Residue-by-residue listing for refined_17 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 - - - -57.9 - - - - - - - 182.5 - 34.7 - 2 GLY 2 - - - - - - - - - - - 176.2 - - - 3 HIS 3 B - - -65.3 - - - - - - - 176.5 - 32.2 - 4 HIS 4 B - 183.6 - - - - - - - - 181.7 - 34.4 - 5 HIS 5 t b - - -57.8 - - - - - - - 180.1 - 34.1 - 6 HIS 6 T A 62.7 - - - - - - - - - 179.9 -.9 30.6 - * * 7 HIS 7 T b - 188.0 - - - - - - - - 181.9 - 33.2 - 8 HIS 8 T ~a - 183.3 - - - - - - - - 180.1 -1.5 34.0 - ** ** 9 LEU 9 t l - - -69.5 - - - - - - - 182.3 -.7 31.6 - +* +* 10 GLU 10 B 56.8 - - 184.7 - - - - - - 181.8 - 33.3 - 11 MET 11 B - 173.8 - - - - - - - - 174.6 - 35.1 - 12 ALA 12 b - - - - - - - - - - 181.3 -.9 33.5 - +* +* 13 SER 13 S b - 186.0 - - - - - - - - 178.1 -1.2 35.2 - * * 14 GLU 14 b - 187.7 - 183.6 - - - - - - 181.6 - 34.1 - 15 GLU 15 B 67.7 - - - - - - - - - 177.4 -1.0 34.3 - * * 16 GLY 16 S - - - - - - - - - - - 181.1 -2.2 - - 17 GLN 17 S B 53.7 - - 186.2 - - - - - - 183.9 - 32.5 - 18 VAL 18 B - 184.5 - - - - - - - - 181.4 - 35.9 - 19 ILE 19 E B - - -57.3 176.3 - - - - - - 180.1 -2.7 35.6 - 20 ALA 20 E B - - - - - - - - - - 181.5 -.8 32.9 - +* +* 21 CYS 21 E B - - -52.6 - - - - - - - 176.6 -2.6 35.5 - Residue-by-residue listing for refined_17 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 S A - - -66.0 - - - - - - - 181.8 -.5 33.8 - ** ** 23 THR 23 h B 57.5 - - - - - - - - - 175.0 - 35.9 - 24 VAL 24 H A 62.0 - - - - -73.8 -22.2 - - - 177.6 - 32.3 - +* +* 25 GLU 25 H A - 181.7 - 182.2 - -63.3 -51.9 - - - 179.0 - 35.8 - * * 26 THR 26 H A - - -56.4 - - -64.3 -34.7 - - - 176.5 - 34.1 - 27 TRP 27 H A - 172.0 - - - -62.6 -54.1 - - - 180.6 -1.4 35.1 - * * 28 ASN 28 H A - 182.6 - - - -59.8 -44.8 - - - 181.0 -3.4 35.4 - +* +* 29 GLU 29 H A - 174.9 - 181.3 - -55.8 -49.1 - - - 180.0 -2.9 35.2 - * * 30 GLN 30 H A - - -87.1 - - -68.5 -33.0 - - - 175.8 -1.8 33.2 - * * 31 LEU 31 H A - - -67.9 182.6 - -70.3 -42.7 - - - 174.3 -1.7 34.0 - 32 GLN 32 H A - 177.4 - 178.3 - -58.2 -46.5 - - - 177.0 -3.0 33.9 - * * 33 LYS 33 H A - 182.1 - 181.1 - -55.7 -46.5 - - - 181.1 -2.8 34.8 - * * 34 ALA 34 H A - - - - - -68.9 -43.6 - - - 183.1 -2.4 34.0 - 35 ASN 35 H A - 190.1 - - - -64.7 -54.0 - - - 181.6 -3.4 36.6 - * +* +* 36 GLU 36 H A - 179.3 - 183.4 - -61.5 -43.3 - - - 185.5 -3.1 34.5 - * * 37 SER 37 H A - - -49.2 - - -88.2 -9.0 - - - 183.4 -1.9 35.6 - * +* +** +** 38 LYS 38 h l - - -80.1 160.4 - - - - - - 176.7 -1.1 31.2 - * * 39 THR 39 e B - - -47.8 - - - - - - - 179.9 -1.2 36.1 - * * * 40 LEU 40 E B - 182.9 - 169.1 - - - - - - 183.5 - 34.4 - 41 VAL 41 E B 56.0 - - - - - - - - - 178.9 -1.5 32.8 - 42 VAL 42 E B - 181.5 - - - - - - - - 183.0 -3.4 34.5 - +* +* 43 VAL 43 E B - 178.5 - - - - - - - - 177.9 -3.2 34.7 - +* +* 44 ASP 44 E B - 169.3 - - - - - - - - 175.4 -3.0 35.5 - * * 45 PHE 45 E B - - -65.5 - - - - - - - 184.7 -2.1 35.0 - 46 THR 46 E B - - -71.5 - - - - - - - 174.5 -2.6 34.8 - 47 ALA 47 t B - - - - - - - - - - 184.3 - 34.3 - 48 SER 48 T A 54.6 - - - - - - - - - 