Residue-by-residue listing for refined_2 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 - - - -57.7 - - - - - - - 181.6 - 34.6 - 2 ALA 2 B - - - - - - - - - - 177.5 - 34.4 - 3 ASP 3 B - - -60.9 - - - - - - - 182.2 - 34.6 - 4 THR 4 a - - -51.8 - - - - - - - 179.4 -1.0 34.0 - * * 5 GLY 5 - - - - - - - - - - - 182.5 - - - 6 GLU 6 B 57.5 - - 189.3 - - - - - - 183.0 -.6 32.8 - +* +* 7 VAL 7 E B - - -65.2 - - - - - - - 179.8 -1.5 33.4 - 8 GLN 8 E B 55.5 - - 173.8 - - - - - - 178.2 - 35.2 - 9 PHE 9 E B 60.0 - - - - - - - - - 180.7 -2.3 32.3 - 10 MET 10 E B 64.9 - - 179.0 - - - - - - 179.3 - 33.6 - 11 LYS 11 E B - - -75.0 172.9 - - - - - - 172.8 -1.6 34.0 - * * 12 PRO 12 E - - - - - -69.6 - - - - - 183.4 - 38.9 - * * 13 PHE 13 e B - 176.6 - - - - - - - - 175.0 -1.2 35.2 - * * 14 ILE 14 t B - - -65.4 - - - - - - - 184.1 - 33.7 - 15 SER 15 T A 50.0 - - - - - - - - - 180.5 -.7 32.2 - +* +* 16 GLU 16 T A - 196.5 - - - - - - - - 189.1 - 34.5 - +* +* 17 LYS 17 T a - - -64.3 178.6 - - - - - - 185.1 - 33.8 - 18 SER 18 T A - - -45.5 - - - - - - - 181.1 -1.7 35.3 - * * 19 SER 19 T A - 186.9 - - - - - - - - 183.1 -.7 33.7 - +* +* Residue-by-residue listing for refined_2 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 T a - - -56.2 174.3 - - - - - - 179.3 -1.6 35.1 - 21 SER 21 t B - - -56.6 - - - - - - - 179.0 -1.3 36.3 - * * 22 LEU 22 E B - 198.6 - 176.2 - - - - - - 182.1 -3.3 34.2 - +* +* 23 GLU 23 E B 51.0 - - 177.3 - - - - - - 177.4 -.5 34.1 - ** ** 24 ILE 24 E B - - -69.3 - - - - - - - 179.6 -2.1 32.8 - 25 PRO 25 h - - - - - -51.2 - - - - - 182.1 - 38.8 - * * * 26 LEU 26 H A - - -66.0 - - -65.0 -39.8 - - - 179.3 - 33.4 - 27 GLY 27 H - - - - - - -66.9 -24.5 - - - 181.6 - - - * * 28 PHE 28 H A - 189.7 - - - -76.9 -30.5 - - - 175.7 - 33.3 - 29 ASN 29 H A - 182.3 - - - -60.8 -47.2 - - - 182.6 -1.2 36.9 - * * 30 GLU 30 H A - 180.5 - 183.8 - -65.2 -30.6 - - - 183.8 -1.5 36.8 - 31 TYR 31 H A - 182.3 - - - -69.2 -27.2 - - - 180.7 -1.1 33.0 - * * * 32 PHE 32 h b 70.9 - - - - - - - - - 160.8 -1.0 30.6 - *** * *** 33 PRO 33 - - - - - -56.8 - - - - - 186.7 - 38.7 - * * * 34 ALA 34 B - - - - - - - - - - 169.9 - 35.3 - +* +* 35 PRO 35 S - - - - - -56.5 - - - - - 189.2 - 39.4 - +* +* +* 36 PHE 36 B - - -64.2 - - - - - - - 176.5 - 33.8 - 37 PRO 37 - - - - - -87.8 - - - - - 178.4 - 38.9 - ** * ** 38 ILE 38 e a - - -56.7 - - - - - - - 178.2 - 34.2 - 39 THR 39 E B 54.4 - - - - - - - - - 181.6 - 33.9 - 40 VAL 40 E B - - -64.1 - - - - - - - 181.5 -3.2 34.7 - +* +* 41 ASP 41 E B - - -64.9 - - - - - - - 178.4 -2.9 32.5 - * * 42 LEU 42 E B - - -61.0 183.9 - - - - - - 177.7 -3.0 35.6 - * * 43 LEU 43 E B - - -62.6 - - - - - - - 177.6 -3.4 35.2 - +* +* 44 ASP 44 E B 93.4 - - - - - - - - - 182.8 -2.4 34.2 - +* +* 45 TYR 45 e A - 185.9 - - - - - - - - 178.8 -.9 34.4 - * * 46 SER 46 T A - - -49.1 - - - - - - - 177.6 - 35.4 - * * 47 GLY 47 t - - - - - - - - - - - 181.7 -1.8 - - 