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 - - - -63.0 - - - - - - - 182.4 - 33.7 - 2 GLY 2 - - - - - - - - - - - 180.1 - - - 3 HIS 3 B - 178.3 - - - - - - - - 178.1 - 33.6 - 4 HIS 4 B - 188.6 - - - - - - - - 188.7 -.9 33.5 - * * * 5 HIS 5 S ~l - - -62.7 - - - - - - - 187.5 - 29.8 - ** * * ** 6 HIS 6 B - 177.8 - - - - - - - - 181.2 - 36.3 - 7 HIS 7 ~l - 177.6 - - - - - - - - 176.7 - 30.1 - ** * ** 8 HIS 8 B - 174.8 - - - - - - - - 176.6 - 35.2 - 9 LEU 9 b - - -66.8 - - - - - - - 185.5 - 32.8 - 10 GLU 10 B - 181.2 - 178.5 - - - - - - 175.0 -1.2 34.2 - * * 11 MET 11 b - 180.1 - 178.8 - - - - - - 182.3 -.8 33.5 - +* +* 12 ALA 12 b - - - - - - - - - - 175.9 -.6 32.5 - +* +* 13 SER 13 B - - -58.5 - - - - - - - 182.9 -1.7 34.5 - 14 GLU 14 b - 181.1 - 174.9 - - - - - - 178.3 -1.0 32.0 - * * 15 GLU 15 B 60.0 - - 184.4 - - - - - - 183.8 -1.8 34.4 - 16 GLY 16 S - - - - - - - - - - - 187.2 -1.2 - - * * * 17 GLN 17 e B 59.4 - - 174.5 - - - - - - 175.7 - 30.7 - 18 VAL 18 E B 64.7 - - - - - - - - - 179.1 - 34.8 - 19 ILE 19 E B - - -58.9 178.9 - - - - - - 178.8 -3.1 33.2 - * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 ALA 20 E B - - - - - - - - - - 180.0 - 34.1 - 21 CYS 21 E B - - -54.1 - - - - - - - 178.9 -.8 35.0 - +* +* 22 HIS 22 S A - - -61.4 - - - - - - - 182.8 - 34.7 - 23 THR 23 h B 55.6 - - - - - - - - - 177.7 - 35.2 - 24 VAL 24 H A 63.1 - - - - -74.3 -22.7 - - - 178.0 - 32.5 - * * 25 GLU 25 H A - 186.9 - - - -62.0 -51.7 - - - 178.7 - 35.4 - * * 26 THR 26 H A - - -54.6 - - -64.9 -37.7 - - - 177.7 - 34.6 - 27 TRP 27 H A - 166.5 - - - -53.4 -55.9 - - - 181.2 -1.6 35.1 - * * * 28 ASN 28 H A - 182.3 - - - -67.7 -40.8 - - - 183.3 -2.7 35.3 - 29 GLU 29 H A - 184.6 - 175.6 - -61.7 -46.7 - - - 179.8 -2.5 33.8 - 30 GLN 30 H A - - -70.2 - - -69.0 -34.1 - - - 176.7 -3.1 32.7 - * * 31 LEU 31 H A - - -70.9 179.8 - -66.3 -41.5 - - - 176.4 -1.6 34.2 - 32 GLN 32 H A - - -61.6 - - -68.6 -34.0 - - - 173.8 -2.4 31.3 - * * 33 LYS 33 H A - 178.9 - 181.0 - -61.2 -47.0 - - - 180.7 -2.1 34.3 - 34 ALA 34 H A - - - - - -65.6 -40.9 - - - 180.3 -2.7 33.8 - 35 ASN 35 H A - 190.6 - - - -59.9 -54.6 - - - 181.3 -2.8 37.7 - * * * * 36 GLU 36 H A - 180.2 - - - -62.1 -39.1 - - - 183.7 -3.0 34.2 - * * 37 SER 37 h A - - -55.3 - - - - - - - 180.6 -2.5 34.5 - 38 LYS 38 T l - 187.5 - 186.3 - - - - - - 181.9 -1.4 33.7 - 39 THR 39 t B - - -52.5 - - - - - - - 180.0 -2.3 35.9 - 40 LEU 40 E B - 183.5 - 168.6 - - - - - - 184.2 -2.7 34.8 - 41 VAL 41 E B 59.7 - - - - - - - - - 177.5 - 32.2 - 42 VAL 42 E B - 180.9 - - - - - - - - 183.0 -2.4 33.9 - 43 VAL 43 E B - 183.4 - - - - - - - - 177.4 -3.1 34.5 - * * 44 ASP 44 E B - 170.4 - - - - - - - - 176.9 -3.5 35.1 - +* +* 45 PHE 45 E B - - -61.8 - - - - - - - 189.2 -2.6 35.7 - +* +* 46 THR 46 E B - 190.6 - - - - - - - - 174.0 -2.8 37.4 - * * * * 47 ALA 47 t B - - - - - - - - - - 178.5 - 33.5 - 48 SER 48 T A - 177.3 - - - - - - - - 182.3 - 34.2 - 49 TRP 49 T A 53.1 - - - - - - - - - 177.9 - 30.1 - * * 50 CYS 50 