182.6 - 34.6 - 49 TRP 49 T A 49.0 - - - - - - - - - 180.6 - 32.7 - 50 CYS 50 h B - 175.4 - 216.4 - - - 69.8 - 2.7 181.2 -2.2 33.2 - ** +* *7.4* *7.4* 51 GLY 51 H - - - - - - -63.3 -63.2 - - - 178.7 -.6 - - ** +* ** 52 PRO 52 H - - - - - -55.8 -55.8 -31.3 - - - 176.8 - 37.5 - * * 53 CYS 53 H A - - -64.2 - - -67.5 -46.5 69.8 - 2.7 179.2 - 34.2 - +* *7.4* *7.4* 54 ARG 54 H A - 181.6 - - - -62.2 -29.6 - - - 178.3 -2.3 34.9 - 55 PHE 55 H A - 176.1 - - - -73.7 -39.6 - - - 187.2 -1.9 35.1 - * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 ILE 56 H A - 192.7 - - - -90.7 -24.6 - - - 181.7 -1.9 33.6 - ** * ** 57 ALA 57 H A - - - - - -51.0 -48.2 - - - 178.3 -2.7 31.1 - * * 58 PRO 58 H - - - - - -55.9 -55.9 -30.6 - - - 180.5 - 39.2 - +* +* 59 PHE 59 H A - 182.9 - - - -79.7 -47.0 - - - 179.7 -1.0 33.8 - * * * 60 PHE 60 H A - 183.2 - - - -61.7 -33.5 - - - 177.1 -2.5 33.8 - 61 ALA 61 H A - - - - - -67.9 -27.6 - - - 178.9 -2.7 33.7 - * * 62 ASP 62 H A - 192.6 - - - -74.5 -40.2 - - - 172.4 -.9 34.5 - * +* +* 63 LEU 63 H A - - -86.2 - - -52.8 -47.6 - - - 177.3 -1.8 35.0 - * * * 64 ALA 64 H A - - - - - -60.8 -30.8 - - - 178.7 -1.9 33.8 - 65 LYS 65 H A - 176.3 - 180.8 - -77.2 -30.7 - - - 183.2 -.9 34.8 - +* +* 66 LYS 66 H A - 185.9 - 181.9 - -83.3 -40.3 - - - 181.1 -1.8 34.5 - +* +* 67 LEU 67 h b - - -66.5 168.7 - - - - - - 182.7 -2.8 33.2 - * * 68 PRO 68 S - - - - - -81.3 - - - - - 181.9 - 39.7 - * +* +* 69 ASN 69 S A - 183.8 - - - - - - - - 179.2 - 33.3 - 70 VAL 70 S B - 177.8 - - - - - - - - 181.9 - 33.5 - 71 LEU 71 E B - - -58.7 178.5 - - - - - - 177.2 -1.8 36.5 - 72 PHE 72 E B - - -60.2 - - - - - - - 182.3 -.6 33.9 - +* +* 73 LEU 73 E B - - -76.1 - - - - - - - 177.2 -2.8 32.0 - 74 LYS 74 E B - 174.8 - - - - - - - - 176.4 -3.2 36.7 - * * 75 VAL 75 E B - 179.3 - - - - - - - - 180.4 -3.6 34.5 - ** ** 76 ASP 76 E B - 187.4 - - - - - - - - 186.0 -1.4 32.9 - * * 77 THR 77 e A - - -51.1 - - - - - - - 175.9 -2.3 33.7 - * * 78 ASP 78 T A - 179.8 - - - - - - - - 176.6 -.5 34.9 - ** ** 79 GLU 79 T A - 191.0 - - - - - - - - 186.4 - 38.6 - * * * 80 LEU 80 h b - - -62.5 179.6 - - - - - - 178.1 -3.4 34.9 - +* +* 81 LYS 81 H A - - -59.8 178.0 - -68.5 -40.8 - - - 181.7 -1.3 34.5 - 82 SER 82 H A - - -51.6 - - -63.2 -34.8 - - - 179.4 - 34.8 - * * 83 VAL 83 H A - 180.2 - - - -72.4 -40.6 - - - 179.3 - 33.6 - 84 ALA 84 H A - - - - - -63.3 -38.8 - - - 178.6 -1.6 34.0 - 85 SER 85 H A - - -59.0 - - -63.7 -33.2 - - - 180.9 -2.3 33.8 - 86 ASP 86 H A - 184.4 - - - -70.2 -36.3 - - - 178.9 -1.2 33.6 - * * 87 TRP 87 h A - - -68.5 - - - - - - - 177.0 -1.6 32.4 - 88 ALA 88 T L - - - - - - - - - - 180.2 -1.1 33.5 - * * 89 ILE 89 t B - - -56.7 - - - - - - - 182.7 -2.8 34.0 - * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 90 GLN 90 A - - -55.2 - - - - - - - 184.5 -.8 35.7 - +* +* 91 ALA 91 S B - - - - - - - - - - 178.0 - 34.2 - 92 MET 92 S B - - -64.4 176.4 - - - - - - -1.7 - 35.1 - 93 PRO 93 e cis - - - - - -90.4 - - - - - 174.5 - 39.7 - ** +* ** 94 THR 94 E B - - -60.6 - - - - - - - 180.1 -.9 33.5 - +* +* 95 PHE 95 E B - - -64.3 - - - - - - - 181.0 -3.2 35.5 - * * 96 MET 96 E B - 179.8 - - - - - - - - 181.8 -3.4 35.0 - +* +* 97 PHE 97 E B - - -68.7 - - - - - - - 177.0 -3.1 36.2 - * * 98 LEU 98 E B 58.6 - - 166.8 - - - - - - 182.7 -2.1 32.4 - 99 LYS 99 E B - 172.2 - 178.8 - - - - - - 178.4 -3.3 34.4 - +* +* 100 GLU 100 e l - - -58.5 167.7 - - - - - - 183.0 -.9 34.0 - +* +* 101 GLY 101 T - - - - - - - - - - - 178.5 - - - 102 LYS 102 E B - 180.6 - 185.9 - - - - - - 182.1 -2.2 36.2 - 103 ILE 103 E B - - -59.8 - - - - - - - 178.3 - 34.3 - 104 LEU 104 E a - - -69.4 184.1 - - - - - - 186.2 -2.3 34.0 - * * 105 ASP 105 E B 47.3 - - - - - - - - - 180.2 -1.9 32.4 - * * 106 LYS 106 E B 48.1 - - - - - - - - - 179.8 - 31.2 - * * 107 VAL 107 E B - 181.1 - - - - - - - - 178.2 -3.0 34.8 - * * 108 VAL 108 E B 58.4 - - - - - - - - - 183.5 - 32.2 - 109 GLY 109 e - - - - - - - - - - - 181.7 -3.3 - - +* +* 110 ALA 110 B - - - - - - - - - - 173.3 - 34.6 - * * 111 LYS 111 h B - - -65.5 180.1 - - - - - - 186.1 -.8 33.7 - * +* +* 112 LYS 112 H A - - -62.0 181.3 - -57.4 -50.2 - - - 183.5 - 34.5 - 113 ASP 113 H A - 185.7 - - - -69.1 -32.4 - - - 178.5 - 33.2 - 114 GLU 114 H A - - -59.4 - - -74.2 -37.3 - - - 178.4 - 34.3 - 115 LEU 115 H A - 187.2 - - - -63.4 -49.4 - - - 178.0 -2.7 35.9 - 116 GLN 116 H A - 183.8 - - - -59.1 -35.9 - - - 176.9 -2.7 35.9 - 117 SER 117 H A - 178.8 - - - -66.2 -40.5 - - - 178.9 -1.5 34.2 - 118 THR 118 H A - - -53.4 - - -67.8 -29.3 - - - 175.5 -2.3 33.4 - 119 ILE 119 H A - - -60.9 - - -64.5 -49.6 - - - 179.2 -1.8 32.9 - 120 ALA 120 H A - - - - - -66.9 -30.0 - - - 176.9 -2.0 32.9 - 121 LYS 121 H A - 186.2 - 185.6 - -56.6 -43.5 - - - 178.2 -2.0 38.0 - * * 122 HIS 122 H A - - -70.0 - - -83.7 -45.4 - - - 181.3 -1.5 33.4 - +* +* 123 LEU 123 h b - - -79.5 - - - - - - - 179.9 -3.5 33.4 - +* +* 124 ALA 124 - - - - - - - - - - - - -1.7 34.5 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * ** ** ** +** +* *7.4* * ** +* *7.4* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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: 56.3 181.7 -63.4 180.0 -70.9 -66.5 -39.5 69.8 - 2.7 179.8 -2.0 34.4 +* *7.4* *7.4* Standard deviations: 5.9 5.4 9.0 9.6 17.7 8.9 9.8 .0 - .0 3.0 .9 1.6 Numbers of values: 13 46 43 28 4 47 47 2 0 2 122 85 119 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_17 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 - 1.236 1.513 1.534 1.456 - 116.68 120.44 109.73 108.03 111.10 122.88 * * 2 GLY 2 1.310 1.231 1.502 - 1.435 120.68 116.69 120.64 - 112.89 - 122.63 * * 3 HIS 3 1.314 1.230 1.511 1.546 1.452 121.20 115.64 121.18 110.36 110.88 113.28 123.11 * +* +* 4 HIS 4 1.304 1.227 1.514 1.548 1.444 122.53 117.22 120.37 110.98 107.51 110.68 122.38 +* * +* 5 HIS 5 1.298 1.232 1.514 1.549 1.447 120.78 116.85 120.42 109.89 109.56 111.54 122.67 ** ** 6 HIS 6 1.327 1.224 1.512 1.568 1.458 120.44 116.85 120.93 111.92 110.93 114.01 122.17 +* ** ** 7 HIS 7 1.308 1.229 1.507 1.538 1.440 119.68 115.50 120.66 