Residue-by-residue listing for refined_5 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 - - 181.5 - - - - - - - - 178.7 - 34.0 - 2 THR 2 B - - -55.3 - - - - - - - 183.0 - 34.4 - 3 GLU 3 e B - 188.3 - 175.8 - - - - - - 183.1 -.7 35.8 - +* +* 4 VAL 4 E B - - -63.4 - - - - - - - 181.0 - 32.8 - 5 TYR 5 E B 67.8 - - - - - - - - - 176.5 -3.3 31.8 - +* +* 6 ASP 6 E B - 181.9 - - - - - - - - 182.8 - 35.2 - 7 LEU 7 E B - - -50.1 - - - - - - - 167.8 -3.4 38.7 - * ** +* * ** 8 GLU 8 E B - 178.2 - 179.1 - - - - - - 183.7 -.6 33.4 - +* +* 9 ILE 9 E B - - -53.9 - - - - - - - 174.7 -3.2 35.2 - +* +* 10 THR 10 E B 55.6 - - - - - - - - - 178.3 -2.6 33.3 - 11 THR 11 E B - - -43.2 - - - - - - - 178.9 - 35.9 - +* +* 12 ASN 12 e A - 183.7 - - - - - - - - 178.8 -1.2 33.7 - * * 13 ALA 13 S A - - - - - - - - - - 182.7 - 34.8 - 14 THR 14 B 57.2 - - - - - - - - - 176.1 - 34.3 - 15 ASP 15 S A - 181.2 - - - - - - - - 180.9 - 34.8 - 16 PHE 16 S B - - -63.7 - - - - - - - 173.6 - 34.8 - * * 17 PRO 17 - - - - - -67.3 - - - - - 184.7 - 39.0 - * * 18 MET 18 E B - 191.9 - 182.8 - - - - - - 179.4 -2.6 35.6 - 19 GLU 19 E B 60.2 - - 176.2 - - - - - - 178.9 - 33.7 - Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 LYS 20 E B - - -81.2 180.1 - - - - - - 175.9 -2.8 34.3 - * * 21 LYS 21 E B - - -107.6 - - - - - - - 175.8 - 37.0 - +** +** 22 TYR 22 E B - - -70.9 - - - - - - - 175.6 -2.6 32.9 - 23 PRO 23 E - - - - - -70.8 - - - - - 179.0 - 39.4 - +* +* 24 ALA 24 e A - - - - - - - - - - 180.1 -2.2 32.9 - 25 GLY 25 T - - - - - - - - - - - 177.8 -.7 - - +* +* 26 MET 26 t B - 174.8 - 178.1 - - - - - - 175.3 -1.6 34.6 - 27 SER 27 h B 55.7 - - - - - - - - - 176.9 - 36.5 - 28 LEU 28 H A - 209.4 - 186.5 - -59.8 -33.0 - - - 182.2 -1.0 35.6 - +* * +* 29 ASN 29 H A - - -69.5 - - -60.5 -39.8 - - - 182.9 -.5 32.2 - +* +* 30 ASP 30 H A - 199.8 - - - -75.0 -34.0 - - - 178.6 - 34.5 - 31 LEU 31 H A - 188.2 - 170.8 - -67.3 -45.1 - - - 174.4 -1.6 35.1 - 32 LYS 32 H A - - -79.6 - - -55.1 -52.8 - - - 182.8 -3.1 36.0 - * * * 33 LYS 33 H A - 196.5 - 177.7 - -60.9 -24.8 - - - 176.9 -2.8 36.1 - * * 34 LYS 34 H A - 224.7 - - - -77.3 -41.1 - - - 176.8 -1.1 35.8 - ** * * ** 35 LEU 35 H A - - -72.4 184.7 - -68.7 -51.3 - - - 180.6 -2.2 34.9 - * * 36 GLU 36 H A - - -64.2 - - -55.6 -30.8 - - - 175.9 -4.2 34.6 - +** +** 37 LEU 37 H A - 181.4 - - - -61.4 -38.6 - - - 180.6 -.8 34.9 - +* +* 38 VAL 38 H A - 181.7 - - - -89.2 -34.1 - - - 183.2 -1.5 35.2 - ** ** 39 VAL 39 H A - 180.7 - - - -80.2 -27.8 - - - 178.2 -3.1 33.3 - * * * * 40 GLY 40 h - - - - - - - - - - - 181.1 -2.6 - - 41 THR 41 b - - -51.7 - - - - - - - 176.4 - 34.2 - 42 THR 42 t B 42.7 - - - - - - - - - 188.2 - 32.3 - * * * 43 VAL 43 T A - 176.2 - - - - - - - - 183.7 - 32.9 - 44 ASP 44 T A - 183.1 - - - - - - - - 183.7 - 33.3 - 45 SER 45 e A - - -57.0 - - - - - - - 177.0 - 35.3 - 46 MET 46 E B - 196.0 - - - - - - - - 189.9 -.6 34.0 - +* +* +* 47 ARG 47 E B - 191.9 - - - - - - - - 185.2 -3.0 35.6 - * * 48 ILE 48 E B - - -59.9 - - - - - - - 180.0 - 34.8 - 49 GLN 49 E B - - -59.5 181.4 - - - - - - 180.4 -3.5 34.2 - ** ** 50 LEU 50 E B - 197.5 - 182.2 - - - - - - 175.0 -3.0 36.1 - * * 51 PHE 51 E B - - -64.9 - - - - - - - 182.2 -2.9 33.9 - * * 52 ASP 52 e b 64.2 - - - - - - - - - 183.3 -2.0 32.6 - 53 GLY 53 S - - - - - - - - - - - 179.4 - - - 54 ASP 54 S a - - -72.3 - - - - - - - 182.6 - 32.5 - 55 ASP 55 S ~a - 181.0 - - - - - - - - 182.6 - 34.2 - ** ** Residue-by-residue listing for refined_5 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 56 GLN 56 e B - - -63.1 - - - - - - - 180.4 - 32.8 - 57 LEU 57 E B - 179.6 - - - - - - - - 180.9 - 34.8 - 58 LYS 58 E A - 206.9 - - - - - - - - 179.2 -2.3 36.5 - * * 59 GLY 59 E - - - - - - - - - - - 179.2 -1.7 - - 60 GLU 60 E B - 183.7 - 173.2 - - - - - - 184.5 - 34.7 - 61 LEU 61 e a - - -70.3 - - - - - - - 170.6 -1.6 30.5 - +* +* 62 THR 62 l - - -51.6 - - - - - - - 181.0 - 32.8 - * * 63 ASP 63 B - - -58.6 - - - - - - - 178.2 - 34.7 - 64 GLY 64 - - - - - - - - - - - 174.6 - - - 65 ALA 65 S A - - - - - - - - - - 176.1 - 33.9 - 66 LYS 66 S B 52.7 - - 174.6 - - - - - - 183.6 - 33.6 - 67 SER 67 B B - - -47.1 - - - - - - - 175.7 - 36.5 - * * 68 LEU 68 T A - - -61.0 169.7 - - - - - - 180.3 -2.6 36.3 - 69 LYS 69 T A - 188.0 - 172.8 - - - - - - 174.9 -2.4 33.3 - 70 ASP 70 T A - 188.2 - - - - - - - - 180.1 - 35.3 - 71 LEU 71 T A - - -64.1 177.4 - - - - - - 177.7 -1.9 35.2 - 72 GLY 72 T - - - - - - - - - - - 181.9 -.8 - - +* +* 73 VAL 73 t B - 187.7 - - - - - - - - 181.4 -2.5 34.6 - 74 ARG 74 t b - - -63.1 184.2 - - - - - - 183.1 -.8 33.5 - +* +* 75 ASP 75 T B 60.2 - - - - - - - - - 178.8 - 33.1 - 76 GLY 76 T - - - - - - - - - - - 176.0 -2.2 - - 77 TYR 77 e B - - -68.0 - - - - - - - 185.6 -1.5 32.7 - 78 ARG 78 E B - - -57.5 183.9 - - - - - - 182.9 -2.9 33.4 - * * 79 ILE 79 E B - - -63.6 - - - - - - - 183.3 -1.1 32.7 - * * 80 HIS 80 E B - 175.4 - - - - - - - - 176.8 -3.4 35.9 - +* +* 81 ALA 81 E B - - - - - - - - - - 180.1 -3.1 33.9 - * * 82 VAL 82 E B 63.5 - - - - - - - - - 183.2 -2.5 33.4 - 83 ASP 83 E B - 178.3 - - - - - - - - 176.6 - 34.1 - 84 VAL 84 e A 66.2 - - - - - - - - - 179.6 -3.1 32.1 - * * 85 THR 85 T A - - -42.4 - - - - - - - 172.7 -.7 36.8 - +* * +* +* 86 GLY 86 T - - - - - - - - - - - 183.1 - - - 87 GLY 87 T - - - - - - - - - - - 