Residue-by-residue listing for refined_7 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 - - - -60.5 179.8 - - - - - - 180.5 - 33.4 - 2 ALA 2 B - - - - - - - - - - 177.5 - 33.6 - 3 ASP 3 b - 176.6 - - - - - - - - 176.4 -.7 33.8 - +* +* 4 THR 4 S A - - -47.1 - - - - - - - 180.3 -.7 35.8 - * +* +* 5 GLY 5 S - - - - - - - - - - - 179.7 - - - 6 GLU 6 l - 182.7 - 177.2 - - - - - - 176.5 - 30.7 - 7 VAL 7 E B - - -64.2 - - - - - - - 185.2 -2.9 32.0 - * * 8 GLN 8 E B 54.4 - - 188.5 - - - - - - 181.0 - 33.9 - 9 PHE 9 E B - 178.5 - - - - - - - - 181.7 -1.7 35.6 - 10 MET 10 E B - - -60.3 - - - - - - - 174.8 - 34.4 - 11 LYS 11 E B - 191.5 - 186.2 - - - - - - 174.9 -1.8 35.4 - 12 PRO 12 E - - - - - -66.1 - - - - - 176.7 - 38.8 - * * 13 PHE 13 e B - 185.3 - - - - - - - - 180.8 -3.2 35.5 - +* +* 14 ILE 14 t B - - -59.0 178.0 - - - - - - 187.1 -.6 34.4 - * +* +* 15 SER 15 T A - 184.5 - - - - - - - - 179.1 -.6 34.2 - +* +* 16 GLU 16 T A - - -54.2 180.3 - - - - - - 182.6 - 35.9 - 17 LYS 17 T a - - -68.0 - - - - - - - 185.9 -.8 30.6 - * +* +* 18 SER 18 T A - - -51.7 - - - - - - - 179.8 -1.9 34.3 - * * 19 SER 19 T A 50.6 - - - - - - - - - 182.9 - 34.5 - Residue-by-residue listing for refined_7 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 - 188.1 - 181.0 - - - - - - 184.2 -2.0 35.0 - 21 SER 21 t B - - -59.8 - - - - - - - 177.8 -2.1 36.4 - 22 LEU 22 E B - - -75.5 178.6 - - - - - - 179.4 -2.6 27.1 - +* +* 23 GLU 23 E B 46.6 - - 179.0 - - - - - - 181.7 -.5 36.1 - * ** ** 24 ILE 24 E B - - -61.5 179.4 - - - - - - 181.1 -1.4 32.8 - 25 PRO 25 h - - - - - -66.5 - - - - - 184.4 - 37.8 - * * 26 LEU 26 H A - - -68.7 - - -69.9 -34.8 - - - 179.6 - 32.1 - 27 GLY 27 H - - - - - - -66.2 -28.9 - - - 179.9 - - - 28 PHE 28 H A - 181.9 - - - -75.9 -31.2 - - - 180.4 - 35.0 - 29 ASN 29 H A 71.6 - - - - -76.1 -26.3 - - - 177.5 -1.1 30.6 - * * * 30 GLU 30 h A - 182.1 - - - - - - - - 178.6 -1.5 34.6 - 31 TYR 31 T A - 172.6 - - - - - - - - 175.1 - 32.3 - 32 PHE 32 t b 62.7 - - - - - - - - - 177.4 -.6 29.8 - +* * +* 33 PRO 33 - - - - - -79.4 - - - - - 178.8 - 38.6 - * * * 34 ALA 34 B - - - - - - - - - - 173.9 - 35.4 - * * 35 PRO 35 - - - - - -58.0 - - - - - 184.4 - 39.1 - * * 36 PHE 36 B 55.5 - - - - - - - - - 180.7 - 30.9 - 37 PRO 37 - - - - - -77.7 - - - - - 179.2 - 38.7 - * * * 38 ILE 38 S A - - -56.9 - - - - - - - 180.3 - 34.5 - 39 THR 39 B 47.4 - - - - - - - - - 178.2 - 33.6 - * * 40 VAL 40 E B - 173.0 - - - - - - - - 182.8 -3.3 36.3 - +* +* 41 ASP 41 E B - 189.9 - - - - - - - - 183.8 -1.4 33.5 - 42 LEU 42 E B - - -57.1 179.9 - - - - - - 179.9 -3.2 35.6 - +* +* 43 LEU 43 E B - - -64.6 - - - - - - - 174.0 -3.0 34.4 - * * * 44 ASP 44 E B - 171.1 - - - - - - - - 185.0 -3.0 34.3 - * * 45 TYR 45 e A - 186.9 - - - - - - - - 180.3 -.6 34.1 - +* +* 46 SER 46 T A - 185.0 - - - - - - - - 179.3 - 33.4 - 47 GLY 47 t - - - - - - - - - - - 179.7 -2.0 - - 48 ARG 48 e