Residue-by-residue listing for refined_17 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 - - - -61.0 - - - - - - - 180.8 - 34.5 - 2 GLY 2 - - - - - - - - - - - 179.3 - - - 3 HIS 3 B - - -68.6 - - - - - - - 180.3 - 33.1 - 4 HIS 4 B - 181.9 - - - - - - - - 179.1 -.8 34.5 - +* +* 5 HIS 5 B - - -63.4 - - - - - - - 178.4 - 34.7 - 6 HIS 6 S A 63.6 - - - - - - - - - 175.6 -.7 31.5 - +* +* 7 HIS 7 S b - 179.2 - - - - - - - - 178.9 - 33.2 - 8 HIS 8 a - 181.0 - - - - - - - - 182.5 -.7 33.8 - +* +* 9 LEU 9 l - - -69.4 - - - - - - - 183.5 - 31.0 - 10 GLU 10 B 56.0 - - 186.8 - - - - - - 180.6 - 33.9 - 11 MET 11 B - 178.9 - - - - - - - - 178.9 - 35.2 - 12 ALA 12 b - - - - - - - - - - 182.6 -.8 33.0 - +* +* 13 SER 13 S b - 183.6 - - - - - - - - 178.3 -1.3 35.3 - 14 GLU 14 B - 181.1 - 184.0 - - - - - - 181.7 - 34.4 - 15 GLU 15 B 68.7 - - - - - - - - - 175.9 -.6 34.0 - +* +* 16 GLY 16 S - - - - - - - - - - - 179.5 -1.9 - - 17 GLN 17 B 54.0 - - 177.4 - - - - - - 180.7 - 31.5 - 18 VAL 18 B - 181.7 - - - - - - - - 180.3 - 36.6 - 19 ILE 19 E B - - -59.2 182.0 - - - - - - 179.9 -2.9 33.0 - * * 20 ALA 20 E B - - - - - - - - - - 182.2 -.9 34.2 - +* +* Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B - - -51.9 - - - - - - - 176.8 -2.9 35.9 - * * 22 HIS 22 S A - - -60.5 - - - - - - - 181.6 -.5 34.1 - ** ** 23 THR 23 h B 57.8 - - - - - - - - - 175.7 - 35.7 - 24 VAL 24 H A 64.0 - - - - -72.1 -22.4 - - - 178.1 - 32.7 - +* +* 25 GLU 25 H A - 181.2 - 179.1 - -59.9 -51.8 - - - 178.6 - 35.1 - * * 26 THR 26 H A - - -55.9 - - -61.3 -43.3 - - - 179.0 - 35.0 - 27 TRP 27 H A - 173.1 - - - -58.1 -55.5 - - - 182.8 -1.5 35.0 - * * 28 ASN 28 H A - 185.0 - - - -65.6 -46.2 - - - 184.8 -3.4 34.8 - +* +* 29 GLU 29 H A - 185.3 - 172.7 - -61.3 -46.5 - - - 178.3 -2.7 32.8 - 30 GLN 30 H A - - -87.1 - - -68.4 -33.6 - - - 176.7 -2.2 31.4 - * * 31 LEU 31 H A - - -68.7 181.1 - -69.2 -45.0 - - - 176.7 -1.7 34.2 - 32 GLN 32 H A - 175.9 - 169.6 - -63.1 -36.6 - - - 175.1 -2.8 32.5 - 33 LYS 33 H A - 180.4 - 185.8 - -62.2 -47.9 - - - 181.6 -2.3 34.9 - 34 ALA 34 H A - - - - - -66.0 -44.0 - - - 180.6 -2.7 33.6 - 35 ASN 35 H A - 184.3 - - - -59.5 -55.1 - - - 181.8 -3.4 37.1 - * +* +* 36 GLU 36 H A - 182.6 - 180.3 - -62.0 -36.1 - - - 182.8 -2.6 34.0 - 37 SER 37 H A - - -55.4 - - -89.3 -1.6 - - - 182.7 -2.1 34.8 - ** *** *** 38 LYS 38 h l - - -84.7 161.1 - - - - - - 178.0 -1.2 32.0 - * * * 39 THR 39 e B - - -48.4 - - - - - - - 179.7 -2.3 35.7 - * * 40 LEU 40 E B - 188.4 - 171.6 - - - - - - 185.2 -.7 34.0 - +* +* 41 VAL 41 E B 57.0 - - - - - - - - - 177.6 -.9 32.9 - +* +* 42 VAL 42 E B - 182.9 - - - - - - - - 182.7 -2.5 34.4 - 43 VAL 43 E B - 183.1 - - - - - - - - 177.0 -2.5 34.6 - 44 ASP 44 E B - 172.4 - - - - - - - - 177.0 -3.2 34.5 - * * 45 PHE 45 E B - - -62.4 - - - - - - - 184.9 -3.1 35.9 - * * 46 THR 46 E B - - -70.3 - - - - - - - 173.0 -2.0 35.6 - * * 47 ALA 47 t B - - - - - - - - - - 183.9 - 34.2 - 48 SER 48 T A 59.8 - - - - - - - - - 181.6 - 33.8 - 49 TRP 49 T A 53.6 - - - - - - - - - 177.6 - 31.0 - 50 CYS 50 h B - 176.3 - 218.7 - - - 52.4 - 2.0 183.2 -2.3 33.6 - ** *** *** 51 GLY 51 H - - - - - - -59.4 -72.3 - - - 180.1 -.6 - - +** +* +** 52 PRO 52 H - - - - - -54.3 -54.3 -35.7 - - - 180.8 - 39.4 - +* +* 53 CYS 53 H A - - -53.1 - - -63.3 -38.1 52.4 - 2.0 182.0 - 35.8 - *** *** 54 ARG 54 H A - 195.7 - - - -66.1 -28.5 - - - 179.3 -1.7 34.3 - 55 PHE 55 H A - 176.9 - - - -79.7 -31.9 - - - 185.2 -1.0 34.6 - * * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 ILE 56 H A - 190.7 - - - -87.0 -22.5 - - - 178.8 -1.5 33.3 - +* * +* 57 ALA 57 H A - - - - - -56.7 -48.9 - - - 177.3 -1.9 31.1 - 58 PRO 58 H - - - - - -61.1 -61.1 -26.7 - - - 177.4 - 38.7 - * * * 59 PHE 59 H A - 179.5 - - - -70.7 -45.8 - - - 177.8 - 34.0 - 60 PHE 60 H A - 187.1 - - - -63.1 -33.4 - - - 175.9 -2.3 34.9 - 61 ALA 61 H A - - - - - -66.3 -27.6 - - - 177.0 -2.2 33.6 - * * 62 ASP 62 H A - 181.1 - - - -71.5 -44.7 - - - 173.4 -.8 35.3 - * +* +* 63 LEU 63 H A - - -84.9 - - -52.7 -45.1 - - - 177.4 -1.8 34.7 - * * * 64 ALA 64 H A - - - - - -62.7 -31.2 - - - 179.4 -2.0 33.5 - 65 LYS 65 H A - 185.6 - 181.1 - -79.3 -36.3 - - - 183.8 -.9 34.4 - * * * 66 LYS 66 H A - 182.1 - 182.3 - -78.2 -41.1 - - - 181.0 -2.7 34.0 - * * 67 LEU 67 h b - - -65.3 - - - - - - - 183.6 -3.1 33.5 - * * 68 PRO 68 T - - - - - -83.4 - - - - - 182.0 - 39.1 - +* * +* 69 ASN 69 e A - 189.0 - - - - - - - - 178.0 - 33.9 - 70 VAL 70 E B - 179.0 - - - - - - - - 182.6 -.6 33.3 - +* +* 71 LEU 71 E B - 208.8 - 183.7 - - - - - - 180.6 -2.9 36.2 - * * * 72 PHE 72 E B - - -58.9 - - - - - - - 179.5 - 34.7 - 73 LEU 73 E B - - -67.5 - - - - - - - 176.4 -2.1 32.7 - 74 LYS 74 E B - 164.5 - - - - - - - - 177.7 -3.0 33.0 - * * * 75 VAL 75 E B - 178.8 - - - - - - - - 178.6 -2.5 34.8 - 76 ASP 76 E B - 185.6 - - - - - - - - 184.1 -.8 33.5 - +* +* 77 THR 77 e A - 181.6 - - - - - - - - 177.2 -1.0 31.7 - * * 78 ASP 78 T A - 185.8 - - - - - - - - 177.7 - 34.5 - 79 GLU 79 T a - 190.9 - - - - - - - - 184.7 - 37.5 - * * 80 LEU 80 h b - - -65.8 178.9 - - - - - - 180.4 -3.3 33.4 - +* +* 81 LYS 81 H A - - -61.1 179.1 - -68.8 -33.3 - - - 179.4 -1.5 33.4 - 82 SER 82 H A - - -57.2 - - -65.8 -41.9 - - - 177.0 - 33.7 - 83 VAL 83 H A - 178.2 - - - -64.4 -41.0 - - - 178.0 - 34.3 - 84 ALA 84 H A - - - - - -62.3 -42.2 - - - 177.7 -1.9 33.9 - 85 SER 85 H A - - -60.0 - - -63.2 -42.7 - - - 182.2 -2.7 34.2 - 86 ASP 86 H A - 183.6 - - - -62.2 -36.6 - - - 179.4 -2.5 34.4 - 87 TRP 87 h A - - -69.9 - - - - - - - 178.2 -2.0 32.5 - 88 ALA 88 T L - - - - - - - - - - 181.6 -1.3 33.7 - 89 ILE 89 t B - - -55.4 - - - - - - - 179.7 -3.1 34.6 - * * 90 GLN 90 A - - -67.5 175.3 - - - - - - 179.5 -.9 33.7 - +* +* 91 ALA 91 S B - - - - - - - - - - 180.9 - 34.2 - 92 MET 92 S B - - -62.9 175.9 - - - - - - -3.7 - 35.1 - 93 PRO 93 e cis - - - - - -93.8 - - - - - 175.0 - 40.0 - +** +* +** Residue-by-residue listing for refined_17 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 94 THR 94 E B - - -55.0 - - - - - - - 179.5 -2.1 33.8 - 95 PHE 95 E B - - -58.6 - - - - - - - 