Residue-by-residue listing for refined_13 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 - - - - - - - - - - - 179.8 - - - 2 HIS 2 B - - -66.4 - - - - - - - 176.1 - 33.6 - 3 HIS 3 B - - -63.9 - - - - - - - 184.1 -.7 34.0 - +* +* 4 HIS 4 B - 183.1 - - - - - - - - 170.6 - 33.4 - +* +* 5 HIS 5 b - - -70.9 - - - - - - - 177.2 -.6 33.6 - +* +* 6 HIS 6 B 66.8 - - - - - - - - - 179.0 - 33.8 - 7 HIS 7 B 68.0 - - - - - - - - - 176.4 - 31.4 - 8 LEU 8 b - - -60.2 179.6 - - - - - - 182.3 - 33.2 - 9 GLU 9 b 56.3 - - - - - - - - - 178.5 -.6 30.3 - +* * +* 10 CYS 10 B 49.5 - - - - - - - - - 184.0 -1.2 32.5 - * * 11 SER 11 B 53.9 - - - - - - - - - 174.4 -.9 35.5 - * * 12 SER 12 A - - -57.4 - - - - - - - 172.7 - 34.0 - * * 13 ASP 13 XX - 181.1 - - - - - - - - 184.4 - 31.5 - **** **** 14 SER 14 b - - -58.7 - - - - - - - 172.5 -2.4 33.1 - * * 15 LEU 15 B - - -64.6 - - - - - - - 184.4 -.9 34.8 - +* +* 16 GLN 16 B - - -62.8 174.1 - - - - - - 169.4 -.7 37.0 - +* +* +* Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 17 LEU 17 B - - -62.3 178.4 - - - - - - 187.7 - 32.9 - * * 18 HIS 18 E B - - -48.1 - - - - - - - 176.3 -2.9 35.4 - * * * 19 ASN 19 E B 57.6 - - - - - - - - - 186.9 - 30.0 - * * * 20 VAL 20 E B - 178.2 - - - - - - - - 177.4 -2.1 35.6 - 21 PHE 21 E B - 181.3 - - - - - - - - 183.3 -2.9 35.4 - * * 22 VAL 22 E B - - -67.1 - - - - - - - 183.7 -3.0 31.5 - * * 23 TYR 23 A 56.0 - - - - - - - - - 180.5 -.5 32.9 - ** ** 24 GLY 24 t - - - - - - - - - - - 182.8 - - - 25 SER 25 T A 51.2 - - - - - - - - - 179.5 - 35.6 - 26 PHE 26 T a - - -66.1 - - - - - - - 180.9 - 34.2 - 27 GLN 27 t a - 188.8 - 178.8 - - - - - - 180.2 -1.3 34.5 - 28 ASP 28 h B - 178.0 - - - - - - - - 181.9 - 35.5 - 29 PRO 29 H - - - - - -66.5 -66.5 -32.6 - - - 183.9 - 38.8 - * * 30 ASP 30 H A - 177.0 - - - -73.0 -34.7 - - - 175.5 - 33.0 - 31 VAL 31 H A - - -55.4 - - -66.3 -29.4 - - - 175.1 - 31.1 - 32 ILE 32 H A - - -80.2 - - -73.1 -41.4 - - - 183.1 -1.1 34.9 - * * 33 ASN 33 H A - 203.6 - - - -57.8 -39.5 - - - 178.8 -2.5 37.4 - * * * 34 VAL 34 H A - 180.1 - - - -81.4 -29.9 - - - 183.9 -2.0 33.3 - * * 35 MET 35 H A - 190.8 - - - -70.0 -31.9 - - - 172.3 -1.2 32.3 - * * * 36 LEU 36 h a 58.9 - - 163.1 - - - - - - 184.9 -2.0 29.4 - * * 37 ASP 37 S ~b - 176.8 - - - - - - - - 183.0 - 35.8 - ** ** 38 ARG 38 B - - -58.9 179.6 - - - - - - 178.6 - 35.1 - 39 THR 39 B - - -55.3 - - - - - - - 174.4 - 35.1 - 40 PRO 40 - - - - - -67.2 - - - - - 179.9 - 39.1 - * * 41 GLU 41 E B - 187.1 - - - - - - - - 187.3 -2.1 34.5 - * * 42 ILE 42 E B - - -51.1 - - - - - - - 174.8 - 34.5 - * * 43 VAL 43 E B 62.4 - - - - - - - - - 174.5 -2.1 33.4 - 44 SER 44 E B - - -61.4 - - - - - - - 181.3 - 35.2 - 45 ALA 45 E B - - - - - - - - - - 179.6 -2.9 34.1 - * * 46 THR 46 E B - - -58.8 - - - - - - - 175.6 -2.8 35.7 - * * 47 LEU 47 E b - 176.8 - - - - - - - - 179.3 -3.8 34.5 - ** ** 48 PRO 48 E - - - - - -83.2 - - - - - 179.4 - 38.4 - +* * +* 49 GLY 49 E - - - - - - - - - - - 180.6 -3.0 - - * * 50 PHE 50 E B - - -67.6 - - - - - - - 181.4 -.7 33.3 - +* +* Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 51 GLN 51 E B - 182.2 - - - - - - - - 173.3 -2.7 35.3 - * * 52 ARG 52 E B 55.0 - - 137.3 - - - - - - 178.4 - 32.9 - ** ** 53 PHE 53 E B - - -67.3 - - - - - - - 183.2 -1.9 35.5 - 54 ARG 54 B 87.5 - - - - - - - - - 179.4 -3.4 30.0 - * +* * +* 55 LEU 55 t a - 185.7 - - - - - - - - 186.4 -.6 36.1 - * +* +* 56 LYS 56 B b - 183.7 - 178.7 - - - - - - 182.6 - 33.6 - 57 GLY 57 T - - - - - - - - - - - 177.2 -.7 - - +* +* 58 ARG 58 T A - 182.0 - - - - - - - - 181.5 -2.0 33.2 - 59 LEU 59 B B - 186.4 - - - - - - - - 186.9 -2.4 32.0 - * * 60 TYR 60 B - - -52.6 - - - - - - - 173.9 - 35.6 - * * 61 PRO 61 - - - - - -73.8 - - - - - 185.2 - 37.7 - * * 62 CYS 62 E B - - -51.5 - - - - - - - 181.9 -2.1 33.6 - * * 63 ILE 63 E B - - -59.1 - - - - - - - 172.0 -.5 36.5 - * ** ** 64 VAL 64 E B - - -66.8 - - - - - - - 177.6 -1.8 33.7 - 65 PRO 65 E - - - - - -60.3 - - - - - 179.9 - 37.7 - * * 66 SER 66 E B - 180.2 - - - - - - - - 187.3 -1.6 34.7 - * * 67 GLU 67 E