B - - -58.3 178.2 - - - - - - 179.8 - 35.1 - 49 SER 49 E B 54.6 - - - - - - - - - 179.8 - 33.8 - 50 TRP 50 E B - - -62.7 - - - - - - - 176.5 -2.4 34.8 - 51 THR 51 E B - - -56.2 - - - - - - - 186.3 - 33.6 - * * 52 VAL 52 E B - - -58.6 - - - - - - - 180.0 -2.1 33.8 - 53 ARG 53 e B - - -60.5 173.6 - - - - - - 180.9 -1.5 36.1 - 54 MET 54 E B - 185.2 - 182.3 - - - - - - 185.9 -.6 34.7 - * +* +* 55 LYS 55 E B - - -71.8 173.7 - - - - - - 175.6 -2.4 33.8 - 56 LYS 56 E B - - -67.7 - - - - - - - 184.3 - 37.4 - * * 57 ARG 57 E B - 199.9 - - - - - - - - 184.2 -3.4 35.0 - +* +* Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 GLY 58 T - - - - - - - - - - - 179.3 -.5 - - ** ** 59 GLU 59 T A - 181.6 - 173.5 - - - - - - 183.7 -.8 34.0 - +* +* 60 LYS 60 E B 61.1 - - 175.8 - - - - - - 176.6 -1.8 35.0 - 61 VAL 61 E B - 180.4 - - - - - - - - 180.1 -.9 34.1 - * * 62 PHE 62 E B - 187.3 - - - - - - - - 179.7 -2.5 35.1 - 63 LEU 63 E B - 184.7 - 164.6 - - - - - - 187.4 -2.8 33.4 - * * 64 THR 64 e b - 176.9 - - - - - - - - 185.6 -1.8 33.3 - 65 VAL 65 T B - 180.7 - - - - - - - - 186.0 - 34.1 - * * 66 GLY 66 h - - - - - - - - - - - 176.8 - - - 67 TRP 67 H A - 170.1 - - - -65.4 -24.9 - - - 181.8 -1.3 34.8 - * * 68 GLU 68 H A - 183.5 - 182.8 - -65.5 -29.8 - - - 176.3 - 33.2 - 69 ASN 69 H A - - -66.4 - - -69.5 -35.9 - - - 180.5 -1.0 33.4 - * * 70 PHE 70 H A - 183.7 - - - -68.5 -49.7 - - - 180.9 -.8 35.4 - +* +* 71 VAL 71 H A 74.3 - - - - -63.7 -33.7 - - - 176.7 -2.8 34.0 - 72 LYS 72 H A - 184.6 - 180.5 - -71.2 -48.7 - - - 183.9 -1.6 34.8 - 73 ASP 73 H A - - -75.0 - - -72.4 -39.6 - - - 179.7 -3.3 31.3 - +* +* 74 ASN 74 h A - - -71.9 - - - - - - - 180.5 -3.2 32.4 - +* +* 75 ASN 75 T ~l - 187.5 - - - - - - - - 182.1 -.5 30.8 - ** ** ** 76 LEU 76 t B - - -56.3 - - - - - - - 174.1 -1.1 33.2 - * * * 77 GLU 77 t B 53.2 - - - - - - - - - 180.8 - 33.0 - 78 ASP 78 T B 65.8 - - - - - - - - - 181.0 - 32.7 - 79 GLY 79 T - - - - - - - - - - - 178.0 -1.1 - - * * 80 LYS 80 e B - - -68.4 173.1 - - - - - - 181.5 -1.3 33.5 - 81 TYR 81 E B - - -60.2 - - - - - - - 182.8 - 34.6 - 82 LEU 82 E B - - -63.0 - - - - - - - 171.5 -2.1 34.7 - * * 83 GLN 83 E B 59.7 - - 168.1 - - - - - - 178.4 -2.8 32.5 - * * 84 PHE 84 E B - - -59.6 - - - - - - - 178.7 -2.6 35.5 - 85 ILE 85 E B - - -53.5 178.9 - - - - - - 181.6 -2.8 34.8 - * * 86 TYR 86 E B 56.0 - - - - - - - - - 173.1 -3.2 33.8 - * +* +* 87 ASP 87 S A - - -68.1 - - - - - - - 183.0 - 33.9 - 88 ARG 88 S l - - -71.1 - - - - - - - 178.1 - 30.0 - * * 89 ASP 89 S b 61.3 - - - - - - - - - 184.0 - 35.5 - 90 ARG 90 e A - - -74.7 - - - - - - - 172.1 - 31.5 - * * 91 THR 91 E B - 197.0 - - - - - - - - 184.0 - 30.9 - 92 PHE 92 E B - - -59.6 - - - - - - - 174.0 -1.9 35.5 - * * 93 TYR 93 E B - - -52.9 - - - - - - - 185.4 -2.4 35.2 - Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 VAL 94 E B - 185.6 - - - - - - - - 176.6 -3.3 34.5 - +* +* 95 