h B 46.9 - - - - - - - -118.6 2.8 185.7 -1.2 30.1 - * *** *7.9* * * *7.9* 51 GLY 51 H - - - - - - -60.7 -65.0 - - - 181.2 -.6 - - ** +* ** 52 PRO 52 H - - - - - -54.0 -54.0 -30.8 - - - 180.7 - 38.7 - * * * 53 CYS 53 H A - - -49.3 153.0 - -69.4 -38.9 - -118.6 2.8 180.5 - 36.2 - * * *** *7.9* *7.9* 54 ARG 54 H A - 189.7 - - - -75.5 -30.3 - - - 180.2 -1.5 34.4 - 55 PHE 55 H A - 180.7 - - - -70.9 -29.3 - - - 183.9 -2.0 34.6 - 56 ILE 56 H A - 192.3 - - - -87.3 -11.3 - - - 182.3 -1.4 34.4 - +* ** ** 57 ALA 57 H A - - - - - -63.5 -45.8 - - - 180.0 -.5 31.1 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 PRO 58 H - - - - - -54.6 -54.6 -38.0 - - - 180.5 - 38.5 - * * 59 PHE 59 H A - 184.4 - - - -72.5 -33.7 - - - 177.8 - 33.4 - 60 PHE 60 H A - 182.3 - - - -65.5 -33.7 - - - 177.2 -1.3 34.8 - * * 61 ALA 61 H A - - - - - -73.5 -28.3 - - - 177.7 -1.9 33.7 - 62 ASP 62 H A - 188.0 - - - -71.8 -44.6 - - - 175.0 -1.1 35.1 - * * 63 LEU 63 H A - - -70.4 179.4 - -53.7 -37.5 - - - 179.7 -2.6 35.5 - 64 ALA 64 H A - - - - - -63.7 -34.8 - - - 178.9 -1.3 32.2 - 65 LYS 65 H A - - -67.3 - - -79.2 -27.2 - - - 185.5 -.9 34.5 - * * * * 66 LYS 66 H A - 184.6 - 180.0 - -74.6 -35.9 - - - 181.5 -1.6 33.9 - 67 LEU 67 h B - - -62.5 178.0 - - - - - - 182.4 -1.8 33.0 - 68 PRO 68 S - - - - - -70.2 - - - - - 184.4 - 37.8 - * * 69 ASN 69 e b - 182.5 - - - - - - - - 184.4 - 33.0 - 70 VAL 70 E B 66.2 - - - - - - - - - 175.3 -1.3 34.5 - 71 LEU 71 E B - 181.6 - - - - - - - - 177.6 -3.2 34.6 - +* +* 72 PHE 72 E B - - -62.5 - - - - - - - 182.4 -1.6 33.3 - 73 LEU 73 E B - - -66.4 165.9 - - - - - - 176.4 -2.1 34.7 - 74 LYS 74 E B - - -68.0 - - - - - - - 179.3 -2.1 36.6 - 75 VAL 75 E B - 180.1 - - - - - - - - 179.3 -3.2 34.1 - +* +* 76 ASP 76 E B - 181.3 - - - - - - - - 183.7 -.6 33.2 - +* +* 77 THR 77 e A 54.7 - - - - - - - - - 176.7 -2.5 32.2 - 78 ASP 78 T A - 181.6 - - - - - - - - 173.2 -.5 34.1 - * ** ** 79 GLU 79 T A - - -72.9 - - - - - - - 182.6 - 35.7 - 80 LEU 80 h b - - -68.4 - - - - - - - 179.4 -3.3 33.9 - +* +* 81 LYS 81 H A - - -61.2 183.6 - -69.7 -39.3 - - - 182.6 -1.9 33.0 - 82 SER 82 H A - - -54.6 - - -64.8 -36.7 - - - 178.2 - 33.6 - 83 VAL 83 H A - 178.8 - - - -62.0 -45.9 - - - 179.4 - 33.4 - 84 ALA 84 H A - - - - - -62.5 -45.4 - - - 179.8 -1.4 33.8 - 85 SER 85 H A - - -57.0 - - -67.6 -31.7 - - - 179.9 -2.5 33.9 - 86 ASP 86 H A - 180.6 - - - -71.3 -36.7 - - - 178.3 -2.3 34.4 - 87 TRP 87 h A - - -68.8 - - - - - - - 176.4 -2.2 32.0 - 88 ALA 88 T L - - - - - - - - - - 180.1 -.8 33.7 - +* +* 89 ILE 89 t B - - -60.3 179.8 - - - - - - 183.3 -3.1 33.7 - * * 90 GLN 90 A 67.3 - - - - - - - - - 182.4 -.9 33.3 - +* +* 91 ALA 91 S B - - - - - - - - - - 182.2 - 33.0 - 92 MET 92 S B - - -58.7 171.3 - - - - - - -2.1 - 36.3 - 93 PRO 93 e cis - - - - - -92.6 - - - - - 177.1 - 39.8 - ** +* ** 94 THR 94 E B - - -63.7 - - - - - - - 179.0 -1.4 33.1 - 95 PHE 95 E B - - -62.4 - - - - - - - 177.3 -3.0 36.8 - * * 96 MET 96 E B - 179.6 - 174.4 - - - - - - 183.6 -3.1 32.6 - * * 97 PHE 97 E B - - -67.0 - - - - - - - 177.9 -3.3 36.6 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 LEU 98 E B - - -53.7 - - - - - - - 175.3 -2.7 35.7 - 99 LYS 99 E B - 179.1 - 170.8 - - - - - - 178.9 -3.2 32.9 - +* +* 100 GLU 100 T l - - -56.6 173.3 - - - - - - 181.0 - 34.0 - 101 GLY 101 T - - - - - - - - - - - 178.1 - - - 102 LYS 102 E B - - -57.4 178.2 - - - - - - 182.0 -2.1 36.0 - 103 ILE 103 E B - - -57.8 177.3 - - - - - - 181.1 - 33.6 - 104 LEU 104 E a - - -62.8 184.3 - - - - - - 189.1 -2.4 34.8 - +* +* 105 ASP 105 E B - 181.4 - - - - - - - - 183.4 -2.2 33.5 - 106 LYS 106 E B - 190.1 - 183.5 - - - - - - 178.9 - 35.2 - 107 VAL 107 E B - 182.2 - - - - - - - - 178.2 -3.3 35.4 - +* +* 108 VAL 108 E B 58.8 - - - - - - - - - 181.7 -.5 32.0 - +* +* 109 GLY 109 e - - - - - - - - - - - 183.2 -2.5 - - 110 ALA 110 B - - - - - - - - - - 170.8 - 34.4 - +* +* 111 LYS 111 h B - - -67.4 182.9 - - - - - - 178.4 -.9 34.7 - * * 112 LYS 112 H A - 186.5 - - - -57.9 -43.9 - - - 184.8 - 36.1 - 113 ASP 113 H A - 187.3 - - - -65.8 -43.3 - - - 179.5 - 33.9 - 114 GLU 114 H A - - -64.1 - - -69.4 -33.8 - - - 179.4 - 33.8 - 115 LEU 115 H A - 188.2 - - - -64.3 -46.2 - - - 176.9 -2.1 35.3 - 116 GLN 116 H A - - -64.1 - - -59.9 -30.8 - - - 179.2 -2.2 33.7 - 117 SER 117 H A - 180.6 - - - -64.9 -40.1 - - - 177.5 -1.2 33.8 - * * 118 THR 118 H A - - -59.5 - - -72.2 -32.8 - - - 176.5 -1.5 33.1 - 119 ILE 119 H A - - -59.8 178.4 - -66.2 -41.1 - - - 176.5 -1.9 33.1 - 120 ALA 120 H A - - - - - -68.8 -31.5 - - - 179.0 -2.7 33.7 - 121 LYS 121 H A - 192.3 - 175.8 - -65.0 -36.2 - - - 175.6 -1.7 36.0 - 122 HIS 122 H A - - -80.1 - - -77.7 -29.1 - - - 179.3 -1.7 33.1 - * * 123 LEU 123 h b - 191.7 - - - - - - - - 182.5 -1.5 35.2 - 124 ALA 124 - - - - - - - - - - - - -.6 34.4 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * * ** +* ** *** *7.9* +* ** +* *7.9* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.1 182.8 -62.3 176.9 -67.8 -66.5 -38.2 - -118.6 2.8 180.0 -2.0 34.2 *** *7.9* *7.9* Standard deviations: 5.9 5.4 6.2 6.7 18.1 6.9 9.1 - .0 .0 3.3 .8 1.7 Numbers of values: 12 47 43 29 4 46 46 0 2 2 122 84 119 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 - 1.239 1.511 1.536 1.460 - 116.75 120.39 110.30 109.33 111.68 122.87 2 GLY 2 1.304 1.239 1.499 - 1.426 120.97 116.32 120.38 - 109.76 - 123.25 +* +* +* 3 HIS 3 1.301 1.234 1.510 1.544 1.436 121.57 115.85 120.92 111.11 110.04 110.94 123.23 ** * ** 4 HIS 4 1.298 1.230 1.530 1.537 1.437 121.67 116.85 119.71 112.78 107.62 109.99 123.44 ** * * * ** 5 HIS 5 1.322 1.237 1.496 1.552 1.461 123.67 113.35 122.36 112.91 107.64 115.46 124.12 * * * * * * +** +** 6 HIS 6 1.303 1.239 1.525 1.550 1.432 124.07 115.72 119.90 110.97 108.87 107.56 124.38 +* * * +* +* 7 HIS 7 1.332 1.232 1.516 1.555 1.462 124.91 114.84 121.57 112.26 111.79 113.81 123.57 * +* * +* +* 8 HIS 8 1.308 1.236 1.521 1.549 1.443 122.70 116.46 120.20 110.62 109.25 109.30 123.32 * * 9 LEU 9 1.314 1.238 1.506 1.553 1.446 121.77 115.06 