Residue-by-residue listing for refined_20 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - 60.0 - - 178.8 - - - - - - 179.7 - 33.8 - 2 GLY 2 - - - - - - - - - - - 182.7 - - - 3 HIS 3 l - - -67.1 - - - - - - - 180.4 - 32.1 - 4 HIS 4 B - - -67.0 - - - - - - - 178.8 - 32.7 - 5 HIS 5 B - - -64.7 - - - - - - - 182.1 - 34.4 - 6 HIS 6 B - 183.8 - - - - - - - - 178.9 - 35.4 - 7 HIS 7 B - 180.4 - - - - - - - - 180.8 - 34.0 - 8 HIS 8 B - 184.2 - - - - - - - - 175.2 - 33.5 - 9 LEU 9 B - - -61.1 176.0 - - - - - - 180.5 - 35.0 - 10 GLU 10 B - - -71.0 - - - - - - - 176.1 -.5 32.0 - +* +* 11 MET 11 B - - -61.1 179.9 - - - - - - 178.3 - 35.3 - 12 ALA 12 B - - - - - - - - - - 177.8 - 34.2 - 13 SER 13 b - 188.9 - - - - - - - - 173.9 - 35.7 - * * 14 GLU 14 S b - 189.4 - - - - - - - - 189.2 - 32.0 - +* +* 15 GLU 15 B 58.4 - - 184.2 - - - - - - 177.9 -2.1 37.0 - 16 GLY 16 S - - - - - - - - - - - 180.9 -.9 - - * * 17 GLN 17 B 56.4 - - - - - - - - - 181.8 - 31.7 - 18 VAL 18 B - 180.0 - - - - - - - - 180.2 - 34.9 - 19 ILE 19 E B - - -64.9 - - - - - - - 179.8 -3.0 33.0 - * * 20 ALA 20 E B - - - - - - - - - - 180.4 -.7 34.3 - +* +* 21 CYS 21 E B - - -53.2 - - - - - - - 174.6 -1.0 35.3 - * * Residue-by-residue listing for refined_20 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 22 HIS 22 A - - -67.9 - - - - - - - 180.4 -.7 33.2 - +* +* 23 THR 23 h B 55.8 - - - - - - - - - 178.2 - 35.1 - 24 VAL 24 H A - 185.9 - - - -74.5 -26.8 - - - 177.8 - 34.5 - * * 25 GLU 25 H A - - -65.9 - - -58.2 -51.5 - - - 179.5 - 36.0 - * * 26 THR 26 H A - - -53.4 - - -69.2 -36.1 - - - 177.3 - 34.0 - 27 TRP 27 H A - 174.1 - - - -58.0 -53.4 - - - 180.1 -1.5 34.6 - * * 28 ASN 28 H A - 186.7 - - - -63.6 -42.8 - - - 180.1 -3.3 34.8 - +* +* 29 GLU 29 H A - 178.0 - 183.3 - -56.0 -48.8 - - - 183.1 -2.5 36.3 - 30 GLN 30 H A - - -67.1 - - -71.0 -41.1 - - - 181.7 -2.7 33.7 - 31 LEU 31 H A - - -66.1 179.9 - -68.2 -45.4 - - - 177.7 -2.1 34.3 - 32 GLN 32 H A - 182.6 - 180.9 - -61.1 -39.8 - - - 178.2 -2.7 33.7 - 33 LYS 33 H A - 185.0 - 182.7 - -60.5 -45.5 - - - 182.5 -1.8 35.5 - 34 ALA 34 H A - - - - - -72.1 -38.5 - - - 181.7 -2.5 33.5 - 35 ASN 35 H A - 189.2 - - - -66.7 -50.7 - - - 182.0 -3.0 36.1 - * * 36 GLU 36 H A - 182.1 - 186.7 - -59.3 -43.8 - - - 184.0 -2.7 36.6 - 37 SER 37 h A - - -58.1 - - - - - - - 184.6 -1.8 35.5 - 38 LYS 38 T l - - -70.3 190.1 - - - - - - 179.4 -1.1 31.2 - * * 39 THR 39 t B - - -45.4 - - - - - - - 182.6 -3.3 34.5 - * +* +* 40 LEU 40 e B - 189.4 - 167.2 - - - - - - 184.2 - 33.7 - 41 VAL 41 E B 59.4 - - - - - - - - - 178.1 -.7 33.4 - +* +* 42 VAL 42 E B - 181.4 - - - - - - - - 182.2 -3.3 34.6 - +* +* 43 VAL 43 E B - 182.4 - - - - - - - - 175.9 -3.1 34.4 - * * 44 ASP 44 E B - 176.1 - - - - - - - - 176.4 -3.1 36.3 - * * 45 PHE 45 E B - - -61.6 - - - - - - - 187.8 -3.4 35.0 - * +* +* 46 THR 46 E B - 182.8 - - - - - - - - 177.1 -2.8 36.0 - * * 47 ALA 47 t B - - - - - - - - - - 184.0 - 34.3 - 48 SER 48 T A - - -53.5 - - - - - - - 185.4 - 34.8 - 49 TRP 49 T A 50.2 - - - - - - - - - 179.4 - 32.1 - 50 CYS 50 h B 51.8 - - - - - - - -109.5 2.0 184.4 -.7 29.8 - ** +* * ** 51 GLY 51 H - - - - - - -58.8 -61.8 - - - 180.3 -.6 - - +* +* +* 52 PRO 52 H - - - - - -54.3 -54.3 -30.7 - - - 179.4 - 38.2 - * * 53 CYS 53 H A - - -53.8 148.1 - -61.7 -45.3 - -109.5 2.0 179.4 - 35.5 - +* ** ** 54 ARG 54 H A - 190.1 - 178.7 - -79.8 -33.8 - - - 181.8 -1.3 32.8 - * * 55 PHE 55 H A - 183.0 - - - -69.8 -19.6 - - - 181.2 -2.8 33.4 - +* * +* 56 ILE 56 h A - 195.2 - - - - - - - - 181.0 -1.6 34.1 - 57 ALA 57 H A - - - - - -60.3 -51.3 - - - 178.1 -1.2 31.3 - * * * Residue-by-residue listing for refined_20 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 58 PRO 58 H - - - - - -59.4 -59.4 -32.1 - - - 179.4 - 38.2 - * * 59 PHE 59 H A - 186.6 - - - -75.0 -38.1 - - - 178.1 - 34.8 - 60 PHE 60 H A - 189.1 - - - -67.8 -33.2 - - - 175.5 -2.5 34.3 - 61 ALA 61 H A - - - - - -70.9 -31.7 - - - 177.4 -2.4 33.8 - 62 ASP 62 H A - 187.7 - - - -72.2 -32.8 - - - 173.7 -1.2 35.3 - * * * 63 LEU 63 H A - 221.6 - 180.4 - -62.0 -41.1 - - - 176.1 -1.6 35.7 - ** ** 64 ALA 64 H A - - - - - -65.2 -31.4 - - - 174.6 -1.5 33.8 - 65 LYS 65 H A - 164.9 - 189.0 - -70.5 -27.8 - - - 181.4 -1.1 36.8 - * * * * 66 LYS 66 H A - 194.6 - - - -82.6 -40.9 - - - 178.5 -1.0 34.7 - * * * 67 LEU 67 h b - - -67.7 171.6 - - - - - - 186.6 -2.5 33.0 - * * 68 PRO 68 T - - - - - -62.4 - - - - - 184.9 - 38.0 - * * 69 ASN 69 T A - - -70.9 - - - - - - - 178.2 - 33.3 - 70 VAL 70 t B - 176.1 - - - - - - - - 181.8 -.8 33.6 - +* +* 71 LEU 71 E B - - -74.4 - - - - - - - 175.7 -2.2 34.2 - 72 PHE 72 E B - - -60.8 - - - - - - - 183.2 -.6 34.3 - +* +* 73 LEU 73 E B - - -69.9 - - - - - - - 177.4 -2.7 33.7 - 74 LYS 74 E B - 190.2 - - - - - - - - 184.3 -2.2 36.1 - 75 VAL 75 E B - 179.6 - - - - - - - - 176.4 -3.7 33.8 - ** ** 76 ASP 76 E B - 184.1 - - - - - - - - 185.6 -.6 34.8 - +* +* 77 THR 77 e A - 183.1 - - - - - - - - 177.2 -3.1 31.8 - * * 78 ASP 78 T A - 184.1 - - - - - - - - 177.5 - 34.5 - 79 GLU 79 T A - - -58.3 - - - - - - - 178.3 - 36.3 - 80 LEU 80 h b - - -72.8 - - - - - - - 186.9 -1.7 35.6 - * * 81 LYS 81 H A - 203.8 - - - -59.2 -51.5 - - - 182.5 -.9 35.2 - * * * * 82 SER 82 H A - - -61.4 - - -77.7 -35.0 - - - 180.4 - 32.3 - * * 83 VAL 83 H A - 178.8 - - - -67.2 -43.4 - - - 178.7 - 32.2 - 84 ALA 84 H A - - - - - -62.9 -42.0 - - - 178.3 -3.1 33.1 - * * 85 SER 85 H A - - -61.0 - - -64.2 -29.3 - - - 176.0 -1.6 31.5 - 86 ASP 86 H A - 184.1 - - - -65.8 -24.8 - - - 176.2 -1.5 33.7 - * * 87 TRP 87 h A - - -71.1 - - - - - - - 179.3 -1.0 33.3 - * * 88 ALA 88 T l - - - - - - - - - - 180.7 -1.8 32.1 - 89 ILE 89 t B - - -56.7 - - - - - - - 176.2 -2.6 33.3 - 90 GLN 90 a - 179.1 - 178.8 - - - - - - 174.5 -.6 33.9 - +* +* 91 ALA 91 S B - - - - - - - - - - 186.4 - 34.3 - * * 92 MET 92 S B - - -55.2 168.2 - - - - - - -2.0 -.6 36.5 - +* +* Residue-by-residue listing for refined_20 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 93 PRO 93 e cis - - - - - -90.5 - - - - - 177.4 - 39.5 - ** +* ** 94 THR 94 E B - - -67.1 - - - - - - - 174.1 -1.9 33.6 - * * 95 PHE 95 E B - - -59.1 - - - - - - - 182.6 -3.4 36.5 - +* +* 96 MET 96 E B - 181.9 - 177.9 - - - - - - 183.5 -3.3 34.3 - +* +* 97 PHE 97 E B - - -66.5 - - - - - - - 177.2 -2.9 36.5 - * * 98 LEU 98 E B - - -55.0 - - - - - - - 177.0 -2.8 34.8 - * * 99 LYS 99 E B - 174.2 - 175.5 - - - - - - 177.3 -3.8 33.7 - ** ** 100 GLU 100 T l - - -54.6 178.7 - - - - - - 180.8 - 33.2 - 101 GLY 101 T - - - - - - - - - - - 178.0 - - - 102 LYS 102 E B - 186.0 - - - - - - - - 183.9 -2.1 33.8 - 103 ILE 103 E B - - -59.1 173.5 - - - - - - 175.4 - 35.4 - 104 LEU 104 E a - - -70.2 186.3 - - - - - - 185.9 -2.4 33.9 - * * 105 ASP 105 E B 43.7 - - - - - - - - - 187.7 -2.3 29.6 - * * * * 106 LYS 106 E B - 186.0 - - - - - - - - 183.1 - 37.5 - * * 107 VAL 107 E B - 180.6 - - - - - - - - 178.8 -3.3 35.2 - +* +* 108 VAL 108 E B - 179.9 - - - - - - - - 180.2 - 34.1 - 109 GLY 109 e - - - - - - - - - - - 182.5 -2.8 - - * * 110 ALA 110 B - - - - - - - - - - 169.4 - 34.9 - +* +* 111 LYS 111 h B - - -70.5 179.4 - - - - - - 181.7 -.9 33.8 - * * 112 LYS 112 H A - 186.7 - 180.3 - -61.5 -43.7 - - - 180.2 - 33.2 - 113 ASP 113 H A - 182.9 - - - -61.8 -40.5 - - - 181.8 - 34.8 - 114 GLU 114 H A - 183.1 - - - -66.6 -41.1 - - - 178.5 - 34.6 - 115 LEU 115 H A - 187.4 - - - -67.2 -47.0 - - - 175.0 -2.3 34.3 - 116 GLN 116 H A - - -73.4 - - -54.2 -37.1 - - - 179.8 -3.0 34.1 - * * 117 SER 117 H A - 183.2 - - - -69.3 -40.4 - - - 179.1 -2.2 34.0 - 118 THR 118 H A - - -50.6 - - -70.4 -31.4 - - - 176.9 -2.2 34.1 - * * 119 ILE 119 H A - - -60.8 178.3 - -66.5 -46.7 - - - 178.9 -2.5 32.4 - 120 ALA 120 H A - - - - - -63.8 -33.4 - - - 176.2 -2.5 33.2 - 121 LYS 121 H A - 183.7 - 182.3 - -57.7 -41.5 - - - 180.6 -2.0 37.5 - * * 122 HIS 122 H A - - -77.2 - - -83.9 -13.9 - - - 180.2 -1.5 33.7 - +* ** ** 123 LEU 123 h b - - -66.8 181.5 - - - - - - 179.7 -.9 33.9 - +* +* 124 ALA 124 - - - - - - - - - - - - -1.4 34.3 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * ** * +* ** +* ** ** +* ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 54.5 184.7 -63.3 178.5 -66.6 -66.0 -39.1 - -109.5 2.0 179.8 -2.0 34.3 ** ** Standard deviations: 5.6 8.0 7.3 8.0 16.2 7.1 9.3 - .0 .0 3.4 .9 1.6 Numbers of values: 8 50 44 28 4 45 45 0 2 2 122 80 119 0 Number of cis-peptides (labelled cis): 1 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_20 Page 6 ---------------------------------------- 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 MET 1 - 1.233 1.509 1.544 1.464 - 116.49 120.43 110.40 109.93 111.32 123.07 2 GLY 2 1.304 1.219 1.498 - 1.429 121.17 115.94 120.07 - 111.64 - 123.96 +* * +* 3 HIS 3 1.340 1.227 1.516 1.543 1.473 123.30 116.52 121.35 109.98 111.33 113.44 122.13 +* +* 4 HIS 4 1.298 1.230 1.502 1.536 1.445 121.03 115.63 120.98 110.59 111.39 112.15 123.38 ** * ** 5 HIS 5 1.305 1.236 1.505 1.536 1.442 122.88 116.52 120.32 109.75 108.93 111.50 123.16 +* +* 6 HIS 6 1.300 1.222 1.520 1.543 1.446 121.96 116.93 120.18 110.19 108.95 109.52 122.89 ** ** 7 HIS 7 1.310 1.231 1.518 1.545 1.454 121.40 116.69 120.40 110.86 109.65 110.67 122.92 * * 8 HIS 8 1.314 1.220 1.501 1.539 1.440 120.81 115.83 120.77 110.02 110.33 112.13 123.39 * * * 9 LEU 9 1.290 1.240 1.506 1.533 1.431 121.61 117.02 119.89 110.52 107.35 110.27 123.04 +** * * +** 10 GLU 10 1.307 1.248 1.508 1.539 1.442 120.69 114.72 121.60 109.99 111.71 113.61 123.64 +* +* +* 11 MET 11 1.291 1.235 1.507 1.536 1.429 122.70 117.12 120.30 109.93 107.70 110.38 122.58 +** +* * +** Residue-by-residue listing for refined_20 Page 7 ---------------------------------------- ................................................................................................................................... 