ILE 95 E B - - -59.0 178.8 - - - - - - 180.9 -2.7 33.6 - 96 ILE 96 E B - - -56.5 - - - - - - - 177.9 -.5 34.6 - ** ** 97 TYR 97 e B - - -72.2 - - - - - - - 181.6 -3.3 33.2 - +* +* 98 GLY 98 S - - - - - - - - - - - 179.0 - - - 99 HIS 99 S A - 188.5 - - - - - - - - 178.2 - 33.9 - 100 ASN 100 S b - 182.7 - - - - - - - - 184.0 - 34.1 - 101 MET 101 B - - -62.5 183.4 - - - - - - 177.2 - 33.3 - 102 CYS 102 - - 183.5 - - - - - - - - - - 34.6 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * * * ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.3 183.4 -62.4 178.2 -69.5 -69.5 -34.9 - - - 180.1 -1.9 34.1 Standard deviations: 8.1 6.5 6.9 5.2 8.9 4.2 8.3 - - - 3.5 1.0 2.0 Numbers of values: 15 33 40 25 5 11 11 0 0 0 101 60 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_7 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 - 1.233 1.523 1.543 1.470 - 116.96 120.57 110.27 110.13 111.74 122.44 2 ALA 2 1.319 1.234 1.517 1.522 1.441 121.27 115.89 120.96 110.60 110.80 110.97 123.13 3 ASP 3 1.304 1.235 1.506 1.535 1.445 122.41 115.81 121.33 109.95 109.63 111.89 122.73 +* +* 4 THR 4 1.290 1.231 1.526 1.542 1.430 121.53 114.25 121.91 109.80 107.31 109.82 123.77 +** * * +** 5 GLY 5 1.308 1.225 1.496 - 1.422 123.03 116.57 119.05 - 109.05 - 124.35 +* * +* * * +* 6 GLU 6 1.318 1.255 1.528 1.538 1.467 124.98 115.45 121.62 111.85 113.55 112.45 122.86 * +* * +* 7 VAL 7 1.294 1.231 1.506 1.560 1.426 121.66 116.15 120.81 111.72 108.89 113.30 123.03 ** +* * * ** 8 GLN 8 1.283 1.233 1.509 1.523 1.414 122.08 115.48 120.94 112.47 111.38 108.72 123.56 *** ** * * *** 9 PHE 9 1.296 1.228 1.511 1.546 1.448 122.85 117.33 119.67 110.89 108.15 108.81 123.00 ** * ** 10 MET 10 1.317 1.232 1.497 1.547 1.451 121.11 115.93 120.68 107.86 110.70 112.89 123.39 * * * * 11 LYS 11 1.303 1.243 1.518 1.538 1.434 121.95 118.46 119.69 109.05 107.49 111.06 121.78 +* * * * +* 12 PRO 12 1.335 1.258 1.525 1.536 1.454 121.97 116.18 120.85 109.96 110.71 104.11 122.93 * * * Residue-by-residue listing for refined_7 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 1.301 1.232 1.514 1.536 1.430 121.60 116.89 120.11 110.15 107.46 109.92 122.99 ** * * ** 14 ILE 14 1.312 1.232 1.503 1.552 1.413 121.19 116.22 120.34 111.31 107.14 110.76 123.43 * * ** * * ** 15 SER 15 1.314 1.229 1.522 1.539 1.453 123.27 116.65 120.67 110.16 111.45 110.38 122.68 * * 16 GLU 16 1.315 1.231 1.517 1.507 1.428 120.68 117.40 120.31 107.64 110.51 110.61 122.30 * +* * +* 17 LYS 17 1.340 1.231 1.487 1.538 1.460 118.38 116.05 120.22 110.13 113.53 114.53 123.59 +* +* ** ** 18 SER 18 1.328 1.210 1.536 1.543 1.456 122.15 116.38 121.04 110.34 111.11 110.20 122.58 * * 19 SER 19 1.310 1.230 1.527 1.521 1.426 122.66 117.58 120.34 111.00 112.17 108.95 122.08 * +* +* 20 LYS 20 1.331 1.232 1.528 1.532 1.460 118.89 116.27 121.33 110.26 111.97 108.92 122.40 +* +* 21 SER 21 1.296 1.223 1.539 1.528 1.440 122.68 118.85 