Residue-by-residue listing for refined_14 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 - - - - - - - - - - - 179.5 - - - 2 HIS 2 B - 178.3 - - - - - - - - 177.2 - 33.8 - 3 HIS 3 S b 65.9 - - - - - - - - - 179.6 -.6 33.6 - +* +* 4 HIS 4 b - - -69.9 - - - - - - - 183.1 - 31.5 - 5 HIS 5 B 57.0 - - - - - - - - - 178.8 -.6 32.2 - +* +* 6 HIS 6 B - 182.6 - - - - - - - - 179.8 -.7 33.8 - +* +* 7 HIS 7 B - 187.4 - - - - - - - - 181.8 - 35.1 - 8 LEU 8 b - - -63.1 179.9 - - - - - - 175.3 -.5 32.4 - ** ** 9 GLU 9 b - 197.9 - - - - - - - - 182.1 -1.4 35.3 - 10 CYS 10 t B - - -58.0 - - - - - - - 179.4 - 34.2 - 11 SER 11 T A - - -56.4 - - - - - - - 175.8 -.7 34.2 - +* +* 12 SER 12 T A 51.7 - - - - - - - - - 182.6 - 35.1 - 13 ASP 13 t XX - 184.8 - - - - - - - - 180.2 -1.7 31.9 - **** **** 14 SER 14 B - - -59.4 - - - - - - - 181.5 - 33.3 - 15 LEU 15 B - - -62.3 - - - - - - - 180.1 -1.0 34.9 - * * 16 GLN 16 B 62.4 - - 175.9 - - - - - - 173.6 - 34.1 - * * 17 LEU 17 B - - -61.4 - - - - - - - 186.1 - 32.8 - * * 18 HIS 18 E B - - -54.0 - - - - - - - 178.0 -2.9 36.4 - * * Residue-by-residue listing for refined_14 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 - - -52.4 - - - - - - - 183.8 - 34.5 - 20 VAL 20 E B - 179.9 - - - - - - - - 178.7 -2.8 34.6 - * * 21 PHE 21 E B - 178.7 - - - - - - - - 179.5 -2.8 35.0 - 22 VAL 22 E B - - -74.0 - - - - - - - 187.3 -2.7 30.2 - * * * 23 TYR 23 A 58.5 - - - - - - - - - 180.9 -.6 32.6 - +* +* 24 GLY 24 t - - - - - - - - - - - 183.6 - - - 25 SER 25 T A - - -54.2 - - - - - - - 178.8 - 34.7 - 26 PHE 26 T a - - -64.3 - - - - - - - 182.8 - 34.3 - 27 GLN 27 t a - 190.8 - 175.7 - - - - - - 181.0 -1.5 34.7 - 28 ASP 28 h B - 183.4 - - - - - - - - 182.3 - 36.0 - 29 PRO 29 H - - - - - -66.9 -66.9 -32.9 - - - 181.8 - 38.9 - * * 30 ASP 30 H A - 178.0 - - - -60.2 -40.1 - - - 179.6 - 32.3 - 31 VAL 31 H A 64.9 - - - - -74.2 -29.4 - - - 178.7 - 31.5 - 32 ILE 32 H A - - -62.2 - - -64.8 -45.5 - - - 176.4 -1.2 33.7 - * * 33 ASN 33 H A - - -72.8 - - -57.1 -37.0 - - - 182.0 -2.5 34.3 - 34 VAL 34 H A - 179.5 - - - -80.2 -42.9 - - - 183.2 -1.3 33.5 - * * * 35 MET 35 H A - 190.5 - - - -69.4 -36.8 - - - 178.4 -3.3 33.7 - +* +* 36 LEU 36 h a 53.6 - - - - - - - - - 181.7 -2.9 26.1 - * ** ** 37 ASP 37 t ~b - 185.7 - - - - - - - - 181.9 -1.0 35.2 - ** * ** 38 ARG 38 S b - - -67.4 - - - - - - - 178.8 - 33.4 - 39 THR 39 B - - -54.0 - - - - - - - 172.9 - 34.7 - * * 40 PRO 40 - - - - - -63.8 - - - - - 184.5 - 39.2 - +* +* 41 GLU 41 E B - - -70.4 173.9 - - - - - - 187.5 -.8 30.0 - * +* * +* 42 ILE 42 E B - - -49.7 - - - - - - - 173.8 - 35.0 - * * * 43 VAL 43 E B 64.0 - - - - - - - - - 175.9 -1.7 33.4 - 44 SER 44 E B - - -59.1 - - - - - - - 180.5 - 34.6 - 45 ALA 45 E B - - - - - - - - - - 181.3 -1.9 34.2 - 46 THR 46 E B - - -58.0 - - - - - - - 176.6 -3.2 35.2 - * * 47 LEU 47 E B - 176.9 - - - - - - - - 181.0 -3.4 34.4 - +* +* 48 PRO 48 E - - - - - -84.0 - - - - - 179.6 - 38.4 - +* * +* 49 GLY 49 E - - - - - - - - - - - 181.8 -3.0 - - * * 50 PHE 50 E B - - -68.7 - - - - - - - 186.4 -.8 32.7 - * +* +* 51 GLN 51 E B - 180.0 - 172.2 - - - - - - 177.9 -2.5 35.5 - 52 ARG 52 E B - 188.8 - 192.5 - - - - - - 177.4 - 35.6 - 53 PHE 53 e B - - -79.5 - - - - - - - 184.2 -1.9 32.4 - 54 ARG 54 B - 187.1 - - - - - - - - 179.4 - 36.6 - 55 LEU 55 S B 64.8 - - 172.7 - - - - - - 178.4 - 32.2 - 56 LYS 56 S ~a - 187.0 - 181.1 - - - - - - 179.2 - 34.9 - ** ** Residue-by-residue listing for refined_14 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 GLY 57 S - - - - - - - - - - - 182.8 -1.9 - - 58 ARG 58 S A - 173.6 - 190.1 - - - - - - 200.2 -2.7 36.3 - *** *** 59 LEU 59 S B - 187.3 - - - - - - - - 182.0 - 35.2 - 60 TYR 60 B - - -53.6 - - - - - - - 174.3 - 37.0 - 61 PRO 61 S - - - - - -59.5 - - - - - 179.9 - 38.6 - * * 62 CYS 62 e B 58.5 - - - - - - - - - 179.6 -1.0 35.1 - * * 63 ILE 63 E B - - -61.4 - - - - - - - 171.5 - 35.8 - * * 64 VAL 64 E B - - -63.9 - - - - - - - 176.6 -1.5 33.9 - 65 PRO 65 E - - - - - -60.0 - - - - - 181.7 - 37.9 - * * 66 SER 66 E B - 184.9 - - - - - - - - 178.4 -2.0 34.5 - 67 GLU 67 E A - - -53.9 176.4 - - - - - - 175.7 - 34.8 - 68 LYS 68 E b - - -62.9 - - - - - - - 178.4 - 32.3 - 69 GLY 69 E - - - - - - - - - - - 176.2 -.6 - - +* +* 70 GLU 70 E B 60.3 - - 181.9 - - - - - - 181.7 - 33.3 - 71 VAL 71 E B - 184.5 - - - - - - - - 174.4 -2.7 35.4 - 72 HIS 72 E B - - -59.7 - - - - - - - 183.4 -.6 34.2 - +* +* 73 GLY 73 E - - - - - - - - - - - 184.7 -3.6 - - ** ** 74 LYS 74 E B - - -61.8 - - - - - - - 175.8 -1.1 35.4 - * * 75 VAL 75 E B - 167.6 - - - - - - - - 174.9 -3.0 35.0 - * * 76 LEU 76 E B - - -57.8 180.8 - - - - - - 179.6 -3.4 36.0 - +* +* 77 MET 77 E B 54.7 - - 177.4 - - - - - - 185.1 -3.1 32.5 - * * 78 GLY 78 E - - - - - - - - - - - 179.6 -1.2 - - * * 79 VAL 79 E B 67.5 - - - - - - - - - 181.3 -1.8 33.5 - 80 THR 80 h B 58.7 - - - - - - - - - 180.2 - 33.1 - 81 SER 81 H A - - -55.3 - - -61.0 -33.2 - - - 180.1 - 33.9 - 82 ASP 82 H A - - -62.0 - - -68.4 -36.1 - - - 178.0 - 33.2 - 83 GLU 83 H A - - -55.7 172.6 - -78.1 -28.4 - - - 176.1 - 35.7 - * * 84 LEU 84 H A - 180.2 - - - -65.9 -51.6 - - - 178.1 -1.9 35.3 - * * 85 GLU 85 H A 56.4 - - 181.0 - -62.7 -29.0 - - - 173.9 -3.0 31.8 - * * * 86 ASN 86 H A - 163.0 - - - -59.9 -48.5 - - - 180.5 -1.1 35.8 - * * * 87 LEU 87 H A - - -61.8 176.9 - -67.4 -39.0 - - - 175.6 -1.9 33.3 - 88 ASP 88 H A - - -65.8 - - -60.3 -45.2 - - - 180.6 -2.5 34.1 - 89 ALA 89 H A - - - - - -64.8 -47.0 - - - 182.9 -2.6 34.7 - 90 VAL 90 H A 59.5 - - - - -72.6 -56.7 - - - 182.8 -2.9 30.6 - +* * +* 91 GLU 91 H A - - -61.5 - - -78.1 -31.0 - - - 183.3 -2.5 33.2 - * * 92 GLY 92 h - - - - - - - - - - - 179.2 -1.2 - - * * Residue-by-residue listing for refined_14 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 93 ASN 93 T A - 181.1 - - - - - - - - 178.8 -.6 33.4 - +* +* 94 GLU 94 e a - - -59.0 184.2 - - - - - - 182.2 -2.0 33.6 - 95 TYR 95 E B - - -60.7 - - - - - - - 181.0 -2.5 34.2 - 96 GLU 96 E B - 182.4 - - - - - - - - 182.1 -2.6 34.5 - 97 ARG 97 E B - 183.4 - 188.4 - - - - - - 178.6 - 36.0 - 98 VAL 98 E B - - -65.5 - - - - - - - 181.8 -2.7 32.3 - 99 THR 99 E B 49.0 - - - - - - - - - 184.6 - 34.5 - 100 VAL 100 E B - - -62.9 - - - - - - - 177.9 -2.7 33.5 - 101 GLY 101 E - - - - - - - - - - - 180.8 - - - 102 ILE 102 E B 54.3 - - - - - - - - - 179.9 -2.9 32.0 - * * 103 VAL 103 E B - 178.3 - - - - - - - - 183.2 -2.8 34.3 - * * 104 ARG 104 E B - - -59.9 190.7 - - - - - - 175.9 -2.6 33.4 - 105 GLU 105 e A - - -61.5 - - - - - - - 179.6 -2.8 35.5 - * * 106 ASP 106 T A - 176.4 - - - - - - - - 186.6 -.6 36.1 - * +* +* 107 ASN 107 T a 63.6 - - - - - - - - - 178.0 - 34.7 - 108 SER 108 t l - 185.3 - - - - - - - - 180.5 -1.9 33.2 - 109 GLU 109 e B - - -63.9 - - - - - - - 183.8 - 32.9 - 110 LYS 110 E B 70.7 - - 171.1 - - - - - - 175.1 - 33.8 - 111 MET 111 E B - - -69.3 178.4 - - - - - - 180.3 -3.3 34.1 - +* +* 112 ALA 112 E B - - - - - - - - - - 179.3 - 33.5 - 113 VAL 113 E B - - -60.5 - - - - - - - 175.1 -2.7 35.0 - 114 LYS 114 E B - - -53.9 186.4 - - - - - - 179.6 -1.7 33.8 - 115 THR 115 E B - 192.8 - - - - - - - - 182.7 -2.1 33.0 - 116 TYR 116 E B - - -62.4 - - - - - - - 180.1 -.5 34.0 - ** ** 117 MET 117 E B 64.0 - - 172.0 - - - - - - 181.1 -2.0 31.9 - 118 TRP 118 E B - 188.7 - - - - - - - - 186.7 -3.1 35.5 - * * * 119 ILE 119 e A - - -54.1 - - - - - - - 182.9 -.8 31.5 - +* +* 120 ASN 120 b - 182.3 - - - - - - - - 189.6 - 32.4 - +* +* 121 LYS 121 A - - -55.0 175.2 - - - - - - 176.6 -1.4 33.5 - 122 ALA 122 b - - - - - - - - - - 178.5 - 32.5 - 123 ASP 123 t B - 176.8 - - - - - - - - 182.3 -.6 32.7 - +* +* 124 PRO 124 T - - - - - -76.2 - - - - - 183.1 - 38.5 - * * 125 ASP 125 T A - - -70.3 - - - - - - - 170.9 - 30.0 - +* * +* 126 MET 126 t b 55.7 - - 181.8 - - - - - - 181.8 -.5 31.0 - +* +* 127 PHE 127 B - 183.0 - - - - - - - - 176.0 -1.7 34.6 - 128 GLY 128 - - - - - - - - - - - 181.2 - - - 129 GLU 129 B - - -54.3 185.2 - - - - - - 187.4 - 31.7 - * * 130 TRP 130 h B - 198.1 - - - - - - - - 186.6 -.6 36.1 - * +* +* 131 ASN 131 H A - - -52.9 - - -61.7 -38.6 - - - 176.0 - 33.3 - 132 PHE 