Residue-by-residue listing for refined_6 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 - - 193.1 - - - - - - - - 178.1 - 34.9 - 2 ALA 2 B - - - - - - - - - - 181.7 - 34.6 - 3 GLU 3 b - - -62.0 - - - - - - - 182.1 - 33.8 - 4 VAL 4 B 60.4 - - - - - - - - - 178.0 - 32.7 - 5 HIS 5 B - - -64.1 - - - - - - - 176.4 - 34.9 - 6 ASN 6 B - - -68.8 - - - - - - - 176.3 - 34.2 - 7 GLN 7 e B - - -63.6 - - - - - - - 175.7 -1.1 33.7 - * * 8 LEU 8 E B - - -66.7 - - - - - - - 188.6 -2.8 32.8 - * * * 9 GLU 9 E B - - -55.9 183.8 - - - - - - 185.2 -1.3 32.2 - 10 ILE 10 E B - - -55.9 176.7 - - - - - - 174.3 -2.0 35.1 - 11 LYS 11 E B 63.9 - - 175.5 - - - - - - 180.3 -2.3 32.8 - 12 PHE 12 E B - - -58.8 - - - - - - - 179.2 - 35.2 - 13 ARG 13 E B - 196.7 - - - - - - - - 183.1 -3.3 35.8 - +* +* 14 LEU 14 E B - - -63.0 - - - - - - - 175.5 -2.2 34.4 - 15 THR 15 e A - 183.2 - - - - - - - - 179.6 -2.1 35.5 - 16 ASP 16 T A - 176.4 - - - - - - - - 179.4 - 36.7 - 17 GLY 17 t - - - - - - - - - - - 178.4 -2.1 - - 18 SER 18 B - - -56.0 - - - - - - - 176.8 - 35.8 - 19 ASP 19 B B 61.2 - - - - - - - - - 180.1 - 32.9 - 20 ILE 20 B - - -59.2 177.6 - - - - - - 180.2 -2.7 34.9 - 21 GLY 21 - - - - - - - - - - - 184.3 - - - 22 PRO 22 - - - - - -60.3 - - - - - 178.9 - 37.9 - * * 23 LYS 23 E B - - -56.0 169.9 - - - - - - 181.3 -2.5 36.4 - 24 ALA 24 E B - - - - - - - - - - 179.7 - 32.9 - Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 25 PHE 25 E B - - -57.1 - - - - - - - 169.9 -2.3 36.8 - +* +* 26 PRO 26 t - - - - - -59.9 - - - - - 180.3 - 39.6 - +* +* 27 ASP 27 T A - 183.8 - - - - - - - - 177.8 - 34.2 - 28 ALA 28 T A - - - - - - - - - - 178.1 - 34.3 - 29 THR 29 t B - - -57.6 - - - - - - - 178.6 -1.6 34.2 - 30 THR 30 h B 56.0 - - - - - - - - - 177.7 - 35.0 - 31 VAL 31 H A - 175.6 - - - -65.2 -26.3 - - - 172.9 -3.2 31.9 - * * +* +* 32 SER 32 H A - - -58.6 - - -59.7 -41.3 - - - 180.2 -1.5 34.0 - 33 ALA 33 H A - - - - - -64.8 -30.0 - - - 173.8 - 32.9 - * * 34 LEU 34 H A - - -83.9 - - -58.8 -44.8 - - - 179.6 -1.0 33.7 - * * * 35 LYS 35 H A - - -63.0 182.1 - -72.0 -36.5 - - - 176.1 -1.4 32.5 - 36 GLU 36 H A - - -61.9 - - -61.1 -36.4 - - - 177.5 -2.3 34.2 - 37 THR 37 H A - - -59.4 - - -74.3 -42.2 - - - 184.3 -2.1 34.0 - 38 VAL 38 H A 76.5 - - - - -62.2 -41.2 - - - 179.1 -2.5 32.3 - 39 ILE 39 H A - - -59.1 182.0 - -62.2 -40.0 - - - 181.5 -2.4 34.0 - 40 SER 40 H A - - -53.3 - - -75.4 -32.5 - - - 182.9 -1.1 35.4 - * * 41 GLU 41 H A - 180.2 - - - -82.8 -34.0 - - - 180.4 -2.5 34.9 - * * 42 TRP 42 h B - 194.6 - - - - - - - - 179.1 -3.0 35.1 - * * 43 PRO 43 t - - - - - -33.7 - - - - - 186.2 - 39.0 - +** * * +** 44 ARG 44 T A 66.6 - - 182.3 - - - - - - 183.7 - 34.2 - 45 GLU 45 T A 62.4 - - 175.7 - - - - - - 182.1 - 33.9 - 46 LYS 46 t B - - -72.7 - - - - - - - 174.4 -1.2 34.0 - * * 47 GLU 47 B - 180.8 - 182.5 - - - - - - 183.0 - 33.2 - 48 ASN 48 S l - 185.4 - - - - - - - - 179.8 - 33.5 - 49 GLY 49 t - - - - - - - - - - - 180.0 - - - 50 PRO 50 T - - - - - -72.3 - - - - - 187.0 - 40.8 - * +* +* 51 LYS 51 T A - 183.7 - 180.0 - - - - - - 187.4 -2.1 33.2 - * * 52 THR 52 t B 53.4 - - - - - - - - - 187.1 -.6 27.4 - * +* +* +* 53 VAL 53 t A 58.0 - - - - - - - - - 186.1 - 35.0 - * * 54 LYS 54 T A - - -56.9 171.8 - - - - - - 185.3 - 35.9 - 55 GLU 55 e A 50.8 - - - - - - - - - 180.0 - 31.1 - 56 VAL 56 E B - 174.6 - - - - - - - - 175.1 -.7 33.4 - +* +* 57 LYS 57 E B - - -83.8 - - - - - - - 177.4 -2.1 33.1 - * * 58 LEU 58 E B - - -65.1 - - - - - - - 175.7 - 34.2 - 59 ILE 59 E B - - -61.7 181.5 - - - - - - 179.1 -2.4 33.8 - 60 SER 60 E B - - -57.0 - - - - - - - 178.5 -2.1 35.1 - 61 ALA 61 T l - - - - - - - - - - 180.9 - 32.6 - 62 GLY 62 T - - - - - - - - - - - 180.2 - - - 63 LYS 63 E B - - -62.5 183.5 - - - - - - 173.5 -1.8 37.1 - * * Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 64 VAL 64 E B - 183.5 - - - - - - - - 187.9 -.5 34.3 - * ** ** 65 LEU 65 e B - - -55.1 182.5 - - - - - - 172.0 -3.2 34.1 - * +* +* 66 GLU 66 t B - 168.1 - - - - - - - - 182.9 - 35.5 - 67 ASN 67 T A 67.8 - - - - - - - - - 181.8 - 32.1 - 68 SER 68 T A - - -50.7 - - - - - - - 178.3 - 34.4 - * * 69 LYS 69 t B - - -72.6 179.6 - - - - - - 178.6 -1.5 33.6 - 70 THR 70 h B 58.9 - - - - - - - - - 178.9 - 34.9 - 71 VAL 71 H A - 183.6 - - - -61.5 -35.5 - - - 178.0 -2.7 34.0 - 72 LYS 72 H A - 184.7 - - - -52.2 -36.9 - - - 181.8 -1.7 36.1 - * * 73 ASP 73 H A - - -73.7 - - -63.6 -29.0 - - - 183.6 -.8 33.8 - +* +* 74 TYR 74 H A - - -54.9 - - -98.3 -3.8 - - - 181.4 -1.6 35.6 - +** *** *** 75 ARG 75 h B - - -67.1 - - - - - - - 171.3 -.9 37.0 - +* * +* 76 SER 76 B - - -59.9 - - - - - - - 183.7 - 35.6 - 77 PRO 77 S - - - - - -56.2 - - - - - 177.7 - 36.8 - 78 VAL 78 S a - 179.7 - - - - - - - - 181.1 - 32.5 - 79 SER 79 b - - -61.5 - - - - - - - 178.3 - 34.6 - 80 ASN 80 b - - -65.9 - - - - - - - 181.9 - 33.0 - 81 LEU 81 t B - - -60.9 - - - - - - - 178.8 -.6 36.8 - +* +* 82 ALA 82 T B - - - - - - - - - - 181.2 - 33.5 - 83 GLY 83 T - - - - - - - - - - - 176.1 -1.7 - - 84 ALA 84 E B - - - - - - - - - - 185.7 -.8 34.3 - +* +* 85 VAL 85 E B - 184.4 - - - - - - - - 178.1 -.7 34.0 - +* +* 86 THR 86 E B - - -57.5 - - - - - - - 181.0 -3.3 34.7 - +* +* 87 THR 87 E B - - -54.5 - - - - - - - 178.6 -.6 35.7 - +* +* 88 MET 88 E B - - -66.3 182.4 - - - - - - 180.0 -2.7 32.9 - 89 HIS 89 E B - - -63.4 - - - - - - - 185.1 -3.1 33.5 - * * 90 VAL 90 E B - 184.8 - - - - - - - - 178.8 -3.5 34.2 - +* +* 91 ILE 91 E B - - -65.3 - - - - - - - 185.4 -1.8 34.8 - 92 ILE 92 E B - - -57.4 - - - - - - - 175.0 -.5 35.7 - ** ** 93 GLN 93 e B - - -66.9 - - - - - - - 175.6 -2.3 34.0 - 94 ALA 94 B - - - - - - - - - - 184.5 - 34.6 - 95 PRO 95 - - - - - -64.7 - - - - - 177.1 - 38.3 - * * 96 VAL 96 b - 181.4 - - - - - - - - 180.4 - 33.2 - 97 THR 97 b - - -55.7 - - - - - - - 