A - - -53.0 - - - - - - - 180.2 - 33.9 - 68 LYS 68 E a - - -59.4 179.8 - - - - - - 184.2 - 34.9 - 69 GLY 69 E - - - - - - - - - - - 176.5 -.6 - - +* +* 70 GLU 70 E B 64.1 - - 182.6 - - - - - - 180.2 - 33.1 - 71 VAL 71 E B - 179.8 - - - - - - - - 176.3 -3.0 34.6 - * * 72 HIS 72 E B - - -64.1 - - - - - - - 183.6 -.6 33.3 - +* +* 73 GLY 73 E - - - - - - - - - - - 184.4 -3.0 - - * * 74 LYS 74 E B - - -81.9 - - - - - - - 176.6 -1.0 33.9 - * * * 75 VAL 75 E B - 170.2 - - - - - - - - 176.6 -3.2 34.5 - +* +* 76 LEU 76 E B - - -58.2 180.8 - - - - - - 181.1 -3.1 36.1 - * * 77 MET 77 E B - - -54.8 179.5 - - - - - - 180.0 -3.8 36.5 - ** ** 78 GLY 78 E - - - - - - - - - - - 178.8 -1.7 - - 79 VAL 79 E B - 177.2 - - - - - - - - 178.3 -3.2 35.2 - +* +* 80 THR 80 h B 57.9 - - - - - - - - - 178.9 - 34.2 - 81 SER 81 H A 52.4 - - - - -64.5 -32.2 - - - 177.1 - 32.4 - 82 ASP 82 H A - 180.0 - - - -68.0 -51.0 - - - 180.9 - 34.7 - * * 83 GLU 83 H A - 184.4 - 178.8 - -60.3 -39.6 - - - 175.9 - 34.3 - 84 LEU 84 H A - 184.6 - - - -57.4 -51.2 - - - 179.4 -2.8 35.1 - * * Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 85 GLU 85 H A - - -65.0 180.5 - -68.6 -29.3 - - - 177.7 -2.0 32.9 - 86 ASN 86 H A - 184.2 - - - -65.5 -46.4 - - - 178.6 -2.4 35.9 - 87 LEU 87 H A - - -62.6 175.4 - -64.9 -41.1 - - - 177.3 -2.8 34.5 - * * 88 ASP 88 H A - 177.4 - - - -62.2 -32.8 - - - 177.8 -2.2 33.8 - 89 ALA 89 H A - - - - - -72.8 -43.1 - - - 181.9 -1.6 34.6 - 90 VAL 90 H A - 176.4 - - - -72.4 -56.8 - - - 182.5 -2.2 34.1 - +* +* 91 GLU 91 H A - - -61.1 - - -78.4 -22.8 - - - 184.3 -3.1 34.0 - * * * * 92 GLY 92 h - - - - - - - - - - - 180.4 -.7 - - +* +* 93 ASN 93 T A - - -62.3 - - - - - - - 183.0 -.7 34.0 - +* +* 94 GLU 94 e A - - -60.1 - - - - - - - 184.8 -1.2 35.0 - * * 95 TYR 95 E B - - -59.2 - - - - - - - 175.1 -1.9 35.6 - 96 GLU 96 E B - 178.8 - - - - - - - - 182.0 -2.0 34.1 - 97 ARG 97 E B - 186.7 - 184.2 - - - - - - 179.4 - 36.0 - 98 VAL 98 E B - - -62.7 - - - - - - - 180.9 -2.8 32.8 - 99 THR 99 E B - 179.4 - - - - - - - - 184.4 - 32.1 - 100 VAL 100 E B - - -63.2 - - - - - - - 179.2 -3.4 35.0 - +* +* 101 GLY 101 E - - - - - - - - - - - 178.6 - - - 102 ILE 102 E B 56.0 - - - - - - - - - 181.0 -2.2 31.9 - 103 VAL 103 E B - 180.6 - - - - - - - - 180.3 -2.7 34.4 - 104 ARG 104 E B - - -61.2 184.4 - - - - - - 180.0 -2.8 34.5 - * * 105 GLU 105 e A - - -62.6 188.6 - - - - - - 174.5 -2.7 31.9 - 106 ASP 106 S A - - -57.2 - - - - - - - 182.9 - 36.9 - 107 ASN 107 S a 56.0 - - - - - - - - - 180.6 - 30.8 - 108 SER 108 S ~a 53.9 - - - - - - - - - 182.7 - 34.3 - ** ** 109 GLU 109 e B 59.0 - - 178.9 - - - - - - 179.5 - 33.0 - 110 LYS 110 E B 58.2 - - 184.1 - - - - - - 184.3 - 32.3 - 111 MET 111 E B - - -76.4 - - - - - - - 179.1 -3.8 35.1 - ** ** 112 ALA 112 E B - - - - - - - - - - 183.5 - 33.3 - 113 VAL 113 E B - - -59.6 - - - - - - - 171.7 -3.0 35.9 - * * * 114 LYS 114 E B - - -69.6 - - - - - - - 176.5 -1.6 32.0 - 115 THR 115 E B - 192.0 - - - - - - - - 181.9 -2.6 33.5 - 116 TYR 116 E B - - -61.0 - - - - - - - 181.1 -.6 33.8 - +* +* 117 MET 117 E B 64.1 - - 174.6 - - - - - - 179.5 -1.8 32.2 - 118 TRP 118 E B - 197.4 - - - - - - - - 185.1 -3.3 36.9 - +* +* 119 ILE 119 e A - - -60.5 - - - - - - - 177.9 -.7 31.1 - +* +* 120 ASN 120 B - 180.1 - - - - - - - - 187.9 - 32.7 - * * 121 LYS 121 S A - - -54.0 174.1 - - - - - - 174.8 -1.0 33.9 - * * 122 ALA 122 S b - - - - - - - - - - 181.7 - 32.3 - 123 ASP 123 B - 185.4 - - - - - - - - 183.1 - 34.8 - 124 PRO 124 S - - - - - -81.0 - - - - - 177.0 - 38.3 - * * * Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 125 ASP 125 S a - - -70.7 - - - - - - - 179.9 - 32.0 - 126 MET 126 B 58.1 - - 175.2 - - - - - - 175.0 - 32.0 - 127 PHE 127 B - 184.1 - - - - - - - - 182.8 -1.1 34.3 - * * 128 GLY 128 - - - - - - - - - - - 182.1 - - - 129 GLU 129 B B - - -56.0 - - - - - - - 187.8 - 35.0 - * * 130 TRP 130 h B - 210.3 - - - - - - - - 188.8 -1.8 33.9 - +* +* +* 131 ASN 131 H a - - -65.7 - - -53.3 -4.5 - - - 176.6 - 31.3 - * *** *** 132 PHE 132 H A - 165.4 - - - -73.2 -36.6 - - - 