Residue-by-residue listing for refined_18 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 - - - -63.8 - - - - - - - 182.4 - 33.9 - 2 GLY 2 - - - - - - - - - - - 176.0 - - - 3 HIS 3 b - - -71.3 - - - - - - - 178.3 -2.2 33.6 - 4 HIS 4 B 61.1 - - - - - - - - - 185.6 -1.3 31.7 - * * 5 HIS 5 B - 190.3 - - - - - - - - 177.4 -.7 35.2 - +* +* 6 HIS 6 B - 185.8 - - - - - - - - 178.9 -.6 33.9 - +* +* 7 HIS 7 B - 186.8 - - - - - - - - 181.3 - 35.8 - 8 HIS 8 B 61.3 - - - - - - - - - 179.7 -.6 30.4 - +* +* 9 LEU 9 b - - -64.3 175.4 - - - - - - 176.0 - 33.7 - 10 GLU 10 b 51.2 - - - - - - - - - 181.2 -.6 31.0 - +* +* 11 MET 11 B - 181.2 - 180.5 - - - - - - 177.2 - 33.5 - 12 ALA 12 B - - - - - - - - - - 183.9 -.9 33.6 - +* +* 13 SER 13 b - - -55.1 - - - - - - - 182.8 -.7 35.3 - +* +* 14 GLU 14 a - 187.0 - - - - - - - - 179.9 - 33.6 - 15 GLU 15 XX - - -65.9 - - - - - - - 175.7 - 31.5 - **** **** 16 GLY 16 S - - - - - - - - - - - 182.7 -2.2 - - 17 GLN 17 e B 53.6 - - 177.7 - - - - - - 175.9 - 30.3 - * * 18 VAL 18 E B - 179.9 - - - - - - - - 179.1 -.6 35.0 - +* +* Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 19 ILE 19 E B - - -58.8 - - - - - - - 180.5 -2.9 33.6 - * * 20 ALA 20 E B - - - - - - - - - - 181.8 -.8 34.1 - +* +* 21 CYS 21 E B - - -50.2 - - - - - - - 174.4 -2.9 35.7 - * * * 22 HIS 22 S A - - -68.6 - - - - - - - 180.2 -.6 33.1 - +* +* 23 THR 23 h B 54.5 - - - - - - - - - 177.6 - 35.1 - 24 VAL 24 H A 62.7 - - - - -68.8 -22.7 - - - 179.4 - 33.3 - * * 25 GLU 25 H A - 181.1 - 184.6 - -62.9 -51.4 - - - 179.5 - 35.9 - * * 26 THR 26 H A - - -55.3 - - -60.5 -40.5 - - - 177.1 - 35.2 - 27 TRP 27 H A - 174.7 - - - -61.3 -52.6 - - - 182.1 -1.5 35.0 - * * 28 ASN 28 H A - 183.9 - - - -60.4 -47.0 - - - 182.0 -3.3 35.0 - +* +* 29 GLU 29 H A - 175.2 - 181.0 - -55.2 -48.3 - - - 179.6 -3.1 35.2 - * * 30 GLN 30 H A - - -85.0 - - -71.2 -33.2 - - - 179.3 -1.6 33.3 - * * 31 LEU 31 H A - - -71.4 181.8 - -66.7 -41.5 - - - 178.0 -1.8 34.2 - 32 GLN 32 H A - - -59.1 185.2 - -60.0 -47.2 - - - 181.7 -2.3 34.5 - 33 LYS 33 H A - 199.5 - - - -62.8 -46.3 - - - 182.7 -1.6 34.5 - 34 ALA 34 H A - - - - - -67.5 -29.6 - - - 182.2 -3.0 33.5 - * * 35 ASN 35 H A - 192.0 - - - -74.0 -54.1 - - - 179.1 -2.2 35.9 - * * 36 GLU 36 H A - - -79.1 - - -62.8 -39.0 - - - 178.9 -2.9 30.1 - * * * 37 SER 37 H A - - -59.9 - - -80.0 -10.8 - - - 182.1 -2.6 34.3 - * +** +** 38 LYS 38 h L - - -65.5 182.7 - - - - - - 180.8 -.6 32.4 - +* +* 39 THR 39 t B - - -47.5 - - - - - - - 178.0 -1.4 35.7 - * * 40 LEU 40 e B - 183.4 - 169.4 - - - - - - 185.1 - 34.1 - 41 VAL 41 E B 56.8 - - - - - - - - - 177.1 -1.0 33.5 - * * 42 VAL 42 E B - 180.0 - - - - - - - - 183.4 -1.4 34.2 - 43 VAL 43 E B - 186.4 - - - - - - - - 174.8 -2.7 34.4 - 44 ASP 44 E B - 167.4 - - - - - - - - 176.3 -2.3 35.0 - 45 PHE 45 E B - - -62.1 - - - - - - - 173.9 -3.0 37.1 - * * * 46 THR 46 E B - 190.4 - - - - - - - - 175.4 -1.6 32.9 - 47 ALA 47 t B - - - - - - - - - - 183.5 - 33.5 - 48 SER 48 T A - - -55.0 - - - - - - - 179.4 - 33.7 - 49 TRP 49 T A 49.7 - - - - - - - - - 