Residue-by-residue listing for refined_7 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 - - - - - - - - - - - 178.4 - - - 2 HIS 2 B 64.1 - - - - - - - - - 182.4 - 32.8 - 3 HIS 3 b 65.5 - - - - - - - - - 175.2 - 34.5 - 4 HIS 4 B - - -63.7 - - - - - - - 175.6 - 35.0 - 5 HIS 5 B 61.6 - - - - - - - - - 181.1 - 30.9 - 6 HIS 6 B - 186.5 - - - - - - - - 181.0 -.7 34.3 - +* +* 7 HIS 7 B - - -64.3 - - - - - - - 166.7 - 36.4 - ** ** 8 LEU 8 b - - -66.6 - - - - - - - 188.6 - 32.9 - * * 9 GLU 9 B - 187.4 - 183.3 - - - - - - 177.6 -1.4 33.7 - 10 CYS 10 B - 178.8 - - - - - - - - 177.2 -1.0 35.6 - * * 11 SER 11 B - - -58.9 - - - - - - - 180.3 - 34.0 - 12 SER 12 A - - -55.9 - - - - - - - 176.3 - 34.3 - 13 ASP 13 XX - - -62.4 - - - - - - - 179.9 - 31.8 - **** **** 14 SER 14 S B - 183.4 - - - - - - - - 178.3 -3.2 35.5 - +* +* 15 LEU 15 S b - - -66.9 - - - - - - - 180.8 - 32.3 - 16 GLN 16 a 55.1 - - - - - - - - - 184.0 -2.1 33.4 - 17 LEU 17 B - - -58.5 - - - - - - - 185.4 - 34.0 - 18 HIS 18 E B - - -53.7 - - - - - - - 175.2 -2.8 36.2 - * * 19 ASN 19 E B 51.4 - - - - - - - - - 185.6 - 29.2 - * * 20 VAL 20 E B - 179.2 - - - - - - - - 177.0 -2.3 35.4 - Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 PHE 21 E B - 179.7 - - - - - - - - 181.1 -2.7 34.5 - 22 VAL 22 E B - - -67.3 - - - - - - - 182.8 -3.2 31.6 - +* +* 23 TYR 23 A 56.2 - - - - - - - - - 182.2 -.5 32.9 - ** ** 24 GLY 24 t - - - - - - - - - - - 180.4 - - - 25 SER 25 T A 51.5 - - - - - - - - - 183.2 - 35.2 - 26 PHE 26 T a - - -67.3 - - - - - - - 178.1 - 33.7 - 27 GLN 27 t A 66.9 - - 177.1 - - - - - - 183.9 -.7 34.3 - +* +* 28 ASP 28 h B - 175.4 - - - - - - - - 182.6 - 36.2 - 29 PRO 29 H - - - - - -71.0 -71.0 -28.9 - - - 181.9 - 38.3 - * * 30 ASP 30 H A - 178.8 - - - -62.3 -44.7 - - - 178.9 - 33.4 - 31 VAL 31 H A 63.8 - - - - -70.9 -29.3 - - - 178.7 - 31.8 - 32 ILE 32 H A - - -63.2 - - -65.9 -41.6 - - - 178.2 -1.1 33.4 - * * 33 ASN 33 H A - - -75.2 - - -53.8 -46.2 - - - 186.2 -2.4 35.6 - * * 34 VAL 34 H A 64.0 - - - - -82.8 -36.0 - - - 185.6 -1.3 31.3 - * * 35 MET 35 H A - 194.7 - - - -68.0 -36.5 - - - 175.3 -2.8 33.2 - 36 LEU 36 h a 53.6 - - 166.7 - - - - - - 183.1 -1.8 29.0 - * * 37 ASP 37 t ~b - 179.6 - - - - - - - - 181.8 -.8 34.8 - ** +* ** 38 ARG 38 S B - - -65.3 - - - - - - - 181.1 - 34.3 - 39 THR 39 B - - -54.3 - - - - - - - 174.2 - 34.4 - * * 40 PRO 40 - - - - - -60.7 - - - - - 180.4 - 39.2 - +* +* 41 GLU 41 E B - 180.8 - 170.1 - - - - - - 184.9 -1.8 33.3 - 42 ILE 42 E B - - -47.8 176.6 - - - - - - 179.9 - 35.9 - * * 43 VAL 43 E B 66.5 - - - - - - - - - 178.9 -2.3 33.5 - 44 SER 44 E B - - -56.4 - - - - - - - 180.4 - 35.5 - 45 ALA 45 E B - - - - - - - - - - 178.9 -2.7 34.8 - 46 THR 46 E B - - -57.0 - - - - - - - 175.7 -2.7 36.4 - 47 LEU 47 E b - 176.0 - - - - - - - - 178.0 -3.6 34.1 - ** ** 48 PRO 48 E - - - - - -84.3 - - - - - 180.3 - 38.8 - +* * +* 49 GLY 49 E - - - - - - - - - - - 180.1 -3.3 - - +* +* 50 PHE 50 E B - - -68.2 - - - - - - - 184.1 -.7 33.4 - +* +* 51 GLN 51 E B - 189.2 - - - - - - - - 178.7 -3.0 35.7 - * * 52 ARG 52 E B 49.5 - - 175.8 - - - - - - 174.9 - 34.3 - 53 PHE 53 E B - - -73.0 - - - - - - - 193.1 -2.6 32.4 - ** ** 54 ARG 54 B - 176.5 - - - - - - - - 172.1 - 32.7 - * * 55 LEU 55 B 65.6 - - 171.5 - - - - - - 178.6 - 34.2 - 56 LYS 56 S b - 189.6 - 173.6 - - - - - - 181.1 - 32.3 - 57 GLY 57 S - - - - - - - - - - - 178.1 -1.6 - - 58 ARG 58 S A - 190.5 - - - - - - - - 181.4 - 35.0 - Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 LEU 59 S B - 186.4 - - - - - - - - 186.5 - 32.0 - * * 60 TYR 60 B - - -45.0 - - - - - - - 170.8 - 38.3 - * +* * +* 61 PRO 61 - - - - - -73.7 - - - - - 185.9 - 37.5 - * * * 62 CYS 62 E B - - -54.1 - - - - - - - 180.4 -2.0 33.4 - 63 ILE 63 E B - - -59.3 - - - - - - - 175.3 - 36.2 - 64 VAL 64 E B - - -60.4 - - - - - - - 177.6 -2.0 34.7 - 65 PRO 65 E - - - - - -66.1 - - - - - 179.2 - 38.0 - * * 66 SER 66 E B - 183.5 - - - - - - - - 185.5 -.9 34.8 - +* +* 67 GLU 67 E A - - -58.1 183.1 - - - - - - 182.4 - 34.0 - 68 LYS 68 E A - - -58.5 186.3 - - - - - - 182.3 - 35.0 - 69 GLY 69 E - - - - - - - - - - - 175.4 -1.5 - - 70 GLU 70 E B 65.6 - - 179.2 - - - - - - 183.6 - 32.1 - 71 VAL 71 E B - 182.0 - - - - - - - - 177.4 -2.9 35.6 - * * 72 HIS 72 E B - - -63.9 - - - - - - - 183.4 -.6 33.5 - +* +* 73 GLY 73 E - - - - - - - - - - - 182.0 -3.0 - - * * 74 LYS 74 E B - - -91.1 - - - - - - - 176.6 -1.4 32.0 - +* +* 75 VAL 75 E B - 164.7 - - - - - - - - 175.7 -3.3 33.9 - * +* +* 76 LEU 76 E B - - -57.2 180.2 - - - - - - 178.4 -3.2 36.5 - +* +* 77 MET 77 E B 54.8 - - 175.9 - - - - - - 184.5 -3.0 32.3 - * * 78 GLY 78 E - - - - - - - - - - - 178.4 -1.2 - - * * 79 VAL 79 E B 66.7 - - - - - - - - - 181.8 -1.8 32.8 - 80 THR 80 h B 60.6 - - - - - - - - - 179.9 -.5 33.4 - ** ** 81 SER 81 H A 45.2 - - - - -59.8 -41.2 - - - 180.7 - 34.1 - * * 82 ASP 82 H A - - -60.6 - - -65.0 -36.7 - - - 179.9 - 35.0 - 83 GLU 83 H A - - -57.2 172.2 - -78.0 -31.1 - - - 178.1 - 35.3 - * * 84 LEU 84 H A - 181.1 - - - -66.3 -47.3 - - - 178.9 -2.2 34.6 - 85 GLU 85 H A 63.0 - - 173.7 - -62.0 -29.4 - - - 178.0 -2.7 32.9 - 86 ASN 86 H A - 176.6 - - - -67.2 -44.1 - - - 177.8 -.9 35.2 - * * 87 LEU 87 H A - - -64.3 174.1 - -64.8 -43.2 - - - 180.1 -1.9 35.3 - 88 ASP 88 H A - 182.6 - - - -65.6 -27.6 - - - 176.6 -2.8 33.9 - * * 89 ALA 89 H A - - - - - -75.5 -48.5 - - - 184.1 -1.3 34.6 - * * 90 VAL 90 H A - 178.1 - - - -69.9 -58.2 - - - 180.4 -2.5 33.5 - +* +* 91 GLU 91 h A - - -63.1 - - - - - - - 181.4 -2.7 32.0 - 92 GLY 92 T - - - - - - - - - - - 178.4 -1.0 - - * * 93 ASN 93 T A - 180.3 - - - - - - - - 180.6 -.5 35.3 - +* +* Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 GLU 94 e a - - -60.4 178.7 - - - - - - 180.8 -1.9 33.2 - 95 TYR 95 E B - - -65.5 - - - - - - - 178.4 -1.3 34.7 - 96 GLU 96 E B - 180.7 - 174.1 - - - - - - 179.3 -2.3 34.7 - 97 ARG 97 E B - 180.6 - 181.9 - - - - - - 182.3 - 35.6 - 98 VAL 98 E B - - -65.3 - - - - - - - 181.9 -2.7 32.1 - 99 THR 99 E B - 181.8 - - - - - - - - 180.9 - 33.0 - 100 VAL 100 E B - - -63.5 - - - - - - - 179.4 -3.4 33.0 - +* +* 101 GLY 101 E - - - - - - - - - - - 181.9 - - - 102 ILE 102 E B 56.9 - - - - - - - - - 178.3 -2.5 32.3 - 103 VAL 103 E B - 180.9 - - - - - - - - 184.2 -2.6 33.6 - 104 ARG 104 E B - 203.6 - 177.5 - - - - - - 183.7 -3.4 35.5 - * +* +* 105 GLU 105 e A - - -57.1 181.7 - - - - - - 172.9 -2.0 33.4 - * * 106 ASP 106 T A - 177.6 - - - - - - - - 170.9 -.6 35.2 - +* +* +* 107 ASN 107 t ~a - - -48.1 - - - - - - - 174.5 -1.8 33.3 - ** * ** 108 SER 108 S a 50.3 - - - - - - - - - 178.8 - 34.6 - 109 GLU 109 e B - - -64.1 190.8 - - - - - - 183.1 - 34.1 - 110 LYS 110 E B 58.3 - - 184.9 - - - - - - 183.5 - 32.6 - 111 MET 111 E B - - -57.4 185.8 - - - - - - 180.4 -3.4 33.4 - +* +* 112 ALA 112 E B - - - - - - - - - - 184.0 - 33.9 - 113 VAL 113 E B - - -57.4 - - - - - - - 175.2 -2.0 34.5 - 114 LYS 114 E B - - -58.0 185.2 - - - - - - 180.4 -1.9 33.3 - 115 THR 115 E B - 189.5 - - - - - - - - 178.3 -2.4 34.4 - 116 TYR 116 E B - - -64.5 - - - - - - - 179.3 -.6 33.8 - +* +* 117 MET 117 E B 64.7 - - 169.8 - - - - - - 180.9 -2.2 33.2 - 118 TRP 118 E B - 194.4 - - - - - - - - 187.8 -3.1 34.9 - * * * 119 ILE 119 e A - - -44.8 - - - - - - - 181.6 -.6 36.5 - * +* +* 120 ASN 120 S A - 178.3 - - - - - - - - 176.8 - 34.1 - 121 LYS 121 l 69.0 - - 185.1 - - - - - - 180.3 - 29.3 - * * 122 ALA 122 a - - - - - - - - - - 179.6 - 34.7 - 123 ASP 123 B - 181.0 - - - - - - - - 182.9 - 34.4 - 124 PRO 124 S - - - - - -77.5 - - - - - 183.1 - 39.0 - * * * 125 ASP 125 S A - 175.7 - - - - - - - - 178.1 - 33.4 - 126 MET 126 S A 69.5 - - 172.2 - - - - - - 178.9 - 33.0 - 127 PHE 127 B - 183.4 - - - - - - - - 184.7 - 33.5 - 128 GLY 128 - - - - - - - - - - - 180.0 -.9 - - +* +* 129 GLU 129 B - - -59.3 - - - - - - - 176.8 - 35.5 - 130 TRP 130 B - - -56.8 - - - - - - - 165.4 -.5 36.4 - +** ** +** 131 ASN 131 h b - - -56.3 - - - - - - - 193.3 - 35.1 - ** ** 132 PHE 132 H A - - -56.4 - - -62.1 -37.4 - - - 180.8 -1.5 