Residue-by-residue listing for refined_15 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 - - 180.6 - 182.2 - - - - - - 178.9 - 34.4 - 2 ALA 2 B - - - - - - - - - - 182.8 - 33.7 - 3 ASP 3 B - 178.8 - - - - - - - - 179.0 -.7 33.0 - +* +* 4 THR 4 S A - - -48.6 - - - - - - - 179.4 -.5 35.8 - * ** ** 5 GLY 5 - - - - - - - - - - - 179.9 - - - 6 GLU 6 B 56.8 - - 175.9 - - - - - - 179.7 - 30.6 - 7 VAL 7 E B - - -61.8 - - - - - - - 180.9 -3.2 33.2 - +* +* 8 GLN 8 E B - - -55.6 181.2 - - - - - - 175.2 - 36.2 - 9 PHE 9 E B - 189.2 - - - - - - - - 181.1 -2.4 33.8 - 10 MET 10 E B - 188.1 - 177.8 - - - - - - 187.6 - 35.6 - * * 11 LYS 11 E B - 194.6 - 180.9 - - - - - - 177.6 -1.2 35.3 - * * 12 PRO 12 - - - - - -61.5 - - - - - 179.6 - 38.1 - * * 13 PHE 13 B 46.7 - - - - - - - - - 169.6 - 34.9 - * +* +* 14 ILE 14 h B - - -59.4 180.3 - - - - - - 185.4 - 32.5 - 15 SER 15 H A 54.2 - - - - -67.2 -14.7 - - - 176.0 - 32.6 - ** ** 16 GLU 16 H A - - -57.4 180.1 - -61.0 -37.1 - - - 179.5 - 34.8 - 17 LYS 17 H a - - -66.7 185.8 - -112.7 -34.1 - - - 183.2 -1.8 27.3 - +*** +* +*** 18 SER 18 H A 59.3 - - - - -59.0 -28.5 - - - 179.0 -3.4 32.7 - +* +* Residue-by-residue listing for refined_15 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 - - -58.9 - - - - - - - 184.4 -.9 33.9 - * * 20 LYS 20 T a - - -59.2 178.2 - - - - - - 182.4 -2.5 34.4 - 21 SER 21 t B 53.3 - - - - - - - - - 173.4 -3.6 34.3 - * ** ** 22 LEU 22 E B - 185.7 - - - - - - - - 183.2 -3.4 32.7 - +* +* 23 GLU 23 E B - - -59.6 - - - - - - - 177.9 -.8 36.2 - +* +* 24 ILE 24 e B - - -63.8 - - - - - - - 176.8 -.9 34.3 - * * 25 PRO 25 h - - - - - -63.6 - - - - - 182.9 - 39.2 - +* +* 26 LEU 26 H A - - -69.4 - - -61.7 -33.3 - - - 178.9 - 31.3 - 27 GLY 27 H - - - - - - -70.7 -34.1 - - - 181.5 - - - 28 PHE 28 H A - 186.5 - - - -85.1 -20.6 - - - 178.9 - 33.5 - +* +* +* 29 ASN 29 H A - 183.3 - - - -60.9 -28.1 - - - 182.9 -2.0 36.0 - * * 30 GLU 30 h A - 183.8 - 183.9 - - - - - - 181.0 -.7 33.4 - +* +* 31 TYR 31 T A - - -60.4 - - - - - - - 179.4 -1.6 33.1 - 32 PHE 32 t B - - -57.7 - - - - - - - 181.4 -1.7 33.4 - 33 PRO 33 - - - - - -62.3 - - - - - 178.3 - 38.5 - * * 34 ALA 34 S A - - - - - - - - - - 176.5 - 32.1 - 35 PRO 35 S - - - - - -58.5 - - - - - 182.3 - 38.3 - * * 36 PHE 36 B - - -64.2 - - - - - - - 173.5 - 34.7 - * * 37 PRO 37 - - - - - -85.6 - - - - - 182.4 - 38.6 - +* * +* 38 ILE 38 e a - - -55.0 - - - - - - - 180.7 - 33.5 - 39 THR 39 E B 47.9 - - - - - - - - - 175.9 - 34.4 - * * 40 VAL 40 E B - - -68.1 - - - - - - - 181.1 -2.5 33.8 - 41 ASP 41 E B - - -67.1 - - - - - - - 185.1 -2.3 31.4 - 42 LEU 42 E B - 183.2 - - - - - - - - 177.1 -3.5 35.7 - +* +* 43 LEU 43 E B - - -75.3 - - - - - - - 179.1 -3.1 33.6 - * * 44 ASP 44 E B - 177.8 - - - - - - - - 177.6 -1.1 35.0 - * * 45 TYR 45 e A - 179.0 - - - - - - - - 176.7 -1.2 33.6 - * * 46 SER 46 T A - 180.6 - - - - - - - - 181.1 - 35.8 - 47 GLY 47 t - - - - - - - - - - - 