177.6 - - - 88 ASN 88 t B 63.1 - - - - - - - - - 188.7 -2.5 29.4 - +* * +* 89 GLU 89 l - 175.2 - - - - - - - - 181.6 - 30.5 - 90 ASP 90 - - 179.7 - - - - - - - - - - 34.6 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * ** +** ** * ** +** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.1 187.3 -62.9 178.5 -69.1 -67.6 -37.8 - - - 179.7 -2.1 34.4 Standard deviations: 6.9 11.2 12.5 4.9 2.5 10.8 8.8 - - - 3.8 1.0 1.7 Numbers of values: 12 32 31 19 2 12 12 0 0 0 89 50 81 0 Residue-by-residue listing for refined_5 Page 4 ---------------------------------------- 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_5 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 MET 1 - 1.230 1.516 1.533 1.467 - 116.52 120.74 110.14 110.33 110.99 122.73 2 THR 2 1.321 1.242 1.526 1.537 1.428 121.27 115.23 121.56 110.84 109.21 110.30 123.18 +* +* 3 GLU 3 1.296 1.218 1.499 1.535 1.419 122.32 117.08 119.55 111.79 106.79 108.12 123.35 ** * ** +* * ** 4 VAL 4 1.298 1.238 1.508 1.575 1.451 122.87 115.64 121.10 110.04 110.11 113.33 123.23 ** * * ** 5 TYR 5 1.288 1.231 1.510 1.533 1.421 122.10 116.30 120.19 112.95 110.79 111.30 123.25 +** +* +* +** 6 ASP 6 1.320 1.249 1.505 1.515 1.462 121.94 115.35 120.81 108.49 108.95 111.15 123.85 7 LEU 7 1.282 1.229 1.499 1.541 1.410 123.28 116.27 120.46 103.95 108.36 111.14 123.26 *** * +** *** * *** 8 GLU 8 1.285 1.229 1.499 1.520 1.425 120.93 116.41 120.49 111.13 105.89 112.43 123.02 *** * +* +* * *** 9 ILE 9 1.285 1.241 1.499 1.557 1.434 121.18 115.52 120.70 108.33 109.65 111.80 123.77 *** * * *** 10 THR 10 1.288 1.224 1.495 1.552 1.420 122.05 116.02 121.13 109.40 109.00 113.77 122.85 +** * +* * +** 11 THR 11 1.262 1.223 1.504 1.543 1.409 121.87 116.30 120.47 108.90 105.71 111.14 123.23 *4.8* * +** +* *4.8* 12 ASN 12 1.262 1.232 1.523 1.545 1.454 121.78 115.03 121.70 111.40 108.88 110.82 123.25 *4.8* *4.8* Residue-by-residue listing for refined_5 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 ALA 13 1.323 1.234 1.524 1.520 1.446 122.94 117.04 120.32 109.26 111.95 110.19 122.63 14 THR 14 1.316 1.233 1.511 1.552 1.442 120.85 116.03 120.77 109.14 110.90 111.65 123.19 15 ASP 15 1.298 1.232 1.509 1.524 1.440 121.97 115.50 121.24 109.80 109.27 110.62 123.23 ** ** 16 PHE 16 1.313 1.238 1.518 1.536 1.449 122.10 117.62 120.24 108.43 111.08 111.45 122.12 * * 17 PRO 17 1.341 1.244 1.521 1.535 1.459 122.40 117.31 120.16 110.06 109.05 103.90 122.53 * * 18 MET 18 1.298 1.225 1.525 1.531 1.441 120.40 117.07 120.17 110.39 109.91 108.61 122.75 ** * ** 19 GLU 19 1.320 1.245 1.530 1.539 1.461 121.45 116.32 120.50 110.02 110.92 111.40 123.16 20 LYS 20 1.316 1.210 1.516 