31.9 - 133 GLU 133 H A - - -58.5 180.1 - -73.2 -28.8 - - - 175.1 - 32.7 - 134 GLU 134 H A - 176.3 - - - -70.4 -47.4 - - - 181.1 - 33.8 - 135 TRP 135 H A - 182.3 - - - -67.1 -44.5 - - - 178.2 -3.0 30.8 - * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 136 LYS 136 H A - - -64.5 - - -60.8 -31.2 - - - 179.6 -3.1 33.2 - * * 137 ARG 137 H A - 175.0 - - - -65.8 -52.0 - - - 181.9 -1.1 36.2 - * * * 138 LEU 138 H A - - -75.2 - - -74.1 -33.8 - - - 184.6 -1.9 33.2 - 139 HIS 139 h A - 189.3 - - - - - - - - 183.8 -2.9 31.7 - * * 140 LYS 140 H A - 179.3 - 192.0 - -46.6 -43.9 - - - 185.8 - 37.2 - +* +* 141 LYS 141 H A - 184.6 - 180.6 - -53.9 -34.5 - - - 180.1 -.6 32.3 - +* +* 142 LYS 142 H A - 188.5 - - - -59.0 -43.6 - - - 182.1 -1.5 34.9 - 143 PHE 143 H A - - -52.6 - - -76.7 -32.8 - - - 179.6 -1.1 34.2 - * * 144 ILE 144 H A - - -57.4 - - -63.3 -33.3 - - - 179.4 -2.1 33.1 - 145 GLU 145 H A - - -68.3 - - -51.8 -39.1 - - - 178.6 -2.0 33.1 - * * 146 THR 146 H A - 182.6 - - - -80.6 -39.3 - - - 179.3 -.8 31.2 - * +* +* 147 PHE 147 H A - - -71.0 - - -67.9 -29.2 - - - 173.9 -1.5 29.9 - * * * 148 LYS 148 H A - 178.4 - 180.6 - -53.8 -42.2 - - - 178.6 -3.1 36.6 - * * 149 LYS 149 H A - - -59.3 180.3 - -75.3 -42.0 - - - 179.9 -.6 33.6 - +* +* 150 ILE 150 H A - - -60.9 176.1 - -61.6 -39.5 - - - 178.9 -2.0 33.2 - 151 MET 151 H A - 183.4 - 179.7 - -62.1 -45.9 - - - 178.1 -3.3 34.6 - +* +* 152 GLU 152 H A - - -62.9 - - -66.5 -30.9 - - - 179.0 -1.3 34.0 - 153 CYS 153 H A - 183.0 - - - -69.2 -33.5 - - - 177.0 -1.9 33.6 - 154 LYS 154 H A - - -62.6 183.2 - -77.2 -27.4 - - - 176.8 -1.8 34.5 - * * * 155 LYS 155 H A - 179.7 - 178.8 - -67.4 -31.4 - - - 174.0 -1.5 34.4 - * * 156 LYS 156 h B - - -65.9 174.8 - - - - - - 180.9 -1.2 35.2 - * * 157 PRO 157 - - - - - -73.1 - - - - - 176.2 - 38.1 - * * 158 GLN 158 B - 187.5 - - - - - - - - 184.4 -.8 34.7 - +* +* 159 GLY 159 - - - - - - - - - - - 181.0 - - - 160 GLN 160 B 59.2 - - 179.3 - - - - - - 178.0 - 34.0 - 161 GLY 161 - - - - - - - - - - - 182.9 - - - 162 ASN 162 b 58.3 - - - - - - - - - 178.4 -.8 31.3 - +* +* 163 ASP 163 B - 176.6 - - - - - - - - 182.4 -1.0 34.4 - * * 164 ASP 164 B - 177.7 - - - - - - - - 174.7 -.7 34.3 - +* +* 165 ILE 165 b - 175.5 - - - - - - - - 179.8 - 30.7 - 166 SER 166 B - - -58.5 - - - - - - - 179.9 - 34.8 - 167 HIS 167 B - - -64.9 - - - - - - - 181.2 -.7 32.6 - +* +* 168 VAL 168 B - - -61.9 - - - - - - - 177.8 - 34.5 - 169 LEU 169 B - - -66.0 - - - - - - - 182.7 - 33.1 - 170 ARG 170 B - - -55.8 183.0 - - - - - - 174.9 - 34.7 - 171 GLU 171 B 57.8 - - 181.6 - - - - - - 180.1 - 35.3 - Residue-by-residue listing for refined_7 Page 6 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 172 ASP 172 B - 188.8 - - - - - - - - 179.5 - 33.1 - 173 GLN 173 - - 184.9 - 184.4 - - - - - - - - 34.8 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * +* +* +* +* +** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.8 182.2 -61.2 179.1 -72.3 -66.4 -38.4 - - - 179.9 -1.9 34.1 Standard deviations: 6.5 6.2 7.2 5.6 7.6 8.0 7.5 - - - 3.8 .9 1.8 Numbers of values: 29 55 66 42 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_7 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 - 1.236 1.500 - 1.456 - 117.03 120.10 - 111.02 - 122.87 2 HIS 2 1.318 1.229 1.515 1.560 1.458 120.74 117.26 120.11 111.11 108.72 112.59 122.61 +* * +* 3 HIS 3 1.303 1.225 1.514 1.559 1.447 120.77 115.78 120.79 110.07 110.20 110.84 123.42 +* * +* 4 HIS 4 1.298 1.236 1.506 1.548 1.441 123.54 118.05 119.43 110.03 106.41 111.06 122.48 ** * +* ** 5 HIS 5 1.299 1.230 1.510 1.567 1.446 119.70 116.03 120.61 112.60 109.38 113.65 123.30 ** +* * * +* ** 6 HIS 6 1.313 1.239 1.532 1.553 1.457 122.20 116.62 120.41 111.79 109.02 109.50 122.94 * * * 7 HIS 7 1.311 1.231 1.505 1.540 1.464 122.17 115.63 121.04 105.53 111.79 111.84 123.32 * ** ** 8 LEU 8 1.305 1.239 1.505 1.554 1.428 120.80 114.51 121.41 111.13 104.57 114.03 123.80 +* * +* ** ** ** 9 GLU 9 1.311 1.238 1.509 1.528 1.430 122.84 114.76 121.72 