179.6 -2.6 - - 48 ARG 48 e B - - -61.2 179.8 - - - - - - 179.0 - 33.8 - 49 SER 49 E B 52.0 - - - - - - - - - 177.0 - 33.8 - 50 TRP 50 E B - - -53.9 - - - - - - - 174.9 -1.8 38.2 - * * 51 THR 51 E B - - -55.8 - - - - - - - 185.5 - 34.4 - 52 VAL 52 E B - - -58.9 - - - - - - - 180.1 -2.4 32.5 - 53 ARG 53 E B - - -76.0 172.6 - - - - - - 184.3 -2.6 32.4 - 54 MET 54 E B - - -60.6 176.9 - - - - - - 178.8 -1.9 36.1 - 55 LYS 55 E B - - -62.5 184.5 - - - - - - 173.1 -2.4 34.2 - * * Residue-by-residue listing for refined_15 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 56 LYS 56 E B - - -68.5 - - - - - - - 179.5 - 34.8 - 57 ARG 57 E B - 178.8 - 180.6 - - - - - - 184.6 -3.0 33.8 - * * 58 GLY 58 T - - - - - - - - - - - 180.6 -.6 - - +* +* 59 GLU 59 T A - - -59.9 178.8 - - - - - - 183.2 -.6 34.6 - +* +* 60 LYS 60 E B 58.5 - - 180.0 - - - - - - 182.0 -1.9 33.0 - 61 VAL 61 E B - 184.0 - - - - - - - - 172.8 - 36.1 - * * 62 PHE 62 E B - - -68.7 - - - - - - - 175.6 -2.4 33.8 - 63 LEU 63 E B - - -70.5 - - - - - - - 185.8 -2.1 32.9 - 64 THR 64 e a - 179.4 - - - - - - - - 181.4 -.8 30.7 - +* +* 65 VAL 65 T B 64.2 - - - - - - - - - 188.0 - 31.6 - * * 66 GLY 66 h - - - - - - - - - - - 174.4 - - - 67 TRP 67 H A - 168.9 - - - -66.2 -28.7 - - - 180.9 - 35.6 - 68 GLU 68 H A - 191.6 - 177.6 - -64.8 -27.0 - - - 175.6 -1.1 33.1 - * * * 69 ASN 69 H A - - -64.6 - - -71.6 -35.6 - - - 180.9 -.7 34.4 - +* +* 70 PHE 70 H A - 171.9 - - - -73.5 -46.2 - - - 182.9 -.9 34.1 - * * 71 VAL 71 H A 73.9 - - - - -64.8 -43.8 - - - 178.6 -3.2 32.2 - +* +* 72 LYS 72 H A 68.8 - - 182.0 - -71.4 -28.9 - - - 182.1 -2.0 31.2 - 73 ASP 73 H A - 186.0 - - - -78.5 -42.3 - - - 185.4 -1.4 34.3 - * * 74 ASN 74 H A - 185.0 - - - -108.1 14.0 - - - 176.7 -3.2 32.4 - +*** *4.7* +* *4.7* 75 ASN 75 h XX - 183.0 - - - - - - - - 179.4 -.6 32.1 - **** +* **** 76 LEU 76 l - - -71.5 - - - - - - - 182.4 -2.4 28.6 - +* +* 77 GLU 77 t B 65.6 - - 175.3 - - - - - - 177.2 - 35.4 - 78 ASP 78 T B 58.6 - - - - - - - - - 182.1 - 33.8 - 79 GLY 79 T - - - - - - - - - - - 178.2 - - - 80 LYS 80 t B - - -61.8 - - - - - - - 188.1 -2.4 33.6 - * * 81 TYR 81 E B - 193.6 - - - - - - - - 187.0 -.9 35.3 - * * * 82 LEU 82 E B 62.2 - - 177.4 - - - - - - 178.0 -.7 31.7 - +* +* 83 GLN 83 E B - 182.8 - 184.1 - - - - - - 180.8 -2.7 35.8 - 84 PHE 84 E B - - -59.2 - - - - - - - 172.5 -3.6 36.2 - * ** ** 85 ILE 85 E B - - -64.3 - - - - - - - 180.1 -2.4 33.5 - 86 TYR 86 E B - 181.1 - - - - - - - - 184.9 -3.3 34.7 - +* +* 87 ASP 87 e A 68.4 - - - - - - - - - 177.4 -.6 32.9 - +* +* 88 ARG 88 S l - - -57.0 - - - - - - - 179.1 - 33.4 - 89 ASP 89 S b - 190.8 - - - - - - - - 185.6 - 34.1 - 90 ARG 90 e A - - -61.3 - - - - - - - 180.6 - 34.6 - 91 THR 91 E B - 179.5 - - - - - - - - 176.2 - 32.4 - 92 PHE 92 E B - - -64.2 - - - - - - - 175.6 -1.7 36.2 - Residue-by-residue listing for refined_15 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 - - -58.0 - - - - - - - 182.8 -2.6 34.2 - 94 VAL 94 E B - 179.7 - - - - - - - - 174.1 -3.4 34.4 - * +* +* 95 ILE 95 E B - - -66.6 - - - - - - - 178.8 -2.5 32.8 - 96 ILE 96 E B - 179.8 - 178.9 - - - - - - 179.0 -.5 34.1 - ** ** 97 TYR 97 E B - - -58.3 - - - - - - - 182.8 -3.6 34.5 - ** ** 98 GLY 98 S - - - - - - - - - - - 180.1 -.9 - - +* +* 99 HIS 99 b - - -61.6 - - - - - - - 177.6 - 33.4 - 100 ASN 100 S a - 180.2 - - - - - - - - 180.6 - 34.7 - 101 MET 101 b - 178.9 - 182.8 - - - - - - 181.6 - 34.7 - 102 CYS 102 - 52.3 - - - - - - - - - - - 31.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * +* +*** *4.7* +* ** +* *4.7* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.9 182.8 -62.3 179.9 -66.3 -73.6 -29.3 - - - 179.9 -2.0 34.0 Standard deviations: 7.8 5.7 5.8 3.2 10.9 16.0 14.1 - - - 3.6 1.0 2.0 Numbers of values: 16 31 41 24 5 16 16 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_15 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 1.517 1.538 1.457 - 116.35 121.02 109.64 109.76 111.21 122.62 2 ALA 2 1.299 1.239 1.513 1.521 1.435 121.80 116.10 120.89 111.26 109.03 110.81 122.99 ** * ** 3 ASP 3 1.308 1.241 1.509 1.530 1.447 121.07 115.28 121.35 110.54 111.44 111.76 123.37 +* +* 4 THR 4 1.303 1.239 1.541 1.540 1.436 122.43 115.26 121.29 109.73 108.60 109.39 123.44 +* * * +* 5 GLY 5 1.319 1.233 1.496 - 1.431 121.86 115.74 120.88 - 111.51 - 123.38 * * * 6 GLU 6 1.301 1.230 1.507 1.545 1.446 121.45 115.36 121.76 112.66 111.38 113.04 122.84 ** * * ** 7 VAL 7 1.293 1.240 1.507 1.555 1.429 121.88 116.12 120.90 110.57 109.66 112.44 122.96 +** +* +** 8 GLN 8 1.286 1.228 1.495 1.515 1.420 121.89 116.35 120.52 108.34 109.28 110.09 123.13 *** * +* *** 9 PHE 9 1.288 1.228 1.510 1.540 1.430 121.39 116.99 120.24 111.26 107.85 111.27 122.75 +** * * +** 10 MET 10 1.289 1.229 1.520 1.530 1.436 121.90 118.32 119.65 112.07 106.72 107.79 122.01 +** * * * +* +* +** 11 LYS 11 1.321 1.234 1.533 1.544 1.456 119.27 117.51 120.08 110.15 111.22 108.96 122.40 * * Residue-by-residue listing for refined_15 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 PRO 12 1.360 1.245 1.530 1.537 1.470 123.22 114.41 121.73 110.36 113.10 104.11 123.86 * +* * * +* 13 PHE 13 1.303 1.224 1.529 1.549 1.445 124.45 117.80 120.74 110.18 113.30 108.96 121.34 +* +* * +* 14 ILE 14 1.314 1.234 1.514 1.560 1.421 119.42 116.81 119.93 111.61 107.45 113.25 123.27 * +* * * * * +* 15 SER 15 1.324 1.224 1.504 1.522 1.460 122.60 115.86 120.93 111.63 112.13 110.83 123.20 16 GLU 16 1.310 1.232 1.510 1.524 1.434 121.66 116.43 121.03 109.36 108.34 111.30 122.53 * * * * 17 LYS 17 1.333 1.215 1.499 1.525 1.428 118.80 117.79 119.16 113.85 114.45 114.35 122.98 * +* +* +* * ** ** 18 SER 18 1.339 1.222 1.522 1.541 1.463 121.49 116.24 120.41 111.04 111.45 111.58 123.31 19 SER 19 1.334 1.228 1.537 1.525 1.453 122.08 116.81 120.78 110.65 112.09 109.94 122.40 20 LYS 20 1.323 1.244 1.529 1.524 1.447 121.01 117.09 