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 - - - -62.4 179.9 - - - - - - 179.1 - 34.6 - 2 GLY 2 - - - - - - - - - - - 179.6 - - - 3 HIS 3 l - 187.1 - - - - - - - - 184.3 - 34.3 - 4 HIS 4 A - 192.4 - - - - - - - - 170.6 - 34.2 - +* +* 5 HIS 5 l - 184.4 - - - - - - - - 174.6 - 31.8 - 6 HIS 6 b - - -73.2 - - - - - - - 178.2 - 32.0 - 7 HIS 7 B - - -64.2 - - - - - - - 171.6 - 36.0 - * * 8 HIS 8 a - - -64.7 - - - - - - - 176.4 - 32.2 - 9 LEU 9 S b - 191.8 - 173.9 - - - - - - 175.4 - 33.2 - 10 GLU 10 b - 197.5 - - - - - - - - 180.1 - 32.7 - 11 MET 11 b - 186.2 - - - - - - - - 177.5 - 33.0 - 12 ALA 12 a - - - - - - - - - - 187.9 - 35.3 - * * 13 SER 13 b 51.9 - - - - - - - - - 174.3 - 34.1 - 14 GLU 14 a - 186.4 - 174.1 - - - - - - 181.1 - 34.8 - 15 GLU 15 B - - -53.5 - - - - - - - 180.4 - 35.6 - 16 GLY 16 S - - - - - - - - - - - 180.4 -1.9 - - 17 GLN 17 S B 52.7 - - 180.2 - - - - - - 177.5 - 34.0 - 18 VAL 18 B 62.7 - - - - - - - - - 183.4 - 35.1 - 19 ILE 19 E B - - -60.1 178.2 - - - - - - 180.2 -2.7 31.6 - 20 ALA 20 E B - - - - - - - - - - 179.7 -.9 34.3 - +* +* 21 CYS 21 E B - - -55.7 - - - - - - - 176.5 -1.5 35.4 - 22 HIS 22 S A - - -66.4 - - - - - - - 181.8 -.5 34.0 - +* +* 23 THR 23 h B 58.2 - - - - - - - - - 177.5 - 34.7 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 24 VAL 24 H A - 180.8 - - - -71.2 -28.8 - - - 179.5 - 34.2 - 25 GLU 25 H A - 179.2 - 182.1 - -57.5 -52.2 - - - 179.3 - 36.2 - * * 26 THR 26 H A - - -54.2 - - -65.7 -44.1 - - - 179.6 - 34.6 - 27 TRP 27 H A - 176.7 - - - -57.5 -48.7 - - - 180.7 -1.8 35.1 - 28 ASN 28 H A - 182.8 - - - -59.8 -50.4 - - - 181.2 -3.6 35.7 - ** ** 29 GLU 29 H A - 181.1 - 182.5 - -59.2 -47.0 - - - 182.3 -2.4 34.4 - 30 GLN 30 H A - - -67.9 - - -64.6 -36.9 - - - 177.0 -2.6 32.4 - 31 LEU 31 H A - - -69.3 181.6 - -67.2 -45.1 - - - 177.7 -2.1 33.6 - 32 GLN 32 H A - 182.3 - 177.2 - -61.5 -39.5 - - - 176.5 -2.4 32.6 - 33 LYS 33 H A - 179.4 - 181.5 - -59.3 -50.3 - - - 182.9 -2.7 34.5 - 34 ALA 34 H A - - - - - -67.2 -44.3 - - - 182.9 -2.7 33.7 - 35 ASN 35 H A - 191.6 - - - -62.0 -54.5 - - - 182.1 -3.4 36.8 - * +* +* 36 GLU 36 H A - 187.1 - - - -60.8 -38.7 - - - 183.7 -2.6 34.2 - 37 SER 37 H A - - -51.9 - - -86.7 -1.0 - - - 183.9 -2.0 35.3 - +* *** *** 38 LYS 38 h l - - -82.4 176.3 - - - - - - 177.3 -1.3 31.7 - * * 39 THR 39 e B - - -50.7 - - - - - - - 181.4 -2.3 35.2 - * * 40 LEU 40 E B - 183.8 - 169.7 - - - - - - 185.8 -1.6 34.4 - 41 VAL 41 E B 60.5 - - - - - - - - - 177.0 -1.2 32.7 - * * 42 VAL 42 E B - 182.5 - - - - - - - - 183.7 -2.9 33.6 - * * 43 VAL 43 E B - 182.7 - - - - - - - - 177.2 -3.0 35.0 - * * 44 ASP 44 E B - 176.2 - - - - - - - - 176.8 -3.2 35.8 - +* +* 45 PHE 45 E B - - -65.6 - - - - - - - 180.6 -1.9 34.3 - 46 THR 46 E B - - -68.0 - - - - - - - 179.8 -3.2 34.6 - +* +* 47 ALA 47 t B - - - - - - - - - - 179.0 - 34.9 - 48 SER 48 T A - - -56.1 - - - - - - - 177.4 - 33.3 - 49 TRP 49 T A 59.1 - - - - - - - - - 181.1 - 32.8 - 50 CYS 50 t B - 173.4 - - - - - - -153.5 2.8 182.1 -1.4 