1.503 1.428 123.46 115.50 120.96 109.45 112.56 110.46 123.54 * * +* +* 21 LYS 21 1.308 1.243 1.525 1.526 1.424 124.79 117.17 120.20 107.54 109.19 109.51 122.62 * +* +* * +* 22 TYR 22 1.300 1.225 1.505 1.540 1.452 121.37 117.98 120.02 109.67 110.34 113.18 121.95 ** +* ** 23 PRO 23 1.335 1.223 1.513 1.534 1.450 122.47 116.78 120.40 109.03 111.15 104.18 122.81 * * * 24 ALA 24 1.315 1.232 1.535 1.517 1.460 121.10 115.26 121.73 111.64 111.07 110.51 122.97 25 GLY 25 1.310 1.225 1.523 - 1.453 121.63 116.45 120.74 - 112.58 - 122.80 * * 26 MET 26 1.318 1.232 1.540 1.551 1.455 122.10 116.46 120.55 111.02 110.50 109.33 122.97 * * 27 SER 27 1.321 1.243 1.501 1.529 1.445 122.98 116.67 120.41 109.07 108.75 109.00 122.92 * * 28 LEU 28 1.322 1.211 1.547 1.537 1.454 120.58 116.33 120.69 109.49 107.73 109.90 122.90 * * * 29 ASN 29 1.344 1.232 1.515 1.542 1.482 122.17 117.19 120.15 109.22 113.37 113.25 122.65 * * +* +* 30 ASP 30 1.317 1.232 1.521 1.523 1.464 120.60 115.04 121.43 110.10 108.93 110.50 123.46 31 LEU 31 1.332 1.234 1.521 1.562 1.462 122.84 114.68 121.54 111.98 107.19 108.77 123.78 +* * * +* 32 LYS 32 1.315 1.160 1.477 1.508 1.445 123.69 117.66 119.31 108.58 111.79 109.32 122.99 +*** ** * * +*** 33 LYS 33 1.300 1.230 1.540 1.474 1.431 122.55 116.14 121.10 110.84 111.31 106.38 122.75 ** +** * ** +** 34 LYS 34 1.322 1.232 1.535 1.527 1.447 122.12 115.27 121.42 109.36 108.09 109.67 123.31 * * 35 LEU 35 1.325 1.207 1.510 1.528 1.445 123.77 115.83 120.42 109.76 111.09 109.91 123.72 * * * 36 GLU 36 1.313 1.214 1.511 1.520 1.436 125.53 116.13 120.66 110.60 111.36 109.46 123.21 * * ** ** 37 LEU 37 1.311 1.228 1.544 1.535 1.453 122.41 115.88 121.06 110.18 110.37 109.52 123.06 * * 38 VAL 38 1.318 1.228 1.535 1.560 1.456 122.63 115.79 121.22 109.17 110.16 110.58 122.98 39 VAL 39 1.321 1.231 1.532 1.567 1.459 122.45 117.03 120.58 111.01 111.85 110.82 122.36 * * 40 GLY 40 1.315 1.230 1.519 - 1.444 120.43 117.06 120.30 - 112.90 - 122.64 41 THR 41 1.309 1.249 1.564 1.574 1.449 121.00 118.04 119.64 113.36 108.62 108.38 122.20 * +* * +* +* +* 42 THR 42 1.316 1.236 1.539 1.535 1.437 122.42 116.10 120.83 112.16 111.19 111.15 123.04 * * * 43 VAL 43 1.328 1.235 1.534 1.568 1.465 123.39 117.23 120.00 110.53 113.70 111.12 122.76 * * Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.306 1.238 1.523 1.526 1.457 121.34 116.01 120.94 110.81 112.08 110.57 123.01 +* +* 45 SER 45 1.309 1.236 1.537 1.483 1.421 122.69 116.84 121.17 110.61 112.99 107.48 121.99 * ** +* +* ** 46 MET 46 1.286 1.237 1.525 1.522 1.439 120.53 116.28 120.76 111.16 107.61 110.71 122.95 *** * *** 47 ARG 47 1.304 1.232 1.533 1.529 1.459 122.75 116.91 