Residue-by-residue listing for refined_14 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 - 62.7 - - 175.6 - - - - - - 178.1 - 34.6 - 2 GLY 2 - - - - - - - - - - - 178.0 - - - 3 HIS 3 B 60.9 - - - - - - - - - 179.0 - 31.9 - 4 HIS 4 B - - -62.1 - - - - - - - 178.9 -.6 34.1 - +* +* 5 HIS 5 B 69.2 - - - - - - - - - 178.2 - 32.1 - 6 HIS 6 B 56.7 - - - - - - - - - 188.1 -.9 30.7 - * +* +* 7 HIS 7 S XX - - -68.4 - - - - - - - 174.6 -.7 31.5 - **** +* **** 8 HIS 8 B 62.3 - - - - - - - - - 181.3 - 31.1 - 9 LEU 9 b - 192.7 - 175.3 - - - - - - 178.1 -.5 34.7 - ** ** 10 GLU 10 B - - -63.2 - - - - - - - 178.0 - 34.5 - 11 MET 11 B 60.0 - - - - - - - - - 181.4 - 32.3 - 12 ALA 12 B - - - - - - - - - - 178.6 -.6 34.4 - +* +* 13 SER 13 B - - -59.0 - - - - - - - 178.9 - 34.8 - 14 GLU 14 t b - 190.0 - - - - - - - - 188.6 - 33.1 - * * 15 GLU 15 T B - - -56.0 168.3 - - - - - - 173.7 -1.3 36.5 - * * 16 GLY 16 T - - - - - - - - - - - 180.1 -1.2 - - * * 17 GLN 17 t B - - -56.6 - - - - - - - 181.1 -.7 32.2 - +* +* 18 VAL 18 B - 181.2 - - - - - - - - 178.9 - 35.2 - 19 ILE 19 E B - - -65.9 - - - - - - - 180.0 -2.7 33.0 - Residue-by-residue listing for refined_14 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 - - - - - - - - - - 180.9 -.8 33.6 - +* +* 21 CYS 21 E B - - -52.3 - - - - - - - 178.6 -1.7 35.9 - 22 HIS 22 A - - -58.6 - - - - - - - 179.5 - 33.4 - 23 THR 23 h B 49.8 - - - - - - - - - 182.2 - 33.7 - 24 VAL 24 H A 62.0 - - - - -67.4 -25.4 - - - 177.6 - 31.8 - * * 25 GLU 25 H A - 182.1 - 180.0 - -66.1 -49.9 - - - 179.2 - 34.5 - 26 THR 26 H A - - -52.5 - - -60.4 -41.3 - - - 176.3 - 34.9 - 27 TRP 27 H A - 170.2 - - - -56.3 -52.9 - - - 180.7 -2.1 34.5 - * * 28 ASN 28 H A - 187.1 - - - -62.0 -48.2 - - - 182.8 -3.0 35.1 - * * 29 GLU 29 H A - 183.5 - 184.2 - -56.7 -48.6 - - - 182.4 -3.3 35.1 - +* +* 30 GLN 30 H A - - -72.1 - - -66.2 -33.0 - - - 177.1 -2.8 33.0 - 31 LEU 31 H A - - -67.0 180.1 - -67.0 -46.9 - - - 179.3 -1.6 34.6 - 32 GLN 32 H A - - -49.7 - - -62.5 -36.5 - - - 178.6 -2.2 35.1 - * * 33 LYS 33 H A - 177.4 - - - -67.3 -44.9 - - - 179.8 -2.2 34.5 - 34 ALA 34 H A - - - - - -65.2 -39.0 - - - 178.6 -2.8 34.0 - * * 35 ASN 35 H A - 188.2 - - - -64.1 -51.5 - - - 180.8 -2.6 36.7 - * * 36 GLU 36 H A - 178.8 - 178.9 - -60.3 -44.0 - - - 181.8 -2.5 35.0 - 37 SER 37 H A - - -57.9 - - -79.7 -9.3 - - - 179.0 -2.9 34.1 - * +** * +** 38 LYS 38 h L - - -59.5 181.7 - - - - - - 179.6 -.6 32.9 - +* +* 39 THR 39 t B - - -45.1 - - - - - - - 177.6 -1.6 36.1 - * * 40 LEU 40 E B - 186.0 - 170.4 - - - - - - 188.0 -1.4 34.1 - * * 41 VAL 41 E B 59.6 - - - - - - - - - 178.6 - 33.0 - 42 VAL 42 E B 64.3 - - - - - - - - - 179.9 -2.7 33.5 - 43 VAL 43 E B - 183.2 - - - - - - - - 178.1 -3.2 34.0 - +* +* 44 ASP 44 E B - 175.2 - - - - - - - - 177.3 -3.0 35.9 - * * 45 PHE 45 E B - - -61.5 - - - - - - - 187.4 -3.0 35.5 - * * * 46 THR 46 E B - 182.7 - - - - - - - - 170.4 -2.2 36.3 - +* +* 47 ALA 47 t B - - - - - - - - - - 180.7 - 33.5 - 48 SER 48 T A - 184.5 - - - - - - - - 