132 H A - 184.7 - - - -61.3 -39.6 - - - 178.9 - 37.4 - * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 133 GLU 133 H A - - -66.2 - - -71.5 -27.0 - - - 180.1 - 33.3 - * * 134 GLU 134 H A - 176.4 - 174.0 - -58.0 -41.5 - - - 177.6 -1.5 31.5 - 135 TRP 135 H A - 176.4 - - - -65.5 -38.1 - - - 179.5 -.9 31.2 - * * 136 LYS 136 H A - - -64.1 180.3 - -62.9 -43.1 - - - 179.7 -.9 33.8 - +* +* 137 ARG 137 H A 65.7 - - 181.5 - -68.1 -35.1 - - - 178.4 -2.7 31.6 - 138 LEU 138 H A - - -61.2 179.6 - -69.8 -35.7 - - - 179.6 -2.2 33.8 - 139 HIS 139 H A - 185.8 - - - -71.6 -39.2 - - - 177.2 -2.5 34.6 - 140 LYS 140 H A - 178.7 - 181.7 - -70.1 -34.8 - - - 185.0 -2.5 36.0 - 141 LYS 141 H A - 191.8 - 178.0 - -50.8 -31.0 - - - 178.5 -2.3 33.7 - * * 142 LYS 142 H A - 183.5 - 183.0 - -54.5 -46.6 - - - 179.1 -.6 36.0 - +* +* 143 PHE 143 H A - - -55.7 - - -77.6 -33.9 - - - 183.1 -1.8 35.4 - * * 144 ILE 144 H A - - -56.9 - - -64.6 -33.4 - - - 176.6 -1.8 32.3 - 145 GLU 145 H A - - -60.7 - - -55.5 -34.8 - - - 177.3 -2.4 33.8 - 146 THR 146 H A - - -56.2 - - -73.9 -46.4 - - - 180.2 -.9 35.3 - +* +* 147 PHE 147 H A - - -77.3 - - -68.4 -29.7 - - - 178.8 -1.8 30.1 - * * 148 LYS 148 H A - 183.8 - 177.1 - -54.5 -41.1 - - - 178.7 -3.2 35.0 - +* +* 149 LYS 149 H A - - -57.5 177.2 - -65.3 -36.5 - - - 181.1 -.7 35.9 - +* +* 150 ILE 150 H A - - -57.7 176.2 - -73.4 -37.4 - - - 178.3 -.9 33.9 - +* +* 151 MET 151 H A - - -63.0 178.3 - -67.6 -40.4 - - - 176.0 -3.0 33.0 - * * 152 GLU 152 H A - - -61.6 179.5 - -65.1 -32.1 - - - 178.8 -2.4 34.1 - 153 CYS 153 H A - 180.3 - - - -71.2 -44.4 - - - 181.9 -1.3 34.3 - * * 154 LYS 154 H A - - -63.3 184.8 - -75.0 -45.3 - - - 185.5 -2.5 34.8 - 155 LYS 155 h a - - -61.2 181.3 - - - - - - 181.4 -2.9 31.8 - * * 156 LYS 156 t B 66.4 - - - - - - - - - 179.3 -.7 32.9 - +* +* 157 PRO 157 S - - - - - -69.3 - - - - - 179.1 - 38.7 - * * 158 GLN 158 B - - -62.7 182.1 - - - - - - 176.7 - 33.1 - 159 GLY 159 - - - - - - - - - - - 182.3 -1.0 - - * * 160 GLN 160 B 52.8 - - 178.1 - - - - - - 179.2 - 32.8 - 161 GLY 161 - - - - - - - - - - - 179.2 -.5 - - ** ** 162 ASN 162 B 57.2 - - - - - - - - - 184.3 - 32.1 - 163 ASP 163 b - 184.1 - - - - - - - - 177.4 - 31.3 - 164 ASP 164 B - 175.0 - - - - - - - - 184.1 -1.4 35.0 - 165 ILE 165 B 50.5 - - - - - - - - - 177.4 -.6 26.2 - +* ** ** 166 SER 166 b - - -56.5 - - - - - - - 183.7 - 34.2 - 167 HIS 167 B 59.7 - - - - - - - - - 181.1 - 34.3 - 168 VAL 168 B - - -64.2 - - - - - - - 173.5 - 33.4 - * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 169 LEU 169 S b - 189.6 - - - - - - - - 186.3 - 34.5 - * * 170 ARG 170 b - 175.8 - 179.2 - - - - - - 172.5 -1.4 36.3 - * * 171 GLU 171 B 60.2 - - 179.1 - - - - - - 181.7 - 32.7 - 172 ASP 172 b - - -63.4 - - - - - - - 180.6 - 31.5 - 173 GLN 173 - - 191.1 - - - - - - - - - -1.5 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * +* * +* *** ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.6 182.8 -61.2 179.7 -68.5 -66.4 -38.5 - - - 180.1 -1.9 34.0 Standard deviations: 5.5 6.7 5.9 5.1 8.9 7.0 6.7 - - - 3.7 .9 2.0 Numbers of values: 29 51 70 44 7 42 42 0 0 0 172 107 161 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_14 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 - 1.228 1.503 - 1.467 - 117.23 120.12 - 111.15 - 122.65 * * 2 HIS 2 1.318 1.230 1.514 1.545 1.451 121.56 115.69 120.62 109.90 110.19 111.71 123.68 3 HIS 3 1.310 1.234 1.508 1.563 1.450 123.30 117.39 119.31 110.49 107.60 112.47 123.30 * +* * * +* 4 HIS 4 1.317 1.232 1.509 1.533 1.459 121.06 115.02 121.55 111.29 111.30 113.06 123.42 +* +* 5 HIS 5 1.297 1.229 1.516 1.556 1.432 122.22 115.45 121.28 112.18 111.19 111.58 123.25 ** * * * ** 6 HIS 6 1.301 1.230 1.510 1.543 1.434 122.07 115.54 120.80 110.95 108.77 111.31 123.64 +* * +* 7 HIS 7 1.300 1.232 1.532 1.539 1.442 123.16 116.43 120.67 111.31 109.29 108.59 122.87 ** * ** 8 LEU 8 1.319 1.232 1.511 1.540 1.451 121.79 115.11 121.30 110.48 112.08 112.36 123.50 * * 9 GLU 9 1.298 1.234 1.513 1.546 1.428 122.99 116.02 120.75 110.91 104.97 110.19 123.01 ** +* ** ** 