120.16 109.90 112.69 109.81 122.75 21 SER 21 1.318 1.234 1.516 1.538 1.438 121.55 115.62 121.44 110.13 112.61 110.07 122.94 * * 22 LEU 22 1.299 1.245 1.496 1.550 1.415 121.01 113.99 121.44 112.89 106.45 112.07 124.51 ** * ** * * +* ** 23 GLU 23 1.284 1.237 1.531 1.527 1.426 123.66 116.22 120.55 110.05 110.65 107.97 123.23 *** +* * * *** 24 ILE 24 1.311 1.242 1.531 1.560 1.449 122.15 117.51 120.40 109.58 109.94 111.57 122.04 * * 25 PRO 25 1.345 1.233 1.525 1.536 1.470 122.91 116.89 120.32 109.64 110.92 103.59 122.76 26 LEU 26 1.322 1.223 1.526 1.551 1.469 121.68 116.45 120.66 111.16 112.36 113.07 122.85 * +* +* 27 GLY 27 1.311 1.223 1.517 - 1.449 120.92 116.29 121.03 - 111.91 - 122.66 * * 28 PHE 28 1.320 1.227 1.539 1.543 1.453 121.39 115.01 121.75 112.03 109.58 110.03 123.22 * * 29 ASN 29 1.320 1.237 1.537 1.538 1.472 124.24 115.91 121.28 109.18 110.76 108.73 122.77 * * * 30 GLU 30 1.330 1.231 1.539 1.534 1.460 122.20 116.52 121.48 110.67 112.06 110.61 121.98 31 TYR 31 1.299 1.227 1.518 1.530 1.451 121.00 116.50 120.75 110.52 111.05 111.67 122.75 ** ** 32 PHE 32 1.310 1.239 1.512 1.526 1.437 121.31 117.18 120.16 111.14 110.13 110.96 122.64 * * * 33 PRO 33 1.343 1.258 1.527 1.535 1.464 123.03 114.33 121.60 109.76 114.00 104.06 124.06 * +* * +* 34 ALA 34 1.325 1.233 1.546 1.528 1.453 123.34 119.84 119.12 111.60 112.36 111.23 121.03 * +* * +* 35 PRO 35 1.382 1.250 1.543 1.543 1.472 122.07 116.02 121.58 110.31 112.54 103.92 122.40 +** +** 36 PHE 36 1.298 1.231 1.524 1.521 1.415 122.32 117.54 120.73 110.44 111.58 109.46 121.66 ** ** ** 37 PRO 37 1.336 1.237 1.521 1.538 1.442 122.32 116.75 120.56 110.57 109.37 104.19 122.68 +* * +* 38 ILE 38 1.294 1.237 1.529 1.562 1.434 120.71 116.74 120.79 111.00 110.09 111.40 122.42 +** * +** 39 THR 39 1.314 1.242 1.510 1.549 1.437 121.03 115.09 121.17 109.19 111.62 111.27 123.74 * * * 40 VAL 40 1.299 1.237 1.511 1.566 1.445 124.15 117.39 120.01 109.67 107.95 112.99 122.60 ** * * ** 41 ASP 41 1.294 1.240 1.500 1.537 1.447 120.56 115.29 121.50 111.95 111.03 112.73 123.21 +** * * +** Residue-by-residue listing for refined_15 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 1.289 1.234 1.506 1.529 1.424 122.47 115.32 120.79 110.02 110.37 108.86 123.87 +** +* +** 43 LEU 43 1.306 1.221 1.504 1.552 1.435 123.01 115.76 120.78 110.07 109.56 112.31 123.46 +* * * * * +* 44 ASP 44 1.289 1.243 1.513 1.549 1.449 123.24 117.46 119.48 110.65 107.90 110.07 123.07 +** * +** 45 TYR 45 1.329 1.239 1.549 1.553 1.466 123.21 115.84 121.03 111.13 110.67 110.50 123.12 * * * 46 SER 46 1.329 1.229 1.541 1.542 1.437 123.99 116.35 120.95 110.19 110.59 108.38 122.70 * * * * 47 GLY 47 1.330 1.227 1.502 - 1.441 121.10 115.43 121.05 - 111.05 - 123.52 48 ARG 48 1.314 1.233 1.503 1.526 1.447 122.28 116.45 120.23 110.31 109.75 111.31 123.31 * * * 49 SER 49 1.298 1.239 1.526 1.534 1.427 121.45 115.06 121.38 111.37 111.20 109.92 123.51 ** +* ** 50 