179.8 - 34.9 - * * 133 GLU 133 H A 60.9 - - - - -72.2 -26.4 - - - 180.5 -2.7 32.0 - * * 134 GLU 134 H A - 178.2 - 179.6 - -56.8 -50.6 - - - 178.5 -.5 34.8 - +* +* 135 TRP 135 H A - 178.4 - - - -65.5 -32.6 - - - 178.8 -1.0 31.2 - * * 136 LYS 136 H A - 179.1 - - - -59.2 -51.5 - - - 179.3 -1.0 34.0 - * * * 137 ARG 137 H A 50.9 - - 178.7 - -70.5 -30.9 - - - 177.7 -2.7 30.9 - 138 LEU 138 H A - - -59.7 181.2 - -70.6 -34.0 - - - 177.9 -2.3 33.4 - 139 HIS 139 H A - 186.1 - - - -75.6 -39.5 - - - 176.3 -2.5 34.4 - 140 LYS 140 H A - 172.1 - 180.0 - -63.3 -35.6 - - - 181.5 -2.5 34.2 - 141 LYS 141 H A - 180.0 - 177.4 - -52.8 -35.3 - - - 179.3 -2.2 33.4 - * * 142 LYS 142 H A - 182.6 - 178.3 - -61.5 -35.8 - - - 177.2 -.7 34.1 - +* +* 143 PHE 143 H A - - -59.7 - - -76.4 -43.3 - - - 183.6 -1.4 36.3 - 144 ILE 144 H A - - -55.2 - - -59.5 -33.8 - - - 177.0 -2.5 32.9 - 145 GLU 145 H A - - -63.6 181.5 - -54.3 -31.6 - - - 175.2 -2.3 33.2 - 146 THR 146 H A - - -64.2 - - -81.1 -48.0 - - - 190.4 -1.6 35.7 - * +* +* 147 PHE 147 H A - 205.6 - - - -76.8 -30.6 - - - 180.4 -1.9 32.0 - * * 148 LYS 148 H A - 178.6 - 178.5 - -56.2 -39.4 - - - 180.6 -3.7 34.5 - ** ** 149 LYS 149 H A - - -58.6 180.0 - -71.8 -33.9 - - - 178.1 - 34.0 - 150 ILE 150 H A - - -61.3 177.0 - -68.8 -38.8 - - - 178.8 -.9 34.7 - * * 151 MET 151 H A - 181.6 - 178.6 - -64.6 -37.8 - - - 176.8 -2.8 34.4 - 152 GLU 152 H A - - -62.8 - - -71.8 -31.0 - - - 178.1 -1.7 33.9 - 153 CYS 153 H A - 180.8 - - - -68.2 -34.5 - - - 178.4 -1.6 34.2 - 154 LYS 154 H A - - -60.7 187.2 - -75.9 -18.1 - - - 179.9 -1.8 33.4 - +* +* 155 LYS 155 h b - 181.8 - 177.8 - - - - - - 177.4 -.6 32.8 - +* +* 156 LYS 156 t B - - -62.7 180.4 - - - - - - 175.6 -2.3 36.4 - 157 PRO 157 B - - - - - -66.8 - - - - - 179.3 - 37.5 - * * 158 GLN 158 T a 50.0 - - - - - - - - - 183.9 -1.6 32.0 - 159 GLY 159 T - - - - - - - - - - - 175.0 - - - 160 GLN 160 B B 58.8 - - 179.3 - - - - - - 178.9 -.7 34.5 - +* +* 161 GLY 161 - - - - - - - - - - - 185.0 - - - 162 ASN 162 a 55.2 - - - - - - - - - 184.8 - 34.8 - Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 163 ASP 163 A 67.1 - - - - - - - - - 177.9 - 34.5 - 164 ASP 164 B - 183.4 - - - - - - - - 182.9 - 33.8 - 165 ILE 165 S A - 186.6 - - - - - - - - 179.2 - 33.6 - 166 SER 166 A 57.1 - - - - - - - - - 175.8 - 31.8 - 167 HIS 167 XX - 178.8 - - - - - - - - 180.1 - 32.4 - **** **** 168 VAL 168 XX - - -53.3 - - - - - - - 177.4 -2.8 29.4 - **** * * **** 169 LEU 169 B - 182.6 - - - - - - - - 184.6 - 35.1 - 170 ARG 170 b - - -63.0 181.3 - - - - - - 173.0 -.6 30.8 - * +* +* 171 GLU 171 B - - -58.1 180.6 - - - - - - 185.5 -1.4 34.8 - 172 ASP 172 B - - -63.2 - - - - - - - 178.4 - 32.1 - 173 GLN 173 - - 188.8 - - - - - - - - - - 34.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* * ** +* * *** +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.7 182.9 -61.6 178.2 -71.3 -67.2 -36.2 - - - 179.9 -1.9 34.0 Standard deviations: 7.4 7.7 6.2 7.8 8.4 7.6 9.5 - - - 3.9 .9 1.8 Numbers of values: 29 56 65 40 7 42 42 0 0 0 172 105 161 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_13 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 - 1.230 1.500 - 1.461 - 116.90 120.17 - 111.08 - 122.93 2 HIS 2 1.311 1.230 1.511 1.538 1.451 122.05 115.92 121.03 109.62 110.79 112.04 123.02 * * 3 HIS 3 1.304 1.235 1.502 1.534 1.453 122.68 117.29 120.10 109.84 108.04 112.05 122.61 +* * * +* 4 HIS 4 1.299 1.230 1.521 1.536 1.437 120.43 115.21 121.48 110.23 112.68 111.03 123.31 ** * ** 5 HIS 5 1.297 1.234 1.505 1.548 1.438 122.85 116.46 120.24 109.77 107.73 113.16 123.29 ** * * +* ** 6 HIS 6 1.296 1.233 1.502 1.561 1.437 122.76 118.04 119.31 111.22 107.01 111.81 122.65 ** * +* * * ** 7 HIS 7 1.298 1.230 1.518 1.560 1.435 119.48 115.47 121.73 112.24 110.81 112.74 122.70 ** +* * * * * ** 8 LEU 8 1.289 1.232 1.499 1.536 1.432 121.50 115.33 121.33 111.07 108.32 112.11 123.18 +** * * * +** 9 GLU 9 1.296 1.245 1.511 1.566 1.423 121.59 114.92 121.75 113.24 111.62 113.01 123.25 ** +* +* +* * ** 10 CYS 10 1.306 1.229 1.514 1.528 1.429 122.23 115.22 