178.8 - 33.1 - 49 TRP 49 T A 49.5 - - - - - - - - - 182.1 - 32.8 - 50 CYS 50 h B - 174.4 - 221.1 - - - 56.6 - 2.0 182.9 -1.4 33.9 - ** +** +** 51 GLY 51 H - - - - - - -61.2 -65.3 - - - 180.7 -.5 - - ** +* ** 52 PRO 52 H - - - - - -59.0 -59.0 -30.5 - - - 179.2 - 38.2 - * * 53 CYS 53 H A - - -54.6 - - -68.4 -37.9 56.6 - 2.0 179.5 - 35.7 - +** +** 54 ARG 54 H A - 189.6 - 179.9 - -78.2 -33.7 - - - 179.4 -1.7 33.7 - * * Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 PHE 55 H A - 181.3 - - - -66.6 -27.1 - - - 182.4 -2.6 34.1 - * * 56 ILE 56 h A - 194.6 - - - - - - - - 182.9 -1.4 33.4 - 57 ALA 57 H A - - - - - -57.0 -50.6 - - - 179.8 -.8 31.2 - +* +* 58 PRO 58 H - - - - - -52.0 -52.0 -41.8 - - - 181.4 - 38.5 - * * * * 59 PHE 59 H A - 182.6 - - - -77.5 -36.9 - - - 180.3 - 32.4 - * * 60 PHE 60 H A - 189.2 - - - -65.1 -35.8 - - - 177.2 -2.3 33.6 - 61 ALA 61 H A - - - - - -70.7 -28.8 - - - 178.2 -2.8 33.8 - 62 ASP 62 H A - 181.3 - - - -71.0 -44.7 - - - 177.6 -1.0 35.6 - * * 63 LEU 63 H A - 175.1 - - - -59.6 -43.4 - - - 176.4 -2.7 36.4 - 64 ALA 64 H A - - - - - -61.3 -32.5 - - - 178.5 -2.1 33.5 - 65 LYS 65 H A - 179.6 - 180.8 - -77.8 -35.0 - - - 185.0 -1.2 35.2 - * * * 66 LYS 66 H A - 181.1 - 178.9 - -74.8 -40.2 - - - 183.9 -2.3 34.3 - 67 LEU 67 h B - - -66.7 172.6 - - - - - - 178.6 -2.6 32.7 - 68 PRO 68 T - - - - - -84.3 - - - - - 181.4 - 39.9 - +* +* +* 69 ASN 69 e A - 183.5 - - - - - - - - 181.9 - 34.2 - 70 VAL 70 E B - 180.7 - - - - - - - - 176.8 -.7 33.8 - +* +* 71 LEU 71 E B - 185.4 - - - - - - - - 184.2 -3.4 34.7 - +* +* 72 PHE 72 E B - - -55.9 - - - - - - - 179.1 -.7 36.2 - +* +* 73 LEU 73 E B - - -69.7 - - - - - - - 173.9 -2.0 33.9 - * * 74 LYS 74 E B - - -89.4 178.5 - - - - - - 180.1 -2.7 34.2 - +* +* 75 VAL 75 E B - 181.0 - - - - - - - - 181.1 -3.1 35.0 - * * 76 ASP 76 E B 82.7 - - - - - - - - - 182.7 -1.0 31.8 - * * * 77 THR 77 e A 51.9 - - - - - - - - - 178.8 -3.2 33.4 - +* +* 78 ASP 78 T A - 180.8 - - - - - - - - 174.2 - 35.3 - 79 GLU 79 T A - - -77.9 - - - - - - - 183.2 - 35.2 - 80 LEU 80 h b - - -67.3 - - - - - - - 176.2 -2.8 32.8 - * * 81 LYS 81 H A - - -65.0 - - -68.8 -37.0 - - - 177.9 -1.8 32.7 - 82 SER 82 H A - - -57.2 - - -62.2 -34.5 - - - 178.4 - 33.7 - 83 VAL 83 H A - 178.9 - - - -74.2 -43.2 - - - 177.2 - 33.0 - 84 ALA 84 H A - - - - - -59.3 -38.8 - - - 179.2 -2.1 34.2 - 85 SER 85 H A - 181.2 - - - -75.2 -32.3 - - - 183.9 -2.7 34.4 - 86 ASP 86 H A - 187.3 - - - -74.2 -30.9 - - - 179.2 -1.7 32.9 - 87 TRP 87 h A - - -59.9 - - - - - - - 181.1 -2.0 32.8 - 88 ALA 88 T l - - - - - - - - - - 180.2 - 31.3 - 89 ILE 89 t B - - -55.6 - - - - - - - 180.6 -2.6 33.3 - 90 GLN 90 A - 192.3 - - - - - - - - 186.3 -1.1 36.3 - * * * 91 ALA 91 S B - - - - - - - - - - 181.2 - 33.3 - 92 MET 92 S B - - -59.9 165.2 - - - - - - -.8 -.6 36.3 - +* +* Residue-by-residue listing for refined_14 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 93 PRO 93 e cis - - - - - -86.3 - - - - - 176.0 - 39.5 - +* +* +* 94 THR 94 E B - - -55.1 - - - - - - - 