180.9 -3.7 35.9 - ** ** 96 MET 96 E B - 184.9 - - - - - - - - 182.3 -3.0 34.3 - * * 97 PHE 97 E B - - -70.4 - - - - - - - 177.3 -2.6 35.3 - 98 LEU 98 E B 58.7 - - 169.0 - - - - - - 180.9 -1.8 32.8 - 99 LYS 99 E B - 170.9 - 179.6 - - - - - - 178.6 -3.3 33.9 - +* +* 100 GLU 100 e l - - -59.8 173.6 - - - - - - 180.9 -.6 33.5 - +* +* 101 GLY 101 T - - - - - - - - - - - 179.0 - - - 102 LYS 102 E B - - -55.9 180.8 - - - - - - 184.5 -2.3 35.3 - 103 ILE 103 E B - - -63.8 - - - - - - - 177.8 - 33.3 - 104 LEU 104 E a - - -69.2 180.6 - - - - - - 185.5 -2.2 34.1 - 105 ASP 105 E B 49.9 - - - - - - - - - 182.0 -2.2 31.8 - 106 LYS 106 E B 48.2 - - - - - - - - - 178.3 - 31.5 - * * 107 VAL 107 E B - 174.3 - - - - - - - - 178.5 -3.2 34.3 - +* +* 108 VAL 108 E B 62.9 - - - - - - - - - 181.6 - 33.2 - 109 GLY 109 e - - - - - - - - - - - 184.8 -2.9 - - * * 110 ALA 110 B - - - - - - - - - - 171.6 - 34.7 - * * 111 LYS 111 h B - - -67.3 - - - - - - - 184.5 -1.0 34.3 - * * 112 LYS 112 H A - 178.5 - 179.4 - -59.5 -50.3 - - - 184.2 - 34.4 - 113 ASP 113 H A - 188.8 - - - -72.6 -32.6 - - - 179.9 - 33.5 - 114 GLU 114 H A - - -62.9 - - -72.8 -39.1 - - - 179.4 - 34.1 - 115 LEU 115 H A - 187.7 - - - -60.5 -49.7 - - - 178.7 -2.6 35.7 - 116 GLN 116 H A - 180.4 - - - -60.2 -34.6 - - - 178.5 -1.9 35.6 - 117 SER 117 H A - 185.0 - - - -68.7 -39.2 - - - 177.2 -1.4 33.9 - 118 THR 118 H A - - -55.2 - - -67.2 -31.1 - - - 174.4 -2.4 33.3 - 119 ILE 119 H A - - -60.9 - - -60.8 -50.0 - - - 178.9 -1.9 33.9 - 120 ALA 120 H A - - - - - -63.0 -30.4 - - - 177.3 -2.2 32.8 - 121 LYS 121 H A - 191.2 - 180.2 - -60.7 -40.8 - - - 178.4 -1.7 35.8 - 122 HIS 122 H A - - -77.6 - - -70.1 -35.2 - - - 179.8 -1.6 33.0 - 123 LEU 123 h B - - -78.8 - - - - - - - 177.8 -1.5 34.7 - 124 ALA 124 - - - - - - - - - - - - - 34.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * ** +** ** *** *** * ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.0 182.6 -64.2 179.6 -73.1 -65.8 -39.3 52.4 - 2.0 179.7 -2.0 34.2 *** *** Standard deviations: 5.8 6.9 9.0 9.6 18.6 7.6 10.9 .0 - .0 2.8 .9 1.6 Numbers of values: 13 48 41 27 4 47 47 2 0 2 122 83 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_17 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_17 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 - 1.230 1.511 1.536 1.459 - 116.64 120.64 109.67 108.70 111.25 122.72 2 GLY 2 1.305 1.226 1.489 - 1.428 120.56 116.39 120.38 - 111.04 - 123.20 +* +* * +* 3 HIS 3 1.298 1.231 1.503 1.534 1.439 121.54 115.76 121.03 110.57 110.17 112.12 123.20 ** * * ** 4 HIS 4 1.303 1.224 1.518 1.542 1.441 121.93 116.55 120.70 110.49 109.42 110.38 122.74 +* +* 5 HIS 5 1.300 1.227 1.512 1.546 1.446 121.61 117.28 120.07 109.52 109.11 111.23 122.63 ** ** 6 HIS 6 1.330 1.227 1.521 1.560 1.471 120.66 115.48 121.39 111.62 110.21 113.26 123.12 +* +* +* 7 HIS 7 1.309 1.234 1.513 1.545 1.431 121.95 115.45 121.11 111.02 108.89 112.11 123.35 * * * 8 HIS 8 1.298 1.219 1.511 1.553 1.441 122.10 115.83 120.00 110.91 109.61 111.05 124.14 ** * ** 9 