119.63 110.60 108.75 107.33 121.51 ** * +* ** 22 LEU 22 1.316 1.240 1.488 1.541 1.440 119.28 112.32 122.40 112.46 113.89 116.32 125.27 +* * +* * *** * *** 23 GLU 23 1.282 1.243 1.546 1.548 1.428 126.40 116.58 120.94 111.93 108.98 106.82 122.39 *** +* +** ** *** 24 ILE 24 1.313 1.245 1.541 1.557 1.448 121.40 117.19 120.67 111.61 111.63 111.02 122.14 * * * 25 PRO 25 1.353 1.246 1.542 1.533 1.468 123.06 115.64 121.43 110.89 113.13 103.82 122.91 26 LEU 26 1.320 1.221 1.523 1.547 1.460 122.88 117.19 120.50 110.78 112.88 112.18 122.29 27 GLY 27 1.315 1.234 1.518 - 1.459 119.89 115.31 121.09 - 111.67 - 123.57 28 PHE 28 1.319 1.226 1.531 1.540 1.451 123.27 117.32 120.51 111.25 110.14 108.60 122.14 * * 29 ASN 29 1.336 1.210 1.512 1.568 1.462 119.45 116.08 120.78 112.02 110.59 114.07 123.13 * +* * * ** ** 30 GLU 30 1.327 1.240 1.537 1.542 1.455 122.23 115.73 121.73 110.72 109.35 109.83 122.54 31 TYR 31 1.319 1.236 1.534 1.546 1.441 121.63 116.85 120.27 113.27 110.94 110.24 122.83 +* +* 32 PHE 32 1.331 1.226 1.543 1.570 1.459 121.53 117.22 121.65 112.79 112.07 113.56 121.00 ** * +* * ** 33 PRO 33 1.338 1.241 1.502 1.526 1.431 122.35 114.63 121.64 109.60 111.48 104.79 123.73 * ** +* +* * ** 34 ALA 34 1.278 1.253 1.507 1.531 1.424 123.55 118.71 118.90 110.50 106.78 109.80 122.34 +*** * +* * * * +* +*** 35 PRO 35 1.348 1.240 1.522 1.535 1.460 121.90 117.77 119.61 110.19 108.92 103.56 122.62 * * 36 PHE 36 1.321 1.232 1.525 1.541 1.416 120.72 116.48 121.17 113.12 112.58 111.63 122.32 ** +* ** 37 PRO 37 1.336 1.232 1.517 1.529 1.444 122.83 116.16 121.21 110.69 111.53 103.43 122.61 * * 38 ILE 38 1.298 1.239 1.511 1.551 1.431 120.81 115.63 121.12 109.92 108.82 111.45 123.23 ** * ** 39 THR 39 1.316 1.231 1.528 1.551 1.424 121.56 114.10 121.66 110.38 112.25 110.98 124.24 +* * +* 40 VAL 40 1.299 1.218 1.518 1.570 1.449 127.13 119.59 118.79 110.48 104.81 109.13 121.61 ** * *** +* * ** * *** 41 ASP 41 1.299 1.247 1.515 1.523 1.452 118.89 115.81 120.84 112.06 110.48 109.67 123.34 ** +* * ** Residue-by-residue listing for refined_7 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 1.309 1.232 1.513 1.534 1.449 122.68 116.14 120.59 108.76 110.26 110.21 123.27 * * 43 LEU 43 1.308 1.235 1.512 1.553 1.445 122.10 115.16 120.99 108.27 110.90 112.37 123.85 +* * * +* 44 ASP 44 1.298 1.241 1.510 1.531 1.448 123.43 115.52 120.64 110.64 108.70 110.65 123.84 ** ** 45 TYR 45 1.309 1.230 1.549 1.541 1.462 124.27 117.54 120.54 111.15 112.83 108.98 121.91 * * * * 46 SER 46 1.322 1.233 1.545 1.541 1.447 120.85 116.62 121.15 111.74 110.43 110.27 122.21 47 GLY 47 1.322 1.239 1.508 - 1.451 120.52 115.89 121.02 - 112.27 - 123.09 48 ARG 48 1.315 1.235 1.522 1.519 1.448 121.69 116.77 120.27 108.90 109.27 110.81 122.97 49 SER 49 1.303 1.242 1.518 1.531 1.440 121.81 116.32 120.58 111.36 110.55 110.08 123.06 +* +* 50 TRP 50 1.304 1.236 1.493 1.540 1.461 121.81 116.19 120.68 