48 ARG 48 e B - - -73.9 - - - - - - - 181.6 - 30.9 - 49 SER 49 E B 53.6 - - - - - - - - - 175.7 - 33.2 - 50 TRP 50 E B - - -68.7 - - - - - - - 176.6 -2.3 34.7 - 51 THR 51 E B - - -52.9 - - - - - - - 186.6 - 34.2 - * * 52 VAL 52 E B - 185.8 - - - - - - - - 178.1 -3.4 35.9 - +* +* 53 ARG 53 E B - - -63.2 183.2 - - - - - - 183.7 -2.5 34.2 - 54 MET 54 E B - 177.9 - 179.9 - - - - - - 177.8 -1.5 35.6 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 LYS 55 E B - - -64.7 - - - - - - - 168.0 -2.5 34.9 - ** ** 56 LYS 56 E B - - -54.1 209.3 - - - - - - 186.6 - 33.8 - +* * +* 57 ARG 57 E B - 183.7 - 172.2 - - - - - - 180.9 -2.5 33.2 - 58 GLY 58 T - - - - - - - - - - - 180.5 -.6 - - +* +* 59 GLU 59 T A - - -62.4 175.6 - - - - - - 182.5 -.6 34.7 - +* +* 60 LYS 60 E B 57.4 - - 187.5 - - - - - - 179.4 -1.6 34.5 - 61 VAL 61 E B - 177.6 - - - - - - - - 176.2 -1.2 34.3 - * * 62 PHE 62 E B - - -65.5 - - - - - - - 174.6 -2.5 33.4 - 63 LEU 63 E B - 191.0 - - - - - - - - 192.8 -2.3 36.4 - ** ** 64 THR 64 e a 55.2 - - - - - - - - - 185.3 -1.6 31.5 - 65 VAL 65 T B 59.1 - - - - - - - - - 184.2 - 31.6 - 66 GLY 66 h - - - - - - - - - - - 175.4 - - - 67 TRP 67 H A - 165.8 - - - -64.2 -31.3 - - - 180.5 -.9 34.9 - * * * 68 GLU 68 H A 58.0 - - 179.6 - -69.5 -26.1 - - - 177.7 -.7 31.7 - * +* +* 69 ASN 69 H A - - -61.8 - - -72.6 -33.1 - - - 180.8 -.5 34.9 - ** ** 70 PHE 70 H A - 181.9 - - - -73.8 -50.9 - - - 183.2 -1.2 35.8 - * * * 71 VAL 71 H A 68.8 - - - - -61.0 -43.8 - - - 179.3 -3.0 33.3 - * * 72 LYS 72 H A - - -61.2 - - -71.4 -34.3 - - - 183.8 -1.9 32.1 - 73 ASP 73 H A - 182.5 - - - -62.4 -41.1 - - - 177.6 -1.5 34.1 - 74 ASN 74 H A - 172.7 - - - -93.6 -20.4 - - - 191.8 -1.7 36.5 - ** +* ** ** 75 ASN 75 h l - 185.9 - - - - - - - - 179.5 -1.2 29.2 - * * * 76 LEU 76 t B 60.4 - - - - - - - - - 188.9 -1.8 28.5 - +* +* +* 77 GLU 77 t B 53.7 - - 181.3 - - - - - - 178.5 - 35.0 - 78 ASP 78 T B - 178.5 - - - - - - - - 183.9 - 35.5 - 79 GLY 79 T - - - - - - - - - - - 174.8 - - - 80 LYS 80 e B - - -64.7 180.4 - - - - - - 183.0 -2.4 33.8 - 81 TYR 81 E B - - -58.3 - - - - - - - 180.4 -1.9 34.0 - 82 LEU 82 E B 52.9 - - - - - - - - - 171.9 -1.1 31.5 - * * * 83 GLN 83 E B - - -73.9 177.8 - - - - - - 185.0 -1.6 31.9 - 84 PHE 84 E B - 187.7 - - - - - - - - 183.2 -3.1 36.4 - * * 85 ILE 85 E B - - -54.8 179.2 - - - - - - 177.4 -2.9 35.3 - * * 86 TYR 86 E B - 176.7 - - - - - - - - 183.0 -3.1 34.9 - * * 87 ASP 87 e A - - -57.9 - - - - - - - 186.8 -1.5 36.2 - * * 88 ARG 88 S l - - -60.5 - - - - - - - 178.9 - 32.0 - 89 ASP 89 S b - 194.9 - - - - - - - - 181.5 - 36.0 - 90 ARG 90 e A 66.5 - - 181.8 - - - - - - 180.0 - 33.8 - 91 THR 91 E B 51.9 - - - - - - - - - 174.4 - 34.5 - 92 PHE 92 E B - - -58.7 - - - - - - - 177.6 -2.1 35.3 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 TYR 93 E B - - -67.4 - - - - - - - 180.0 -1.9 33.6 - 94 VAL 94 E B - 184.7 - - - - - - - - 177.7 -3.0 34.8 - * * 95 ILE 