Residue-by-residue listing for refined_20 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLY 1 - - - - - - - - - - - 181.2 - - - 2 HIS 2 XX - - -67.5 - - - - - - - 185.1 - 30.3 - **** * **** 3 HIS 3 b 56.7 - - - - - - - - - 173.6 - 31.5 - * * 4 HIS 4 b - - -71.8 - - - - - - - 172.6 - 34.5 - * * 5 HIS 5 b 60.3 - - - - - - - - - 180.2 - 31.8 - 6 HIS 6 b - 184.9 - - - - - - - - 184.1 - 33.7 - 7 HIS 7 B 66.9 - - - - - - - - - 172.7 - 32.1 - * * 8 LEU 8 B 57.3 - - - - - - - - - 182.6 -1.0 27.7 - * +* +* 9 GLU 9 A 52.0 - - 184.3 - - - - - - 172.8 -.9 33.3 - * +* +* 10 CYS 10 S B - 184.0 - - - - - - - - 185.5 - 34.6 - 11 SER 11 b - - -55.5 - - - - - - - 174.3 -.8 34.1 - +* +* 12 SER 12 t A - - -55.1 - - - - - - - 177.0 -.6 35.2 - +* +* 13 ASP 13 T XX - 178.9 - - - - - - - - 183.6 - 30.5 - **** **** 14 SER 14 T A - 185.2 - - - - - - - - 183.8 -1.4 34.2 - 15 LEU 15 t B - - -68.8 - - - - - - - 177.1 -2.6 34.1 - 16 GLN 16 S p - - -61.1 - - - - - - - 175.8 - 33.8 - 17 LEU 17 S B - - -60.9 - - - - - - - 188.1 - 34.0 - * * Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 18 HIS 18 E B - - -52.3 - - - - - - - 182.8 -3.0 35.7 - * * 19 ASN 19 E B - - -49.5 - - - - - - - 183.6 - 36.2 - * * 20 VAL 20 E B - 179.9 - - - - - - - - 177.9 -2.8 34.7 - * * 21 PHE 21 E B - 176.1 - - - - - - - - 183.9 -2.8 34.5 - * * 22 VAL 22 E B - - -56.3 - - - - - - - 183.8 -3.0 33.3 - * * 23 TYR 23 a 59.6 - - - - - - - - - 178.8 - 31.4 - 24 GLY 24 t - - - - - - - - - - - 181.8 - - - 25 SER 25 T A 50.9 - - - - - - - - - 184.1 - 36.2 - 26 PHE 26 T a - - -53.4 - - - - - - - 184.1 - 36.0 - 27 GLN 27 t A 59.6 - - 171.9 - - - - - - 183.6 -1.4 33.1 - 28 ASP 28 h B - 173.3 - - - - - - - - 181.1 - 35.1 - 29 PRO 29 H - - - - - -62.3 -62.3 -29.5 - - - 179.1 - 37.5 - * * 30 ASP 30 H A - 171.7 - - - -64.9 -42.8 - - - 179.6 - 32.9 - 31 VAL 31 H A 70.3 - - - - -68.1 -28.7 - - - 179.8 - 31.5 - 32 ILE 32 H A - - -59.0 - - -64.8 -44.0 - - - 176.7 -1.3 33.7 - 33 ASN 33 H A - - -74.6 - - -58.7 -35.6 - - - 181.9 -1.9 34.2 - 34 VAL 34 H A - 181.4 - - - -82.1 -47.4 - - - 184.9 -1.2 32.6 - * * * 35 MET 35 H A - 201.9 - - - -62.8 -36.3 - - - 174.1 -3.5 33.8 - * * ** ** 36 LEU 36 h a 50.4 - - 162.5 - - - - - - 185.0 -2.3 28.7 - * * 37 ASP 37 t ~b - 179.0 - - - - - - - - 185.4 -.9 35.5 - ** * ** 38 ARG 38 B - - -55.2 178.0 - - - - - - 170.7 - 37.8 - +* * +* 39 THR 39 B - - -48.0 - - - - - - - 174.6 - 35.4 - * * 40 PRO 40 - - - - - -61.7 - - - - - 180.6 - 39.0 - * * 41 GLU 41 E B - 180.1 - 176.7 - - - - - - 187.2 -1.1 32.8 - * * * 42 ILE 42 E B - - -48.4 178.2 - - - - - - 178.1 - 35.7 - * * 43 VAL 43 E B 64.4 - - - - - - - - - 176.2 -1.7 34.0 - 44 SER 44 E B - - -56.0 - - - - - - - 182.3 - 36.2 - 45 ALA 45 E B - - - - - - - - - - 180.0 -3.0 34.4 - * * 46 THR 46 E B - - -61.8 - - - - - - - 177.0 -2.4 35.4 - 47 LEU 47 E B - 175.1 - - - - - - - - 180.9 -3.4 34.7 - +* +* 48 PRO 48 E - - - - - -81.7 - - - - - 178.6 - 38.4 - * * * 49 GLY 49 E - - - - - - - - - - - 182.1 -3.0 - - * * 50 PHE 50 E B - - -67.1 - - - - - - - 181.3 -.8 34.0 - +* +* 51 GLN 51 E B - 184.5 - - - - - - - - 180.1 -2.5 33.6 - 52 ARG 52 E B - 174.4 - - - - - - - - 178.3 - 36.2 - 53 PHE 53 E B - - -61.4 - - - - - - - 178.4 -1.6 34.8 - 54 ARG 54 B 57.2 - - - - - - - - - 174.9 -1.3 31.8 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 LEU 55 b - 188.7 - 165.1 - - - - - - 185.3 - 32.6 - 56 LYS 56 B - - -56.7 185.6 - - - - - - 181.0 - 33.3 - 57 GLY 57 S - - - - - - - - - - - 179.3 -.7 - - +* +* 58 ARG 58 S A 65.1 - - - - - - - - - 183.4 - 32.9 - 59 LEU 59 S B - 182.7 - - - - - - - - 189.9 - 32.0 - +* +* 60 TYR 60 B - - -49.0 - - - - - - - 173.1 - 37.8 - * * * * 61 PRO 61 - - - - - -55.7 - - - - - 185.6 - 39.1 - * * 62 CYS 62 E B 52.4 - - - - - - - - - 178.4 -.8 33.6 - +* +* 63 ILE 63 E B - - -62.7 - - - - - - - 174.1 - 35.9 - * * 64 VAL 64 E B - - -63.2 - - - - - - - 178.0 -1.3 34.4 - 65 PRO 65 E - - - - - -62.4 - - - - - 178.8 - 37.8 - * * 66 SER 66 E B - 184.7 - - - - - - - - 178.7 -1.8 34.8 - 67 GLU 67 E A - 181.9 - 181.7 - - - - - - 177.3 - 33.5 - 68 LYS 68 E b - - -57.7 - - - - - - - 176.4 - 32.4 - 69 GLY 69 E - - - - - - - - - - - 175.0 - - - 70 GLU 70 E B 75.0 - - - - - - - - - 184.5 - 31.7 - 71 VAL 71 E B - 182.3 - - - - - - - - 178.8 -2.6 35.6 - 72 HIS 72 E B - - -58.2 - - - - - - - 182.7 -.5 34.4 - ** ** 73 GLY 73 E - - - - - - - - - - - 182.7 -3.4 - - +* +* 74 LYS 74 E B - - -83.0 - - - - - - - 176.7 -.5 32.8 - * ** ** 75 VAL 75 E B - 165.0 - - - - - - - - 172.6 -2.7 34.3 - * * * 76 LEU 76 E B - - -61.6 181.0 - - - - - - 179.5 -3.2 35.9 - +* +* 77 MET 77 E B 55.8 - - 180.7 - - - - - - 184.7 -2.2 32.5 - 78 GLY 78 E - - - - - - - - - - - 179.1 -1.1 - - * * 79 VAL 79 E B 67.8 - - - - - - - - - 181.6 -1.9 32.5 - 80 THR 80 h B - - -48.2 - - - - - - - 180.4 - 36.2 - * * 81 SER 81 H A - - -59.2 - - -55.5 -37.4 - - - 177.8 - 32.4 - 82 ASP 82 H A - - -67.9 - - -58.9 -51.0 - - - 177.9 - 33.1 - * * 83 GLU 83 H A - - -64.6 - - -67.5 -28.1 - - - 174.8 - 32.9 - * * 84 LEU 84 H A - 180.5 - - - -63.7 -42.8 - - - 176.8 -2.0 34.7 - 85 GLU 85 H A - - -61.1 178.5 - -70.3 -31.9 - - - 175.4 -2.4 34.1 - 86 ASN 86 H A - 173.2 - - - -61.1 -49.5 - - - 178.3 -2.0 36.4 - 87 LEU 87 H A - - -58.0 177.1 - -62.2 -42.5 - - - 179.9 -3.0 35.7 - * * 88 ASP 88 H A - 182.2 - - - -65.1 -38.6 - - - 177.8 -2.1 34.5 - 89 ALA 89 H A - - - - - -66.7 -43.6 - - - 182.2 -2.5 35.0 - 90 VAL 90 H A - 175.2 - - - -72.3 -58.4 - - - 181.7 -2.6 33.7 - +* +* 91 GLU 91 H A - - -62.2 - - -79.8 -42.6 - - - 188.2 -3.0 33.3 - * * * * Residue-by-residue listing for refined_20 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 92 GLY 92 h - - - - - - - - - - - 177.7 -.8 - - +* +* 93 ASN 93 T A - 185.6 - - - - - - - - 183.4 - 35.3 - 94 GLU 94 e a - - -58.6 177.3 - - - - - - 181.5 -2.1 34.2 - 95 TYR 95 E B - - -66.1 - - - - - - - 178.9 -1.5 34.6 - 96 GLU 96 E B 59.0 - - 183.3 - - - - - - 180.1 -2.1 32.8 - 97 ARG 97 E B - 183.0 - 179.4 - - - - - - 183.8 - 35.4 - 98 VAL 98 E B - - -66.8 - - - - - - - 182.0 -3.0 30.9 - * * 99 THR 99 E B 50.8 - - - - - - - - - 180.5 - 36.7 - 100 VAL 100 E B - - -63.8 - - - - - - - 178.2 -2.6 32.8 - 101 GLY 101 E - - - - - - - - - - - 181.7 - - - 102 ILE 102 E B 55.5 - - - - - - - - - 179.1 -3.1 31.6 - * * 103 VAL 103 E B - 179.9 - - - - - - - - 180.0 -2.9 33.4 - * * 104 ARG 104 E B - - -64.3 176.1 - - - - - - 178.8 -2.8 35.7 - * * 105 GLU 105 e A - - -58.9 180.6 - - - - - - 175.9 -2.0 34.2 - 106 ASP 106 T A - 173.6 - - - - - - - - 179.4 -1.1 36.0 - * * 107 ASN 107 T a - 172.4 - - - - - - - - 183.8 - 34.2 - 108 SER 108 T ~l - - -56.6 - - - - - - - 180.4 -2.8 29.6 - ** * ** 109 GLU 109 E B 47.7 - - 178.0 - - - - - - 180.6 -.8 35.4 - * +* +* 110 LYS 110 E B 67.5 - - 177.2 - - - - - - 184.1 - 31.8 - 111 MET 111 E B - 176.1 - 175.7 - - - - - - 180.8 -3.6 36.8 - ** ** 112 ALA 112 E B - - - - - - - - - - 180.0 -3.3 33.8 - +* +* 113 VAL 113 E B - - -58.4 - - - - - - - 174.9 -2.0 34.2 - 114 LYS 114 E B - - -58.9 181.8 - - - - - - 178.2 -1.9 34.2 - 115 THR 115 E B - 192.2 - - - - - - - - 182.5 -2.0 32.8 - 116 TYR 116 E B - - -63.1 - - - - - - - 179.6 - 34.0 - 117 MET 117 E B 64.6 - - 175.3 - - - - - - 181.8 -1.8 32.7 - 118 TRP 118 E B - 188.8 - - - - - - - - 189.2 -2.9 35.7 - +* * +* 119 ILE 119 e A - - -48.6 - - - - - - - 182.9 -.7 35.7 - * +* +* 120 ASN 120 S A - 181.6 - - - - - - - - 176.9 - 33.0 - 121 LYS 121 l 55.6 - - 186.4 - - - - - - 172.8 - 26.3 - * ** ** 122 ALA 122 b - - - - - - - - - - 183.4 - 33.2 - 123 ASP 123 B - 180.4 - - - - - - - - 181.9 - 34.0 - 124 PRO 124 S - - - - - -83.5 - - - - - 178.4 - 38.4 - +* * +* 125 ASP 125 S A - - -72.1 - - - - - - - 179.8 - 32.3 - 126 MET 126 b 50.7 - - - - - - - - - 175.0 - 26.0 - ** ** 127 PHE 127 B 59.6 - - - - - - - - - 181.1 -1.3 31.4 - 128 GLY 128 - - - - - - - - - - - 181.7 - - - 129 GLU 129 B 61.7 - - 177.5 - - - - - - 174.6 - 35.3 - 130 TRP 130 t B - 201.4 - - - - - - - - 182.1 - 34.2 - * * 131 ASN 131 h a - - -60.5 - - - - - - - 175.4 - 33.2 - 132 PHE 132 H A - - -61.0 - - -65.6 -33.0 - - - 179.7 - 34.1 - Residue-by-residue listing for refined_20 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 - - -65.7 - - -63.8 -28.7 - - - 176.9 -3.0 33.7 - * * 134 GLU 134 H A - 180.2 - - - -61.3 -50.2 - - - 178.4 - 35.0 - 135 TRP 135 H A - 177.6 - - - -69.0 -30.9 - - - 177.8 -1.0 32.9 - * * 136 LYS 136 H A - 180.0 - 175.8 - -60.9 -40.9 - - - 177.8 -2.1 33.0 - 137 ARG 137 H A 62.2 - - 179.0 - -74.9 -32.8 - - - 176.2 -2.1 30.4 - 138 LEU 138 H A - - -84.5 - - -68.8 -21.7 - - - 176.5 -1.7 33.4 - * +* +* 139 HIS 139 h A - 180.9 - - - - - - - - 176.1 -1.4 33.2 - 140 LYS 140 H A - 181.3 - 180.9 - -60.1 -39.9 - - - 180.9 -1.4 35.0 - 141 LYS 141 H A - 170.6 - 183.5 - -50.7 -35.1 - - - 184.3 -1.0 35.0 - * * * 142 LYS 142 H A - 193.2 - - - -68.9 -33.8 - - - 174.4 -.8 33.0 - +* +* 143 PHE 143 H A - - -61.9 - - -77.3 -35.6 - - - 180.5 -1.4 34.3 - * * 144 ILE 144 H A - - -54.7 - - -64.1 -33.4 - - - 177.7 -2.4 33.1 - 145 GLU 145 H A - - -69.3 181.5 - -54.4 -30.4 - - - 175.0 -2.3 30.4 - 146 THR 146 H A - - -54.6 - - -64.4 -41.8 - - - 175.6 -1.1 35.0 - * * 147 PHE 147 H A - - -82.5 - - -76.4 -28.7 - - - 175.8 -.8 29.8 - * +* * +* 148 LYS 148 H A - - -79.8 - - -52.9 -44.3 - - - 179.2 -2.5 33.2 - * * 149 LYS 149 H A - - -56.4 177.4 - -57.2 -43.8 - - - 182.4 -1.5 36.3 - 150 ILE 150 H A - - -57.5 175.3 - -66.7 -45.7 - - - 181.1 -.8 33.6 - +* +* 151 MET 151 H A 60.4 - - 182.4 - -74.3 -32.2 - - - 177.6 -2.9 31.1 - * * 152 GLU 152 H A - - -59.4 - - -63.2 -39.4 - - - 179.5 -2.9 34.0 - * * 153 CYS 153 H A - - -59.2 - - -69.2 -31.3 - - - 175.4 -1.6 33.4 - 154 LYS 154 H A - - -62.8 184.3 - -74.1 -21.6 - - - 180.2 -1.1 34.9 - +* * +* 155 LYS 155 h ~l - 184.8 - 177.9 - - - - - - 174.4 -1.2 28.8 - ** * * ** 156 LYS 156 t b - 181.0 - - - - - - - - 183.5 -.6 33.0 - +* +* 157 PRO 157 - - - - - -83.1 - - - - - 178.4 - 38.5 - +* * +* 158 GLN 158 B 53.1 - - - - - - - - - 182.6 - 31.4 - 159 GLY 159 - - - - - - - - - - - 178.7 - - - 160 GLN 160 B - 182.2 - 183.2 - - - - - - 177.7 -1.3 35.6 - 161 GLY 161 - - - - - - - - - - - 183.9 - - - 162 ASN 162 S b - 187.6 - - - - - - - - 178.7 - 32.9 - 163 ASP 163 b - 172.9 - - - - - - - - 179.4 -1.1 34.1 - * * 164 ASP 164 b - 176.3 - - - - - - - - 177.1 - 34.1 - 165 ILE 165 b - 178.7 - 177.5 - - - - - - 185.8 - 31.2 - 166 SER 166 b - 180.2 - - - - - - - - 172.5 - 33.4 - * * 167 HIS 167 B - - -70.5 - - - - - - - 178.5 -1.0 34.0 - * * 168 VAL 168 B - - -65.8 - - - - - - - 180.1 - 31.6 - 169 LEU 169 B - 187.1 - - - - - - - - 181.1 -.9 34.1 - * * Residue-by-residue listing for refined_20 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 170 ARG 170 B - 181.8 - 183.3 - - - - - - 174.8 -.8 33.5 - +* +* 171 GLU 171 B - 198.9 - - - - - - - - 187.8 -1.0 35.3 - * * * 172 ASP 172 b - - -65.0 - - - - - - - 178.5 - 30.4 - 173 GLN 173 - - 179.7 - - - - - - - - - - 34.5 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * +* * +* +* ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.0 181.4 -61.6 178.7 -70.1 -65.6 -37.6 - - - 179.7 -1.9 33.8 Standard deviations: 6.7 7.1 8.1 4.9 12.1 7.2 8.1 - - - 3.7 .9 2.1 Numbers of values: 30 55 65 38 7 40 40 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_20 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 - 1.244 1.494 - 1.461 - 116.35 119.43 - 110.48 - 124.23 * * 2 HIS 2 1.341 1.235 1.524 1.543 1.474 123.64 116.13 121.08 112.71 111.91 112.81 122.77 * * * * 3 HIS 3 1.320 1.240 1.536 1.560 1.453 120.85 115.41 121.44 111.90 113.59 111.59 123.03 * * 4 HIS 4 1.310 1.233 1.518 1.558 1.465 124.74 116.38 119.91 108.72 108.17 112.51 123.66 * * +* * * +* 5 HIS 5 1.326 1.239 1.512 1.562 1.464 124.05 116.60 119.71 111.37 108.73 113.72 123.67 +* * +* +* 6 HIS 6 1.315 1.244 1.513 1.553 1.457 123.49 115.93 120.95 110.23 108.25 112.22 123.08 * * * * * 7 HIS 7 1.299 1.235 1.522 1.567 1.442 120.83 116.50 121.46 111.27 111.63 112.45 121.96 ** +* * ** 8 LEU 8 1.298 1.222 1.514 1.575 1.423 119.34 114.55 122.11 116.53 109.34 114.18 123.06 ** ** +* * *** ** *** 9 GLU 9 1.292 1.228 1.515 1.526 1.435 122.77 