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 GLU 1 - - - -64.4 - - - - - - - 181.1 - 33.7 - 2 ALA 2 B - - - - - - - - - - 178.4 - 33.9 - 3 GLU 3 B 56.7 - - - - - - - - - 184.2 - 31.5 - 4 VAL 4 B 66.3 - - - - - - - - - 184.1 - 32.6 - 5 HIS 5 S A - 188.7 - - - - - - - - 175.5 - 33.3 - 6 ASN 6 S A - - -67.6 - - - - - - - 175.3 - 32.0 - 7 GLN 7 S B - - -59.2 176.6 - - - - - - 182.5 - 35.4 - 8 LEU 8 E B - - -63.6 - - - - - - - 183.0 -2.4 31.5 - 9 GLU 9 E B - - -65.5 - - - - - - - 178.6 -.9 33.4 - +* +* 10 ILE 10 E B - - -55.4 180.4 - - - - - - 175.3 -2.9 35.7 - * * 11 LYS 11 E B 55.8 - - 162.5 - - - - - - 182.2 -2.9 32.5 - * * 12 PHE 12 E B - - -59.0 - - - - - - - 175.5 - 35.3 - 13 ARG 13 E B - - -59.4 - - - - - - - 179.6 -3.3 36.1 - +* +* 14 LEU 14 t B - - -64.5 - - - - - - - 180.1 -3.2 34.2 - +* +* 15 THR 15 T A 50.2 - - - - - - - - - 180.1 - 33.8 - 16 ASP 16 T A - 177.4 - - - - - - - - 178.9 - 36.0 - 17 GLY 17 t - - - - - - - - - - - 177.2 -1.6 - - 18 SER 18 B 43.7 - - - - - - - - - 180.3 - 34.3 - * * 19 ASP 19 B B 74.4 - - - - - - - - - 177.9 - 33.7 - 20 ILE 20 B - - -56.9 179.8 - - - - - - 177.4 -2.6 35.2 - 21 GLY 21 - - - - - - - - - - - 184.8 - - - 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 PRO 22 - - - - - -58.0 - - - - - 183.0 - 37.6 - * * 23 LYS 23 E B - 191.1 - - - - - - - - 183.2 -2.9 37.5 - * * * 24 ALA 24 E B - - - - - - - - - - 180.2 - 33.3 - 25 PHE 25 E B - - -54.5 - - - - - - - 170.4 -3.6 36.4 - +* ** ** 26 PRO 26 t - - - - - -62.7 - - - - - 176.5 - 39.5 - +* +* 27 ASP 27 T A - - -69.2 - - - - - - - 184.6 - 36.0 - 28 ALA 28 T A - - - - - - - - - - 178.5 - 33.4 - 29 THR 29 t B - - -59.1 - - - - - - - 182.3 -1.8 34.1 - 30 THR 30 h B 56.2 - - - - - - - - - 177.2 - 34.9 - 31 VAL 31 H A - 178.4 - - - -63.6 -30.7 - - - 175.3 -3.1 34.3 - * * 32 SER 32 H A - 183.7 - - - -61.6 -42.0 - - - 179.6 -2.1 34.5 - 33 ALA 33 H A - - - - - -66.7 -31.1 - - - 171.4 - 32.5 - * * 34 LEU 34 H A - - -83.5 - - -56.1 -50.3 - - - 180.2 -1.3 34.8 - * * 35 LYS 35 H A - - -63.0 178.6 - -66.0 -41.3 - - - 175.8 -1.9 32.1 - 36 GLU 36 H A - - -61.5 - - -56.5 -40.3 - - - 176.6 -2.8 35.1 - 37 THR 37 H A - - -59.6 - - -63.9 -46.8 - - - 180.3 -2.4 34.0 - 38 VAL 38 H A - 178.5 - - - -57.6 -48.3 - - - 181.2 -2.4 34.0 - 39 ILE 39 H A - - -54.4 173.4 - -60.3 -38.1 - - - 181.9 -3.0 34.8 - * * 40 SER 40 H A - - -54.3 - - -76.0 -40.8 - - - 184.4 -1.8 34.7 - 41 GLU 41 H A - - -57.3 - - -78.0 -29.2 - - - 179.3 -3.0 34.6 - * * * 42 TRP 42 h B - 194.4 - - - - - - - - 181.9 -2.4 35.5 - 43 PRO 43 t - - - - - -37.1 - - - - - 179.4 - 39.2 - +** +* +** 44 ARG 44 T A - - -69.2 - - - - - - - 183.6 - 33.8 - 45 GLU 45 T A - 186.5 - 187.3 - - - - - - 190.4 - 36.6 - +* +* 46 LYS 46 t b 77.2 - - - - - - - - - 182.6 -1.0 30.0 - * * * 47 GLU 47 b 62.1 - - 186.1 - - - - - - 177.4 - 36.4 - 48 ASN 48 S a - - -71.2 - - - - - - - 178.2 - 33.7 - 49 GLY 49 S - - - - - - - - - - - 173.8 - - - * * 50 PRO 50 S - - - - - -57.4 - - - - - 178.8 - 40.4 - +* +* 51 LYS 51 a 49.2 - - 184.9 - - - - - - 174.9 -.8 29.6 - +* * +* 52 THR 52 g B 55.1 - - - - - - - - - 180.4 - 30.8 - 53 VAL 53 G A 60.6 - - - - - - - - - 184.9 - 33.5 - 54 LYS 54 G A - - -57.9 - - - - - - - 176.5 - 33.0 - 55 GLU 55 e a 52.1 - - - - - - - - - 175.9 -1.6 27.7 - +* +* 56 VAL 56 E B 56.7 - - - - - - - - - 180.8 -1.1 32.1 - * * 57 LYS 57 E B - 183.8 - 179.8 - - - - - - 187.3 -2.5 33.8 - * * 58 LEU 58 E B - 192.5 - - - - - - - - 177.6 - 35.2 - 59 ILE 59 E B - - -63.7 183.6 - - - - - - 179.6 -2.5 33.7 - 60 SER 60 E B - 187.7 - - - - - - - - 178.9 -2.4 35.1 - Residue-by-residue listing for refined_18 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 61 ALA 61 e l - - - - - - - - - - 180.1 -.5 32.9 - +* +* 62 GLY 62 T - - - - - - - - - - - 179.9 - - - 63 LYS 63 E B - 184.6 - 179.3 - - - - - - 180.4 -1.5 34.6 - 64 VAL 64 E B - 183.0 - - - - - - - - 182.0 - 34.6 - 65 LEU 65 e B - - -70.7 - - - - - - - 176.4 -2.8 32.8 - * * 66 GLU 66 t B - 191.1 - - - - - - - - 187.5 -.7 34.3 - * +* +* 67 ASN 67 T A - - -60.0 - - - - - - - 186.0 - 35.0 - * * 68 SER 68 T A - - -48.4 - - - - - - - 185.1 - 34.9 - * * 69 LYS 69 t B - - -66.6 - - - - - - - 180.8 -2.1 33.9 - 70 THR 70 h B 53.5 - - - - - - - - - 178.4 - 35.3 - 71 VAL 71 H A - 178.8 - - - -58.8 -47.0 - - - 182.3 -2.4 35.1 - 72 LYS 72 H A - 179.5 - 180.5 - -55.8 -33.5 - - - 183.6 -2.2 34.3 - 73 ASP 73 H A - 185.3 - - - -63.4 -36.8 - - - 182.6 - 33.8 - 74 TYR 74 H A - - -62.7 - - -98.4 -18.2 - - - 182.5 -1.0 34.8 - +** +* * +** 75 ARG 75 h B - 189.0 - 180.6 - - - - - - 173.5 -1.9 35.5 - * * 76 SER 76 B - - -50.3 - - - - - - - 179.9 - 37.2 - * * 77 PRO 77 - - - - - -65.8 - - - - - 180.8 - 38.1 - * * 78 VAL 78 S b - 182.7 - - - - - - - - 175.3 - 31.9 - 79 SER 79 B - - -53.8 - - - - - - - 179.1 -2.0 35.8 - 80 ASN 80 B - 180.6 - - - - - - - - 177.2 - 32.3 - 81 LEU 81 b 62.8 - - 172.6 - - - - - - 183.5 -1.2 34.2 - * * 82 ALA 82 S B - - - - - - - - - - 180.9 - 32.9 - 83 GLY 83 S - - - - - - - - - - - 183.6 -.5 - - ** ** 84 ALA 84 e B - - - - - - - - - - 173.2 - 34.3 - * * 85 VAL 85 E B - 182.7 - - - - - - - - 178.5 -1.1 34.8 - * * 86 THR 86 E B - - -50.6 - - - - - - - 180.0 -2.6 34.0 - * * 87 THR 87 E B - - -55.3 - - - - - - - 180.4 - 35.1 - 88 MET 88 E B - - -63.3 181.5 - - - - - - 181.0 -2.6 33.7 - 89 HIS 89 E B - 184.3 - - - - - - - - 179.8 -3.5 33.7 - +* +* 90 VAL 90 E B - 177.8 - - - - - - - - 178.4 -3.4 34.2 - +* +* 91 ILE 91 E B - - -68.1 181.1 - - - - - - 178.2 -3.0 33.8 - * * 92 ILE 92 E B - - -70.7 - - - - - - - 180.9 -.6 34.8 - +* +* 93 GLN 93 e B - - -59.7 177.8 - - - - - - 178.4 -2.7 34.8 - 94 ALA 94 B - - - - - - - - - - 180.9 -.8 34.3 - +* +* 95 PRO 95 - - - - - -76.0 - - - - - 178.0 - 38.8 - * * 96 VAL 96 B - 181.0 - - - - - - - - 183.0 - 34.6 - 97 THR 97 S b - - -53.5 - - - - - - - 175.9 - 31.7 - Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 98 GLU 98 b - 177.5 - 188.2 - - - - - - 187.4 -1.8 35.4 - * * 99 LYS 99 b 59.8 - - 182.3 - - - - - - 171.3 - 28.1 - * +* +* 100 GLU 100 b - 186.4 - - - - - - - - 186.7 -1.8 32.6 - * * 101 LYS 101 - - 182.0 - - - - - - - - - -1.5 35.