LEU 9 1.345 1.227 1.512 1.558 1.468 123.55 115.85 121.44 111.44 110.61 113.91 122.69 * * * ** ** 10 GLU 10 1.292 1.239 1.504 1.525 1.432 121.28 115.78 120.86 111.79 110.80 109.44 123.35 +** * * +** 11 MET 11 1.297 1.227 1.513 1.530 1.436 121.88 116.88 120.13 110.33 109.13 109.62 122.95 ** * ** 12 ALA 12 1.318 1.236 1.521 1.524 1.446 121.01 115.38 120.80 111.31 110.06 111.28 123.77 Residue-by-residue listing for refined_17 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 13 SER 13 1.314 1.240 1.527 1.557 1.438 124.09 117.02 120.13 110.27 107.32 110.12 122.86 * * * * * * 14 GLU 14 1.301 1.238 1.521 1.528 1.434 122.28 116.30 120.97 110.54 109.07 110.44 122.68 ** * ** 15 GLU 15 1.309 1.237 1.517 1.556 1.437 121.07 116.35 120.79 109.87 109.98 111.72 122.86 * * * * 16 GLY 16 1.305 1.230 1.500 - 1.446 120.82 116.98 120.16 - 113.82 - 122.85 +* +* 17 GLN 17 1.306 1.230 1.492 1.535 1.436 120.82 114.07 121.62 111.05 112.10 113.07 124.31 +* +* * * +* +* 18 VAL 18 1.283 1.242 1.527 1.557 1.437 123.97 118.76 119.29 109.44 107.23 108.99 121.95 *** * * * * * *** 19 ILE 19 1.325 1.237 1.518 1.552 1.438 118.91 115.58 121.36 110.66 109.92 112.39 123.05 * +* +* 20 ALA 20 1.307 1.231 1.504 1.523 1.438 122.10 116.29 120.60 110.89 109.16 110.49 123.09 +* * * +* 21 CYS 21 1.299 1.228 1.507 1.507 1.413 121.71 116.14 120.86 109.39 109.58 109.20 122.98 ** * ** ** 22 HIS 22 1.297 1.232 1.512 1.546 1.446 121.59 115.15 121.45 110.49 108.22 111.44 123.39 ** * ** 23 THR 23 1.330 1.248 1.509 1.561 1.439 122.77 116.89 120.12 108.02 108.60 111.58 122.99 * * 24 VAL 24 1.319 1.222 1.537 1.568 1.442 120.86 115.80 121.21 111.37 108.89 112.55 122.98 * * * 25 GLU 25 1.340 1.233 1.520 1.523 1.456 122.57 116.05 120.33 109.11 110.55 110.23 123.62 26 THR 26 1.330 1.237 1.534 1.547 1.457 122.16 114.90 121.27 109.92 109.96 109.93 123.81 27 TRP 27 1.313 1.234 1.548 1.536 1.448 123.48 116.35 120.77 111.57 112.15 107.57 122.82 * * +* +* 28 ASN 28 1.316 1.243 1.529 1.548 1.465 122.63 115.78 120.94 110.53 111.01 109.31 123.25 29 GLU 29 1.320 1.235 1.534 1.535 1.454 122.57 117.14 120.04 112.30 111.98 109.91 122.82 * * 30 GLN 30 1.328 1.228 1.519 1.496 1.427 122.43 118.29 119.64 112.59 114.52 110.34 122.07 +* +* * * * +* 31 LEU 31 1.325 1.225 1.499 1.486 1.419 120.72 115.86 120.76 110.09 110.45 110.54 123.37 * ** ** ** 32 GLN 32 1.309 1.228 1.520 1.527 1.435 121.98 116.14 120.50 113.46 110.18 109.85 123.30 * * +* +* 33 LYS 33 1.322 1.232 1.529 1.532 1.444 121.96 116.57 120.50 109.12 109.72 110.84 122.93 34 ALA 34 1.335 1.226 1.517 1.521 1.453 121.81 115.97 120.33 110.52 111.24 110.78 123.69 35 ASN 35 1.322 1.232 1.496 1.530 1.467 123.05 114.32 121.80 107.52 109.94 109.27 123.82 * * * 36 GLU 36 1.300 1.236 1.540 1.520 1.456 122.53 116.97 120.91 110.48 112.34 109.77 122.11 ** ** 37 SER 37 1.309 1.238 1.536 1.514 1.439 120.97 117.41 119.96 109.98 112.40 109.22 122.63 * * 38 LYS 38 1.352 1.237 1.506 1.514 1.472 121.71 115.00 121.59 112.14 111.96 110.97 123.35 +* * +* 39 THR 39 1.300 1.241 1.507 1.525 