33.6 - *6.3* *7.9* *7.9* 51 GLY 51 h - - - - - - - - - - - 182.3 - - - 52 PRO 52 H - - - - - -52.0 -52.0 -30.3 - - - 179.7 - 37.7 - * * * * 53 CYS 53 H A 57.7 - - - - -64.8 -32.9 - -153.5 2.8 176.8 - 35.7 - *6.3* *7.9* *7.9* 54 ARG 54 H A - 191.9 - - - -73.9 -38.6 - - - 179.3 -1.8 34.7 - 55 PHE 55 H A - 175.7 - - - -63.6 -33.7 - - - 182.9 -1.4 33.9 - 56 ILE 56 H A - 191.1 - - - -87.4 -11.3 - - - 182.9 -2.0 34.5 - +* ** ** 57 ALA 57 H A - - - - - -55.4 -50.2 - - - 179.6 -.5 30.7 - ** ** 58 PRO 58 H - - - - - -62.0 -62.0 -29.7 - - - 180.3 - 38.5 - * * 59 PHE 59 H A - 186.9 - - - -72.0 -40.5 - - - 180.4 - 35.7 - 60 PHE 60 H A - 192.0 - - - -73.0 -33.6 - - - 176.0 -2.2 34.8 - 61 ALA 61 H A - - - - - -67.5 -32.1 - - - 176.4 -2.5 33.8 - 62 ASP 62 H A - 180.1 - - - -64.8 -44.9 - - - 175.3 -1.4 35.8 - 63 LEU 63 H A - - -65.5 181.1 - -57.5 -45.0 - - - 178.1 -1.7 35.4 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 64 ALA 64 H A - - - - - -60.8 -31.3 - - - 177.8 -2.1 33.4 - 65 LYS 65 H A - 176.9 - 184.8 - -72.9 -37.7 - - - 186.9 -1.2 35.2 - * * * 66 LYS 66 H A - - -65.4 170.6 - -85.5 -32.7 - - - 182.1 -1.8 33.3 - +* +* 67 LEU 67 h B - - -68.7 171.7 - - - - - - 178.2 -2.6 32.3 - 68 PRO 68 S - - - - - -82.6 - - - - - 182.0 - 39.5 - +* +* +* 69 ASN 69 e A - - -64.5 - - - - - - - 181.3 - 35.5 - 70 VAL 70 E B - 179.8 - - - - - - - - 177.2 - 34.5 - 71 LEU 71 E B - 177.4 - - - - - - - - 179.1 -3.2 34.7 - +* +* 72 PHE 72 E B - - -59.4 - - - - - - - 183.7 -.5 34.0 - +* +* 73 LEU 73 E B - - -72.9 157.1 - - - - - - 181.9 -2.0 33.7 - * * 74 LYS 74 E B - 193.0 - - - - - - - - 180.7 -2.1 36.7 - 75 VAL 75 E B - 180.7 - - - - - - - - 176.6 -3.5 34.2 - +* +* 76 ASP 76 E B - 188.1 - - - - - - - - 185.6 -.8 34.3 - +* +* 77 THR 77 e A 57.8 - - - - - - - - - 174.3 -2.6 32.2 - 78 ASP 78 T A - 174.2 - - - - - - - - 178.8 - 34.8 - 79 GLU 79 T a - 187.0 - - - - - - - - 187.3 - 38.3 - * * * 80 LEU 80 h b - 186.2 - - - - - - - - 183.6 -3.1 34.3 - * * 81 LYS 81 H A 58.8 - - 178.8 - -68.7 -28.3 - - - 180.6 -1.4 32.5 - 82 SER 82 H A 53.1 - - - - -61.6 -36.9 - - - 176.9 - 32.4 - 83 VAL 83 H A - 174.0 - - - -68.1 -36.8 - - - 177.6 - 32.9 - 84 ALA 84 H A - - - - - -61.1 -43.0 - - - 178.1 -1.0 34.2 - * * 85 SER 85 H A - 182.8 - - - -68.1 -39.8 - - - 181.7 -2.3 34.6 - 86 ASP 86 H A - 182.1 - - - -63.4 -36.6 - - - 177.5 -2.4 33.9 - 87 TRP 87 h A - - -69.5 - - - - - - - 179.9 -2.3 32.6 - 88 ALA 88 T L - - - - - - - - - - 179.7 -.9 33.2 - +* +* 89 ILE 89 t b - - -57.2 - - - - - - - 182.4 -2.9 33.2 - * * 90 GLN 90 A - 183.9 - 180.9 - - - - - - 180.4 -1.4 35.3 - 91 ALA 91 S B - - - - - - - - - - 181.0 - 34.3 - 92 MET 92 S B - - -56.2 181.5 - - - - - - .1 - 35.1 - 93 PRO 93 e cis - - - - - -81.1 - - - - - 176.7 - 39.0 - * * * 94 THR 94 E B - - -55.7 - - - - - - - 177.6 -.7 34.4 - +* +* 95 PHE 95 E B - - -48.6 - - - - - - - 183.3 -3.2 36.6 - * +* +* 96 MET 96 E B - 189.7 - - - - - - - - 182.8 -3.2 34.4 - +* +* 97 PHE 97 E B - - -69.7 - - - - - - - 176.8 -3.0 35.7 - * * 98 LEU 