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 - 63.3 - - 178.8 - - - - - - 176.5 - 34.7 - 2 GLY 2 - - - - - - - - - - - 184.4 - - - 3 HIS 3 l - 181.6 - - - - - - - - 186.2 - 31.9 - * * 4 HIS 4 A 68.6 - - - - - - - - - 178.7 - 30.9 - 5 HIS 5 l - 177.8 - - - - - - - - 177.3 - 32.6 - 6 HIS 6 a - 182.5 - - - - - - - - 183.9 - 33.3 - 7 HIS 7 XX - - -70.9 - - - - - - - 182.7 - 30.7 - **** **** 8 HIS 8 l - - -62.3 - - - - - - - 177.1 - 30.8 - 9 LEU 9 b - 192.7 - 175.9 - - - - - - 179.4 - 33.9 - 10 GLU 10 b - 179.6 - 172.9 - - - - - - 171.5 - 33.7 - * * 11 MET 11 B - - -63.2 178.9 - - - - - - 185.0 - 33.4 - 12 ALA 12 b - - - - - - - - - - 176.1 -1.0 31.4 - * * 13 SER 13 b - - -60.8 - - - - - - - 175.6 -2.5 33.3 - 14 GLU 14 A - 185.6 - 177.4 - - - - - - 178.0 - 33.9 - 15 GLU 15 b - - -69.5 - - - - - - - 187.2 - 34.3 - * * 16 GLY 16 S - - - - - - - - - - - 176.7 -.8 - - +* +* 17 GLN 17 B 51.2 - - - - - - - - - 181.8 - 30.5 - 18 VAL 18 B 66.9 - - - - - - - - - 180.7 - 35.0 - 19 ILE 19 E B - - -67.2 - - - - - - - 183.7 -2.7 32.1 - 20 ALA 20 E B - - - - - - - - - - 179.2 -.8 33.8 - +* +* 21 CYS 21 E B - - -53.1 - - - - - - - 178.9 -2.2 35.4 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 HIS 22 S A - - -59.3 - - - - - - - 182.1 -.8 34.2 - +* +* 23 THR 23 h B 58.6 - - - - - - - - - 176.0 - 35.7 - 24 VAL 24 H A 62.1 - - - - -72.2 -22.8 - - - 179.1 - 33.0 - * * 25 GLU 25 H A - 183.3 - 178.2 - -64.1 -51.0 - - - 176.5 - 34.6 - * * 26 THR 26 H A - - -58.6 - - -61.2 -43.8 - - - 179.0 - 34.8 - 27 TRP 27 H A - 177.7 - - - -56.5 -48.5 - - - 177.9 -1.8 34.8 - 28 ASN 28 H A - 177.9 - - - -58.1 -48.8 - - - 181.8 -3.1 35.2 - * * 29 GLU 29 H A - 183.4 - - - -58.0 -47.6 - - - 181.5 -2.5 34.9 - 30 GLN 30 H A - - -66.7 - - -67.5 -41.6 - - - 177.5 -2.7 33.2 - 31 LEU 31 H A - - -70.4 182.6 - -66.6 -39.3 - - - 177.4 -2.5 34.7 - 32 GLN 32 H A - 183.1 - 179.4 - -62.5 -39.8 - - - 179.1 -2.7 34.3 - 33 LYS 33 H A - 185.8 - 177.6 - -68.1 -39.8 - - - 181.4 -2.2 33.5 - 34 ALA 34 H A - - - - - -76.7 -29.7 - - - 183.2 -2.4 33.6 - 35 ASN 35 H A - 192.0 - - - -75.2 -54.8 - - - 178.6 -2.6 36.5 - * * 36 GLU 36 H A - - -78.1 - - -64.0 -30.9 - - - 178.0 -2.2 29.8 - * * 37 SER 37 H A - - -57.0 - - -88.8 -10.5 - - - 183.2 -1.2 34.8 - +* +** * +** 38 LYS 38 h l - 188.0 - 177.9 - - - - - - 180.4 -.5 28.7 - +* * +* 39 THR 39 t B - - -45.7 - - - - - - - 179.2 -2.2 35.8 - * * 40 LEU 40 e B 69.2 - - 174.7 - - - - - - 181.9 - 34.2 - 41 VAL 41 E B 59.1 - - - - - - - - - 176.6 - 32.9 - 42 VAL 42 E B - 178.4 - - - - - - - - 183.7 -2.5 34.0 - 43 VAL 43 E B - 184.8 - - - - - - - - 176.4 -2.1 34.7 - 44 ASP 44 E B - 169.4 - - - - - - - - 177.1 -2.9 33.8 - * * 45 PHE 45 E B - - -59.6 - - - - - - - 187.3 -3.3 35.8 - * +* +* 46 THR 46 E B - 187.8 - - - - - - - - 176.6 -2.6 35.1 - 47 ALA 47 t B - - - - - - - - - - 182.0 - 34.1 - 48 SER 48 T A - - -53.2 - - - - - - - 177.3 - 34.2 - 49 TRP 49 T A 56.2 - - - - - - - - - 179.7 - 