.94 * * * * 126 MET 126 1.336 1.231 1.508 1.555 1.479 119.36 115.93 121.13 109.60 110.22 114.84 122.93 * * * +** +** 127 PHE 127 1.316 1.242 1.518 1.530 1.433 121.18 114.32 121.50 111.69 111.31 112.39 124.09 * * * 128 GLY 128 1.306 1.238 1.485 - 1.421 123.17 116.89 119.64 - 109.29 - 123.44 +* +* +* +* * +* Residue-by-residue listing for refined_8 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 129 GLU 129 1.299 1.231 1.521 1.548 1.436 120.86 117.46 120.22 108.92 109.69 110.38 122.29 ** * ** 130 TRP 130 1.315 1.234 1.536 1.556 1.449 120.44 116.69 120.03 110.97 109.15 112.89 123.28 * * * 131 ASN 131 1.326 1.232 1.564 1.533 1.493 125.37 119.05 119.74 109.13 115.45 110.09 121.22 +* +* ** * +* * ** 132 PHE 132 1.337 1.227 1.504 1.532 1.469 120.25 114.91 121.48 108.90 108.64 112.72 123.59 * * * 133 GLU 133 1.321 1.219 1.514 1.504 1.443 122.68 115.31 121.21 110.90 109.46 109.84 123.47 * * 134 GLU 134 1.324 1.220 1.524 1.531 1.448 122.67 116.28 121.02 111.45 109.43 109.91 122.68 135 TRP 135 1.321 1.237 1.525 1.530 1.443 120.66 116.02 120.63 111.74 109.95 111.68 123.32 136 LYS 136 1.337 1.212 1.536 1.544 1.463 122.53 116.24 120.47 110.91 110.94 111.79 123.30 137 ARG 137 1.331 1.224 1.528 1.516 1.446 123.67 117.20 120.55 110.00 112.70 109.91 122.25 * * 138 LEU 138 1.313 1.226 1.526 1.541 1.462 120.95 114.67 121.76 110.72 110.26 111.62 123.56 * * 139 HIS 139 1.300 1.236 1.551 1.561 1.474 124.37 115.46 121.30 111.40 109.97 108.79 123.24 ** * +* * * ** 140 LYS 140 1.333 1.209 1.521 1.535 1.468 124.56 117.99 119.55 110.03 114.03 111.18 122.45 * +* * +* 141 LYS 141 1.321 1.236 1.533 1.513 1.470 120.90 117.03 120.17 109.76 113.30 112.11 122.79 142 LYS 142 1.326 1.235 1.513 1.534 1.469 121.53 113.65 121.89 107.82 108.76 109.94 124.45 * * * 143 PHE 143 1.294 1.233 1.543 1.526 1.427 124.69 115.74 120.97 111.38 110.68 106.71 123.26 +** +* +* ** +** 144 ILE 144 1.328 1.210 1.528 1.576 1.469 123.35 118.04 119.39 109.96 113.16 112.77 122.57 * * * 145 GLU 145 1.333 1.238 1.523 1.508 1.483 121.58 117.17 120.07 108.76 113.84 112.54 122.75 * * * * 146 THR 146 1.317 1.227 1.533 1.556 1.433 120.16 116.19 121.03 111.79 109.83 112.86 122.70 * * * 147 PHE 147 1.327 1.214 1.495 1.524 1.440 122.02 116.71 120.04 112.38 111.68 113.05 123.24 * * +* +* 148 LYS 148 1.327 1.218 1.523 1.540 1.444 121.06 115.78 121.08 110.46 108.27 112.09 123.10 * * 149 LYS 149 1.332 1.218 1.507 1.531 1.450 122.05 116.91 120.23 112.31 112.22 112.72 122.86 * * * 150 ILE 150 1.311 1.226 1.538 1.564 1.454 121.52 116.26 120.91 112.32 110.12 111.30 122.76 * * * 151 MET 151 1.324 1.224 1.529 1.528 1.468 122.23 115.57 120.96 108.90 109.67 110.86 123.47 152 GLU 152 1.332 1.224 1.543 1.531 1.436 124.86 116.21 120.96 113.56 109.80 104.96 122.80 * +* +* *** *** 153 CYS 153 1.329 1.237 1.531 1.534 1.454 121.86 116.60 120.72 109.84 110.55 111.21 122.69 154 LYS 154 1.330 1.240 1.522 1.537 1.458 121.48 115.41 121.06 109.08 109.28 110.73 123.50 155 LYS 155 1.322 1.229 1.531 1.539 1.438 122.54 116.41 120.06 111.60 109.16 110.52 123.48 * * 156 LYS 156 1.334 1.232 1.520 1.552 1.472 124.39 117.50 120.30 107.84 110.82 112.95 122.16 * * * * * 157 PRO 157 1.338 1.242 1.531 1.525 1.444 123.18 117.68 120.23 109.11 108.85 101.58 122.09 * * * * 158 GLN 158 1.306 1.240 1.506 1.533 1.437 119.70 115.44 120.81 111.70 107.58 112.47 123.64 +* * * * * +* 159 GLY 159 1.306 1.237 1.502 - 1.429 121.14 116.92 119.98 - 109.45 - 123.09 +* * * +* Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 160 GLN 160 1.304 1.233 1.520 1.540 1.437 122.02 116.02 120.84 110.48 109.54 111.74 123.12 +* * +* 161 GLY 161 1.303 1.230 1.482 - 1.433 121.51 117.63 119.37 - 108.29 - 123.00 +* +* * * +* 162 ASN 162 1.297 1.243 1.513 1.537 1.443 119.99 114.49 121.39 111.74 112.32 111.89 124.09 ** ** 163 ASP 163 1.304 1.234 1.507 1.543 1.450 125.10 117.59 119.17 110.16 106.26 110.55 123.19 +* +* +* +* 164 ASP 164 1.316 1.239 1.505 1.541 1.467 120.88 115.54 121.17 109.50 111.18 112.74 123.28 * * 165 ILE 165 1.297 1.239 1.512 1.574 1.432 122.78 115.74 120.03 111.33 108.70 112.34 124.21 ** * * * ** 166 SER 166 1.318 1.234 1.528 1.526 1.445 124.40 115.86 