98 E B - - -55.8 - - - - - - - 176.1 -2.9 35.3 - * * 99 LYS 99 E B - 177.1 - 169.8 - - - - - - 179.3 -3.0 32.8 - * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 GLU 100 e l - - -59.0 167.3 - - - - - - 185.5 -.9 34.3 - +* +* 101 GLY 101 T - - - - - - - - - - - 177.5 - - - 102 LYS 102 E B - - -57.2 178.9 - - - - - - 182.2 -1.9 35.9 - 103 ILE 103 E B - - -69.5 177.6 - - - - - - 177.8 - 33.0 - 104 LEU 104 E a - - -66.3 182.0 - - - - - - 185.4 -1.7 33.4 - 105 ASP 105 E B 55.5 - - - - - - - - - 180.0 -2.1 32.0 - 106 LYS 106 E B 55.1 - - - - - - - - - 175.7 - 32.3 - 107 VAL 107 E B - 181.2 - - - - - - - - 179.4 -3.0 35.1 - * * 108 VAL 108 E B 61.7 - - - - - - - - - 183.8 - 32.7 - 109 GLY 109 e - - - - - - - - - - - 179.8 -3.4 - - +* +* 110 ALA 110 B - - - - - - - - - - 180.1 - 33.9 - 111 LYS 111 h B - - -56.5 180.4 - - - - - - 186.4 -1.1 36.1 - * * * 112 LYS 112 H A - 186.1 - 177.9 - -69.1 -45.5 - - - 181.9 -.5 33.4 - ** ** 113 ASP 113 H A - 180.2 - - - -72.1 -42.9 - - - 179.6 - 33.2 - 114 GLU 114 H A - 183.4 - 181.7 - -67.8 -29.8 - - - 177.4 - 33.0 - 115 LEU 115 H A - 189.7 - - - -62.5 -49.8 - - - 174.4 -1.7 34.2 - 116 GLN 116 H A - - -79.9 - - -55.6 -34.2 - - - 178.4 -1.8 32.5 - 117 SER 117 H A - 180.9 - - - -66.6 -38.6 - - - 179.2 -1.6 34.0 - 118 THR 118 H A - - -53.2 - - -72.1 -38.4 - - - 177.1 -2.1 35.3 - 119 ILE 119 H A - - -58.4 175.1 - -63.6 -47.3 - - - 179.4 -2.7 34.0 - 120 ALA 120 H A - - - - - -63.2 -31.3 - - - 175.6 -3.2 33.1 - +* +* 121 LYS 121 H A - 178.7 - 191.5 - -58.6 -45.6 - - - 181.2 -1.5 37.6 - * * 122 HIS 122 H A - - -73.7 - - -76.2 -36.1 - - - 178.6 -1.6 33.0 - 123 LEU 123 h b - - -61.6 185.0 - - - - - - 181.2 -2.6 34.9 - 124 ALA 124 - - - - - - - - - - - - -1.5 34.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * +* +* *** *6.3* *7.9* +* ** +* *7.9* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.3 183.6 -62.8 177.8 -69.4 -65.9 -38.4 - -153.5 2.8 179.8 -2.1 34.3 *6.3* *7.9* *7.9* Standard deviations: 3.4 5.7 7.9 6.4 14.9 7.8 9.9 - .0 .0 3.2 .8 1.5 Numbers of values: 13 49 40 31 4 46 46 0 2 2 122 78 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_20 Page 5 ---------------------------------------- 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 - 1.235 1.504 1.536 1.469 - 116.31 120.44 108.84 109.79 111.61 123.24 2 GLY 2 1.316 1.237 1.504 - 1.434 120.93 116.36 120.05 - 110.99 - 123.59 * * 3 HIS 3 1.348 1.232 1.543 1.554 1.488 123.61 114.60 122.21 111.78 108.73 109.29 123.11 * * +* * +* 4 HIS 4 1.316 1.226 1.543 1.541 1.440 123.13 114.52 121.50 113.42 108.60 108.03 123.98 +* * +* 5 HIS 5 1.337 1.232 1.541 1.558 1.476 125.61 116.09 120.92 112.26 114.85 110.16 122.94 * ** * * ** 6 HIS 6 1.321 1.221 1.522 1.556 1.474 123.49 116.18 120.99 109.87 110.75 114.04 122.78 * ** ** 7 HIS 7 1.310 1.233 1.509 1.555 1.469 123.27 117.77 119.73 107.10 107.55 112.00 122.49 * * +* * +* 8 HIS 8 1.314 1.240 1.517 1.541 1.449 120.06 116.28 120.28 111.29 108.33 113.28 123.36 * * +* +* 9 LEU 9 1.323 1.245 1.521 1.570 