32.3 - 50 CYS 50 h B - 170.1 - 221.7 - - - 51.1 - 2.0 184.2 -1.7 34.2 - ** *** *** 51 GLY 51 H - - - - - - -51.9 -67.5 - - - 181.2 -.6 - - * ** +* ** 52 PRO 52 H - - - - - -65.2 -65.2 -30.8 - - - 180.2 - 38.2 - * * 53 CYS 53 H A - - -53.1 - - -66.4 -38.0 51.1 - 2.0 179.6 - 36.0 - *** *** 54 ARG 54 H A - 182.7 - 179.0 - -77.1 -29.9 - - - 179.4 -2.4 35.7 - 55 PHE 55 H A - 178.2 - - - -72.9 -30.5 - - - 184.4 -1.7 34.5 - 56 ILE 56 H A - 195.7 - - - -86.8 -9.6 - - - 180.4 -1.8 34.1 - +* +** +** 57 ALA 57 H A - - - - - -60.3 -52.6 - - - 177.9 - 31.2 - * * 58 PRO 58 H - - - - - -62.4 -62.4 -28.9 - - - 180.2 - 38.7 - * * 59 PHE 59 H A - 188.4 - - - -68.7 -39.9 - - - 178.6 -.5 34.9 - ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 60 PHE 60 H A - 181.7 - - - -73.3 -34.5 - - - 176.9 -2.1 33.8 - 61 ALA 61 H A - - - - - -67.1 -29.4 - - - 176.2 -2.3 33.9 - 62 ASP 62 H A - 180.4 - - - -69.2 -45.7 - - - 176.0 -1.4 36.0 - 63 LEU 63 H A - - -66.5 180.9 - -57.9 -40.8 - - - 177.9 -1.7 35.2 - 64 ALA 64 H A - - - - - -61.3 -32.1 - - - 180.4 -2.2 33.8 - 65 LYS 65 H A - 191.6 - 173.7 - -80.1 -19.3 - - - 179.2 -.9 32.5 - * +* * +* 66 LYS 66 H A - - -63.7 181.2 - -79.5 -40.6 - - - 181.3 -.9 34.1 - * * * 67 LEU 67 h B - - -66.3 - - - - - - - 182.4 -1.9 34.2 - 68 PRO 68 T - - - - - -86.5 - - - - - 182.8 - 39.1 - +* * +* 69 ASN 69 T A - - -65.2 - - - - - - - 183.0 - 35.1 - 70 VAL 70 t B - 181.4 - - - - - - - - 180.2 -.6 34.3 - +* +* 71 LEU 71 E B - 202.6 - - - - - - - - 182.5 -1.7 35.5 - * * 72 PHE 72 E B - - -58.4 - - - - - - - 177.8 - 35.0 - 73 LEU 73 E B - - -79.3 - - - - - - - 180.4 -2.5 31.3 - 74 LYS 74 E B - 173.7 - - - - - - - - 177.0 -3.1 36.2 - * * 75 VAL 75 E B - 177.8 - - - - - - - - 175.6 -2.9 34.2 - * * 76 ASP 76 E B - 182.7 - - - - - - - - 185.9 -.6 33.3 - * +* +* 77 THR 77 e A 54.3 - - - - - - - - - 175.3 -3.5 32.7 - ** ** 78 ASP 78 T A - 179.8 - - - - - - - - 177.6 - 35.2 - 79 GLU 79 T a - - -61.7 181.6 - - - - - - 185.6 -.7 35.2 - +* +* 80 LEU 80 h b - - -66.7 181.2 - - - - - - 177.8 -2.5 32.6 - 81 LYS 81 H A - - -61.8 186.5 - -70.1 -34.5 - - - 180.2 -1.6 32.0 - 82 SER 82 H A - - -54.9 - - -63.7 -37.3 - - - 177.9 - 33.9 - 83 VAL 83 H A - 178.3 - - - -69.7 -43.3 - - - 178.5 - 34.1 - 84 ALA 84 H A - - - - - -58.4 -46.2 - - - 180.8 -1.8 33.9 - 85 SER 85 H A - 184.6 - - - -66.9 -36.2 - - - 182.7 -3.0 33.8 - * * 86 ASP 86 H A - 185.8 - - - -65.0 -38.0 - - - 181.9 -2.0 35.1 - 87 TRP 87 h A - - -66.9 - - - - - - - 178.0 -2.0 33.1 - 88 ALA 88 T l - - - - - - - - - - 180.3 -1.3 33.2 - * * 89 ILE 89 t B - - -55.7 - - - - - - - 182.3 -3.1 34.2 - * * 90 GLN 90 a - 182.0 - 177.9 - - - - - - 180.3 -.7 34.1 - +* +* 91 ALA 91 S B - - - - - - - - - - 183.3 - 33.7 - 92 MET 92 S B - - -57.9 173.8 - - - - - - -4.5 - 36.6 - 93 PRO 93 e cis - - - - - -91.2 - - - - - 178.0 - 39.3 - ** +* ** 94 THR 94 E B - - -57.0 - - - - - - - 180.6 -2.8 33.5 - * * 95 PHE 95 E B - - -59.9 - - - - - - - 183.2 -2.9 37.2 - * * 96 MET 96 E B - 198.8 - - - - - - - - 183.7 -3.3 35.4 - +* +* 97 PHE 97 E B - - -67.7 - - - - - - - 175.8 -3.3 37.2 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 LEU 98 E B 65.3 - - - - - - - - - 176.0 -1.2 33.3 - * * 99 LYS 99 E B - 174.5 - 178.0 - - - - - - 177.1 -3.5 32.3 - +* +* 100 GLU 100 T L - - -60.9 180.7 - - - - - - 179.6 - 33.4 - 101 GLY 101 T - - - - - - - - - - - 178.7 - - - 102 LYS 102 E B - 183.0 - 177.9 - - - - - - 182.5 -2.0 34.3 - 103 ILE 103 E B - - -59.8 - - - - - - - 178.3 - 34.5 - 104 LEU 104 E a - - -63.6 181.3 - - - - - - 188.0 -2.7 34.7 - * * 105 ASP 105 E B - - -57.5 - - - - - - - 175.5 -1.8 34.8 - 106 LYS 106 E B 57.9 - - 179.0 - - - - - - 179.2 - 33.1 - 107 VAL 107 E B - 180.8 - - - - - - - - 179.6 -2.5 34.4 - 108 VAL 108 E B 61.4 - - - - - - - - - 180.3 -.5 33.0 - ** ** 109 GLY 109 e - - - - - - - - - - - 181.5 -3.0 - - * * 110 ALA 110 B - - - - - - - - - - 175.9 - 34.1 - 111 LYS 111 h B - - -70.0 182.0 - - - - - - 180.1 -.9 34.2 - +* +* 112 LYS 112 H A - 180.6 - 191.0 - -69.4 -52.7 - - - 186.8 - 37.5 - * * * * 113 ASP 113 H A - 181.9 - - - -73.3 -45.2 - - - 182.4 - 32.5 - 114 GLU 114 H A - 184.5 - - - -64.7 -35.0 - - - 178.4 - 33.4 - 115 LEU 115 H A - 187.3 - - - -68.3 -49.4 - - - 176.1 -.9 34.5 - * * 116 GLN 116 H A - - -69.8 - - -55.8 -36.4 - - - 180.0 -2.2 33.6 - 117 SER 117 H A - 181.8 - - - -71.6 -38.2 - - - 177.1 -2.5 33.8 - 118 THR 118 H A - - -58.2 - - -67.4 -34.7 - - - 176.0 -2.2 34.0 - 119 ILE 119 H A - - -60.5 - - -65.5 -49.4 - - - 179.7 -2.5 33.5 - 120 ALA 120 H A - - - - - -62.1 -31.7 - - - 176.7 -2.7 33.3 - 121 LYS 121 H A - 188.3 - 181.3 - -60.2 -42.0 - - - 180.2 -2.0 36.5 - 122 HIS 122 H A - - -75.6 - - -78.3 -29.8 - - - 179.1 -1.4 32.3 - * * 123 LEU 123 h B - - -88.1 - - - - - - - 178.6 -1.9 32.8 - * * 124 ALA 124 - - - - - - - - - - - - - 33.9 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * ** ** +* +** *** * ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.1 183.3 -63.3 180.8 -76.3 -67.5 -38.3 51.1 - 2.0 179.8 -2.0 34.1 *** *** Standard deviations: 5.5 6.5 7.9 8.7 14.7 7.8 10.8 .0 - .0 3.0 .8 1.7 Numbers of values: 13 46 43 29 4 47 47 2 0 2 122 78 119 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 - 1.229 1.516 1.542 1.471 - 116.62 120.29 109.17 109.75 111.21 123.08 2 GLY 2 1.314 1.244 1.507 - 1.439 120.79 115.64 120.10 - 113.04 - 124.23 * * 3 HIS 3 1.338 1.222 1.528 1.559 1.460 124.07 116.05 121.16 112.97 108.99 111.79 122.76 * * +* +* 4 HIS 4 1.326 1.224 1.530 1.556 1.473 121.20 116.63 119.83 111.49 112.82 112.98 123.53 * * * 5 HIS 5 1.346 1.228 1.543 1.568 1.481 122.92 116.62 121.02 112.05 112.10 110.54 122.32 * +* * * +* 6 HIS 6 1.313 1.227 1.516 1.551 1.453 120.99 115.97 120.34 110.71 109.65 111.85 123.65 * * * 7 HIS 7 1.334 1.229 1.513 1.535 1.469 123.52 115.27 121.19 110.94 112.51 113.89 123.54 * +* +* 8 HIS 8 1.311 1.234 1.506 1.543 1.458 123.81 115.00 121.70 111.18 111.16 114.26 