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 ALA 12 1.291 1.246 1.520 1.520 1.431 120.86 116.59 120.75 110.76 109.33 110.35 122.66 +** * +** 13 SER 13 1.291 1.251 1.526 1.541 1.430 121.86 118.48 119.76 111.22 106.47 108.63 121.74 +** * * * +* * +** 14 GLU 14 1.309 1.230 1.523 1.530 1.431 119.17 113.82 122.34 112.86 106.92 112.43 123.68 * * * * * +* * +* 15 GLU 15 1.301 1.239 1.505 1.530 1.430 123.98 116.02 120.49 109.57 110.05 107.58 123.49 ** * * +* ** 16 GLY 16 1.319 1.228 1.504 - 1.445 120.97 116.25 120.73 - 112.29 - 123.02 17 GLN 17 1.311 1.235 1.486 1.540 1.428 121.75 114.20 121.36 112.73 111.18 111.72 124.41 * +* +* * +* 18 VAL 18 1.271 1.246 1.524 1.551 1.441 123.14 117.53 119.76 110.30 109.16 110.19 122.71 **** **** 19 ILE 19 1.317 1.229 1.516 1.574 1.436 120.89 116.75 120.99 110.08 109.11 113.52 122.23 * * * * 20 ALA 20 1.298 1.228 1.496 1.516 1.432 120.40 116.51 120.70 110.25 109.15 110.94 122.79 ** * * ** 21 CYS 21 1.298 1.233 1.499 1.509 1.411 121.13 115.84 121.09 109.55 109.59 110.06 123.01 ** * * ** ** 22 HIS 22 1.287 1.228 1.501 1.536 1.439 121.57 114.89 121.31 111.15 108.54 112.03 123.79 *** * * *** 23 THR 23 1.326 1.250 1.513 1.556 1.433 122.90 116.45 120.38 108.89 108.91 111.53 123.17 * * 24 VAL 24 1.311 1.224 1.523 1.543 1.444 121.79 115.02 121.34 109.83 108.34 111.37 123.60 * * * 25 GLU 25 1.327 1.224 1.526 1.504 1.418 124.29 116.95 120.28 110.64 111.59 107.12 122.74 * ** * +* ** 26 THR 26 1.334 1.227 1.536 1.542 1.453 121.09 115.64 121.11 110.57 109.82 110.74 123.22 27 TRP 27 1.321 1.236 1.536 1.532 1.457 122.74 115.78 121.00 111.37 110.90 108.56 123.20 * * 28 ASN 28 1.317 1.244 1.533 1.549 1.458 122.82 115.03 120.90 111.28 109.62 109.04 124.02 29 GLU 29 1.329 1.235 1.529 1.529 1.462 124.24 116.59 120.48 108.94 111.87 108.29 122.91 * * * 30 GLN 30 1.319 1.227 1.515 1.491 1.414 122.17 117.26 120.14 110.41 113.30 109.98 122.60 +* ** ** 31 LEU 31 1.319 1.230 1.498 1.480 1.416 121.55 116.38 120.16 110.33 112.06 109.54 123.46 * ** ** ** 32 GLN 32 1.314 1.224 1.530 1.528 1.441 121.19 115.70 120.67 111.24 109.17 110.73 123.56 * * 33 LYS 33 1.335 1.241 1.528 1.536 1.459 122.87 116.03 120.77 109.27 110.21 109.72 123.17 34 ALA 34 1.334 1.217 1.521 1.521 1.446 121.59 116.65 120.60 110.69 111.69 110.58 122.74 35 ASN 35 1.311 1.241 1.510 1.521 1.467 122.20 114.00 121.73 108.35 110.02 109.60 124.26 * * * 36 GLU 36 1.308 1.238 1.535 1.523 1.469 124.41 116.26 121.10 108.45 112.04 108.21 122.63 * +* * +* 37 SER 37 1.307 1.240 1.523 1.513 1.437 121.61 116.35 120.15 110.01 112.15 108.41 123.49 +* * * +* 38 LYS 38 1.335 1.236 1.512 1.512 1.458 122.61 115.45 121.77 110.59 111.88 