10 CYS 10 1.294 1.229 1.516 1.527 1.428 121.47 116.20 120.77 110.78 110.37 110.23 123.03 ** +* ** 11 SER 11 1.313 1.232 1.541 1.523 1.449 122.78 115.70 121.37 111.64 110.84 108.88 122.92 * * 12 SER 12 1.323 1.234 1.536 1.531 1.442 122.81 114.96 120.71 110.94 109.80 108.81 124.32 Residue-by-residue listing for refined_14 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 1.353 1.225 1.519 1.545 1.481 125.59 117.29 120.59 111.95 110.47 112.09 122.06 +* * ** ** 14 SER 14 1.311 1.231 1.518 1.528 1.445 120.13 116.11 120.31 111.16 110.04 111.01 123.56 * * 15 LEU 15 1.330 1.228 1.508 1.547 1.430 122.72 116.89 120.27 109.32 109.43 111.19 122.80 * * 16 GLN 16 1.301 1.238 1.507 1.540 1.431 120.51 115.59 121.15 109.61 110.71 111.53 123.24 +* * +* 17 LEU 17 1.295 1.243 1.488 1.516 1.417 122.19 115.67 121.23 110.29 108.88 113.26 123.10 ** +* ** +* ** 18 HIS 18 1.270 1.243 1.493 1.534 1.421 121.42 116.30 120.32 109.34 108.26 109.29 123.34 **** +* +* * **** 19 ASN 19 1.295 1.239 1.521 1.541 1.429 121.27 116.97 120.40 109.98 107.28 111.60 122.61 ** +* * ** 20 VAL 20 1.307 1.226 1.521 1.570 1.458 121.90 116.75 120.48 109.47 110.09 111.25 122.77 +* * +* 21 PHE 21 1.309 1.242 1.517 1.550 1.448 121.27 116.14 120.76 111.19 108.85 109.21 123.11 * * 22 VAL 22 1.311 1.235 1.502 1.556 1.440 121.78 114.36 121.87 112.23 111.03 114.26 123.77 * * * +* +* 23 TYR 23 1.296 1.223 1.520 1.509 1.438 123.22 117.81 119.80 111.27 115.31 109.82 122.39 ** * * * ** 24 GLY 24 1.309 1.222 1.495 - 1.444 118.60 116.20 120.24 - 113.09 - 123.51 * * * * 25 SER 25 1.322 1.233 1.536 1.523 1.458 122.75 116.50 120.94 110.80 111.99 108.65 122.53 * * 26 PHE 26 1.310 1.217 1.515 1.522 1.445 121.41 116.58 120.82 109.70 110.66 110.82 122.50 * * 27 GLN 27 1.316 1.234 1.552 1.527 1.455 122.03 114.90 122.16 112.14 109.88 107.94 122.87 * * +* +* 28 ASP 28 1.307 1.220 1.530 1.531 1.439 123.89 119.19 119.63 109.86 107.61 109.09 121.17 +* * * * * +* 29 PRO 29 1.337 1.233 1.524 1.535 1.477 122.38 116.59 120.94 109.71 112.52 103.72 122.44 30 ASP 30 1.314 1.242 1.518 1.531 1.467 121.05 116.36 120.59 110.92 111.28 112.14 122.93 * * 31 VAL 31 1.325 1.222 1.533 1.571 1.450 120.53 116.88 120.65 111.49 110.17 113.59 122.43 * * * * 32 ILE 32 1.334 1.246 1.538 1.549 1.455 121.71 116.06 120.78 110.46 109.96 111.31 123.13 33 ASN 33 1.339 1.225 1.518 1.541 1.471 122.25 116.16 121.13 108.28 111.28 112.12 122.70 34 VAL 34 1.307 1.230 1.533 1.557 1.450 121.44 116.67 120.64 110.12 111.29 111.59 122.68 +* +* 35 MET 35 1.327 1.227 1.536 1.550 1.441 121.81 118.23 119.87 112.54 111.17 109.00 121.82 * * * 36 LEU 36 1.334 1.239 1.532 1.570 1.457 119.24 117.78 119.50 115.04 115.16 114.16 122.68 +* * +** * ** +** 37 ASP 37 1.338 1.227 1.509 1.538 1.482 121.97 115.14 121.44 108.10 110.15 111.28 123.41 * * * 38 ARG 38 1.306 1.210 1.495 1.545 1.464 123.15 118.19 119.23 111.30 108.88 111.36 122.49 +* * * +* 39 THR 39 1.304 1.231 1.524 1.533 1.431 120.35 117.29 120.42 109.34 111.48 110.53 122.25 +* * +* 40 PRO 40 1.342 1.229 1.522 1.531 1.461 122.76 116.92 119.77 110.01 109.51 103.46 123.30 41 GLU 41 1.320 1.235 1.494 1.503 1.462 121.68 114.02 121.77 112.58 113.77 112.35 124.21 * * * * * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 ILE 42 1.293 1.236 1.518 1.570 1.448 121.91 115.57 121.08 106.58 111.50 113.15 123.34 +** * * +** 43 VAL 43 1.296 1.238 1.528 1.559 1.448 122.46 117.31 119.98 109.89 108.91 112.87 122.67 ** ** 44 SER 44 1.307 1.242 1.528 1.515 1.435 121.39 116.21 121.05 110.90 109.81 109.40 122.72 +* * +* 45 ALA 45 1.300 1.226 1.501 1.505 1.441 122.12 115.20 121.08 110.30 110.90 110.27 123.71 ** * ** 46 THR 46 1.285 1.226 1.517 1.541 1.424 123.18 115.72 120.83 109.43 110.43 110.28 123.43 *** +* *** 47 LEU 47 1.296 1.235 1.535 1.538 1.430 123.01 117.57 120.51 111.32 109.24 109.73 121.86 ** * ** 48 PRO 48 1.340 1.245 1.531 1.529 1.451 122.57 115.82 121.28 111.02 112.41 103.14 122.89 * * 49 GLY 49 1.315 1.226 1.508 - 1.438 121.11 116.27 120.81 - 111.84 - 122.91 50 PHE 50 1.315 1.214 1.490 1.533 1.449 122.29 116.99 