Residue-by-residue listing for 1abc 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 0.1 5.8 0.8 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 ----------------------------------------------------------------------------------------------------------------------------------- 1A PRO 1 e - - - - - - - - - - - 178.3 - 38.6 - * * 2A GLN 2 E B - 145.4 - 172.2 - - - - - - 179.9 - 24.3 - ** +** +** 3A ILE 3 E B - - -67.1 128.2 - - - - - - 182.6 -2.1 31.0 - +** +** 4A THR 4 B 76.0 - - - - - - - - - 188.6 - 34.9 - * * 5A LEU 5 S A - - -47.7 174.4 - - - - - - 177.4 - 27.8 - * +* +* 6A TRP 6 S A - - -40.7 - - - - - - - 179.3 - 28.5 - +* +* +* 7A GLN 7 S B - - -80.4 192.6 - - - - - - 175.5 - 32.3 - 8A ARG 8 B - - -93.4 176.8 - - - - - - 176.4 - 36.3 - +* +* 9A PRO 9 e - - - - - -62.0 - - - - - 181.6 - 40.4 - +* +* 10A LEU 10 E B - - -116.1 - - - - - - - 183.5 -3.2 34.9 - *** +* *** 11A VAL 11 E B 101.2 - - - - - - - - - 180.4 -2.7 38.2 - ** * ** 12A THR 12 E B - - -72.1 - - - - - - - 177.7 - 30.0 - * * 13A ILE 13 E B 79.1 - - 166.4 - - - - - - 176.8 -3.1 30.4 - * * * 14A ARG 14 E B - - -71.1 185.9 - - - - - - 179.5 -2.9 28.2 - * +* +* Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 15A ILE 15 E b - 171.2 - 175.8 - - - - - - 178.0 -1.9 25.9 - ** ** 16A GLY 16 T - - - - - - - - - - - 179.3 - - - 17A GLY 17 T - - - - - - - - - - - 178.9 - - - 18A GLN 18 E B - - -42.8 - - - - - - - 177.1 -0.7 30.4 - +* +* * +* 19A LEU 19 E B - - -75.4 - - - - - - - 180.5 - 24.9 - +** +** 20A LYS 20 E B - - -63.9 - - - - - - - 180.5 -2.3 32.9 - 21A GLU 21 E B - 222.7 - - - - - - - - 180.1 - 36.2 - ** ** 22A ALA 22 E B - - - - - - - - - - 179.2 -3.0 32.0 - * * 23A LEU 23 E B - 201.1 - - - - - - - - 173.8 -2.7 36.3 - * * * 24A LEU 24 E b - - -99.5 - - - - - - - 181.6 -2.3 34.0 - ** ** 25A ASP 25 e b - 183.4 - - - - - - - - 179.4 -1.5 35.8 - 26A THR 26 T A 69.9 - - - - - - - - - 177.7 -0.8 35.6 1 +* * +* 27A GLY 27 T - - - - - - - - - - - 178.7 - - 1 * * 28A ALA 28 B B - - - - - - - - - - 179.6 -1.4 31.1 - 29A ASP 29 S A - - -74.6 - - - - - - - 183.8 -2.2 37.6 - * * 30A ASP 30 S B - - -71.3 - - - - - - - 179.4 - 38.5 - * * 31A THR 31 e B - - -59.8 - - - - - - - 177.4 - 33.6 - 32A VAL 32 E B 26.5 - - - - - - - - - 176.7 -1.2 22.7 - ** * *** *** 33A LEU 33 E B - - -83.8 - - - - - - - 177.5 -3.3 31.7 - * +* +* 34A GLU 34 S B 60.1 - - 163.1 - - - - - - 180.6 - 39.2 - +* +* 35A GLU 35 S b - 207.1 - - - - - - - - 178.2 - 32.1 - * * 36A MET 36 B 69.2 - - 195.7 - - - - - - 178.1 - 31.0 - 37A ASN 37 B - - -81.3 - - - - - - - 177.9 - 24.1 - +** +** 38A LEU 38 B - - -45.8 147.8 - - - - - - 179.3 -0.5 29.4 - * +* ** * ** 39A PRO 39 S - - - - - -54.1 - - - - - 179.7 - 35.4 - * * 40A GLY 40 S - - - - - - - - - - - 177.8 - - - 41A LYS 41 B - - -48.1 - - - - - - - 179.4 - 35.8 - * * 42A TRP 42 B 65.7 - - - - - - - - - 179.4 - 29.1 - * * 43A LYS 43 E B 49.7 - - 208.2 - - - - - - 178.4 -1.5 28.5 - +* +* +* 44A PRO 44 E - - - - - -79.8 - - - - - 177.1 - 41.4 - * ** ** 45A LYS 45 E B - - -97.5 - - - - - - - 180.1 -1.3 33.7 - ** ** 46A MET 46 E B - 213.7 - 138.1 - - - - - - 174.9 - 37.1 1 +* ** * ** Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 47A ILE 47 E B 76.9 - - 176.6 - - - - - - 179.6 -1.0 33.8 - * * 48A GLY 48 E - - - - - - - - - - - 180.6 -1.8 - - 49A GLY 49 E - - - - - - - - - - - 177.4 -2.4 - - 50A ILE 50 T A 47.8 - - 195.1 - - - - - - 181.6 -0.6 26.6 1 * +* ** * ** 51A GLY 51 T - - - - - - - - - - - 182.6 -1.1 - - * * 52A GLY 52 E - - - - - - - - - - - 179.6 -0.7 - - +* +* 53A PHE 53 E B - - -84.9 - - - - - - - 178.2 - 34.1 - * * 54A ILE 54 E B 59.7 - - 171.3 - - - - - - 178.3 -2.2 29.7 - * * 55A LYS 55 E B - 190.9 - 159.2 - - - - - - 180.8 - 33.3 - 56A VAL 56 E b - - -81.9 - - - - - - - 179.7 -4.3 29.3 - * *** * *** 57A ARG 57 E B 99.8 - - 163.7 - - - - - - 184.4 -1.6 30.2 - ** * ** 58A GLN 58 E B - 191.6 - 177.8 - - - - - - 177.7 -4.0 37.6 - +** * +** 59A TYR 59 E B - - -64.2 - - - - - - - 180.6 -1.8 35.6 - 60A ASP 60 E B - - -76.9 - - - - - - - 180.4 -0.5 33.8 - +* +* 61A GLN 61 E ~l 71.6 - - 147.2 - - - - - - 176.9 - 22.8 - ** +* *** *** 62A ILE 62 E B - - -67.8 - - - - - - - 180.6 -1.4 39.1 - * * 63A PRO 63 E - - - - - -74.1 - - - - - 180.1 - 39.9 - +* +* 64A VAL 64 E B - 174.3 - - - - - - - - 178.0 -1.8 33.3 - 65A GLU 65 E B - 194.4 - 163.6 - - - - - - 182.1 -3.4 36.8 1 +* * +* 66A ILE 66 E b - - -50.4 - - - - - - - 181.4 -3.4 36.5 1 * +* * +* 67A ABA 67 e l 49.5 - - - - - - - - - 177.3 -1.0 23.1 1 * *** * *** 68A GLY 68 T - - - - - - - - - - - 178.7 - - - 69A HIS 69 E B - - -67.9 - - - - - - - 178.1 -0.6 29.6 - +* * +* 70A LYS 70 E B - - -98.8 - - - - - - - 178.4 -0.6 35.1 - ** +* ** 71A ALA 71 E B - - - - - - - - - - 176.5 -1.6 40.1 - +* +* 72A ILE 72 E b - - -59.0 155.2 - - - - - - 179.0 - 28.3 - * +* +* 73A GLY 73 E - - - - - - - - - - - 178.9 -2.4 - - 74A THR 74 E B - - -40.6 - - - - - - - 184.4 - 25.9 - +* ** ** 75A VAL 75 E B - 155.9 - - - - - - - - 180.3 -1.6 33.4 - +* +* 76A LEU 76 E B - - -62.7 186.9 - - - - - - 179.6 -3.6 39.0 - ** * ** 77A VAL 77 E B - - -31.6 - - - - - - - 180.2 -1.5 30.9 - ** ** 78A GLY 78 e - - - - - - - - - - - 182.6 -2.6 - - Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 79A PRO 79 - - - - - -78.4 - - - - - 180.0 - 36.5 - * * 80A THR 80 B - 174.4 - - - - - - - - 180.0 -1.6 29.8 - * * 81A PRO 81 S - - - - - -58.5 - - - - - 179.5 - 39.5 - +* +* 82A VAL 82 S B 47.0 - - - - - - - - - 178.9 - 33.0 - * * 83A ASN 83 e B - - -71.6 - - - - - - - 178.3 - 35.2 - 84A ILE 84 E B 77.3 - - 211.2 - - - - - - 175.7 -3.2 31.9 - +* +* +* 85A ILE 85 E B - - -60.3 - - - - - - - 180.4 -3.1 35.2 - * * 86A GLY 86 h - - - - - - - - - - - 177.4 -0.9 - - +* +* 87A ARG 87 H A - - -73.9 179.4 - -62.5 -11.6 - - - 181.2 -2.6 33.4 - ** ** 88A ASN 88 H A 81.1 - - - - -77.3 -33.8 - - - 179.1 - 31.0 1 * * * * 89A LEU 89 H A - - -30.5 186.9 - -100.8 -19.0 - - - 179.5 -1.2 29.6 - ** +** +* * * +** 90A LEU 90 H A - - -76.7 194.2 - -70.6 -33.3 - - - 178.0 -1.3 35.8 1 * * 91A THR 91 h A 52.7 - - - - - - - - - 182.9 -0.8 28.3 - +* +* +* 92A GLN 92 T A - - -68.8 182.5 - - - - - - 181.7 - 29.9 - * * 93A ILE 93 T A 88.9 - - 199.1 - - - - - - 182.6 -0.7 31.8 - +* * +* +* 94A GLY 94 T - - - - - - - - - - - 179.1 - - 1 * * 95A ABA 95 e B 97.3 - - - - - - - - - 179.6 -3.9 28.9 2 ** +** * ** +** 96A THR 96 E B 65.2 - - - - - - - - - 177.1 -1.6 34.5 - 97A LEU 97 E B - - -82.0 173.2 - - - - - - 181.5 -2.4 32.1 - * * 98A ASN 98 E B - - -62.2 - - - - - - - 180.5 -2.8 34.3 - * * 99A PHE 99 e - 63.7 - - - - - - - - - - -1.5 29.8 - * * 100B PRO 1 e - - - - - - - - - - - 176.6 - 42.4 - ** ** 101B GLN 2 E B - 184.1 - 182.5 - - - - - - 180.8 - 30.3 - * * 102B ILE 3 E B - - -66.6 160.2 - - - - - - 178.5 -3.1 37.1 - * * 103B THR 4 E B 60.7 - - - - - - - - - 180.3 - 28.2 - +* +* 104B LEU 5 e A - - -93.6 - - - - - - - 178.0 -0.6 33.4 - +* +* +* 105B TRP 6 S A - - -58.2 - - - - - - - 179.6 - 31.4 - 106B GLN 7 S B - - -54.5 - - - - - - - 179.1 - 27.8 1 +* * +* 107B ARG 8 B - - -58.1 188.6 - - - - - - 180.0 - 36.7 - 108B PRO 9 e - - - - - -72.7 - - - - - 179.4 - 31.5 - 109B LEU 10 E B - - -84.9 - - - - - - - 183.2 -2.4 31.6 - * * Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 110B VAL 11 E B - 161.1 - - - - - - - - 178.4 -2.3 38.7 - * * * 111B THR 12 E B - - -43.5 - - - - - - - 177.8 - 29.9 - +* * +* 112B ILE 13 E B 70.7 - - 179.1 - - - - - - 176.8 -1.8 35.8 - 113B ARG 14 E B - 154.4 - 196.4 - - - - - - 178.5 -0.7 33.1 - +* * +* +* 114B ILE 15 E B - - -24.2 - - - - - - - 182.5 -2.3 34.9 - +** +** 115B GLY 16 T - - - - - - - - - - - 177.9 - - - 116B GLY 17 T - - - - - - - - - - - 182.5 - - 1 * * 117B GLN 18 E B - - -95.7 - - - - - - - 177.0 -1.1 28.5 - +* * +* +* 118B LEU 19 E B - 213.2 - - - - - - - - 182.1 - 30.9 - +* +* 119B LYS 20 E B - - -67.3 158.1 - - - - - - 177.9 -3.3 33.6 - * +* +* 120B GLU 21 E B - - -82.2 187.2 - - - - - - 180.9 - 29.8 - * * * 121B ALA 22 E B - - - - - - - - - - 175.9 -2.1 32.7 - 122B LEU 23 E B - 174.0 - - - - - - - - 174.7 -3.7 34.7 - ** ** 123B LEU 24 E B - - -100.4 - - - - - - - 181.1 -2.4 36.6 - ** ** 124B ASP 25 e b - 174.8 - - - - - - - - 176.6 -2.3 35.1 - 125B THR 26 T A 57.4 - - - - - - - - - 177.5 - 29.2 1 * * * 126B GLY 27 T - - - - - - - - - - - 179.2 - - 1 * * 127B ALA 28 B B - - - - - - - - - - 177.9 -2.1 34.7 - 128B ASP 29 S A - - -59.7 - - - - - - - 181.5 -0.8 28.7 - +* * +* 129B ASP 30 S B - - -56.1 - - - - - - - 179.0 - 32.3 - 130B THR 31 e B - - -62.7 - - - - - - - 179.5 - 32.8 - 131B VAL 32 E B 23.3 - - - - - - - - - 179.2 -1.7 24.5 - +** +** +** 132B LEU 33 E B - - -54.2 181.0 - - - - - - 179.6 -2.6 33.3 - 133B GLU 34 B - 205.8 - 218.7 - - - - - - 181.0 - 33.1 1 * ** * ** 134B GLU 35 S B - - -57.8 - - - - - - - 178.6 - 28.3 - +* +* 135B MET 36 B 80.3 - - 189.9 - - - - - - 182.0 - 29.7 - * * * 136B ASN 37 b - 223.7 - - - - - - - - 179.9 - 32.5 - ** ** 137B LEU 38 B - - -66.3 185.9 - - - - - - 176.4 -0.8 30.1 - +* * +* 138B PRO 39 - - - - - -74.0 - - - - - 179.4 - 38.6 - * * 139B GLY 40 S - - - - - - - - - - - 177.7 - - - 140B LYS 41 B 33.6 - - 130.9 - - - - - - 178.2 - 35.3 1 +* +** * +** 141B TRP 42 B 57.4 - - - - - - - - - 178.1 - 32.0 - 142B LYS 43 E B - - -44.1 167.6 - - - - - - 177.3 -1.2 34.8 - +* * +* Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 143B PRO 44 E - - - - - -82.0 - - - - - 176.8 - 36.6 - * * 144B LYS 45 E b 44.5 - - 141.8 - - - - - - 182.9 -1.7 24.6 - * +* +** +** 145B MET 46 E B - - -72.8 188.1 - - - - - - 178.7 - 32.4 - 146B ILE 47 E B 43.1 - - - - - - - - - 180.1 -2.1 29.4 - * * * 147B GLY 48 E - - - - - - - - - - - 180.3 -2.8 - - * * 148B GLY 49 E - - - - - - - - - - - 181.3 -1.9 - 1 * * 149B ILE 50 T B - - -57.3 - - - - - - - 175.7 - 37.3 - 150B GLY 51 T - - - - - - - - - - - 177.5 - - - 151B GLY 52 E - - - - - - - - - - - 181.0 -2.0 - - 152B PHE 53 E B - - -78.7 - - - - - - - 176.1 - 36.7 - 153B ILE 54 E B 67.0 - - 148.4 - - - - - - 181.5 -2.1 30.7 - +* +* 154B LYS 55 E B - 201.4 - 171.2 - - - - - - 183.1 - 28.5 - * +* +* 155B VAL 56 E B - - -73.3 - - - - - - - 181.1 -3.8 31.0 - ** ** 156B ARG 57 E B - - -71.1 178.8 - - - - - - 180.4 -2.5 33.5 - 157B GLN 58 E B - 179.8 - 199.5 - - - - - - 177.3 -3.5 35.8 1 * +* * +* 158B TYR 59 E B - - -64.2 - - - - - - - 182.2 -2.7 33.8 - 159B ASP 60 E B - - -80.0 - - - - - - - 179.7 - 28.9 - * * 160B GLN 61 E l - - -73.2 207.2 - - - - - - 181.7 - 32.8 - +* +* 161B ILE 62 E B - - -50.3 217.0 - - - - - - 176.9 -3.2 29.6 - * ** +* * ** 162B PRO 63 E - - - - - -69.4 - - - - - 180.2 - 36.1 - 163B VAL 64 E B - 185.9 - - - - - - - - 180.4 -2.7 33.7 - 164B GLU 65 E b - 162.5 - 155.7 - - - - - - 182.3 - 27.9 - * * +* +* 165B ILE 66 E B - 143.9 - - - - - - - - 180.2 -2.8 23.6 1 ** * +** * +** 166B ABA 67 T l 49.3 - - - - - - - - - 175.5 -2.3 26.5 1 ** * ** 167B GLY 68 T - - - - - - - - - - - 176.2 - - - 168B HIS 69 E B - - -62.7 - - - - - - - 181.1 -2.3 38.4 - * * 169B LYS 70 E B - - -33.0 139.7 - - - - - - 178.5 -0.6 34.0 - ** ** +* ** 170B ALA 71 E B - - - - - - - - - - 181.0 -3.8 27.6 - ** +* ** 171B ILE 72 E B - 203.4 - - - - - - - - 180.9 - 34.4 - * * 172B GLY 73 E - - - - - - - - - - - 179.0 -1.5 - - 173B THR 74 E B - - -49.1 - - - - - - - 183.6 - 