179.8 -1.5 34.5 - 95 PHE 95 E B - - -51.4 - - - - - - - 180.7 -3.1 36.4 - * * * 96 MET 96 E B - 176.2 - 179.7 - - - - - - 182.7 -3.1 34.8 - * * 97 PHE 97 E B - - -69.2 - - - - - - - 177.4 -3.2 35.8 - +* +* 98 LEU 98 E B - - -53.3 - - - - - - - 175.9 -2.7 35.2 - 99 LYS 99 E B - 180.2 - 177.9 - - - - - - 176.3 -3.4 33.7 - +* +* 100 GLU 100 T l - - -57.0 177.4 - - - - - - 180.7 - 33.5 - 101 GLY 101 T - - - - - - - - - - - 177.8 - - - 102 LYS 102 E B - 178.3 - 180.9 - - - - - - 179.2 -2.2 34.2 - 103 ILE 103 E B - - -59.0 172.0 - - - - - - 175.8 - 35.5 - 104 LEU 104 E a - - -66.6 187.5 - - - - - - 183.3 -2.2 32.7 - 105 ASP 105 E B 64.0 - - - - - - - - - 182.0 -2.1 31.8 - 106 LYS 106 E B - - -60.1 173.8 - - - - - - 175.5 - 35.5 - 107 VAL 107 E B - 181.2 - - - - - - - - 183.5 -3.2 35.1 - +* +* 108 VAL 108 E B 57.8 - - - - - - - - - 180.2 - 33.0 - 109 GLY 109 e - - - - - - - - - - - 178.9 -2.2 - - 110 ALA 110 B - - - - - - - - - - 179.9 - 33.9 - 111 LYS 111 h B - - -55.3 - - - - - - - 184.6 -1.0 36.5 - * * 112 LYS 112 H A - 180.8 - 178.8 - -69.9 -51.3 - - - 184.5 -.6 33.9 - * +* +* 113 ASP 113 H A - - -64.4 - - -72.3 -42.7 - - - 181.6 - 33.3 - 114 GLU 114 H A - 178.4 - 169.4 - -67.5 -28.8 - - - 179.7 - 31.5 - 115 LEU 115 H A - 186.8 - - - -58.6 -53.8 - - - 177.9 -1.3 34.6 - * * * 116 GLN 116 H A - - -67.3 - - -58.1 -35.7 - - - 179.1 -1.1 31.5 - * * 117 SER 117 H A - - -55.4 - - -65.7 -35.9 - - - 178.1 -1.3 33.8 - 118 THR 118 H A - - -57.3 - - -75.3 -31.8 - - - 176.4 -2.2 34.1 - 119 ILE 119 H A - - -59.5 176.0 - -66.8 -47.6 - - - 179.0 -2.2 33.3 - 120 ALA 120 H A - - - - - -63.9 -30.8 - - - 176.9 -3.0 33.8 - * * 121 LYS 121 H A - 187.7 - 182.9 - -58.8 -32.5 - - - 179.3 -1.4 38.1 - * * 122 HIS 122 H A - - -73.9 - - -93.7 -43.2 - - - 186.0 -1.2 34.6 - ** * * ** 123 LEU 123 h B - - -83.0 - - - - - - - 178.1 -3.0 33.8 - * * * 124 ALA 124 - - - - - - - - - - - - - 34.3 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** +* ** +** +** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.9 182.7 -61.7 178.8 -70.4 -66.6 -39.3 56.6 - 2.0 179.8 -2.0 34.2 +** +** Standard deviations: 8.2 5.3 8.6 9.9 17.5 7.9 9.5 .0 - .0 3.0 .9 1.7 Numbers of values: 15 42 45 27 4 46 46 2 0 2 122 83 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_14 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_14 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 - 1.234 1.513 1.543 1.466 - 116.64 120.57 108.79 110.13 111.57 122.78 2 GLY 2 1.310 1.239 1.500 - 1.429 120.33 116.26 120.65 - 112.10 - 123.08 * * * 3 HIS 3 1.306 1.224 1.515 1.565 1.444 121.43 116.01 121.32 111.74 109.63 113.06 122.62 +* +* +* +* 4 HIS 4 1.293 1.238 1.497 1.531 1.441 121.14 117.00 120.17 110.15 108.83 111.52 122.82 +** * +** 5 HIS 5 1.307 1.234 1.533 1.571 1.445 120.42 116.10 121.24 112.12 109.40 112.48 122.55 +* ** * * ** 6 HIS 6 1.306 1.224 1.514 1.564 1.437 120.62 115.50 120.32 113.96 108.80 112.81 124.17 +* +* * ** * ** 7 HIS 7 1.327 1.241 1.513 1.552 1.477 124.36 115.20 121.59 