Residue-by-residue listing for refined_18 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -67.6 - - - - - - - 181.3 - 33.2 - 2 GLY 2 - - - - - - - - - - - 178.3 - - - 3 HIS 3 t B - 180.8 - - - - - - - - 183.0 - 34.0 - 4 HIS 4 T B - 197.4 - - - - - - - - 186.9 -.9 33.2 - * +* +* 5 HIS 5 T ~l - - -61.7 - - - - - - - 179.5 - 31.6 - ** ** 6 HIS 6 t b - 179.4 - - - - - - - - 174.2 -.6 31.9 - +* +* 7 HIS 7 B - 177.9 - - - - - - - - 181.0 -2.0 33.9 - 8 HIS 8 B - 182.6 - - - - - - - - 175.8 - 34.3 - 9 LEU 9 B - - -67.2 - - - - - - - 184.9 -.6 33.2 - +* +* 10 GLU 10 B - 185.5 - 179.1 - - - - - - 182.9 - 35.8 - 11 MET 11 b - 181.4 - 178.9 - - - - - - 178.7 - 33.3 - 12 ALA 12 B - - - - - - - - - - 180.9 -.9 33.9 - +* +* 13 SER 13 B - - -57.9 - - - - - - - 177.5 -.9 34.8 - +* +* 14 GLU 14 b - 181.8 - 179.6 - - - - - - 186.5 - 35.3 - * * 15 GLU 15 B 56.8 - - 171.1 - - - - - - 174.8 -1.3 35.8 - * * 16 GLY 16 S - - - - - - - - - - - 183.8 -1.5 - - 17 GLN 17 e B 51.5 - - 179.3 - - - - - - 180.6 - 28.6 - +* +* 18 VAL 18 E B 62.9 - - - - - - - - - 179.6 - 35.8 - Residue-by-residue listing for refined_18 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 ILE 19 E B - - -57.4 179.1 - - - - - - 180.5 -3.0 33.2 - * * 20 ALA 20 E B - - - - - - - - - - 176.8 - 34.1 - 21 CYS 21 E B - - -53.6 - - - - - - - 181.0 -2.0 35.9 - 22 HIS 22 A - - -59.2 - - - - - - - 182.6 -.6 33.6 - +* +* 23 THR 23 h B 58.1 - - - - - - - - - 174.7 - 35.6 - 24 VAL 24 H A 64.5 - - - - -73.8 -22.4 - - - 179.1 - 33.3 - +* +* 25 GLU 25 H A - 192.9 - - - -62.8 -51.2 - - - 179.1 - 35.9 - * * 26 THR 26 H A - - -54.9 - - -66.7 -32.7 - - - 177.6 - 34.5 - 27 TRP 27 H A - 168.4 - - - -53.3 -55.3 - - - 180.6 -1.4 33.7 - * * * 28 ASN 28 H A - 183.6 - - - -69.8 -40.4 - - - 182.4 -2.1 34.3 - 29 GLU 29 H A - 184.1 - 182.3 - -56.3 -48.8 - - - 181.2 -2.2 34.8 - 30 GLN 30 H A - - -71.5 - - -66.2 -37.5 - - - 178.5 -3.1 33.9 - * * 31 LEU 31 H A - - -67.0 181.2 - -66.9 -40.9 - - - 174.6 -1.5 34.4 - 32 GLN 32 H A - - -64.4 - - -62.2 -38.8 - - - 176.7 -2.6 33.1 - 33 LYS 33 H A - - -64.4 176.2 - -63.4 -45.8 - - - 178.9 -2.1 33.2 - 34 ALA 34 H A - - - - - -65.3 -43.6 - - - 180.7 -2.8 33.8 - * * 35 ASN 35 H A - 187.1 - - - -58.0 -54.5 - - - 181.0 -3.2 37.4 - * +* * +* 36 GLU 36 H A - 185.1 - - - -62.2 -39.8 - - - 183.2 -3.0 34.3 - * * 37 SER 37 h A - - -54.0 - - - - - - - 180.6 -2.3 34.8 - 38 LYS 38 T l - 189.6 - 188.6 - - - - - - 182.6 -1.3 33.9 - 39 THR 39 t B - - -52.5 - - - - - - - 180.5 -2.6 35.2 - 40 LEU 40 E B - 184.9 - 171.0 - - - - - - 183.5 -2.6 35.6 - 41 VAL 41 E B 58.9 - - - - - - - - - 178.5 -1.1 31.6 - * * 42 VAL 42 E B - 181.9 - - - - - - - - 182.0 -2.5 34.2 - 43 VAL 43 E B - 183.7 - - - - - - - - 177.9 -3.1 35.0 - * * 44 ASP 44 E B - 171.1 - - - - - - - - 178.1 -3.1 34.1 - * * 45 PHE 45 E B - - -63.0 - - - - - - - 186.1 -3.0 36.4 - * * * 46 THR 46 E B - 179.3 - - - - - - - - 175.4 -2.3 36.0 - 47 ALA 47 t B - - - - - - - - - - 183.1 - 33.7 - 48 SER 48 T A - 181.4 - - - - - - - - 180.6 - 33.5 - 49 TRP 49 T A 53.4 - - - - - - - - - 181.5 - 32.8 - 50 CYS 50 h B - 177.5 - 215.2 - - - 60.8 - 2.0 181.0 -1.7 34.2 - ** ** ** 51 GLY 51 H - - - - - - -64.2 -66.7 - - - 181.5 -.6 - - ** +* ** 52 PRO 52 H - - - - - -56.6 -56.6 -31.9 - - - 179.6 - 38.7 - * * 53 CYS 53 H A - - -54.6 - - -64.8 -40.1 60.8 - 2.0 180.7 - 35.5 - ** ** 54 ARG 54 H A - 182.8 - - - -70.9 -31.0 - - - 181.7 -1.4 35.2 - 55 PHE 55 H A - 177.7 - - - -77.2 -30.5 - - - 184.2 -1.6 34.3 - 56 ILE 56 H A - 191.2 - - - -87.4 -21.0 - - - 181.7 -1.8 33.9 - +* +* +* Residue-by-residue listing for refined_18 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 H A - - - - - -50.3 -45.2 - - - 178.4 -1.3 31.7 - * * 58 PRO 58 H - - - - - -53.1 -53.1 -33.0 - - - 181.3 - 38.4 - * * * * 59 PHE 59 H A - 184.0 - - - -73.7 -35.1 - - - 178.7 -1.3 33.6 - 60 PHE 60 H A - 182.0 - - - -67.4 -34.3 - - - 177.5 -1.1 34.8 - * * 61 ALA 61 H A - - - - - -68.6 -31.5 - - - 177.4 -1.9 33.8 - 62 ASP 62 H A - 176.4 - - - -68.8 -49.7 - - - 175.9 -1.1 35.5 - * * 63 LEU 63 H A - - -67.5 181.1 - -54.0 -35.9 - - - 180.4 -2.4 35.4 - 64 ALA 64 H A - - - - - -62.1 -40.1 - - - 178.4 -1.6 31.0 - 65 LYS 65 H A - - -71.2 - - -80.2 -25.0 - - - 186.1 -1.1 32.5 - * * * * * 66 LYS 66 H A - - -71.5 162.1 - -86.2 -29.2 - - - 176.8 -1.8 32.0 - +* +* 67 LEU 67 h B - - -74.7 - - - - - - - 182.7 -2.4 31.5 - 68 PRO 68 S - - - - - -80.4 - - - - - 185.0 - 37.3 - * * 69 ASN 69 e b - 182.1 - - - - - - - - 184.1 - 33.5 - 70 VAL 70 E B 63.3 - - - - - - - - - 171.5 -1.9 34.4 - * * 71 LEU 71 E B - 179.3 - - - - - - - - 176.5 -3.1 34.9 - * * 72 PHE 72 E B - - -62.1 - - - - - - - 181.9 -.9 33.6 - * * 73 LEU 73 E B - - -68.1 165.0 - - - - - - 177.5 -2.1 33.9 - 74 LYS 74 E B - - -67.9 - - - - - - - 175.3 -2.6 37.2 - 75 VAL 75 E B - 179.6 - - - - - - - - 179.6 -2.9 33.9 - * * 76 ASP 76 E B - 182.7 - - - - - - - - 184.9 -.5 33.4 - ** ** 77 THR 77 e A 53.9 - - - - - - - - - 178.7 -2.2 33.8 - 78 ASP 78 T A - 185.3 - - - - - - - - 174.3 - 34.9 - 79 GLU 79 T a - - -70.6 - - - - - - - 181.4 -.6 35.5 - +* +* 80 LEU 80 h b - - -67.6 - - - - - - - 181.0 -3.4 33.6 - +* +* 81 LYS 81 H A - - -60.9 181.6 - -68.6 -43.8 - - - 180.4 -1.9 33.4 - 82 SER 82 H A - - -58.4 - - -62.8 -34.4 - - - 177.1 - 33.2 - 83 VAL 83 H A - 179.1 - - - -66.3 -45.5 - - - 178.6 - 33.7 - 84 ALA 84 H A - - - - - -64.4 -31.5 - - - 179.1 -1.8 34.0 - 85 SER 85 H A - - -55.7 - - -75.1 -33.4 - - - 184.1 -2.1 35.1 - 86 ASP 86 H A - 182.5 - - - -76.9 -37.2 - - - 180.4 -1.9 34.3 - 87 TRP 87 h A - - -66.0 - - - - - - - 180.1 -2.3 32.7 - 88 ALA 88 T l - - - - - - - - - - 180.5 -.5 31.4 - +* +* 89 ILE 89 t b - - -64.1 182.0 - - - - - - 179.6 -1.8 32.2 - 90 GLN 90 A 67.1 - - - - - - - - - 179.8 -.7 33.6 - +* +* 91 ALA 91 S B - - - - - - - - - - 180.9 - 32.3 - 92 MET 92 S B - - -61.9 171.2 - - - - - - -.2 - 35.7 - 93 PRO 93 e cis - - - - - -89.2 - - - - - 177.8 - 39.5 - ** +* ** 94 THR 94 E B - - -59.0 - - - - - - - 178.6 -2.0 34.0 - 95 PHE 95 E B - - -64.5 - - - - - - - 179.9 -2.8 36.0 - * * Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 