32.7 - * * 174B VAL 75 E B - 145.4 - - - - - - - - 180.4 -2.2 35.8 - ** ** 175B LEU 76 E B - - -62.7 202.4 - - - - - - 179.8 -2.3 38.6 - * * * 176B VAL 77 E B - 176.2 - - - - - - - - 182.1 -3.0 28.4 - * +* +* Residue-by-residue listing for 1abc Page 7 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 177B GLY 78 e - - - - - - - - - - - 182.4 -2.1 - - 178B PRO 79 S - - - - - -76.8 - - - - - 178.9 - 35.8 - * * 179B THR 80 B - 166.9 - - - - - - - - 182.4 -2.3 37.9 - * * 180B PRO 81 S - - - - - -73.3 - - - - - 179.9 - 37.9 - * * 181B VAL 82 S B - 191.7 - - - - - - - - 175.6 - 34.2 - 182B ASN 83 E B - - -58.2 - - - - - - - 180.1 -0.5 28.4 - ** +* ** 183B ILE 84 E B - - -36.5 201.3 - - - - - - 177.4 -3.2 38.3 - ** * +* * ** 184B ILE 85 E B - - -54.6 - - - - - - - 182.8 -2.9 30.6 - * * 185B GLY 86 h - - - - - - - - - - - 180.9 -0.6 - - +* +* 186B ARG 87 H A - - -64.2 177.5 - -67.2 -9.1 - - - 182.9 -2.6 38.2 - +** * +** 187B ASN 88 H A 74.3 - - - - -59.8 -39.8 - - - 182.7 - 25.7 - ** ** 188B LEU 89 H A - - -110.3 - - -101.1 -26.7 - - - 180.3 -1.0 31.8 - +** *** * * *** 189B LEU 90 H A - - -55.8 167.9 - -61.6 -32.5 - - - 182.7 -1.7 28.4 - +* +* 190B THR 91 H A 67.1 - - - - -65.6 -24.9 - - - 180.8 -1.7 30.1 - * * * 191B GLN 92 H A - - -74.8 178.1 - -83.7 -24.8 - - - 176.4 -1.5 32.0 - +* * +* 192B ILE 93 H A 78.7 - - 190.3 - -87.9 -26.5 - - - 175.1 -0.8 27.1 1 +* * +* +* * +* 193B GLY 94 h - - - - - - - - - - - 180.6 -1.4 - 1 * * 194B ABA 95 t B - 197.0 - - - - - - - - 177.1 -2.3 33.0 2 ** ** 195B THR 96 E B - - -32.6 - - - - - - - 172.8 -2.8 30.9 - ** * * ** 196B LEU 97 E B - - -94.0 - - - - - - - 179.8 -3.1 31.7 - +* * +* 197B ASN 98 E B - - -71.9 - - - - - - - 176.7 -2.2 36.3 - 198B PHE 99 e - 56.6 - - - - - - - - - - -1.2 29.3 - * * * 199C SER 1 - - - -55.9 - - - - - - - 179.9 - 30.6 - 200C LEU 2 B B - - -88.9 - - - - - - - 182.4 - 30.0 - * * * 201C ASN 3 B b - - -49.2 - - - - - - - 179.8 -2.2 32.5 1 * * * 202C PHE 4 - - - -69.8 - - - - - - - - -1.1 32.3 1 * * * 203C PRO 6 - - - - - - - - - - - 175.1 - 41.2 - ** ** 204C ILE 7 B B - - -56.5 - - - - - - - 182.6 -1.5 25.8 - ** ** 205C VAL 8 B - 113.0 - - - - - - - - - - -2.1 32.5 - *** *** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** *** ** *** +** * *** +** * *** *** ** *** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for 1abc Page 8 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 65.5 183.5 -66.4 176.9 -71.3 -76.2 -25.7 - - - 179.4 -2.0 32.5 * * Standard deviations: 19.7 22.3 18.5 20.9 8.7 15.2 9.5 - - - 2.3 0.9 4.1 Numbers of values: 39 32 87 59 12 11 11 0 0 0 201 121 179 28 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 1abc Page 9 ---------------------------------------- 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 - - - - - - - - - - ( 0.020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( 0.016) ( 0.015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( 0.014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( 0.018) ( 0.016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( 0.021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( 0.033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( 0.027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( 0.019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( 0.020) ( 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 ----------------------------------------------------------------------------------------------------------------------------------- 1A PRO 1 - 1.242 1.516 1.515 1.464 - 116.17 116.50 110.93 111.72 102.81 127.32 +** +*** +*** 2A GLN 2 1.320 1.237 1.503 1.462 1.487 117.31 115.43 122.24 125.94 100.74 112.42 122.03 * *** +* ** *8.3* +*** * *8.3* 3A ILE 3 1.300 1.225 1.543 1.551 1.485 121.53 112.50 124.70 116.35 100.85 112.29 122.80 ** * +* ** *** +*** +*** 4A THR 4 1.285 1.233 1.521 1.556 1.461 133.90 115.15 116.07 120.21 108.60 99.88 128.50 *** *6.8* +** *5.0* *6.8* *** *6.8* 5A LEU 5 1.350 1.243 1.492 1.538 1.455 117.59 115.86 112.72 120.03 119.98 104.38 131.23 +* +* ** *4.8* *5.2* *** +*** *5.1* *5.2* 6A TRP 6 1.318 1.235 1.520 1.525 1.439 121.13 116.40 113.49 112.48 104.02 119.07 130.11 **** * +** *5.0* **** *5.0* 7A GLN 7 1.326 1.237 1.534 1.485 1.490 118.29 115.65 118.98 105.39 106.27 118.29 125.15 ** +* +* * ** +* *4.6* * *4.6* 8A ARG 8 1.332 1.245 1.545 1.528 1.478 119.66 117.06 117.16 106.20 108.58 111.47 125.72 * * ** ** +* ** 9A PRO 9 1.339 1.257 1.534 1.495 1.468 123.97 118.98 124.33 108.09 113.38 102.43 116.69 * +* * ** * +*** +*** 10A LEU 10 1.314 1.200 1.531 1.503 1.470 125.59 110.48 117.71 104.80 114.25 113.30 131.42 * +* * ** +** +* +** * +* *5.3* *5.3* 11A VAL 11 1.292 1.253 1.524 1.571 1.447 128.97 110.92 127.46 117.52 114.55 96.67 121.62 +** * * **** +** +*** +*** * *8.7* *8.7* Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 12A THR 12 1.317 1.252 1.535 1.573 1.464 123.18 109.96 118.25 111.35 109.25 115.96 131.77 * * *** * * +** *5.5* *5.5* 13A ILE 13 1.356 1.253 1.536 1.548 1.479 116.85 113.33 120.48 114.83 109.05 111.85 126.16 +* * * +** * +** +* +** 14A ARG 14 1.333 1.234 1.538 1.500 1.477 117.90 112.45 117.84 106.06 100.09 126.13 129.70 * * ** +* +* ** +*** * 9.2* **** * 9.2* 15A ILE 15 1.286 1.217 1.507 1.559 1.499 115.81 114.14 121.30 123.68 97.21 115.07 124.07 *** ** *** * *6.6* *5.0* ** *6.6* 16A GLY 16 1.329 1.247 1.519 - 1.454 125.34 110.85 124.74 - 124.24 - 124.40 +** +** +* **** **** 17A GLY 17 1.328 1.259 1.514 - 1.441 126.47 117.43 115.27 - 110.68 - 127.29 * *** +** +** *** 18A GLN 18 1.332 1.255 1.543 1.511 1.496 119.12 115.05 124.08 112.30 110.02 113.44 120.75 * +* * +* * +* * +* 19A LEU 19 1.313 1.219 1.589 1.474 1.457 125.14 108.96 122.91 108.57 99.88 128.67 128.12 * *** +** +* +*** * **** *10.7* *** *10.7* 20A LYS 20 1.306 1.235 1.534 1.509 1.447 124.98 113.58 122.49 113.68 104.37 110.54 123.85 +* * +* * +* ** ** 21A GLU 21 1.282 1.232 1.548 1.534 1.432 134.54 114.97 117.02 104.27 106.92 114.16 127.96 *** * * *7.1* ** *** +* ** *** *7.1* 22A ALA 22 1.337 1.255 1.542 1.521 1.462 116.88 105.96 122.71 108.07 107.44 116.46 131.28 * +** *5.1* * +* * **** *5.2* *5.2* 23A LEU 23 1.328 1.228 1.517 1.527 1.458 120.60 114.93 119.56 110.73 112.47 106.38 125.50 ** +* ** 24A LEU 24 1.302 1.219 1.544 1.530 1.459 126.00 117.71 130.50 118.88 105.24 103.19 111.77 +* ** *5.7* *4.6* ** **** *7.0* *7.0* 25A ASP 25 1.306 1.269 1.517 1.554 1.456 129.25 114.22 124.93 115.87 118.30 100.31 120.85 +* +* * **** ** *** +** *6.0* * *6.0* 26A THR 26 1.346 1.209 1.520 1.573 1.463 121.20 123.33 119.78 109.55 110.64 109.60 116.88 * * * +*** * +*** +*** 27A GLY 27 1.282 1.249 1.529 - 1.447 131.85 116.59 116.84 - 109.66 - 126.56 *** *6.6* +* ** *6.6* 28A ALA 28 1.312 1.234 1.523 1.541 1.456 126.20 116.55 120.71 107.31 109.72 118.03 122.69 * ** ** *5.1* *5.1* 29A ASP 29 1.307 1.212 1.537 1.529 1.467 122.86 117.07 122.11 103.91 112.02 111.29 120.39 +* *** +* *** 30A ASP 30 1.310 1.226 1.520 1.544 1.449 127.10 112.65 120.65 109.73 114.84 104.13 126.68 * +** +* * +*** ** +*** 31A THR 31 1.345 1.248 1.532 1.571 1.474 116.98 113.40 120.78 113.86 106.13 109.37 125.81 * * +** * ** +* * +* +** 32A VAL 32 1.331 1.223 1.525 1.505 1.475 119.94 111.52 123.45 122.02 108.90 114.32 125.00 * ** +* *5.9* +* * *5.9* 33A LEU 33 1.335 1.229 1.538 1.535 1.452 124.12 109.70 130.33 115.88 109.33 108.79 119.94 * *** *5.6* *** * +* *5.6* 34A GLU 34 1.309 1.254 1.533 1.509 1.456 125.25 116.19 116.10 101.57 100.44 112.04 127.54 * * * +* +** **** +*** +** **** 35A GLU 35 1.308 1.234 1.515 1.535 1.479 120.27 118.10 121.82 109.90 118.04 110.72 120.08 +* * ** +* ** 36A MET 36 1.313 1.256 1.543 1.498 1.464 128.24 111.66 121.10 108.75 107.95 116.86 127.24 * * +* +*** ** * +*** +** +*** 37A ASN 37 1.336 1.228 1.546 1.517 1.483 116.07 110.28 122.68 117.93 102.02 120.67 126.95 * * *** +** * **** *** *6.0* ** *6.0* 38A LEU 38 1.315 1.244 1.561 1.510 1.452 124.20 109.66 123.04 110.87 103.47 118.88 127.18 * +* * * *** * +** *4.9* +** *4.9* Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 39A PRO 39 1.332 1.242 1.523 1.537 1.475 119.03 119.20 122.47 117.22 109.23 101.81 118.32 +* +*** * * +** +*** 40A GLY 40 1.316 1.243 1.526 - 1.452 128.48 112.85 130.04 - 117.64 - 117.06 *4.6* +* **** +* +*** *4.6* 41A LYS 41 1.320 1.260 1.517 1.517 1.468 128.49 121.67 119.91 113.63 102.98 106.11 118.32 * +*** +** +* +** +** +** +*** 42A TRP 42 1.305 1.261 1.538 1.514 1.475 123.99 112.48 125.58 116.67 105.91 112.68 121.94 +* * * +* +** *** +* * *** 43A LYS 43 1.318 1.219 1.516 1.491 1.473 118.71 114.49 115.72 115.71 98.60 117.43 129.68 +* +* +** +** **** **** **** **** 44A PRO 44 1.311 1.264 1.531 1.532 1.467 121.03 121.33 110.74 106.39 107.66 103.79 127.92 +* +* +** *5.9* +* +* **** *5.9* 45A LYS 45 1.287 1.238 1.526 1.548 1.467 124.68 113.00 126.39 106.07 116.20 113.46 120.54 +** +* +* *** ** +* +* +* *** 46A MET 46 1.327 1.237 1.498 1.527 1.449 125.58 115.78 121.71 109.40 123.60 103.59 122.25 * ** **** **** **** 47A ILE 47 1.320 1.240 1.559 1.579 1.499 127.75 118.29 122.00 113.59 111.03 107.60 119.68 +* * ** *** * ** ** ** *** 48A GLY 48 1.320 1.237 1.511 - 1.476 123.67 116.41 117.59 - 109.82 - 125.99 +* +* +* +* +* 49A GLY 49 1.328 1.255 1.541 - 1.513 120.90 120.40 112.49 - 107.85 - 127.08 * * +*** +* +*** +* +** +*** 50A ILE 50 1.340 1.250 1.564 1.576 1.459 117.26 122.23 113.96 103.74 106.86 128.41 123.81 +* * ** *** **** ** +* * 9.9* * 9.9* 51A GLY 51 1.307 1.252 1.507 - 1.470 121.92 120.17 120.46 - 122.37 - 119.36 +* * * +* *** ** *** 52A GLY 52 1.312 1.265 1.536 - 1.485 127.37 117.25 119.14 - 106.96 - 123.60 * +* * ** +*** +* +*** 53A PHE 53 1.329 1.206 1.522 1.549 1.484 124.68 117.19 121.73 106.02 118.52 112.10 120.96 * * +* ** +** * +** 54A ILE 54 1.319 1.226 1.546 1.579 1.436 130.67 109.33 122.23 102.39 106.47 125.81 128.40 * * *5.0* *** *** +* *8.4* *** *8.4* 55A LYS 55 1.298 1.265 1.541 1.546 1.448 123.61 114.60 116.96 107.17 107.12 115.85 128.41 ** +* * ** +* * *** *** *** 56A VAL 56 1.325 1.235 1.511 1.551 1.496 117.34 120.30 118.66 116.87 108.79 111.43 121.04 +* ** ** * +*** * +*** 57A ARG 57 1.303 1.220 1.509 1.502 1.515 119.69 120.17 118.65 120.37 97.09 109.99 120.83 +* * +** * +* * *5.4* *5.0* * *5.4* 58A GLN 58 1.275 1.237 1.522 1.562 1.416 135.11 113.19 123.54 106.67 119.78 107.35 123.02 +*** +* ** *7.4* +* +* +* *** +* *7.4* 59A TYR 59 1.323 1.204 1.512 1.517 1.444 127.22 113.43 125.37 106.19 112.33 111.99 121.08 * *** * +** ** * *** 60A ASP 60 1.296 1.223 1.527 1.537 1.452 129.15 111.46 122.73 112.94 114.08 107.28 125.59 ** **** ** * * * +* +* **** 61A GLN 61 1.318 1.231 1.542 1.532 1.438 129.93 111.06 129.09 117.52 109.64 118.59 119.74 * *4.6* +** *4.9* +*** *4.8* ** *4.9* 62A ILE 62 1.335 1.220 1.531 1.576 1.442 132.24 120.27 113.81 105.91 108.13 108.64 125.92 * *5.9* ** **** * * +* +* *5.9* 63A PRO 63 1.314 1.262 1.503 1.554 1.473 128.07 121.84 114.76 107.17 114.18 104.92 123.34 +* +* * * * *** +*** +* +* +*** 64A VAL 64 1.327 1.221 1.507 1.528 1.477 115.31 120.29 112.31 110.68 102.65 113.55 127.36 +*** ** *5.0* *** * +** *5.0* 65A GLU 65 1.303 1.242 1.522 1.519 1.489 119.86 119.30 116.24 106.87 108.02 110.12 124.42 +* +* * +* +** +* * +** Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 