120.38 111.33 109.73 112.02 122.63 +* +* 51 GLN 51 1.290 1.233 1.487 1.510 1.421 120.64 114.80 120.90 111.24 111.37 107.58 124.29 +** +* * +* +* +** 52 ARG 52 1.315 1.236 1.493 1.545 1.420 122.16 116.13 120.61 108.73 106.73 111.54 123.26 * +* ** +* ** 53 PHE 53 1.267 1.217 1.489 1.524 1.421 121.23 116.03 120.75 112.23 110.34 111.40 123.15 **** +* +* * **** 54 ARG 54 1.285 1.230 1.522 1.530 1.425 121.88 117.18 119.93 110.07 107.62 108.16 122.88 *** +* * * *** 55 LEU 55 1.307 1.247 1.529 1.559 1.446 121.04 115.40 121.03 110.68 111.21 112.93 123.57 +* * * +* 56 LYS 56 1.314 1.233 1.526 1.532 1.448 123.97 115.46 121.03 109.52 108.26 110.83 123.52 * * * * 57 GLY 57 1.328 1.237 1.524 - 1.446 121.40 116.72 120.69 - 112.78 - 122.59 58 ARG 58 1.323 1.228 1.510 1.533 1.464 121.40 116.51 120.80 105.66 113.79 111.14 122.66 ** ** 59 LEU 59 1.293 1.228 1.520 1.535 1.433 119.74 114.41 121.53 111.79 113.37 106.95 124.05 +** * * ** +** 60 TYR 60 1.315 1.234 1.525 1.543 1.449 124.40 118.44 119.64 108.32 109.02 108.83 121.91 * +* * +* 61 PRO 61 1.352 1.235 1.533 1.541 1.461 122.16 115.79 121.07 110.58 111.55 103.53 123.00 62 CYS 62 1.306 1.244 1.535 1.535 1.434 122.72 116.59 120.38 111.19 109.91 108.52 123.03 +* * * +* 63 ILE 63 1.326 1.214 1.490 1.566 1.458 122.59 116.47 120.10 107.27 109.48 112.05 123.40 +* +* 64 VAL 64 1.286 1.240 1.522 1.580 1.451 122.23 118.54 119.41 109.07 107.23 113.64 121.99 *** * * * * *** 65 PRO 65 1.337 1.242 1.536 1.533 1.459 122.18 116.27 120.98 110.68 111.52 104.32 122.74 * * 66 SER 66 1.301 1.237 1.501 1.530 1.437 122.12 116.23 120.27 110.45 109.32 110.51 123.49 +* * * +* 67 GLU 67 1.313 1.225 1.514 1.519 1.450 121.56 115.30 121.04 110.23 108.93 110.05 123.64 * * 68 LYS 68 1.317 1.242 1.498 1.548 1.428 122.46 115.23 121.29 110.73 109.17 113.59 123.25 * +* +* +* 69 GLY 69 1.300 1.232 1.502 - 1.428 119.88 115.24 121.10 - 113.19 - 123.66 ** * ** 70 GLU 70 1.304 1.245 1.512 1.534 1.431 123.60 116.70 120.44 111.26 108.05 111.88 122.83 +* * * * +* Residue-by-residue listing for refined_14 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.297 1.218 1.496 1.553 1.434 121.23 116.41 120.66 108.03 109.98 111.69 122.93 ** * * ** 72 HIS 72 1.289 1.231 1.501 1.553 1.434 120.81 116.61 120.18 111.07 105.20 111.80 123.09 +** * * * ** +** 73 GLY 73 1.291 1.233 1.484 - 1.417 120.45 116.16 120.69 - 111.67 - 123.13 +** +* ** +** 74 LYS 74 1.299 1.236 1.520 1.536 1.431 121.50 115.87 120.72 109.95 110.82 109.24 123.40 ** * ** 75 VAL 75 1.309 1.230 1.515 1.551 1.437 122.91 115.17 120.57 108.95 111.03 110.83 124.26 * * * 76 LEU 76 1.316 1.238 1.513 1.540 1.434 123.36 116.82 120.41 108.12 107.29 111.06 122.74 * * * * 77 MET 77 1.290 1.233 1.495 1.520 1.441 121.28 116.43 120.62 111.47 110.55 111.83 122.95 +** * +** 78 GLY 78 1.310 1.230 1.508 - 1.424 119.62 115.90 120.92 - 110.53 - 123.18 * +* +* 79 VAL 79 1.328 1.247 1.526 1.585 1.446 121.71 117.29 120.25 111.29 108.35 111.79 122.43 +* * +* 80 THR 80 1.307 1.235 1.524 1.545 1.440 120.29 116.36 120.59 109.91 110.69 112.60 123.05 +* +* 81 SER 81 1.308 1.223 1.543 1.519 1.452 122.67 117.37 120.23 110.59 112.09 109.90 122.38 +* +* 82 ASP 82 1.332 1.224 1.515 1.535 1.476 121.32 115.49 121.43 109.73 110.66 112.36 123.08 * * 83 GLU 83 1.299 1.213 1.543 1.522 1.452 122.84 116.22 121.10 110.83 108.40 108.10 122.68 ** * ** 84 LEU 84 1.332 1.222 1.530 1.534 1.467 122.30 116.19 120.80 108.97 109.68 110.35 122.99 85 GLU 85 1.341 1.226 1.521 1.541 1.469 121.99 115.15 121.31 112.21 110.50 111.95 123.53 * * 86 ASN 86 1.321 1.233 1.512 1.526 1.453 123.54 115.13 120.86 109.98 109.80 108.67 123.98 * * * 87 LEU 87 1.317 1.239 1.503 1.526 1.445 123.33 115.96 120.49 111.42 110.50 110.70 123.53 * * 88 ASP 88 1.327 1.214 1.494 1.529 1.455 121.33 115.57 121.17 108.15 109.82 113.01 123.25 * * * * 89 ALA 89 1.299 1.233 1.528 1.509 1.437 122.79 116.73 120.63 110.32 111.74 109.20 122.63 ** * ** 90 VAL 90 1.318 1.232 1.557 1.587 1.453 121.36 117.49 120.25 112.73 113.05 112.34 122.21 +* +* +* +* 91 GLU 91 1.322 1.236 1.520 1.528 1.470 