121.40 111.07 108.30 112.74 123.45 * * * * * 10 GLU 10 1.293 1.232 1.512 1.519 1.422 122.54 115.25 121.34 111.32 111.74 109.13 123.39 +** +* +** 11 MET 11 1.292 1.246 1.508 1.539 1.424 122.20 115.59 121.29 111.50 107.68 111.56 122.97 +** +* * +** 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.308 1.235 1.507 1.526 1.429 121.18 115.48 121.28 111.36 111.24 111.72 123.11 * +* +* 13 SER 13 1.305 1.242 1.510 1.524 1.421 121.96 115.81 121.09 111.14 108.30 110.04 123.05 +* +* * +* 14 GLU 14 1.303 1.234 1.522 1.534 1.420 121.26 114.49 121.95 113.50 110.52 110.65 123.35 +* +* +* +* 15 GLU 15 1.306 1.249 1.512 1.538 1.431 122.79 117.70 119.84 111.60 108.05 109.91 122.47 +* * * +* 16 GLY 16 1.306 1.235 1.514 - 1.423 118.50 117.84 119.78 - 112.58 - 122.38 +* +* * +* 17 GLN 17 1.331 1.240 1.480 1.511 1.444 119.12 111.42 123.65 109.13 114.84 114.61 124.92 ** * ** +* * ** * ** 18 VAL 18 1.255 1.238 1.537 1.541 1.393 124.47 117.96 120.05 112.05 108.31 109.02 121.94 *5.3* *** +* * * * *5.3* 19 ILE 19 1.310 1.226 1.520 1.561 1.444 119.97 116.68 120.76 111.17 109.75 111.70 122.50 * * 20 ALA 20 1.301 1.233 1.516 1.521 1.440 121.09 117.00 120.48 110.60 109.70 110.56 122.50 +* +* 21 CYS 21 1.311 1.232 1.512 1.511 1.428 121.38 116.04 120.88 109.58 109.62 110.27 123.08 * +* +* 22 HIS 22 1.303 1.226 1.516 1.535 1.444 121.50 115.96 121.12 109.12 109.64 111.35 122.92 +* +* 23 THR 23 1.318 1.248 1.516 1.555 1.447 122.07 116.63 120.23 108.33 109.64 111.56 123.13 24 VAL 24 1.322 1.240 1.546 1.570 1.449 121.45 115.88 121.19 111.54 109.73 112.31 122.91 * * * 25 GLU 25 1.337 1.235 1.525 1.533 1.455 122.44 115.96 120.58 109.43 109.32 109.93 123.42 26 THR 26 1.336 1.225 1.530 1.544 1.454 122.09 115.55 120.81 109.94 109.89 110.54 123.62 27 TRP 27 1.327 1.228 1.535 1.539 1.458 123.25 116.22 120.67 111.06 111.57 108.19 123.05 * * 28 ASN 28 1.316 1.231 1.525 1.531 1.461 121.81 115.32 121.34 109.57 110.29 109.63 123.31 29 GLU 29 1.314 1.229 1.535 1.529 1.455 123.13 116.85 120.62 111.41 111.58 109.48 122.51 * * 30 GLN 30 1.324 1.228 1.512 1.495 1.419 121.63 116.71 120.61 111.56 112.67 110.37 122.68 +* ** ** 31 LEU 31 1.311 1.229 1.508 1.490 1.411 121.85 116.84 120.31 110.34 111.65 110.00 122.84 * +* ** ** 32 GLN 32 1.309 1.228 1.510 1.528 1.444 120.94 116.63 120.15 112.53 110.55 112.40 123.20 * * * * 33 LYS 33 1.332 1.231 1.516 1.532 1.452 121.24 116.22 120.60 108.93 109.59 111.95 123.18 34 ALA 34 1.336 1.222 1.515 1.523 1.444 121.55 115.81 120.67 110.70 110.48 110.72 123.50 35 ASN 35 1.320 1.239 1.513 1.528 1.465 122.98 114.15 121.75 107.02 109.13 108.85 124.06 * +* +* 36 GLU 36 1.315 1.225 1.538 1.535 1.461 123.62 117.13 120.75 110.57 112.52 109.55 122.12 * * 37 SER 37 1.309 1.246 1.543 1.514 1.448 121.20 116.70 119.98 110.37 112.62 109.00 123.32 * * 38 LYS 38 1.355 1.238 1.552 1.519 1.444 124.11 114.78 122.81 112.09 109.90 109.32 122.30 +* * * * * +* 39 THR 39 1.298 1.236 1.511 1.527 1.415 122.55 115.07 121.70 109.26 108.97 109.71 123.23 ** ** * ** 