115.57 121.47 112.59 110.70 109.51 122.96 +** * * +** 10 CYS 10 1.304 1.235 1.517 1.533 1.425 121.57 116.19 120.31 111.00 106.15 110.70 123.45 +* +* +* +* 11 SER 11 1.310 1.240 1.528 1.520 1.434 122.62 115.56 121.18 110.78 112.57 109.41 123.21 * * * Residue-by-residue listing for refined_20 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 1.325 1.234 1.528 1.526 1.441 122.20 114.26 121.09 110.60 108.56 109.22 124.64 * * 13 ASP 13 1.344 1.235 1.521 1.536 1.470 125.95 116.80 120.15 111.83 114.50 112.26 123.04 * ** * * ** 14 SER 14 1.311 1.228 1.535 1.544 1.434 121.76 116.98 120.62 111.17 111.29 109.60 122.37 * * * 15 LEU 15 1.309 1.237 1.524 1.537 1.440 122.09 115.38 120.29 109.82 112.18 110.64 124.33 * * 16 GLN 16 1.351 1.248 1.530 1.544 1.478 124.42 116.22 120.99 110.65 112.09 110.16 122.75 +* * +* +* 17 LEU 17 1.321 1.231 1.487 1.524 1.424 121.85 115.87 120.98 108.77 107.99 113.38 123.14 +* +* * +* +* 18 HIS 18 1.274 1.245 1.493 1.529 1.420 120.93 115.19 121.03 109.91 109.31 109.48 123.76 +*** +* +* +*** 19 ASN 19 1.292 1.249 1.523 1.533 1.428 122.47 116.79 120.39 109.78 107.40 109.11 122.80 +** +* * +** 20 VAL 20 1.308 1.225 1.531 1.574 1.460 122.12 116.44 120.48 109.55 110.40 110.96 123.08 * * * 21 PHE 21 1.314 1.241 1.517 1.540 1.454 122.48 115.91 120.64 111.12 108.72 109.91 123.45 * * 22 VAL 22 1.309 1.232 1.510 1.548 1.442 122.12 116.20 120.83 110.30 110.77 111.90 122.96 * * 23 TYR 23 1.310 1.228 1.525 1.537 1.435 120.31 117.71 119.82 112.70 113.64 110.88 122.47 * * * * 24 GLY 24 1.322 1.220 1.507 - 1.453 119.58 115.77 121.03 - 112.65 - 123.15 25 SER 25 1.299 1.232 1.531 1.511 1.454 123.86 116.15 121.06 109.82 112.83 107.25 122.79 ** * +* ** 26 PHE 26 1.321 1.215 1.528 1.543 1.442 121.22 117.80 120.11 108.59 111.09 109.62 122.05 27 GLN 27 1.335 1.237 1.526 1.535 1.485 120.38 116.21 120.65 109.30 112.37 112.17 123.13 * * 28 ASP 28 1.297 1.210 1.525 1.520 1.438 122.35 118.62 120.11 110.67 110.68 108.69 121.27 ** * * * * * ** 29 PRO 29 1.341 1.233 1.537 1.522 1.469 122.23 117.10 120.63 110.61 113.46 104.45 122.26 * * 30 ASP 30 1.321 1.237 1.516 1.535 1.464 121.05 116.17 120.68 110.76 110.79 111.79 123.09 31 VAL 31 1.332 1.220 1.524 1.585 1.453 120.78 116.25 120.77 111.04 109.28 114.48 122.96 +* +* +* 32 ILE 32 1.334 1.238 1.540 1.544 1.442 122.21 116.50 120.82 111.06 110.47 110.56 122.64 33 ASN 33 1.327 1.227 1.512 1.532 1.470 121.75 116.18 120.97 108.51 111.22 111.91 122.85 34 VAL 34 1.303 1.224 1.528 1.549 1.444 121.08 116.82 120.30 110.49 112.19 112.08 122.87 +* +* 35 MET 35 1.329 1.234 1.537 1.545 1.458 121.80 116.96 120.77 111.99 109.91 109.65 122.24 36 LEU 36 1.329 1.228 1.517 1.569 1.442 120.19 116.71 119.71 112.46 112.25 115.39 123.50 +* * +** +** 37 ASP 37 1.324 1.221 1.502 1.555 1.481 123.46 114.94 121.57 107.93 108.80 111.66 123.46 * * * * * 38 ARG 38 1.308 1.220 1.489 1.518 1.449 122.19 116.50 120.09 105.40 109.97 110.23 123.41 +* +* ** ** 39 THR 39 1.296 1.239 1.533 1.534 1.431 121.19 118.20 119.95 108.55 108.11 111.20 121.74 ** * * ** 40 PRO 40 1.338 1.233 1.518 1.531 1.464 122.77 116.96 119.68 110.25 109.99 103.48 123.33 41 GLU 41 1.324 1.240 1.521 1.530 1.461 121.40 115.76 120.80 111.19 109.90 111.75 123.43 42 ILE 42 1.301 1.240 1.526 1.548 1.431 121.53 115.98 121.07 108.88 110.53 110.04 122.95 +* * +* Residue-by-residue listing for refined_20 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.301 1.228 1.539 1.559 1.451 122.29 117.19 120.08 109.83 109.96 111.57 122.71 +* +* 44 SER 44 1.317 1.247 1.534 1.523 1.452 121.92 116.61 120.64 109.33 108.55 108.79 122.72 * * 45 ALA 45 1.302 1.223 1.510 1.505 1.436 121.99 115.01 121.52 110.11 111.66 109.95 123.47 +* * +* 46 THR 46 1.284 1.215 1.521 1.534 1.425 123.23 116.16 120.49 109.37 110.53 109.91 123.34 *** +* *** 47 LEU 47 1.299 1.230 1.533 1.535 1.435 123.03 117.94 120.14 110.68 109.91 109.66 121.87 ** * ** 48 PRO 48 1.344 1.247 1.523 1.540 1.452 122.88 115.61 121.19 110.31 112.80 104.00 123.20 49 GLY 49 1.316 1.235 1.506 - 1.436 121.32 116.49 120.58 - 111.89 - 122.93 50 PHE 50 1.322 1.219 1.511 1.549 1.457 123.01 117.54 119.69 110.45 109.08 111.27 122.77 51 GLN 51 1.316 1.235 1.525 1.527 1.452 120.98 114.67 121.26 111.58 110.66 109.92 124.01 52 ARG 52 1.312 1.226 1.515 1.544 1.451 124.44 116.12 120.39 111.00 109.66 107.34 123.48 * +* +* +* 53 PHE 53 1.313 1.239 1.510 1.533 1.451 122.29 116.86 119.99 109.45 109.27 110.92 123.13 * * 54 ARG 54 1.316 1.234 1.505 1.566 1.447 121.87 116.05 119.34 113.10 111.41 111.16 124.59 +* +* +* 55 LEU 55 1.328 1.235 1.517 1.575 1.477 125.55 116.16 120.63 111.72 106.68 112.96 123.20 ** * ** +* * ** 56 LYS 56 1.312 1.237 1.521 1.526 1.453 121.46 115.55 121.07 110.69 112.27 110.76 123.37 * * 57 GLY 57 1.308 1.239 1.505 - 1.429 121.84 116.34 120.76 - 110.58 - 122.88 * * * 58 ARG 58 1.305 1.232 1.518 1.571 1.447 121.20 115.78 121.10 112.02 109.71 111.31 123.12 +* ** * ** 59 LEU 59 1.314 1.241 1.516 1.552 1.433 122.12 115.22 121.18 112.88 109.93 111.57 123.58 * * * * * 60 TYR 60 1.293 1.247 1.513 1.544 1.419 123.25 117.94 119.52 109.06 108.27 107.46 122.50 +** ** * +* +** 61 PRO 61 1.346 1.228 1.519 1.539 1.454 122.53 116.82 120.40 109.79 109.60 104.01 122.76 62 CYS 62 1.302 1.250 1.524 1.534 1.431 120.93 115.15 121.07 112.35 112.30 108.91 123.74 +* * * +* 63 ILE 63 1.322 1.227 1.505 1.571 1.449 123.72 116.69 120.11 108.34 108.45 111.11 123.15 * * * 64 VAL 64 1.298 1.246 1.523 1.574 1.449 122.66 118.19 119.64 108.88 107.45 113.06 122.12 ** * * ** 65 PRO 65 1.337 1.236 1.534 1.532 1.461 122.36 115.80 121.25 110.73 112.82 104.21 122.95 * * 66 SER 66 1.307 1.238 1.510 1.534 1.434 122.47 116.69 120.24 109.79 108.26 110.98 123.06 +* * * +* 67 GLU 67 1.306 1.230 1.529 1.527 1.435 121.65 116.72 120.74 111.81 109.95 110.12 122.52 +* * +* 68 LYS 68 1.327 1.230 1.501 1.568 1.454 120.82 116.33 120.73 108.82 109.70 115.23 122.74 * +* +** +** 69 GLY 69 1.291 1.244 1.482 - 1.420 119.49 115.88 120.48 - 111.54 - 123.62 +** +* +* +** 70 GLU 70 1.293 1.234 1.511 1.559 1.411 122.28 116.76 120.44 112.76 107.73 113.18 122.80 +** * ** * * +* +** 71 VAL 71 1.293 1.219 1.484 1.551 1.437 121.48 115.96 120.92 108.09 109.16 111.61 123.11 +** +* * +** 72 HIS 72 1.283 1.225 1.491 1.535 1.422 120.67 115.99 120.47 111.17 106.84 110.86 123.50 *** +* +* +* *** Residue-by-residue listing for refined_20 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 73 GLY 73 1.287 1.235 1.482 - 1.411 120.99 116.59 120.42 - 110.30 - 122.99 *** +* ** *** 74 LYS 74 1.289 1.224 1.502 1.534 1.435 121.38 114.26 121.69 109.70 112.63 112.46 124.05 +** * * * +** 75 VAL 75 1.286 1.227 1.523 1.554 1.446 123.80 115.44 120.52 109.30 112.05 111.11 124.03 *** * *** 76 LEU 76 1.322 1.237 1.511 1.539 1.445 123.28 117.10 120.25 107.73 107.25 111.55 122.63 * * * 77 MET 77 1.290 1.236 1.505 1.520 1.441 121.04 116.51 120.52 112.17 111.12 110.81 122.96 +** * +** 78 GLY 78 1.315 1.238 1.517 - 1.429 119.57 116.62 120.88 - 111.67 - 122.50 * * 79 VAL 79 1.327 1.242 1.541 1.579 1.451 120.57 116.68 120.63 111.54 109.62 112.34 122.64 * * * 80 THR 80 1.312 1.238 1.556 1.531 1.423 122.89 116.62 120.52 110.45 110.64 107.41 122.85 * * +* ** ** 81 SER 81 1.333 1.227 1.543 1.528 1.457 123.14 117.79 119.55 111.69 113.28 110.48 122.63 82 ASP 82 1.344 1.220 1.510 1.536 1.482 121.04 115.90 120.90 109.28 110.77 112.88 123.18 * * * * 83 GLU 83 1.314 1.203 1.541 1.537 1.448 122.31 117.76 120.36 110.67 110.53 111.91 121.88 * * * 84 LEU 84 1.329 1.232 1.529 1.531 1.470 120.84 115.52 121.29 108.52 109.14 111.82 123.18 85 GLU 85 1.326 1.199 1.517 1.526 1.452 122.58 115.37 121.11 110.88 109.35 110.32 123.50 +* +* 86 ASN 86 1.309 1.224 1.530 1.528 1.461 124.44 115.79 120.84 110.29 109.85 107.28 123.34 * +* +* +* 87 LEU 87 1.320 1.235 1.516 1.541 1.464 123.02 114.67 121.63 108.73 108.85 110.37 123.68 88 ASP 88 1.321 1.205 1.515 1.526 1.449 123.00 116.22 120.91 110.73 110.42 109.69 122.86 * * 89 ALA 89 1.302 1.228 1.524 1.516 1.444 123.00 116.22 120.89 109.94 110.76 109.55 122.88 +* +* 90 VAL 90 1.316 1.238 1.551 1.573 1.455 121.90 