95 E B - - -61.8 - - - - - - - 184.1 -2.0 32.9 - 96 ILE 96 E B - - -55.3 175.6 - - - - - - 176.5 -.6 35.6 - +* +* 97 TYR 97 E B - - -56.7 - - - - - - - 188.5 -3.7 33.3 - * ** ** 98 GLY 98 S - - - - - - - - - - - 185.1 -.8 - - +* +* 99 HIS 99 B - 195.6 - - - - - - - - 184.8 - 34.0 - 100 ASN 100 S XX - - -64.5 - - - - - - - 183.9 - 29.8 - **** * **** 101 MET 101 B - 179.7 - 181.4 - - - - - - 177.9 - 34.5 - 102 CYS 102 - 49.0 - - - - - - - - - - -1.1 31.5 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* * * +* ** ** +* *** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.2 183.9 -61.5 180.6 -64.4 -69.5 -34.3 - - - 180.5 -1.8 34.2 Standard deviations: 9.9 7.6 6.4 7.5 14.8 8.5 9.0 - - - 4.7 .9 2.0 Numbers of values: 21 26 41 24 5 14 14 0 0 0 101 64 95 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_2 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 - 1.232 1.513 1.548 1.459 - 117.09 120.15 109.14 109.03 111.73 122.71 2 ALA 2 1.317 1.234 1.511 1.530 1.450 121.55 116.37 120.63 109.88 110.79 110.56 123.00 3 ASP 3 1.311 1.226 1.513 1.543 1.455 121.30 117.18 120.49 108.90 108.17 112.12 122.24 * * * 4 THR 4 1.310 1.243 1.546 1.550 1.458 120.38 116.24 120.92 111.08 111.51 109.71 122.82 * * * * 5 GLY 5 1.326 1.233 1.497 - 1.449 120.99 114.85 121.38 - 112.39 - 123.76 * * 6 GLU 6 1.282 1.243 1.527 1.537 1.448 123.11 115.98 120.80 112.74 110.90 110.00 123.20 *** * *** 7 VAL 7 1.323 1.238 1.518 1.569 1.461 122.76 116.47 120.61 109.51 110.72 112.69 122.91 * * 8 GLN 8 1.312 1.237 1.522 1.514 1.423 122.08 116.58 120.78 109.57 110.87 109.64 122.63 * +* +* 9 PHE 9 1.301 1.238 1.518 1.548 1.461 121.45 117.03 120.16 111.64 110.73 111.88 122.80 ** ** 10 MET 10 1.320 1.230 1.509 1.536 1.452 121.00 115.97 120.82 109.76 110.84 111.84 123.20 11 LYS 11 1.305 1.237 1.516 1.546 1.450 122.78 117.66 120.07 109.84 110.75 111.39 122.21 +* +* 12 PRO 12 1.346 1.232 1.521 1.540 1.454 122.06 116.43 120.68 110.01 109.06 104.21 122.89 * * * Residue-by-residue listing for refined_2 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 PHE 13 1.287 1.232 1.532 1.532 1.439 122.16 117.35 120.13 110.72 111.37 108.40 122.52 *** * *** 14 ILE 14 1.339 1.235 1.513 1.587 1.429 120.79 116.42 120.26 109.91 106.42 113.75 123.31 +* +* +* * +* 15 SER 15 1.314 1.234 1.536 1.530 1.456 122.96 116.75 120.43 112.41 113.86 109.83 122.79 * * * 16 GLU 16 1.316 1.226 1.547 1.555 1.436 121.43 118.12 120.02 111.50 110.23 109.14 121.73 * * * * 17 LYS 17 1.343 1.232 1.488 1.515 1.473 118.83 116.45 120.61 109.01 113.65 111.14 122.88 * +* +* +* 18 SER 18 1.303 1.194 1.538 1.528 1.430 121.10 116.71 120.84 110.26 109.97 109.08 122.44 +* +* * +* 19 SER 19 1.327 1.228 1.542 1.538 1.451 122.35 117.62 120.25 110.75 112.51 110.07 122.12 20 LYS 20 1.325 1.229 1.520 1.534 1.477 120.11 115.89 121.27 109.80 110.66 109.58 122.83 21 SER 21 1.289 1.236 1.507 1.533 1.428 122.86 117.49 119.70 109.42 106.78 109.44 