TRP 50 1.299 1.225 1.502 1.526 1.414 124.70 117.70 119.89 108.18 107.63 107.65 122.40 ** * ** +* * * +* ** 51 THR 51 1.282 1.237 1.518 1.538 1.422 120.02 116.34 120.90 111.12 106.63 110.89 122.73 *** +* +* *** 52 VAL 52 1.296 1.241 1.513 1.566 1.427 120.82 115.53 121.11 111.18 111.01 112.41 123.33 ** +* ** 53 ARG 53 1.294 1.242 1.510 1.529 1.428 122.50 115.35 121.20 113.10 110.85 110.25 123.45 +** +* +* +** 54 MET 54 1.307 1.228 1.499 1.537 1.449 122.37 116.69 120.45 108.33 109.42 110.26 122.85 +* * +* 55 LYS 55 1.301 1.238 1.506 1.534 1.438 120.76 115.62 120.76 109.21 110.98 111.64 123.61 ** * ** 56 LYS 56 1.312 1.241 1.502 1.527 1.429 122.56 115.07 121.36 108.86 107.66 112.07 123.56 * * +* * +* 57 ARG 57 1.258 1.241 1.494 1.523 1.429 122.81 115.48 120.98 111.16 107.98 111.14 123.50 *5.1* * +* * *5.1* 58 GLY 58 1.299 1.238 1.495 - 1.414 120.53 116.01 120.61 - 110.05 - 123.33 ** * ** ** 59 GLU 59 1.298 1.233 1.522 1.522 1.437 121.88 116.83 120.52 110.40 111.07 109.58 122.65 ** * ** 60 LYS 60 1.319 1.234 1.532 1.522 1.440 120.94 115.75 121.12 111.33 112.63 110.31 123.13 61 VAL 61 1.316 1.225 1.534 1.564 1.451 122.83 116.24 120.64 108.00 110.17 110.43 123.10 62 PHE 62 1.314 1.244 1.505 1.537 1.452 123.06 116.48 120.57 109.01 109.52 112.72 122.92 * * * 63 LEU 63 1.308 1.215 1.497 1.552 1.459 120.77 117.05 120.45 110.42 107.93 113.46 122.48 +* * * * +* +* 64 THR 64 1.297 1.236 1.542 1.568 1.436 119.53 117.99 120.34 113.38 113.37 111.37 121.66 ** * * * +* ** 65 VAL 65 1.311 1.236 1.535 1.557 1.432 119.74 116.63 120.89 113.51 108.79 111.96 122.40 * * * ** ** 66 GLY 66 1.308 1.222 1.511 - 1.444 120.69 114.91 121.62 - 109.50 - 123.45 +* * +* 67 TRP 67 1.326 1.223 1.495 1.551 1.446 124.08 114.93 121.34 109.64 108.12 110.22 123.70 * * * * * 68 GLU 68 1.315 1.223 1.550 1.533 1.432 121.61 115.86 121.25 112.72 108.90 110.12 122.80 * * * * 69 ASN 69 1.340 1.212 1.501 1.536 1.464 122.91 115.66 120.99 109.47 109.56 111.41 123.30 * * 70 PHE 70 1.309 1.235 1.496 1.534 1.449 122.59 115.56 120.95 110.44 110.62 110.67 123.49 * * * Residue-by-residue listing for refined_15 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 1.312 1.200 1.515 1.557 1.422 121.24 117.22 120.72 111.80 110.14 112.41 122.02 * +* +* * +* 72 LYS 72 1.312 1.235 1.525 1.538 1.444 119.27 117.30 120.22 111.32 111.42 113.38 122.48 * * +* +* 73 ASP 73 1.341 1.230 1.531 1.526 1.468 119.41 117.17 120.47 109.08 112.76 110.63 122.31 * * 74 ASN 74 1.320 1.234 1.533 1.549 1.449 121.26 114.77 121.96 114.33 110.23 109.19 123.28 ** ** 75 ASN 75 1.337 1.235 1.528 1.532 1.484 124.74 115.58 120.71 111.51 112.75 111.21 123.71 * +* +* 76 LEU 76 1.309 1.251 1.531 1.526 1.492 123.34 117.10 120.84 111.30 115.28 114.51 122.03 * * +* * ** ** 77 GLU 77 1.292 1.245 1.499 1.529 1.446 120.27 115.58 120.59 107.90 109.33 111.59 123.82 +** * * +** 78 ASP 78 1.316 1.236 1.529 1.548 1.442 121.92 115.50 121.53 111.01 108.35 111.26 