1.407 121.54 116.14 121.08 108.80 107.29 111.04 122.78 ** +** * +** 40 LEU 40 1.265 1.236 1.528 1.561 1.424 120.75 117.10 120.08 113.29 105.71 109.75 122.78 *4.5* +* +* +* +* *4.5* 41 VAL 41 1.302 1.233 1.530 1.563 1.429 121.10 115.97 120.92 112.23 111.91 110.36 123.07 +* +* * +* 42 VAL 42 1.309 1.238 1.522 1.541 1.442 122.50 116.90 120.61 109.25 108.44 112.03 122.49 * * Residue-by-residue listing for refined_17 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 1.304 1.224 1.522 1.550 1.448 120.84 115.89 120.36 108.99 111.06 111.32 123.75 +* +* 44 ASP 44 1.311 1.250 1.526 1.549 1.457 123.73 116.00 120.93 110.97 109.73 109.85 122.99 * * * 45 PHE 45 1.314 1.241 1.521 1.523 1.425 122.52 115.98 120.52 108.95 108.44 110.01 123.43 * +* +* 46 THR 46 1.308 1.208 1.525 1.557 1.446 122.96 116.63 120.34 109.93 110.17 109.30 122.95 +* * * +* 47 ALA 47 1.304 1.242 1.513 1.520 1.447 122.59 116.94 119.72 110.32 107.27 111.35 123.34 +* * +* 48 SER 48 1.318 1.237 1.548 1.528 1.472 122.79 116.87 120.68 110.29 113.32 109.78 122.45 * * 49 TRP 49 1.324 1.232 1.535 1.546 1.451 121.55 117.54 120.41 112.26 113.57 111.78 122.01 * * 50 CYS 50 1.314 1.235 1.525 1.534 1.455 120.41 115.83 120.54 110.47 109.98 111.28 123.62 * * 51 GLY 51 1.333 1.234 1.521 - 1.461 122.75 118.70 119.64 - 114.00 - 121.65 * * * 52 PRO 52 1.357 1.231 1.527 1.532 1.483 122.96 115.43 121.47 109.66 112.01 102.96 123.08 * * * 53 CYS 53 1.311 1.227 1.531 1.504 1.449 122.86 116.10 121.24 108.96 111.15 109.00 122.64 * * * 54 ARG 54 1.319 1.230 1.538 1.535 1.452 122.33 115.56 121.06 111.19 109.53 109.69 123.37 55 PHE 55 1.329 1.235 1.535 1.546 1.460 123.29 117.28 120.47 109.92 111.84 109.93 122.22 56 ILE 56 1.321 1.235 1.542 1.572 1.464 120.25 116.22 120.94 110.63 110.78 111.65 122.81 * * 57 ALA 57 1.325 1.230 1.565 1.526 1.462 121.94 120.22 119.20 112.17 113.10 111.56 120.56 +* ** * +* ** 58 PRO 58 1.386 1.234 1.530 1.532 1.476 122.03 116.10 120.97 109.93 111.81 103.87 122.93 +** +** 59 PHE 59 1.322 1.213 1.526 1.540 1.450 121.82 115.89 121.10 111.22 108.93 110.49 122.98 60 PHE 60 1.313 1.229 1.546 1.535 1.464 123.16 115.80 121.38 111.84 109.36 108.11 122.81 * * * * 61 ALA 61 1.323 1.238 1.543 1.520 1.462 122.58 116.21 120.98 110.78 110.86 110.47 122.80 62 ASP 62 1.330 1.222 1.494 1.505 1.473 122.45 114.63 121.31 108.57 108.85 110.73 124.05 * * * 63 LEU 63 1.314 1.227 1.528 1.531 1.438 123.77 115.95 120.61 110.93 110.73 109.14 123.42 * * * * 64 ALA 64 1.322 1.227 1.529 1.518 1.463 122.69 116.09 121.43 110.61 111.60 110.59 122.44 65 LYS 65 1.310 1.238 1.530 1.540 1.447 121.57 115.93 121.06 110.28 110.41 110.34 123.01 * * 66 LYS 66 1.317 1.235 1.532 1.538 1.450 122.01 117.38 120.07 110.63 112.02 109.94 122.54 67 LEU 67 1.324 1.215 1.526 1.552 1.442 121.45 117.96 120.50 110.22 110.11 111.88 121.53 * * 68 PRO 68 1.339 1.242 1.533 1.523 1.461 122.29 116.70 120.80 110.38 113.41 102.50 122.50 69 ASN 69 1.317 1.230 1.537 1.536 1.459 121.18 115.54 122.04 111.34 109.97 110.02 122.42 70 VAL 70 1.306 1.226 1.515 