121.83 115.80 121.03 110.60 112.30 110.78 123.14 92 GLY 92 1.322 1.232 1.514 - 1.463 122.62 116.54 120.54 - 114.27 - 122.92 * * 93 ASN 93 1.322 1.232 1.537 1.542 1.454 121.94 117.09 120.57 111.01 110.99 110.80 122.33 94 GLU 94 1.337 1.235 1.536 1.528 1.468 120.68 117.02 120.47 109.38 112.31 111.44 122.51 95 TYR 95 1.322 1.229 1.524 1.538 1.462 121.94 117.24 120.45 110.21 110.20 110.61 122.32 96 GLU 96 1.311 1.236 1.515 1.539 1.447 120.80 115.76 120.60 110.61 110.09 110.00 123.64 * * 97 ARG 97 1.319 1.234 1.507 1.528 1.441 122.43 116.26 120.78 108.22 109.21 110.39 122.96 98 VAL 98 1.290 1.247 1.502 1.536 1.433 121.38 115.74 120.61 110.87 111.07 112.66 123.65 +** * * +** 99 THR 99 1.301 1.251 1.521 1.534 1.412 122.62 116.08 121.13 111.61 110.05 109.18 122.78 +* * ** * * ** 100 VAL 100 1.314 1.238 1.528 1.562 1.454 120.85 115.90 121.21 109.49 112.27 112.01 122.88 * * Residue-by-residue listing for refined_14 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 1.304 1.237 1.502 - 1.432 120.82 116.58 120.37 - 110.54 - 123.04 +* * +* 102 ILE 102 1.302 1.206 1.492 1.569 1.443 121.75 116.77 120.35 111.76 110.54 112.63 122.88 +* * +* * * +* 103 VAL 103 1.283 1.224 1.488 1.552 1.426 121.52 116.90 120.02 110.61 107.45 111.62 123.04 *** +* +* * *** 104 ARG 104 1.309 1.231 1.490 1.526 1.433 119.88 115.04 121.00 108.28 111.02 113.67 123.90 * +* * * +* +* 105 GLU 105 1.304 1.221 1.534 1.528 1.445 122.86 114.28 121.79 110.66 108.08 108.78 123.92 +* * * +* 106 ASP 106 1.330 1.230 1.521 1.541 1.445 124.89 115.82 120.90 109.47 111.28 108.54 123.26 +* * +* 107 ASN 107 1.323 1.233 1.526 1.534 1.464 121.82 116.88 119.90 109.53 113.01 109.66 123.21 108 SER 108 1.335 1.229 1.547 1.556 1.473 123.35 117.06 120.85 111.45 111.78 110.34 122.06 * * * 109 GLU 109 1.314 1.248 1.514 1.515 1.445 121.00 116.26 120.46 111.84 111.13 110.44 123.27 * * 110 LYS 110 1.321 1.236 1.516 1.533 1.429 121.18 114.79 121.63 108.60 111.23 112.63 123.56 +* * +* 111 MET 111 1.287 1.234 1.474 1.511 1.431 123.97 115.20 121.09 108.86 109.54 112.52 123.70 *** ** * * * *** 112 ALA 112 1.267 1.237 1.501 1.517 1.432 121.21 115.87 120.81 111.01 109.95 111.05 123.29 **** * * **** 113 VAL 113 1.303 1.236 1.506 1.565 1.446 122.94 116.73 120.75 107.74 108.48 112.91 122.51 +* +* 114 LYS 114 1.284 1.232 1.500 1.514 1.423 120.24 117.38 119.94 111.18 108.37 110.91 122.65 *** * +* * *** 115 THR 115 1.294 1.246 1.515 1.562 1.429 120.21 115.80 120.41 110.88 109.26 112.60 123.79 ** * ** 116 TYR 116 1.301 1.232 1.505 1.536 1.424 122.54 115.80 120.93 111.36 109.55 110.31 123.25 +* +* +* 117 MET 117 1.308 1.244 1.509 1.548 1.442 121.35 115.16 120.88 110.61 110.13 113.82 123.94 +* +* +* 118 TRP 118 1.299 1.241 1.524 1.528 1.432 123.73 117.05 120.34 111.51 108.17 108.10 122.59 ** * * * * ** 119 ILE 119 1.322 1.236 1.521 1.582 1.462 119.37 116.67 120.13 108.95 111.66 115.55 123.12 +* * ** ** 120 ASN 120 1.321 1.221 1.513 1.533 1.462 121.30 115.07 121.76 111.92 110.29 111.53 123.18 121 LYS 121 1.298 1.232 1.522 1.517 1.450 122.84 116.71 120.55 112.31 113.18 108.46 122.74 ** * * ** 122 ALA 122 1.311 1.236 1.520 1.525 1.434 121.03 115.80 121.33 111.50 110.22 111.84 122.74 * * * 123 ASP 123 1.309 1.246 1.513 1.544 1.456 122.21 117.26 120.79 110.68 109.80 112.59 121.94 * * * 124 PRO 124 1.329 1.230 1.529 1.527 1.454 122.55 117.01 120.54 110.54 113.40 103.32 122.45 125 ASP 125 1.320 1.247 1.505 1.515 1.448 120.59 117.70 120.13 111.98 113.77 113.14 122.14 +* +* 126 MET 126 1.319 1.235 1.512 1.531 1.431 119.04 114.47 122.49 112.78 108.67 113.31 122.83 * * * +* +* 127 PHE 127 1.287 1.237 1.495 1.542 1.411 122.01 114.93 121.18 110.62 108.88 110.61 123.85 *** * ** *** 128 GLY 128 1.276 1.238 1.476 - 1.424 121.71 118.00 119.30 - 108.55 - 122.71 +*** ** +* * +*** 129 GLU 129 1.301 1.234 1.500 1.526 1.430 119.10 114.49 121.52 113.37 110.30 111.18 123.98 ** * * * +* ** Residue-by-residue listing for refined_14 Page 12 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 130 TRP 130 1.296 1.231 1.528 1.557 1.425 123.19 118.19 119.05 