111.19 108.50 111.93 123.70 +* * +* 8 HIS 8 1.319 1.223 1.516 1.555 1.456 122.73 116.14 119.99 110.11 109.68 111.47 123.87 * * 9 LEU 9 1.345 1.237 1.520 1.555 1.478 123.09 116.23 121.19 110.62 111.57 113.41 122.58 * * * +* +* 10 GLU 10 1.300 1.239 1.520 1.525 1.436 121.28 115.18 121.17 111.77 111.44 110.05 123.64 ** * ** 11 MET 11 1.308 1.237 1.517 1.543 1.444 123.31 116.24 120.82 110.22 110.68 109.44 122.90 * * Residue-by-residue listing for refined_17 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 1.304 1.227 1.513 1.519 1.433 121.36 115.73 121.21 111.08 108.57 111.36 122.92 +* * +* 13 SER 13 1.291 1.244 1.520 1.550 1.425 122.22 117.09 120.34 111.30 107.72 109.20 122.57 +** * +* * +** 14 GLU 14 1.296 1.237 1.518 1.521 1.421 120.85 115.98 120.97 110.98 108.54 110.65 122.93 ** +* ** 15 GLU 15 1.304 1.238 1.509 1.548 1.434 121.59 116.01 120.59 109.64 109.73 111.59 123.39 +* * +* 16 GLY 16 1.320 1.224 1.499 - 1.447 121.15 116.12 120.71 - 112.62 - 123.17 17 GLN 17 1.303 1.240 1.493 1.530 1.426 122.10 114.80 121.26 111.97 110.70 111.44 123.94 +* * +* +* 18 VAL 18 1.282 1.236 1.529 1.558 1.441 123.08 117.80 119.68 109.55 108.50 109.69 122.52 *** * *** 19 ILE 19 1.330 1.232 1.520 1.545 1.442 120.38 116.93 120.38 109.04 109.07 110.33 122.69 20 ALA 20 1.311 1.229 1.507 1.523 1.442 121.11 115.81 121.22 111.23 110.17 111.61 122.97 * * 21 CYS 21 1.299 1.235 1.508 1.506 1.410 121.72 115.67 121.01 109.74 109.80 109.48 123.30 ** * +** +** 22 HIS 22 1.299 1.231 1.508 1.542 1.444 122.08 115.45 121.05 110.43 109.21 111.64 123.48 ** ** 23 THR 23 1.323 1.251 1.513 1.555 1.447 122.83 116.64 120.17 107.38 109.15 111.67 123.18 * * 24 VAL 24 1.322 1.217 1.539 1.576 1.442 121.08 115.57 121.31 111.75 108.53 112.91 123.09 * * * 25 GLU 25 1.336 1.233 1.529 1.521 1.459 123.30 116.28 120.62 109.43 110.60 108.88 123.08 26 THR 26 1.335 1.232 1.540 1.554 1.463 121.47 115.19 121.43 110.59 109.73 110.71 123.36 27 TRP 27 1.313 1.234 1.543 1.536 1.447 123.18 115.52 121.22 111.74 110.48 107.74 123.22 * +* +* 28 ASN 28 1.319 1.228 1.532 1.534 1.462 123.70 115.95 120.64 109.57 111.28 109.21 123.40 * * 29 GLU 29 1.329 1.231 1.533 1.528 1.473 123.36 116.21 120.84 109.35 112.22 109.25 122.94 30 GLN 30 1.308 1.230 1.514 1.489 1.421 123.03 117.17 120.23 112.60 113.20 108.49 122.59 * ** +* * * ** 31 LEU 31 1.315 1.220 1.507 1.486 1.405 121.24 116.20 120.34 110.93 110.41 109.97 123.46 ** +** +** 32 GLN 32 1.319 1.230 1.521 1.536 1.450 122.33 115.83 120.39 110.95 109.51 110.72 123.75 33 LYS 33 1.334 1.233 1.529 1.547 1.456 122.74 116.38 120.54 109.84 110.06 110.32 123.07 34 ALA 34 1.332 1.217 1.521 1.519 1.451 122.06 116.25 120.65 109.98 111.74 110.53 123.09 35 ASN 35 1.313 1.231 1.506 1.523 1.465 122.93 114.83 121.37 107.95 110.27 109.30 123.79 * * * 36 GLU 36 1.310 1.231 1.531 1.529 1.466 122.59 116.70 120.66 109.40 112.38 110.19 122.62 * * 37 SER 37 1.310 1.231 1.529 1.514 1.436 121.00 116.84 120.00 109.60 111.71 108.75 123.16 * * * * 38 LYS 38 1.352 1.236 1.503 1.501 1.474 122.52 