110.97 111.34 110.41 123.51 * * * 10 CYS 10 1.283 1.230 1.492 1.532 1.411 123.13 117.11 120.07 109.95 107.32 110.20 122.80 *** +* ** * *** 11 SER 11 1.292 1.245 1.520 1.513 1.421 120.34 116.56 120.48 111.93 109.09 109.66 122.91 +** +* +** Residue-by-residue listing for refined_7 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 1.299 1.235 1.523 1.515 1.423 121.12 115.55 120.44 111.77 109.36 109.15 124.01 ** +* ** 13 ASP 13 1.349 1.234 1.523 1.537 1.492 125.37 116.17 120.91 110.05 113.69 112.68 122.92 * +* ** * ** 14 SER 14 1.294 1.253 1.534 1.545 1.427 123.46 116.98 120.56 111.11 109.05 108.42 122.45 ** * +* * ** 15 LEU 15 1.320 1.236 1.523 1.542 1.415 121.75 114.47 121.73 111.76 110.04 112.15 123.67 ** ** 16 GLN 16 1.309 1.235 1.510 1.559 1.444 123.81 114.69 121.89 113.28 109.12 109.48 123.21 * * * +* +* 17 LEU 17 1.318 1.233 1.487 1.530 1.415 121.93 114.76 121.63 109.28 109.36 112.60 123.57 +* ** * ** 18 HIS 18 1.270 1.244 1.496 1.535 1.426 122.38 115.90 120.47 108.91 108.85 109.78 123.58 **** * +* **** 19 ASN 19 1.292 1.236 1.518 1.546 1.424 121.86 115.17 121.56 114.53 110.85 113.28 123.18 +** +* ** +* +** 20 VAL 20 1.305 1.224 1.522 1.566 1.450 122.85 116.52 120.27 109.30 110.48 110.17 123.20 +* +* 21 PHE 21 1.311 1.232 1.514 1.538 1.444 122.39 116.25 120.89 110.77 108.53 110.30 122.83 * * 22 VAL 22 1.296 1.239 1.519 1.550 1.432 121.53 114.99 121.41 111.79 111.69 112.48 123.60 ** * * ** 23 TYR 23 1.319 1.223 1.518 1.534 1.456 122.92 117.03 120.48 110.60 113.83 110.86 122.48 24 GLY 24 1.311 1.220 1.494 - 1.431 118.71 116.95 119.97 - 113.31 - 123.08 * * * * * 25 SER 25 1.320 1.229 1.529 1.529 1.457 121.74 115.65 121.23 110.37 111.19 108.65 123.07 * * 26 PHE 26 1.311 1.215 1.519 1.532 1.437 121.97 116.81 120.69 111.52 112.24 109.56 122.39 * * * 27 GLN 27 1.332 1.234 1.527 1.539 1.479 120.66 114.51 121.82 109.34 108.90 111.62 123.67 * * 28 ASP 28 1.296 1.217 1.525 1.525 1.432 124.05 118.80 119.78 110.23 109.32 108.08 121.42 ** * * * * ** 29 PRO 29 1.343 1.231 1.527 1.531 1.461 121.92 116.36 120.70 109.89 112.57 104.44 122.92 * * 30 ASP 30 1.325 1.245 1.514 1.536 1.471 122.04 115.92 120.74 110.09 110.74 111.73 123.30 31 VAL 31 1.322 1.230 1.533 1.568 1.450 121.21 116.42 121.03 111.42 109.98 113.28 122.52 * * * * 32 ILE 32 1.329 1.237 1.531 1.539 1.439 121.25 116.37 120.47 110.54 110.28 111.56 123.11 * * 33 ASN 33 1.336 1.223 1.511 1.548 1.470 121.78 115.53 121.34 106.63 110.63 112.14 123.13 +* +* 34 VAL 34 1.304 1.234 1.531 1.544 1.438 121.36 117.24 120.07 111.47 114.37 111.89 122.69 +* * * * +* 35 MET 35 1.322 1.238 1.529 1.541 1.454 121.06 117.02 120.81 112.31 110.67 109.86 122.13 * * 36 LEU 36 1.314 1.237 1.516 1.569 1.435 119.70 116.63 119.63 113.05 111.52 114.76 123.65 * +* * * +* +** +** 37 ASP 37 1.338 1.230 1.515 1.540 1.482 123.47 115.35 121.43 108.74 109.55 111.44 123.22 * * 38 ARG 38 1.311 1.226 1.501 1.530 1.457 122.41 116.32 120.42 110.11 110.36 110.64 123.25 * * * 39 THR 39 1.308 1.243 1.528 1.539 1.429 121.81 116.97 120.88 110.52 111.25 109.97 122.06 +* +* +* 40 PRO 40 1.339 1.233 1.523 1.532 1.459 123.00 116.58 120.15 109.85 110.34 103.53 123.25 Residue-by-residue listing for refined_7 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 1.308 1.236 1.515 1.526 1.443 122.04 115.41 121.12 111.72 109.78 110.63 123.44 * * 42 ILE 42 1.300 1.238 1.515 1.545 1.436 121.74 115.88 120.70 108.35 109.37 110.56 123.42 ** * ** 43 VAL 43 1.296 1.229 1.534 1.554 1.449 122.22 117.09 120.31 109.81 110.36 112.14 122.58 ** ** 44 SER 44 1.309 1.243 1.547 1.521 1.442 121.85 116.25 121.04 109.86 110.10 108.90 122.69 * * * 45 ALA 45 1.314 1.224 1.515 1.499 1.449 122.58 115.49 121.43 109.50 111.59 109.76 123.08 * * 46 THR 46 1.294 1.219 1.512 1.526 1.432 123.03 116.48 120.14 108.22 109.92 109.70 123.38 ** * * ** 47 LEU 47 1.299 1.230 1.527 1.532 1.426 122.34 117.68 120.38 110.99 109.74 110.39 121.86 ** +* ** 48 PRO 48 1.336 1.242 1.523 1.543 1.445 122.67 116.41 120.87 110.30 110.77 103.93 