120.19 110.50 109.81 108.26 122.89 +* * +* 48 ILE 48 1.334 1.240 1.531 1.553 1.454 121.83 115.67 121.01 109.37 111.71 110.44 123.31 49 GLN 49 1.310 1.227 1.513 1.511 1.438 123.00 116.39 120.40 110.11 110.52 110.60 123.22 * * * 50 LEU 50 1.306 1.241 1.530 1.554 1.454 122.13 116.10 120.94 109.42 108.67 109.27 122.96 +* * +* 51 PHE 51 1.293 1.233 1.507 1.538 1.443 122.35 117.81 120.05 110.69 107.51 111.68 122.11 +** * +** 52 ASP 52 1.306 1.246 1.515 1.525 1.427 119.96 115.19 121.04 110.89 111.34 111.92 123.77 +* +* +* 53 GLY 53 1.312 1.233 1.523 - 1.457 122.70 117.46 120.20 - 114.32 - 122.35 * * * 54 ASP 54 1.315 1.227 1.499 1.521 1.443 120.97 116.57 120.06 110.48 111.92 112.20 123.35 * * * 55 ASP 55 1.326 1.221 1.500 1.544 1.467 122.51 115.39 120.61 108.81 110.55 112.08 123.99 * * 56 GLN 56 1.317 1.246 1.523 1.539 1.454 123.27 114.47 121.93 109.66 113.04 112.24 123.60 * * 57 LEU 57 1.301 1.236 1.505 1.540 1.435 122.76 115.95 120.82 110.30 108.76 110.41 123.23 +* * +* 58 LYS 58 1.296 1.224 1.528 1.538 1.437 121.47 115.12 121.72 110.35 105.93 108.28 123.14 ** * +* * ** 59 GLY 59 1.310 1.233 1.492 - 1.425 121.30 116.89 120.25 - 110.31 - 122.85 * * +* +* 60 GLU 60 1.285 1.240 1.517 1.535 1.410 122.15 117.54 119.57 113.60 106.20 108.14 122.86 *** +** +* +* * *** 61 LEU 61 1.321 1.228 1.486 1.550 1.463 120.49 114.52 120.83 112.52 111.40 113.31 124.63 +* * * +* * +* 62 THR 62 1.277 1.228 1.569 1.563 1.464 124.13 117.79 120.83 112.47 113.38 109.28 121.32 +*** ** * +* * * +*** 63 ASP 63 1.328 1.222 1.497 1.534 1.472 120.29 116.73 120.38 107.65 110.81 112.38 122.89 * * * * 64 GLY 64 1.306 1.226 1.486 - 1.442 119.91 116.45 120.22 - 112.36 - 123.32 +* +* +* 65 ALA 65 1.320 1.236 1.521 1.523 1.452 121.53 114.69 121.75 110.98 108.45 110.75 123.56 66 LYS 66 1.317 1.247 1.523 1.530 1.426 123.49 117.17 120.01 111.55 108.93 110.80 122.81 +* +* 67 SER 67 1.313 1.243 1.504 1.515 1.419 121.29 114.50 121.45 108.24 110.23 109.39 124.03 * * ** ** 68 LEU 68 1.293 1.234 1.523 1.515 1.439 123.85 115.10 121.62 110.71 109.52 107.21 123.22 +** * +* +** 69 LYS 69 1.319 1.232 1.528 1.536 1.441 122.26 116.79 120.48 112.13 109.82 110.26 122.72 * * 70 ASP 70 1.347 1.222 1.518 1.529 1.483 121.24 115.17 121.58 108.14 108.53 111.35 123.17 * * * * 71 LEU 71 1.324 1.232 1.526 1.538 1.468 122.35 116.02 120.75 108.81 110.66 110.47 123.23 72 GLY 72 1.321 1.234 1.500 - 1.440 121.68 116.30 120.64 - 112.00 - 123.06 Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 VAL 73 1.307 1.227 1.517 1.547 1.434 121.47 116.09 120.75 109.44 108.43 111.69 123.11 +* * +* 74 ARG 74 1.306 1.236 1.513 1.526 1.444 121.74 116.31 120.61 110.68 110.53 