40 LEU 40 1.262 1.216 1.526 1.568 1.428 122.37 118.29 119.65 113.30 105.57 108.61 122.02 *4.8* +* +* * +* ** * *4.8* 41 VAL 41 1.300 1.228 1.528 1.566 1.439 119.88 115.87 121.15 112.11 112.19 111.31 122.95 ** * * * ** 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 1.306 1.238 1.511 1.540 1.440 122.36 116.27 120.86 109.58 108.47 112.51 122.85 +* +* 43 VAL 43 1.294 1.230 1.517 1.542 1.433 121.01 115.26 120.70 109.11 110.94 111.43 124.04 ** * ** 44 ASP 44 1.300 1.239 1.516 1.533 1.442 124.18 116.08 120.90 110.18 109.26 109.75 122.94 ** * ** 45 PHE 45 1.301 1.238 1.513 1.515 1.428 122.34 117.13 119.93 110.25 107.85 109.15 122.93 ** +* * ** 46 THR 46 1.311 1.226 1.533 1.547 1.436 120.61 115.88 120.82 108.66 110.73 107.68 123.28 * * ** ** 47 ALA 47 1.314 1.229 1.514 1.514 1.436 123.29 116.88 120.51 110.50 108.74 111.85 122.61 * * * 48 SER 48 1.296 1.241 1.550 1.543 1.446 122.06 116.72 120.94 111.69 110.83 109.11 122.32 ** * ** 49 TRP 49 1.333 1.233 1.536 1.542 1.451 121.20 118.25 119.86 111.94 114.95 112.59 121.88 * * * * 50 CYS 50 1.318 1.238 1.539 1.544 1.462 120.03 114.97 121.41 113.92 112.15 111.83 123.61 ** ** 51 GLY 51 1.339 1.233 1.526 - 1.466 123.40 119.07 119.45 - 115.16 - 121.47 +* * +* 52 PRO 52 1.364 1.230 1.530 1.544 1.485 122.99 115.43 121.36 110.07 112.24 103.70 123.18 * * * 53 CYS 53 1.309 1.225 1.529 1.510 1.447 122.92 116.02 121.60 109.07 109.98 108.74 122.36 * * * 54 ARG 54 1.309 1.230 1.539 1.535 1.436 121.25 115.69 121.06 111.17 109.45 109.76 123.22 * * * 55 PHE 55 1.326 1.235 1.536 1.546 1.468 123.18 116.71 120.88 109.97 111.65 109.86 122.41 56 ILE 56 1.316 1.237 1.555 1.575 1.459 121.11 115.51 121.58 110.80 110.04 110.10 122.87 * * * 57 ALA 57 1.328 1.230 1.563 1.526 1.465 122.96 120.53 118.94 111.70 114.84 111.28 120.53 +* ** * * +* ** 58 PRO 58 1.378 1.240 1.536 1.530 1.481 122.10 116.57 120.78 110.14 113.16 103.60 122.64 ** ** 59 PHE 59 1.327 1.225 1.531 1.536 1.456 121.40 115.71 121.16 111.44 110.18 110.59 123.10 60 PHE 60 1.315 1.230 1.537 1.546 1.464 123.22 115.77 121.32 111.98 109.37 108.26 122.88 * * 61 ALA 61 1.321 1.237 1.537 1.521 1.452 122.02 116.31 121.12 110.88 110.56 110.37 122.57 62 ASP 62 1.328 1.239 1.501 1.521 1.473 121.88 114.22 121.48 109.08 108.19 110.86 124.29 * * * 63 LEU 63 1.322 1.237 1.527 1.534 1.436 124.20 115.58 120.88 110.26 110.61 108.71 123.52 * * * * 64 ALA 64 1.321 1.227 1.519 1.529 1.444 122.46 116.70 120.68 112.03 112.17 111.03 122.62 * * 65 LYS 65 1.312 1.231 1.521 1.529 1.450 120.84 116.23 120.74 109.32 111.09 110.90 123.02 * * 66 LYS 66 1.318 1.240 1.529 1.528 1.452 121.67 117.03 120.74 110.23 112.16 110.40 122.23 67 LEU 67 1.303 1.217 1.535 1.524 1.435 120.45 117.18 120.58 113.14 110.73 109.21 122.16 +* * +* +* 68 PRO 68 1.342 1.241 1.556 1.536 1.480 123.52 117.04 120.73 110.69 115.11 103.46 122.22 * * * 69 ASN 69 1.328 1.244 1.501 1.546 1.467 122.35 113.67 122.59 111.63 108.51 111.74 123.42 * * * * 70 VAL 70 1.286 1.241 1.543 1.518 1.421 123.15 116.19 