121.69 113.15 110.38 110.23 123.05 +* +* +* +* 11 SER 11 1.301 1.234 1.521 1.544 1.425 122.10 116.82 120.48 110.82 110.14 108.53 122.70 ** +* * ** Residue-by-residue listing for refined_13 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 1.316 1.240 1.525 1.524 1.449 121.14 113.93 121.61 111.47 107.94 110.34 124.46 * * * 13 ASP 13 1.335 1.231 1.510 1.535 1.457 125.77 116.84 120.40 111.05 114.00 112.18 122.76 ** ** 14 SER 14 1.292 1.230 1.520 1.519 1.422 120.61 115.54 121.22 111.31 112.69 110.30 123.13 +** +* +** 15 LEU 15 1.308 1.237 1.502 1.534 1.408 122.75 116.03 120.90 109.99 106.42 111.60 123.02 +* * +** +* +** 16 GLN 16 1.289 1.245 1.492 1.531 1.429 121.89 116.05 120.67 107.51 109.77 109.77 123.26 +** +* +* * +** 17 LEU 17 1.295 1.237 1.501 1.522 1.411 120.49 116.43 120.64 111.56 106.11 112.84 122.88 ** * ** +* * ** 18 HIS 18 1.266 1.235 1.470 1.535 1.426 121.07 115.44 120.83 109.36 109.18 110.65 123.69 *4.5* +** +* *4.5* 19 ASN 19 1.260 1.230 1.505 1.539 1.396 121.67 115.15 121.41 115.28 109.68 112.20 123.33 *5.0* *** +** *5.0* 20 VAL 20 1.302 1.223 1.515 1.571 1.448 122.69 116.58 120.31 109.33 110.36 110.06 123.11 +* * +* 21 PHE 21 1.309 1.238 1.507 1.541 1.438 121.59 116.16 120.73 110.48 107.32 109.74 123.11 * * * * 22 VAL 22 1.296 1.230 1.510 1.554 1.432 121.36 114.93 121.55 111.76 111.69 112.66 123.52 ** * * ** 23 TYR 23 1.308 1.225 1.520 1.532 1.452 122.61 117.18 120.33 111.00 113.25 110.65 122.50 +* +* 24 GLY 24 1.317 1.227 1.504 - 1.448 119.39 116.02 120.56 - 112.72 - 123.36 25 SER 25 1.318 1.236 1.532 1.511 1.459 123.23 115.69 121.20 110.31 112.32 107.57 123.10 +* +* 26 PHE 26 1.309 1.216 1.515 1.529 1.438 122.51 115.96 121.02 110.77 110.33 110.13 122.89 * * * 27 GLN 27 1.330 1.228 1.551 1.540 1.463 122.08 114.96 122.25 111.68 109.66 108.85 122.75 * * 28 ASP 28 1.301 1.227 1.516 1.537 1.440 123.85 118.76 119.85 110.36 107.49 109.56 121.37 +* * * * * +* 29 PRO 29 1.329 1.219 1.518 1.514 1.461 121.82 116.56 120.73 109.25 113.19 104.03 122.68 30 ASP 30 1.309 1.226 1.527 1.518 1.446 121.70 117.22 120.51 111.71 111.22 110.46 122.24 * * 31 VAL 31 1.331 1.237 1.536 1.566 1.468 119.89 116.06 120.96 110.97 109.90 114.54 122.97 * +* +* 32 ILE 32 1.343 1.235 1.515 1.565 1.455 122.25 113.69 121.98 110.34 109.20 110.21 124.27 * * 33 ASN 33 1.291 1.227 1.534 1.507 1.440 125.40 115.42 121.61 109.73 110.21 106.11 122.97 +** * ** +** +** 34 VAL 34 1.314 1.233 1.546 1.565 1.451 122.47 117.06 120.70 110.73 111.34 111.30 122.22 * * 35 MET 35 1.336 1.243 1.530 1.548 1.448 121.54 116.42 120.98 113.54 110.30 110.14 122.60 +* +* 36 LEU 36 1.323 1.224 1.529 1.557 1.441 120.26 116.97 119.70 111.64 112.37 115.16 123.29 * +** +** 37 ASP 37 1.340 1.238 1.508 1.547 1.491 123.62 114.24 122.19 107.66 109.17 111.13 123.57 +* * * +* 38 ARG 38 1.310 1.235 1.502 1.524 1.438 122.59 116.32 120.59 109.62 109.97 110.12 123.07 * * * * 39 THR 39 1.302 1.234 1.537 1.546 1.429 121.91 118.00 120.22 109.40 110.13 110.43 121.69 +* +* +* 40 PRO 40 1.338 1.227 1.526 1.531 1.461 122.90 116.54 120.33 109.45 110.67 104.01 123.12 Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 GLU 41 1.311 1.227 1.533 1.529 1.454 122.30 117.22 120.41 110.77 108.65 110.09 122.37 * * 42 ILE 42 1.304 1.231 1.527 1.579 1.454 120.69 115.87 121.02 108.04 111.01 112.57 123.09 +* * +* 43 VAL 43 1.298 1.236 1.539 1.561 1.442 122.15 117.16 120.20 110.45 109.82 112.03 122.60 ** ** 44 SER 44 1.312 1.243 1.538 1.522 1.445 121.78 116.56 120.76 110.33 109.17 109.18 122.67 * * 45 ALA 45 1.308 1.230 1.505 1.509 1.437 121.81 115.22 121.41 110.17 111.09 110.50 123.36 +* * +* 46 THR 46 1.285 1.219 1.509 1.537 1.427 122.60 116.58 120.03 108.87 109.67 110.28 123.37 *** +* *** 47 LEU 47 1.301 1.231 1.530 1.538 1.428 122.44 117.89 120.42 111.01 109.22 109.99 121.60 +* +* +* 48 PRO 48 1.336 1.240 1.522 1.527 1.443 122.16 116.10 120.88 111.05 111.32 103.51 122.99 +* +* 49 GLY 49 1.306 1.228 1.508 - 1.432 120.56 116.61 120.55 - 111.95 - 122.84 +* * +* 50 PHE 50 1.323 1.224 1.508 1.541 1.457 122.68 116.80 120.07 110.60 110.02 