114.23 122.04 113.08 111.71 111.13 123.63 +* * * +* +* 39 THR 39 1.298 1.242 1.511 1.520 1.407 122.43 116.09 121.18 108.27 107.21 110.85 122.71 ** +** * +** 40 LEU 40 1.261 1.241 1.548 1.565 1.420 120.96 117.25 120.30 113.38 106.33 108.87 122.44 *4.8* * +* +* +* +* *4.8* 41 VAL 41 1.307 1.238 1.538 1.564 1.440 121.38 115.68 121.09 112.09 111.86 110.47 123.20 +* * +* 42 VAL 42 1.313 1.238 1.521 1.537 1.441 123.15 116.14 120.94 109.28 109.00 111.65 122.92 * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.302 1.224 1.525 1.546 1.441 122.08 115.68 120.80 109.45 111.28 110.64 123.52 +* +* 44 ASP 44 1.301 1.234 1.522 1.526 1.452 123.88 116.67 120.39 109.27 110.60 109.58 122.90 +* * +* 45 PHE 45 1.311 1.234 1.529 1.527 1.434 122.19 116.37 120.13 110.43 109.23 109.65 123.49 * * * 46 THR 46 1.326 1.228 1.526 1.557 1.453 122.83 114.92 121.51 109.42 112.13 110.34 123.57 47 ALA 47 1.298 1.238 1.520 1.518 1.441 124.19 116.87 119.61 110.56 107.33 110.95 123.52 ** * * ** 48 SER 48 1.319 1.229 1.537 1.525 1.472 123.72 116.07 121.17 110.22 113.17 108.93 122.74 * * 49 TRP 49 1.304 1.232 1.536 1.533 1.446 122.46 117.53 120.43 111.95 113.65 109.86 122.00 +* +* 50 CYS 50 1.313 1.236 1.526 1.524 1.446 120.36 115.54 120.82 110.17 111.56 111.58 123.61 * * 51 GLY 51 1.329 1.233 1.526 - 1.457 122.43 118.92 119.58 - 113.44 - 121.50 * * * 52 PRO 52 1.365 1.227 1.531 1.539 1.471 122.53 116.53 120.76 111.16 112.46 104.32 122.70 +* * +* 53 CYS 53 1.319 1.226 1.531 1.518 1.453 121.36 116.45 120.74 109.25 110.42 111.25 122.79 54 ARG 54 1.336 1.235 1.542 1.544 1.466 122.62 115.10 121.67 110.58 109.59 109.40 123.23 55 PHE 55 1.314 1.231 1.545 1.546 1.448 123.35 116.96 120.71 110.32 111.77 108.84 122.32 * * 56 ILE 56 1.320 1.239 1.544 1.560 1.461 120.83 116.52 120.50 110.11 112.61 110.98 122.97 57 ALA 57 1.328 1.230 1.551 1.522 1.470 122.66 120.11 118.95 111.70 114.24 111.50 120.93 * +* * * * +* 58 PRO 58 1.380 1.239 1.531 1.526 1.484 122.23 115.89 121.11 109.35 112.54 103.35 123.00 ** * ** 59 PHE 59 1.319 1.216 1.522 1.543 1.443 121.73 116.51 120.59 111.90 109.39 110.04 122.82 60 PHE 60 1.325 1.235 1.540 1.539 1.473 122.50 116.08 121.16 111.41 110.70 109.79 122.75 61 ALA 61 1.318 1.239 1.536 1.520 1.454 121.88 116.55 120.97 110.72 110.92 110.38 122.48 62 ASP 62 1.328 1.228 1.509 1.511 1.466 121.69 114.84 121.42 109.53 108.59 111.07 123.74 63 LEU 63 1.319 1.232 1.536 1.530 1.447 123.74 116.02 120.61 110.56 110.89 108.91 123.35 * * 64 ALA 64 1.329 1.226 1.534 1.520 1.473 123.19 115.39 121.82 110.57 111.23 110.23 122.72 65 LYS 65 1.306 1.246 1.547 1.542 1.450 123.13 116.24 121.00 111.38 111.05 108.47 122.74 +* * * +* 66 LYS 66 1.320 1.233 1.522 1.540 1.461 121.88 116.51 120.60 109.53 111.02 110.71 122.89 67 LEU 67 1.317 1.219 1.520 1.510 1.436 121.98 116.31 121.26 112.02 111.66 109.71 122.41 * * * 68 PRO 68 1.330 1.238 1.530 1.523 1.464 123.31 117.29 120.46 109.52 114.15 102.35 122.24 69 ASN 69 1.311 1.226 1.517 1.535 1.454 120.60 115.71 121.12 111.45 110.22 110.75 123.12 * * 