121.06 110.19 112.01 109.61 122.66 *** +* * *** 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 LEU 71 1.296 1.230 1.524 1.538 1.434 122.08 116.89 120.41 110.47 108.26 110.60 122.65 ** * * ** 72 PHE 72 1.303 1.224 1.483 1.523 1.452 121.78 116.49 120.40 109.91 109.04 112.71 123.08 +* +* * +* 73 LEU 73 1.282 1.222 1.512 1.527 1.430 121.51 115.74 120.78 111.05 111.43 108.94 123.46 *** * *** 74 LYS 74 1.312 1.231 1.505 1.532 1.417 123.72 116.76 120.52 109.06 107.37 109.30 122.70 * ** * * ** 75 VAL 75 1.287 1.233 1.500 1.557 1.433 120.86 116.24 120.46 109.95 108.61 112.09 123.29 *** * * *** 76 ASP 76 1.310 1.226 1.501 1.514 1.440 120.91 115.98 120.84 110.83 109.54 111.69 123.16 * * * 77 THR 77 1.306 1.232 1.523 1.536 1.440 122.77 116.79 120.44 111.26 112.83 111.52 122.76 +* +* 78 ASP 78 1.329 1.234 1.505 1.523 1.455 120.89 114.84 121.29 110.20 108.18 111.44 123.87 * * 79 GLU 79 1.312 1.241 1.523 1.511 1.424 123.26 115.94 120.93 109.42 110.74 109.04 123.13 * +* +* 80 LEU 80 1.323 1.241 1.531 1.543 1.416 123.03 116.03 121.06 110.25 111.51 110.96 122.84 ** ** 81 LYS 81 1.317 1.239 1.510 1.524 1.452 121.57 115.89 120.78 110.10 111.54 112.01 123.32 82 SER 82 1.326 1.217 1.522 1.512 1.437 121.69 116.75 120.16 110.95 110.91 110.39 123.06 * * 83 VAL 83 1.334 1.229 1.535 1.562 1.464 121.58 116.34 120.97 110.23 110.09 112.03 122.64 84 ALA 84 1.323 1.233 1.525 1.517 1.459 121.77 116.29 120.84 110.57 110.83 110.40 122.85 85 SER 85 1.314 1.242 1.545 1.527 1.444 121.83 116.40 120.60 111.32 111.35 109.49 122.99 * * 86 ASP 86 1.329 1.227 1.518 1.539 1.473 122.91 116.12 121.18 110.50 110.66 109.95 122.67 87 TRP 87 1.314 1.229 1.526 1.524 1.442 121.68 116.22 120.37 111.54 112.40 111.57 123.40 * * 88 ALA 88 1.345 1.240 1.530 1.527 1.478 123.43 115.51 121.25 111.01 111.52 109.96 123.21 * * * 89 ILE 89 1.311 1.234 1.520 1.545 1.440 122.74 114.98 121.42 111.38 109.95 110.55 123.56 * * * 90 GLN 90 1.309 1.229 1.528 1.561 1.424 123.06 117.13 120.33 110.43 112.25 111.51 122.53 * +* +* +* 91 ALA 91 1.316 1.229 1.513 1.517 1.452 121.00 115.89 121.14 111.09 111.17 110.98 122.97 92 MET 92 1.300 1.233 1.526 1.525 1.439 122.53 118.75 119.83 109.26 109.22 108.77 121.41 ** * * * ** 93 PRO 93 1.334 1.237 1.532 1.522 1.448 124.03 116.68 121.05 110.03 111.16 102.26 122.23 * * 94 THR 94 1.284 1.235 1.519 1.528 1.424 120.60 116.17 120.55 111.17 110.31 111.42 123.28 *** +* *** 95 PHE 95 1.314 1.227 1.497 1.528 1.415 122.48 116.90 120.50 107.57 108.04 110.35 122.59 * * ** * * ** 96 MET 96 1.281 1.228 1.504 1.538 1.426 120.46 114.97 121.23 112.83 108.71 111.18 123.80 *** * +* * *** 97 PHE 97 1.291 1.244 1.495 1.523 1.409 124.24 116.15 120.98 109.08 109.94 108.82 122.85 +** * +** * +** 98 LEU 98 1.282 1.221 1.520 1.559 1.414 120.77 117.00 120.42 107.13 107.38 112.86 122.58 *** * ** +* * * *** 99 LYS 99 1.286 1.227 1.480 1.519 1.429 121.85 115.16 120.39 111.70 108.96 111.75 124.33 *** ** +* *** 100 GLU 100 1.325 1.237 1.541 1.514 1.455 123.94 115.67 121.45 110.64 