96 MET 96 E B - 175.3 - 179.0 - - - - - - 185.3 -3.0 33.2 - * * 97 PHE 97 E B - - -68.6 - - - - - - - 174.4 -2.9 36.3 - * * 98 LEU 98 E B - - -57.0 - - - - - - - 175.8 -2.9 35.0 - * * 99 LYS 99 E B - 175.5 - 173.0 - - - - - - 185.9 -2.9 32.0 - * * * 100 GLU 100 T l - - -53.9 181.8 - - - - - - 184.0 - 33.7 - 101 GLY 101 T - - - - - - - - - - - 179.9 - - - 102 LYS 102 E B - - -55.0 170.0 - - - - - - 181.7 -1.7 37.1 - 103 ILE 103 E B - - -62.1 171.7 - - - - - - 179.2 - 34.1 - 104 LEU 104 E a - - -63.8 188.8 - - - - - - 194.9 -2.3 36.3 - +** +** 105 ASP 105 E B - 168.8 - - - - - - - - 183.0 -2.6 34.9 - 106 LYS 106 E B - 193.6 - 184.7 - - - - - - 179.6 - 35.0 - 107 VAL 107 E B - 183.8 - - - - - - - - 180.2 -3.4 35.8 - +* +* 108 VAL 108 E B 66.1 - - - - - - - - - 183.5 -.6 32.6 - +* +* 109 GLY 109 e - - - - - - - - - - - 182.8 -2.2 - - 110 ALA 110 B - - - - - - - - - - 168.9 -.6 34.3 - +* +* +* 111 LYS 111 h B - - -62.1 183.5 - - - - - - 184.4 -.7 34.4 - +* +* 112 LYS 112 H A - 189.6 - - - -55.0 -50.5 - - - 182.7 - 34.8 - 113 ASP 113 H A - 183.1 - - - -67.3 -40.2 - - - 179.4 - 33.2 - 114 GLU 114 H A - - -63.8 - - -66.3 -36.8 - - - 179.6 - 33.6 - 115 LEU 115 H A - 187.3 - - - -65.3 -47.2 - - - 177.0 -2.7 34.9 - 116 GLN 116 H A - - -59.1 - - -59.4 -37.1 - - - 179.0 -2.3 34.2 - 117 SER 117 H A - 183.6 - - - -70.7 -30.7 - - - 178.4 -2.2 33.6 - 118 THR 118 H A - - -56.7 - - -73.0 -29.6 - - - 173.9 -1.9 33.3 - * * 119 ILE 119 H A - - -60.8 178.2 - -60.8 -40.8 - - - 177.3 -1.7 33.7 - 120 ALA 120 H A - - - - - -65.0 -30.5 - - - 177.0 -1.4 33.0 - 121 LYS 121 H A - 186.7 - 186.5 - -57.7 -44.3 - - - 179.8 -1.0 36.2 - * * 122 HIS 122 H A - - -73.6 - - -70.4 -36.6 - - - 177.7 -1.5 32.6 - 123 LEU 123 h B - - -83.6 - - - - - - - 183.1 -1.6 33.1 - * * 124 ALA 124 - - - - - - - - - - - - -1.1 34.2 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * ** ** +* ** ** +** ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.7 182.4 -63.1 179.3 -69.8 -66.0 -38.7 60.8 - 2.0 180.1 -1.9 34.2 ** ** Standard deviations: 5.4 5.9 6.6 9.6 17.7 8.1 9.0 .0 - .0 3.5 .8 1.6 Numbers of values: 11 45 46 28 4 46 46 2 0 2 122 88 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_18 Page 5 ---------------------------------------- KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_18 Page 6 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - 1.230 1.502 1.535 1.467 - 116.20 120.45 110.63 110.27 111.75 123.34 * * 2 GLY 2 1.307 1.242 1.498 - 1.434 121.35 116.82 120.24 - 110.38 - 122.95 +* * +* 3 HIS 3 1.293 1.231 1.500 1.537 1.432 121.60 116.15 120.83 111.30 108.28 110.80 123.01 +** * * * +** 4 HIS 4 1.304 1.232 1.532 1.533 1.430 120.65 116.82 119.38 112.91 108.43 110.10 123.80 +* * * +* 5 HIS 5 1.348 1.235 1.511 1.557 1.494 124.71 115.51 121.39 110.04 109.41 114.82 123.09 * * +* +* +** +** 6 HIS 6 1.324 1.231 1.519 1.547 1.435 121.73 114.39 121.83 111.78 110.84 112.44 123.63 * * * 7 HIS 7 1.288 1.229 1.495 1.545 1.421 123.37 116.72 120.11 110.81 106.94 112.00 123.12 +** * +* +* +** 8 HIS 8 