123.16 * * ** ** 9 LEU 9 1.292 1.238 1.507 1.563 1.427 122.52 114.60 121.03 112.22 106.25 110.94 124.04 +** +* +* * +* +** 10 GLU 10 1.312 1.228 1.498 1.542 1.436 123.57 116.07 120.82 109.59 109.93 112.44 123.00 * * * * * * 11 MET 11 1.293 1.237 1.497 1.533 1.430 120.65 115.84 120.95 110.96 106.76 112.46 123.09 +** * * +* * +** 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 1.316 1.236 1.507 1.521 1.440 121.55 114.35 121.68 111.99 111.89 112.23 123.77 * * 13 SER 13 1.297 1.223 1.509 1.550 1.423 124.60 115.79 121.24 110.48 108.54 112.67 122.74 ** +* +* * ** 14 GLU 14 1.307 1.230 1.522 1.539 1.450 121.38 112.88 123.12 112.20 106.34 110.41 123.98 +* +* * * +* +* 15 GLU 15 1.315 1.239 1.518 1.544 1.425 125.30 116.78 120.89 111.57 109.70 109.63 122.32 * +* +* +* 16 GLY 16 1.290 1.224 1.489 - 1.438 119.82 114.79 121.67 - 110.18 - 123.53 +** +* +** 17 GLN 17 1.299 1.235 1.487 1.549 1.410 122.59 115.29 120.90 113.47 110.52 113.09 123.78 ** +* +** +* +* +** 18 VAL 18 1.269 1.232 1.533 1.554 1.411 122.16 117.76 120.19 112.12 108.89 108.58 122.02 **** ** * +* **** 19 ILE 19 1.318 1.232 1.518 1.573 1.444 119.82 116.02 121.04 111.16 109.50 113.44 122.94 * * * * 20 ALA 20 1.302 1.230 1.503 1.521 1.439 121.92 116.30 120.94 110.81 110.63 110.51 122.75 +* * * +* 21 CYS 21 1.301 1.227 1.499 1.500 1.411 121.27 116.23 121.05 109.75 108.62 109.90 122.68 ** * +* ** ** 22 HIS 22 1.289 1.228 1.502 1.532 1.442 121.24 115.18 121.36 110.44 108.81 111.06 123.45 +** * +** 23 THR 23 1.316 1.251 1.510 1.557 1.434 122.58 116.70 120.17 107.75 108.43 111.93 123.14 * * 24 VAL 24 1.311 1.215 1.541 1.563 1.437 121.17 116.12 121.07 111.27 109.47 111.98 122.78 * * * 25 GLU 25 1.332 1.245 1.533 1.517 1.456 122.49 116.15 120.63 110.46 110.44 109.51 123.22 26 THR 26 1.336 1.234 1.536 1.554 1.462 121.96 115.26 121.09 109.41 109.61 110.84 123.62 27 TRP 27 1.326 1.237 1.534 1.536 1.457 123.54 115.31 121.13 111.64 110.43 108.19 123.54 * * * 28 ASN 28 1.320 1.229 1.521 1.537 1.458 123.46 115.65 120.67 109.51 110.91 109.75 123.67 29 GLU 29 1.326 1.242 1.530 1.539 1.462 123.33 115.88 120.90 110.47 110.82 109.15 123.20 30 GLN 30 1.319 1.234 1.515 1.487 1.412 122.71 117.50 119.95 111.79 113.06 109.40 122.54 ** ** ** 31 LEU 31 1.326 1.206 1.498 1.485 1.419 121.47 115.96 120.65 109.30 111.18 110.37 123.38 * * ** ** ** 32 GLN 32 1.294 1.236 1.521 1.524 1.441 123.01 116.00 120.78 112.14 109.83 108.77 123.15 ** * * ** 33 LYS 33 1.321 1.227 1.527 1.544 1.442 121.30 116.39 120.75 111.15 109.86 110.95 122.81 34 ALA 34 1.330 1.223 1.531 1.521 1.451 121.53 116.87 120.31 110.50 112.06 110.46 122.81 35 ASN 35 1.326 1.236 1.501 1.518 1.473 122.05 115.57 121.19 107.27 110.16 110.11 123.24 * * * 36 GLU 36 1.322 1.238 1.534 1.541 1.472 120.70 117.56 120.34 111.42 113.74 113.95 122.10 ** ** 37 SER 37 1.317 1.236 1.532 1.513 1.445 120.70 115.45 120.64 110.21 110.77 109.37 123.88 38 LYS 38 1.336 1.235 1.547 1.514 1.418 125.04 114.14 