107.88 110.13 112.29 123.12 +* +* * * +* 51 THR 51 1.291 1.237 1.536 1.528 1.412 120.77 115.24 121.50 112.03 108.46 110.38 123.25 +** ** * +** 52 VAL 52 1.301 1.216 1.519 1.551 1.435 123.57 116.80 120.66 110.14 110.83 111.39 122.50 ** * * ** 53 ARG 53 1.292 1.224 1.532 1.519 1.449 121.69 117.30 120.16 110.49 109.76 107.60 122.54 +** +* +** 54 MET 54 1.322 1.218 1.506 1.527 1.467 121.68 116.91 120.22 109.37 108.92 111.06 122.87 55 LYS 55 1.304 1.230 1.511 1.518 1.433 121.74 115.66 121.06 110.63 113.06 109.91 123.27 +* * +* 56 LYS 56 1.313 1.239 1.504 1.533 1.438 122.34 116.39 120.52 106.38 104.63 111.03 123.07 * * * +* ** ** 57 ARG 57 1.273 1.233 1.509 1.547 1.434 121.63 115.79 120.95 111.82 106.98 109.21 123.20 +*** * +* +*** 58 GLY 58 1.301 1.227 1.504 - 1.425 120.34 116.17 120.42 - 110.45 - 123.40 +* +* +* 59 GLU 59 1.306 1.244 1.537 1.529 1.442 122.06 115.68 121.87 112.21 110.32 108.83 122.41 +* * +* 60 LYS 60 1.312 1.232 1.510 1.533 1.432 121.93 116.18 120.90 109.28 110.21 110.59 122.91 * * * 61 VAL 61 1.300 1.232 1.497 1.549 1.430 121.25 116.34 120.49 109.73 107.76 112.53 123.15 ** * * * ** 62 PHE 62 1.286 1.242 1.492 1.535 1.413 120.65 115.46 121.19 111.46 107.37 109.36 123.33 *** +* ** * *** 63 LEU 63 1.276 1.202 1.507 1.539 1.416 121.36 116.12 120.35 114.78 107.32 108.60 123.53 +*** * ** ** * * +*** 64 THR 64 1.289 1.243 1.574 1.598 1.443 123.16 115.92 120.92 113.78 111.56 108.48 123.15 +** ** ** ** +* +** 65 VAL 65 1.316 1.235 1.531 1.566 1.466 125.41 115.15 121.51 110.22 111.73 110.55 123.32 ** ** 66 GLY 66 1.311 1.228 1.482 - 1.421 122.09 114.38 121.72 - 108.59 - 123.85 * +* +* * +* 67 TRP 67 1.321 1.234 1.514 1.531 1.450 123.20 115.42 121.41 110.42 110.16 109.63 123.12 68 GLU 68 1.309 1.209 1.532 1.520 1.443 121.03 116.39 120.97 111.48 109.80 110.84 122.61 * * * 69 ASN 69 1.318 1.198 1.518 1.536 1.454 121.69 116.19 120.93 110.66 110.33 111.33 122.82 +* +* 70 PHE 70 1.311 1.238 1.523 1.551 1.455 123.40 115.69 121.00 109.60 109.23 110.08 123.30 * * * 71 VAL 71 1.333 1.218 1.520 1.571 1.459 122.09 114.98 121.42 110.25 109.20 111.73 123.59 * * Residue-by-residue listing for refined_7 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 1.301 1.226 1.540 1.522 1.433 123.16 116.67 120.50 110.71 111.03 108.93 122.81 ** * ** 73 ASP 73 1.332 1.232 1.522 1.546 1.482 121.87 117.76 120.45 110.09 114.65 113.03 121.78 * * * * 74 ASN 74 1.301 1.232 1.511 1.542 1.470 120.34 114.81 120.78 110.99 111.26 112.11 124.40 +* +* 75 ASN 75 1.328 1.240 1.532 1.534 1.477 125.22 116.53 121.41 111.84 112.97 112.54 122.05 +* * +* 76 LEU 76 1.314 1.230 1.514 1.546 1.443 119.90 115.20 121.11 109.03 111.75 113.03 123.67 * * * 77 GLU 77 1.297 1.247 1.520 1.551 1.436 124.21 116.77 119.97 110.94 109.00 112.45 123.24 ** * * * * ** 78 ASP 78 1.326 1.238 1.515 1.541 1.476 121.49 115.59 121.22 109.78 111.32 112.88 123.17 * * 79 GLY 79 1.304 1.225 1.500 - 1.436 121.02 115.92 120.96 - 111.03 - 123.12 +* +* 80 LYS 80 1.313 1.237 1.519 1.535 1.446 121.73 116.39 120.89 111.36 110.39 110.63 122.72 * * 81 TYR 81 1.302 1.228 1.493 1.535 1.438 121.93 117.11 119.95 110.42 107.98 110.83 122.92 +* +* * * +* 82 LEU 82 1.298 1.240 1.498 1.551 1.439 120.70 115.93 120.43 108.30 110.78 112.11 123.61 ** * * ** 83 GLN 83 1.309 1.243 1.504 1.537 1.429 121.44 115.52 120.94 109.94 108.85 114.12 123.50 * +* ** ** 84 PHE 84 1.288 1.232 1.507 1.539 1.429 122.24 116.96 120.01 109.84 108.16 110.13 123.00 +** +* * +** 85 ILE 85 1.312 1.235 1.516 1.552 1.447 120.79 115.70 120.64 109.04 108.17 111.81 123.59 * * * 86 TYR 86 1.299 1.229 1.526 1.540 1.449 122.78 116.92 120.60 111.08 111.72 109.92 122.48 ** ** 87 ASP 87 1.316 1.230 1.525 1.545 1.472 121.60 114.89 121.37 109.88 108.72 111.89 123.70 88 ARG 88 1.345 1.236 1.513 1.559 1.494 125.19 115.66 121.20 110.81 111.80 115.34 123.10 * * +* +* +** +** 89 ASP 89 1.301 1.231 1.518 1.523 1.421 122.91 116.40 120.60 110.37 108.43 109.26 123.00 ** +* ** 90 ARG 90 1.298 1.228 1.526 1.551 1.445 121.83 118.74 119.91 110.89 113.47 112.66 121.35 ** * * * * ** 91 THR 91 1.310 1.234 1.540 1.573 1.444 117.76 117.00 120.77 112.96 109.19 113.35 122.17 * * ** +* * ** 92 PHE 92 1.315 1.231 1.513 1.545 1.453 120.82 116.49 120.56 108.40 110.62 110.74 122.94 93 TYR 93 1.307 1.235 1.515 1.531 1.447 121.40 117.49 119.80 109.43 106.34 111.09 122.70 +* +* +* 94 VAL 94 1.305 1.239 1.522 1.549 1.444 120.83 115.98 121.02 108.94 111.45 111.39 123.00 +* +* 95 ILE 95 1.307 1.236 1.526 1.561 1.442 121.85 116.07 120.80 110.27 108.86 112.32 123.12 +* +* 96 ILE 96 1.306 1.232 1.523 1.593 1.449 122.45 116.74 120.28 108.82 108.20 112.76 122.96 +* +* * +* 97 TYR 97 1.308 1.241 1.509 1.525 1.435 121.34 114.36 121.54 109.85 111.36 112.18 124.11 +* * +* 98 GLY 98 1.294 1.235 1.495 - 1.422 123.51 118.19 119.46 - 108.05 - 122.35 ** * +* +* +* ** 99 HIS 99 1.297 1.230 1.511 1.539 1.449 119.80 115.12 121.19 110.68 108.17 111.44 123.69 ** * * ** Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 ASN 100 1.310 1.243 1.515 1.536 1.446 123.18 115.68 120.65 110.58 108.09 111.20 123.61 * * * 101 MET 101 1.324 1.239 1.515 1.534 1.460 122.81 115.41 120.97 109.35 112.46 112.02 123.63 102 CYS 102 1.306 - 1.522 1.538 1.430 123.13 - - 111.07 107.56 110.21 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +* ** ** ** *** +* * ** ** *** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 1.273 1.345 1.308 .014 +*** * * C-N (Pro) 1.341 .016 5 1.335 1.353 1.342 .007 C-O C-O 1.231 .020 101 1.198 1.258 1.233 .010 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.487 1.574 1.519 .014 +* ** CH2G*-C (Gly) 1.516 .018 7 1.482 1.518 1.500 .011 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.522 1.531 1.527 .004 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.528 1.598 1.560 .017 ** CH1E-CH2E (the rest) 