1.451 122.73 115.61 120.93 111.64 108.69 111.65 123.37 ** ** 10 GLU 10 1.309 1.242 1.511 1.558 1.440 122.20 113.79 121.97 112.75 106.54 112.02 123.90 * * * * +* +* 11 MET 11 1.309 1.240 1.508 1.564 1.442 124.55 113.96 121.70 111.93 107.16 112.19 123.88 * +* +* * * +* 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 1.297 1.225 1.508 1.531 1.446 124.29 114.17 121.37 110.16 107.09 110.04 124.32 ** * * * ** 13 SER 13 1.328 1.243 1.515 1.521 1.437 124.43 114.79 121.45 111.27 113.68 108.69 123.70 * +* * +* 14 GLU 14 1.298 1.237 1.533 1.531 1.429 122.87 113.75 122.87 112.75 106.57 108.34 123.36 ** +* * * * +* * ** 15 GLU 15 1.323 1.245 1.518 1.551 1.439 123.77 116.95 120.22 108.44 108.06 111.37 122.82 * * * * * 16 GLY 16 1.314 1.235 1.497 - 1.456 120.28 115.24 121.44 - 111.35 - 123.32 * * * 17 GLN 17 1.303 1.242 1.483 1.524 1.423 122.58 114.26 121.37 109.91 110.48 111.45 124.36 +* +* +* +* 18 VAL 18 1.270 1.244 1.521 1.554 1.417 123.24 118.88 119.52 111.50 106.90 109.57 121.56 **** ** * * +* * **** 19 ILE 19 1.318 1.225 1.522 1.546 1.432 117.61 115.80 121.21 112.55 111.18 111.83 122.98 * ** +* ** 20 ALA 20 1.317 1.235 1.502 1.525 1.446 122.27 116.57 120.53 110.14 109.80 110.74 122.89 * * 21 CYS 21 1.300 1.226 1.509 1.508 1.410 121.20 115.95 121.01 109.73 109.57 109.65 123.01 ** * +** +** 22 HIS 22 1.296 1.228 1.514 1.544 1.446 121.93 115.98 121.07 110.17 109.24 111.59 122.94 ** ** 23 THR 23 1.326 1.247 1.511 1.556 1.444 121.73 116.26 120.46 108.49 109.79 112.15 123.28 24 VAL 24 1.317 1.203 1.520 1.554 1.446 121.81 115.87 120.76 109.87 109.17 111.68 123.35 * * 25 GLU 25 1.320 1.234 1.527 1.516 1.455 123.31 116.10 120.63 109.33 110.95 108.23 123.24 * * 26 THR 26 1.324 1.231 1.529 1.541 1.447 121.57 115.54 120.85 109.85 109.91 110.59 123.58 27 TRP 27 1.328 1.232 1.536 1.537 1.453 123.03 115.04 121.34 111.33 110.74 108.13 123.58 * * 28 ASN 28 1.311 1.240 1.520 1.532 1.457 124.28 115.88 120.60 109.53 110.95 108.95 123.51 * * * 29 GLU 29 1.332 1.235 1.520 1.531 1.454 121.99 116.22 120.65 109.62 110.94 110.79 123.12 30 GLN 30 1.323 1.231 1.513 1.492 1.412 122.13 117.22 120.26 111.82 113.37 110.24 122.51 +* ** ** 31 LEU 31 1.315 1.225 1.508 1.486 1.411 121.19 116.78 120.06 110.61 111.53 110.55 123.16 ** ** ** 32 GLN 32 1.324 1.229 1.520 1.534 1.448 120.91 115.90 120.41 111.57 109.80 111.75 123.66 33 LYS 33 1.327 1.235 1.524 1.541 1.449 122.34 116.57 120.38 109.64 110.21 110.94 123.03 34 ALA 34 1.331 1.230 1.518 1.520 1.451 121.43 116.00 120.62 110.34 111.50 110.72 123.37 35 ASN 35 1.319 1.234 1.508 1.533 1.465 123.01 115.02 121.43 108.21 109.76 108.92 123.50 36 GLU 36 1.311 1.228 1.544 1.537 1.462 122.38 116.81 120.77 110.36 111.58 110.05 122.39 * * 37 SER 37 1.319 1.235 1.541 1.521 1.444 121.31 117.23 119.87 109.61 112.48 108.84 122.90 38 LYS 38 1.349 1.237 1.501 1.516 1.477 122.25 115.89 121.04 110.64 112.61 112.69 123.02 * * * * * 39 THR 39 1.290 1.241 1.512 1.522 1.406 121.32 115.69 121.40 109.75 107.57 110.70 122.89 +** +** * +** 40 