179.1 -1.3 35.2 - 98 GLU 98 B - 186.9 - 182.6 - - - - - - 188.7 -.7 34.8 - +* +* +* 99 LYS 99 S l - 181.1 - 179.1 - - - - - - 185.2 - 31.0 - 100 GLU 100 B - 181.8 - 178.9 - - - - - - 175.9 - 34.0 - 101 LYS 101 - - - -62.7 182.2 - - - - - - - -.9 31.5 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +** +** *** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.3 183.0 -62.0 179.6 -57.9 -67.6 -34.0 - - - 179.9 -1.9 34.4 Standard deviations: 6.9 6.3 7.0 3.8 13.0 11.5 9.9 - - - 3.9 .9 1.8 Numbers of values: 12 23 47 21 6 15 15 0 0 0 100 55 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_6 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 - 1.231 1.530 1.552 1.450 - 116.37 120.78 111.60 107.70 109.15 122.80 * * * 2 ALA 2 1.313 1.245 1.513 1.523 1.448 122.40 116.31 119.11 110.34 108.97 110.31 124.58 * * 3 GLU 3 1.347 1.245 1.512 1.546 1.480 124.32 115.20 121.05 108.51 111.42 112.54 123.74 * * * * * 4 VAL 4 1.305 1.239 1.523 1.559 1.433 122.21 114.88 121.65 111.39 111.34 111.61 123.44 +* * * +* 5 HIS 5 1.294 1.231 1.513 1.545 1.461 122.36 117.20 120.19 108.96 108.40 111.56 122.61 +** * +** 6 ASN 6 1.299 1.239 1.498 1.550 1.449 120.79 117.31 120.27 109.26 109.17 112.30 122.32 ** * * * ** 7 GLN 7 1.317 1.249 1.483 1.525 1.410 119.26 114.78 121.47 108.15 109.54 114.06 123.75 +* +** * * ** +** 8 LEU 8 1.274 1.232 1.498 1.536 1.410 121.42 116.32 120.99 112.47 106.59 112.15 122.66 +*** * +** * +* +*** 9 GLU 9 1.272 1.215 1.496 1.509 1.411 120.64 115.09 121.53 112.73 111.26 110.77 123.38 **** * * ** * **** 10 ILE 10 1.280 1.241 1.504 1.564 1.436 122.33 115.66 120.82 108.77 110.10 111.41 123.50 *** * *** 11 LYS 11 1.297 1.249 1.512 1.539 1.432 121.46 116.07 120.62 110.25 109.06 113.30 123.31 ** * +* ** Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 PHE 12 1.298 1.230 1.508 1.537 1.436 121.48 116.65 120.53 109.49 108.66 110.70 122.81 ** * ** 13 ARG 13 1.300 1.225 1.517 1.548 1.438 121.42 116.78 120.48 110.50 106.27 109.42 122.75 ** * +* ** 14 LEU 14 1.295 1.233 1.513 1.546 1.434 121.60 115.17 121.03 108.92 111.33 111.67 123.78 ** * ** 15 THR 15 1.320 1.222 1.540 1.545 1.473 124.74 114.17 122.13 110.02 110.23 108.95 123.69 +* * +* +* 16 ASP 16 1.304 1.221 1.536 1.548 1.463 124.77 115.96 121.49 109.82 110.03 107.49 122.53 +* +* +* +* 17 GLY 17 1.316 1.224 1.502 - 1.449 121.58 115.18 121.22 - 111.48 - 123.50 18 SER 18 1.297 1.247 1.520 1.529 1.432 122.70 117.58 119.92 110.42 108.26 108.80 122.48 ** * * * ** 19 ASP 19 1.302 1.233 1.508 1.530 1.418 121.75 115.37 121.05 110.95 110.32 111.94 123.54 +* ** ** 20 ILE 20 1.299 1.240 1.521 1.562 1.446 123.14 116.48 119.77 110.14 108.81 110.57 123.74 ** ** 21 GLY 21 1.331 1.240 1.524 - 1.453 121.54 117.74 119.96 - 112.40 - 122.29 22 PRO 22 1.345 1.237 1.523 1.536 1.464 123.28 115.20 121.40 110.26 113.84 104.37 123.41 * * * * 23 LYS 23 1.305 1.213 1.478 1.516 1.449 