122.81 +** +* +* +** 22 LEU 22 1.298 1.242 1.508 1.552 1.429 120.25 115.12 121.03 111.55 105.75 111.10 123.76 ** * +* +* ** 23 GLU 23 1.282 1.233 1.536 1.529 1.422 123.09 116.06 121.44 111.97 111.59 108.70 122.46 *** +* * *** 24 ILE 24 1.306 1.246 1.538 1.577 1.441 121.31 117.31 120.24 110.40 109.24 113.26 122.39 +* * * +* 25 PRO 25 1.358 1.244 1.540 1.530 1.475 123.60 115.52 121.28 110.01 113.31 103.21 123.18 * * 26 LEU 26 1.321 1.237 1.520 1.555 1.457 122.98 115.72 121.19 110.07 110.76 111.99 123.07 * * 27 GLY 27 1.315 1.236 1.514 - 1.444 120.82 116.12 120.61 - 112.46 - 123.24 28 PHE 28 1.322 1.215 1.535 1.545 1.445 121.90 116.90 120.32 112.55 109.43 109.99 122.74 * * 29 ASN 29 1.350 1.245 1.512 1.555 1.491 121.72 113.49 121.89 107.19 108.11 110.34 124.57 +* * +* * +* * +* 30 GLU 30 1.311 1.244 1.514 1.514 1.439 124.59 115.08 121.16 109.30 110.70 107.59 123.76 * * +* +* +* 31 TYR 31 1.311 1.230 1.525 1.542 1.422 122.43 118.66 119.70 111.71 112.07 110.47 121.62 * +* * +* 32 PHE 32 1.335 1.232 1.549 1.566 1.451 117.62 118.79 121.23 111.17 115.58 112.53 119.60 * +* ** * +* * ** ** 33 PRO 33 1.336 1.254 1.515 1.515 1.441 120.68 115.39 121.11 109.52 108.65 104.89 123.49 * +* * * +* * +* 34 ALA 34 1.270 1.242 1.503 1.530 1.441 121.81 118.46 119.12 110.26 109.84 109.29 122.39 **** * * **** 35 PRO 35 1.356 1.234 1.519 1.530 1.451 121.24 117.20 119.88 109.74 106.92 103.97 122.91 +* +* 36 PHE 36 1.293 1.235 1.523 1.518 1.420 122.44 116.90 120.89 111.29 113.03 109.25 122.17 +** +* +** 37 PRO 37 1.339 1.233 1.523 1.532 1.441 122.67 116.93 120.66 110.81 110.31 103.19 122.39 +* +* 38 ILE 38 1.301 1.240 1.510 1.550 1.444 120.31 115.55 121.49 109.90 108.50 111.89 122.94 +* +* 39 THR 39 1.303 1.240 1.508 1.546 1.420 120.90 115.54 120.80 110.28 109.71 111.69 123.66 +* ** ** 40 VAL 40 1.287 1.232 1.507 1.559 1.438 124.03 117.47 119.92 109.59 108.14 111.65 122.60 *** * * * *** 41 ASP 41 1.295 1.241 1.501 1.537 1.442 120.36 115.35 121.24 110.49 111.51 112.52 123.41 ** * * ** Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 LEU 42 1.302 1.226 1.489 1.533 1.434 122.31 115.75 120.51 107.81 108.78 111.76 123.72 +* +* * * +* 43 LEU 43 1.287 1.237 1.503 1.556 1.426 122.29 117.16 120.16 108.85 107.71 111.84 122.67 *** * * +* * *** 44 ASP 44 1.297 1.231 1.503 1.551 1.443 119.32 115.18 120.84 108.87 108.57 112.85 123.98 ** * * * * ** 45 TYR 45 1.298 1.226 1.553 1.527 1.458 124.38 117.30 120.56 111.00 112.74 108.61 122.14 ** * * * ** 46 SER 46 1.320 1.237 1.531 1.517 1.455 121.60 115.54 121.34 109.54 109.44 109.49 123.10 47 GLY 47 1.319 1.235 1.507 - 1.434 121.65 117.48 120.11 - 113.40 - 122.42 * * 48 ARG 48 1.323 1.233 1.490 1.548 1.456 120.65 116.36 120.30 112.07 110.59 113.59 123.33 +* * +* +* 49 SER 49 1.302 1.242 1.529 1.534 1.426 120.57 115.10 121.32 111.91 112.28 109.91 123.54 +* +* +* 50 TRP 50 1.308 1.225 1.520 1.551 1.467 123.14 117.01 120.24 108.67 109.87 