111.79 123.12 51 GLN 51 1.312 1.235 1.519 1.532 1.444 121.72 115.82 120.33 109.36 110.87 109.76 123.83 * * 52 ARG 52 1.330 1.245 1.513 1.558 1.441 122.32 115.77 121.12 109.50 109.04 113.95 123.10 * ** ** 53 PHE 53 1.281 1.224 1.490 1.533 1.442 121.92 118.23 119.61 109.71 107.41 110.34 122.16 *** +* * * *** 54 ARG 54 1.308 1.237 1.520 1.568 1.420 117.79 114.41 121.79 113.60 111.44 113.08 123.79 * +* +* ** +* +* ** 55 LEU 55 1.299 1.245 1.518 1.542 1.446 124.16 113.12 122.14 110.61 105.25 108.88 124.72 ** * +* ** * ** 56 LYS 56 1.329 1.236 1.525 1.528 1.450 125.19 114.73 121.65 111.36 112.48 109.56 123.62 +* +* 57 GLY 57 1.304 1.237 1.501 - 1.429 122.05 115.69 121.09 - 109.74 - 123.21 +* * +* 58 ARG 58 1.314 1.228 1.513 1.568 1.442 121.33 116.06 120.89 112.24 108.80 111.07 123.04 * +* * +* 59 LEU 59 1.306 1.228 1.519 1.553 1.433 121.70 116.81 120.69 113.13 108.77 111.81 122.47 +* * * +* +* 60 TYR 60 1.279 1.235 1.523 1.536 1.438 121.96 119.26 119.28 111.14 108.99 108.23 121.39 +*** * +* * * +*** 61 PRO 61 1.352 1.236 1.525 1.544 1.451 121.54 115.14 121.30 111.19 109.98 104.80 123.47 * +* * +* 62 CYS 62 1.304 1.242 1.531 1.535 1.431 122.55 115.46 121.07 112.03 111.22 109.54 123.46 +* * * +* 63 ILE 63 1.320 1.212 1.514 1.570 1.454 123.00 117.02 119.76 107.66 109.48 110.49 123.19 * * 64 VAL 64 1.306 1.240 1.519 1.574 1.468 123.13 118.49 119.34 108.67 107.94 114.04 122.13 +* * * * * +* 65 PRO 65 1.343 1.233 1.534 1.537 1.460 122.32 115.64 121.37 110.80 112.53 104.39 122.99 * * 66 SER 66 1.299 1.221 1.508 1.529 1.432 123.25 116.68 120.40 110.98 107.48 110.10 122.92 ** * * ** 67 GLU 67 1.295 1.236 1.538 1.524 1.445 121.79 116.72 120.74 110.96 112.30 109.57 122.54 ** ** 68 LYS 68 1.327 1.232 1.536 1.533 1.461 121.22 117.34 120.44 108.92 111.74 110.42 122.20 69 GLY 69 1.317 1.242 1.518 - 1.456 119.59 115.73 120.82 - 114.01 - 123.44 Residue-by-residue listing for refined_13 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 ----------------------------------------------------------------------------------------------------------------------------------- 70 GLU 70 1.322 1.236 1.524 1.552 1.444 123.37 116.60 120.75 110.92 108.71 112.24 122.64 * * * 71 VAL 71 1.300 1.216 1.503 1.561 1.445 121.75 116.66 120.73 108.89 109.79 111.99 122.59 ** * ** 72 HIS 72 1.295 1.225 1.487 1.538 1.444 120.72 115.81 120.47 111.04 107.30 112.34 123.68 ** +* * * ** 73 GLY 73 1.289 1.239 1.485 - 1.417 120.75 116.40 120.63 - 110.92 - 122.96 +** +* ** +** 74 LYS 74 1.287 1.232 1.502 1.538 1.438 121.77 114.35 121.56 109.81 111.95 111.24 124.07 *** * * *** 75 VAL 75 1.291 1.228 1.525 1.546 1.435 123.32 115.42 120.72 109.22 111.29 111.07 123.86 +** * +** 76 LEU 76 1.314 1.225 1.522 1.538 1.444 123.71 117.14 120.08 108.80 108.38 109.94 122.70 * * * * 77 MET 77 1.312 1.223 1.509 1.498 1.429 122.68 116.31 121.01 108.50 111.06 108.72 122.65 * +* +* * +* 78 GLY 78 1.291 1.233 1.501 - 1.443 120.43 115.29 121.15 - 111.62 - 123.57 +** +** 79 VAL 79 1.303 1.231 1.509 1.550 1.438 122.71 116.95 120.35 109.23 109.65 110.70 122.70 +* * +* 80 THR 80 1.294 1.241 1.530 1.547 1.431 120.78 118.02 120.14 110.70 108.78 110.97 121.83 ** * ** 81 SER 81 1.312 1.238 1.537 1.533 1.447 119.98 115.69 120.98 112.81 110.29 110.56 123.28 * * * 82 ASP 82 1.332 1.217 1.508 1.531 1.459 122.22 115.69 120.76 109.17 110.11 111.06 123.53 83 GLU 83 1.320 1.227 1.544 1.531 1.455 123.23 116.69 120.54 112.25 110.16 108.27 122.75 * * * 84 LEU 84 1.336 1.234 1.534 1.540 1.470 122.60 115.91 121.06 108.94 110.39 110.46 123.02 85 GLU 85 1.324 1.226 1.523 1.525 1.455 122.28 115.77 121.00 111.25 111.32 110.96 123.23 86 ASN 86 1.314 1.219 1.525 1.537 1.455 123.28 115.36 121.47 109.61 108.89 109.16 123.16 * * 87 LEU 87 1.319 1.227 1.515 1.534 1.457 122.78 115.67 120.76 110.00 109.92 110.59 123.56 88 ASP 88 1.329 1.212 1.523 1.534 1.469 122.50 115.99 121.14 110.84 110.70 110.40 122.85 89 ALA 89 1.308 1.234 1.539 1.521 1.447 122.33 115.91 120.90 110.41 110.89 109.45 123.20 +* +* 90 VAL 90 1.322 1.237 1.556 1.574 1.467 123.13 116.63 121.05 