LEU 40 1.265 1.225 1.530 1.564 1.427 121.29 118.08 119.66 113.67 105.57 108.79 122.24 *4.6* +* +* +* ** * *4.6* 41 VAL 41 1.306 1.238 1.529 1.564 1.442 120.11 115.70 121.21 111.49 112.23 111.12 123.08 +* * +* 42 VAL 42 1.309 1.243 1.516 1.538 1.433 122.40 115.67 121.12 109.96 108.43 112.53 123.19 * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.297 1.232 1.522 1.549 1.439 122.16 115.93 120.48 109.07 110.55 110.80 123.59 ** ** 44 ASP 44 1.305 1.236 1.515 1.535 1.453 123.32 116.86 120.40 109.00 108.94 109.91 122.72 +* +* 45 PHE 45 1.304 1.244 1.530 1.524 1.421 121.60 115.82 120.86 110.74 110.46 109.94 123.31 +* +* +* 46 THR 46 1.319 1.210 1.529 1.538 1.450 123.39 115.86 121.10 110.52 110.55 109.72 123.02 * * * 47 ALA 47 1.296 1.229 1.497 1.510 1.444 123.16 117.45 119.49 109.76 108.51 110.50 123.06 ** * ** 48 SER 48 1.307 1.221 1.545 1.517 1.449 121.59 117.06 120.69 111.96 111.74 109.48 122.21 +* +* 49 TRP 49 1.336 1.221 1.534 1.555 1.465 121.13 116.02 121.36 111.04 111.01 111.61 122.62 * * 50 CYS 50 1.307 1.241 1.530 1.540 1.439 122.30 116.10 120.92 112.08 110.23 109.83 122.97 +* * * +* 51 GLY 51 1.314 1.230 1.533 - 1.452 121.58 119.03 119.68 - 114.12 - 121.29 * * * * 52 PRO 52 1.363 1.227 1.540 1.536 1.488 123.84 116.64 120.81 110.43 114.27 104.15 122.54 * * * * 53 CYS 53 1.314 1.232 1.532 1.502 1.465 122.47 115.03 121.91 109.50 110.72 108.59 123.06 * * * * 54 ARG 54 1.298 1.223 1.539 1.551 1.441 122.36 116.01 121.00 112.09 108.12 108.97 122.96 ** * * * ** 55 PHE 55 1.322 1.228 1.539 1.546 1.462 122.50 116.72 120.82 110.73 111.90 110.08 122.45 56 ILE 56 1.313 1.237 1.549 1.564 1.457 121.10 115.99 121.24 110.14 110.59 110.48 122.72 * * * 57 ALA 57 1.330 1.229 1.558 1.526 1.463 122.43 120.43 118.99 112.13 114.20 111.71 120.57 +* ** * * * +* ** 58 PRO 58 1.379 1.237 1.532 1.533 1.478 121.73 115.81 121.05 109.97 112.10 103.91 123.11 ** ** 59 PHE 59 1.321 1.227 1.528 1.540 1.459 122.72 115.06 121.68 110.19 108.81 108.89 123.25 60 PHE 60 1.311 1.227 1.539 1.534 1.455 123.25 116.24 121.12 111.95 109.48 108.27 122.64 * * * 61 ALA 61 1.326 1.231 1.531 1.521 1.464 121.90 115.52 121.14 110.69 109.90 110.59 123.34 62 ASP 62 1.323 1.231 1.502 1.518 1.470 123.25 114.32 121.64 109.37 109.08 109.27 124.04 * * 63 LEU 63 1.306 1.236 1.535 1.528 1.433 123.87 115.50 121.01 110.83 110.41 108.22 123.47 +* * * * +* 64 ALA 64 1.321 1.235 1.532 1.517 1.461 123.26 115.90 121.28 110.85 111.57 110.49 122.76 65 LYS 65 1.313 1.240 1.532 1.534 1.447 122.54 115.99 120.89 109.76 111.39 109.32 123.11 * * 66 LYS 66 1.307 1.231 1.521 1.518 1.453 122.04 117.75 119.95 111.20 114.32 109.45 122.30 +* * +* 67 LEU 67 1.313 1.225 1.521 1.513 1.436 120.77 116.52 121.28 111.95 113.39 110.30 122.19 * * * 68 PRO 68 1.338 1.235 1.541 1.527 1.470 123.21 116.00 121.02 110.00 112.27 102.40 122.97 69 ASN 69 1.334 1.239 1.506 1.527 1.452 122.91 115.67 121.10 108.80 110.51 110.18 123.23 70 VAL 70 1.309 1.234 1.515 1.558 1.427 122.32 115.82 120.72 109.66 109.32 111.61 123.44 * +* +* 