111.13 123.07 +* +* 75 ASP 75 1.315 1.241 1.489 1.519 1.453 122.25 113.87 122.07 109.75 112.38 111.93 124.03 * +* * +* 76 GLY 76 1.289 1.236 1.509 - 1.439 121.61 116.62 120.70 - 113.03 - 122.67 +** +** 77 TYR 77 1.311 1.235 1.499 1.528 1.429 120.95 116.55 120.66 111.35 108.19 112.57 122.77 * * +* * * +* 78 ARG 78 1.288 1.236 1.501 1.519 1.420 120.62 115.32 121.28 112.20 111.22 109.65 123.40 +** * +* * +** 79 ILE 79 1.297 1.225 1.507 1.552 1.426 121.97 114.88 121.55 111.70 110.21 111.82 123.56 ** +* * ** 80 HIS 80 1.281 1.216 1.515 1.524 1.418 123.27 116.28 120.71 110.42 110.71 108.12 123.01 *** ** * *** 81 ALA 81 1.292 1.237 1.527 1.521 1.430 121.77 116.67 120.60 111.55 109.44 110.06 122.71 +** * +** 82 VAL 82 1.304 1.238 1.530 1.566 1.440 122.05 116.33 120.48 111.67 109.06 111.17 123.15 +* * +* 83 ASP 83 1.305 1.231 1.506 1.532 1.459 121.93 115.95 121.38 109.07 111.81 111.51 122.67 +* +* 84 VAL 84 1.293 1.231 1.531 1.565 1.424 120.79 114.85 122.41 112.82 108.67 112.05 122.65 +** +* +* +** 85 THR 85 1.323 1.229 1.521 1.540 1.449 121.44 114.93 121.70 107.39 108.10 110.26 123.36 * * 86 GLY 86 1.306 1.235 1.490 - 1.430 121.44 114.17 121.64 - 108.78 - 124.18 +* * * * * +* 87 GLY 87 1.323 1.241 1.505 - 1.442 121.88 117.44 120.15 - 112.81 - 122.41 88 ASN 88 1.319 1.237 1.499 1.556 1.440 119.37 116.06 119.94 113.55 109.37 114.77 123.99 * * * +* +** +** 89 GLU 89 1.319 1.242 1.522 1.555 1.454 122.96 113.94 122.62 113.15 108.54 113.80 123.21 * * * +* +* +* 90 ASP 90 1.296 - 1.492 1.532 1.431 123.26 - - 110.53 107.74 110.76 - ** +* * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.8* +*** ** +** +** ** * * *** +* +** * *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 87 1.262 1.347 1.308 .016 *4.8* * * C-N (Pro) 1.341 .016 2 1.335 1.341 1.338 .003 C-O C-O 1.231 .020 89 1.160 1.249 1.232 .011 +*** CA-C CH1E-C (except Gly) 1.525 .021 81 1.477 1.569 1.518 .016 ** ** CH2G*-C (Gly) 1.516 .018 9 1.486 1.523 1.505 .014 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.517 1.523 1.520 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.535 1.575 1.556 .012 * CH1E-CH2E (the rest) 1.530 .020 59 1.474 1.562 1.530 .015 +** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 79 1.409 1.483 1.444 .017 +** * NH1-CH2G* (Gly) 1.451 .016 9 1.425 1.457 1.441 .009 +* N-CH1E (Pro) 1.466 .015 2 1.450 1.459 1.454 .004 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 78 113.87 118.04 116.07 .94 * CH2G*-C-NH1 (Gly) 116.4 2.1 9 114.17 117.46 116.54 .93 * CH1E-C-N (Pro) 116.9 1.5 2 116.78 117.31 117.04 .26 O-C-N O-C-NH1 (except Pro) 123.0 1.6 87 121.32 124.63 123.07 .52 * * O-C-N (Pro) 122.0 1.4 2 