110.64 112.29 109.86 122.31 * * * 91 GLU 91 1.317 1.233 1.532 1.529 1.470 122.46 115.53 121.02 110.55 111.85 109.85 123.44 92 GLY 92 1.322 1.222 1.519 - 1.465 123.24 117.75 119.99 - 115.52 - 122.25 +* * +* 93 ASN 93 1.318 1.234 1.525 1.530 1.468 120.90 116.42 120.84 108.96 111.37 111.64 122.74 94 GLU 94 1.320 1.229 1.533 1.536 1.459 121.11 117.02 120.39 109.03 111.70 110.21 122.59 95 TYR 95 1.324 1.224 1.512 1.533 1.465 121.70 116.11 120.60 108.11 110.90 110.56 123.29 * * 96 GLU 96 1.315 1.242 1.521 1.541 1.440 121.65 115.48 120.92 110.37 109.07 111.19 123.60 97 ARG 97 1.313 1.243 1.510 1.532 1.439 122.49 116.31 120.68 108.85 108.81 110.01 123.00 * * 98 VAL 98 1.295 1.233 1.503 1.540 1.438 121.45 116.32 120.39 110.25 110.77 112.73 123.28 ** * * ** 99 THR 99 1.298 1.242 1.523 1.565 1.436 121.55 115.91 121.14 111.95 109.64 112.61 122.92 ** * * ** 100 VAL 100 1.304 1.239 1.514 1.555 1.436 122.56 115.68 120.93 108.65 110.79 111.38 123.39 +* * +* 101 GLY 101 1.300 1.230 1.500 - 1.421 121.04 116.17 120.50 - 111.50 - 123.33 ** +* ** Residue-by-residue listing for refined_13 Page 11 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 102 ILE 102 1.306 1.212 1.505 1.582 1.445 122.29 117.15 120.24 111.95 109.70 113.08 122.59 +* +* * +* 103 VAL 103 1.286 1.234 1.501 1.556 1.436 121.37 116.42 120.14 110.13 108.50 111.52 123.41 *** * * *** 104 ARG 104 1.314 1.230 1.502 1.526 1.449 121.67 116.50 120.30 109.02 110.16 111.52 123.19 * * * 105 GLU 105 1.320 1.235 1.525 1.529 1.449 120.96 115.79 120.79 111.67 111.61 111.86 123.41 106 ASP 106 1.330 1.233 1.503 1.544 1.470 122.52 114.13 122.10 105.63 108.10 111.82 123.76 * * ** * ** 107 ASN 107 1.309 1.232 1.531 1.562 1.426 122.57 117.84 119.68 114.13 111.84 111.27 122.42 * +* +* ** ** 108 SER 108 1.320 1.234 1.525 1.543 1.456 121.63 116.91 120.59 110.39 111.78 110.00 122.47 109 GLU 109 1.321 1.250 1.506 1.522 1.439 120.29 115.36 121.11 110.55 111.14 111.73 123.53 110 LYS 110 1.295 1.233 1.520 1.532 1.428 121.20 114.62 121.87 111.97 110.50 111.62 123.50 ** +* ** 111 MET 111 1.275 1.227 1.473 1.507 1.434 124.95 115.19 120.94 108.89 110.93 110.57 123.86 +*** ** * * +* +*** 112 ALA 112 1.274 1.232 1.499 1.512 1.446 121.49 116.37 120.37 110.78 109.10 111.62 123.25 +*** * +*** 113 VAL 113 1.298 1.224 1.504 1.562 1.445 121.81 116.47 120.63 107.26 109.72 111.79 122.90 ** ** 114 LYS 114 1.297 1.227 1.505 1.548 1.435 120.49 116.48 120.54 110.24 109.43 114.33 122.95 ** * ** ** 115 THR 115 1.289 1.247 1.517 1.562 1.424 121.61 116.41 120.27 110.50 107.77 112.72 123.32 +** +* * +** 116 TYR 116 1.297 1.231 1.506 1.532 1.426 122.00 115.53 121.07 111.92 109.56 110.02 123.38 ** +* ** 117 MET 117 1.307 1.247 1.503 1.551 1.441 121.78 115.09 120.70 110.45 110.20 113.65 124.18 +* * * +* +* 118 TRP 118 1.303 1.240 1.505 1.529 1.430 123.51 117.18 119.94 110.25 106.20 107.87 122.85 +* * * +* +* +* 119 ILE 119 1.312 1.259 1.532 1.583 1.468 118.91 115.60 121.14 110.51 110.53 114.97 123.21 * * +* +* ** ** 120 ASN 120 1.318 1.217 1.521 1.533 1.443 121.53 115.25 121.78 112.13 109.31 111.25 122.96 * * 121 LYS 121 1.295 1.240 1.519 1.517 1.451 123.29 115.68 121.09 112.39 111.56 108.39 123.23 ** * * ** 122 ALA 122 1.309 1.235 1.510 1.525 1.428 122.18 115.08 121.63 111.91 108.78 112.31 123.13 * +* * +* 123 ASP 123 1.306 1.238 1.515 1.530 1.446 122.19 117.94 119.91 110.23 108.98 110.18 122.14 +* +* 124 PRO 124 1.337 1.235 1.538 1.524 1.454 122.77 117.78 120.16 110.74 114.20 103.15 122.05 125 ASP 125 1.319 1.237 1.491 1.534 1.455 120.23 117.09 120.35 110.04 110.96 113.80 122.56 +* +* +* 126 MET 126 1.326 1.241 1.526 1.540 1.437 119.27 115.35 122.04 111.28 110.44 112.72 122.49 * * * * 127 PHE 127 1.284 1.235 1.484 1.537 1.422 122.07 116.72 120.09 110.49 106.40 111.88 123.17 *** +* +* +* *** 128 GLY 128 1.280 1.232 1.469 - 1.401 119.53 114.94 121.31 - 109.67 - 123.75 +*** +** *** +*** 129 GLU 129 1.278 1.221 1.505 1.543 1.413 122.55 117.81 119.66 110.78 106.34 110.62 122.52 +*** ** +* +*** 130 TRP 130 1.296 1.216 1.534 1.519 1.452 120.37 116.40 119.99 