179.1 - 31.1 - 50 CYS 50 h B - 174.8 - 218.2 - - - 56.2 - 2.0 181.4 -2.1 34.9 - ** +** +** 51 GLY 51 H - - - - - - -62.5 -62.1 - - - 180.2 -.6 - - ** +* ** 52 PRO 52 H - - - - - -57.5 -57.5 -32.3 - - - 180.1 - 39.1 - * * 53 CYS 53 H A - - -52.2 - - -69.6 -38.3 56.2 - 2.0 178.0 - 35.8 - +** +** Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 54 ARG 54 H A - 182.4 - 176.7 - -71.9 -28.8 - - - 177.4 -1.8 33.9 - 55 PHE 55 H A - 181.6 - - - -70.0 -36.2 - - - 182.2 -1.8 34.2 - 56 ILE 56 H A - 189.0 - - - -87.9 -22.3 - - - 182.0 -1.6 33.8 - +* +* +* 57 ALA 57 H A - - - - - -49.5 -49.9 - - - 180.1 -1.8 32.1 - * * 58 PRO 58 H - - - - - -55.2 -55.2 -38.3 - - - 181.7 - 38.4 - * * 59 PHE 59 H A - 185.4 - - - -71.8 -31.7 - - - 177.6 -.7 32.5 - +* +* 60 PHE 60 H A - 182.4 - - - -64.2 -37.6 - - - 178.1 -1.4 34.0 - 61 ALA 61 H A - - - - - -71.3 -30.6 - - - 178.3 -1.8 33.7 - 62 ASP 62 H A - 185.2 - - - -70.6 -43.4 - - - 177.3 -1.5 35.6 - 63 LEU 63 H A - 171.9 - - - -58.4 -42.4 - - - 176.6 -2.8 36.4 - 64 ALA 64 H A - - - - - -58.0 -32.2 - - - 180.3 -1.8 33.9 - 65 LYS 65 H A - 179.5 - 178.9 - -77.3 -29.5 - - - 181.2 -.8 33.9 - * +* +* 66 LYS 66 H A - 180.2 - 176.6 - -76.6 -35.5 - - - 177.9 -1.3 32.6 - 67 LEU 67 h b - - -70.0 - - - - - - - 183.6 -2.0 32.8 - 68 PRO 68 T - - - - - -72.7 - - - - - 185.4 - 40.0 - +* +* 69 ASN 69 T A 64.2 - - - - - - - - - 179.0 - 35.2 - 70 VAL 70 t B - 177.8 - - - - - - - - 182.4 -.6 33.3 - +* +* 71 LEU 71 E B - 204.3 - 180.0 - - - - - - 181.7 -1.3 35.5 - * * 72 PHE 72 E B - - -60.9 - - - - - - - 177.9 -1.2 34.4 - * * 73 LEU 73 E B - - -69.5 - - - - - - - 177.2 -2.5 33.7 - 74 LYS 74 E B - 189.8 - - - - - - - - 179.1 -3.2 33.4 - +* +* 75 VAL 75 E B - 176.2 - - - - - - - - 177.8 -2.7 34.5 - 76 ASP 76 E B - 183.3 - - - - - - - - 184.9 -1.1 33.4 - * * 77 THR 77 e A 55.9 - - - - - - - - - 177.8 -1.8 33.2 - 78 ASP 78 T A - 184.5 - - - - - - - - 175.2 - 35.0 - 79 GLU 79 T a - - -67.0 - - - - - - - 182.4 - 35.4 - 80 LEU 80 h b - - -69.0 - - - - - - - 181.4 -3.4 33.2 - +* +* 81 LYS 81 H A - - -60.4 177.5 - -69.2 -41.2 - - - 181.9 -1.2 33.7 - * * 82 SER 82 H A - - -56.0 - - -70.2 -39.7 - - - 178.1 - 33.3 - 83 VAL 83 H A - 179.1 - - - -67.4 -42.5 - - - 178.2 - 33.0 - 84 ALA 84 H A - - - - - -58.0 -45.9 - - - 180.9 -2.1 34.1 - 85 SER 85 H A - 182.7 - - - -68.0 -31.0 - - - 181.6 -2.4 33.9 - 86 ASP 86 H A - 184.1 - - - -69.1 -37.2 - - - 179.7 -1.8 34.8 - 87 TRP 87 h A - - -65.1 - - - - - - - 176.7 -2.0 32.8 - 88 ALA 88 T L - - - - - - - - - - 180.3 -1.1 33.2 - * * 89 ILE 89 t b - - -54.6 - - - - - - - 180.0 -3.0 33.4 - * * 90 GLN 90 A - 178.3 - 178.9 - - - - - - 182.9 -1.2 34.5 - * * 91 ALA 91 S B - - - - - - - - - - 180.8 - 33.6 - 92 MET 92 S B - - -53.2 170.3 - - - - - - -4.0 - 36.8 - 93 PRO 93 e cis - - - - - -94.7 - - - - - 174.3 - 40.0 - +** +* +** Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 94 THR 94 E B - - -59.8 - - - - - - - 178.5 -2.7 33.6 - 95 PHE 95 E B - - -62.2 - - - - - - - 181.4 -2.8 36.1 - * * 96 MET 96 E B - 182.5 - 178.2 - - - - - - 179.1 -3.3 34.3 - +* +* 97 PHE 97 E B - - -69.3 - - - - - - - 179.2 -2.8 35.8 - * * 98 LEU 98 E B 58.7 - - 168.9 - - - - - - 185.2 -2.1 31.4 - 99 LYS 99 E B - 177.5 - 177.6 - - - - - - 180.3 -3.7 35.1 - ** ** 100 GLU 100 T l - - -59.9 168.8 - - - - - - 183.8 - 34.1 - 101 GLY 101 T - - - - - - - - - - - 177.4 - - - 102 LYS 102 E B - - -62.9 185.2 - - - - - - 186.6 -2.1 32.9 - * * 103 ILE 103 E B - - -56.6 174.6 - - - - - - 173.6 - 35.2 - * * 104 LEU 104 E a - - -69.6 182.2 - - - - - - 185.3 -2.2 33.8 - 105 ASP 105 E B 48.4 - - - - - - - - - 181.5 -2.0 31.2 - 106 LYS 106 E B - - -63.4 - - - - - - - 168.9 - 37.7 - +* * +* 107 VAL 107 E B - 181.6 - - - - - - - - 181.4 -2.5 34.2 - 108 VAL 108 E B 59.3 - - - - - - - - - 182.3 -.5 32.3 - ** ** 109 GLY 109 e - - - - - - - - - - - 182.6 -3.1 - - * * 110 ALA 110 B - - - - - - - - - - 171.0 - 34.2 - +* +* 111 LYS 111 h B - - -64.9 181.1 - - - - - - 180.7 -.9 35.5 - * * 112 LYS 112 H A - 184.2 - 181.2 - -66.2 -40.2 - - - 179.9 - 33.3 - 113 ASP 113 H A 65.8 - - - - -62.1 -41.0 - - - 182.9 - 34.5 - 114 GLU 114 H A - 195.2 - - - -73.3 -35.7 - - - 177.2 - 35.1 - 115 LEU 115 H A - 185.7 - - - -62.0 -45.0 - - - 179.2 -2.2 35.9 - 116 GLN 116 H A - - -52.6 - - -60.3 -39.0 - - - 179.7 -2.5 34.1 - 117 SER 117 H A - - -57.7 - - -68.6 -38.6 - - - 176.8 -1.9 34.3 - 118 THR 118 H A - - -61.8 - - -65.0 -39.2 - - - 177.2 -2.6 33.7 - 119 ILE 119 H A - - -60.4 175.7 - -62.7 -44.5 - - - 178.7 -2.7 33.7 - 120 ALA 120 H A - - - - - -67.0 -31.7 - - - 176.4 -2.3 33.1 - 121 LYS 121 H A - 185.4 - 181.6 - -62.5 -41.4 - - - 177.3 -2.0 36.4 - 122 HIS 122 H A - - -76.4 - - -71.5 -35.5 - - - 178.3 -2.0 32.4 - 123 LEU 123 h B - - -64.7 181.6 - - - - - - 178.2 -2.0 35.3 - 124 ALA 124 - - - - - - - - - - - - - 34.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * ** +** +* +** +** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.4 183.4 -62.7 179.7 -70.0 -66.2 -38.8 56.2 - 2.0 179.6 -1.9 34.2 +** +** Standard deviations: 5.4 6.8 7.7 8.7 18.2 7.1 9.0 .0 - .0 3.0 .8 1.7 Numbers of values: 14 44 44 29 4 47 47 2 0 2 122 87 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_18 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_18 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 - 1.231 1.505 1.545 1.465 - 116.85 119.84 110.22 109.06 111.64 123.31 2 GLY 2 1.323 1.231 1.517 - 1.452 121.59 116.14 120.65 - 113.83 - 123.19 3 HIS 3 1.316 1.242 1.500 1.543 1.444 122.41 116.19 120.61 109.56 109.64 112.61 123.11 * * * 4 HIS 4 1.308 1.227 1.507 1.557 1.441 120.60 116.22 121.10 112.48 108.49 112.93 122.63 * * * * * 5 HIS 5 1.289 1.229 1.509 1.534 1.431 120.71 116.46 120.68 110.51 109.75 109.38 122.86 +** * +** 6 HIS 6 1.296 1.227 1.499 1.537 1.430 121.35 115.51 120.98 110.52 108.18 111.80 123.43 ** * * * ** 7 HIS 7 1.290 1.234 1.512 1.542 1.431 122.02 117.44 119.38 110.96 106.41 108.84 123.15 +** * +* +** 8 HIS 8 1.322 1.230 1.509 1.565 1.459 120.16 115.16 121.14 111.79 110.96 114.36 123.65 +* ** ** 9 LEU 9 1.300 1.239 1.505 1.538 1.428 122.22 115.55 121.26 110.61 110.22 