122.73 * * 49 GLY 49 1.305 1.231 1.508 - 1.434 120.60 116.15 120.85 - 111.51 - 123.00 +* * +* 50 PHE 50 1.315 1.216 1.507 1.546 1.449 122.85 117.38 119.87 111.11 109.00 111.63 122.74 * * 51 GLN 51 1.305 1.239 1.510 1.533 1.440 120.89 115.30 120.80 109.24 109.58 109.80 123.87 +* +* 52 ARG 52 1.312 1.235 1.506 1.553 1.437 122.91 115.86 121.26 109.94 110.58 111.13 122.88 * * * * 53 PHE 53 1.283 1.208 1.466 1.514 1.426 121.42 116.72 120.23 113.32 107.07 111.54 123.05 *** * +** +* +* * *** 54 ARG 54 1.288 1.227 1.499 1.558 1.404 119.53 112.71 122.08 113.80 113.79 108.53 125.21 +** * * +** * +* +* * * +** 55 LEU 55 1.288 1.244 1.499 1.558 1.419 126.71 118.75 118.78 110.17 103.27 113.47 122.43 +** * * ** +** * * +** +* +** 56 LYS 56 1.288 1.236 1.505 1.539 1.428 119.28 114.63 121.45 112.59 109.93 111.42 123.85 +** +* * * +** 57 GLY 57 1.308 1.232 1.500 - 1.431 121.84 116.44 120.52 - 110.39 - 123.02 +* * +* 58 ARG 58 1.321 1.230 1.504 1.558 1.451 121.15 114.96 121.49 110.75 106.93 110.30 123.50 * +* +* 59 LEU 59 1.296 1.243 1.526 1.537 1.418 121.91 115.72 120.39 113.32 109.51 111.15 123.83 ** ** +* ** 60 TYR 60 1.305 1.233 1.521 1.546 1.443 123.77 119.33 119.45 107.49 107.45 108.15 121.22 +* * +* * * * * +* 61 PRO 61 1.347 1.223 1.537 1.540 1.444 121.05 115.89 121.09 111.13 109.93 104.99 122.96 * +* +* 62 CYS 62 1.309 1.248 1.533 1.540 1.440 122.23 115.18 121.27 111.56 112.13 109.90 123.55 * * 63 ILE 63 1.326 1.229 1.509 1.563 1.455 123.27 116.96 120.11 108.04 109.25 110.69 122.91 64 VAL 64 1.309 1.237 1.531 1.572 1.456 122.38 118.21 119.83 108.57 108.37 112.46 121.93 * * * * * 65 PRO 65 1.341 1.240 1.542 1.536 1.470 122.55 116.09 121.01 110.94 112.41 103.70 122.88 66 SER 66 1.313 1.229 1.518 1.523 1.443 122.94 116.78 120.15 110.49 108.35 110.05 123.05 * * * 67 GLU 67 1.310 1.240 1.532 1.509 1.457 122.22 116.91 120.41 109.64 113.49 110.07 122.68 * * * 68 LYS 68 1.320 1.242 1.513 1.517 1.462 121.44 116.47 120.69 108.83 111.47 110.30 122.83 69 GLY 69 1.301 1.236 1.508 - 1.427 119.89 115.45 120.81 - 112.99 - 123.74 +* +* +* Residue-by-residue listing for refined_7 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 1.310 1.247 1.506 1.546 1.440 123.40 116.29 120.54 111.16 107.97 113.86 123.16 * * +* +* 71 VAL 71 1.296 1.214 1.496 1.551 1.435 122.16 116.43 120.89 108.46 109.79 111.07 122.66 ** * * ** 72 HIS 72 1.292 1.228 1.493 1.537 1.431 120.33 115.95 120.65 111.38 107.34 111.76 123.38 +** +* * * +** 73 GLY 73 1.284 1.236 1.482 - 1.417 121.27 116.73 120.23 - 110.31 - 123.04 *** +* ** *** 74 LYS 74 1.290 1.227 1.503 1.538 1.433 121.34 114.56 121.31 110.75 112.97 112.40 124.12 +** * * * +** 75 VAL 75 1.301 1.225 1.520 1.555 1.447 123.44 115.10 120.84 109.51 112.01 111.47 124.07 ** ** 76 LEU 76 1.316 1.230 1.524 1.540 1.442 123.81 117.54 119.87 107.86 108.28 110.36 122.56 * * * * 77 MET 77 1.307 1.221 1.507 1.535 1.466 121.29 116.98 120.50 111.08 110.68 112.39 122.52 +* * +* 78 GLY 78 1.310 1.234 1.506 - 1.433 119.47 116.06 121.23 - 110.95 - 122.70 * * * 79 VAL 79 1.317 1.249 1.536 1.584 1.437 120.81 116.88 120.43 112.16 108.17 112.00 122.61 +* * * * +* 80 THR 80 1.316 1.241 1.524 1.565 1.445 120.83 116.38 120.77 110.06 110.23 112.33 122.85 81 SER 81 1.300 1.239 1.551 1.518 1.446 122.67 116.34 120.79 112.29 112.23 107.79 122.82 ** * * +* ** 82 ASP 82 1.334 1.225 1.515 1.530 1.480 122.70 115.39 121.81 108.68 110.90 110.69 122.80 * * 83 GLU 83 1.295 1.231 1.538 1.517 1.441 122.30 116.29 120.82 111.09 109.21 108.30 122.87 ** * ** 84 LEU 84 1.334 1.232 1.523 1.523 1.457 122.27 116.72 120.39 108.53 110.63 111.48 122.89 85 GLU 85 1.344 1.223 1.531 1.551 1.466 121.29 115.29 121.30 110.69 109.63 112.33 123.40 * * * * 86 ASN 86 1.321 1.220 1.531 1.534 1.450 123.51 115.82 121.06 110.88 109.64 108.74 123.09 * * * 87 LEU 87 1.325 1.238 1.512 1.536 1.468 122.92 114.93 121.24 109.12 109.77 110.33 123.81 88 ASP 88 1.321 1.214 1.514 1.532 1.458 123.01 116.00 121.29 111.02 110.34 110.22 122.71 89 ALA 89 1.302 1.237 