71 LEU 71 1.297 1.238 1.509 1.536 1.430 122.37 116.34 120.58 110.28 108.87 110.50 123.06 ** * ** 72 PHE 72 1.299 1.241 1.501 1.517 1.430 121.29 115.30 121.49 109.92 109.23 111.62 123.20 ** * * ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 LEU 73 1.275 1.227 1.497 1.517 1.434 122.71 115.10 121.21 112.08 111.33 109.31 123.69 +*** * * * +*** 74 LYS 74 1.299 1.235 1.510 1.543 1.428 122.71 116.89 120.48 109.91 106.41 108.57 122.59 ** +* +* * ** 75 VAL 75 1.286 1.234 1.492 1.553 1.430 120.68 115.87 120.59 109.65 109.46 111.98 123.53 *** +* * *** 76 ASP 76 1.305 1.223 1.501 1.513 1.433 120.99 116.23 120.45 110.30 106.92 111.33 123.24 +* * * +* +* 77 THR 77 1.298 1.230 1.530 1.529 1.447 122.62 116.99 120.76 111.27 113.39 111.24 122.22 ** ** 78 ASP 78 1.314 1.238 1.500 1.531 1.456 120.52 113.48 121.89 109.90 107.52 110.89 124.59 * * * * * 79 GLU 79 1.304 1.232 1.512 1.522 1.432 124.29 114.16 122.08 106.65 109.69 108.42 123.72 +* * * * +* * +* 80 LEU 80 1.302 1.240 1.529 1.530 1.412 123.58 113.77 122.72 113.30 109.28 107.94 123.48 +* ** * * * +* +* ** 81 LYS 81 1.308 1.233 1.531 1.529 1.445 124.09 117.26 120.31 111.54 113.25 110.58 122.44 +* * +* 82 SER 82 1.327 1.229 1.533 1.526 1.453 120.93 116.13 120.83 112.28 111.41 110.62 122.98 * * 83 VAL 83 1.325 1.227 1.530 1.554 1.450 122.09 116.37 120.90 111.55 110.25 111.35 122.69 * * 84 ALA 84 1.328 1.233 1.522 1.515 1.460 121.56 115.59 120.96 110.17 109.82 110.63 123.44 85 SER 85 1.322 1.234 1.537 1.544 1.441 122.35 116.02 120.84 110.71 109.91 109.81 123.12 86 ASP 86 1.327 1.223 1.530 1.536 1.470 122.90 116.67 120.81 110.60 111.67 110.15 122.51 87 TRP 87 1.318 1.229 1.519 1.523 1.452 121.55 116.47 119.98 110.42 112.43 111.87 123.56 88 ALA 88 1.344 1.237 1.534 1.534 1.475 123.49 115.74 121.51 111.39 110.76 110.60 122.70 * * 89 ILE 89 1.320 1.242 1.524 1.558 1.448 121.88 115.09 121.55 110.81 109.49 112.08 123.28 90 GLN 90 1.304 1.233 1.521 1.525 1.440 122.89 115.95 121.20 110.50 110.02 108.83 122.85 +* +* 91 ALA 91 1.306 1.223 1.505 1.517 1.445 121.63 117.25 119.98 110.68 109.00 110.43 122.75 +* +* 92 MET 92 1.309 1.236 1.514 1.526 1.437 121.61 119.22 119.46 110.13 109.00 109.82 121.32 * * +* * +* 93 PRO 93 1.351 1.227 1.525 1.539 1.473 124.98 116.23 121.14 109.36 112.78 103.96 122.58 94 THR 94 1.298 1.229 1.514 1.522 1.429 121.71 116.18 120.37 109.91 109.30 111.06 123.39 ** +* ** 95 PHE 95 1.305 1.237 1.505 1.525 1.413 122.81 117.17 120.08 109.54 105.90 109.12 122.72 +* ** +* ** 96 MET 96 1.289 1.232 1.506 1.515 1.438 120.58 115.70 120.80 110.46 109.77 110.30 123.50 +** * +** 97 PHE 97 1.292 1.247 1.511 1.518 1.411 123.24 115.78 121.54 109.43 110.87 109.28 122.68 +** ** +** 98 LEU 98 1.295 1.223 1.509 1.556 1.426 120.92 116.93 120.57 107.01 107.68 113.40 122.47 ** * +* +* * +* ** 99 LYS 99 1.283 1.213 1.473 1.518 1.425 121.12 115.15 120.41 111.46 108.98 112.14 124.34 *** ** +* *** 100 GLU 100 1.320 1.224 1.537 1.525 1.459 124.38 116.19 121.07 108.93 110.85 111.36 122.73 * * 101 GLY 101 1.310 