112.87 106.03 106.70 122.75 ** * +* * * +* ** ** 131 ASN 131 1.316 1.233 1.524 1.536 1.480 121.69 115.69 121.38 110.66 111.28 111.06 122.92 * * 132 PHE 132 1.315 1.234 1.547 1.507 1.417 124.68 115.17 121.59 111.26 109.90 104.73 123.21 * * * ** +* *** *** 133 GLU 133 1.318 1.232 1.526 1.529 1.453 123.75 116.97 120.30 110.52 111.52 111.18 122.73 * * 134 GLU 134 1.341 1.230 1.519 1.541 1.456 121.07 117.61 120.16 110.82 111.60 113.33 122.20 +* +* 135 TRP 135 1.317 1.230 1.527 1.536 1.445 119.08 116.42 120.77 111.39 110.89 113.52 122.77 * +* +* 136 LYS 136 1.313 1.236 1.510 1.504 1.451 121.24 116.72 120.09 109.23 111.34 111.59 123.19 * * * 137 ARG 137 1.334 1.194 1.519 1.539 1.450 120.69 117.34 120.01 111.25 110.70 113.23 122.61 +* +* +* 138 LEU 138 1.335 1.228 1.516 1.536 1.469 121.31 115.56 121.48 110.02 110.22 111.35 122.95 139 HIS 139 1.309 1.232 1.541 1.541 1.456 121.95 115.15 121.37 111.36 109.20 109.27 123.48 * * 140 LYS 140 1.318 1.234 1.530 1.530 1.460 123.96 115.01 121.00 109.31 110.68 108.66 123.97 * * * 141 LYS 141 1.332 1.218 1.523 1.538 1.468 125.43 115.98 120.56 111.11 112.11 109.90 123.44 ** ** 142 LYS 142 1.325 1.239 1.541 1.532 1.463 123.24 115.47 121.33 109.26 110.23 108.82 123.21 143 PHE 143 1.319 1.239 1.525 1.536 1.456 122.77 114.93 121.74 109.47 109.61 109.91 123.33 144 ILE 144 1.320 1.204 1.523 1.555 1.453 122.83 117.74 119.80 110.98 111.73 112.20 122.46 * * 145 GLU 145 1.329 1.232 1.542 1.530 1.477 121.42 115.82 121.22 109.86 110.70 111.08 122.94 146 THR 146 1.325 1.243 1.546 1.548 1.443 122.41 115.76 121.16 109.94 109.65 109.69 123.05 * * * 147 PHE 147 1.328 1.213 1.499 1.519 1.461 122.60 116.73 119.92 111.58 114.34 113.08 123.35 * * +* +* 148 LYS 148 1.303 1.224 1.533 1.526 1.450 123.40 115.75 120.85 110.93 110.02 108.79 123.28 +* * +* 149 LYS 149 1.332 1.234 1.529 1.529 1.462 122.51 115.03 121.60 108.75 109.48 109.73 123.36 150 ILE 150 1.321 1.225 1.540 1.568 1.451 123.26 116.21 121.06 111.30 109.95 110.47 122.69 * * * 151 MET 151 1.318 1.239 1.522 1.535 1.458 122.44 116.34 120.60 111.14 110.64 111.36 123.04 152 GLU 152 1.335 1.229 1.528 1.535 1.462 121.68 115.54 121.30 109.95 109.74 111.20 123.15 153 CYS 153 1.318 1.228 1.529 1.538 1.448 122.73 116.80 120.54 110.39 111.18 110.12 122.66 154 LYS 154 1.326 1.225 1.502 1.509 1.456 121.09 116.55 120.60 107.79 112.90 111.21 122.85 * * * * 155 LYS 155 1.304 1.232 1.517 1.535 1.442 120.36 117.22 120.14 112.10 112.70 111.33 122.64 +* * +* 156 LYS 156 1.316 1.238 1.519 1.576 1.456 121.60 117.65 119.94 110.53 109.93 112.72 122.40 ** * ** 157 PRO 157 1.349 1.230 1.534 1.536 1.472 122.97 116.62 120.82 110.19 112.56 103.42 122.55 158 GLN 158 1.315 1.230 1.513 1.526 1.438 121.29 115.52 121.15 110.85 110.64 111.47 123.20 * * * 159 GLY 159 1.303 1.228 1.496 - 1.438 121.62 115.47 121.36 - 110.19 - 123.18 +* * +* 160 GLN 160 1.307 1.235 1.517 1.537 1.439 122.55 115.47 121.12 111.63 111.11 111.05 123.38 +* +* 161 GLY 161 1.303 1.235 1.507 - 1.432 121.15 116.32 120.64 - 111.67 - 123.03 +* * +* Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 162 ASN 162 1.329 1.247 1.517 1.556 1.463 121.47 116.88 120.40 112.00 109.86 112.25 122.69 * * * 163 ASP 163 1.317 1.237 1.507 1.536 1.450 120.86 114.21 121.91 111.68 111.85 112.70 123.80 * * 164 ASP 164 1.300 1.239 1.496 1.528 1.439 123.19 116.83 120.20 110.24 108.02 110.27 122.96 ** * * ** 165 ILE 165 1.302 1.231 1.531 1.572 1.437 120.76 114.63 122.38 114.67 115.25 114.49 122.91 +* * * +** * +* +** 166 SER 166 1.308 1.235 1.522 1.532 1.432 123.25 115.49 121.25 111.01 108.31 110.55 123.14 +* * * +* 167 HIS 167 1.306 1.237 1.515 1.557 1.444 123.04 117.13 120.03 110.65 108.95 110.83 122.81 +* * +* 168 VAL 168 1.301 1.235 1.512 1.563 1.441 120.99 115.88 120.97 109.50 111.66 112.47 123.13 +* +* 169 LEU 169 1.311 1.242 1.514 1.564 1.434 121.47 115.80 120.56 111.88 104.55 110.77 123.44 * +* * ** ** 170 ARG 170 1.320 1.245 1.516 1.548 1.448 122.14 115.28 120.97 109.08 110.83 108.94 123.74 171 GLU 171 1.306 1.232 1.516 1.540 1.424 122.89 116.71 121.07 111.96 