111.33 123.09 ** +* ** 10 GLU 10 1.293 1.237 1.517 1.559 1.435 122.01 117.32 120.15 112.57 109.92 113.31 122.43 +** * * * +* +** 11 MET 11 1.312 1.232 1.509 1.530 1.452 120.71 116.01 120.47 109.71 110.87 111.96 123.51 * * 12 ALA 12 1.306 1.239 1.516 1.519 1.431 121.75 115.38 121.35 111.32 109.00 110.83 123.27 +* * +* Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 SER 13 1.288 1.245 1.539 1.513 1.437 123.01 117.38 120.22 111.38 110.25 107.68 122.40 +** * +* +** 14 GLU 14 1.325 1.237 1.541 1.543 1.446 120.78 116.37 120.00 111.65 110.27 110.11 123.61 15 GLU 15 1.347 1.233 1.525 1.548 1.486 124.88 115.97 121.72 109.37 113.72 113.86 122.30 * * +* +* +* 16 GLY 16 1.309 1.232 1.492 - 1.438 120.04 117.32 120.22 - 113.06 - 122.46 * * * 17 GLN 17 1.311 1.235 1.479 1.503 1.423 118.55 112.30 122.72 111.05 114.06 113.62 124.97 * ** * +* +* +* * * +* * ** 18 VAL 18 1.275 1.239 1.507 1.555 1.426 124.24 117.96 119.71 109.40 107.15 111.80 122.31 +*** +* * * +*** 19 ILE 19 1.299 1.235 1.522 1.548 1.437 119.47 116.13 121.01 110.43 109.98 111.64 122.86 ** * * ** 20 ALA 20 1.310 1.235 1.505 1.523 1.443 121.94 116.42 120.78 110.63 109.52 110.69 122.79 * * 21 CYS 21 1.297 1.230 1.510 1.507 1.410 121.13 115.80 120.92 109.47 110.13 109.29 123.25 ** * +** +** 22 HIS 22 1.303 1.228 1.502 1.530 1.448 122.39 115.20 121.04 110.60 109.51 112.19 123.73 +* * +* 23 THR 23 1.320 1.250 1.509 1.559 1.436 122.90 116.63 119.99 108.48 108.23 112.18 123.38 * * * 24 VAL 24 1.314 1.213 1.533 1.570 1.443 121.94 115.94 120.97 111.20 109.42 111.62 123.05 * * * 25 GLU 25 1.330 1.232 1.527 1.517 1.454 122.99 115.88 120.59 108.86 110.26 109.27 123.53 26 THR 26 1.333 1.237 1.535 1.538 1.455 122.34 115.02 121.29 109.92 110.00 109.63 123.68 * * 27 TRP 27 1.316 1.232 1.544 1.543 1.443 122.96 115.41 121.21 112.07 110.41 107.73 123.32 * +* +* 28 ASN 28 1.313 1.239 1.541 1.531 1.460 123.94 115.92 120.61 110.18 112.37 108.73 123.46 * * * * 29 GLU 29 1.329 1.251 1.539 1.540 1.472 123.70 115.85 121.17 110.00 111.86 108.89 122.98 * * * 30 GLN 30 1.308 1.226 1.517 1.502 1.419 123.04 117.53 120.00 112.28 113.09 108.78 122.47 * * ** * * ** 31 LEU 31 1.324 1.222 1.493 1.483 1.420 121.77 116.89 119.74 109.02 112.43 110.92 123.35 +* ** ** ** 32 GLN 32 1.314 1.233 1.517 1.516 1.445 120.74 115.24 121.19 108.70 109.56 111.85 123.51 * * 33 LYS 33 1.325 1.233 1.539 1.554 1.444 122.10 116.99 120.37 111.29 109.07 109.71 122.57 * * 34 ALA 34 1.340 1.232 1.522 1.523 1.456 120.84 116.03 120.79 110.54 111.31 110.78 123.16 35 ASN 35 1.318 1.231 1.503 1.517 1.452 122.09 115.43 121.23 108.60 109.82 109.81 123.33 * * 36 GLU 36 1.310 1.235 1.525 1.537 1.460 121.65 117.63 120.16 111.51 113.24 113.67 122.19 * +* +* 37 SER 37 1.318 1.237 1.544 1.520 1.444 120.30 116.49 120.19 110.00 111.54 110.07 123.30 38 LYS 38 1.353 1.232 1.520 1.515 1.478 123.51 115.26 121.70 110.97 111.34 111.68 122.98 +* * * +* 39 THR 39 1.298 1.245 1.522 1.523 1.426 122.58 115.78 121.20 108.91 109.13 110.12 122.99 ** +* ** 40 LEU 40 1.285 1.240 1.534 1.567 1.424 121.87 