66A ILE 66 1.313 1.245 1.530 1.566 1.444 123.26 - 117.16 103.67 114.69 112.96 - * ** ** * ** 67A GLY 68 - 1.266 1.512 - 1.432 - 118.58 114.93 - 111.13 - 126.41 +* * * +** ** +** 68A HIS 69 1.320 1.250 1.530 1.534 1.464 114.64 110.96 122.16 108.11 97.96 123.30 126.86 +*** +** * *4.7* *7.5* ** *7.5* 69A LYS 70 1.287 1.244 1.543 1.522 1.462 122.21 113.74 121.37 111.72 111.60 107.24 124.72 +** * +* * +** 70A ALA 71 1.320 1.242 1.522 1.546 1.443 129.70 128.38 113.33 109.79 109.92 102.73 118.24 **** *6.1* **** *5.1* +** *6.1* 71A ILE 72 1.291 1.237 1.544 1.581 1.438 132.56 119.80 113.95 106.52 106.56 124.12 126.22 +** +* * *6.0* +* **** * +* *7.4* ** *7.4* 72A GLY 73 1.314 1.263 1.504 - 1.446 120.50 111.40 122.72 - 118.40 - 125.88 * +* ** ** +* ** 73A THR 74 1.344 1.270 1.524 1.558 1.504 119.57 109.22 127.49 118.05 101.89 118.32 123.04 * +* ** * *** +*** **** *** **** **** 74A VAL 75 1.314 1.248 1.559 1.559 1.448 127.10 112.79 118.35 111.70 100.07 113.50 128.80 * +* *** +* * * +*** * +*** +*** 75A LEU 76 1.320 1.251 1.520 1.519 1.449 125.94 116.85 118.38 109.70 114.51 103.26 124.76 * ** * * **** * **** 76A VAL 77 1.316 1.223 1.539 1.525 1.474 119.04 110.48 117.50 109.12 108.49 116.72 132.01 * +** +* *** *5.6* *5.6* 77A GLY 78 1.328 1.247 1.535 - 1.458 122.49 114.91 118.86 - 109.41 - 126.09 * * * +* +* 78A PRO 79 1.338 1.236 1.519 1.550 1.443 125.79 119.96 117.05 109.87 117.10 106.13 122.99 +* ** ** ** +** +** 79A THR 80 1.287 1.241 1.517 1.586 1.462 124.48 118.08 121.58 116.49 108.90 111.63 120.28 +** +* +* *** +* *** 80A PRO 81 1.313 1.233 1.525 1.539 1.456 123.64 117.06 122.47 106.75 114.14 105.70 120.34 +* +* ** * ** 81A VAL 82 1.304 1.243 1.540 1.519 1.478 127.57 113.81 124.81 115.89 103.92 108.21 121.32 +* * *** * ** *** +** +* * *** 82A ASN 83 1.306 1.259 1.536 1.519 1.436 130.40 118.00 114.20 109.94 107.51 110.10 127.73 +* * * *4.8* +*** * +** *4.8* 83A ILE 84 1.324 1.274 1.514 1.567 1.496 114.56 116.62 125.93 117.87 113.87 104.81 117.31 ** ** +*** *** +*** +*** +*** +*** 84A ILE 85 1.316 1.271 1.554 1.564 1.480 124.64 119.23 120.53 111.17 102.92 110.06 120.24 +* * * +* +* +** +* +** 85A GLY 86 1.321 1.230 1.513 - 1.452 122.48 115.70 120.87 - 112.24 - 123.43 * * 86A ARG 87 1.316 1.257 1.552 1.527 1.457 127.39 118.39 115.64 105.20 111.07 116.10 125.96 * * *** * *** +** *** +* *** 87A ASN 88 1.326 1.250 1.528 1.545 1.464 122.67 116.63 120.32 111.33 113.19 112.86 122.94 * * 88A LEU 89 1.318 1.240 1.536 1.504 1.451 123.74 119.60 118.06 112.63 109.24 114.68 122.34 * * +* +* * ** ** 89A LEU 90 1.317 1.255 1.534 1.512 1.475 125.45 109.39 127.98 114.00 115.24 102.65 122.59 * ** *** **** ** * *4.6* *4.6* 90A THR 91 1.348 1.251 1.552 1.577 1.443 119.14 116.45 119.62 111.21 108.21 118.94 123.93 * * * * * * **** **** 91A GLN 92 1.312 1.251 1.528 1.519 1.473 117.13 116.66 113.70 111.29 110.09 115.28 129.40 * +** **** +** **** **** 92A ILE 93 1.321 1.246 1.527 1.564 1.486 119.14 114.12 120.11 114.84 107.79 110.48 125.72 * * * +** * +* +** Residue-by-residue listing for 1abc 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 ----------------------------------------------------------------------------------------------------------------------------------- 93A GLY 94 1.319 1.264 1.532 - 1.463 128.09 - 118.11 - 114.65 - - +* **** * **** 94A THR 96 - 1.250 1.523 1.588 1.490 - 127.17 110.86 112.89 111.28 107.63 121.92 +* +* *5.5* *5.8* +* ** *5.8* 95A LEU 97 1.308 1.236 1.530 1.477 1.467 126.14 117.62 124.05 111.37 105.14 113.42 118.31 * +** ** +* ** +* +** +** 96A ASN 98 1.280 1.225 1.520 1.528 1.476 129.17 118.58 116.83 114.76 109.65 105.91 124.58 +*** **** * ** ** +** **** 97A PHE 99 1.296 1.267 1.550 1.518 1.464 128.46 - 118.72 110.55 110.33 115.96 - ** +* * +*** * *** +*** 98B PRO 1 - 1.243 1.522 1.541 1.454 - 109.51 128.88 106.57 117.51 101.50 121.60 *4.9* *4.8* +* ** * *4.9* 99B GLN 2 1.326 1.240 1.548 1.504 1.483 124.83 118.65 109.42 109.01 98.04 120.75 131.82 * * * +* * *6.7* *4.7* *6.0* *5.5* *6.7* 100B ILE 3 1.308 1.225 1.520 1.586 1.483 117.75 120.07 116.01 108.79 112.53 107.83 123.89 * +* * ** +* +** ** +** 101B THR 4 1.326 1.283 1.541 1.568 1.465 122.16 113.82 120.87 113.45 109.99 115.93 125.30 +** * * +* +** * +** 102B LEU 5 1.352 1.252 1.528 1.559 1.454 123.90 120.20 120.36 115.94 120.84 102.13 119.41 +* * * * +* *** *** *4.9* ** *4.9* 103B TRP 6 1.319 1.250 1.538 1.538 1.478 128.88 114.83 122.02 107.95 107.72 117.52 123.14 * +*** * * **** **** 104B GLN 7 1.324 1.234 1.506 1.527 1.487 116.45 120.11 119.91 119.86 107.41 110.91 119.96 +* +** +* *5.1* * +* *5.1* 105B ARG 8 1.310 1.268 1.493 1.517 1.510 118.26 120.54 117.35 113.90 108.77 103.11 122.11 * +* +* +** +* ** ** +* **** **** 106B PRO 9 1.326 1.213 1.512 1.520 1.481 119.44 120.18 116.39 119.29 115.51 102.76 123.38 ** +** *4.8* * *4.8* 107B LEU 10 1.344 1.229 1.522 1.525 1.464 127.64 117.57 117.86 106.08 112.93 117.12 124.25 * *** +* ** +*** +*** 108B VAL 11 1.299 1.250 1.528 1.565 1.471 123.39 116.66 122.01 116.62 110.47 97.43 121.29 ** *** *8.3* * *8.3* 109B THR 12 1.329 1.236 1.535 1.574 1.469 119.50 110.67 120.87 110.62 105.76 118.31 128.23 * * +** +* **** *** **** 110B ILE 13 1.292 1.240 1.538 1.575 1.435 134.52 113.70 122.06 104.07 107.89 115.37 123.96 +** * * *7.1* * ** * ** *7.1* 111B ARG 14 1.309 1.234 1.514 1.527 1.484 118.80 118.34 116.58 112.06 110.83 109.94 125.00 * * +* * ** * * ** 112B ILE 15 1.308 1.252 1.531 1.559 1.479 120.23 112.62 118.14 107.18 107.60 113.41 129.18 * * * +* +* * * +*** +*** 113B GLY 16 1.331 1.273 1.548 - 1.510 114.63 114.31 120.60 - 98.93 - 125.04 ** +* +*** +*** *4.7* * *4.7* 114B GLY 17 1.315 1.241 1.525 - 1.494 115.24 110.61 128.07 - 107.60 - 121.32 +** *** +** *** +* * *** 115B GLN 18 1.314 1.244 1.522 1.521 1.472 123.31 109.12 124.39 116.18 112.81 111.06 126.49 * +*** ** *** ** +*** 116B LEU 19 1.338 1.243 1.516 1.513 1.480 118.92 121.79 113.63 124.12 97.28 104.82 124.39 * +* +** **** *7.4* *5.0* *** *7.4* 117B LYS 20 1.303 1.257 1.527 1.550 1.484 123.31 117.18 125.33 114.10 115.00 105.88 117.37 +* * * +** ** * +** +*** +*** 118B GLU 21 1.324 1.258 1.539 1.505 1.482 122.94 114.95 119.14 106.25 105.95 121.61 125.83 * * * ** +* *6.5* +* *6.5* 119B ALA 22 1.313 1.224 1.514 1.544 1.483 118.99 121.31 116.72 114.12 109.70 109.02 121.97 * * +* +** ** ** +** Residue-by-residue listing for 1abc Page 14 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 120B LEU 23 1.290 1.240 1.509 1.522 1.465 123.46 118.76 119.91 112.10 109.31 108.27 121.32 +** * * * * +** 121B LEU 24 1.333 1.273 1.548 1.516 1.498 120.02 116.59 118.03 111.75 110.61 104.81 125.00 ** * ** +* *** * *** 122B ASP 25 1.323 1.240 1.505 1.520 1.464 116.09 108.58 127.96 113.77 122.66 101.49 123.08 *** +*** **** +* **** *5.3* *5.3* 123B THR 26 1.338 1.258 1.519 1.558 1.487 122.21 124.82 114.37 117.65 108.75 110.82 120.60 * +* **** +*** +*** * **** 124B GLY 27 1.309 1.264 1.521 - 1.449 126.61 118.66 122.31 - 113.09 - 118.93 * +* +*** * +** +*** 125B ALA 28 1.349 1.258 1.498 1.533 1.455 123.10 117.63 116.13 108.62 109.76 111.80 125.95 * * * +** * +* +** 126B ASP 29 1.306 1.249 1.528 1.525 1.475 119.27 117.33 110.56 107.50 107.87 121.48 132.11 +* * *6.0* * * *6.5* *5.7* *6.5* 127B ASP 30 1.307 1.244 1.536 1.523 1.454 121.64 109.17 118.33 108.67 109.34 114.94 132.48 +* +*** * +** *5.9* *5.9* 128B THR 31 1.368 1.245 1.529 1.558 1.481 118.21 115.27 119.64 111.71 101.32 114.06 125.03 +** * +* * +*** +* * +*** 129B VAL 32 1.283 1.238 1.520 1.538 1.444 128.96 112.90 126.66 124.36 108.68 110.27 120.39 *** **** +* *** *6.9* +* *6.9* 130B LEU 33 1.326 1.224 1.525 1.544 1.464 122.65 112.66 121.20 116.37 104.60 107.48 126.07 +* *** ** +* +* *** 131B GLU 34 1.323 1.253 1.535 1.496 1.460 115.59 113.12 119.35 103.85 106.69 118.74 127.53 * +* *** +* *** +* *4.8* +** *4.8* 132B GLU 35 1.322 1.238 1.538 1.515 1.472 118.31 107.99 131.27 113.77 108.19 115.84 120.66 +* **** *6.2* +* * *** * *6.2* 133B MET 36 1.297 1.232 1.555 1.500 1.432 134.23 106.85 128.22 114.32 106.00 114.15 124.93 ** * * * *7.0* *4.7* **** ** +* ** * *7.0* 134B ASN 37 1.331 1.228 1.518 1.560 1.485 121.49 117.19 117.62 114.96 117.46 105.51 125.19 +* * +* +** ** +** * +** 135B LEU 38 1.332 1.234 1.543 1.516 1.472 117.64 111.48 122.29 110.14 109.67 116.18 126.23 ** ** *** ** *** 136B PRO 39 1.312 1.252 1.531 1.526 1.473 120.09 116.60 121.35 111.04 103.67 103.88 121.97 +* * *** *** 137B GLY 40 1.297 1.243 1.540 - 1.466 121.26 108.68 125.02 - 106.21 - 126.26 ** * +*** ** ** ** +*** 138B LYS 41 1.308 1.252 1.540 1.516 1.448 125.20 111.95 119.74 108.72 102.99 111.92 128.31 * * +* ** +** *** *** 139B TRP 42 1.323 1.238 1.523 1.543 1.465 121.54 112.19 123.05 111.98 111.48 111.63 124.75 ** * * ** 140B LYS 43 1.321 1.234 1.543 1.521 1.461 127.35 114.35 120.30 105.66 103.52 115.45 125.31 *** ** +** +** * *** 141B PRO 44 1.304 1.220 1.529 1.533 1.466 118.38 115.24 125.74 115.04 101.33 103.73 119.02 ** * +** +** **** ** **** 142B LYS 45 1.295 1.224 1.546 1.496 1.452 131.71 106.82 125.61 113.80 103.75 122.91 127.43 ** +* *5.6* *4.7* +** +* +** *7.3* +** *7.3* 143B MET 46 1.285 1.243 1.516 1.560 1.470 127.93 110.54 120.55 118.29 107.22 106.29 128.39 *** * *** +** **** * ** *** **** 144B ILE 47 1.339 1.277 1.539 1.546 1.487 118.23 116.82 124.22 121.49 103.24 108.58 118.87 ** +* +* ** *5.6* +** +* +** *5.6* 145B GLY 48 1.292 1.257 1.531 - 1.466 124.02 111.96 124.15 - 118.42 - 123.88 +** * ** ** +* ** +** 146B GLY 49 1.343 1.242 1.522 - 1.480 120.09 122.98 110.25 - 109.25 - 126.77 +* *** *5.0* * ** *5.0* Residue-by-residue listing for 1abc Page 15 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 147B ILE 50 1.323 1.263 1.531 1.566 1.464 118.73 124.43 114.59 106.41 110.53 110.15 120.86 +* +* **** +*** * * **** 148B GLY 51 1.324 1.231 1.507 - 1.477 121.91 118.84 121.20 - 118.72 - 119.95 +* * ** +* ** 149B GLY 52 1.310 1.259 1.517 - 1.448 133.63 113.75 122.12 - 119.91 - 124.08 * * *7.7* * +** *7.7* 150B PHE 53 1.352 1.228 1.500 1.583 1.464 124.63 115.99 123.89 108.24 117.40 107.71 120.11 +* * +** +* +* ** +* +* +** 151B ILE 54 1.309 1.253 1.550 1.561 1.471 128.29 113.07 122.37 110.13 107.45 116.75 124.48 * * * +*** +* * *** +*** 152B LYS 55 1.296 1.254 1.519 1.531 1.498 118.51 108.79 122.84 118.90 108.90 110.14 128.35 ** * ** +* +*** * *4.6* *** *4.6* 153B VAL 56 1.353 1.233 1.540 1.545 1.497 115.29 109.31 117.22 109.22 107.68 116.77 133.44 +* ** +*** *** ** * *** *6.5* *6.5* 154B ARG 57 1.313 1.225 1.516 1.494 1.459 121.88 114.80 122.32 111.36 98.42 113.26 122.86 * +* *4.6* +* *4.6* 155B GLN 58 1.275 1.238 1.519 1.544 1.464 125.65 111.41 123.58 111.63 112.25 106.53 124.99 +*** ** ** +* ** * +*** 156B TYR 59 1.311 1.221 1.519 1.497 1.469 127.75 115.92 119.13 109.04 109.64 112.02 124.91 * +* *** * *** 157B ASP 60 1.309 1.234 1.510 1.535 1.491 124.11 119.15 114.75 118.77 111.08 108.77 125.82 * +* * * +*** *4.6* * +* *4.6* 158B GLN 61 1.296 1.268 1.525 1.536 1.474 124.16 112.00 127.98 111.81 119.32 107.49 119.98 ** +* * ** **** +** +* +* **** 159B ILE 62 1.339 1.227 1.517 1.580 1.447 121.38 113.57 116.21 112.37 108.68 116.01 130.20 * * +** * +** *4.5* *4.5* 160B PRO 63 1.311 1.231 1.528 1.528 1.458 124.35 111.61 124.81 110.60 