1.291 1.232 1.510 1.543 1.431 121.24 116.01 120.53 110.65 109.48 110.71 123.42 +** * +** 9 LEU 9 1.306 1.235 1.504 1.549 1.438 121.33 116.34 120.50 110.90 107.93 112.52 123.15 +* * * * * +* 10 GLU 10 1.288 1.229 1.511 1.527 1.428 121.93 116.53 120.54 111.36 108.31 107.83 122.91 +** +* * +* +** 11 MET 11 1.307 1.239 1.515 1.534 1.440 121.05 115.62 121.02 111.33 110.96 110.69 123.30 +* +* Residue-by-residue listing for refined_18 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.310 1.234 1.512 1.520 1.438 121.87 116.12 121.06 110.89 109.43 110.69 122.75 * * * 13 SER 13 1.291 1.237 1.523 1.528 1.430 121.77 115.85 120.50 110.65 110.45 109.48 123.64 +** * +** 14 GLU 14 1.311 1.230 1.535 1.538 1.440 123.74 115.91 121.09 111.83 107.86 108.18 122.87 * * * * * 15 GLU 15 1.321 1.242 1.531 1.536 1.450 121.87 116.44 121.16 108.56 112.42 109.42 122.40 16 GLY 16 1.309 1.236 1.508 - 1.444 120.86 117.53 120.11 - 114.23 - 122.36 * * 17 GLN 17 1.303 1.234 1.484 1.520 1.429 119.92 112.72 122.57 112.70 114.30 114.06 124.70 +* +* +* +* * * * ** * ** 18 VAL 18 1.276 1.238 1.528 1.547 1.411 124.24 117.73 120.13 110.85 108.98 108.43 122.11 +*** ** * +* +*** 19 ILE 19 1.314 1.221 1.527 1.555 1.444 119.90 117.26 120.48 111.67 109.48 111.18 122.20 * * * 20 ALA 20 1.304 1.234 1.520 1.522 1.444 121.01 116.57 120.66 110.44 110.79 110.41 122.76 +* +* 21 CYS 21 1.309 1.230 1.509 1.514 1.425 121.67 116.95 120.28 109.16 107.77 109.88 122.76 * +* * +* 22 HIS 22 1.304 1.235 1.517 1.546 1.450 120.74 116.16 120.96 110.32 110.26 111.65 122.87 +* +* 23 THR 23 1.324 1.249 1.514 1.557 1.446 121.81 116.22 120.55 107.33 109.94 111.96 123.21 24 VAL 24 1.324 1.235 1.544 1.570 1.449 121.63 115.41 121.45 110.76 108.69 112.20 123.13 * * 25 GLU 25 1.336 1.244 1.527 1.530 1.450 122.76 115.36 121.18 109.18 108.75 109.53 123.43 26 THR 26 1.332 1.227 1.527 1.538 1.447 122.48 115.62 120.72 110.33 110.33 110.09 123.65 27 TRP 27 1.326 1.230 1.533 1.541 1.451 122.83 116.79 120.49 111.52 111.49 109.66 122.68 28 ASN 28 1.319 1.237 1.519 1.528 1.460 120.59 115.35 120.85 109.87 110.22 110.73 123.75 29 GLU 29 1.330 1.236 1.532 1.534 1.467 123.09 116.70 120.28 109.39 111.50 110.07 122.99 30 GLN 30 1.332 1.230 1.510 1.497 1.431 122.72 116.59 120.73 110.80 112.26 109.71 122.67 +* * +* 31 LEU 31 1.316 1.220 1.508 1.485 1.407 121.96 116.39 120.50 110.83 111.00 109.41 123.10 ** +** +** 32 GLN 32 1.312 1.224 1.510 1.522 1.452 121.97 116.42 120.30 110.49 110.60 111.74 123.28 * * 33 LYS 33 1.319 1.225 1.512 1.525 1.451 121.62 116.78 120.24 110.69 110.58 111.45 122.96 34 ALA 34 1.331 1.225 1.523 1.523 1.451 121.17 115.40 120.73 110.63 110.26 110.65 123.83 35 ASN 35 1.328 1.232 1.501 1.529 1.473 123.79 114.47 121.63 107.22 110.10 108.90 123.88 * * +* +* 36 GLU 36 1.306 1.238 1.548 1.534 1.459 122.91 116.68 120.88 110.76 111.71 109.42 122.40 +* * +* 37 SER 37 1.319 1.242 1.546 1.521 1.448 121.76 117.05 119.80 109.97 112.45 109.16 123.15 38 LYS 38 1.363 1.232 1.551 1.516 1.446 124.08 115.37 122.43 111.64 109.85 109.53 122.14 ** * * ** 