116.74 120.57 113.21 105.90 109.69 122.66 *** +* +* +* +* *** 41 VAL 41 1.295 1.233 1.534 1.565 1.429 121.40 116.33 120.85 112.07 111.28 109.86 122.78 ** +* * ** Residue-by-residue listing for refined_18 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 1.311 1.239 1.516 1.541 1.446 122.17 117.04 120.38 109.50 108.27 112.09 122.57 * * * 43 VAL 43 1.310 1.235 1.528 1.560 1.443 120.60 115.60 120.78 108.87 111.16 111.76 123.61 * * 44 ASP 44 1.312 1.241 1.511 1.546 1.466 123.28 117.28 120.23 109.56 109.73 110.53 122.43 * * 45 PHE 45 1.317 1.246 1.522 1.527 1.415 120.13 116.00 120.92 107.36 108.92 109.79 123.08 ** * ** 46 THR 46 1.298 1.222 1.524 1.543 1.426 122.73 117.65 119.84 111.35 108.33 112.34 122.50 ** +* * * ** 47 ALA 47 1.299 1.237 1.514 1.512 1.439 121.53 116.24 120.26 110.90 108.24 111.50 123.50 ** * ** 48 SER 48 1.309 1.228 1.550 1.524 1.465 123.74 117.12 120.34 110.86 113.57 109.32 122.53 * * * * 49 TRP 49 1.328 1.239 1.542 1.548 1.458 121.62 116.62 120.94 112.15 113.38 111.82 122.42 * * 50 CYS 50 1.310 1.234 1.526 1.530 1.450 121.57 115.92 120.62 110.18 110.52 109.64 123.45 * * 51 GLY 51 1.332 1.230 1.530 - 1.463 122.18 119.21 119.58 - 114.31 - 121.22 * * * 52 PRO 52 1.365 1.226 1.524 1.533 1.485 122.59 115.31 121.48 109.60 111.73 103.53 123.20 +* * * +* 53 CYS 53 1.303 1.219 1.532 1.507 1.446 122.93 116.06 121.47 110.09 110.02 108.15 122.45 +* * * +* 54 ARG 54 1.312 1.224 1.533 1.529 1.453 122.15 115.57 121.53 111.63 109.57 109.74 122.91 * * 55 PHE 55 1.315 1.230 1.541 1.542 1.450 122.60 116.83 120.67 110.76 111.02 109.87 122.49 * * 56 ILE 56 1.321 1.241 1.557 1.575 1.464 121.39 115.50 121.14 110.72 110.93 110.70 123.32 +* * +* 57 ALA 57 1.336 1.235 1.557 1.524 1.477 124.12 120.14 118.99 110.86 114.72 110.84 120.86 +* * +* * * * +* 58 PRO 58 1.376 1.236 1.527 1.536 1.472 122.11 116.77 120.65 110.14 112.81 104.00 122.55 ** ** 59 PHE 59 1.326 1.225 1.527 1.535 1.441 120.34 116.64 120.65 111.30 110.34 112.01 122.69 60 PHE 60 1.326 1.233 1.534 1.543 1.459 121.46 115.59 121.36 111.21 109.13 110.38 123.01 61 ALA 61 1.324 1.238 1.536 1.522 1.454 122.11 115.92 121.07 110.93 110.59 110.29 123.00 62 ASP 62 1.326 1.230 1.498 1.517 1.474 122.68 114.39 121.45 108.68 109.56 110.17 124.16 * * 63 LEU 63 1.305 1.235 1.529 1.515 1.414 124.90 115.07 121.23 111.23 109.91 106.59 123.68 +* ** +* ** ** 64 ALA 64 1.318 1.231 1.532 1.521 1.456 123.06 116.30 121.07 110.48 111.48 110.20 122.63 65 LYS 65 1.323 1.236 1.530 1.542 1.456 121.99 116.28 120.88 111.37 110.95 109.75 122.83 66 LYS 66 1.319 1.234 1.529 1.538 1.450 121.56 116.77 120.46 111.61 111.59 111.16 122.77 67 LEU 67 1.321 1.226 1.535 1.545 1.442 121.88 117.45 120.73 111.08 110.62 111.77 121.82 68 PRO 68 1.349 1.243 1.526 1.544 1.480 123.32 115.39 121.31 108.62 113.21 103.24 123.30 * * 69 ASN 69 1.313 1.226 1.523 1.528 1.441 122.98 116.91 120.55 110.24 111.84 108.78 122.53 * * * 70 VAL 70 1.311 1.235 1.508 1.557 1.442 121.18 116.23 120.64 110.73 108.77 112.32 123.11 * * 71 LEU 71 1.301 1.234 1.526 1.550 1.431 121.29 116.79 