116.90 120.53 110.96 111.92 110.35 122.55 * * * 91 GLU 91 1.313 1.230 1.523 1.515 1.468 122.21 115.60 120.88 110.27 113.69 110.43 123.49 * * 92 GLY 92 1.326 1.229 1.519 - 1.474 123.70 116.81 120.48 - 115.65 - 122.69 * +* * +* 93 ASN 93 1.306 1.239 1.547 1.544 1.455 121.76 116.39 121.15 110.39 109.40 109.15 122.42 +* * +* 94 GLU 94 1.332 1.230 1.541 1.538 1.461 121.47 116.12 120.99 111.17 111.49 109.27 122.88 95 TYR 95 1.316 1.220 1.510 1.530 1.464 123.66 117.30 120.04 108.88 109.92 111.44 122.66 * * 96 GLU 96 1.313 1.243 1.500 1.553 1.448 120.83 115.52 120.85 111.07 109.95 112.22 123.58 * * * * * 97 ARG 97 1.313 1.225 1.503 1.540 1.431 121.63 116.19 120.88 110.79 107.33 109.51 122.93 * * * * * 98 VAL 98 1.291 1.243 1.485 1.536 1.429 121.29 114.44 121.33 110.87 113.22 113.63 124.23 +** +* +* * +** 99 THR 99 1.292 1.232 1.506 1.531 1.405 123.50 116.41 120.75 109.57 109.15 108.35 122.82 +** +** * +* +** 100 VAL 100 1.299 1.243 1.524 1.560 1.449 120.51 115.87 121.30 110.00 111.74 112.54 122.83 ** ** 101 GLY 101 1.297 1.213 1.487 - 1.427 121.42 117.02 120.06 - 109.90 - 122.92 ** +* * ** Residue-by-residue listing for refined_20 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 1.299 1.214 1.496 1.573 1.437 121.15 116.39 120.72 112.06 111.18 112.77 122.86 ** * * * * ** 103 VAL 103 1.282 1.222 1.498 1.550 1.418 121.53 115.41 120.94 110.85 108.68 112.20 123.61 *** * ** *** 104 ARG 104 1.300 1.215 1.508 1.530 1.436 122.79 116.97 119.92 109.00 109.76 110.06 123.11 ** * ** 105 GLU 105 1.320 1.229 1.524 1.532 1.471 122.50 113.08 122.24 111.36 108.80 109.78 124.68 +* * +* 106 ASP 106 1.314 1.224 1.542 1.530 1.452 126.41 117.46 120.55 111.44 111.64 106.33 121.99 * +** ** +** 107 ASN 107 1.331 1.222 1.543 1.532 1.440 121.36 115.98 120.82 111.49 111.79 108.87 123.14 108 SER 108 1.325 1.224 1.534 1.539 1.466 124.76 114.35 121.98 113.30 111.81 113.13 123.55 +* +* +* +* 109 GLU 109 1.321 1.232 1.507 1.524 1.439 125.11 118.10 119.38 109.98 108.07 109.85 122.51 +* * +* 110 LYS 110 1.312 1.240 1.521 1.527 1.442 119.23 115.00 121.31 110.94 110.73 113.11 123.69 * * +* +* 111 MET 111 1.284 1.229 1.525 1.514 1.419 124.35 117.31 120.15 111.02 108.85 106.41 122.53 *** ** * ** *** 112 ALA 112 1.305 1.227 1.515 1.517 1.444 121.49 115.88 120.83 110.64 110.98 110.48 123.28 +* +* 113 VAL 113 1.319 1.232 1.518 1.568 1.456 123.03 117.03 120.52 108.14 108.63 113.64 122.41 * * * 114 LYS 114 1.296 1.231 1.519 1.518 1.441 120.81 117.37 119.94 110.37 108.98 110.88 122.68 ** ** 115 THR 115 1.306 1.245 1.523 1.563 1.447 121.31 116.39 120.05 110.59 108.96 113.01 123.55 +* +* 116 TYR 116 1.310 1.230 1.518 1.535 1.439 122.80 115.88 120.94 110.79 110.19 110.54 123.16 * * * 117 MET 117 1.304 1.239 1.526 1.549 1.452 122.11 116.14 120.33 110.73 109.43 112.64 123.51 +* * +* 118 TRP 118 1.318 1.240 1.535 1.532 1.460 123.36 117.20 119.98 111.09 108.86 107.82 122.82 +* +* 119 ILE 119 1.342 1.240 1.524 1.547 1.471 120.52 116.66 120.48 105.71 112.08 112.40 122.82 +* +* 120 ASN 120 1.324 1.224 1.510 1.542 1.463 120.75 114.95 121.08 111.38 109.76 111.53 123.95 121 LYS 121 1.334 1.230 1.548 1.551 1.481 125.94 116.45 121.01 114.75 116.68 113.12 122.52 * * * ** ** +* +* ** 122 ALA 122 1.298 1.225 1.503 1.522 1.428 122.76 115.22 121.35 111.39 107.65 111.90 123.24 ** * +* * * ** 123 ASP 123 1.298 1.240 1.524 1.535 1.451 121.76 117.65 120.33 110.68 110.49 110.44 122.01 ** ** 124 PRO 124 1.337 1.229 1.546 1.524 1.455 122.90 118.26 119.88 110.69 114.72 102.91 121.87 * * 125 ASP 125 1.321 1.222 1.502 1.538 1.467 120.36 117.48 120.49 109.45 111.61 113.62 122.03 * +* +* 126 MET 126 1.312 1.229 1.531 1.559 1.445 119.28 114.95 122.45 115.03 114.47 114.61 122.49 * * * +** * ** +** 127 PHE 127 1.310 1.244 1.519 1.557 1.441 122.41 115.52 121.53 112.23 110.18 112.99 122.91 * * * * * 128 GLY 128 1.294 1.239 1.497 - 1.428 121.33 116.10 120.03 - 110.63 - 123.86 ** * * ** 129 GLU 129 1.308 1.234 1.521 1.537 1.447 122.56 115.67 121.25 108.93 111.14 110.19 123.08 * * Residue-by-residue listing