111.76 122.75 +* * +* 51 THR 51 1.307 1.243 1.535 1.532 1.442 121.51 115.71 121.20 110.30 108.72 110.95 123.08 +* +* 52 VAL 52 1.297 1.219 1.530 1.555 1.445 123.33 117.61 120.05 109.73 109.91 109.12 122.33 ** * ** 53 ARG 53 1.317 1.238 1.515 1.529 1.450 121.13 115.49 120.98 109.39 109.72 111.72 123.53 54 MET 54 1.311 1.225 1.501 1.532 1.454 122.95 116.95 120.39 109.15 110.41 109.72 122.65 * * * 55 LYS 55 1.313 1.234 1.514 1.543 1.450 120.06 117.03 120.39 106.73 112.25 112.63 122.57 * +* * +* 56 LYS 56 1.325 1.237 1.497 1.525 1.424 119.77 116.50 120.62 107.99 105.34 114.98 122.87 * +* * * ** +** +** 57 ARG 57 1.267 1.230 1.510 1.539 1.427 121.02 115.05 121.27 112.95 110.23 109.62 123.62 **** +* * **** 58 GLY 58 1.309 1.234 1.491 - 1.425 121.48 115.96 120.74 - 111.03 - 123.28 * * +* +* 59 GLU 59 1.293 1.219 1.520 1.518 1.435 121.83 116.60 120.77 110.35 110.84 109.54 122.63 +** * +** 60 LYS 60 1.315 1.232 1.533 1.528 1.443 122.02 117.03 120.46 111.59 110.82 108.64 122.48 * * 61 VAL 61 1.316 1.237 1.506 1.566 1.456 121.82 116.00 120.73 108.80 109.68 112.60 123.26 62 PHE 62 1.301 1.242 1.489 1.531 1.423 121.47 115.05 121.35 109.63 110.00 112.79 123.57 ** +* +* * ** 63 LEU 63 1.279 1.220 1.521 1.518 1.420 121.73 117.75 119.96 110.27 104.24 108.82 122.25 +*** ** ** +*** 64 THR 64 1.303 1.242 1.538 1.549 1.446 119.97 115.67 121.45 111.22 116.00 111.26 122.87 +* +* +* 65 VAL 65 1.300 1.236 1.512 1.561 1.443 122.41 115.19 121.28 112.12 111.25 112.46 123.52 ** * ** 66 GLY 66 1.312 1.221 1.482 - 1.424 121.33 114.85 121.43 - 109.58 - 123.70 * +* +* * +* 67 TRP 67 1.318 1.235 1.501 1.530 1.439 122.61 114.49 121.93 110.56 108.79 109.92 123.48 * * * 68 GLU 68 1.302 1.211 1.544 1.531 1.431 120.93 115.97 121.35 112.93 109.90 111.60 122.64 +* * * +* 69 ASN 69 1.323 1.217 1.517 1.549 1.465 122.75 114.74 121.58 109.50 109.30 110.80 123.67 70 PHE 70 1.309 1.240 1.516 1.549 1.447 124.54 115.00 121.28 109.87 109.40 109.13 123.72 * +* +* Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.335 1.210 1.505 1.565 1.447 122.31 115.82 120.62 110.33 110.53 112.25 123.57 * * 72 LYS 72 1.311 1.233 1.525 1.537 1.448 122.07 117.39 119.67 110.99 112.31 112.13 122.92 * * 73 ASP 73 1.349 1.236 1.527 1.530 1.495 120.70 116.20 121.05 109.16 112.42 110.86 122.74 * +* +* 74 ASN 74 1.304 1.243 1.499 1.551 1.472 121.99 113.36 121.85 108.43 109.14 109.59 124.68 +* * * * * +* 75 ASN 75 1.304 1.241 1.508 1.531 1.435 124.29 115.10 122.36 113.13 109.32 115.21 122.27 +* * * +* +** +** 76 LEU 76 1.295 1.227 1.502 1.565 1.405 120.12 115.04 121.26 116.60 109.58 113.11 123.65 ** * +* +** *** +* *** 77 GLU 77 1.284 1.241 1.504 1.526 1.428 123.01 115.22 120.34 110.66 111.15 108.96 124.43 *** +* *** 78 ASP 78 1.324 1.236 1.526 1.536 1.460 123.29 116.86 120.40 110.16 108.93 109.21 122.70 79 GLY 79 1.302 1.247 1.508 - 1.446 120.63 115.46 121.16 - 110.46 - 123.38 +* +* 80 LYS 80 1.324 1.239 1.516 1.546 1.442 