122.82 * * 79 GLY 79 1.288 1.216 1.497 - 1.427 121.73 116.27 120.71 - 110.37 - 123.01 +** * * +** 80 LYS 80 1.317 1.224 1.510 1.530 1.445 121.09 116.49 120.41 111.57 108.77 110.79 123.09 81 TYR 81 1.303 1.229 1.514 1.543 1.442 121.97 117.94 119.59 113.11 107.26 107.16 122.44 +* +* * +* +* 82 LEU 82 1.309 1.240 1.531 1.562 1.449 120.16 115.07 121.11 111.83 113.71 111.46 123.80 * +* +* 83 GLN 83 1.325 1.230 1.533 1.543 1.457 123.84 117.00 120.00 109.18 108.52 109.82 123.00 * * 84 PHE 84 1.313 1.228 1.514 1.536 1.455 122.60 116.65 120.25 107.27 110.41 110.67 123.09 * * * 85 ILE 85 1.306 1.240 1.520 1.586 1.449 122.31 116.56 120.33 109.14 107.53 114.25 123.07 +* +* * +* +* 86 TYR 86 1.308 1.225 1.522 1.542 1.448 121.63 117.07 120.46 111.68 109.04 109.05 122.46 +* +* 87 ASP 87 1.317 1.232 1.512 1.531 1.468 121.18 114.97 121.17 111.42 112.03 110.64 123.77 88 ARG 88 1.331 1.242 1.533 1.551 1.478 124.25 116.92 120.71 109.71 111.75 111.80 122.37 * * * * 89 ASP 89 1.323 1.223 1.537 1.547 1.438 121.45 117.45 120.35 111.76 108.15 110.09 122.19 * * * 90 ARG 90 1.294 1.229 1.511 1.558 1.447 122.65 116.11 121.38 109.59 109.63 111.24 122.51 ** * ** 91 THR 91 1.301 1.237 1.534 1.556 1.422 120.59 115.54 121.06 111.67 111.86 111.52 123.32 +* +* * +* 92 PHE 92 1.318 1.235 1.508 1.534 1.452 122.92 116.92 120.05 106.87 108.57 111.59 123.03 +* +* 93 TYR 93 1.303 1.227 1.513 1.533 1.444 121.40 116.53 120.50 110.64 108.40 110.94 122.96 +* +* 94 VAL 94 1.304 1.229 1.520 1.561 1.446 121.97 115.97 121.19 109.56 111.01 111.16 122.74 +* +* 95 ILE 95 1.296 1.239 1.514 1.587 1.437 121.77 116.18 120.51 109.75 108.14 114.56 123.30 ** +* * * +* ** 96 ILE 96 1.301 1.243 1.520 1.570 1.436 121.94 115.67 121.38 110.78 109.06 111.19 122.88 ** * * ** 97 TYR 97 1.299 1.243 1.507 1.529 1.423 121.58 115.25 121.12 110.13 108.24 111.24 123.62 ** +* * ** 98 GLY 98 1.289 1.238 1.486 - 1.415 122.08 117.13 119.89 - 109.08 - 122.97 +** +* ** * +** Residue-by-residue listing for refined_15 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 1.308 1.231 1.513 1.542 1.448 121.33 116.39 120.85 109.90 110.87 112.01 122.71 * * 100 ASN 100 1.309 1.232 1.517 1.540 1.456 121.23 115.24 121.08 109.11 109.27 111.47 123.67 * * 101 MET 101 1.318 1.229 1.512 1.544 1.450 123.74 116.52 120.07 109.60 108.49 111.24 123.36 * * 102 CYS 102 1.313 - 1.534 1.539 1.448 122.30 - - 113.20 112.21 111.13 - * +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.1* +* +* +* ** +* +* ** +* ** * *5.1* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 1.258 1.341 1.309 .015 *5.1* * C-N (Pro) 1.341 .016 5 1.336 1.382 1.353 .016 +** C-O C-O 1.231 .020 101 1.200 1.258 1.233 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.494 1.550 1.519 .014 * * CH2G*-C (Gly) 1.516 .018 7 1.486 1.517 1.501 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.521 1.528 1.525 .003 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.538 1.587 