for refined_20 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 1.295 1.227 1.514 1.549 1.434 122.32 117.94 118.61 110.84 104.61 111.98 123.42 ** * * ** ** 131 ASN 131 1.327 1.226 1.560 1.544 1.502 124.86 118.37 119.86 108.84 115.07 111.37 121.76 +* ** +* * * ** 132 PHE 132 1.337 1.234 1.535 1.541 1.465 121.53 115.80 120.87 108.96 109.74 112.09 123.31 133 GLU 133 1.337 1.236 1.519 1.526 1.467 123.12 115.69 121.11 110.50 111.08 110.70 123.20 134 GLU 134 1.321 1.218 1.533 1.533 1.444 122.30 116.32 121.30 110.69 109.02 109.45 122.33 135 TRP 135 1.315 1.233 1.530 1.532 1.449 121.22 115.98 121.16 111.97 110.46 110.60 122.83 136 LYS 136 1.316 1.231 1.541 1.533 1.442 122.11 117.38 120.30 111.81 111.06 110.42 122.31 137 ARG 137 1.333 1.223 1.539 1.536 1.463 120.21 117.06 120.44 112.04 112.14 113.20 122.49 * +* +* 138 LEU 138 1.336 1.225 1.504 1.521 1.487 121.97 115.64 121.21 109.22 111.58 112.08 123.15 * +* +* 139 HIS 139 1.303 1.238 1.546 1.547 1.455 122.13 116.72 120.23 111.91 110.76 110.21 123.02 +* +* 140 LYS 140 1.349 1.230 1.508 1.534 1.467 122.17 115.19 120.73 108.58 109.29 111.38 124.03 * * 141 LYS 141 1.337 1.216 1.517 1.538 1.461 124.06 116.65 120.51 109.35 111.86 109.97 122.80 * * 142 LYS 142 1.314 1.234 1.538 1.531 1.440 121.00 116.16 121.23 112.10 110.55 110.35 122.61 * * * 143 PHE 143 1.317 1.237 1.516 1.522 1.453 121.47 115.20 121.45 109.50 109.38 111.33 123.35 144 ILE 144 1.328 1.202 1.516 1.560 1.452 122.54 117.05 120.01 109.83 110.40 112.91 122.94 * * 145 GLU 145 1.329 1.239 1.530 1.520 1.464 122.33 116.63 120.32 112.08 113.23 112.56 123.04 * * * 146 THR 146 1.325 1.234 1.554 1.547 1.448 121.89 115.46 121.44 110.46 108.86 109.71 123.07 * * * 147 PHE 147 1.327 1.225 1.502 1.522 1.459 123.27 116.55 120.18 112.08 113.02 113.64 123.25 * * +* +* 148 LYS 148 1.324 1.205 1.504 1.530 1.443 122.01 116.44 120.05 110.27 110.81 111.96 123.40 * * * 149 LYS 149 1.327 1.232 1.526 1.526 1.468 122.18 114.57 121.73 107.97 109.29 109.83 123.67 * * 150 ILE 150 1.312 1.242 1.547 1.567 1.436 123.61 116.91 120.52 111.77 111.24 109.96 122.52 * * * * * * * 151 MET 151 1.326 1.229 1.537 1.547 1.471 121.63 117.90 119.85 111.45 112.86 112.61 122.24 * * 152 GLU 152 1.338 1.227 1.525 1.537 1.470 120.69 115.62 121.07 109.01 109.46 112.21 123.28 * * 153 CYS 153 1.327 1.230 1.539 1.521 1.458 122.52 116.69 120.79 111.28 111.42 110.08 122.52 154 LYS 154 1.338 1.226 1.509 1.512 1.474 121.61 113.58 121.56 108.87 109.49 110.93 124.86 * * * 155 LYS 155 1.312 1.243 1.509 1.540 1.440 126.36 113.93 122.18 113.05 112.15 114.56 123.76 * +** * +* ** +** 156 LYS 156 1.298 1.228 1.522 1.548 1.427 123.74 116.50 121.29 112.02 107.43 111.78 122.01 ** +* * * * ** 157 PRO 157 1.334 1.245 1.523 1.545 1.442 122.72 115.64 121.20 110.53 112.69 103.79 123.16 +* +* 158 GLN 158 1.306 1.234 1.516 1.565 1.441 123.01 116.60 120.09 114.00 109.77 111.41 123.28 +* +* ** ** 159 GLY 159 1.316 1.228 1.506 - 1.446 121.15 116.01 120.71 - 112.47 - 123.28 160 GLN 160 1.300 1.243 1.521 1.534 1.436 122.49 116.96 119.72 110.25 108.29 109.31 123.30 ** * * ** 161 GLY 161 1.327 1.244 1.515 - 1.454 121.29 116.64 119.94 - 111.22 - 123.41 Residue-by-residue listing for refined_20 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 1.324 1.242 1.518 1.546 1.460 121.81 114.45 121.67 111.19 110.72 111.51 123.83 163 ASP 163 1.307 1.233 1.505 1.543 1.443 124.32 116.15 120.38 110.35 108.98 111.29 123.41 +* * +* 164 ASP 164 1.306 1.238 1.500 1.540 1.455 122.22 115.64 120.88 109.63 109.93 111.74 123.43 +* * +* 165 ILE 165 1.292 1.234 1.523 1.563 1.431 123.04 114.64 122.06 112.80 109.06 113.19 123.24 +** * +* +** 166 SER 166 1.298 1.237 1.532 1.536 1.433 123.00 115.82 121.19 111.57 112.91 109.59 122.91 ** * ** 167 HIS 167 1.316 1.238 1.492 1.532 1.445 121.56 116.35 120.47 108.42 108.63 113.33 123.18 +* +* +* 168 VAL 168 1.283 1.234 1.527 1.560 1.429 121.35 115.56 121.64 112.43 110.79 112.33 122.73 *** +* +* *** 169 LEU 169 1.311 1.240 1.510 1.565 1.438 121.44 116.19 120.70 112.36 107.48 110.06 