1.530 .020 75 1.507 1.570 1.537 .011 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.412 1.494 1.445 .016 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.421 1.459 1.434 .014 +* * N-CH1E (Pro) 1.466 .015 5 1.431 1.468 1.451 .013 ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 89 112.32 119.59 116.28 1.08 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.38 118.19 116.06 1.08 CH1E-C-N (Pro) 116.9 1.5 5 114.63 117.77 116.08 1.02 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.00 125.27 122.98 .69 * * O-C-N (Pro) 122.0 1.4 5 122.61 123.73 122.96 .41 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.76 127.13 121.98 1.57 ** *** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.89 123.51 121.49 1.30 +* C-N-CH1E (Pro) 122.6 5.0 5 121.90 123.06 122.42 .46 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.79 122.40 120.76 .61 * CH2G*-C-O (Gly) 120.8 2.1 7 119.05 121.72 120.53 .88 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.50 110.60 110.55 .05 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.82 113.78 110.63 1.32 ** CH2E-CH1E-C (the rest) 110.1 1.9 75 106.38 114.78 110.50 1.38 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.63 114.65 110.02 2.01 ** * NH1-CH2G*-C (Gly) 112.5 2.9 7 108.05 112.27 110.16 1.50 +* N-CH1E-C (Pro) 111.8 2.5 5 108.92 113.13 111.16 1.37 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.80 110.97 110.39 .59 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.48 113.35 111.29 1.29 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.43 104.79 103.94 .48 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.82 116.32 110.94 1.82 ** *** ------------------------------------------------------------------------------------------------------------- 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_7 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] 1 1.1% 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 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 3.5 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 60 1.0 .8 .2 .7 Inside f. Overall G-factor 102 -.1 -.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 15 8.1 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 33 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 40 6.9 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 88 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 25 5.2 20.4 5.0 -3.0 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 8.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .97 3 Residue-by-residue listing for refined_7 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.44 Chi1-chi2 distribution -.33 Chi1 only .05 Chi3 & chi4 .41 Omega -.03 ------ -.16 ===== Main-chain covalent forces:- Main-chain bond lengths -.09 Main-chain bond angles .33 ------ .16 ===== OVERALL AVERAGE -.05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.