122.66 115.37 112.20 112.02 123.11 * ** +* * * +** +** 39 THR 39 1.308 1.237 1.527 1.529 1.441 123.60 116.56 120.74 108.10 108.58 110.83 122.63 +* * +* 40 LEU 40 1.297 1.240 1.534 1.534 1.389 122.39 116.42 120.76 111.00 109.45 110.55 122.80 ** +*** +*** 41 VAL 41 1.301 1.238 1.526 1.568 1.426 121.35 115.79 120.90 111.63 111.04 111.35 123.25 +* * +* * +* 42 VAL 42 1.305 1.237 1.511 1.538 1.437 122.53 116.40 120.84 110.07 108.38 111.94 122.75 +* * * +* 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 1.300 1.234 1.516 1.553 1.437 121.05 115.89 120.52 108.90 110.32 111.59 123.59 ** * ** 44 ASP 44 1.305 1.246 1.506 1.529 1.450 122.47 115.60 120.97 110.06 110.50 111.41 123.39 +* +* 45 PHE 45 1.303 1.238 1.510 1.519 1.413 122.49 116.34 120.71 110.09 107.33 109.33 122.91 +* ** * ** 46 THR 46 1.291 1.235 1.527 1.567 1.428 121.03 116.41 120.63 110.45 109.77 109.80 122.89 +** * +* * +** 47 ALA 47 1.298 1.234 1.502 1.518 1.431 122.72 116.22 120.31 110.66 107.98 111.11 123.47 ** * * * ** 48 SER 48 1.304 1.224 1.543 1.525 1.451 122.71 116.51 120.92 111.16 111.39 109.14 122.56 +* +* 49 TRP 49 1.326 1.235 1.531 1.543 1.455 121.27 116.22 120.76 111.29 111.73 111.72 123.02 50 CYS 50 1.313 1.226 1.520 1.540 1.446 122.33 115.75 120.57 111.27 109.63 109.97 123.68 * * 51 GLY 51 1.324 1.245 1.528 - 1.461 122.96 118.72 119.62 - 114.85 - 121.66 * * * 52 PRO 52 1.354 1.226 1.526 1.539 1.469 122.54 115.61 121.23 110.65 111.93 103.90 123.14 53 CYS 53 1.312 1.229 1.537 1.518 1.453 122.87 115.72 121.53 109.28 110.21 108.72 122.74 * * * 54 ARG 54 1.310 1.231 1.528 1.519 1.446 122.88 115.34 121.38 110.94 109.55 107.82 123.26 * +* +* 55 PHE 55 1.319 1.232 1.532 1.544 1.455 122.77 116.91 120.81 110.07 111.29 110.08 122.25 56 ILE 56 1.317 1.234 1.544 1.572 1.450 120.51 115.74 121.41 110.68 109.69 110.89 122.81 * * 57 ALA 57 1.326 1.236 1.553 1.521 1.454 122.30 120.27 119.12 112.24 112.99 111.44 120.60 * ** * * ** 58 PRO 58 1.381 1.231 1.525 1.537 1.474 121.70 115.67 121.35 109.98 111.21 103.93 122.97 +** +** 59 PHE 59 1.318 1.233 1.541 1.539 1.450 122.31 115.70 121.13 111.15 109.06 109.05 123.16 60 PHE 60 1.328 1.223 1.532 1.538 1.464 123.08 116.67 120.67 111.51 110.82 109.77 122.64 61 ALA 61 1.326 1.232 1.528 1.521 1.472 121.57 114.85 121.90 110.59 109.75 110.61 123.25 62 ASP 62 1.309 1.229 1.503 1.507 1.455 123.02 114.54 121.55 109.67 109.14 108.71 123.90 * * * * * 63 LEU 63 1.310 1.235 1.525 1.512 1.437 123.66 115.64 120.87 110.50 111.00 108.56 123.48 * * * * * 64 ALA 64 1.317 1.224 1.530 1.524 1.448 122.85 116.64 120.96 110.66 111.20 110.34 122.40 65 LYS 65 1.329 1.246 1.539 1.543 1.451 121.03 116.17 121.23 112.56 110.69 110.56 122.60 * * 66 LYS 66 1.327 1.230 1.524 1.529 1.454 121.63 116.84 120.42 108.96 111.30 111.69 122.74 67 LEU 67 1.319 1.215 1.526 1.547 1.442 121.96 118.22 120.34 109.47 110.50 111.60 121.44 * * 68 PRO 68 1.339 1.231 1.538 1.529 1.462 122.11 116.46 120.94 110.52 112.84 102.41 