108.25 107.88 123.56 +* +*** ** * **** * **** 161B VAL 64 1.287 1.260 1.526 1.546 1.454 125.59 114.61 120.00 117.04 105.36 106.05 125.36 *** * ** +*** ** *** * +*** 162B GLU 65 1.315 1.237 1.526 1.480 1.495 122.31 109.09 125.75 117.04 105.86 113.80 125.13 +** +* +*** +** +*** +* +* * +*** 163B ILE 66 1.329 1.229 1.519 1.565 1.479 123.26 - 125.64 127.48 107.53 108.73 - * +** *8.4* * +* *8.4* 164B GLY 68 - 1.244 1.491 - 1.417 - 113.60 120.92 - 123.18 - 125.48 * ** * +*** +* +*** 165B HIS 69 1.299 1.266 1.541 1.579 1.456 130.37 121.23 118.56 108.94 104.19 107.33 120.17 ** +* ** *4.8* +** * +** +* +* *4.8* 166B LYS 70 1.308 1.226 1.534 1.524 1.470 118.92 112.16 125.72 106.16 106.95 115.48 122.08 +* +* ** +** ** +* +** +** 167B ALA 71 1.318 1.238 1.525 1.511 1.488 119.16 113.99 118.00 124.02 103.15 108.48 127.99 +* * * +* * 9.0* +** * *** * 9.0* 168B ILE 72 1.309 1.276 1.523 1.568 1.480 124.01 112.87 123.74 119.25 102.98 103.13 123.39 * ** * * * +* +* *4.6* +** *4.9* *4.9* 169B GLY 73 1.341 1.209 1.509 - 1.482 117.11 116.29 113.61 - 109.53 - 130.04 * +* ** *** * **** **** 170B THR 74 1.308 1.248 1.537 1.567 1.453 125.98 110.55 123.82 108.63 109.34 114.93 125.62 +* ** +** +* ** +* +** 171B VAL 75 1.318 1.239 1.516 1.557 1.465 121.31 113.20 120.31 112.02 107.71 107.48 126.44 * * * ** ** ** 172B LEU 76 1.294 1.232 1.518 1.534 1.446 127.03 119.49 116.51 113.45 109.49 101.08 124.00 +** +** +* +** +* *5.5* *5.5* 173B VAL 77 1.318 1.253 1.513 1.540 1.499 120.52 116.74 116.79 119.58 101.39 113.03 126.39 * ** ** *4.8* +*** ** *4.8* Residue-by-residue listing for 1abc Page 16 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 174B GLY 78 1.306 1.221 1.514 - 1.479 120.12 115.71 118.61 - 107.44 - 125.66 +* +* * +* +* +* 175B PRO 79 1.323 1.250 1.522 1.523 1.475 121.09 115.72 119.61 115.11 114.86 101.82 124.66 * +** * * +* +** 176B THR 80 1.331 1.232 1.524 1.575 1.470 123.14 118.19 116.64 112.80 109.28 103.16 125.17 * ** +* *4.9* * *4.9* 177B PRO 81 1.329 1.224 1.509 1.529 1.457 124.91 120.53 116.38 106.31 118.41 107.21 123.07 ** +** +* +** +*** +*** 178B VAL 82 1.289 1.248 1.531 1.535 1.447 128.14 110.21 120.92 108.13 105.91 113.95 128.87 +** +*** +** +* * +*** +*** 179B ASN 83 1.322 1.239 1.565 1.489 1.477 116.93 114.42 115.13 108.72 102.59 122.31 130.45 +* ** * +** *** *** *6.9* *4.7* *6.9* 180B ILE 84 1.311 1.249 1.527 1.597 1.450 122.13 120.28 116.67 108.48 115.49 106.00 123.05 * ** ** ** +* *** *** 181B ILE 85 1.317 1.246 1.557 1.561 1.489 124.25 115.11 121.10 110.28 102.89 118.24 123.76 +* +* * +** +*** +*** 182B GLY 86 1.294 1.230 1.503 - 1.465 122.13 119.81 113.67 - 111.19 - 126.42 ** +* *** ** *** 183B ARG 87 1.330 1.248 1.507 1.542 1.475 121.46 115.44 119.81 103.23 111.37 111.48 124.73 +*** * +*** 184B ASN 88 1.341 1.245 1.530 1.509 1.491 114.47 112.87 125.05 120.09 108.18 112.88 121.96 * +* **** +* +** *5.3* * * *5.3* 185B LEU 89 1.283 1.261 1.513 1.522 1.458 125.31 118.75 116.35 120.77 112.54 102.17 124.73 *** +* ** * +** *5.6* *4.9* * *5.6* 186B LEU 90 1.350 1.242 1.520 1.537 1.494 116.74 112.54 116.39 113.54 110.66 114.95 131.05 +* +* +** +* +** +* +** *5.0* *5.0* 187B THR 91 1.327 1.260 1.528 1.562 1.474 121.42 115.34 111.39 108.53 111.28 117.60 133.17 * *5.5* +*** *6.4* *6.4* 188B GLN 92 1.316 1.277 1.517 1.531 1.457 120.69 119.95 117.90 114.06 116.74 107.30 122.10 ** +* +* ** +* +* ** 189B ILE 93 1.331 1.258 1.554 1.555 1.493 120.32 117.06 127.44 120.04 108.75 111.03 115.45 * * +* +*** *5.0* *4.7* *5.0* 190B GLY 94 1.315 1.261 1.500 - 1.444 128.96 - 119.80 - 112.05 - - * +* *4.9* *4.9* 191B THR 96 - 1.228 1.533 1.599 1.456 - 116.33 122.09 113.50 110.00 112.66 121.56 ** +* ** 192B LEU 97 1.332 1.229 1.569 1.511 1.473 123.44 115.04 116.98 100.42 105.10 124.06 127.87 ** ** *5.1* ** *8.0* *** *8.0* 193B ASN 98 1.294 1.254 1.518 1.550 1.477 119.71 118.28 116.92 105.78 116.35 110.50 124.71 ** * * * * ** ** +* * ** 194B PHE 99 1.311 1.251 1.532 1.502 1.471 122.34 - 114.18 113.72 104.17 116.02 - * * +*** +* +** *** +*** 195C ACE 0 - 1.251 - - - - - - - - - 107.65 * * 9.6* * 9.6* 196C SER 1 1.356 1.241 1.514 1.515 1.434 118.03 105.58 126.37 108.26 119.30 113.48 128.05 +* * ** *5.3* *** +** +* *** *5.3* 197C LEU 2 1.338 1.209 1.510 1.500 1.469 119.69 115.84 119.99 124.71 104.43 103.34 124.13 * +* * *7.7* ** **** *7.7* 198C ASN 3 1.312 1.235 1.541 1.536 1.471 127.08 108.84 123.96 111.28 109.92 112.02 127.20 * +** +*** +* +** +*** 199C PHE 4 1.328 1.460 1.535 1.541 1.466 126.66 - 104.73 117.90 113.32 104.28 - *11.5* +** * 9.5* **** +*** *11.5* 200C PRO 6 - 1.256 1.526 1.571 1.500 - 112.20 126.42 114.36 121.30 94.19 121.33 * ** ** *** *** ** +*** *8.0* *8.0* Residue-by-residue listing for 1abc Page 17 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 201C ILE 7 1.322 1.226 1.581 1.551 1.437 132.44 114.14 117.78 106.64 96.93 130.94 128.04 +** * *6.0* * +* * *5.1* *11.4* *** *11.4* 202C VAL 8 1.316 1.380 1.497 1.566 1.477 115.64 - 129.12 119.16 112.43 103.38 - *7.5* * * *** *4.9* *4.6* *4.8* *7.5* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** *11.5* *** *** +*** *7.7* *6.1* * 9.5* * 9.0* *5.1* *11.4* * 9.6* *11.