123.30 116.67 119.97 107.82 107.06 110.64 123.33 +* ** * * ** 24 ALA 24 1.267 1.244 1.519 1.533 1.459 119.96 116.11 120.98 111.15 110.69 111.36 122.91 **** **** 25 PHE 25 1.314 1.224 1.505 1.538 1.446 122.13 118.58 120.23 105.74 108.46 111.82 121.13 * * ** * ** 26 PRO 26 1.311 1.231 1.527 1.525 1.449 121.30 116.78 120.75 109.54 109.58 103.33 122.47 +* * +* 27 ASP 27 1.287 1.220 1.537 1.518 1.453 121.63 115.45 121.96 111.77 109.64 109.11 122.53 +** +** 28 ALA 28 1.322 1.236 1.544 1.517 1.453 122.59 116.89 120.56 110.19 111.53 109.77 122.55 29 THR 29 1.325 1.243 1.538 1.555 1.460 121.86 115.86 120.89 109.89 110.83 110.88 123.24 30 THR 30 1.314 1.232 1.532 1.551 1.437 122.56 117.04 120.38 109.42 110.33 110.55 122.57 * * * 31 VAL 31 1.319 1.235 1.542 1.556 1.459 121.83 116.32 121.20 113.00 110.20 111.27 122.46 +* +* 32 SER 32 1.327 1.228 1.547 1.533 1.452 121.40 116.76 120.47 110.43 110.16 110.58 122.71 * * 33 ALA 33 1.347 1.234 1.527 1.516 1.467 122.19 116.51 120.55 110.79 111.26 111.22 122.93 * * 34 LEU 34 1.333 1.230 1.521 1.547 1.459 121.94 116.17 120.92 110.41 110.30 111.35 122.85 35 LYS 35 1.319 1.222 1.524 1.517 1.442 121.26 116.32 121.06 111.63 111.14 111.22 122.61 36 GLU 36 1.309 1.245 1.528 1.522 1.457 121.74 115.66 121.38 110.63 110.47 110.01 122.95 * * 37 THR 37 1.311 1.224 1.534 1.547 1.432 121.79 117.06 120.10 110.14 110.87 111.03 122.79 * * * 38 VAL 38 1.339 1.210 1.528 1.575 1.464 121.53 116.44 120.32 111.09 110.68 112.70 123.17 * * * 39 ILE 39 1.328 1.230 1.528 1.563 1.474 121.95 115.64 121.37 109.21 110.68 112.00 122.97 40 SER 40 1.308 1.234 1.540 1.525 1.447 122.29 115.80 121.21 110.27 110.99 108.56 122.99 +* * +* 41 GLU 41 1.313 1.237 1.549 1.529 1.436 123.84 116.67 120.63 112.57 111.85 106.76 122.68 * * * * * ** ** 42 TRP 42 1.319 1.248 1.537 1.547 1.460 122.43 117.74 119.15 110.62 108.96 109.33 123.02 Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 PRO 43 1.377 1.241 1.531 1.518 1.475 124.52 115.47 121.29 110.42 113.27 102.45 123.24 ** ** 44 ARG 44 1.323 1.228 1.516 1.536 1.454 122.90 116.39 120.47 109.63 111.92 110.79 123.14 45 GLU 45 1.315 1.234 1.525 1.526 1.456 121.66 116.35 120.72 109.66 112.00 110.91 122.93 * * 46 LYS 46 1.313 1.231 1.507 1.524 1.416 122.09 114.80 121.30 110.62 112.24 110.12 123.86 * ** ** 47 GLU 47 1.294 1.238 1.487 1.534 1.417 124.15 115.75 119.59 110.78 106.14 113.34 124.62 ** +* ** * +* +* * ** 48 ASN 48 1.309 1.228 1.544 1.550 1.470 123.85 115.62 122.07 111.47 109.07 110.71 122.28 * * * * 49 GLY 49 1.314 1.217 1.498 - 1.409 120.81 117.74 120.01 - 110.48 - 122.25 * +** +** 50 PRO 50 1.312 1.226 1.542 1.535 1.498 124.20 116.86 120.51 109.08 113.27 101.20 122.48 +* ** +* ** 51 LYS 51 1.301 1.223 1.535 1.541 1.454 121.02 117.96 120.02 110.31 113.89 110.69 122.02 +* +* 52 THR 52 1.316 1.217 1.549 1.556 1.442 120.27 114.21 122.32 113.57 116.58 113.28 123.47 * ** +* * ** 