122.60 69 ASN 69 1.318 1.232 1.516 1.522 1.441 122.19 116.36 120.74 109.52 111.76 109.61 122.91 70 VAL 70 1.311 1.225 1.515 1.559 1.448 122.13 116.57 120.34 109.84 109.21 111.62 123.06 * * 71 LEU 71 1.306 1.236 1.548 1.552 1.439 121.50 117.61 120.19 111.74 106.90 108.25 122.18 +* * * +* * +* 72 PHE 72 1.324 1.239 1.522 1.529 1.464 121.35 115.86 120.95 108.05 111.18 111.23 123.18 * * 73 LEU 73 1.312 1.231 1.501 1.539 1.457 122.85 114.33 121.67 109.43 112.41 114.68 124.00 * * ** ** 74 LYS 74 1.294 1.240 1.509 1.538 1.427 124.45 116.52 120.30 109.73 108.63 108.93 123.15 ** +* +* ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 75 VAL 75 1.301 1.245 1.510 1.559 1.435 121.15 115.86 120.94 109.53 109.70 112.07 123.19 +* * +* 76 ASP 76 1.307 1.239 1.515 1.515 1.432 121.24 115.23 121.36 111.45 108.35 111.22 123.40 +* * * +* 77 THR 77 1.301 1.238 1.536 1.539 1.454 124.02 116.74 120.87 111.03 113.64 110.71 122.36 +* * +* 78 ASP 78 1.311 1.235 1.511 1.520 1.448 121.04 114.40 121.49 110.62 107.31 109.55 124.06 * * * 79 GLU 79 1.318 1.239 1.546 1.520 1.423 123.77 117.06 120.79 109.96 111.94 108.85 122.13 * +* * +* 80 LEU 80 1.326 1.238 1.525 1.511 1.424 121.85 115.42 121.49 111.27 113.90 110.44 123.04 +* +* 81 LYS 81 1.309 1.228 1.514 1.514 1.452 122.31 116.51 120.65 111.47 112.55 111.46 122.84 * * 82 SER 82 1.323 1.229 1.524 1.516 1.452 121.36 115.68 121.13 111.04 110.29 109.99 123.15 83 VAL 83 1.320 1.229 1.523 1.547 1.443 121.82 115.74 121.07 110.18 109.25 111.32 123.15 84 ALA 84 1.325 1.230 1.526 1.522 1.451 121.93 116.46 120.70 110.58 110.63 110.46 122.79 85 SER 85 1.321 1.238 1.537 1.536 1.440 121.60 117.05 120.28 110.90 111.07 110.29 122.64 86 ASP 86 1.337 1.239 1.526 1.534 1.469 121.37 115.61 121.05 108.77 110.88 110.54 123.25 87 TRP 87 1.315 1.244 1.522 1.525 1.446 122.61 115.90 120.28 111.13 112.19 110.56 123.82 88 ALA 88 1.343 1.235 1.528 1.536 1.473 123.91 116.14 120.98 111.23 111.54 110.57 122.83 * * * 89 ILE 89 1.317 1.242 1.517 1.555 1.444 122.07 115.50 121.11 109.88 109.04 111.69 123.36 90 GLN 90 1.303 1.237 1.531 1.534 1.437 121.74 116.22 121.00 111.56 110.56 109.46 122.77 +* * +* 91 ALA 91 1.314 1.232 1.520 1.514 1.444 121.96 116.81 120.81 111.06 109.80 110.54 122.37 * * 92 MET 92 1.303 1.234 1.520 1.516 1.437 121.54 118.42 120.00 108.45 110.05 108.93 121.57 +* * * +* 93 PRO 93 1.336 1.240 1.534 1.525 1.455 124.06 117.03 120.59 110.44 110.70 102.56 122.33 94 THR 94 1.293 1.231 1.516 1.525 1.425 120.69 115.80 120.75 110.30 110.10 111.73 123.44 +** +* +** 95 PHE 95 1.302 1.238 1.503 1.524 1.417 122.92 116.74 120.25 108.57 107.29 108.84 123.00 +* * ** * ** 96 MET 96 1.298 1.233 1.508 1.507 1.432 120.67 115.49 121.02 109.71 108.90 109.65 123.49 ** * * ** 97 PHE 97 1.289 1.243 1.514 1.522 1.418 123.68 116.86 120.76 107.79 110.49 108.82 122.39 +** ** * * +** 98 LEU 98 1.292 1.233 1.528 1.557 1.413 120.82 116.80 120.47 112.88 109.72 110.02 122.73 +** * ** * +** 99 LYS 99 