122.53 122.81 122.67 .14 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 78 119.37 125.53 122.07 1.10 * ** C-NH1-CH2G* (Gly) 120.6 1.7 9 119.91 122.70 121.40 .76 * C-N-CH1E (Pro) 122.6 5.0 2 122.40 122.47 122.44 .03 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 80 119.31 122.62 120.80 .65 * CH2G*-C-O (Gly) 120.8 2.1 9 120.15 121.64 120.54 .45 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.26 111.64 110.86 .96 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.39 113.36 110.43 1.63 +* CH2E-CH1E-C (the rest) 110.1 1.9 59 103.95 113.60 110.21 1.59 *** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 79 105.71 113.70 109.89 1.80 +* NH1-CH2G*-C (Gly) 112.5 2.9 9 108.78 114.32 112.12 1.54 * N-CH1E-C (Pro) 111.8 2.5 2 109.05 111.15 110.10 1.05 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 110.06 110.75 110.38 .27 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.38 113.77 111.15 1.23 +* * N-CH1E-CH2E (Pro) 103.0 1.1 2 103.90 104.18 104.04 .14 * NH1-CH1E-CH2E (the rest) 110.5 1.7 57 106.38 114.77 110.52 1.71 ** +** ------------------------------------------------------------------------------------------------------------- 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_5 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] 69 89.6% Residues in additional allowed regions [a,b,l,p] 7 9.1% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.3% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 77 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 9 Number of proline residues 2 ---- Total number of residues 90 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 77 89.6 83.8 10.0 .6 Inside b. Omega angle st dev 89 3.8 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 81 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 50 1.0 .8 .2 .8 Inside f. Overall G-factor 90 .0 -.4 .3 1.1 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 32 11.2 19.0 5.3 -1.5 BETTER c. Chi-1 gauche plus st dev 31 12.5 17.5 4.9 -1.0 BETTER d. Chi-1 pooled st dev 75 11.8 18.2 4.8 -1.3 BETTER e. Chi-2 trans st dev 19 4.9 20.4 5.0 -3.1 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% 89.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 13.1 2 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .97 3 Residue-by-residue listing for refined_5 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.39 Chi1-chi2 distribution -.29 Chi1 only -.18 Chi3 & chi4 .47 Omega -.06 ------ -.15 ===== Main-chain covalent forces:- Main-chain bond lengths -.18 Main-chain bond angles .40 ------ .16 ===== OVERALL AVERAGE -.05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.