120.50 111.42 106.84 108.80 122.67 ** * +* * ** 72 PHE 72 1.307 1.236 1.505 1.528 1.440 121.16 115.61 121.26 109.30 110.40 111.34 123.13 +* +* Residue-by-residue listing for refined_18 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 1.286 1.236 1.491 1.548 1.433 122.70 115.83 121.01 108.41 109.36 113.83 123.16 *** +* * +* *** 74 LYS 74 1.284 1.238 1.502 1.548 1.407 121.51 115.42 121.05 112.81 108.18 110.54 123.51 *** * +** * * *** 75 VAL 75 1.293 1.237 1.493 1.550 1.427 122.20 115.91 120.74 109.48 108.72 111.96 123.33 +** +* +* +** 76 ASP 76 1.297 1.230 1.513 1.510 1.423 120.46 115.96 120.70 111.48 108.17 111.25 123.31 ** +* * ** 77 THR 77 1.305 1.233 1.536 1.542 1.443 122.88 117.06 120.34 110.76 113.16 110.58 122.59 +* +* 78 ASP 78 1.325 1.235 1.502 1.529 1.467 121.89 113.86 122.15 110.17 107.60 110.29 123.99 * * * * 79 GLU 79 1.302 1.235 1.537 1.512 1.414 123.95 117.06 120.68 110.43 111.22 108.40 122.25 +* ** * * ** 80 LEU 80 1.320 1.231 1.517 1.533 1.416 122.12 115.53 121.26 110.47 111.26 111.66 123.15 ** ** 81 LYS 81 1.309 1.238 1.524 1.524 1.454 122.72 116.42 120.88 110.67 111.97 110.20 122.69 * * 82 SER 82 1.324 1.236 1.522 1.519 1.444 121.10 116.47 120.51 111.27 110.66 110.62 123.00 83 VAL 83 1.324 1.226 1.528 1.557 1.452 121.09 116.42 120.67 110.90 109.71 112.13 122.85 84 ALA 84 1.328 1.231 1.523 1.516 1.458 121.79 116.02 120.87 109.97 110.78 110.59 123.07 85 SER 85 1.323 1.235 1.541 1.540 1.443 121.72 116.79 120.55 111.04 111.19 109.97 122.63 86 ASP 86 1.335 1.230 1.515 1.530 1.470 121.75 115.94 121.07 108.99 110.77 110.81 122.96 87 TRP 87 1.315 1.238 1.523 1.528 1.443 121.86 115.52 120.53 111.35 111.36 111.18 123.95 * * 88 ALA 88 1.349 1.235 1.528 1.533 1.476 124.48 116.42 120.83 111.00 112.13 110.45 122.69 * +* +* 89 ILE 89 1.316 1.244 1.524 1.550 1.443 121.04 115.27 121.44 109.81 109.93 112.60 123.24 90 GLN 90 1.304 1.231 1.518 1.535 1.441 122.31 116.20 121.01 110.49 110.37 110.06 122.77 +* +* 91 ALA 91 1.308 1.231 1.509 1.510 1.437 121.16 116.03 121.20 110.96 110.57 110.60 122.76 * * * 92 MET 92 1.294 1.242 1.521 1.507 1.431 121.31 118.59 119.76 107.40 109.10 109.74 121.64 ** * * * * ** 93 PRO 93 1.324 1.243 1.539 1.521 1.447 123.77 117.10 120.68 109.50 111.55 102.28 122.18 * * * 94 THR 94 1.297 1.234 1.514 1.530 1.427 120.21 116.13 120.70 109.85 109.38 112.26 123.17 ** +* ** 95 PHE 95 1.302 1.244 1.493 1.516 1.410 122.09 116.24 120.67 108.83 107.40 110.30 123.06 +* +* +** * +** 96 MET 96 1.286 1.237 1.497 1.511 1.415 120.64 114.77 121.33 110.96 110.01 109.95 123.89 *** * ** *** 97 PHE 97 1.287 1.248 1.506 1.513 1.397 123.45 116.26 121.03 109.97 109.06 109.12 122.69 *** *** *** 98 LEU 98 1.289 1.217 1.523 1.568 1.417 120.79 116.73 120.68 112.48 110.18 112.91 122.57 +** +* ** * * +** 99 LYS 99 1.293 1.237 1.490 1.520 1.435 122.44 114.72 120.83 110.58 110.04 109.21 124.42 +** +* * +** 100 GLU 100 1.328 1.230 1.532 1.521 1.459 124.36 115.63 121.36 109.86 110.48 110.83 122.96 * * 101 GLY 101 1.316 1.224 1.524 - 1.441 121.40 117.12 120.56 - 112.39 - 122.33 