53 VAL 53 1.317 1.234 1.531 1.575 1.459 125.96 115.82 121.01 110.24 112.41 109.29 123.15 * ** * ** 54 LYS 54 1.309 1.227 1.516 1.530 1.450 123.29 115.71 121.16 109.73 110.83 108.52 123.08 * * * 55 GLU 55 1.297 1.237 1.534 1.539 1.448 121.68 117.23 120.32 111.51 114.72 111.91 122.39 ** * ** 56 VAL 56 1.318 1.234 1.546 1.564 1.465 121.20 116.53 120.64 109.94 112.12 111.55 122.79 57 LYS 57 1.337 1.234 1.521 1.541 1.474 123.04 116.05 120.45 109.15 111.99 112.67 123.49 * * 58 LEU 58 1.327 1.233 1.530 1.567 1.460 122.55 116.56 120.57 108.64 109.74 112.61 122.84 +* * +* 59 ILE 59 1.309 1.239 1.521 1.563 1.455 122.64 115.97 120.93 110.12 109.42 111.94 123.05 * * 60 SER 60 1.309 1.235 1.521 1.517 1.437 122.37 116.21 120.05 110.35 109.77 109.33 123.64 * * * 61 ALA 61 1.337 1.239 1.530 1.533 1.477 123.98 115.61 121.22 111.31 111.53 111.18 123.12 * * 62 GLY 62 1.309 1.227 1.515 - 1.437 121.37 117.20 120.32 - 112.74 - 122.48 * * 63 LYS 63 1.325 1.235 1.500 1.519 1.417 121.92 117.06 119.75 106.95 109.40 110.11 123.20 * ** +* ** 64 VAL 64 1.307 1.238 1.512 1.545 1.439 120.43 116.20 120.71 109.85 105.92 112.41 123.04 +* +* +* 65 LEU 65 1.293 1.236 1.510 1.521 1.420 121.49 114.47 121.64 109.75 112.81 110.53 123.89 +** ** +** 66 GLU 66 1.292 1.242 1.512 1.541 1.431 123.94 116.79 120.19 111.14 107.15 108.91 123.02 +** * * * +** 67 ASN 67 1.313 1.228 1.520 1.546 1.449 121.19 115.76 120.88 111.21 110.91 112.54 123.29 * * * 68 SER 68 1.328 1.233 1.555 1.527 1.457 122.66 116.74 120.98 110.51 112.22 109.27 122.28 * * 69 LYS 69 1.308 1.238 1.513 1.511 1.429 122.74 116.43 120.69 110.22 110.95 111.18 122.87 +* +* +* 70 THR 70 1.308 1.232 1.507 1.545 1.408 121.75 117.84 119.34 109.98 108.33 111.03 122.83 * +** * +** 71 VAL 71 1.324 1.241 1.538 1.556 1.463 120.85 114.33 121.53 110.29 108.79 111.48 124.05 Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.331 1.231 1.530 1.523 1.453 125.42 116.04 120.94 109.38 111.40 108.30 122.98 ** * ** 73 ASP 73 1.321 1.235 1.525 1.535 1.446 123.32 116.79 120.38 110.23 112.86 110.44 122.81 74 TYR 74 1.319 1.240 1.515 1.518 1.449 121.99 115.75 121.18 109.34 110.79 109.23 123.06 75 ARG 75 1.305 1.232 1.499 1.498 1.408 122.61 114.97 121.05 107.43 111.27 109.12 123.97 +* * +* +** * +** 76 SER 76 1.283 1.231 1.528 1.515 1.400 123.45 118.79 119.14 111.64 105.72 108.54 121.99 *** *** * +* * *** 77 PRO 77 1.342 1.241 1.513 1.516 1.461 122.41 114.78 121.68 110.58 114.28 105.34 123.52 * ** * ** 78 VAL 78 1.301 1.238 1.503 1.558 1.440 122.72 115.43 120.98 110.49 109.92 113.28 123.55 ** * * ** 79 SER 79 1.291 1.234 1.530 1.545 1.460 123.85 116.50 120.55 109.53 110.17 110.79 122.94 +** * +** 80 ASN 80 1.315 1.244 1.502 1.534 1.456 122.33 115.13 121.42 110.69 110.08 112.07 123.39 * * * 81 LEU 81 1.308 1.232 1.516 1.510 1.385 123.43 115.74 120.96 108.76 110.23 108.63 123.28 +* * +*** * +*** 82 ALA 82 1.298 1.235 1.499 