113.66 122.77 +* +* 39 THR 39 1.282 1.238 1.515 1.520 1.399 121.28 115.80 121.18 110.11 108.03 111.22 122.99 *** *** * *** 40 LEU 40 1.276 1.242 1.537 1.551 1.428 122.10 116.27 120.59 113.86 108.41 108.67 123.12 +*** * +* +* * +*** 41 VAL 41 1.314 1.238 1.540 1.565 1.439 122.01 115.93 121.06 111.39 111.41 110.64 122.99 * * * * Residue-by-residue listing for refined_20 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.308 1.234 1.518 1.538 1.442 122.77 116.62 120.66 109.11 108.92 111.69 122.73 * * 43 VAL 43 1.302 1.232 1.525 1.551 1.440 121.22 115.52 120.73 109.04 111.04 111.52 123.74 +* +* 44 ASP 44 1.304 1.231 1.521 1.536 1.451 123.93 117.04 120.19 109.04 108.35 109.30 122.72 +* * * +* 45 PHE 45 1.303 1.238 1.515 1.514 1.425 121.96 116.19 120.46 110.03 108.37 110.27 123.33 +* +* * +* 46 THR 46 1.298 1.241 1.531 1.562 1.442 122.11 115.08 121.12 109.79 111.39 108.53 123.80 ** +* ** 47 ALA 47 1.318 1.240 1.517 1.519 1.436 123.64 116.47 120.67 110.34 108.26 110.97 122.85 * * * * 48 SER 48 1.298 1.229 1.546 1.516 1.445 122.27 116.95 120.72 110.31 112.80 108.66 122.32 ** * ** 49 TRP 49 1.317 1.239 1.535 1.535 1.461 121.34 118.35 120.09 111.32 114.89 110.62 121.56 * * * 50 CYS 50 1.312 1.240 1.527 1.544 1.451 119.27 114.80 121.42 113.70 112.32 112.51 123.78 * * +* * +* 51 GLY 51 1.329 1.237 1.519 - 1.455 123.30 118.85 119.25 - 114.51 - 121.91 +* * +* 52 PRO 52 1.363 1.218 1.525 1.525 1.473 122.94 116.48 120.58 110.31 112.65 103.96 122.93 * * 53 CYS 53 1.324 1.234 1.528 1.518 1.456 122.14 116.41 121.22 108.38 110.14 110.39 122.36 54 ARG 54 1.317 1.221 1.530 1.524 1.438 120.36 116.26 120.97 111.17 110.36 111.55 122.73 * * 55 PHE 55 1.328 1.231 1.536 1.545 1.466 122.19 116.92 120.96 110.79 111.54 110.79 122.07 56 ILE 56 1.315 1.219 1.540 1.581 1.444 120.14 116.11 120.97 110.29 108.83 111.74 122.85 +* +* 57 ALA 57 1.341 1.220 1.545 1.527 1.465 122.29 120.27 119.00 111.55 113.21 112.01 120.73 ** * * * ** 58 PRO 58 1.378 1.236 1.537 1.539 1.473 121.80 115.76 121.28 110.36 111.78 104.17 122.94 ** * ** 59 PHE 59 1.319 1.229 1.534 1.539 1.454 122.19 115.34 121.45 110.86 109.03 109.53 123.20 60 PHE 60 1.314 1.226 1.544 1.543 1.456 123.85 115.86 121.55 112.33 109.06 108.68 122.58 * * * * * 61 ALA 61 1.324 1.233 1.528 1.523 1.459 122.36 115.85 121.09 110.65 110.25 110.66 123.05 62 ASP 62 1.323 1.216 1.513 1.511 1.465 122.16 114.74 121.91 109.28 108.45 110.16 123.34 63 LEU 63 1.304 1.228 1.559 1.528 1.451 123.09 116.06 121.17 110.24 108.72 108.55 122.75 +* +* * +* 64 ALA 64 1.337 1.220 1.531 1.520 1.482 123.17 114.54 122.21 110.62 110.39 110.43 123.14 * * 65 LYS 65 1.294 1.238 1.548 1.520 1.454 124.60 115.97 121.37 110.88 110.42 105.88 122.66 +** * +* +** +** 66 LYS 66 1.313 1.233 1.538 1.564 1.451 122.18 116.39 120.87 112.11 108.63 108.85 122.72 * +* * +* 67 LEU 67 1.321 1.225 1.524 1.506 1.434 122.31 116.44 121.06 111.78 111.23 110.22 122.50 * * * 68 PRO 68 1.338 1.237 1.536 1.538 1.469 123.45 117.17 120.50 110.48 115.24 103.62 122.32 * * 69 ASN 69 1.324 1.232 1.514 1.524 1.450 121.65 116.92 120.58 109.94 113.07 111.22 122.49 70 VAL 70 