1.531 1.518 1.434 121.66 116.03 120.71 110.35 110.34 109.83 123.21 +* * +* 90 VAL 90 1.328 1.233 1.542 1.564 1.456 122.02 117.43 120.30 110.42 112.45 110.91 122.24 91 GLU 91 1.319 1.226 1.519 1.531 1.461 120.77 115.75 121.15 111.75 111.39 111.68 123.04 92 GLY 92 1.327 1.230 1.516 - 1.465 122.72 116.08 120.65 - 113.49 - 123.27 * * 93 ASN 93 1.323 1.228 1.533 1.538 1.456 122.68 116.95 120.50 109.13 110.54 110.00 122.55 94 GLU 94 1.335 1.227 1.538 1.543 1.466 121.17 116.37 121.11 111.36 111.84 110.38 122.49 95 TYR 95 1.311 1.224 1.506 1.518 1.461 122.70 116.05 120.54 108.01 110.81 111.83 123.40 * * * 96 GLU 96 1.312 1.245 1.499 1.547 1.442 122.15 115.34 120.70 110.24 108.51 110.80 123.94 * * * 97 ARG 97 1.312 1.229 1.503 1.534 1.428 122.40 115.65 120.93 110.10 107.89 109.66 123.40 * * +* * +* 98 VAL 98 1.295 1.238 1.486 1.537 1.439 122.21 115.26 120.87 109.76 112.02 113.65 123.87 ** +* * * ** 99 THR 99 1.297 1.236 1.521 1.570 1.430 121.56 115.70 121.48 111.27 109.24 112.27 122.77 ** * * ** 100 VAL 100 1.297 1.237 1.523 1.558 1.456 121.09 115.94 121.27 109.56 111.92 112.62 122.78 ** ** Residue-by-residue listing for refined_7 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 1.302 1.230 1.494 - 1.427 121.21 116.59 120.42 - 110.58 - 122.99 +* * +* +* 102 ILE 102 1.298 1.219 1.503 1.579 1.439 121.60 116.75 120.29 111.74 110.66 112.26 122.96 ** * * * ** 103 VAL 103 1.290 1.231 1.495 1.548 1.428 121.47 116.42 120.32 110.86 107.55 112.18 123.23 +** * +* * +** 104 ARG 104 1.301 1.238 1.510 1.525 1.421 121.25 116.11 120.27 110.46 108.02 109.37 123.60 ** +* * ** 105 GLU 105 1.327 1.237 1.526 1.526 1.470 123.16 114.97 121.19 110.94 111.09 110.55 123.83 106 ASP 106 1.326 1.239 1.524 1.515 1.456 123.83 116.18 120.82 110.53 108.91 108.94 123.00 * * 107 ASN 107 1.342 1.226 1.524 1.564 1.462 120.00 114.43 121.86 107.98 108.17 115.00 123.67 +* * * +** +** 108 SER 108 1.299 1.232 1.516 1.531 1.421 125.62 114.47 121.95 111.81 106.29 109.80 123.58 ** +* ** +* ** 109 GLU 109 1.346 1.231 1.487 1.531 1.434 121.92 115.31 121.12 109.27 108.19 112.60 123.56 * +* * * * +* 110 LYS 110 1.252 1.238 1.504 1.525 1.422 121.81 115.76 121.02 112.49 109.83 111.00 123.19 *5.5* * +* * *5.5* 111 MET 111 1.290 1.235 1.474 1.517 1.438 122.36 114.26 121.75 108.28 110.68 113.67 123.98 +** ** * +* +** 112 ALA 112 1.257 1.227 1.496 1.510 1.436 122.03 116.38 120.32 110.48 108.58 111.37 123.30 *5.1* * * *5.1* 113 VAL 113 1.296 1.228 1.508 1.564 1.443 121.77 116.68 120.67 108.45 109.32 112.76 122.62 ** ** 114 LYS 114 1.289 1.223 1.514 1.522 1.427 120.40 117.39 120.01 111.61 108.97 111.11 122.56 +** +* +** 115 THR 115 1.304 1.235 1.516 1.565 1.449 120.86 115.85 120.57 109.30 109.35 112.01 123.58 +* +* 116 TYR 116 1.309 1.230 1.528 1.532 1.437 122.93 115.66 120.94 111.39 110.31 110.04 123.36 * * * 117 MET 117 1.317 1.237 1.522 1.547 1.469 122.93 116.39 120.11 109.04 109.56 113.57 123.50 +* +* 118 TRP 118 1.322 1.255 1.535 1.535 1.454 122.42 116.74 120.30 110.43 109.12 109.74 122.95 * * 119 ILE 119 1.333 1.241 1.522 1.546 1.471 120.34 115.58 121.05 105.57 110.81 111.84 123.29 +* +* 120 ASN 120 1.319 1.220 1.502 1.535 1.455 122.13 114.46 120.99 110.73 109.83 110.49 124.55 * * 121 LYS 121 1.332 1.221 1.554 1.561 1.483 127.09 117.63 120.20 112.55 115.59 112.56 122.14 * +* * +** * +* * +** 122 ALA 122 1.311 1.238 1.514 1.523 1.448 122.18 115.15 121.46 110.71 109.37 109.62 123.39 * * 123 ASP 123 1.321 1.231 1.537 1.539 1.461 122.67 117.74 120.42 110.63 109.53 110.11 121.83 124 PRO 124 1.335 1.234 1.535 1.528 1.472 122.78 116.29 121.05 110.18 113.21 102.74 122.64 125 ASP 125 1.304 1.220 1.525 1.543 1.447 122.50 116.97 120.44 112.31 110.69 109.69 122.56 +* * +* 126 MET 126 1.346 1.231 1.529 1.549 1.486 121.09 116.71 120.70 108.41 111.22 113.66 122.58 * * +* +* 127 PHE 127 1.332 1.238 1.508 1.541 1.441 120.65 115.98 120.78 110.98 108.22 111.86 123.23 * * 128 GLY 128 1.298 1.242 1.489 - 1.434 120.47 115.59 120.65 - 112.25 - 123.76 ** +* * ** 