112.01 109.85 109.19 123.59 ** * ** Residue-by-residue listing for refined_13 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 1.344 1.231 1.532 1.542 1.507 124.81 117.83 120.28 109.70 116.14 112.52 121.88 * +** +* +* * +** 132 PHE 132 1.297 1.240 1.543 1.512 1.399 122.19 115.61 121.07 112.43 109.49 107.63 123.29 ** *** * +* *** 133 GLU 133 1.331 1.233 1.499 1.538 1.456 122.67 113.90 121.70 112.49 110.44 111.51 124.40 * * * * 134 GLU 134 1.303 1.219 1.513 1.526 1.437 123.57 117.51 119.95 110.98 109.70 109.25 122.45 +* * * +* 135 TRP 135 1.322 1.225 1.532 1.541 1.447 119.43 116.85 120.35 111.58 111.13 113.26 122.76 * +* +* 136 LYS 136 1.328 1.235 1.538 1.540 1.459 121.24 116.33 120.86 109.98 109.85 111.24 122.79 137 ARG 137 1.323 1.220 1.515 1.517 1.453 121.32 117.39 120.10 111.75 113.05 112.52 122.50 * * 138 LEU 138 1.320 1.234 1.517 1.529 1.461 120.92 115.94 121.07 110.43 110.25 111.46 122.99 139 HIS 139 1.314 1.232 1.531 1.539 1.449 121.56 115.71 120.97 110.80 108.96 110.20 123.31 * * 140 LYS 140 1.332 1.225 1.528 1.545 1.457 122.65 115.84 120.87 110.22 110.62 110.67 123.27 141 LYS 141 1.327 1.220 1.531 1.542 1.462 123.81 116.83 120.03 111.05 112.22 110.24 123.10 * * 142 LYS 142 1.329 1.237 1.543 1.534 1.464 121.92 115.92 121.19 111.00 110.35 109.80 122.87 143 PHE 143 1.326 1.239 1.523 1.537 1.459 122.43 114.73 121.65 107.01 108.63 111.09 123.62 +* +* 144 ILE 144 1.329 1.213 1.526 1.563 1.459 123.40 117.39 119.91 110.46 111.58 112.03 122.68 145 GLU 145 1.330 1.233 1.541 1.530 1.471 121.95 116.10 121.23 110.64 111.38 111.07 122.67 146 THR 146 1.311 1.246 1.535 1.550 1.436 122.22 115.54 121.35 108.95 110.89 109.85 123.07 * * * 147 PHE 147 1.316 1.222 1.529 1.518 1.439 121.24 116.71 120.34 111.29 113.68 111.26 122.95 * * 148 LYS 148 1.316 1.227 1.524 1.536 1.464 122.84 115.98 121.03 110.54 110.74 109.67 122.93 149 LYS 149 1.321 1.225 1.526 1.526 1.445 121.48 115.52 121.21 111.05 109.83 110.26 123.23 150 ILE 150 1.319 1.233 1.531 1.555 1.454 122.73 115.79 121.14 109.85 109.56 110.74 123.05 151 MET 151 1.321 1.235 1.534 1.531 1.435 122.99 116.07 121.13 111.20 110.14 109.45 122.79 * * 152 GLU 152 1.321 1.228 1.533 1.528 1.458 122.06 115.99 120.95 110.79 110.50 110.33 123.05 153 CYS 153 1.323 1.228 1.538 1.537 1.457 122.58 116.17 120.92 110.82 110.62 109.83 122.91 154 LYS 154 1.332 1.236 1.508 1.514 1.467 122.66 115.05 121.43 110.14 111.23 111.36 123.49 155 LYS 155 1.306 1.231 1.527 1.527 1.439 123.13 113.68 122.28 112.03 110.62 110.72 123.74 +* * * * +* 156 LYS 156 1.287 1.245 1.516 1.543 1.446 125.72 119.42 118.82 108.49 106.64 110.26 121.75 *** ** +* * +* *** 157 PRO 157 1.352 1.233 1.537 1.537 1.457 121.86 115.27 121.69 111.03 111.72 104.69 122.84 * +* +* 158 GLN 158 1.311 1.236 1.523 1.568 1.462 123.12 114.50 121.95 113.43 110.86 110.66 123.45 * +* +* +* 159 GLY 159 1.304 1.231 1.491 - 1.441 122.55 114.41 121.92 - 108.50 - 123.67 +* * * * +* 160 GLN 160 1.302 1.232 1.521 1.536 1.431 122.87 116.66 120.05 110.85 107.97 110.55 123.24 +* * * +* 161 GLY 161 1.302 1.227 1.495 - 1.450 121.19 115.10 121.38 - 110.12 - 123.52 +* * +* 162 ASN 162 1.308 1.232 1.519 1.543 1.454 122.86 115.28 121.53 110.78 110.26 109.45 123.08 +* +* 163 ASP 163 1.315 1.232 1.529 1.532 1.469 122.55 116.90 120.60 109.26 111.79 110.59 122.49 164 ASP 164 1.319 1.237 1.507 1.524 1.452 120.66 116.44 120.65 109.51 109.21 112.17 122.90 Residue-by-residue listing for refined_13 Page 13 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 165 ILE 165 1.299 1.230 1.547 1.571 1.442 121.09 116.47 121.55 111.98 110.23 110.20 121.97 ** * * * ** 166 SER 166 1.317 1.244 1.529 1.541 1.442 120.35 115.68 120.57 112.55 110.72 111.66 123.75 * * 167 HIS 167 1.353 1.228 1.528 1.541 1.479 124.61 115.52 119.74 111.63 112.21 110.93 124.73 +* * +* * +* 168 VAL 168 1.338 1.234 1.543 1.572 1.485 127.00 115.75 121.82 111.28 114.74 114.27 122.41 * * +** * +* +** 169 LEU 169 1.309 1.232 1.514 1.540 1.444 121.99 117.30 120.14 110.65 107.12 110.05 122.55 * * * 170 ARG 170 1.308 1.235 1.513 1.525 1.443 120.65 114.48 