Residue-by-residue listing for refined_18 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - 179.3 - 178.1 - - - - - - 179.2 - 33.6 - 2 ALA 2 l - - - - - - - - - - 177.0 - 31.2 - 3 ASP 3 B - 179.7 - - - - - - - - 180.4 - 33.1 - 4 THR 4 A - - -51.6 - - - - - - - 180.8 -.8 35.2 - * +* +* 5 GLY 5 S - - - - - - - - - - - 176.8 - - - 6 GLU 6 B - 177.6 - 182.5 - - - - - - 179.5 -.7 35.0 - +* +* 7 VAL 7 E B - - -63.8 - - - - - - - 177.6 -1.1 34.0 - * * 8 GLN 8 E B 59.8 - - 185.1 - - - - - - 180.9 - 33.8 - 9 PHE 9 E B - 182.2 - - - - - - - - 177.7 -1.7 34.5 - 10 MET 10 E B - 178.7 - 183.1 - - - - - - 174.4 - 35.5 - 11 LYS 11 E B - 192.4 - 182.7 - - - - - - 171.5 -.7 35.6 - * +* +* 12 PRO 12 - - - - - -67.0 - - - - - 182.0 - 38.7 - * * 13 PHE 13 B - - -58.7 - - - - - - - 181.1 - 33.6 - 14 ILE 14 h B - - -65.7 - - - - - - - 187.4 - 33.4 - * * 15 SER 15 H A - 186.4 - - - -62.6 -37.4 - - - 178.9 - 32.0 - 16 GLU 16 H A - - -66.4 180.4 - -63.0 -27.7 - - - 184.2 - 33.7 - * * 17 LYS 17 H A 68.4 - - 183.4 - -97.3 -28.7 - - - 176.9 -1.0 32.3 - +** * +** 18 SER 18 H A - 178.5 - - - -72.3 -13.6 - - - 175.0 -2.8 33.5 - ** ** Residue-by-residue listing for refined_18 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 SER 19 h A - - -60.1 - - - - - - - 183.3 -1.0 34.5 - * * 20 LYS 20 T a - - -56.0 177.6 - - - - - - 183.5 -1.6 33.9 - 21 SER 21 t B 54.3 - - - - - - - - - 175.0 -1.9 34.9 - 22 LEU 22 E B - 190.1 - - - - - - - - 185.1 -1.8 33.3 - 23 GLU 23 E B 62.9 - - 178.9 - - - - - - 175.5 - 34.9 - 24 ILE 24 E B - - -63.5 - - - - - - - 177.7 -2.3 33.9 - 25 PRO 25 h - - - - - -67.6 - - - - - 182.8 - 38.7 - * * 26 LEU 26 H A - - -63.7 179.6 - -61.4 -30.0 - - - 178.0 - 32.7 - 27 GLY 27 H - - - - - - -65.6 -35.0 - - - 180.0 - - - 28 PHE 28 H A - 189.9 - - - -88.4 -21.1 - - - 178.1 -.8 33.3 - +* +* +* +* 29 ASN 29 H A - 179.1 - - - -56.1 -24.0 - - - 180.0 -1.9 35.0 - * * 30 GLU 30 h A - 182.0 - 179.5 - - - - - - 178.3 -.7 33.8 - +* +* 31 TYR 31 T A - - -63.9 - - - - - - - 179.9 -2.4 33.3 - 32 PHE 32 t B - - -65.3 - - - - - - - 180.1 -2.0 33.9 - 33 PRO 33 - - - - - -77.0 - - - - - 177.5 - 38.8 - * * * 34 ALA 34 S A - - - - - - - - - - 178.9 - 32.2 - 35 PRO 35 S - - - - - -56.9 - - - - - 180.6 - 38.5 - * * 36 PHE 36 B - - -63.2 - - - - - - - 172.1 - 37.5 - * * * 37 PRO 37 - - - - - -77.1 - - - - - 181.8 - 39.2 - * +* +* 38 ILE 38 S a - - -56.9 - - - - - - - 175.2 - 31.9 - 39 THR 39 B 52.8 - - - - - - - - - 178.9 - 33.8 - 40 VAL 40 E B 69.1 - - - - - - - - - 185.8 -3.2 33.9 - +* +* 41 ASP 41 E B - - -61.4 - - - - - - - 182.0 -2.3 32.3 - 42 LEU 42 E B - 185.7 - - - - - - - - 184.2 -3.1 35.5 - * * 43 LEU 43 E B - - -69.2 - - - - - - - 184.0 -3.3 33.6 - +* +* 44 ASP 44 E B - 173.9 - - - - - - - - 179.0 -.7 36.3 - +* +* 45 TYR 45 e A - 175.7 - - - - - - - - 183.4 -.6 35.0 - +* +* 46 SER 46 T A - 184.0 - - - - - - - - 178.4 - 33.5 - 47 GLY 47 t - - - - - - - - - - - 178.1 -1.7 - - 48 ARG 48 e B - 181.6 - - - - - - - - 184.3 - 35.2 - 49 SER 49 E B 56.1 - - - - - - - - - 177.7 - 33.2 - 50 TRP 50 E B - - -52.7 - - - - - - - 174.2 -2.4 37.3 - * * 51 THR 51 E B - - -55.9 - - - - - - - 186.8 - 34.2 - * * 52 VAL 52 E B - 182.6 - - - - - - - - 178.4 -3.0 35.3 - * * 53 ARG 53 e B - - -60.0 187.2 - - - - - - 179.6 -2.9 33.2 - * * 54 MET 54 E B - - -63.5 178.6 - - - - - - 178.7 -.7 34.3 - +* +* 55 LYS 55 E B - - -66.9 184.1 - - - - - - 174.3 -1.6 34.5 - 56 LYS 56 E B - - -54.7 - - - - - - - 181.3 - 35.2 - Residue-by-residue listing for refined_18 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 ARG 57 E b - - -56.8 182.0 - - - - - - 187.9 -3.1 33.2 - * * * 58 GLY 58 T - - - - - - - - - - - 176.6 -.9 - - * * 59 GLU 59 T A - - -63.3 177.9 - - - - - - 187.5 -.7 34.4 - * +* +* 60 LYS 60 E B - 192.1 - - - - - - - - 183.6 -2.0 36.0 - 61 VAL 61 E B - 183.0 - - - - - - - - 178.4 -.8 34.5 - +* +* 62 PHE 62 E B - - -66.0 - - - - - - - 171.7 -1.8 34.8 - * * 63 LEU 63 E B - - -66.8 - - - - - - - 191.3 -2.1 33.8 - +* +* 64 THR 64 e a - 176.8 - - - - - - - - 181.3 -1.6 29.1 - * * 65 VAL 65 T B - - -63.8 - - - - - - - 184.9 - 31.0 - 66 GLY 66 h - - - - - - - - - - - 172.2 - - - * * 67 TRP 67 H A - 169.1 - - - -63.6 -29.5 - - - 179.3 -.6 36.0 - +* +* 68 GLU 68 H A - 183.9 - - - -64.0 -26.1 - - - 174.4 -.7 33.4 - * +* +* 69 ASN 69 H A - - -66.4 - - -75.7 -38.8 - - - 183.2 -1.0 35.1 - * * 70 PHE 70 H A - 175.7 - - - -71.5 -43.1 - - - 180.8 -1.2 34.2 - * * 71 VAL 71 H A 69.1 - - - - -62.4 -41.4 - - - 176.0 -3.3 32.2 - +* +* 72 LYS 72 H A - - -62.9 188.2 - -71.2 -42.3 - - - 187.9 -1.2 32.9 - * * * 73 ASP 73 H A - 185.4 - - - -76.8 -35.7 - - - 183.2 -2.6 32.5 - 74 ASN 74 h A - 186.9 - - - - - - - - 176.6 -3.4 31.5 - +* +* 75 ASN 75 t XX - 180.0 - - - - - - - - 180.1 -.5 33.0 - **** ** **** 76 LEU 76 l - - -79.4 - - - - - - - 179.7 -2.2 28.5 - +* +* 77 GLU 77 t B - 184.9 - 181.1 - - - - - - 182.2 - 34.2 - 78 ASP 78 T B 58.2 - - - - - - - - - 180.7 - 33.1 - 79 GLY 79 T - - - - - - - - - - - 176.8 - - - 80 LYS 80 t B - - -63.9 175.8 - - - - - - 187.7 -1.2 33.9 - * * * 81 TYR 81 E B - - -55.6 - - - - - - - 183.5 -.9 34.3 - * * 82 LEU 82 E B - - -62.7 - - - - - - - 171.8 -.7 34.2 - * +* +* 83 GLN 83 E B - - -72.8 - - - - - - - 177.2 -3.1 36.7 - * * 84 PHE 84 E B - - -65.2 - - - - - - - 176.1 -2.7 34.5 - 85 ILE 85 E B - - -56.1 - - - - - - - 187.1 -3.5 35.5 - * ** ** 86 TYR 86 E B - - -58.9 - - - - - - - 173.7 -3.5 35.5 - * ** ** 87 ASP 87 e A - 161.9 - - - - - - - - 175.4 -1.7 35.4 - * * 88 ARG 88 S l - - -66.6 172.5 - - - - - - 179.6 -.7 31.8 - +* +* Residue-by-residue listing for refined_18 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 89 ASP 89 S a - 189.8 - - - - - - - - 182.5 - 34.8 - 90 ARG 90 e a - 192.0 - - - - - - - - 182.7 - 35.7 - 91 THR 91 E B - - -54.2 - - - - - - - 169.4 - 34.1 - +* +* 92 PHE 92 E B - - -72.0 - - - - - - - 177.5 -1.6 35.2 - 93 TYR 93 E B - 180.5 - - - - - - - - 