120.91 110.99 113.25 108.52 123.19 +* * +* 167 HIS 167 1.320 1.231 1.520 1.550 1.448 122.14 114.94 121.55 111.82 109.82 112.30 123.48 * * 168 VAL 168 1.311 1.234 1.508 1.575 1.443 123.53 116.38 120.39 110.36 108.18 114.05 123.17 * * * * * * 169 LEU 169 1.297 1.244 1.501 1.537 1.439 121.99 115.94 120.45 109.49 109.31 110.43 123.61 ** * ** 170 ARG 170 1.311 1.240 1.516 1.526 1.444 122.11 116.65 120.46 109.41 108.93 110.24 122.89 * * 171 GLU 171 1.299 1.248 1.514 1.545 1.430 120.59 116.83 120.52 111.38 108.47 110.56 122.62 ** * ** 172 ASP 172 1.302 1.221 1.494 1.536 1.433 120.58 114.70 121.61 111.62 109.95 113.57 123.56 +* * * +* +* 173 GLN 173 1.299 - 1.510 1.530 1.432 123.34 - - 110.30 107.39 109.35 - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.8* * +** ** *** ** * * *** +** *** * *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 1.262 1.346 1.311 .015 *4.8* * * C-N (Pro) 1.341 .016 7 1.334 1.359 1.344 .009 * C-O C-O 1.231 .020 172 1.208 1.249 1.231 .009 * CA-C CH1E-C (except Gly) 1.525 .021 161 1.465 1.564 1.520 .015 +** +* CH2G*-C (Gly) 1.516 .018 12 1.482 1.530 1.504 .014 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.505 1.520 1.514 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.528 1.583 1.559 .015 +* CH1E-CH2E (the rest) 1.530 .020 128 1.500 1.571 1.535 .013 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.395 1.493 1.446 .017 *** +* NH1-CH2G* (Gly) 1.451 .016 12 1.421 1.458 1.437 .011 +* N-CH1E (Pro) 1.466 .015 7 1.444 1.475 1.458 .013 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 2.0 153 113.41 119.05 116.21 1.09 * * CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.60 118.29 116.61 .75 CH1E-C-N (Pro) 116.9 1.5 7 115.46 117.83 116.65 .80 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 120.67 124.67 123.00 .65 * * O-C-N (Pro) 122.0 1.4 7 122.02 123.15 122.64 .44 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 118.37 125.37 122.04 1.35 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.89 123.47 121.17 1.39 * +* C-N-CH1E (Pro) 122.6 5.0 7 121.89 124.01 122.76 .63 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.91 122.58 120.76 .63 * * CH2G*-C-O (Gly) 120.8 2.1 12 119.37 120.95 120.33 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.98 110.63 110.26 .27 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.15 113.04 110.26 1.39 +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.99 116.30 110.54 1.63 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.10 115.45 110.27 1.86 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 108.29 115.57 111.74 2.12 * * N-CH1E-C (Pro) 111.8 2.5 7 108.85 113.93 111.66 1.95 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.93 111.63 110.43 .70 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.93 114.06 111.92 1.20 +* N-CH1E-CH2E (Pro) 103.0 1.1 7 101.42 104.66 103.06 1.12 * +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 104.96 115.36 110.80 1.87 *** +** ------------------------------------------------------------------------------------------------------------- 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_8 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] 20 13.1% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% 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 4.1 6.0 3.0 -.6 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 99 .9 .8 .2 .5 Inside f. Overall G-factor 173 -.1 -.4 .3 1.0 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 22 6.6 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 54 7.4 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 74 6.6 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 150 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 39 4.9 20.4 5.0 -3.1 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 8.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_8 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.54 Chi1-chi2 distribution -.14 Chi1 only .01 Chi3 & chi4 .20 Omega -.17 ------ -.21 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .35 ------ .18 ===== OVERALL AVERAGE -.08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.