1.558 1.439 122.17 116.61 120.35 111.05 108.30 112.09 122.96 +* * +* 71 LEU 71 1.302 1.232 1.539 1.547 1.438 121.30 117.77 119.99 110.67 107.18 108.32 122.23 +* * * * +* 72 PHE 72 1.315 1.238 1.518 1.525 1.455 120.83 116.29 120.91 108.71 110.49 111.34 122.80 73 LEU 73 1.312 1.228 1.512 1.539 1.446 121.93 114.76 121.36 108.55 112.26 113.84 123.88 * +* +* 74 LYS 74 1.303 1.235 1.504 1.562 1.437 124.14 115.31 121.10 112.14 109.52 111.18 123.55 +* +* * * * +* Residue-by-residue listing for refined_17 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 1.296 1.243 1.502 1.551 1.431 122.20 116.41 120.51 109.54 108.20 111.63 123.05 ** * * * ** 76 ASP 76 1.303 1.224 1.505 1.511 1.433 120.45 116.33 120.53 110.68 108.49 111.66 123.11 +* * +* 77 THR 77 1.304 1.232 1.545 1.564 1.455 122.20 117.48 120.64 111.85 113.05 111.65 121.87 +* * +* 78 ASP 78 1.315 1.229 1.505 1.526 1.458 120.24 113.71 122.00 110.08 107.49 111.06 124.28 * * * 79 GLU 79 1.311 1.236 1.512 1.520 1.440 124.11 115.03 121.82 107.24 109.83 108.85 123.15 * * +* +* 80 LEU 80 1.303 1.237 1.505 1.511 1.398 122.60 114.74 121.73 111.98 111.52 109.79 123.48 +* *** *** 81 LYS 81 1.305 1.219 1.515 1.517 1.440 122.39 116.63 120.52 110.85 111.43 110.64 122.83 +* +* 82 SER 82 1.326 1.231 1.528 1.511 1.448 121.31 116.12 120.71 111.41 110.67 109.82 123.14 83 VAL 83 1.332 1.231 1.525 1.557 1.459 121.82 115.32 121.43 109.73 108.99 111.52 123.23 84 ALA 84 1.320 1.216 1.523 1.505 1.444 122.19 116.72 120.28 110.51 110.73 110.39 123.00 85 SER 85 1.325 1.235 1.532 1.537 1.452 121.69 115.74 120.96 110.13 110.68 110.57 123.24 86 ASP 86 1.322 1.234 1.525 1.534 1.464 122.60 115.99 121.09 110.32 111.22 109.88 122.89 87 TRP 87 1.317 1.229 1.530 1.525 1.444 122.21 116.85 119.89 111.06 113.35 110.96 123.26 88 ALA 88 1.345 1.239 1.539 1.530 1.486 123.35 116.01 121.20 110.71 111.53 110.13 122.73 * * * 89 ILE 89 1.310 1.236 1.519 1.552 1.442 122.11 116.12 120.81 109.01 109.53 111.75 123.04 * * 90 GLN 90 1.304 1.237 1.521 1.517 1.435 122.05 116.25 120.86 111.44 111.46 109.72 122.88 +* * +* 91 ALA 91 1.313 1.238 1.508 1.511 1.440 121.43 116.48 120.96 110.28 109.86 110.54 122.56 * * 92 MET 92 1.299 1.240 1.515 1.515 1.426 121.32 117.83 120.58 109.21 110.40 110.33 121.58 ** +* ** 93 PRO 93 1.321 1.247 1.524 1.534 1.450 123.78 117.02 120.67 109.17 110.66 103.09 122.28 * * * 94 THR 94 1.292 1.226 1.517 1.526 1.421 119.66 116.06 120.77 109.94 109.04 112.05 123.16 +** +* * +** 95 PHE 95 1.296 1.237 1.505 1.523 1.403 123.01 116.53 120.66 109.66 107.88 109.70 122.80 ** +** * +** 96 MET 96 1.285 1.238 1.495 1.518 1.429 121.02 115.64 120.58 110.32 109.07 110.83 123.77 *** * +* *** 97 PHE 97 1.295 1.247 1.498 1.502 1.399 122.70 115.15 121.88 109.45 111.21 109.75 122.97 ** * * *** *** 98 LEU 98 1.277 1.224 1.514 1.549 1.392 122.15 116.92 120.63 112.14 109.38 111.70 122.45 +*** *** * +*** 99 LYS 99 1.283 1.221 1.482 1.526 1.425 121.46 115.13 120.51 109.92 109.74 111.87 124.30 *** ** +* *** 100 GLU 100 1.327 1.225 1.527 1.527 1.456 123.91 