185.0 -2.4 33.9 - 94 VAL 94 E B - 186.8 - - - - - - - - 172.1 -1.7 35.0 - * * 95 ILE 95 E B - 184.9 - - - - - - - - 186.1 -2.6 31.5 - * * 96 ILE 96 E B - - -51.6 - - - - - - - 173.1 - 35.5 - * * * 97 TYR 97 E B - - -62.8 - - - - - - - 183.8 -3.6 35.8 - ** ** 98 GLY 98 - - - - - - - - - - - 184.5 -.9 - - +* +* 99 HIS 99 S XX - - -58.2 - - - - - - - 174.0 - 32.1 - **** * **** 100 ASN 100 S b - 180.5 - - - - - - - - 185.6 -2.7 33.4 - 101 MET 101 b - - -67.0 178.6 - - - - - - 175.5 - 30.5 - 102 CYS 102 - - - -61.5 - - - - - - - - -1.6 34.4 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * +** ** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.2 182.1 -62.2 180.8 -69.1 -70.1 -31.6 - - - 179.7 -1.8 34.2 Standard deviations: 6.5 6.5 5.8 3.7 8.4 11.0 8.5 - - - 4.4 .9 1.9 Numbers of values: 9 35 44 21 5 15 15 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_18 Page 5 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - 1.230 1.509 1.535 1.454 - 115.53 120.15 110.59 109.78 111.39 124.32 2 ALA 2 1.329 1.240 1.522 1.526 1.453 124.61 115.80 121.51 111.82 112.67 112.16 122.61 +* * +* 3 ASP 3 1.306 1.239 1.500 1.537 1.448 121.64 115.88 120.77 110.64 109.73 112.18 123.27 +* * +* 4 THR 4 1.310 1.237 1.536 1.546 1.439 121.83 115.63 121.25 110.21 109.53 109.63 123.10 * * * * 5 GLY 5 1.321 1.239 1.492 - 1.435 121.09 115.17 120.60 - 110.85 - 124.23 * * 6 GLU 6 1.305 1.241 1.523 1.532 1.449 123.21 115.95 120.84 109.82 109.91 110.00 123.20 +* +* 7 VAL 7 1.301 1.231 1.507 1.564 1.444 122.25 116.68 120.28 109.55 109.29 112.45 123.03 ** ** 8 GLN 8 1.296 1.240 1.509 1.519 1.418 121.83 116.23 120.43 111.38 109.63 110.47 123.33 ** ** ** 9 PHE 9 1.298 1.240 1.523 1.548 1.451 121.28 115.86 120.56 111.08 110.28 109.47 123.58 ** ** 10 MET 10 1.319 1.236 1.503 1.535 1.446 123.17 116.31 120.33 108.10 108.93 111.47 123.32 * * * 11 LYS 11 1.302 1.221 1.519 1.536 1.432 121.99 119.91 118.83 109.78 106.90 110.15 121.15 +* * +* * +* * +* 12 PRO 12 1.335 1.246 1.533 1.533 1.462 121.48 116.95 120.61 110.52 109.86 103.70 122.43 Residue-by-residue listing for refined_18 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 13 PHE 13 1.306 1.234 1.504 1.539 1.449 121.48 116.00 120.74 110.07 110.27 111.82 123.26 +* * +* 14 ILE 14 1.312 1.231 1.504 1.588 1.442 121.40 117.00 119.97 110.92 106.66 113.08 123.03 * +* +* +* 15 SER 15 1.304 1.230 1.514 1.530 1.447 121.35 116.30 120.44 112.12 111.75 111.35 123.17 +* * +* 16 GLU 16 1.309 1.232 1.521 1.507 1.444 121.66 117.27 120.44 109.73 112.41 110.98 122.22 * * * 17 LYS 17 1.322 1.233 1.502 1.545 1.460 118.97 114.50 121.82 111.66 108.37 112.75 123.61 * +* * * +* 18 SER 18 1.313 1.201 1.536 1.549 1.420 122.87 116.71 120.49 112.79 109.49 109.60 122.78 * * +* * +* 19 SER 19 1.339 1.228 1.531 1.537 1.459 122.56 116.36 121.02 109.80 110.48 110.48 122.61 20 LYS 20 1.322 1.232 1.512 1.537 1.445 121.16 116.76 120.46 110.28 111.35 110.85 122.78 21 SER 21 1.306 1.244 1.516 