39 THR 39 1.297 1.237 1.519 1.523 1.422 122.32 114.91 121.65 109.56 109.81 110.18 123.44 ** +* ** 40 LEU 40 1.273 1.214 1.532 1.566 1.433 123.08 118.57 119.72 112.70 105.73 107.80 121.69 **** +* * * * +* +* **** 41 VAL 41 1.302 1.234 1.531 1.562 1.440 119.78 115.55 121.28 112.40 112.47 111.57 123.14 +* * * +* 42 VAL 42 1.311 1.242 1.512 1.542 1.441 122.35 116.11 120.91 109.19 108.60 112.39 122.96 * * 43 VAL 43 1.295 1.237 1.514 1.538 1.432 121.43 115.63 120.53 108.82 110.33 111.16 123.83 ** * ** Residue-by-residue listing for refined_18 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.303 1.249 1.520 1.532 1.445 123.23 115.85 120.90 110.97 110.15 110.18 123.15 +* +* 45 PHE 45 1.317 1.238 1.516 1.521 1.429 122.36 116.55 120.36 108.65 108.46 109.51 123.01 +* +* 46 THR 46 1.305 1.220 1.534 1.555 1.436 121.38 116.17 120.70 109.75 110.76 108.68 123.13 +* * +* +* 47 ALA 47 1.316 1.241 1.517 1.516 1.442 123.49 117.10 119.94 110.69 108.20 111.48 122.95 * * 48 SER 48 1.313 1.227 1.539 1.538 1.456 122.47 117.15 120.34 111.01 112.16 110.18 122.51 * * 49 TRP 49 1.320 1.232 1.526 1.540 1.464 121.42 116.75 120.92 111.05 112.37 111.01 122.33 50 CYS 50 1.307 1.240 1.529 1.517 1.437 121.24 116.01 120.70 110.89 111.15 109.63 123.28 +* * +* 51 GLY 51 1.327 1.235 1.527 - 1.460 122.30 118.87 119.64 - 113.84 - 121.49 * * 52 PRO 52 1.367 1.224 1.524 1.532 1.479 122.70 115.78 121.16 109.99 111.90 103.68 123.04 +* +* 53 CYS 53 1.313 1.227 1.533 1.517 1.454 122.71 115.90 121.36 109.42 110.48 109.28 122.72 * * 54 ARG 54 1.321 1.232 1.534 1.539 1.448 122.13 115.24 121.31 110.69 109.39 109.07 123.42 55 PHE 55 1.319 1.232 1.542 1.543 1.453 123.24 117.21 120.60 110.92 112.29 109.22 122.17 56 ILE 56 1.318 1.242 1.551 1.567 1.463 120.91 115.59 121.16 110.43 110.92 110.80 123.19 * * * 57 ALA 57 1.332 1.234 1.563 1.531 1.474 123.60 120.43 119.03 111.31 114.79 110.95 120.54 +* * ** * * +* ** 58 PRO 58 1.383 1.233 1.543 1.531 1.477 122.21 117.19 120.44 110.24 113.50 103.51 122.35 +** +** 59 PHE 59 1.329 1.226 1.536 1.541 1.462 121.10 115.73 121.24 111.19 109.95 110.62 122.99 60 PHE 60 1.316 1.226 1.537 1.542 1.462 123.03 116.07 121.06 111.69 109.61 108.45 122.84 * * 61 ALA 61 1.328 1.239 1.536 1.523 1.466 121.89 115.57 121.50 110.68 110.43 110.36 122.92 62 ASP 62 1.315 1.236 1.489 1.520 1.475 123.13 114.10 121.46 110.06 108.92 109.23 124.41 +* * +* 63 LEU 63 1.305 1.230 1.525 1.522 1.428 123.66 116.01 120.79 110.45 110.79 108.57 123.17 +* +* * * +* 64 ALA 64 1.317 1.225 1.522 1.528 1.437 121.78 118.03 120.00 112.58 112.73 111.82 121.97 * * * 65 LYS 65 1.321 1.231 1.527 1.531 1.464 119.28 116.17 120.70 110.35 112.25 112.13 123.12 * * 66 LYS 66 1.313 1.239 1.522 1.508 1.450 122.09 118.11 119.91 112.74 114.78 109.19 121.97 * * * * * 67 LEU 67 1.309 1.228 1.534 1.543 1.442 119.56 117.92 120.41 112.62 110.20 112.24 121.62 * * * * * 68 PRO 68 1.345 1.241 1.547 1.529 1.460 122.33 117.14 120.63 111.36 114.91 103.61 122.19 * * * 69 ASN 69 1.327 1.237 1.509 1.536 1.468 122.07 113.84 122.51 111.34 109.10 