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * +** +** +* +* ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.4 184.0 -61.3 179.8 -59.5 -65.5 -38.3 - - - 179.9 -2.1 34.3 Standard deviations: 8.6 4.9 7.1 5.8 12.9 11.3 8.7 - - - 3.7 .9 2.1 Numbers of values: 17 27 38 20 6 15 15 0 0 0 100 53 96 0 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 5 ---------------------------------------- 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 GLU 1 - 1.239 1.515 1.552 1.469 - 117.16 119.90 110.19 109.18 111.86 122.93 * * 2 ALA 2 1.322 1.237 1.518 1.519 1.445 121.28 115.51 120.99 110.57 111.16 110.42 123.49 3 GLU 3 1.305 1.235 1.518 1.562 1.434 124.29 117.61 119.69 112.18 108.62 113.51 122.69 +* +* * * * +* +* 4 VAL 4 1.319 1.226 1.531 1.553 1.455 120.59 116.16 120.94 111.15 110.88 111.89 122.90 5 HIS 5 1.315 1.227 1.543 1.551 1.470 122.36 116.31 121.56 111.89 111.06 109.96 122.13 * * 6 ASN 6 1.327 1.231 1.504 1.542 1.469 120.58 115.00 121.45 110.50 109.80 113.70 123.55 +* +* 7 GLN 7 1.308 1.228 1.511 1.523 1.427 123.15 118.30 119.26 110.86 106.11 109.50 122.43 * +* * +* +* 8 LEU 8 1.295 1.220 1.505 1.521 1.445 119.83 116.83 120.55 111.05 112.38 112.84 122.61 ** * * ** 9 GLU 9 1.312 1.242 1.506 1.529 1.430 120.19 114.18 122.17 108.18 111.73 113.48 123.65 * * * * +* +* 10 ILE 10 1.293 1.235 1.520 1.565 1.427 123.31 117.06 120.09 108.88 108.21 110.98 122.82 +** +* * +** 11 LYS 11 1.307 1.242 1.506 1.533 1.439 120.98 116.02 120.74 109.26 109.74 114.33 123.24 +* ** ** 12 PHE 12 1.294 1.222 1.513 1.525 1.435 121.54 116.56 120.29 109.16 110.64 110.05 123.13 ** * ** Residue-by-residue listing for refined_18 Page 6 ---------------------------------------- ................................................................................................................................... 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 ARG 13 1.308 1.226 1.510 1.532 1.448 122.33 117.41 119.79 107.89 107.97 110.93 122.80 +* * * +* 14 LEU 14 1.297 1.235 1.522 1.540 1.446 121.72 116.87 120.27 109.62 110.03 111.45 122.84 ** ** 15 THR 15 1.325 1.232 1.528 1.543 1.461 122.41 114.80 121.50 110.20 111.34 110.86 123.64 16 ASP 16 1.310 1.227 1.533 1.540 1.458 123.77 115.85 121.45 110.10 110.63 108.08 122.68 * * * * 17 GLY 17 1.316 1.227 1.509 - 1.444 121.05 115.84 121.14 - 112.03 - 123.02 18 SER 18 1.293 1.236 1.518 1.537 1.424 122.42 118.68 119.40 113.12 108.02 108.48 121.83 +** +* * +* * * +** 19 ASP 19 1.314 1.239 1.505 1.526 1.422 119.36 115.12 121.14 109.80 111.31 111.68 123.74 * +* * +* 20 ILE 20 1.294 1.253 1.515 1.570 1.435 123.09 116.20 119.97 109.02 107.74 111.67 123.78 ** * * * * ** 21 GLY 21 1.328 1.238 1.514 - 1.442 121.36 118.35 119.71 - 110.65 - 121.94 22 PRO 