1.539 1.433 120.67 116.46 120.38 110.74 111.10 109.10 123.14 +* * +* 22 LEU 22 1.319 1.245 1.512 1.556 1.440 121.05 115.56 120.52 112.18 107.06 111.47 123.92 * * * * 23 GLU 23 1.301 1.238 1.550 1.542 1.434 122.60 116.57 121.11 110.72 111.64 108.81 122.29 ** * * ** 24 ILE 24 1.309 1.243 1.534 1.554 1.448 121.27 117.54 120.47 109.76 109.74 111.86 121.96 * * 25 PRO 25 1.346 1.234 1.534 1.538 1.463 122.76 116.67 120.54 110.06 111.23 103.92 122.79 26 LEU 26 1.326 1.233 1.519 1.523 1.470 122.55 116.88 120.17 110.25 113.14 111.49 122.94 27 GLY 27 1.320 1.237 1.516 - 1.449 120.28 115.84 121.22 - 111.36 - 122.93 28 PHE 28 1.323 1.228 1.543 1.533 1.440 121.41 115.79 121.29 111.59 110.09 110.59 122.90 29 ASN 29 1.331 1.231 1.533 1.541 1.492 124.02 115.46 121.49 109.68 110.96 109.57 123.02 +* * +* 30 GLU 30 1.319 1.236 1.553 1.530 1.456 123.42 116.17 121.44 112.01 111.67 108.83 122.38 * * * 31 TYR 31 1.307 1.239 1.530 1.539 1.458 121.65 116.48 120.73 110.13 110.90 111.82 122.79 +* +* 32 PHE 32 1.322 1.239 1.526 1.538 1.454 122.28 118.04 120.11 109.87 110.49 111.37 121.85 33 PRO 33 1.345 1.252 1.540 1.546 1.456 122.61 115.56 121.33 109.80 112.68 103.90 123.11 * * 34 ALA 34 1.315 1.241 1.560 1.530 1.456 122.99 119.44 119.04 111.49 112.66 111.01 121.52 +* +* * +* 35 PRO 35 1.381 1.249 1.538 1.538 1.479 122.79 114.90 121.68 109.76 114.09 103.90 123.43 +** * * +** 36 PHE 36 1.312 1.237 1.520 1.533 1.421 123.98 118.72 119.99 107.53 109.66 108.85 121.26 * +* * * * * +* 37 PRO 37 1.331 1.230 1.519 1.547 1.449 121.36 118.10 119.78 110.16 108.22 103.94 122.11 * * * 38 ILE 38 1.317 1.225 1.517 1.557 1.452 119.45 116.62 120.64 111.58 109.32 113.11 122.72 * * * 39 THR 39 1.297 1.236 1.518 1.557 1.431 121.19 116.41 120.72 110.20 108.81 112.16 122.85 ** * ** 40 VAL 40 1.285 1.239 1.527 1.561 1.420 122.30 117.92 119.98 112.22 107.06 110.68 122.09 *** ** * * *** 41 ASP 41 1.297 1.242 1.505 1.529 1.441 119.76 115.01 121.39 111.99 112.06 110.96 123.59 ** * ** 42 LEU 42 1.305 1.233 1.535 1.545 1.436 123.23 116.16 120.56 111.72 108.01 108.04 123.24 +* * * * +* 43 LEU 43 1.317 1.234 1.523 1.558 1.457 123.26 114.26 121.69 109.36 112.74 111.71 123.98 * * Residue-by-residue listing for refined_18 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.310 1.241 1.522 1.538 1.450 125.30 116.04 120.20 109.28 109.25 108.91 123.75 * +* +* 45 TYR 45 1.321 1.224 1.534 1.533 1.457 124.75 117.37 120.32 110.31 112.83 108.60 122.28 +* * +* 46 SER 46 1.312 1.236 1.548 1.541 1.449 121.18 116.57 120.99 111.58 111.52 109.83 122.45 * * * 47 GLY 47 1.323 1.227 1.509 - 1.453 120.78 115.76 121.01 - 112.27 - 123.24 48 ARG 48 1.310 1.232 1.527 1.525 1.454 122.47 116.82 120.41 111.53 108.59 108.20 122.75 * * * 49 SER 49 1.299 1.236 1.523 1.533 1.441 120.56 114.98 121.56 111.33 112.74 110.14 123.41 ** ** 50 TRP 50 1.301 1.234 1.513 1.518 1.413 124.00 117.00 120.31 108.71 109.05 108.02 122.68 +* ** * * ** 51 THR 51 1.300 1.232 1.527 