111.00 123.46 * * * 70 VAL 70 1.286 1.243 1.541 1.522 1.417 123.14 115.37 121.47 110.29 112.83 109.50 122.97 *** ** * *** 71 LEU 71 1.294 1.229 1.521 1.539 1.428 122.61 117.24 120.25 110.05 107.48 110.88 122.45 ** +* * ** 72 PHE 72 1.299 1.237 1.492 1.517 1.444 120.84 116.19 120.47 109.36 109.03 112.82 123.34 ** +* * ** 73 LEU 73 1.290 1.231 1.516 1.516 1.435 122.05 115.48 121.01 111.26 112.16 109.34 123.50 +** * +** Residue-by-residue listing for refined_18 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 74 LYS 74 1.310 1.242 1.496 1.522 1.417 123.75 116.50 120.44 107.58 108.72 109.51 123.05 * * ** * * ** 75 VAL 75 1.289 1.235 1.505 1.559 1.428 121.01 115.94 120.81 110.08 108.05 112.42 123.23 +** +* * +** 76 ASP 76 1.300 1.227 1.506 1.512 1.431 121.02 116.00 120.74 111.29 109.22 111.09 123.25 ** * ** 77 THR 77 1.306 1.230 1.524 1.534 1.448 123.07 116.96 120.47 110.00 113.16 110.56 122.56 +* +* 78 ASP 78 1.316 1.230 1.507 1.519 1.452 120.99 114.22 121.81 110.16 107.57 110.33 123.96 * * 79 GLU 79 1.305 1.232 1.523 1.507 1.416 123.54 116.39 120.87 110.19 110.75 108.64 122.73 +* * ** * * ** 80 LEU 80 1.315 1.244 1.528 1.535 1.415 122.61 115.48 121.44 110.76 111.24 110.92 123.06 ** ** 81 LYS 81 1.316 1.233 1.519 1.525 1.452 122.37 116.52 120.68 110.43 111.50 111.13 122.80 82 SER 82 1.322 1.230 1.528 1.514 1.449 121.72 116.55 120.53 111.04 111.47 110.65 122.90 83 VAL 83 1.329 1.230 1.534 1.559 1.462 121.63 116.00 121.04 110.40 109.62 111.55 122.90 84 ALA 84 1.327 1.230 1.532 1.520 1.465 122.23 115.89 121.29 110.58 111.06 110.10 122.81 85 SER 85 1.311 1.229 1.536 1.531 1.443 121.93 116.02 121.12 110.13 110.25 109.36 122.83 * * 86 ASP 86 1.326 1.229 1.525 1.536 1.463 122.05 116.81 120.86 110.08 111.79 110.15 122.29 87 TRP 87 1.314 1.242 1.515 1.515 1.453 121.37 115.58 120.38 110.56 112.59 111.45 124.03 * * 88 ALA 88 1.334 1.241 1.518 1.525 1.456 123.96 114.93 121.72 111.82 111.85 112.24 123.23 * * * 89 ILE 89 1.302 1.239 1.520 1.562 1.426 122.26 114.53 121.84 112.62 110.40 111.55 123.46 +* +* +* +* 90 GLN 90 1.314 1.235 1.530 1.561 1.433 123.29 116.55 121.10 110.11 110.95 111.78 122.34 * +* * +* 91 ALA 91 1.312 1.231 1.510 1.528 1.444 121.12 115.41 121.53 111.66 110.84 111.80 123.05 * * 92 MET 92 1.286 1.235 1.511 1.521 1.435 122.21 118.80 119.65 109.89 108.62 109.24 121.55 *** * * *** 93 PRO 93 1.332 1.234 1.525 1.520 1.458 124.43 116.78 121.03 110.05 111.57 102.61 122.13 94 THR 94 1.278 1.229 1.508 1.516 1.418 120.35 115.97 120.79 110.34 110.04 111.06 123.24 +*** ** +*** 95 PHE 95 1.301 1.225 1.493 1.520 1.403 122.24 116.24 120.78 109.05 107.99 110.16 122.98 ** +* +** * +** 96 MET 96 1.272 1.232 1.509 1.527 1.424 121.33 114.98 121.30 113.23 109.07 109.63 123.70 **** +* +* **** 97 PHE 97 1.294 1.251 1.501 1.519 1.410 123.88 115.74 121.44 108.61 111.53 109.12 122.83 +** * * +** * +** 98 LEU 98 1.282 1.226 1.517 1.554 1.414 120.92 117.21 120.46 107.83 107.12 113.31 122.32 *** * ** * * +* *** 99 LYS 99 1.280 1.228 1.474 1.521 1.429 121.13 114.71 120.62 111.91 108.46 