122.13 116.71 120.45 110.50 107.95 111.89 122.83 * * 81 TYR 81 1.304 1.226 1.479 1.526 1.444 121.08 116.74 120.24 110.52 109.33 111.17 123.00 +* ** ** 82 LEU 82 1.289 1.244 1.509 1.552 1.416 120.37 115.10 121.23 113.29 112.77 110.82 123.62 +** * ** +* +** 83 GLN 83 1.300 1.238 1.490 1.536 1.433 122.30 114.96 120.83 112.28 108.19 112.87 124.19 ** +* * * * * ** 84 PHE 84 1.296 1.239 1.516 1.538 1.428 122.93 116.13 120.58 111.81 107.87 106.74 123.26 ** +* * ** ** 85 ILE 85 1.307 1.231 1.520 1.557 1.448 122.08 116.27 120.41 108.56 110.21 111.00 123.31 +* +* 86 TYR 86 1.313 1.237 1.543 1.544 1.449 122.12 116.34 120.57 111.73 109.82 108.35 123.05 * * * 87 ASP 87 1.346 1.222 1.515 1.546 1.495 122.56 116.54 120.06 105.86 111.80 111.65 123.39 * +* ** ** 88 ARG 88 1.328 1.233 1.525 1.545 1.490 123.70 115.38 121.46 109.91 110.13 114.02 123.14 +* * ** ** 89 ASP 89 1.306 1.232 1.529 1.552 1.428 123.37 118.56 119.54 111.43 104.34 108.57 121.87 +* * +* * ** * ** 90 ARG 90 1.282 1.232 1.528 1.538 1.456 120.92 115.62 121.30 110.69 109.92 110.79 123.08 *** *** 91 THR 91 1.313 1.248 1.523 1.541 1.431 122.52 115.65 120.93 109.73 111.36 110.61 123.30 * * * 92 PHE 92 1.312 1.231 1.515 1.522 1.436 122.63 117.16 120.12 108.76 108.56 111.04 122.71 * * * 93 TYR 93 1.301 1.237 1.506 1.535 1.458 121.45 116.44 120.33 110.03 109.83 111.87 123.22 ** ** 94 VAL 94 1.312 1.238 1.529 1.556 1.443 121.63 116.37 120.87 108.91 109.80 111.55 122.75 * * 95 ILE 95 1.315 1.235 1.524 1.582 1.454 121.37 116.19 120.43 109.83 108.46 113.97 123.38 * +* * +* 96 ILE 96 1.321 1.235 1.524 1.557 1.455 122.62 116.12 120.92 108.78 110.25 110.38 122.95 97 TYR 97 1.301 1.249 1.493 1.519 1.440 122.31 114.53 121.30 111.97 107.89 111.12 124.16 ** +* * ** 98 GLY 98 1.288 1.232 1.497 - 1.419 122.29 115.01 121.36 - 107.35 - 123.60 +** * +* +* +** Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 HIS 99 1.322 1.241 1.543 1.554 1.450 123.25 116.46 119.97 112.29 109.53 109.23 123.56 * * * 100 ASN 100 1.332 1.245 1.504 1.554 1.478 125.28 115.53 121.15 111.84 110.08 115.36 123.29 * * * +* +** +** 101 MET 101 1.296 1.237 1.521 1.536 1.439 122.52 115.84 121.17 110.65 110.89 109.75 122.99 ** ** 102 CYS 102 1.298 - 1.524 1.546 1.423 122.58 - - 113.78 110.09 111.31 - ** +* +* ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** +* +** ** * *** ** +** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 96 1.267 1.350 1.309 .016 **** +* * C-N (Pro) 1.341 .016 5 1.336 1.358 1.347 .009 * C-O C-O 1.231 .020 101 1.194 1.254 1.234 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.479 1.553 1.518 .015 ** * CH2G*-C (Gly) 1.516 .018 7 1.482 1.514 1.500 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.530 1.530 1.530 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.532 1.587 1.559 .014 +* CH1E-CH2E (the rest) 1.530 .020 75 1.514 1.566 1.537 .012 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.405 1.495 