109.20 111.02 115.22 123.20 * * +** +** 8 HIS 8 1.290 1.226 1.510 1.565 1.421 122.05 114.96 121.88 113.41 108.30 113.18 122.99 +** +* +* +* * +* +** 9 LEU 9 1.290 1.244 1.506 1.566 1.423 122.17 115.55 121.14 111.79 106.72 110.17 123.15 +** +* +* +* +** 10 GLU 10 1.293 1.235 1.508 1.548 1.434 121.94 117.25 119.83 109.52 107.98 111.99 122.92 +** * * +** 11 MET 11 1.305 1.234 1.523 1.554 1.443 120.87 116.09 121.11 111.63 109.83 112.32 122.77 +* * * +* Residue-by-residue listing for refined_14 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 1.310 1.234 1.510 1.522 1.444 121.56 116.52 120.74 110.33 110.23 110.32 122.72 * * 13 SER 13 1.305 1.232 1.518 1.541 1.451 122.73 117.58 119.65 110.45 108.59 110.10 122.76 +* +* 14 GLU 14 1.318 1.226 1.520 1.527 1.443 120.81 114.53 121.90 111.88 107.93 111.40 123.53 * * 15 GLU 15 1.292 1.227 1.517 1.521 1.438 123.26 116.21 120.69 109.70 111.61 107.56 123.08 +** * +* +** 16 GLY 16 1.314 1.242 1.507 - 1.450 120.79 117.43 120.19 - 114.20 - 122.38 * * 17 GLN 17 1.313 1.228 1.493 1.498 1.433 119.64 113.94 121.81 110.31 111.50 112.77 124.23 * +* +* * * * * +* 18 VAL 18 1.273 1.242 1.524 1.555 1.440 123.92 117.50 119.78 109.60 108.76 110.51 122.72 +*** * +*** 19 ILE 19 1.317 1.229 1.522 1.572 1.439 120.70 116.48 120.86 110.23 109.46 113.09 122.64 * * 20 ALA 20 1.304 1.235 1.513 1.521 1.437 121.49 116.33 120.80 110.97 110.10 110.85 122.87 +* * +* 21 CYS 21 1.305 1.227 1.505 1.509 1.418 121.63 116.39 120.58 109.02 109.05 109.74 123.02 +* * ** ** 22 HIS 22 1.298 1.224 1.507 1.528 1.446 121.16 115.25 121.30 111.01 109.56 111.32 123.42 ** ** 23 THR 23 1.316 1.248 1.518 1.553 1.444 122.67 116.67 120.19 110.06 109.57 111.99 123.14 24 VAL 24 1.328 1.227 1.541 1.573 1.457 121.75 116.61 120.85 111.91 111.27 112.26 122.51 * * * 25 GLU 25 1.328 1.224 1.513 1.517 1.457 121.47 116.10 120.38 109.12 110.20 111.12 123.52 26 THR 26 1.331 1.227 1.529 1.544 1.458 121.54 115.20 121.05 109.49 108.92 110.86 123.72 27 TRP 27 1.325 1.231 1.533 1.541 1.447 123.10 116.08 120.65 111.46 110.80 108.86 123.24 28 ASN 28 1.321 1.238 1.521 1.532 1.456 122.31 115.47 120.70 108.82 110.65 110.62 123.82 29 GLU 29 1.331 1.237 1.524 1.533 1.455 123.43 116.14 120.39 109.58 111.09 109.74 123.41 30 GLN 30 1.324 1.211 1.511 1.493 1.421 123.04 117.55 120.03 111.48 113.47 109.85 122.42 +* +* +* 31 LEU 31 1.313 1.233 1.514 1.490 1.418 121.63 116.24 120.65 110.13 111.30 109.63 123.10 * ** ** ** 32 GLN 32 1.325 1.237 1.530 1.541 1.457 121.63 114.07 121.76 109.34 108.55 110.72 124.16 * * 33 LYS 33 1.315 1.230 1.539 1.556 1.446 125.10 117.01 120.32 113.75 110.65 106.82 122.65 * * +* +* ** ** 34 ALA 34 1.334 1.232 1.514 1.521 1.459 121.95 115.58 120.76 110.23 110.58 110.72 123.65 35 ASN 35 1.327 1.226 1.505 1.518 1.463 122.55 114.65 121.54 107.27 109.38 110.07 123.81 * * 36 GLU 36 1.313 1.232 1.519 1.517 1.466 122.91 116.37 121.06 108.96 111.98 110.02 122.56 * * 37 SER 37 1.305 1.231 1.524 1.516 1.431 121.10 115.84 120.58 111.21 111.03 109.50 123.58 +* * +* 38 LYS 38 1.347 1.230 1.509 1.506 1.463 124.14 114.61 122.15 111.88 110.93 110.27 123.21 * * * * 39 THR 39 1.294 1.243 1.516 1.523 1.411 122.23 116.45 120.61 108.87 107.62 110.11 122.88 +** ** * +** 40 LEU 40 1.289 1.218 1.529 1.563 1.439 121.02 117.67 119.98 113.37 105.48 109.49 122.34 +** +* * +* ** +** 41 VAL 41 1.300 1.234 1.522 1.571 1.443 120.41 115.77 121.15 111.51 111.74 110.99 123.07 ** * * ** 42 VAL 42 1.301 1.243 1.520 1.560 1.426 121.78 116.14 121.01 110.67 109.23 112.02 122.80 +* +* +* Residue-by-residue listing for refined_14 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 1.291 1.235 1.509 1.543 1.424 121.29 115.07 121.06 109.59 109.52 112.12 123.85 +** +* +** 44 ASP 44 1.287 1.242 1.518 1.530 1.436 123.46 116.44 120.68 110.54 108.88 108.39 122.76 *** * * *** 45 PHE 45 1.311 1.235 1.513 1.523 1.425 121.39 116.52 120.44 109.98 108.00 109.80 122.99 * +* * +* 46 THR 46 1.304 1.220 1.531 1.571 1.440 121.17 116.20 120.71 109.67 110.48 108.68 122.86 +* * +* +* 47 ALA 47 1.310 1.237 1.506 1.513 1.446 123.89 117.80 119.41 110.48 107.23 112.19 122.77 * * * * * 48 SER 48 1.307 1.228 1.550 1.542 1.456 121.18 116.60 120.87 111.43 110.98 110.67 122.53 +* * +* 49 TRP 49 1.329 1.228 1.532 1.545 1.466 122.04 116.37 121.10 111.23 112.26 110.95 122.53 50 CYS 50 1.308 1.235 1.525 1.530 1.451 121.66 115.72 120.56 111.37 110.86 109.70 123.71 +* +* 51 GLY 51 1.331 1.234 1.518 - 1.462 122.97 118.82 119.63 - 114.45 - 121.54 * * * 52 PRO 52 1.359 1.229 1.522 1.541 1.469 122.53 115.19 121.57 110.73 111.11 104.01 123.23 * * * 53 CYS 53 1.310 1.229 1.535 1.514 1.439 122.84 116.91 120.97 109.25 110.45 109.18 122.12 * * 54 ARG 54 1.318 1.224 1.530 1.535 1.449 120.76 115.62 121.16 111.04 109.24 110.97 123.17 55 PHE 55 1.321 1.230 1.534 1.541 1.459 122.90 117.09 120.90 110.55 111.74 109.94 122.01 56 ILE 56 1.316 1.240 1.549 1.570 1.449 120.24 115.92 121.23 110.55 110.50 111.61 122.80 * * * 57 ALA 57 1.334 1.231 1.551 1.528 1.463 122.32 119.94 118.82 111.61 113.76 111.76 121.24 * +* * * +* 58 PRO 58 1.383 1.237 1.534 1.539 1.474 122.35 117.28 120.41 109.61 113.44 104.22 122.28 +** * +** 59 PHE 59 1.325 1.228 1.520 1.537 1.448 120.09 116.75 120.58 110.97 110.91 112.31 122.66 * * 60 PHE 60 1.323 1.230 1.538 1.538 1.455 120.97 115.86 121.16 111.58 109.55 110.33 122.96 61 ALA 61 1.328 1.234 1.534 1.523 1.461 122.14 116.17 120.97 110.64 110.77 110.43 122.85 62 ASP 62 1.330 1.227 1.481 1.513 1.474 122.02 113.80 121.67 107.82 109.11 111.17 124.53 ** * * ** 63 LEU 63 1.296 1.234 1.536 1.515 1.402 124.82 115.56 121.06 111.90 109.55 105.99 123.36 ** +** +* +** +** 64 ALA 64 1.330 1.227 1.529 1.523 1.466 123.12 115.96 121.40 110.55 111.40 110.68 122.63 65 LYS 65 1.309 1.225 1.529 1.538 1.449 122.21 115.28 121.23 110.55 110.13 109.04 123.45 * * 66 LYS 66 1.309 1.235 1.533 1.537 1.449 123.46 117.52 120.26 110.65 112.95 109.19 122.23 * * 67 LEU 67 1.318 1.218 1.519 1.503 1.438 120.69 116.36 121.22 111.39 114.25 110.00 122.42 * * * * 68 PRO 68 1.339 1.233 