123.07 * +* * * * +* 170 ARG 170 1.306 1.241 1.517 1.526 1.433 121.13 115.45 121.01 109.91 111.14 111.76 123.53 +* * +* 171 GLU 171 1.311 1.239 1.547 1.554 1.440 122.27 118.44 119.22 113.16 104.59 107.75 122.33 * * * * +* ** +* ** 172 ASP 172 1.311 1.236 1.520 1.536 1.469 121.15 114.18 121.59 111.45 113.62 113.17 124.22 * * +* +* 173 GLN 173 1.314 - 1.517 1.537 1.444 125.89 - - 109.96 106.58 111.65 - * ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +* +* ** +** +** +* * *** ** +** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 1.274 1.351 1.313 .015 +*** +* * C-N (Pro) 1.341 .016 7 1.334 1.346 1.340 .004 C-O C-O 1.231 .020 172 1.199 1.250 1.232 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 161 1.484 1.560 1.521 .015 +* +* CH2G*-C (Gly) 1.516 .018 12 1.482 1.519 1.501 .013 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.505 1.522 1.515 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.531 1.585 1.556 .015 +* CH1E-CH2E (the rest) 1.530 .020 128 1.511 1.575 1.538 .014 ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.405 1.502 1.449 .016 +** ** NH1-CH2G* (Gly) 1.451 .016 12 1.411 1.474 1.439 .018 ** * N-CH1E (Pro) 1.466 .015 7 1.442 1.469 1.457 .008 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 2.0 153 113.08 118.62 116.20 1.01 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.77 117.02 116.39 .37 CH1E-C-N (Pro) 116.9 1.5 7 115.61 118.26 116.60 .90 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.27 124.86 123.06 .60 * * O-C-N (Pro) 122.0 1.4 7 121.87 123.33 122.79 .50 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.23 126.41 122.27 1.37 * +** C-NH1-CH2G* (Gly) 120.6 1.7 11 119.49 123.70 121.06 1.16 +* C-N-CH1E (Pro) 122.6 5.0 7 122.23 122.90 122.63 .24 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.61 122.45 120.71 .64 * CH2G*-C-O (Gly) 120.8 2.1 12 119.43 121.03 120.40 .44 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.94 111.39 110.52 .57 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 105.71 112.80 110.06 1.48 +* +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.40 116.53 110.74 1.55 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.59 116.68 110.26 1.92 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 109.90 115.65 111.58 1.48 * N-CH1E-C (Pro) 111.8 2.5 7 109.60 114.72 112.30 1.71 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.55 111.90 110.47 .89 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 107.41 114.48 111.60 1.59 ** +* N-CH1E-CH2E (Pro) 103.0 1.1 7 102.91 104.45 103.84 .47 * NH1-CH1E-CH2E (the rest) 110.5 1.7 121 106.33 115.39 111.01 1.76 ** +** ------------------------------------------------------------------------------------------------------------- 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_20 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] 124 81.0% Residues in additional allowed regions [a,b,l,p] 24 15.7% Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0% Residues in disallowed regions [XX] 2 1.3% ---- ------ 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 81.0 83.8 10.0 -.3 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 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 99 .9 .8 .2 .3 Inside f. Overall G-factor 173 -.1 -.4 .3 1.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 30 6.7 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 55 7.1 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 65 8.1 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 150 8.6 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 38 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% 81.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 3 Residue-by-residue listing for refined_20 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.55 Chi1-chi2 distribution -.31 Chi1 only -.06 Chi3 & chi4 .33 Omega -.11 ------ -.22 ===== Main-chain covalent forces:- Main-chain bond lengths .03 Main-chain bond angles .35 ------ .22 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.