1.293 1.225 1.517 1.553 1.442 121.56 117.08 120.12 111.10 108.63 111.51 122.76 +** +** 71 LEU 71 1.312 1.230 1.499 1.539 1.432 121.41 115.59 120.91 109.27 111.24 111.63 123.50 * * * * Residue-by-residue listing for refined_20 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 PHE 72 1.295 1.232 1.495 1.513 1.429 122.10 115.56 120.98 109.57 108.05 111.91 123.44 ** * +* * ** 73 LEU 73 1.279 1.227 1.502 1.542 1.432 122.49 115.71 120.83 109.20 111.37 112.33 123.46 +*** * * * +*** 74 LYS 74 1.304 1.244 1.514 1.542 1.435 122.14 116.82 120.69 110.18 105.89 109.24 122.48 +* * +* +* 75 VAL 75 1.295 1.229 1.498 1.557 1.431 120.99 115.12 121.52 109.91 110.70 111.86 123.35 ** * * ** 76 ASP 76 1.291 1.240 1.513 1.507 1.425 121.79 116.22 120.68 111.09 107.53 109.66 123.08 +** * +* * +** 77 THR 77 1.301 1.217 1.530 1.548 1.444 122.32 118.23 119.80 111.09 113.34 112.12 121.94 ** * ** 78 ASP 78 1.316 1.234 1.500 1.515 1.459 119.49 114.24 121.57 109.25 108.20 111.65 124.19 * * * * 79 GLU 79 1.317 1.228 1.521 1.513 1.433 123.87 115.71 121.21 109.74 109.81 108.09 123.06 * * * * 80 LEU 80 1.312 1.223 1.527 1.533 1.424 123.39 115.81 120.75 109.95 109.04 109.46 123.43 * +* +* 81 LYS 81 1.323 1.228 1.548 1.561 1.467 123.16 117.59 120.48 112.34 110.58 107.14 121.72 * +* * +* +* 82 SER 82 1.305 1.235 1.523 1.522 1.448 120.23 116.64 120.64 111.84 111.85 111.11 122.68 +* +* 83 VAL 83 1.319 1.227 1.531 1.548 1.452 120.89 117.00 120.34 111.24 111.20 112.19 122.63 84 ALA 84 1.328 1.229 1.525 1.520 1.455 121.23 116.61 120.86 111.11 110.43 111.07 122.50 85 SER 85 1.323 1.235 1.544 1.515 1.446 121.57 117.04 120.56 113.03 112.20 110.63 122.39 +* +* 86 ASP 86 1.336 1.222 1.535 1.534 1.478 121.64 115.51 121.55 110.19 109.97 111.31 122.93 * * 87 TRP 87 1.319 1.242 1.525 1.524 1.451 123.68 114.97 120.82 110.95 110.92 110.83 124.21 * * 88 ALA 88 1.345 1.225 1.518 1.533 1.470 125.18 116.39 121.03 111.55 111.69 111.65 122.52 * +* +* 89 ILE 89 1.316 1.243 1.523 1.548 1.439 121.25 114.50 121.61 109.88 111.22 112.18 123.87 90 GLN 90 1.303 1.239 1.535 1.530 1.440 123.49 115.55 121.55 111.85 108.39 110.02 122.90 +* * +* 91 ALA 91 1.325 1.231 1.519 1.518 1.439 122.16 116.50 120.83 110.92 108.17 110.39 122.66 * * 92 MET 92 1.302 1.227 1.510 1.523 1.441 121.38 118.44 119.84 109.55 109.59 108.23 121.72 +* * * +* 93 PRO 93 1.334 1.241 1.533 1.526 1.458 123.72 116.28 121.00 110.05 112.05 102.45 122.71 94 THR 94 1.298 1.220 1.510 1.541 1.431 121.61 115.88 120.73 109.18 110.98 112.54 123.39 ** * ** 95 PHE 95 1.296 1.235 1.497 1.521 1.401 122.55 116.68 120.62 109.27 105.30 109.72 122.65 ** * +** ** +** 96 MET 96 1.276 1.233 1.494 1.519 1.423 120.79 114.95 121.36 112.01 109.36 109.23 123.68 +*** * +* * +*** 97 PHE 97 1.283 1.247 1.501 1.512 1.396 123.19 116.29 121.13 109.40 109.89 108.51 122.58 *** * *** * *** 98 LEU 98 1.288 1.220 1.514 1.559 1.423 120.35 116.79 120.52 107.70 107.54 113.49 122.67 +** * +* * * +* +** 99 LYS 99 1.282 1.232 1.477 1.514 1.420 121.91 114.34 120.82 111.12 109.39 111.00 124.76 *** ** +* * *** 100 GLU 100 1.318 1.222 1.546 1.527 1.442 124.15 115.62 