1.546 1.528 1.476 123.42 116.58 121.03 109.66 112.66 101.95 122.39 69 ASN 69 1.317 1.228 1.529 1.548 1.464 121.96 115.50 121.94 111.72 109.82 109.41 122.54 70 VAL 70 1.309 1.230 1.520 1.560 1.439 121.70 116.08 120.74 110.24 109.82 111.79 123.11 * * 71 LEU 71 1.301 1.237 1.525 1.535 1.433 122.33 116.34 120.75 110.87 107.51 110.19 122.89 +* * * +* 72 PHE 72 1.306 1.242 1.511 1.521 1.451 121.86 115.90 120.76 107.68 109.96 110.23 123.34 +* * +* 73 LEU 73 1.295 1.222 1.507 1.544 1.441 122.80 115.41 120.77 107.92 111.37 113.28 123.82 ** * +* ** Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 LYS 74 1.305 1.229 1.493 1.494 1.408 124.08 116.47 120.60 110.33 109.79 110.61 122.90 +* +* +* +** * +** 75 VAL 75 1.284 1.245 1.499 1.555 1.436 121.58 117.34 120.10 109.71 107.87 111.21 122.53 *** * * * *** 76 ASP 76 1.316 1.232 1.517 1.515 1.372 119.54 114.05 122.46 113.21 110.02 111.56 123.44 *4.5* * * +* *4.5* 77 THR 77 1.288 1.223 1.528 1.542 1.432 123.93 116.23 120.66 111.33 112.47 110.19 123.11 +** * * * +** 78 ASP 78 1.328 1.237 1.510 1.520 1.454 121.88 114.97 121.37 109.67 108.69 109.92 123.65 79 GLU 79 1.308 1.242 1.519 1.522 1.422 123.33 116.55 120.97 110.55 110.71 108.89 122.47 * +* +* 80 LEU 80 1.315 1.243 1.522 1.522 1.404 121.77 115.85 121.19 110.58 113.08 111.44 122.93 +** +** 81 LYS 81 1.310 1.227 1.524 1.530 1.450 121.44 116.37 120.75 111.25 110.46 111.63 122.86 * * 82 SER 82 1.327 1.219 1.531 1.521 1.454 121.98 116.64 120.82 110.87 111.06 110.26 122.51 83 VAL 83 1.324 1.233 1.529 1.554 1.452 121.13 116.11 120.82 111.05 109.49 111.94 123.03 84 ALA 84 1.331 1.228 1.532 1.523 1.460 121.95 115.92 121.13 110.19 110.48 110.40 122.95 85 SER 85 1.317 1.242 1.548 1.543 1.440 122.39 116.94 120.82 110.98 111.21 109.42 122.22 * * 86 ASP 86 1.329 1.222 1.517 1.536 1.469 121.55 116.90 120.74 110.57 111.80 111.53 122.35 87 TRP 87 1.309 1.229 1.515 1.511 1.443 120.64 115.52 120.62 111.07 111.91 111.10 123.85 * * 88 ALA 88 1.331 1.235 1.521 1.525 1.460 123.86 115.34 121.61 111.80 111.89 112.34 122.94 * * * 89 ILE 89 1.303 1.234 1.505 1.556 1.438 121.57 115.00 121.44 110.80 109.44 112.02 123.51 +* * +* 90 GLN 90 1.300 1.237 1.523 1.553 1.432 122.30 115.52 121.24 110.37 107.23 108.54 123.16 ** * * * * ** 91 ALA 91 1.312 1.230 1.506 1.512 1.448 121.38 115.02 121.51 110.89 111.51 110.77 123.47 * * 92 MET 92 1.294 1.230 1.521 1.516 1.441 122.99 118.63 119.86 109.55 109.45 108.30 121.51 ** * * ** 93 PRO 93 1.335 1.223 1.530 1.527 1.461 123.97 116.68 121.09 109.89 112.05 102.68 122.19 94 THR 94 1.287 1.232 1.513 1.524 1.426 120.73 117.02 120.08 109.68 108.32 111.38 122.89 +** +* * +** 95 PHE 95 1.306 1.230 1.500 1.527 1.408 121.02 116.41 120.69 109.17 106.96 109.61 122.89 +* * +** +* +** 96 MET 96 1.277 1.225 1.499 1.516 1.429 121.39 115.23 121.15 111.79 109.24 108.67 123.63 +*** * +* * +*** 97 PHE 97 1.285 1.248 1.505 1.514 1.405 123.50 115.83 121.30 109.79 110.80 108.92 122.87 *** +** *** 98 LEU 98 1.291 1.224 1.520 1.557 1.423 121.09 117.01 120.53 