107.35 112.41 122.14 +* +* * * +* 172 ASP 172 1.296 1.237 1.500 1.536 1.439 119.94 114.48 121.32 112.22 110.20 112.77 124.06 ** * * * ** 173 GLN 173 1.304 - 1.515 1.553 1.433 123.65 - - 112.22 106.89 109.30 - +* * * * * +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** ** ** ** * * +** ** *** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 1.353 1.311 .015 **** +* * C-N (Pro) 1.341 .016 7 1.329 1.352 1.341 .007 C-O C-O 1.231 .020 172 1.194 1.251 1.232 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 161 1.474 1.557 1.518 .015 ** +* CH2G*-C (Gly) 1.516 .018 12 1.476 1.524 1.502 .012 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.505 1.525 1.514 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.533 1.587 1.560 .014 +* CH1E-CH2E (the rest) 1.530 .020 128 1.503 1.576 1.534 .013 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.411 1.482 1.445 .015 ** * NH1-CH2G* (Gly) 1.451 .016 12 1.417 1.467 1.438 .015 ** * N-CH1E (Pro) 1.466 .015 7 1.451 1.477 1.462 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 2.0 153 114.02 119.19 116.18 .98 * * CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.24 118.00 116.39 .71 CH1E-C-N (Pro) 116.9 1.5 7 115.79 117.01 116.43 .46 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.17 124.32 123.04 .54 * O-C-N (Pro) 122.0 1.4 7 122.44 123.30 122.77 .30 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.04 125.59 121.98 1.21 * ** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.60 122.62 120.82 1.07 * * C-N-CH1E (Pro) 122.6 5.0 7 122.16 122.97 122.51 .27 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 119.05 122.49 120.75 .60 * CH2G*-C-O (Gly) 120.8 2.1 12 119.30 121.36 120.56 .51 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.30 111.50 110.78 .50 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 106.58 114.67 110.16 1.67 * +** CH2E-CH1E-C (the rest) 110.1 1.9 128 105.66 115.04 110.63 1.28 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.55 115.31 110.22 1.82 ** * NH1-CH2G*-C (Gly) 112.5 2.9 12 108.55 114.27 111.62 1.50 * N-CH1E-C (Pro) 111.8 2.5 7 109.51 113.40 111.92 1.15 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.20 111.84 110.59 .98 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.18 115.55 112.15 1.40 * ** N-CH1E-CH2E (Pro) 103.0 1.1 7 103.14 104.32 103.56 .35 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 104.73 114.16 110.77 1.70 *** ** ------------------------------------------------------------------------------------------------------------- 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_14 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] 129 84.3% Residues in additional allowed regions [a,b,l,p] 21 13.7% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% Residues in disallowed regions [XX] 1 .7% ---- ------ Number of non-glycine and non-proline residues 153 100.0% Number of end-residues (excl. Gly and Pro) 1 Number of glycine residues 12 Number of proline residues 7 ---- Total number of residues 173 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 153 84.3 83.8 10.0 .1 Inside b. Omega angle st dev 172 3.7 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 161 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 107 .9 .8 .2 .5 Inside f. Overall G-factor 173 .0 -.4 .3 1.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 29 5.5 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 51 6.7 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 70 5.9 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 150 7.5 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 44 5.1 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% 84.3 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_14 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.42 Chi1-chi2 distribution -.19 Chi1 only -.09 Chi3 & chi4 .50 Omega -.02 ------ -.11 ===== Main-chain covalent forces:- Main-chain bond lengths -.02 Main-chain bond angles .41 ------ .23 ===== OVERALL AVERAGE .01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.