1.237 1.524 - 1.450 120.90 115.64 121.31 - 110.99 - 123.06 * * 102 LYS 102 1.324 1.233 1.527 1.539 1.447 122.73 117.05 120.09 109.35 107.84 109.79 122.86 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 103 ILE 103 1.313 1.234 1.523 1.566 1.462 122.29 116.02 120.77 110.74 112.04 111.55 123.19 * * 104 LEU 104 1.327 1.235 1.516 1.521 1.426 121.79 116.91 120.24 110.09 111.73 111.48 122.85 +* +* 105 ASP 105 1.323 1.226 1.503 1.520 1.459 121.19 115.41 121.15 110.11 113.63 112.47 123.40 * * * 106 LYS 106 1.319 1.245 1.533 1.562 1.449 122.09 115.75 121.33 112.00 112.33 111.08 122.92 +* +* 107 VAL 107 1.311 1.232 1.521 1.558 1.450 122.88 116.92 120.42 108.82 108.26 111.69 122.65 * * * 108 VAL 108 1.304 1.245 1.538 1.561 1.445 121.24 116.25 120.80 111.93 109.98 111.45 122.92 +* * +* 109 GLY 109 1.313 1.237 1.510 - 1.439 121.26 118.13 119.89 - 109.74 - 121.97 * * 110 ALA 110 1.318 1.238 1.499 1.526 1.438 118.78 115.09 121.68 110.61 108.71 111.29 123.23 * * +* +* 111 LYS 111 1.292 1.219 1.509 1.520 1.404 122.57 117.28 119.89 111.45 107.20 107.64 122.82 +** +** * +* +** 112 LYS 112 1.315 1.236 1.528 1.525 1.444 121.59 116.43 120.68 111.63 112.05 109.69 122.86 113 ASP 113 1.318 1.238 1.523 1.535 1.461 121.13 116.23 120.98 110.85 110.90 111.21 122.77 114 GLU 114 1.328 1.241 1.525 1.530 1.455 121.40 116.78 120.75 110.36 110.73 111.94 122.46 115 LEU 115 1.327 1.216 1.502 1.513 1.446 120.74 115.70 120.67 109.90 108.13 111.54 123.59 * * * 116 GLN 116 1.325 1.221 1.518 1.526 1.474 122.02 116.48 120.62 110.20 112.11 112.21 122.88 * * 117 SER 117 1.311 1.243 1.534 1.546 1.454 121.99 115.39 121.48 111.21 109.78 110.11 123.11 * * 118 THR 118 1.306 1.236 1.533 1.530 1.432 122.72 115.53 121.37 110.31 109.25 109.31 123.08 +* * * +* 119 ILE 119 1.319 1.222 1.534 1.560 1.443 122.25 116.52 120.42 110.36 109.36 111.41 123.00 120 ALA 120 1.337 1.225 1.521 1.517 1.466 122.42 116.51 120.51 110.58 111.49 111.16 122.97 121 LYS 121 1.324 1.237 1.516 1.500 1.460 122.14 114.37 121.62 106.76 109.49 108.83 124.00 * +* +* 122 HIS 122 1.314 1.233 1.524 1.533 1.437 123.28 117.32 120.07 110.95 112.45 110.96 122.61 * * * 123 LEU 123 1.328 1.242 1.521 1.495 1.401 122.14 115.39 121.16 110.38 110.57 109.31 123.39 +* +** +** 124 ALA 124 1.302 - 1.505 1.523 1.434 123.16 - - 110.69 108.64 110.82 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * ** ** +** ** ** * +* ** ** +* *4.6* ----------------------------------------------------------------------------------------------------------------------------------- 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 1.265 1.349 1.313 .014 *4.6* * * C-N (Pro) 1.341 .016 4 1.338 1.379 1.358 .015 ** * C-O C-O 1.231 .020 123 1.203 1.247 1.233 .008 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.473 1.558 1.521 .014 ** +* CH2G*-C (Gly) 1.516 .018 5 1.497 1.533 1.513 .013 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.534 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.522 1.566 1.549 .013 CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.570 1.531 .017 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.401 1.488 1.445 .017 +** +* NH1-CH2G* (Gly) 1.451 .016 5 1.434 1.456 1.446 .008 * N-CH1E (Pro) 1.466 .015 4 1.470 1.488 1.477 .007 * ------------------------------------------------------------------------------------------------------------- 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 2.0 114 113.48 120.43 116.05 1.08 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.24 119.03 116.88 1.46 * CH1E-C-N (Pro) 116.9 1.5 4 115.81 116.64 116.17 .31 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.57 124.59 123.04 .60 +* O-C-N (Pro) 122.0 1.4 4 122.54 123.11 122.80 .25 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 117.61 125.61 122.25 1.16 ** ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.28 121.58 120.99 .43 C-N-CH1E (Pro) 122.6 5.0 4 121.73 124.98 123.44 1.17 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.99 122.87 120.86 .64 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.68 121.44 120.47 .75 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.76 112.13 110.63 .58 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.49 112.55 110.37 1.01 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 106.65 113.67 110.48 1.40 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.57 114.85 110.07 1.89 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.74 114.12 111.44 1.45 N-CH1E-C (Pro) 111.8 2.5 4 112.10 114.27 112.85 .85 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.04 111.71 110.75 .41 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.31 112.53 111.18 .83 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.40 104.15 103.61 .70 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.64 114.04 110.26 1.43 +* ** ------------------------------------------------------------------------------------------------------------- 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] 96 85.0% Residues in additional allowed regions [a,b,l,p] 17 15.0% 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 85.0 83.8 10.0 .1 Inside b. Omega angle st dev 122 3.2 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 1.5 3.1 1.6 -1.0 Inside e. H-bond energy st dev 78 .8 .8 .2 .1 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 3.4 18.1 6.5 -2.3 BETTER b. Chi-1 trans st dev 49 5.7 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 40 7.9 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.2 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 31 6.4 20.4 5.0 -2.8 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% 85.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .82 2 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 -.24 Chi1-chi2 distribution -.03 Chi1 only .21 Chi3 & chi4 .50 Omega .08 ------ .02 ===== Main-chain covalent forces:- Main-chain bond lengths .03 Main-chain bond angles .43 ------ .26 ===== OVERALL AVERAGE .10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.