115.62 121.28 110.53 110.51 111.16 123.09 * * 101 GLY 101 1.319 1.227 1.518 - 1.433 121.43 116.87 120.35 - 112.36 - 122.78 * * 102 LYS 102 1.319 1.230 1.519 1.528 1.449 121.54 116.37 120.28 109.91 109.18 109.68 123.34 103 ILE 103 1.314 1.240 1.529 1.556 1.471 123.28 115.46 121.20 110.79 112.92 110.59 123.33 * * 104 LEU 104 1.326 1.233 1.510 1.523 1.430 122.65 116.25 120.54 109.74 111.26 111.03 123.20 * * 105 ASP 105 1.312 1.223 1.513 1.529 1.448 122.24 115.83 121.07 111.25 112.84 112.00 123.06 * * Residue-by-residue listing for refined_17 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 1.311 1.225 1.529 1.564 1.449 122.23 116.43 120.97 113.08 112.27 111.13 122.57 * +* +* +* 107 VAL 107 1.307 1.219 1.513 1.562 1.451 122.11 116.83 120.61 109.73 109.64 111.60 122.55 +* +* 108 VAL 108 1.299 1.237 1.532 1.557 1.433 121.38 116.39 120.76 111.56 109.92 111.21 122.80 ** * * ** 109 GLY 109 1.310 1.242 1.505 - 1.443 120.78 117.48 120.25 - 109.93 - 122.27 * * 110 ALA 110 1.313 1.230 1.499 1.520 1.435 119.39 115.05 121.17 109.56 111.19 110.48 123.77 * * * * * 111 LYS 111 1.298 1.231 1.512 1.511 1.414 123.81 116.97 119.89 111.22 107.59 110.39 123.14 ** ** * * ** 112 LYS 112 1.306 1.240 1.533 1.530 1.449 122.83 116.16 120.76 110.67 112.68 109.14 123.06 +* +* 113 ASP 113 1.313 1.229 1.531 1.535 1.458 121.66 115.95 121.33 111.41 110.86 110.29 122.69 * * 114 GLU 114 1.322 1.233 1.519 1.521 1.463 121.70 116.22 120.55 109.40 111.07 111.19 123.22 115 LEU 115 1.325 1.229 1.502 1.516 1.455 122.21 114.65 121.42 108.56 109.05 110.29 123.92 * * 116 GLN 116 1.312 1.242 1.539 1.504 1.417 123.70 116.33 120.69 111.32 110.83 107.15 122.96 * * ** * +* ** 117 SER 117 1.324 1.233 1.538 1.535 1.445 121.68 116.46 120.82 111.20 109.38 110.31 122.69 118 THR 118 1.334 1.232 1.548 1.551 1.447 121.57 116.73 120.93 111.21 109.82 111.17 122.32 * * 119 ILE 119 1.336 1.225 1.527 1.564 1.462 121.15 115.80 120.96 109.76 108.89 112.22 123.18 120 ALA 120 1.321 1.221 1.523 1.521 1.459 122.42 116.55 120.24 111.23 111.27 111.09 123.20 121 LYS 121 1.327 1.230 1.514 1.498 1.460 122.71 114.90 121.48 108.42 110.03 109.74 123.61 +* +* 122 HIS 122 1.310 1.229 1.519 1.523 1.437 122.63 117.03 120.12 110.49 112.67 111.20 122.85 * * * 123 LEU 123 1.317 1.230 1.534 1.518 1.409 121.99 116.67 121.06 111.05 111.36 108.92 122.27 +** +** 124 ALA 124 1.304 - 1.508 1.519 1.446 121.98 - - 110.65 109.16 110.73 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.5* * ** ** *** +* ** +* +* ** +* *4.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 Page 11 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 119 1.265 1.352 1.313 .014 *4.5* +* * C-N (Pro) 1.341 .016 4 1.321 1.386 1.351 .024 * +** C-O C-O 1.231 .020 123 1.208 1.250 1.232 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.482 1.565 1.521 .014 ** +* CH2G*-C (Gly) 1.516 .018 5 1.489 1.521 1.507 .012 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.505 1.530 1.520 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.572 1.554 .011 