70 VAL 70 1.310 1.231 1.518 1.562 1.447 122.26 116.16 120.86 110.49 108.89 112.23 122.92 * * 71 LEU 71 1.303 1.228 1.518 1.523 1.420 121.82 116.93 120.30 109.31 109.50 108.54 122.74 +* +* * +* 72 PHE 72 1.310 1.242 1.492 1.513 1.443 121.05 115.46 121.40 109.08 109.33 112.43 123.14 * +* * +* 73 LEU 73 1.275 1.222 1.490 1.528 1.429 121.95 114.12 121.67 109.67 112.96 113.48 124.21 +*** +* +* * +* +*** 74 LYS 74 1.291 1.232 1.501 1.545 1.417 124.07 116.81 120.60 109.61 106.78 109.00 122.55 +** * ** * +* +** 75 VAL 75 1.276 1.244 1.484 1.553 1.418 120.14 116.15 120.49 110.00 106.81 112.16 123.36 +*** +* ** +* +*** Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 76 ASP 76 1.305 1.220 1.493 1.508 1.422 119.92 115.14 121.14 111.47 107.74 112.17 123.64 +* +* * +* * +* 77 THR 77 1.294 1.233 1.536 1.507 1.430 123.28 116.15 121.48 112.36 112.20 108.42 122.36 +** * * * +* +** 78 ASP 78 1.311 1.228 1.513 1.523 1.446 121.05 114.19 121.82 110.34 107.82 110.12 123.99 * * * * 79 GLU 79 1.308 1.243 1.520 1.523 1.444 124.55 114.18 122.00 106.73 109.19 107.80 123.80 * +* * +* +* +* 80 LEU 80 1.318 1.238 1.521 1.514 1.407 123.75 115.64 121.24 110.66 112.41 108.73 123.10 +** * * +** 81 LYS 81 1.306 1.228 1.523 1.537 1.448 122.39 115.55 121.16 110.45 109.66 110.17 123.25 +* +* 82 SER 82 1.321 1.237 1.538 1.511 1.452 122.88 116.53 120.74 110.68 111.87 108.50 122.72 * * 83 VAL 83 1.326 1.233 1.525 1.560 1.456 121.26 115.63 121.21 110.32 109.46 111.90 123.11 84 ALA 84 1.324 1.236 1.526 1.515 1.451 122.17 116.22 120.83 110.75 110.67 110.10 122.95 85 SER 85 1.325 1.235 1.534 1.524 1.445 121.89 116.96 120.50 110.92 111.75 109.93 122.50 86 ASP 86 1.329 1.231 1.519 1.534 1.467 121.03 115.68 121.31 110.45 110.22 111.28 122.93 87 TRP 87 1.320 1.230 1.524 1.522 1.446 122.21 116.06 120.32 111.34 112.52 111.12 123.62 88 ALA 88 1.344 1.238 1.528 1.534 1.473 123.62 115.95 120.82 110.96 111.53 110.30 123.17 * * * 89 ILE 89 1.324 1.238 1.516 1.556 1.447 121.96 115.45 121.08 110.00 109.29 111.78 123.45 90 GLN 90 1.303 1.232 1.512 1.529 1.430 122.02 115.84 121.15 109.04 109.92 109.88 122.99 +* * +* 91 ALA 91 1.315 1.229 1.505 1.518 1.438 121.23 115.52 121.15 110.28 111.34 110.32 123.33 * * 92 MET 92 1.295 1.237 1.520 1.523 1.436 122.59 118.12 120.11 109.66 109.28 110.21 121.77 ** * ** 93 PRO 93 1.328 1.238 1.526 1.526 1.452 123.29 116.00 121.34 109.86 111.92 102.59 122.65 94 THR 94 1.285 1.231 1.505 1.533 1.418 121.40 116.29 120.43 110.30 108.49 112.40 123.27 *** ** *** 95 PHE 95 1.300 1.226 1.494 1.522 1.405 121.97 115.69 120.75 110.08 108.29 109.89 123.55 ** * +** * +** 96 MET 96 1.287 1.237 1.497 1.522 1.429 122.43 115.49 121.05 109.54 108.88 110.70 123.46 *** * +* *** 97 PHE 97 1.279 1.245 1.495 1.503 1.392 122.75 115.41 121.82 109.21 110.21 109.02 122.77 +*** * * *** +*** 98 LEU 98 1.269 1.225 1.510 1.545 1.389 121.19 116.38 120.98 112.19 109.72 112.05 122.62 **** +*** * **** 99 LYS 99 1.281 1.234 1.470 1.524 1.422 121.75 114.35 120.91 109.81 109.64 111.30 124.69 *** +** +* * *** 