1.535 1.429 120.45 116.02 120.87 111.07 107.27 110.82 123.08 ** +* * ** 52 VAL 52 1.301 1.214 1.520 1.564 1.445 122.76 117.63 120.26 111.02 109.34 108.92 122.04 +* +* +* 53 ARG 53 1.301 1.248 1.498 1.517 1.440 120.55 115.35 121.07 109.72 110.91 112.32 123.58 ** * * ** 54 MET 54 1.302 1.230 1.501 1.528 1.450 121.72 116.33 120.78 109.47 110.08 111.40 122.88 +* * +* 55 LYS 55 1.306 1.241 1.495 1.539 1.434 121.81 115.70 120.76 108.63 109.99 112.21 123.53 +* * * * +* 56 LYS 56 1.299 1.227 1.494 1.528 1.420 121.33 116.07 120.61 109.18 105.70 111.83 123.25 ** * ** +* ** 57 ARG 57 1.271 1.244 1.490 1.528 1.432 121.72 114.96 121.35 112.25 107.61 111.19 123.61 **** +* * * * **** 58 GLY 58 1.301 1.233 1.506 - 1.418 120.53 116.67 120.40 - 108.23 - 122.90 +* ** * ** 59 GLU 59 1.295 1.240 1.526 1.506 1.443 121.53 116.57 120.61 109.50 111.02 110.52 122.80 ** * ** 60 LYS 60 1.320 1.232 1.535 1.540 1.451 121.47 116.74 120.67 110.30 109.31 108.33 122.59 * * 61 VAL 61 1.313 1.239 1.522 1.551 1.455 121.59 115.86 120.91 109.29 110.84 111.17 123.22 * * 62 PHE 62 1.317 1.245 1.513 1.540 1.446 122.14 115.75 120.78 108.19 110.87 111.81 123.46 * * 63 LEU 63 1.311 1.221 1.506 1.556 1.463 121.45 116.95 120.00 110.06 105.75 113.02 123.02 * * +* * +* 64 THR 64 1.311 1.227 1.558 1.576 1.447 120.55 118.65 119.92 114.51 115.37 111.19 121.43 * +* * * ** * ** 65 VAL 65 1.317 1.236 1.516 1.553 1.454 120.33 116.21 120.66 112.02 110.65 113.45 123.05 * * * 66 GLY 66 1.316 1.224 1.505 - 1.449 120.87 115.00 121.46 - 110.09 - 123.52 67 TRP 67 1.320 1.217 1.512 1.543 1.447 123.82 113.75 122.26 109.87 107.51 109.36 123.94 * * * * 68 GLU 68 1.296 1.222 1.573 1.557 1.431 124.61 116.15 121.56 116.26 109.31 106.20 122.19 ** ** * * +* *** +** *** 69 ASN 69 1.335 1.215 1.504 1.550 1.473 122.60 115.22 121.08 108.04 108.62 112.12 123.65 * * * * 70 PHE 70 1.314 1.226 1.501 1.540 1.451 123.50 116.29 120.31 110.72 110.96 110.15 123.40 * * * 71 VAL 71 1.319 1.221 1.517 1.557 1.439 121.36 115.98 121.24 111.17 110.40 112.79 122.78 * * Residue-by-residue listing for refined_18 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.308 1.227 1.515 1.527 1.452 120.21 116.39 120.86 109.18 111.46 113.02 122.73 +* * +* 73 ASP 73 1.319 1.229 1.532 1.530 1.464 120.32 117.67 120.41 111.35 113.86 110.39 121.91 74 ASN 74 1.318 1.231 1.547 1.558 1.450 120.96 116.39 120.90 113.85 111.80 110.31 122.71 * * +* +* 75 ASN 75 1.352 1.238 1.510 1.542 1.508 123.79 115.13 120.90 110.39 112.45 111.28 123.97 +* +** * +** 76 LEU 76 1.308 1.245 1.513 1.515 1.473 122.94 115.56 121.58 112.65 115.03 113.55 122.80 +* * * +* +* 77 GLU 77 1.292 1.243 1.511 1.509 1.418 120.65 113.88 121.67 110.70 109.82 110.33 124.44 +** * ** * +** 78 ASP 78 1.290 1.236 1.521 1.539 1.463 124.44 115.87 120.99 110.77 111.69 111.19 123.09 +** +* +** 79 GLY 79 1.311 1.234 1.501 - 1.448 121.26 115.25 121.67 - 110.35 - 123.08 * * 80 LYS 80 1.304 1.233 1.517 1.530 1.435 122.47 117.38 