1.298 1.240 1.497 1.532 1.431 121.69 114.75 120.94 110.46 110.25 113.27 124.27 ** * * +* ** 100 GLU 100 1.329 1.223 1.533 1.525 1.452 123.77 115.66 121.22 111.79 111.58 109.70 123.05 * * 101 GLY 101 1.317 1.231 1.525 - 1.452 121.71 117.68 120.04 - 113.80 - 122.28 102 LYS 102 1.314 1.229 1.516 1.529 1.455 120.59 116.77 120.15 110.22 109.49 110.67 123.07 * * 103 ILE 103 1.314 1.238 1.521 1.555 1.457 122.38 116.24 120.65 109.13 110.71 111.40 123.11 * * 104 LEU 104 1.313 1.229 1.517 1.528 1.422 121.58 116.42 121.02 109.44 110.86 110.74 122.52 * +* +* 105 ASP 105 1.315 1.226 1.495 1.528 1.446 120.81 115.37 121.14 108.09 111.79 111.57 123.48 * * * 106 LYS 106 1.295 1.243 1.520 1.537 1.440 122.39 116.42 120.73 110.90 109.84 111.80 122.82 ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 107 VAL 107 1.303 1.228 1.509 1.561 1.449 122.03 116.48 120.30 109.46 108.77 112.02 123.18 +* +* 108 VAL 108 1.305 1.242 1.533 1.559 1.429 121.45 116.00 121.12 111.54 110.35 111.42 122.84 +* +* * +* 109 GLY 109 1.304 1.239 1.500 - 1.433 120.78 117.18 120.33 - 110.34 - 122.48 +* * +* 110 ALA 110 1.311 1.232 1.512 1.523 1.434 119.73 115.22 121.22 110.64 110.07 110.48 123.51 * * * * 111 LYS 111 1.305 1.223 1.498 1.516 1.425 123.55 117.06 119.65 110.35 109.72 110.89 123.29 +* * +* * +* 112 LYS 112 1.303 1.236 1.535 1.520 1.429 121.47 115.46 121.23 107.75 110.25 108.29 123.19 +* +* * * +* 113 ASP 113 1.324 1.227 1.502 1.526 1.459 122.20 116.40 120.65 110.68 112.94 111.59 122.95 * * 114 GLU 114 1.314 1.236 1.522 1.533 1.457 121.21 116.35 120.96 111.12 110.47 110.77 122.67 * * 115 LEU 115 1.316 1.216 1.506 1.505 1.436 120.73 115.79 120.78 110.16 108.66 110.65 123.41 * * * 116 GLN 116 1.320 1.234 1.524 1.534 1.483 122.23 116.51 120.37 109.18 111.61 111.89 123.12 * * 117 SER 117 1.320 1.224 1.524 1.533 1.443 121.52 116.06 121.00 111.37 109.66 110.33 122.93 118 THR 118 1.319 1.237 1.538 1.546 1.441 122.10 116.18 121.17 110.98 109.71 110.58 122.64 119 ILE 119 1.325 1.220 1.526 1.559 1.444 121.44 116.34 120.57 110.61 109.32 111.91 123.00 120 ALA 120 1.326 1.223 1.523 1.521 1.466 122.12 116.04 120.56 110.84 111.07 110.87 123.40 121 LYS 121 1.324 1.225 1.516 1.505 1.455 123.03 115.10 121.51 108.32 109.72 108.96 123.38 * * 122 HIS 122 1.313 1.225 1.519 1.521 1.439 122.61 117.82 119.94 110.81 113.40 111.48 122.24 * * * 123 LEU 123 1.312 1.234 1.511 1.513 1.411 120.80 115.63 121.27 111.54 112.01 110.73 123.08 * ** ** 124 ALA 124 1.296 - 1.512 1.526 1.431 122.27 - - 111.30 108.65 110.57 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** +*** +* ** * +** +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- 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 1.269 1.346 1.313 .013 **** * * C-N (Pro) 1.341 .016 4 1.336 1.381 1.353 .018 +** C-O C-O 1.231 .020 123 1.206 1.251 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.487 1.553 1.521 .013 +* * CH2G*-C (Gly) 1.516 .018 5 1.489 1.528 1.510 .015 