1.518 1.407 122.72 114.79 121.57 111.22 108.31 111.61 123.49 ** * +** * +** 83 GLY 83 1.284 1.236 1.510 - 1.439 120.71 116.08 120.87 - 112.02 - 123.04 *** *** 84 ALA 84 1.327 1.231 1.511 1.522 1.445 121.26 116.69 120.29 110.73 107.89 110.68 123.02 * * 85 VAL 85 1.304 1.230 1.510 1.549 1.439 121.32 115.26 121.52 109.18 110.71 112.16 123.22 +* +* 86 THR 86 1.280 1.237 1.524 1.548 1.419 123.05 116.37 120.92 110.53 108.07 110.72 122.67 +*** ** * +*** 87 THR 87 1.294 1.232 1.523 1.544 1.421 121.21 116.83 120.78 109.84 109.15 109.58 122.39 +** +* * +** 88 MET 88 1.304 1.227 1.489 1.531 1.439 120.76 116.06 120.63 110.83 109.72 112.36 123.29 +* +* * +* 89 HIS 89 1.301 1.227 1.497 1.537 1.437 121.28 115.93 120.62 111.30 108.11 111.53 123.43 ** * * * ** 90 VAL 90 1.290 1.244 1.497 1.543 1.430 121.66 113.87 121.70 109.79 110.70 111.39 124.43 +** * * * +** 91 ILE 91 1.285 1.241 1.510 1.537 1.424 123.74 115.19 120.85 111.02 108.50 109.83 123.95 *** +* * *** 92 ILE 92 1.304 1.234 1.529 1.558 1.434 122.66 116.19 120.80 108.70 110.59 110.29 123.00 +* * +* 93 GLN 93 1.302 1.225 1.484 1.547 1.417 122.52 115.80 120.31 108.39 107.55 114.13 123.81 +* +* ** * ** ** 94 ALA 94 1.276 1.247 1.532 1.523 1.451 121.72 117.68 120.04 110.30 108.16 110.48 122.23 +*** * +*** 95 PRO 95 1.344 1.248 1.521 1.535 1.462 122.98 115.74 121.30 110.05 113.56 104.10 122.96 96 VAL 96 1.320 1.235 1.515 1.549 1.433 121.52 114.97 121.34 110.22 108.76 112.95 123.53 * * 97 THR 97 1.300 1.236 1.520 1.537 1.423 122.97 115.73 120.95 110.45 110.20 109.27 123.27 ** +* * ** 98 GLU 98 1.299 1.239 1.507 1.519 1.430 122.81 116.10 119.48 110.89 106.64 110.26 124.42 ** * +* ** 99 LYS 99 1.322 1.240 1.519 1.544 1.461 124.10 115.26 121.59 111.72 108.98 114.18 123.13 * ** ** 100 GLU 100 1.300 1.233 1.520 1.522 1.435 121.98 115.14 120.51 110.95 111.67 109.78 124.32 ** * ** Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 LYS 101 1.330 - 1.519 1.528 1.464 124.57 - - 111.48 113.49 111.75 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** +* +*** ** * ** +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 Page 10 ---------------------------------------- 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 1.267 1.347 1.309 .016 **** * * C-N (Pro) 1.341 .016 6 1.311 1.377 1.339 .022 +* ** C-O C-O 1.231 .020 100 1.210 1.249 1.234 .008 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.478 1.555 1.520 .016 ** * CH2G*-C (Gly) 1.516 .018 5 1.498 1.524 1.510 .009 CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.516 1.533 1.523 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.537 1.575 1.554 .010 * CH1E-CH2E (the rest) 1.530 .020 62 1.498 1.567 1.532 .013 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.385 1.480 1.442 .019 +*** * NH1-CH2G* (Gly) 1.451 .016 5 1.409 1.453 1.437 .015 +** N-CH1E (Pro) 1.466 .015 6 1.449 1.498 1.468 .015 * ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 Page 11 ---------------------------------------- +-----------------+ | 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 89 113.87 118.79 116.09 .94 * * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.18 117.74 116.79 1.01 CH1E-C-N (Pro) 116.9 1.5 6 114.78 116.86 115.80 .78 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.13 124.62 123.10 .60 * * O-C-N (Pro) 122.0 1.4 6 122.47 123.52 123.01 .42 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.26 125.96 122.33 1.20 * ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.71 121.58 121.20 .37 C-N-CH1E (Pro) 122.6 5.0 6 121.30 124.52 123.12 1.08 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 119.11 122.32 120.78 .66 CH2G*-C-O (Gly) 120.8 2.1 5 119.96 121.22 120.48 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.19 111.31 110.75 .42 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.70 113.57 110.28 1.07 ** CH2E-CH1E-C (the rest) 110.1 1.9 62 105.74 112.73 110.13 1.32 ** * N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.72 116.58 110.04 1.93 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 5 110.48 112.74 111.82 .79 N-CH1E-C (Pro) 111.8 2.5 6 109.58 114.28 112.97 1.55 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.77 111.61 110.83 .58 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 108.95 113.28 111.21 1.19 +* * N-CH1E-CH2E (Pro) 103.0 1.1 6 101.20 105.34 103.46 1.35 +* ** NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.76 114.18 110.72 1.68 ** ** ------------------------------------------------------------------------------------------------------------- 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_6 Page 12 ---------------------------------------- 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] 79 89.8% Residues in additional allowed regions [a,b,l,p] 9 10.2% 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 89.8 83.8 10.0 .6 Inside b. Omega angle st dev 100 3.9 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 55 .9 .8 .2 .2 Inside f. Overall G-factor 101 .0 -.4 .3 1.2 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 12 6.9 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 23 6.3 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 47 7.0 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 82 7.7 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 21 3.8 20.4 5.0 -3.3 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 89.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 2 Residue-by-residue listing for refined_6 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.42 Chi1-chi2 distribution -.18 Chi1 only .18 Chi3 & chi4 .44 Omega -.08 ------ -.11 ===== Main-chain covalent forces:- Main-chain bond lengths -.18 Main-chain bond angles .41 ------ .16 ===== OVERALL AVERAGE -.02 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.