1.445 .018 +** +* NH1-CH2G* (Gly) 1.451 .016 7 1.419 1.449 1.434 .011 +* * N-CH1E (Pro) 1.466 .015 5 1.441 1.475 1.452 .013 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 89 113.36 118.79 116.25 1.06 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.85 117.48 115.68 .88 CH1E-C-N (Pro) 116.9 1.5 5 115.39 117.20 116.29 .73 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 119.60 124.68 123.02 .69 ** * O-C-N (Pro) 122.0 1.4 5 122.39 123.49 122.97 .37 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.62 125.28 121.91 1.30 ** +* C-NH1-CH2G* (Gly) 120.6 1.7 7 120.63 122.29 121.31 .52 C-N-CH1E (Pro) 122.6 5.0 5 120.68 123.60 122.05 1.03 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.12 122.36 120.72 .58 CH2G*-C-O (Gly) 120.8 2.1 7 120.11 121.43 120.97 .46 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 109.88 110.26 110.07 .19 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.56 112.12 109.94 .89 * CH2E-CH1E-C (the rest) 110.1 1.9 75 105.86 116.60 110.52 1.69 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.24 116.00 110.03 1.99 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 107.35 113.40 110.95 1.90 +* N-CH1E-C (Pro) 111.8 2.5 5 106.92 113.31 109.65 2.13 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.29 110.56 109.92 .64 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.12 113.97 111.71 1.28 * * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.19 104.89 103.89 .64 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.74 115.36 110.79 1.76 ** +** ------------------------------------------------------------------------------------------------------------- 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_2 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] 78 88.6% 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] 1 1.1% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 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 88.6 83.8 10.0 .5 Inside b. Omega angle st dev 101 4.7 6.0 3.0 -.4 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 64 .9 .8 .2 .3 Inside f. Overall G-factor 102 -.1 -.4 .3 1.0 Inside 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 21 9.9 18.1 6.5 -1.3 BETTER b. Chi-1 trans st dev 26 7.6 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 41 6.4 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 88 8.8 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 24 7.5 20.4 5.0 -2.6 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% 88.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 3 Residue-by-residue listing for refined_2 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.43 Chi1-chi2 distribution -.41 Chi1 only -.10 Chi3 & chi4 .50 Omega -.22 ------ -.23 ===== Main-chain covalent forces:- Main-chain bond lengths -.16 Main-chain bond angles .36 ------ .14 ===== OVERALL AVERAGE -.10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.