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.514 1.536 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.573 1.554 .012 * CH1E-CH2E (the rest) 1.530 .020 84 1.485 1.568 1.530 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.389 1.483 1.443 .017 +*** * NH1-CH2G* (Gly) 1.451 .016 5 1.433 1.461 1.445 .010 * N-CH1E (Pro) 1.466 .015 4 1.455 1.474 1.465 .007 ------------------------------------------------------------------------------------------------------------- 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 2.0 114 112.88 120.27 116.10 .92 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.79 118.72 116.80 1.41 * CH1E-C-N (Pro) 116.9 1.5 4 115.61 117.03 116.19 .59 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.60 124.27 123.01 .58 * O-C-N (Pro) 122.0 1.4 4 122.33 123.14 122.76 .31 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.73 125.30 122.15 1.08 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.82 122.96 121.21 1.06 * C-N-CH1E (Pro) 122.6 5.0 4 121.70 124.06 122.60 .89 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.12 123.12 120.86 .52 * CH2G*-C-O (Gly) 120.8 2.1 5 119.62 121.67 120.35 .70 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.50 112.24 111.01 .53 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.75 112.12 110.18 1.10 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.27 115.37 110.56 1.34 * +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 106.25 113.90 110.26 1.55 +* NH1-CH2G*-C (Gly) 112.5 2.9 5 110.18 114.85 112.44 1.87 N-CH1E-C (Pro) 111.8 2.5 4 110.70 112.84 111.67 .80 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.34 112.23 110.78 .51 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.58 113.44 111.35 .93 +* * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.41 103.93 103.20 .72 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.82 114.68 110.55 1.49 +* ** ------------------------------------------------------------------------------------------------------------- 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] 97 85.8% Residues in additional allowed regions [a,b,l,p] 15 13.3% 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 85.8 83.8 10.0 .2 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 78 .8 .8 .2 .1 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 13 5.5 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 46 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 43 7.9 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.4 18.2 4.8 -2.2 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% 85.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .83 2 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 -.25 Chi1-chi2 distribution .00 Chi1 only .08 Chi3 & chi4 .28 Omega .04 ------ -.03 ===== Main-chain covalent forces:- Main-chain bond lengths .05 Main-chain bond angles .47 ------ .29 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.