22 1.333 1.235 1.529 1.523 1.456 122.40 115.02 121.42 111.08 112.91 104.01 123.56 * * * 23 LYS 23 1.291 1.222 1.524 1.542 1.440 123.85 118.83 118.81 109.77 105.53 107.48 122.35 +** * * * ** +* +** 24 ALA 24 1.310 1.243 1.530 1.523 1.463 120.58 116.23 120.53 111.03 111.44 110.47 123.23 * * 25 PHE 25 1.324 1.233 1.530 1.531 1.451 123.14 117.20 120.64 106.59 110.26 111.03 122.08 +* +* 26 PRO 26 1.316 1.233 1.546 1.524 1.465 123.42 115.79 121.09 108.37 112.69 103.89 123.12 +* +* 27 ASP 27 1.325 1.244 1.533 1.537 1.488 123.88 115.91 120.81 107.15 112.51 110.29 123.27 +* * +* +* 28 ALA 28 1.328 1.227 1.530 1.521 1.461 122.40 117.07 120.17 110.58 113.27 110.24 122.76 29 THR 29 1.313 1.234 1.543 1.533 1.451 121.71 116.24 120.69 111.32 110.99 109.34 123.06 * * * * 30 THR 30 1.323 1.229 1.527 1.543 1.442 122.45 115.99 120.76 109.14 111.64 110.51 123.25 31 VAL 31 1.321 1.240 1.526 1.543 1.458 123.29 115.60 121.33 110.29 109.94 110.66 123.06 32 SER 32 1.318 1.225 1.534 1.535 1.433 121.52 116.04 120.80 110.91 108.70 110.15 123.07 * * 33 ALA 33 1.337 1.231 1.535 1.511 1.448 122.42 117.19 120.11 111.83 111.26 110.82 122.70 34 LEU 34 1.349 1.227 1.508 1.549 1.475 121.38 115.41 121.23 108.45 109.12 112.01 123.32 * * 35 LYS 35 1.316 1.218 1.516 1.517 1.439 122.10 117.03 119.62 112.48 111.65 110.76 123.32 * * * 36 GLU 36 1.339 1.233 1.526 1.533 1.465 122.21 115.68 121.19 109.00 109.28 110.70 123.13 37 THR 37 1.323 1.224 1.534 1.549 1.440 122.44 116.79 120.16 110.30 110.37 111.03 123.01 38 VAL 38 1.336 1.222 1.519 1.564 1.461 122.13 115.61 120.59 109.34 109.89 112.24 123.73 39 ILE 39 1.324 1.231 1.546 1.570 1.468 122.71 116.37 120.96 109.43 110.24 110.83 122.65 * * 40 SER 40 1.327 1.242 1.547 1.527 1.454 121.68 117.22 120.35 109.87 112.80 109.25 122.39 * * 41 GLU 41 1.330 1.237 1.517 1.519 1.439 121.88 115.71 121.03 110.13 111.54 109.79 123.26 * * 42 TRP 42 1.306 1.245 1.554 1.544 1.442 122.77 118.48 119.27 112.46 107.28 107.26 122.13 +* * * * * +* +* 43 PRO 43 1.367 1.233 1.540 1.518 1.485 124.45 116.36 121.05 109.76 115.43 102.22 122.58 +* * * +* 44 ARG 44 1.333 1.225 1.526 1.552 1.469 121.36 115.13 121.20 108.00 110.14 113.47 123.65 * * +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 GLU 45 1.315 1.231 1.552 1.549 1.468 124.24 116.32 120.19 109.33 111.12 107.82 123.45 * * +* +* 46 LYS 46 1.345 1.236 1.547 1.526 1.462 125.22 113.46 122.29 111.60 117.36 111.68 124.25 * * +* * ** ** 47 GLU 47 1.321 1.229 1.537 1.539 1.449 125.96 115.28 121.29 109.91 112.05 107.32 123.42 ** +* ** 48 ASN 48 1.333 1.236 1.542 1.544 1.487 125.48 116.56 120.59 108.92 114.10 111.20 122.84 +* ** * ** 49 GLY 49 1.294 1.232 1.508 - 1.434 122.09 118.20 119.70 - 109.89 - 122.08 +** * +** 50 PRO 50 1.336 1.215 1.517 1.527 1.466 122.99 116.83 120.44 108.56 111.47 102.85 122.66 51 LYS 51 1.297 1.230 1.505 1.544 1.432 120.61 116.57 120.51 114.44 112.15 112.22 122.91 ** * ** * ** 52 THR 52 1.304 1.236 1.539 1.551 1.426 