121.24 112.51 111.07 109.36 123.04 * * * 101 GLY 101 1.332 1.238 1.528 - 1.458 122.09 116.90 120.39 - 113.60 - 122.71 Residue-by-residue listing for refined_20 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 102 LYS 102 1.317 1.222 1.547 1.565 1.459 121.83 116.85 120.31 113.29 108.38 109.03 122.84 * +* +* * +* 103 ILE 103 1.324 1.229 1.532 1.560 1.480 123.58 116.65 120.73 108.04 112.02 110.63 122.63 * * * 104 LEU 104 1.316 1.238 1.503 1.521 1.437 121.09 116.03 120.82 108.51 110.95 112.62 123.13 * * * * 105 ASP 105 1.315 1.237 1.480 1.541 1.420 122.08 114.50 121.53 112.68 112.21 114.11 123.95 ** +* * ** ** 106 LYS 106 1.287 1.233 1.536 1.550 1.413 122.95 116.65 120.70 113.50 107.28 103.65 122.65 *** ** +* * **** **** 107 VAL 107 1.317 1.224 1.527 1.567 1.460 122.57 117.14 120.30 109.19 109.81 110.69 122.55 * * 108 VAL 108 1.317 1.234 1.525 1.541 1.452 121.74 116.50 120.28 109.53 110.11 111.63 123.22 109 GLY 109 1.317 1.238 1.508 - 1.450 121.04 117.09 120.28 - 111.19 - 122.63 110 ALA 110 1.321 1.230 1.503 1.525 1.434 120.02 114.40 121.60 109.48 111.32 110.26 123.97 * * * 111 LYS 111 1.293 1.248 1.493 1.525 1.414 124.52 118.32 118.79 111.15 106.45 111.88 122.89 +** * ** +* * * +* +** 112 LYS 112 1.315 1.229 1.526 1.521 1.431 120.19 115.96 120.54 110.70 110.33 111.57 123.42 * * 113 ASP 113 1.331 1.220 1.515 1.532 1.470 122.78 115.83 121.05 108.82 110.96 110.91 123.10 114 GLU 114 1.317 1.240 1.523 1.528 1.457 122.22 116.24 121.16 110.37 110.24 109.89 122.59 115 LEU 115 1.314 1.212 1.506 1.505 1.436 120.68 115.18 120.85 110.12 108.62 110.96 123.95 * * * * 116 GLN 116 1.317 1.236 1.527 1.536 1.479 123.17 116.47 120.84 109.69 111.44 110.73 122.69 * * 117 SER 117 1.315 1.237 1.522 1.536 1.440 121.44 115.79 121.04 111.48 109.33 110.14 123.10 * * 118 THR 118 1.314 1.228 1.544 1.542 1.433 121.82 116.72 121.09 110.83 109.78 110.50 122.16 * * * 119 ILE 119 1.326 1.221 1.527 1.556 1.447 121.06 116.98 120.04 110.73 110.07 112.97 122.91 120 ALA 120 1.342 1.228 1.517 1.516 1.474 121.46 115.25 120.98 110.91 110.66 110.99 123.76 121 LYS 121 1.318 1.226 1.521 1.502 1.457 124.09 114.62 121.76 108.59 109.62 107.11 123.62 * * +* +* 122 HIS 122 1.311 1.234 1.529 1.519 1.443 123.27 118.15 119.65 109.55 114.04 110.68 122.20 * * * 123 LEU 123 1.327 1.238 1.522 1.500 1.408 121.64 115.42 121.33 111.15 111.86 109.57 123.21 +* +** +** 124 ALA 124 1.304 - 1.509 1.528 1.433 123.27 - - 110.77 108.53 110.63 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** ** *** +* ** * +* ** **** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 Page 11 ---------------------------------------- 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 .014 119 1.271 1.345 1.311 .015 **** * * C-N (Pro) 1.341 .016 4 1.334 1.378 1.354 .018 ** C-O C-O 1.231 .020 123 1.212 1.251 1.232 .008 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.477 1.559 1.521 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.498 1.528 1.512 .011 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.516 1.533 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.520 1.581 1.552 .013 +* CH1E-CH2E (the rest) 1.530 .020 84 1.480 1.565 1.528 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.396 1.482 1.443 .018 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.429 1.458 1.448 .010 * N-CH1E (Pro) 1.466 .015 4 1.458 1.473 1.468 .006 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 Page 12 ---------------------------------------- +-----------------+ | 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 2.0 114 113.82 120.27 116.16 1.04 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.94 118.85 117.01 1.01 * CH1E-C-N (Pro) 116.9 1.5 4 115.76 117.17 116.43 .51 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.73 124.76 122.99 .63 * * O-C-N (Pro) 122.0 1.4 4 122.32 122.94 122.73 .25 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.17 125.18 122.10 1.19 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.97 123.30 121.71 .89 +* C-N-CH1E (Pro) 122.6 5.0 4 121.80 123.72 122.98 .74 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.79 122.34 120.82 .58 * CH2G*-C-O (Gly) 120.8 2.1 5 119.25 120.73 120.14 .50 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.48 111.55 110.74 .52 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.04 111.39 110.01 .85 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.70 113.86 110.56 1.31 * +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.30 114.89 110.05 1.73 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 111.19 114.51 112.65 1.24 N-CH1E-C (Pro) 111.8 2.5 4 111.78 115.24 112.93 1.37 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.26 112.01 110.84 .50 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.53 113.52 111.43 1.03 +* * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.45 104.17 103.55 .67 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 103.65 114.11 110.17 1.81 **** ** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_20 Page 13 ---------------------------------------- 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] 102 90.3% Residues in additional allowed regions [a,b,l,p] 11 9.7% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 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 113 90.3 83.8 10.0 .6 Inside b. Omega angle st dev 122 3.4 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.6 3.1 1.6 -.9 Inside e. H-bond energy st dev 80 .9 .8 .2 .6 Inside f. Overall G-factor 124 .0 -.4 .3 1.4 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 8 5.6 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 50 8.0 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 44 7.3 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 102 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 28 8.0 20.4 5.0 -2.5 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 90.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_20 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.15 Chi1-chi2 distribution -.24 Chi1 only .06 Chi3 & chi4 .34 Omega .01 ------ -.05 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .42 ------ .22 ===== OVERALL AVERAGE .04 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.