107.11 107.33 113.52 122.45 +** * +* +* * +* +** 99 LYS 99 1.285 1.230 1.492 1.514 1.428 121.34 115.05 120.55 110.38 109.55 111.58 124.31 *** +* +* *** 100 GLU 100 1.324 1.232 1.542 1.525 1.453 124.12 115.43 121.42 111.61 111.08 109.83 123.08 * * 101 GLY 101 1.328 1.233 1.526 - 1.452 122.01 117.34 120.16 - 113.61 - 122.49 102 LYS 102 1.320 1.222 1.520 1.532 1.454 120.95 116.74 120.17 109.40 110.14 111.45 123.09 103 ILE 103 1.319 1.247 1.521 1.555 1.462 122.47 116.61 120.21 108.28 109.96 110.96 123.16 104 LEU 104 1.317 1.233 1.508 1.518 1.422 120.96 116.84 120.13 110.22 111.01 112.55 123.02 +* * +* 105 ASP 105 1.328 1.218 1.502 1.517 1.451 121.23 115.45 121.23 110.07 112.85 113.06 123.28 * +* +* Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 106 LYS 106 1.303 1.245 1.530 1.527 1.451 122.46 115.45 120.88 108.93 111.28 109.61 123.67 +* +* 107 VAL 107 1.311 1.239 1.517 1.555 1.454 123.94 116.94 120.31 108.83 107.13 111.93 122.75 * * * * 108 VAL 108 1.299 1.238 1.532 1.554 1.436 121.44 115.78 121.34 111.42 111.61 110.92 122.87 ** * * ** 109 GLY 109 1.310 1.239 1.499 - 1.429 121.23 117.42 120.27 - 110.41 - 122.31 * * * 110 ALA 110 1.307 1.242 1.499 1.518 1.429 119.40 115.32 121.25 110.89 108.44 111.15 123.42 +* * +* * +* 111 LYS 111 1.297 1.226 1.493 1.522 1.412 122.55 116.99 119.92 110.11 106.67 108.54 123.06 ** +* ** +* * ** 112 LYS 112 1.306 1.206 1.509 1.520 1.425 121.05 116.69 120.43 110.98 111.56 109.96 122.81 +* * +* +* 113 ASP 113 1.304 1.242 1.510 1.531 1.457 121.40 115.78 120.85 110.59 111.54 111.11 123.35 +* +* 114 GLU 114 1.318 1.242 1.527 1.537 1.446 122.61 117.16 120.27 112.41 112.55 111.39 122.57 * * 115 LEU 115 1.329 1.229 1.512 1.514 1.456 120.97 116.02 120.55 109.17 109.81 111.08 123.39 116 GLN 116 1.325 1.229 1.518 1.549 1.477 121.46 116.73 120.29 109.68 111.76 114.36 122.96 ** ** 117 SER 117 1.321 1.235 1.537 1.528 1.454 121.39 116.17 120.95 111.13 110.26 110.20 122.86 118 THR 118 1.321 1.228 1.533 1.538 1.443 121.98 116.27 121.32 110.49 109.70 110.71 122.40 119 ILE 119 1.311 1.224 1.536 1.549 1.443 121.16 116.63 120.56 110.87 109.56 111.62 122.70 * * 120 ALA 120 1.331 1.223 1.531 1.516 1.471 122.32 115.03 121.59 110.69 110.66 110.28 123.38 121 LYS 121 1.313 1.234 1.527 1.485 1.460 124.74 114.91 121.52 108.19 110.27 106.26 123.54 * ** +* * ** ** 122 HIS 122 1.312 1.227 1.533 1.530 1.445 123.25 116.84 120.60 109.19 112.60 110.38 122.56 * * 123 LEU 123 1.315 1.233 1.516 1.511 1.422 122.80 115.01 121.52 111.00 114.09 109.20 123.47 * +* * +* 124 ALA 124 1.309 - 1.515 1.528 1.439 123.58 - - 110.63 108.15 110.81 - * * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** ** *4.5* +* +* * ** ** +** * *4.