122.46 116.39 120.71 112.16 110.85 113.51 122.88 +* +* * * +* 53 VAL 53 1.314 1.232 1.539 1.572 1.463 124.05 115.43 121.50 110.55 110.95 111.40 123.03 * * * * 54 LYS 54 1.319 1.227 1.530 1.528 1.442 122.91 117.91 120.05 111.19 112.80 110.47 122.02 55 GLU 55 1.319 1.235 1.521 1.537 1.466 119.20 116.26 121.20 112.71 114.35 114.86 122.39 * * * +** +** 56 VAL 56 1.310 1.229 1.544 1.571 1.448 121.35 116.51 121.13 112.02 109.93 112.23 122.31 * * * * 57 LYS 57 1.316 1.236 1.535 1.539 1.460 121.71 117.31 119.97 112.31 109.05 109.40 122.72 * * 58 LEU 58 1.330 1.242 1.550 1.574 1.453 121.43 116.36 120.78 111.92 109.95 107.95 122.86 * ** +* ** 59 ILE 59 1.327 1.226 1.526 1.566 1.467 122.87 116.31 120.60 109.90 110.23 111.94 123.08 60 SER 60 1.310 1.243 1.513 1.537 1.441 122.44 116.40 119.85 109.97 108.07 110.42 123.65 * * * 61 ALA 61 1.338 1.234 1.532 1.532 1.473 123.69 115.91 121.08 111.27 111.71 110.75 122.96 * * 62 GLY 62 1.316 1.233 1.522 - 1.445 121.58 117.30 120.41 - 113.40 - 122.29 63 LYS 63 1.317 1.228 1.517 1.545 1.449 121.23 117.02 119.84 110.77 108.60 110.24 123.12 64 VAL 64 1.319 1.244 1.519 1.554 1.458 121.64 116.63 120.37 109.17 109.00 111.75 123.00 65 LEU 65 1.310 1.233 1.513 1.533 1.423 121.56 115.36 120.96 110.81 111.93 111.65 123.66 * +* +* 66 GLU 66 1.316 1.239 1.541 1.559 1.450 122.62 115.89 120.12 113.38 107.29 108.48 123.99 * +* * * +* 67 ASN 67 1.336 1.239 1.530 1.541 1.494 125.37 116.82 120.10 107.22 114.57 111.03 123.07 +* ** +* * ** 68 SER 68 1.317 1.233 1.531 1.513 1.464 122.32 115.97 121.05 109.37 113.20 109.28 122.98 69 LYS 69 1.289 1.220 1.523 1.506 1.440 122.90 116.42 120.60 110.96 112.17 109.45 122.97 +** * +** 70 THR 70 1.315 1.237 1.533 1.532 1.426 123.21 116.25 120.53 109.65 111.71 109.30 123.22 * +* * +* 71 VAL 71 1.336 1.236 1.525 1.562 1.468 122.95 115.43 121.03 108.52 110.43 111.26 123.51 72 LYS 72 1.325 1.226 1.530 1.531 1.463 123.54 116.76 120.33 109.98 112.51 109.90 122.90 * * 73 ASP 73 1.319 1.239 1.531 1.535 1.465 121.66 116.38 121.10 110.02 111.54 110.95 122.48 74 TYR 74 1.317 1.234 1.503 1.515 1.441 121.32 116.08 120.95 109.52 111.24 110.20 122.98 * * 75 ARG 75 1.303 1.241 1.528 1.530 1.402 122.10 115.64 120.90 110.12 110.55 109.16 123.42 +* +** +** 76 SER 76 1.306 1.240 1.534 1.518 1.426 122.67 118.55 119.51 109.39 107.54 107.64 121.93 +* +* * * +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 77 PRO 77 1.335 1.249 1.538 1.531 1.463 122.29 116.68 121.08 110.72 112.36 103.77 122.23 78 VAL 78 1.319 1.244 1.511 1.533 1.436 121.15 113.22 122.61 110.45 110.66 113.70 123.95 * * * * * 79 SER 79 1.263 1.232 1.528 1.528 1.428 124.14 118.24 119.81 110.56 107.16 108.91 121.95 *4.7* +* * * * *4.7* 80 ASN 80 1.304 1.245 1.519 1.536 1.448 119.74 115.57 121.25 111.22 110.88 112.21 123.06 +* * * +* 81 LEU 81 1.314 1.245 1.521 1.527 1.382 123.23 116.40 120.48 110.62 109.99 110.71 123.11 * +*** +*** 82 ALA 82 1.310 1.238 1.517 1.524 1.426 122.03 