1.561 .012 +* CH1E-CH2E (the rest) 1.530 .020 75 1.515 1.562 1.536 .010 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.414 1.492 1.444 .015 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.414 1.449 1.432 .013 ** * N-CH1E (Pro) 1.466 .015 5 1.442 1.472 1.464 .011 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 89 113.99 119.84 116.32 .95 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.91 117.13 115.97 .65 CH1E-C-N (Pro) 116.9 1.5 5 114.33 116.89 115.68 1.11 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.03 124.51 122.94 .58 * O-C-N (Pro) 122.0 1.4 5 122.40 124.06 123.15 .67 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.80 124.74 121.89 1.30 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 7 120.53 122.08 121.27 .57 C-N-CH1E (Pro) 122.6 5.0 5 122.07 123.22 122.71 .44 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.12 121.96 120.75 .57 CH2G*-C-O (Gly) 120.8 2.1 7 119.89 121.62 120.83 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 111.26 111.60 111.43 .17 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.00 113.51 110.62 1.41 ** CH2E-CH1E-C (the rest) 110.1 1.9 75 106.87 114.33 110.55 1.42 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 106.45 115.28 110.15 1.86 +* * NH1-CH2G*-C (Gly) 112.5 2.9 7 109.08 111.91 110.49 .97 * N-CH1E-C (Pro) 111.8 2.5 5 109.37 114.00 111.98 1.65 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 110.81 111.23 111.02 .21 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.39 114.56 111.91 1.25 * +* N-CH1E-CH2E (Pro) 103.0 1.1 5 103.59 104.19 103.97 .21 * NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.16 114.51 110.79 1.47 +* ** ------------------------------------------------------------------------------------------------------------- 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_15 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] 77 87.5% Residues in additional allowed regions [a,b,l,p] 10 11.4% 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 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 101 3.6 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 1.0 Inside f. Overall G-factor 102 .0 -.4 .3 1.2 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 16 7.8 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 31 5.7 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 41 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 24 3.2 20.4 5.0 -3.4 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% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 1.00 3 Residue-by-residue listing for refined_15 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.55 Chi1-chi2 distribution -.11 Chi1 only -.15 Chi3 & chi4 .47 Omega -.05 ------ -.16 ===== Main-chain covalent forces:- Main-chain bond lengths -.07 Main-chain bond angles .41 ------ .21 ===== OVERALL AVERAGE -.03 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.