120.03 112.36 108.22 109.71 122.59 +* * * * +* 81 TYR 81 1.310 1.226 1.488 1.533 1.442 120.53 116.59 120.38 110.36 109.31 110.88 123.02 * +* +* 82 LEU 82 1.291 1.231 1.509 1.553 1.425 120.74 115.12 120.92 109.15 111.23 111.91 123.95 +** * +* +** 83 GLN 83 1.300 1.246 1.494 1.533 1.437 123.38 116.32 120.55 106.89 106.20 111.43 123.12 ** * * +* +* ** 84 PHE 84 1.277 1.225 1.491 1.530 1.422 120.77 116.22 120.36 109.44 108.90 111.79 123.41 +*** +* +* +*** 85 ILE 85 1.292 1.246 1.509 1.558 1.430 121.98 117.03 120.32 109.38 105.40 111.40 122.65 +** * ** +** 86 TYR 86 1.299 1.236 1.503 1.535 1.438 120.16 113.52 121.81 107.97 112.29 110.71 124.66 ** * * * * * ** 87 ASP 87 1.307 1.234 1.513 1.529 1.452 124.81 114.47 121.32 111.49 108.70 108.05 124.21 +* +* * +* 88 ARG 88 1.340 1.234 1.512 1.525 1.462 124.84 117.11 120.28 111.68 113.77 111.08 122.59 +* +* 89 ASP 89 1.316 1.233 1.490 1.509 1.440 119.86 115.26 121.02 108.32 110.59 111.61 123.72 +* * * +* 90 ARG 90 1.312 1.230 1.520 1.538 1.430 121.39 116.71 120.99 109.84 109.36 109.32 122.30 * * * 91 THR 91 1.319 1.230 1.559 1.555 1.458 119.08 115.82 121.34 110.05 113.17 110.08 122.75 +* * +* 92 PHE 92 1.316 1.212 1.509 1.534 1.455 123.93 117.86 119.56 107.54 107.41 112.61 122.56 * * * * * 93 TYR 93 1.296 1.229 1.514 1.534 1.453 121.06 117.72 119.80 111.82 108.58 110.06 122.47 ** ** 94 VAL 94 1.318 1.232 1.532 1.556 1.462 119.77 116.01 120.77 108.33 112.47 110.90 123.22 * * 95 ILE 95 1.325 1.235 1.539 1.604 1.457 122.76 116.32 121.07 113.99 107.01 112.58 122.54 ** ** * ** 96 ILE 96 1.314 1.232 1.510 1.588 1.455 121.81 116.52 120.33 107.48 109.85 112.29 123.15 * +* +* 97 TYR 97 1.313 1.236 1.496 1.528 1.434 121.25 116.48 120.34 107.70 106.27 112.00 123.18 * * * * +* +* 98 GLY 98 1.297 1.231 1.492 - 1.430 119.99 116.00 119.90 - 112.45 - 124.09 ** * * ** 99 HIS 99 1.345 1.223 1.524 1.552 1.481 124.43 115.48 121.22 111.15 108.91 113.18 123.27 * * * +* +* +* Residue-by-residue listing for refined_18 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 1.302 1.233 1.510 1.539 1.435 124.05 116.59 120.51 111.67 106.86 111.72 122.81 +* * * +* +* 101 MET 101 1.318 1.237 1.513 1.532 1.459 121.52 114.34 121.44 111.87 113.94 112.54 124.15 * * 102 CYS 102 1.307 - 1.515 1.538 1.438 124.76 - - 110.40 106.91 111.36 - +* * +* +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** ** +** +* +* * *** ** +** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 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 1.271 1.352 1.310 .013 **** +* * C-N (Pro) 1.341 .016 5 1.331 1.381 1.348 .018 +** C-O C-O 1.231 .020 101 1.201 1.252 1.233 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.488 1.573 1.519 .017 +* ** CH2G*-C (Gly) 1.516 .018 7 1.492 1.516 1.503 .008 * CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.526 1.530 1.528 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.535 1.604 1.563 .016 ** CH1E-CH2E (the rest) 1.530 .020 75 1.506 