115.75 120.96 111.29 111.20 111.23 123.28 * +* +* 83 GLY 83 1.312 1.241 1.502 - 1.445 121.20 116.67 120.67 - 110.73 - 122.65 * * 84 ALA 84 1.312 1.232 1.511 1.523 1.429 119.96 114.85 121.54 110.42 111.17 110.16 123.58 * +* +* 85 VAL 85 1.299 1.225 1.500 1.555 1.429 123.49 117.65 119.95 108.75 106.40 112.88 122.38 ** * +* +* ** 86 THR 86 1.275 1.239 1.525 1.534 1.432 119.61 116.54 120.67 110.55 108.97 111.12 122.75 +*** * * +*** 87 THR 87 1.298 1.232 1.523 1.538 1.424 121.16 116.53 120.67 110.16 109.20 110.00 122.79 ** +* ** 88 MET 88 1.307 1.231 1.508 1.531 1.441 121.21 116.47 120.67 111.07 110.12 110.77 122.86 +* +* 89 HIS 89 1.305 1.235 1.507 1.539 1.439 121.53 115.01 121.17 110.63 109.68 111.36 123.82 +* +* 90 VAL 90 1.288 1.235 1.486 1.546 1.425 123.02 114.28 121.65 110.09 109.15 111.74 124.04 +** +* +* +** 91 ILE 91 1.271 1.244 1.500 1.532 1.397 122.80 114.41 121.32 111.36 109.67 110.72 124.25 **** * *** * **** 92 ILE 92 1.298 1.234 1.506 1.577 1.419 123.04 116.04 120.75 109.77 107.53 111.81 123.17 ** * ** * ** 93 GLN 93 1.294 1.220 1.501 1.531 1.414 121.83 115.67 120.81 110.94 108.68 109.93 123.46 +** * ** +** 94 ALA 94 1.299 1.240 1.522 1.525 1.439 122.04 117.57 120.33 110.77 109.45 110.27 122.09 ** ** 95 PRO 95 1.334 1.252 1.524 1.533 1.453 122.41 116.02 120.77 110.66 111.79 103.21 123.20 * * 96 VAL 96 1.314 1.240 1.520 1.547 1.451 122.13 117.12 119.98 109.95 108.46 111.10 122.87 * * 97 THR 97 1.321 1.234 1.533 1.542 1.436 121.19 113.35 122.28 112.05 111.82 111.89 124.16 * * * * 98 GLU 98 1.296 1.247 1.503 1.540 1.431 126.30 116.31 120.79 109.79 104.50 111.15 122.71 ** * * +** ** +** 99 LYS 99 1.298 1.240 1.505 1.537 1.410 119.92 115.35 121.71 113.38 115.04 113.68 122.89 ** +** +* * +* +** 100 GLU 100 1.310 1.235 1.507 1.548 1.422 120.61 113.59 122.14 113.81 104.46 111.78 123.95 * +* * +* ** ** 101 LYS 101 1.285 - 1.501 1.573 1.409 123.93 - - 113.84 105.62 108.10 - *** * ** +** * +* +* * *** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.7* * +* ** +*** +** * * ** ** +** * *4.7* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 9 ---------------------------------------- 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 94 1.263 1.349 1.313 .016 *4.7* * * C-N (Pro) 1.341 .016 6 1.316 1.367 1.337 .015 +* +* C-O C-O 1.231 .020 100 1.215 1.253 1.234 .007 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.486 1.554 1.523 .014 +* * CH2G*-C (Gly) 1.516 .018 5 1.502 1.522 1.511 .007 CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.511 1.532 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.532 1.577 1.552 .014 * CH1E-CH2E (the rest) 1.530 .020 62 1.506 1.574 1.535 .013 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.382 1.494 1.444 .020 +*** +* NH1-CH2G* (Gly) 1.451 .016 5 1.434 1.445 1.442 .004 * N-CH1E (Pro) 1.466 .015 6 1.453 1.485 1.465 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 Page 10 ---------------------------------------- +-----------------+ | 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 89 113.22 118.83 116.22 1.13 * * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.84 118.35 117.27 .94 CH1E-C-N (Pro) 116.9 1.5 6 115.02 116.83 116.12 .61 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.83 124.25 123.01 .56 O-C-N (Pro) 122.0 1.4 6 122.23 123.56 122.89 .44 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.20 126.30 122.27 1.43 * +** C-NH1-CH2G* (Gly) 120.6 1.7 5 121.05 122.09 121.46 .36 C-N-CH1E (Pro) 122.6 5.0 6 122.29 124.45 122.99 .76 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.81 122.61 120.72 .70 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.70 121.14 120.33 .56 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.42 111.83 110.97 .44 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.52 112.16 110.16 1.01 * CH2E-CH1E-C (the rest) 110.1 1.9 62 106.59 114.44 110.44 1.68 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.46 117.36 110.24 2.23 ** ** NH1-CH2G*-C (Gly) 112.5 2.9 5 109.89 113.40 111.34 1.24 N-CH1E-C (Pro) 111.8 2.5 6 111.47 115.43 112.78 1.29 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 110.16 111.23 110.54 .34 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.30 113.70 111.40 1.04 * * N-CH1E-CH2E (Pro) 103.0 1.1 6 102.22 104.01 103.33 .64 NH1-CH1E-CH2E (the rest) 110.5 1.7 56 107.26 114.86 110.57 1.84 +* +** ------------------------------------------------------------------------------------------------------------- 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 11 ---------------------------------------- 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] 76 86.4% Residues in additional allowed regions [a,b,l,p] 12 13.6% 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 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 6 ---- Total number of residues 101 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 88 86.4 83.8 10.0 .3 Inside b. Omega angle st dev 100 3.7 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 2.1 3.1 1.6 -.7 Inside e. H-bond energy st dev 53 .9 .8 .2 .2 Inside f. Overall G-factor 101 -.1 -.4 .3 1.0 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 17 8.6 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 27 4.9 19.0 5.3 -2.7 BETTER c. Chi-1 gauche plus st dev 38 7.1 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 82 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 20 5.8 20.4 5.0 -2.9 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% 86.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .86 2 Residue-by-residue listing for refined_18 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.63 Chi1-chi2 distribution -.47 Chi1 only .07 Chi3 & chi4 .33 Omega -.06 ------ -.24 ===== Main-chain covalent forces:- Main-chain bond lengths -.01 Main-chain bond angles .36 ------ .20 ===== OVERALL AVERAGE -.08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.