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.564 1.530 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.392 1.486 1.444 .017 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.428 1.461 1.442 .011 * N-CH1E (Pro) 1.466 .015 4 1.450 1.483 1.468 .013 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 2.0 114 113.71 120.22 116.20 .92 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.39 118.70 117.28 .79 * CH1E-C-N (Pro) 116.9 1.5 4 115.43 117.02 116.32 .61 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.56 124.31 122.98 .58 +* O-C-N (Pro) 122.0 1.4 4 122.28 123.08 122.70 .32 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.91 124.14 122.04 .99 +* * C-NH1-CH2G* (Gly) 120.6 1.7 5 120.56 122.75 121.27 .79 * C-N-CH1E (Pro) 122.6 5.0 4 122.03 123.78 122.76 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.20 122.04 120.79 .54 CH2G*-C-O (Gly) 120.8 2.1 5 119.64 120.38 120.16 .27 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.56 112.17 110.73 .59 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.02 112.23 110.15 1.06 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.24 113.46 110.51 1.19 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.71 114.52 110.24 1.59 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.93 114.00 112.23 1.57 N-CH1E-C (Pro) 111.8 2.5 4 110.66 113.41 111.97 .98 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.13 111.56 110.76 .41 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.99 112.55 111.30 .92 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.50 103.87 103.11 .49 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.15 113.91 110.44 1.23 +* ** ------------------------------------------------------------------------------------------------------------- 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_17 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] 102 90.3% Residues in additional allowed regions [a,b,l,p] 11 9.7% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 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 90.3 83.8 10.0 .6 Inside b. Omega angle st dev 122 2.8 6.0 3.0 -1.1 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.6 3.1 1.6 -1.0 Inside e. H-bond energy st dev 83 .9 .8 .2 .2 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 5.8 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 48 6.9 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 41 9.0 17.5 4.9 -1.8 BETTER d. Chi-1 pooled st dev 102 8.1 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 27 9.6 20.4 5.0 -2.2 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% 90.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .86 2 Residue-by-residue listing for refined_17 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.19 Chi1-chi2 distribution -.24 Chi1 only .00 Chi3 & chi4 .45 Omega .10 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths .03 Main-chain bond angles .50 ------ .31 ===== OVERALL AVERAGE .09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.