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for 1abc Page 18 ---------------------------------------- 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 0.014 182 1.275 1.368 1.317 0.018 +*** +** C-N (Pro) 1.341 0.016 12 1.304 1.339 1.321 0.011 ** * C-O C-O 1.231 0.020 202 1.200 1.460 1.244 0.024 +* *11.5* CA-C CH1E-C (except Gly) 1.525 0.021 175 1.492 1.589 1.529 0.016 +* *** CH2G*-C (Gly) 1.516 0.018 26 1.491 1.548 1.520 0.014 * +* CA-CB CH1E-CH3E (Ala) 1.521 0.033 6 1.511 1.546 1.533 0.013 CH1E-CH1E (Ile,Thr,Val) 1.540 0.027 56 1.505 1.599 1.562 0.018 * ** CH1E-CH2E (the rest) 1.530 0.020 113 1.462 1.583 1.524 0.021 *** +** N-CA NH1-CH1E (except Gly,Pro)1.458 0.019 160 1.416 1.515 1.468 0.018 ** +** NH1-CH2G* (Gly) 1.451 0.016 26 1.417 1.513 1.464 0.022 ** +*** N-CH1E (Pro) 1.466 0.015 15 1.443 1.500 1.467 0.013 +* ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for 1abc Page 19 ---------------------------------------- +-----------------+ | 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 2.0 154 105.58 128.38 115.05 4.14 *5.3* *6.1* CH2G*-C-NH1 (Gly) 116.4 2.1 24 108.68 122.98 115.74 3.51 +*** *** CH1E-C-N (Pro) 116.9 1.5 15 109.51 121.84 117.08 3.61 *4.9* *** O-C-N O-C-NH1 (except Pro) 123.0 1.6 179 107.65 133.44 124.50 3.92 * 9.6* *6.5* O-C-N (Pro) 122.0 1.4 15 116.69 127.92 122.37 2.95 +*** **** C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 158 114.47 135.11 123.03 4.76 **** *7.4* C-NH1-CH2G* (Gly) 120.6 1.7 24 114.63 133.63 123.55 4.68 +*** *7.7* +* C-N-CH1E (Pro) 122.6 5.0 12 118.38 128.07 122.48 2.93 * CA-C-O CH1E-C-O (except Gly) 120.8 1.7 175 104.73 131.27 120.21 4.54 * 9.5* *6.2* CH2G*-C-O (Gly) 120.8 2.1 26 110.25 130.04 119.71 4.61 *5.0* **** CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 6 107.31 124.02 111.99 5.81 ** * 9.0* CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 56 102.39 127.48 113.17 5.61 *** *8.4* +* CH2E-CH1E-C (the rest) 110.1 1.9 113 100.42 125.94 111.62 5.04 *5.1* *8.3* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 160 96.93 123.60 108.57 5.32 *5.1* **** NH1-CH2G*-C (Gly) 112.5 2.9 26 98.93 124.24 112.72 5.95 *4.7* **** N-CH1E-C (Pro) 111.8 2.5 15 101.33 121.30 112.55 5.39 **** +*** N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 6 102.73 118.03 111.09 5.14 *5.1* *5.1* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 56 96.67 130.94 112.14 6.59 *8.7* *11.4* N-CH1E-CH2E (Pro) 103.0 1.1 15 94.19 107.88 103.37 3.11 *8.0* **** NH1-CH1E-CH2E (the rest) 110.5 1.7 98 100.31 128.67 111.76 6.07 *6.0* *10.7* ------------------------------------------------------------------------------------------------------------- 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 1abc Page 20 ---------------------------------------- B A D C O N T A C T S L I S T I N G ....................................................................... Residue Residue ----------- ----------- No. Type No. Type Contact Distance Chain Atom Chain Atom type (Angstroms) ----------------------------------------------------------------------- 1. 26 A THR O --> 305 HOH O Main-Het 2.6 2. 27 A GLY O --> 358 HOH O Main-Het 2.6 3. 46 A MET O --> 378 HOH O Main-Het 2.4 4. 50 A ILE O --> 342 HOH O Main-Het 2.6 5. 65 A GLU OE1 --> 309 HOH O Side-Het 2.3 6. 66 A ILE C --> 67 A ABA CA Main-Het 2.4 7. 67 A ABA O --> 68 A GLY N Het-Main 2.2 8. 88 A ASN O --> 337 HOH O Main-Het 2.5 9. 90 A LEU O --> 95 A ABA N Main-Het 2.6 10. 94 A GLY C --> 95 A ABA CA Main-Het 2.4 11. 95 A ABA O --> 96 A THR N Het-Main 2.3 12. 95 A ABA O --> 317 HOH O Het-Het 2.6 13. 7 B GLN OE1 --> 310 HOH O Side-Het 2.4 14. 17 B GLY O --> 319 HOH O Main-Het 2.4 15. 26 B THR O --> 304 HOH O Main-Het 2.3 16. 27 B GLY O --> 361 HOH O Main-Het 2.4 17. 34 B GLU O --> 35 B GLU C Main-Main 2.6 18. 41 B LYS O --> 338 HOH O Main-Het 2.5 19. 49 B GLY O --> 50 B ILE C Main-Main 2.6 20. 58 B GLN O --> 320 HOH O Main-Het 2.2 21. 66 B ILE C --> 67 B ABA CA Main-Het 2.5 22. 67 B ABA O --> 68 B GLY N Het-Main 2.2 23. 93 B ILE O --> 323 HOH O Main-Het 2.5 24. 94 B GLY C --> 95 B ABA CA Main-Het 2.4 25. 95 B ABA O --> 96 B THR N Het-Main 2.3 26. 95 B ABA O --> 302 HOH O Het-Het 2.4 27. 3 C ASN O --> 301 HOH O Main-Het 2.6 28. 4 C PHE C --> 5 C CH2 C Main-Het 1.6 29. 5 C CH2 C --> 6 C PRO N Het-Main 1.5 30. 8 C VAL C --> 9 C OME O Main-Het 1.5 Residue-by-residue listing for 1abc Page 21 ---------------------------------------- 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] 143 89.9% Residues in additional allowed regions [a,b,l,p] 15 9.4% Residues in generously allowed regions [~a,~b,~l,~p] 1 0.6% Residues in disallowed regions [XX] 0 0.0% ---- ------ Number of non-glycine and non-proline residues 159 100.0% Number of end-residues (excl. Gly and Pro) 5 Number of glycine residues 26 Number of proline residues 15 ---- Total number of residues 205 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 159 89.9 78.2 10.0 1.2 BETTER b. Omega angle st dev 201 2.3 6.0 3.0 -1.2 BETTER c. Bad contacts / 100 residues 30 14.6 9.0 10.0 0.6 Inside d. Zeta angle st dev 179 4.1 3.1 1.6 0.6 Inside e. H-bond energy st dev 121 0.9 0.9 0.2 0.1 Inside f. Overall G-factor 205 -1.1 -0.6 0.3 -1.9 WORSE 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 39 19.7 21.8 6.5 -0.3 Inside b. Chi-1 trans st dev 32 22.3 22.0 5.3 0.1 Inside c. Chi-1 gauche plus st dev 87 18.5 20.5 4.9 -0.4 Inside d. Chi-1 pooled st dev 158 19.6 21.2 4.8 -0.3 Inside e. Chi-2 trans st dev 59 20.9 22.6 5.0 -0.3 Inside 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% 89.9 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 18.6 3 H-bond energy st dev 0.87 0.24 <0.63 <0.87 <1.11 >1.11 0.93 3 Residue-by-residue listing for 1abc Page 22 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -0.63 Chi1-chi2 distribution -0.68 Chi1 only -0.41 Chi3 & chi4 0.23 Omega 0.32 ------ -0.23 ===== Main-chain covalent forces:- Main-chain bond lengths -0.33 Main-chain bond angles -4.47 ------ -2.72 ===== OVERALL AVERAGE -1.14 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.