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 1.273 1.347 1.311 .014 +*** * * C-N (Pro) 1.341 .016 4 1.335 1.383 1.354 .019 +** C-O C-O 1.231 .020 123 1.206 1.248 1.232 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.481 1.551 1.520 .013 ** * CH2G*-C (Gly) 1.516 .018 5 1.499 1.526 1.510 .011 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.512 1.528 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.523 1.573 1.554 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.485 1.571 1.530 .018 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.372 1.477 1.443 .018 *4.5* NH1-CH2G* (Gly) 1.451 .016 5 1.429 1.462 1.444 .013 * N-CH1E (Pro) 1.466 .015 4 1.461 1.476 1.470 .006 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 2.0 114 113.80 119.94 116.11 .93 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.26 118.82 117.45 .81 * CH1E-C-N (Pro) 116.9 1.5 4 115.19 117.28 116.43 .77 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 121.24 124.53 122.99 .55 * O-C-N (Pro) 122.0 1.4 4 122.19 123.23 122.52 .41 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.40 125.10 122.01 1.16 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.33 122.97 121.47 .93 * C-N-CH1E (Pro) 122.6 5.0 4 122.35 123.97 123.07 .66 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.82 122.46 120.85 .58 * CH2G*-C-O (Gly) 120.8 2.1 5 119.63 120.65 120.18 .33 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.19 111.80 110.76 .47 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.28 111.91 110.22 .92 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.11 113.96 110.47 1.38 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.48 114.25 110.14 1.66 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.41 114.45 112.95 1.51 N-CH1E-C (Pro) 111.8 2.5 4 111.11 113.44 112.31 .85 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.28 112.34 110.98 .67 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.68 113.09 111.31 .92 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 101.95 104.22 103.21 .94 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 105.99 115.22 110.49 1.67 +** +** ------------------------------------------------------------------------------------------------------------- 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_14 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] 106 93.8% Residues in additional allowed regions [a,b,l,p] 6 5.3% 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 93.8 83.8 10.0 1.0 BETTER 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 83 .9 .8 .2 .4 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 15 8.2 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 42 5.3 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 45 8.6 17.5 4.9 -1.8 BETTER d. Chi-1 pooled st dev 102 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 27 9.9 20.4 5.0 -2.1 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% 93.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_14 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.16 Chi1-chi2 distribution -.19 Chi1 only -.10 Chi3 & chi4 .45 Omega .16 ------ .01 ===== Main-chain covalent forces:- Main-chain bond lengths -.04 Main-chain bond angles .44 ------ .24 ===== OVERALL AVERAGE .09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.