112.97 124.63 +*** ** +* * * +*** 100 GLU 100 1.317 1.214 1.526 1.518 1.458 125.09 116.39 120.53 108.30 110.03 113.13 123.08 +* +* +* 101 GLY 101 1.318 1.233 1.523 - 1.453 121.31 115.89 120.86 - 111.79 - 123.24 102 LYS 102 1.322 1.233 1.527 1.538 1.458 122.81 117.23 119.83 108.13 107.79 109.05 122.94 * * * 103 ILE 103 1.316 1.229 1.520 1.559 1.464 121.87 116.44 120.87 109.91 110.63 111.17 122.69 104 LEU 104 1.315 1.237 1.496 1.530 1.431 121.05 115.42 121.28 106.43 111.65 111.24 123.29 * * +* +* Residue-by-residue listing for refined_18 Page 10 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 105 ASP 105 1.303 1.226 1.488 1.520 1.430 121.01 115.40 120.90 112.23 111.34 107.54 123.67 +* +* * * +* +* 106 LYS 106 1.274 1.233 1.521 1.540 1.429 122.04 116.61 120.41 109.81 109.00 110.54 122.97 +*** +* +*** 107 VAL 107 1.305 1.231 1.499 1.550 1.446 122.19 116.75 120.40 107.99 108.09 111.56 122.85 +* * * +* 108 VAL 108 1.297 1.239 1.550 1.575 1.426 120.50 116.20 121.48 113.47 109.19 110.52 122.29 ** * * +* +* ** 109 GLY 109 1.316 1.236 1.515 - 1.445 121.08 117.53 120.17 - 110.14 - 122.30 110 ALA 110 1.310 1.233 1.504 1.513 1.442 120.58 115.32 121.27 109.20 112.40 110.85 123.38 * * 111 LYS 111 1.299 1.238 1.498 1.521 1.416 123.19 116.63 119.59 110.10 105.93 112.01 123.77 ** * ** +* ** 112 LYS 112 1.310 1.224 1.526 1.542 1.441 123.24 116.30 120.77 112.15 110.54 107.91 122.86 * * +* +* 113 ASP 113 1.316 1.227 1.524 1.519 1.462 121.82 116.91 120.39 110.66 111.96 110.79 122.67 114 GLU 114 1.329 1.229 1.511 1.525 1.467 121.18 116.52 120.54 109.05 110.91 112.38 122.94 * * 115 LEU 115 1.317 1.227 1.505 1.509 1.446 121.44 115.10 121.22 109.44 109.13 110.57 123.67 * * 116 GLN 116 1.312 1.236 1.527 1.532 1.466 122.16 116.13 121.15 109.68 110.28 111.10 122.70 * * 117 SER 117 1.319 1.226 1.539 1.537 1.442 121.60 116.32 121.34 111.54 109.70 110.37 122.32 118 THR 118 1.312 1.234 1.537 1.532 1.440 122.05 116.71 120.96 110.93 110.34 111.25 122.33 * * 119 ILE 119 1.325 1.224 1.535 1.556 1.450 120.61 115.25 121.39 110.94 108.19 111.49 123.22 * * 120 ALA 120 1.326 1.225 1.535 1.519 1.460 123.09 116.62 120.54 111.18 111.23 110.81 122.83 121 LYS 121 1.337 1.230 1.519 1.510 1.470 122.26 114.77 121.50 107.66 109.13 110.15 123.72 * * 122 HIS 122 1.321 1.239 1.522 1.526 1.444 123.02 117.32 120.19 111.12 112.64 111.17 122.50 123 LEU 123 1.324 1.234 1.519 1.515 1.412 121.76 115.40 121.42 111.93 110.88 110.33 123.16 ** ** 124 ALA 124 1.303 - 1.504 1.526 1.436 122.98 - - 110.73 108.81 110.68 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** ** +** +* ** * +* +* +** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 11 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 119 1.272 1.363 1.311 .016 **** ** * C-N (Pro) 1.341 .016 4 1.332 1.383 1.357 .019 +** C-O C-O 1.231 .020 123 1.214 1.251 1.233 .006 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.474 1.563 1.521 .016 ** +* CH2G*-C (Gly) 1.516 .018 5 1.498 1.527 1.514 .010 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.513 