121.75 111.61 113.50 112.68 123.71 +* * +* 171 GLU 171 1.305 1.238 1.508 1.531 1.429 123.62 116.15 120.69 109.55 106.06 111.75 123.05 +* +* * +* +* 172 ASP 172 1.302 1.238 1.488 1.540 1.439 121.06 114.22 121.67 110.25 112.05 113.22 124.10 +* +* * +* +* 173 GLN 173 1.285 - 1.509 1.563 1.422 123.93 - - 112.85 105.55 110.11 - *** +* +* * * ** *** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.0* * +** +* *** +** +* * +** ** +** * *5.0* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_13 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 1.260 1.353 1.309 .016 *5.0* +* * C-N (Pro) 1.341 .016 7 1.329 1.352 1.341 .008 C-O C-O 1.231 .020 172 1.212 1.259 1.232 .008 * CA-C CH1E-C (except Gly) 1.525 .021 161 1.470 1.556 1.519 .015 +** * CH2G*-C (Gly) 1.516 .018 12 1.469 1.519 1.499 .013 +** CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.509 1.525 1.517 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.537 1.583 1.561 .012 +* CH1E-CH2E (the rest) 1.530 .020 128 1.498 1.568 1.535 .012 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.396 1.507 1.445 .016 *** +** NH1-CH2G* (Gly) 1.451 .016 12 1.401 1.465 1.439 .018 *** N-CH1E (Pro) 1.466 .015 7 1.443 1.461 1.455 .006 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_13 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 2.0 153 113.12 119.42 116.14 1.08 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.41 117.75 115.92 .89 CH1E-C-N (Pro) 116.9 1.5 7 115.14 117.78 116.15 .85 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.37 124.73 123.04 .58 * * O-C-N (Pro) 122.0 1.4 7 122.05 123.47 122.88 .41 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 117.79 127.00 122.14 1.30 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.39 123.24 120.94 1.20 +* C-N-CH1E (Pro) 122.6 5.0 7 121.54 122.90 122.20 .47 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.82 122.28 120.81 .66 * CH2G*-C-O (Gly) 120.8 2.1 12 119.99 121.92 120.84 .52 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.17 111.91 110.82 .67 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.26 111.98 109.95 1.26 * CH2E-CH1E-C (the rest) 110.1 1.9 128 105.63 115.28 110.71 1.42 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 105.25 116.14 110.05 1.80 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 108.50 115.52 111.44 1.87 * * N-CH1E-C (Pro) 111.8 2.5 7 109.98 114.20 111.94 1.36 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.45 112.31 110.97 1.09 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.85 114.97 111.76 1.44 ** N-CH1E-CH2E (Pro) 103.0 1.1 7 103.15 104.80 104.08 .56 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.11 115.16 110.80 1.47 +** +** ------------------------------------------------------------------------------------------------------------- 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_13 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] 19 12.4% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3% Residues in disallowed regions [XX] 3 2.0% ---- ------ 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 84.3 83.8 10.0 .1 Inside b. Omega angle st dev 172 3.9 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 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 105 .9 .8 .2 .6 Inside f. Overall G-factor 173 .0 -.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 29 7.4 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 56 7.7 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 65 6.2 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 150 8.2 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 40 7.8 20.4 5.0 -2.5 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 .94 3 Residue-by-residue listing for refined_13 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.53 Chi1-chi2 distribution -.18 Chi1 only .11 Chi3 & chi4 .38 Omega -.09 ------ -.17 ===== Main-chain covalent forces:- Main-chain bond lengths -.09 Main-chain bond angles .40 ------ .19 ===== OVERALL AVERAGE -.05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.