100 GLU 100 1.314 1.235 1.549 1.532 1.447 124.32 115.99 121.11 110.10 110.24 110.95 122.88 * * * * 101 GLY 101 1.327 1.218 1.532 - 1.452 121.64 117.05 120.47 - 112.85 - 122.48 102 LYS 102 1.321 1.231 1.519 1.527 1.462 121.74 117.06 119.79 109.06 108.87 109.12 123.13 103 ILE 103 1.319 1.233 1.520 1.553 1.464 122.21 116.19 120.87 109.27 110.87 111.49 122.93 104 LEU 104 1.307 1.237 1.503 1.533 1.425 121.68 115.78 121.03 110.17 110.87 111.01 123.14 +* * +* +* 105 ASP 105 1.295 1.211 1.495 1.535 1.438 122.33 115.78 121.10 111.34 112.01 111.63 123.06 ** * * * ** 106 LYS 106 1.294 1.227 1.508 1.555 1.433 122.08 116.22 120.53 113.33 111.54 111.58 123.23 ** * * +* ** 107 VAL 107 1.304 1.235 1.523 1.565 1.444 122.20 116.67 120.42 109.15 109.11 111.61 122.90 +* +* Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 108 VAL 108 1.315 1.243 1.535 1.567 1.447 121.55 115.91 121.43 111.81 110.20 112.31 122.65 * * * 109 GLY 109 1.301 1.242 1.498 - 1.436 121.45 117.77 119.85 - 109.25 - 122.38 +* * * +* 110 ALA 110 1.307 1.240 1.506 1.511 1.432 119.31 115.43 121.16 109.79 111.52 110.08 123.40 +* * * +* 111 LYS 111 1.305 1.226 1.513 1.513 1.416 123.39 117.05 119.94 112.14 108.16 110.15 123.01 +* ** * * ** 112 LYS 112 1.316 1.231 1.527 1.505 1.433 123.05 116.63 120.49 109.99 113.52 109.21 122.86 * * * 113 ASP 113 1.317 1.233 1.530 1.533 1.464 121.51 116.40 120.81 111.06 111.25 110.77 122.77 114 GLU 114 1.329 1.235 1.513 1.526 1.467 121.66 115.76 121.04 109.21 110.12 111.37 123.20 115 LEU 115 1.319 1.224 1.497 1.514 1.446 122.40 114.66 121.37 108.65 108.67 110.13 123.95 * * 116 GLN 116 1.310 1.236 1.545 1.505 1.415 123.94 116.05 120.83 111.52 110.23 106.73 123.09 * * ** * ** ** 117 SER 117 1.327 1.229 1.521 1.549 1.458 122.35 115.72 121.11 110.95 109.44 110.32 123.14 118 THR 118 1.315 1.230 1.548 1.548 1.434 122.20 116.63 121.14 111.61 109.77 110.76 122.21 * * * * 119 ILE 119 1.326 1.217 1.530 1.559 1.447 121.14 116.92 120.41 110.73 109.67 112.45 122.60 120 ALA 120 1.323 1.229 1.522 1.507 1.474 121.80 115.21 121.08 110.58 111.04 111.45 123.69 121 LYS 121 1.314 1.224 1.521 1.501 1.455 124.23 115.28 121.41 108.53 108.99 106.47 123.31 * * * ** ** 122 HIS 122 1.313 1.230 1.524 1.524 1.433 122.38 116.86 120.46 110.67 111.65 110.92 122.67 * * * 123 LEU 123 1.322 1.244 1.511 1.512 1.409 122.69 114.78 121.40 111.24 111.86 110.38 123.76 +** +** 124 ALA 124 1.296 - 1.508 1.531 1.431 123.86 - - 110.73 107.61 110.63 - ** * * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.8* * +** ** +*** +* +* * +* +* ** * *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 1.261 1.352 1.312 .015 *4.8* +* * C-N (Pro) 1.341 .016 4 1.328 1.380 1.351 .022 ** C-O C-O 1.231 .020 123 1.211 1.251 1.232 .007 * * CA-C CH1E-C (except Gly) 1.525 .021 119 1.470 1.551 1.520 .015 +** * CH2G*-C (Gly) 1.516 .018 5 1.498 1.532 1.511 .014 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.507 1.534 1.520 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.507 1.576 1.552 .015 * * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.568 1.529 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.389 1.478 1.443 .018 +*** * NH1-CH2G* (Gly) 1.451 .016 5 1.435 1.457 1.445 .009 N-CH1E (Pro) 1.466 .015 4 1.452 1.484 1.468 .011 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 2.0 114 114.12 120.11 116.06 .85 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.12 118.92 117.31 .97 * CH1E-C-N (Pro) 116.9 1.5 4 115.89 117.29 116.43 .55 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.93 124.69 123.04 .53 * * O-C-N (Pro) 122.0 1.4 4 122.24 123.00 122.65 .27 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.31 124.55 122.18 1.05 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.68 122.43 121.47 .58 * C-N-CH1E (Pro) 122.6 5.0 4 122.23 123.31 122.84 .47 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.95 122.04 120.85 .51 * CH2G*-C-O (Gly) 120.8 2.1 5 119.58 120.71 120.25 .45 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.79 111.70 110.68 .49 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.38 112.36 110.14 1.23 * CH2E-CH1E-C (the rest) 110.1 1.9 84 106.73 113.38 110.44 1.17 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 106.33 114.24 110.22 1.59 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.25 113.44 112.21 1.50 * N-CH1E-C (Pro) 111.8 2.5 4 111.92 114.15 112.77 .83 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.08 111.61 110.73 .55 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.42 112.91 111.26 1.03 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.35 104.32 103.15 .77 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.47 114.01 110.24 1.42 ** ** ------------------------------------------------------------------------------------------------------------- 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_17 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] 100 88.5% Residues in additional allowed regions [a,b,l,p] 12 10.6% Residues in generously allowed regions [~a,~b,~l,~p] 1 .9% 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 88.5 83.8 10.0 .5 Inside b. Omega angle st dev 122 3.0 6.0 3.0 -1.0 BETTER 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 -1.0 Inside e. H-bond energy st dev 85 .9 .8 .2 .4 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 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 13 5.9 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 46 5.4 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 43 9.0 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 102 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 28 9.6 20.4 5.0 -2.2 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 88.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 3 Residue-by-residue listing for refined_17 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.23 Chi1-chi2 distribution -.10 Chi1 only .13 Chi3 & chi4 .30 Omega .12 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .48 ------ .25 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.