102 LYS 102 1.319 1.221 1.514 1.514 1.451 121.25 116.29 120.44 110.87 110.37 111.68 123.27 103 ILE 103 1.305 1.226 1.534 1.557 1.468 123.32 116.50 120.62 108.98 112.34 109.99 122.86 +* +* Residue-by-residue listing for refined_18 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 ----------------------------------------------------------------------------------------------------------------------------------- 104 LEU 104 1.327 1.227 1.504 1.524 1.436 121.87 115.96 120.71 109.02 110.52 112.43 123.31 * * * * 105 ASP 105 1.318 1.236 1.514 1.532 1.444 121.78 114.83 121.53 111.64 113.79 112.01 123.58 106 LYS 106 1.315 1.238 1.513 1.531 1.447 123.82 116.06 120.76 105.80 110.56 109.88 123.18 * ** ** 107 VAL 107 1.304 1.238 1.509 1.557 1.439 121.44 116.72 120.22 109.29 106.05 113.21 123.04 +* * +* * +* 108 VAL 108 1.298 1.245 1.528 1.560 1.430 121.32 115.75 121.52 112.43 110.97 111.25 122.70 ** * +* ** 109 GLY 109 1.311 1.240 1.506 - 1.432 120.80 117.57 120.16 - 109.81 - 122.27 * * * 110 ALA 110 1.307 1.235 1.506 1.522 1.429 119.33 114.77 121.53 110.53 110.37 110.36 123.57 +* +* * +* 111 LYS 111 1.298 1.237 1.485 1.501 1.413 123.97 118.23 119.21 108.91 107.07 110.99 122.55 ** +* * ** * * * ** 112 LYS 112 1.299 1.227 1.525 1.519 1.424 119.87 115.82 120.48 111.16 109.75 111.16 123.61 ** +* * ** 113 ASP 113 1.325 1.234 1.530 1.553 1.473 123.44 116.14 121.24 109.47 110.78 110.85 122.59 * * 114 GLU 114 1.319 1.221 1.505 1.520 1.447 121.87 115.45 120.96 110.24 108.60 109.76 123.58 115 LEU 115 1.318 1.218 1.504 1.509 1.436 122.16 115.47 120.95 108.76 109.06 109.88 123.57 * * * 116 GLN 116 1.324 1.240 1.514 1.544 1.478 121.54 115.33 120.92 108.06 109.67 113.13 123.74 * * +* +* 117 SER 117 1.317 1.223 1.530 1.519 1.437 122.17 115.90 121.06 111.29 109.87 109.40 123.01 * * 118 THR 118 1.316 1.232 1.536 1.541 1.434 122.57 116.86 120.59 111.21 110.58 110.41 122.52 * * 119 ILE 119 1.328 1.224 1.533 1.553 1.450 121.07 116.24 120.75 110.65 109.30 111.47 122.93 120 ALA 120 1.327 1.220 1.529 1.521 1.462 122.02 116.08 120.63 110.95 111.30 110.95 123.29 121 LYS 121 1.325 1.233 1.515 1.506 1.462 123.40 114.83 121.72 108.63 109.64 108.86 123.44 * * 122 HIS 122 1.312 1.228 1.512 1.518 1.437 122.22 116.98 120.36 111.01 112.26 111.64 122.65 * * * 123 LEU 123 1.317 1.241 1.524 1.495 1.400 122.26 115.72 121.00 110.34 111.27 108.56 123.26 +* *** * *** 124 ALA 124 1.301 - 1.508 1.528 1.437 123.25 - - 110.67 108.15 110.99 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** ** *** +* +* * ** +* ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 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 1.275 1.353 1.312 .014 +*** +* * C-N (Pro) 1.341 .016 4 1.324 1.376 1.354 .020 * ** C-O C-O 1.231 .020 123 1.213 1.251 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.479 1.557 1.520 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.492 1.530 1.514 .014 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.533 1.521 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.523 1.575 1.551 .012 * CH1E-CH2E (the rest) 1.530 .020 84 1.483 1.568 1.529 .017 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.397 1.486 1.442 .018 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.432 1.463 1.445 .011 * N-CH1E (Pro) 1.466 .015 4 1.447 1.485 1.471 .014 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 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 2.0 114 112.30 120.14 116.15 .95 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.14 119.21 117.47 .99 * CH1E-C-N (Pro) 116.9 1.5 4 115.31 117.10 116.14 .80 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.86 124.97 123.00 .57 * * O-C-N (Pro) 122.0 1.4 4 122.18 123.30 122.81 .46 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.55 124.90 122.02 1.18 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.04 122.18 121.20 .73 C-N-CH1E (Pro) 122.6 5.0 4 122.11 123.77 122.95 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.99 122.72 120.80 .56 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.58 120.65 120.23 .38 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.97 111.32 110.75 .32 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.48 112.43 110.22 1.05 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 105.80 113.21 110.36 1.32 ** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.90 114.72 110.20 1.66 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.81 114.31 112.68 1.58 N-CH1E-C (Pro) 111.8 2.5 4 111.55 113.21 112.32 .70 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.20 111.50 110.70 .33 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.63 113.21 111.45 .97 * * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.28 104.00 103.26 .63 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.59 114.36 110.58 1.59 ** ** ------------------------------------------------------------------------------------------------------------- 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_18 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] 101 89.4% 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] 1 .9% ---- ------ 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 89.4 83.8 10.0 .6 Inside b. Omega angle st dev 122 3.0 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 87 .8 .8 .2 .1 Inside f. Overall G-factor 124 .1 -.4 .3 1.5 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 14 5.4 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 44 6.8 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 44 7.7 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 29 8.7 20.4 5.0 -2.3 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% 89.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.7 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_18 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.22 Chi1-chi2 distribution -.23 Chi1 only .03 Chi3 & chi4 .26 Omega .12 ------ -.04 ===== Main-chain covalent forces:- Main-chain bond lengths -.04 Main-chain bond angles .45 ------ .25 ===== OVERALL AVERAGE .06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.