129 GLU 129 1.307 1.237 1.517 1.533 1.429 122.17 115.83 120.88 109.50 109.41 109.95 123.28 +* +* +* Residue-by-residue listing for refined_7 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 1.241 1.475 1.536 1.442 122.27 116.52 120.30 105.81 108.06 112.74 123.09 ** ** ** * * ** 131 ASN 131 1.293 1.229 1.530 1.540 1.429 119.67 116.20 120.70 110.30 102.81 111.39 122.95 +** +* * +** +** 132 PHE 132 1.323 1.217 1.515 1.539 1.457 122.34 117.61 119.88 111.19 113.43 111.83 122.48 133 GLU 133 1.314 1.230 1.527 1.526 1.458 120.65 115.31 121.05 111.88 110.03 111.04 123.62 * * 134 GLU 134 1.323 1.225 1.518 1.567 1.457 123.15 116.04 121.08 113.32 108.61 109.09 122.73 +* +* +* 135 TRP 135 1.312 1.235 1.544 1.539 1.433 121.05 117.48 120.25 113.05 112.34 111.78 122.24 * * +* +* 136 LYS 136 1.328 1.231 1.520 1.533 1.473 121.28 115.49 120.91 109.81 110.99 112.15 123.60 137 ARG 137 1.314 1.233 1.528 1.517 1.442 122.94 116.09 121.31 108.57 111.58 108.90 122.59 * * 138 LEU 138 1.304 1.209 1.508 1.542 1.448 121.42 115.86 121.28 110.42 111.51 111.60 122.78 +* * +* 139 HIS 139 1.289 1.231 1.541 1.549 1.475 122.17 115.24 121.00 112.76 111.32 111.17 123.76 +** * +** 140 LYS 140 1.327 1.230 1.538 1.533 1.473 125.25 117.19 119.68 107.31 113.23 108.32 123.12 +* * * +* 141 LYS 141 1.345 1.226 1.538 1.544 1.479 122.21 116.72 120.17 110.72 112.69 111.75 123.06 * * * 142 LYS 142 1.330 1.238 1.531 1.564 1.464 122.25 115.71 121.31 111.02 109.37 109.40 122.97 +* +* 143 PHE 143 1.313 1.227 1.521 1.526 1.446 121.99 115.60 121.24 110.62 109.85 110.38 123.15 * * 144 ILE 144 1.318 1.208 1.525 1.561 1.456 122.21 116.56 120.33 110.48 110.54 112.10 123.08 * * 145 GLU 145 1.324 1.237 1.538 1.526 1.471 122.96 117.46 120.28 110.75 113.28 110.40 122.25 146 THR 146 1.323 1.235 1.547 1.569 1.446 119.99 116.60 120.83 112.12 110.52 113.09 122.49 * * * * 147 PHE 147 1.334 1.213 1.500 1.519 1.461 121.89 115.57 120.73 112.86 112.58 112.83 123.70 * * * * 148 LYS 148 1.304 1.229 1.537 1.529 1.448 124.05 115.58 121.28 110.09 109.32 107.39 123.13 +* * +* +* 149 LYS 149 1.329 1.230 1.526 1.535 1.448 122.00 115.71 121.10 111.38 110.14 110.45 123.17 150 ILE 150 1.325 1.231 1.538 1.563 1.462 122.76 116.70 120.52 110.70 111.63 111.37 122.77 151 MET 151 1.319 1.233 1.525 1.524 1.437 122.78 116.11 120.78 110.73 110.11 109.61 123.09 * * 152 GLU 152 1.330 1.227 1.536 1.536 1.457 121.58 116.19 121.07 110.12 110.03 110.99 122.73 153 CYS 153 1.325 1.233 1.538 1.536 1.457 122.55 116.62 120.62 111.10 111.06 110.28 122.76 154 LYS 154 1.327 1.231 1.507 1.508 1.458 121.71 114.86 121.42 109.49 110.10 110.79 123.71 * * 155 LYS 155 1.316 1.241 1.535 1.531 1.452 123.26 115.52 121.04 111.69 109.73 109.03 123.44 156 LYS 156 1.331 1.234 1.523 1.533 1.453 122.58 117.81 120.33 108.79 109.21 110.96 121.85 157 PRO 157 1.324 1.234 1.533 1.529 1.452 122.16 116.05 121.22 110.83 112.52 103.76 122.66 * * 158 GLN 158 1.304 1.239 1.521 1.552 1.429 122.22 116.68 119.52 112.97 106.14 108.71 123.78 +* * +* +* +* * +* 159 GLY 159 1.329 1.238 1.515 - 1.460 122.29 116.69 120.75 - 114.32 - 122.56 160 GLN 160 1.302 1.238 1.513 1.536 1.442 121.11 116.03 120.83 110.44 110.61 110.73 123.14 +* +* 161 GLY 161 1.300 1.233 1.498 - 1.434 121.42 115.57 120.76 - 109.74 - 123.65 ** * ** Residue-by-residue listing for refined_7 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 1.315 1.229 1.523 1.559 1.451 122.57 115.24 121.64 111.90 112.29 112.51 123.09 * * * * 163 ASP 163 1.310 1.234 1.515 1.536 1.453 122.63 116.37 120.58 110.39 109.45 110.52 123.03 * * 164 ASP 164 1.308 1.236 1.515 1.536 1.461 122.11 115.75 121.05 109.30 111.98 110.86 123.19 +* +* 165 ILE 165 1.304 1.237 1.533 1.576 1.430 122.44 115.09 122.06 112.82 110.11 113.51 122.75 +* * * +* * +* 166 SER 166 1.300 1.231 1.526 1.537 1.431 122.23 116.86 120.56 110.68 109.32 109.70 122.56 ** * ** 167 HIS 167 1.315 1.237 1.502 1.532 1.456 120.90 115.50 120.87 110.48 110.72 112.52 123.62 * * * * 168 VAL 168 1.299 1.245 1.527 1.554 1.444 