110.80 109.97 122.87 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 GLY 101 1.322 1.233 1.522 - 1.447 121.42 116.46 120.74 - 112.46 - 122.80 102 LYS 102 1.319 1.224 1.512 1.527 1.451 121.80 117.29 119.95 108.62 108.34 110.02 122.75 * * 103 ILE 103 1.307 1.233 1.522 1.556 1.453 121.40 116.47 120.78 110.33 109.94 111.75 122.72 +* +* 104 LEU 104 1.311 1.236 1.503 1.521 1.428 121.08 116.27 120.72 108.63 111.40 111.19 122.94 * * +* +* 105 ASP 105 1.314 1.225 1.469 1.543 1.452 120.37 115.73 120.84 111.32 109.98 111.03 123.42 * +** +** 106 LYS 106 1.261 1.228 1.515 1.523 1.416 120.83 116.44 120.42 110.48 109.73 109.28 123.13 *4.8* ** *4.8* 107 VAL 107 1.306 1.235 1.509 1.559 1.443 122.14 116.69 120.37 108.45 108.33 111.71 122.93 +* * +* 108 VAL 108 1.301 1.242 1.535 1.568 1.433 121.04 115.86 121.33 112.39 110.12 112.03 122.76 ** * * * ** 109 GLY 109 1.314 1.243 1.508 - 1.439 121.15 117.30 120.33 - 110.38 - 122.37 * * 110 ALA 110 1.310 1.227 1.502 1.520 1.434 119.78 114.82 121.37 109.80 110.95 110.66 123.79 * * * * * 111 LYS 111 1.295 1.240 1.496 1.528 1.412 123.72 116.98 119.53 109.33 106.82 112.23 123.49 ** * ** * +* * ** 112 LYS 112 1.308 1.233 1.528 1.538 1.434 122.31 114.97 121.48 110.86 109.01 107.73 123.50 * * +* +* 113 ASP 113 1.315 1.234 1.539 1.521 1.453 122.93 116.67 120.67 111.02 112.10 109.53 122.63 * * 114 GLU 114 1.327 1.230 1.518 1.523 1.471 121.79 116.31 120.78 109.46 111.35 111.37 122.91 115 LEU 115 1.319 1.234 1.511 1.514 1.451 121.39 114.73 121.58 109.62 108.85 109.92 123.68 116 GLN 116 1.319 1.226 1.526 1.531 1.464 122.41 116.18 120.85 109.80 111.27 111.38 122.95 117 SER 117 1.317 1.236 1.531 1.535 1.444 122.18 116.51 120.77 111.65 110.09 109.82 122.69 118 THR 118 1.322 1.236 1.540 1.544 1.440 121.66 116.59 120.99 111.68 110.35 110.81 122.37 * * 119 ILE 119 1.320 1.240 1.537 1.552 1.457 121.16 116.15 121.00 110.82 109.77 111.89 122.80 120 ALA 120 1.329 1.220 1.526 1.519 1.457 121.77 115.49 121.21 110.78 110.03 110.69 123.29 121 LYS 121 1.317 1.229 1.522 1.503 1.461 123.79 115.06 121.57 110.49 109.44 107.59 123.37 * * +* +* 122 HIS 122 1.318 1.232 1.517 1.524 1.445 122.54 116.99 119.77 109.88 112.28 111.87 123.24 123 LEU 123 1.334 1.240 1.531 1.520 1.428 122.74 115.07 120.98 112.33 109.20 107.29 123.92 +* * +* +* 124 ALA 124 1.314 - 1.510 1.531 1.442 124.07 - - 110.27 107.95 111.13 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.3* +** +* *** +* ** +* ** ** +** +* *5.3* ----------------------------------------------------------------------------------------------------------------------------------- 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 1.255 1.355 1.312 .016 *5.3* +* * C-N (Pro) 1.341 .016 4 1.334 1.378 1.355 .018 ** C-O C-O 1.231 .020 123 1.216 1.249 1.233 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.469 1.563 1.521 .016 +** +* CH2G*-C (Gly) 1.516 .018 5 1.499 1.526 1.514 .009 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.514 1.531 