1.531 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.516 1.575 1.549 .016 * CH1E-CH2E (the rest) 1.530 .020 84 1.485 1.566 1.529 .014 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.403 1.494 1.443 .017 +** +* NH1-CH2G* (Gly) 1.451 .016 5 1.434 1.460 1.447 .009 * N-CH1E (Pro) 1.466 .015 4 1.458 1.479 1.468 .010 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 12 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 114 112.72 120.43 116.15 1.02 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.89 118.87 117.33 .98 * CH1E-C-N (Pro) 116.9 1.5 4 115.78 117.19 116.72 .56 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.54 124.70 122.98 .62 +* * O-C-N (Pro) 122.0 1.4 4 122.13 123.04 122.43 .36 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.28 125.09 122.06 1.10 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.86 122.30 121.38 .49 C-N-CH1E (Pro) 122.6 5.0 4 122.21 124.43 122.92 .89 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.03 122.57 120.83 .60 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.64 120.86 120.20 .39 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.20 112.58 110.95 .78 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.33 113.47 110.37 1.38 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 106.43 113.23 110.45 1.32 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.73 114.79 110.21 1.71 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.14 114.23 112.08 1.70 N-CH1E-C (Pro) 111.8 2.5 4 111.57 114.91 112.97 1.34 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.10 112.24 110.99 .62 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.43 112.42 110.97 1.05 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.61 103.68 103.35 .43 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.54 114.82 110.42 1.46 +* +** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_18 Page 13 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 101 89.4% Residues in additional allowed regions [a,b,l,p] 11 9.7% Residues in generously allowed regions [~a,~b,~l,~p] 1 .9% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 113 89.4 83.8 10.0 .6 Inside b. Omega angle st dev 122 3.5 6.0 3.0 -.8 Inside 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 88 .8 .8 .2 .0 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 11 5.4 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 45 5.9 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 46 6.6 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 6.8 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 28 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% 89.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .83 2 Residue-by-residue listing for refined_18 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.16 Chi1-chi2 distribution .02 Chi1 only -.06 Chi3 & chi4 .36 Omega .04 ------ .00 ===== Main-chain covalent forces:- Main-chain bond lengths -.04 Main-chain bond angles .45 ------ .24 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.