1.558 1.535 .011 * * N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.413 1.508 1.446 .016 ** +** NH1-CH2G* (Gly) 1.451 .016 7 1.418 1.453 1.440 .012 ** N-CH1E (Pro) 1.466 .015 5 1.449 1.479 1.462 .010 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_18 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 89 113.52 119.91 116.28 1.11 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 115.00 116.67 115.67 .54 CH1E-C-N (Pro) 116.9 1.5 5 114.90 118.10 116.43 1.12 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.15 124.66 123.02 .68 * * O-C-N (Pro) 122.0 1.4 5 122.11 123.43 122.77 .47 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.97 125.30 122.05 1.47 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 7 119.99 121.26 120.68 .42 C-N-CH1E (Pro) 122.6 5.0 5 121.36 122.79 122.20 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.83 122.26 120.71 .59 * CH2G*-C-O (Gly) 120.8 2.1 7 119.90 121.67 120.89 .58 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 111.49 111.82 111.66 .16 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.48 114.51 110.71 1.72 ** CH2E-CH1E-C (the rest) 110.1 1.9 75 106.89 116.26 110.39 1.54 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.40 115.37 110.02 2.16 ** * NH1-CH2G*-C (Gly) 112.5 2.9 7 108.23 112.45 110.80 1.34 * N-CH1E-C (Pro) 111.8 2.5 5 108.22 114.09 111.22 2.06 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 111.01 112.16 111.59 .57 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.92 113.45 111.59 1.24 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.70 103.94 103.87 .09 NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.20 113.55 110.71 1.46 +** +* ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_18 Page 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] 75 85.2% Residues in additional allowed regions [a,b,l,p] 11 12.5% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 2 2.3% ---- ------ 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 85.2 83.8 10.0 .1 Inside b. Omega angle st dev 101 4.4 6.0 3.0 -.5 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 64 .9 .8 .2 .7 Inside f. Overall G-factor 102 .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 9 6.5 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 35 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 44 5.8 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 88 7.1 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 21 3.7 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% 85.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .97 3 Residue-by-residue listing for refined_18 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.39 Chi1-chi2 distribution -.10 Chi1 only -.04 Chi3 & chi4 .43 Omega -.31 ------ -.19 ===== Main-chain covalent forces:- Main-chain bond lengths -.01 Main-chain bond angles .36 ------ .21 ===== OVERALL AVERAGE -.05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.