122.71 116.45 120.57 109.81 110.45 110.78 122.98 ** ** 169 LEU 169 1.309 1.237 1.507 1.551 1.444 121.41 116.49 120.59 110.43 109.22 112.69 122.92 * * * * 170 ARG 170 1.302 1.235 1.508 1.525 1.438 121.06 115.31 121.16 108.77 110.69 111.28 123.52 +* * +* 171 GLU 171 1.303 1.249 1.529 1.530 1.446 122.83 117.72 120.22 110.47 108.47 109.24 122.05 +* +* 172 ASP 172 1.307 1.233 1.504 1.529 1.446 119.54 115.38 121.11 110.59 110.81 111.78 123.49 +* * * +* 173 GLN 173 1.300 - 1.513 1.529 1.435 122.35 - - 110.27 108.32 110.46 - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.5* * +** +* +** +** +* * ** +** +** * *5.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 1.252 1.349 1.311 .016 *5.5* * * C-N (Pro) 1.341 .016 7 1.324 1.347 1.338 .007 * C-O C-O 1.231 .020 172 1.208 1.255 1.232 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 161 1.466 1.554 1.519 .015 +** * CH2G*-C (Gly) 1.516 .018 12 1.482 1.516 1.501 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.499 1.523 1.513 .009 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.526 1.584 1.558 .013 +* CH1E-CH2E (the rest) 1.530 .020 128 1.508 1.569 1.537 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.404 1.492 1.447 .016 +** +* NH1-CH2G* (Gly) 1.451 .016 12 1.417 1.465 1.438 .014 ** N-CH1E (Pro) 1.466 .015 7 1.444 1.472 1.458 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 2.0 153 112.71 119.33 116.14 .98 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 12 115.45 117.03 116.28 .52 CH1E-C-N (Pro) 116.9 1.5 7 115.89 116.58 116.24 .22 O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.22 125.21 123.07 .56 * * O-C-N (Pro) 122.0 1.4 7 122.64 123.25 122.86 .20 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.28 127.09 122.10 1.22 * +** C-NH1-CH2G* (Gly) 120.6 1.7 11 118.71 122.72 120.90 1.16 * * C-N-CH1E (Pro) 122.6 5.0 7 121.05 123.00 122.30 .61 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.78 122.08 120.77 .56 * CH2G*-C-O (Gly) 120.8 2.1 12 119.97 121.23 120.58 .34 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.50 110.71 110.26 .46 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 105.57 112.82 110.04 1.54 +* +* CH2E-CH1E-C (the rest) 110.1 1.9 128 105.53 114.53 110.57 1.53 ** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 102.81 115.59 110.02 1.87 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 12 109.74 114.32 111.74 1.43 N-CH1E-C (Pro) 111.8 2.5 7 109.93 113.21 111.68 1.20 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.62 111.37 110.15 .71 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.70 113.65 111.83 1.01 * * N-CH1E-CH2E (Pro) 103.0 1.1 7 102.74 104.99 103.87 .66 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.39 115.00 110.85 1.53 +* +** ------------------------------------------------------------------------------------------------------------- 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_7 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] 135 88.2% Residues in additional allowed regions [a,b,l,p] 15 9.8% 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 88.2 83.8 10.0 .4 Inside b. Omega angle st dev 172 3.8 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 99 .9 .8 .2 .5 Inside f. Overall G-factor 173 .0 -.4 .3 1.2 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 6.5 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 55 6.2 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 66 7.2 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 150 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 42 5.6 20.4 5.0 -3.0 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% 88.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_7 Page 17 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.45 Chi1-chi2 distribution -.25 Chi1 only .07 Chi3 & chi4 .31 Omega -.04 ------ -.15 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .41 ------ .22 ===== OVERALL AVERAGE -.03 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.