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.518 1.575 1.550 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.490 1.568 1.530 .014 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.393 1.478 1.442 .016 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.423 1.466 1.440 .016 +* N-CH1E (Pro) 1.466 .015 4 1.448 1.485 1.473 .015 * * ------------------------------------------------------------------------------------------------------------- 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 2.0 114 111.42 120.53 116.09 1.08 ** ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.32 119.07 117.40 1.01 * CH1E-C-N (Pro) 116.9 1.5 4 115.43 117.04 116.43 .60 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.53 124.92 123.01 .61 +* * O-C-N (Pro) 122.0 1.4 4 122.22 123.18 122.57 .39 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.12 124.91 122.07 1.13 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 118.50 123.40 121.09 1.56 * +* C-N-CH1E (Pro) 122.6 5.0 4 122.10 124.03 123.16 .71 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.94 123.65 120.85 .65 * +* CH2G*-C-O (Gly) 120.8 2.1 5 119.45 120.74 120.14 .46 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.80 112.03 110.87 .57 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.33 112.39 110.47 1.18 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.02 113.92 110.61 1.34 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.57 114.95 110.14 1.64 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.76 115.16 112.07 1.91 N-CH1E-C (Pro) 111.8 2.5 4 111.16 115.11 112.92 1.45 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.96 111.85 110.87 .51 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 107.68 112.51 111.06 1.18 ** N-CH1E-CH2E (Pro) 103.0 1.1 4 102.26 103.70 103.25 .58 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.29 115.46 110.39 1.55 +* +** ------------------------------------------------------------------------------------------------------------- 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] 10 8.8% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.8% 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 89.4 83.8 10.0 .6 Inside b. Omega angle st dev 122 3.3 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 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 84 .8 .8 .2 .2 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 12 5.9 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 47 5.4 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 43 6.2 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 102 6.7 18.2 4.8 -2.4 BETTER e. Chi-2 trans st dev 29 6.7 20.4 5.0 -2.7 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 7.6 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 -.16 Chi1-chi2 distribution -.02 Chi1 only .02 Chi3 & chi4 .46 Omega .00 ------ .00 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .43 ------ .23 ===== OVERALL AVERAGE .07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.