Residue-by-residue listing for refined_19 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 - - 180.0 - 179.5 - - - - - - 179.4 - 33.8 - 2 ALA 2 b - - - - - - - - - - 180.2 - 34.7 - 3 ASP 3 B - 184.0 - - - - - - - - 181.9 - 33.9 - 4 THR 4 A - - -54.4 - - - - - - - 183.5 - 34.9 - 5 GLY 5 - - - - - - - - - - - 180.4 - - - 6 GLU 6 b - 186.0 - 174.5 - - - - - - 182.8 - 35.2 - 7 VAL 7 E B - - -61.8 - - - - - - - 179.2 -2.7 32.7 - 8 GLN 8 E B - - -65.0 - - - - - - - 175.1 - 35.7 - 9 PHE 9 E B - 183.1 - - - - - - - - 180.0 -2.0 34.8 - 10 MET 10 E B - 180.2 - 180.5 - - - - - - 180.8 - 34.5 - 11 LYS 11 E B - 188.5 - 187.1 - - - - - - 174.0 -1.3 36.3 - * * 12 PRO 12 - - - - - -53.5 - - - - - 180.7 - 39.3 - * +* +* 13 PHE 13 B - 183.6 - - - - - - - - 179.2 - 35.4 - 14 ILE 14 t B - - -57.6 178.1 - - - - - - 188.0 - 34.5 - * * 15 SER 15 T A - 186.2 - - - - - - - - 179.1 - 33.8 - 16 GLU 16 T A - 182.4 - 182.4 - - - - - - 183.0 - 34.0 - 17 LYS 17 T A - 192.9 - 180.5 - - - - - - 180.9 -1.5 32.9 - 18 SER 18 T A 58.2 - - - - - - - - - 172.9 -2.7 33.1 - * * 19 SER 19 T A 51.8 - - - - - - - - - 183.4 - 35.4 - 20 LYS 20 T a 57.0 - - 183.9 - - - - - - 185.2 -1.4 34.4 - 21 SER 21 t B 54.0 - - - - - - - - - 175.8 -2.1 35.7 - 22 LEU 22 E B - - -67.9 179.9 - - - - - - 177.4 -2.2 33.2 - 23 GLU 23 E B - - -60.1 172.6 - - - - - - 174.2 - 36.5 - Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 24 ILE 24 E B - - -63.2 180.5 - - - - - - 188.0 -2.8 32.3 - * * * 25 PRO 25 h - - - - - -49.8 - - - - - 178.8 - 38.1 - * * * 26 LEU 26 H A - 189.4 - 171.5 - -63.0 -37.8 - - - 178.3 - 34.8 - 27 GLY 27 H - - - - - - -67.8 -28.8 - - - 177.7 - - - 28 PHE 28 H A - 183.0 - - - -72.9 -42.9 - - - 174.8 - 35.2 - 29 ASN 29 H A - 170.9 - - - -63.0 -40.2 - - - 178.4 -2.4 34.6 - 30 GLU 30 H A - 179.1 - 182.8 - -63.2 -25.5 - - - 181.0 -2.7 35.6 - * * 31 TYR 31 H A - 184.2 - - - -80.6 -27.6 - - - 176.8 -.7 33.6 - * * +* +* 32 PHE 32 h b 61.7 - - - - - - - - - 172.0 -1.0 31.8 - * * * 33 PRO 33 - - - - - -89.1 - - - - - 180.5 - 38.2 - ** * ** 34 ALA 34 B - - - - - - - - - - 172.1 - 35.5 - * * 35 PRO 35 - - - - - -59.2 - - - - - 187.4 - 38.9 - * * * 36 PHE 36 B 57.0 - - - - - - - - - 175.9 - 31.2 - 37 PRO 37 - - - - - -66.4 - - - - - 181.4 - 39.0 - * * 38 ILE 38 S A - - -59.0 - - - - - - - 176.4 - 32.6 - 39 THR 39 B 50.5 - - - - - - - - - 180.5 - 32.8 - 40 VAL 40 E B - 177.2 - - - - - - - - 180.7 -3.1 35.2 - * * 41 ASP 41 E B - - -64.2 - - - - - - - 173.5 -2.1 34.9 - * * 42 LEU 42 E B - - -59.2 184.8 - - - - - - 180.1 -2.4 34.8 - 43 LEU 43 E B - - -67.3 - - - - - - - 176.2 -2.9 33.7 - * * 44 ASP 44 e B - 184.7 - - - - - - - - 181.2 -2.3 36.7 - 45 TYR 45 S A 59.1 - - - - - - - - - 172.7 - 30.8 - * * 46 SER 46 S b - 182.1 - - - - - - - - 182.7 - 35.1 - 47 GLY 47 S - - - - - - - - - - - 179.8 - - - 48 ARG 48 e B - - -81.6 - - - - - - - 179.2 - 30.5 - 49 SER 49 E B 53.2 - - - - - - - - - 180.2 - 35.8 - 50 TRP 50 E B - - -59.9 - - - - - - - 175.4 -2.9 33.5 - * * 51 THR 51 E B - - -57.8 - - - - - - - 185.1 - 35.4 - 52 VAL 52 E B - 182.8 - - - - - - - - 177.1 -2.5 35.1 - 53 ARG 53 e B - - -58.5 182.1 - - - - - - 180.9 -1.7 36.2 - 54 MET 54 E B - 177.3 - 179.3 - - - - - - 180.0 -1.2 35.2 - * * 55 LYS 55 E B - 184.8 - 181.8 - - - - - - 176.1 -3.1 33.2 - * * 56 LYS 56 E B - 171.5 - 168.2 - - - - - - 187.0 - 33.3 - * * 57 ARG 57 E b - 188.7 - - - - - - - - 180.4 -2.0 34.8 - 58 GLY 58 T - - - - - - - - - - - 184.1 - - - 59 GLU 59 T A - - -58.8 - - - - - - - 180.3 - 34.9 - 60 LYS 60 E B 58.6 - - 179.1 - - - - - - 180.3 -1.0 33.8 - * * 61 VAL 61 E B - 181.4 - - - - - - - - 176.5 -1.6 34.3 - Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 62 PHE 62 E B - - -66.7 - - - - - - - 174.8 -3.3 34.0 - +* +* 63 LEU 63 E B - 192.0 - - - - - - - - 189.8 -3.1 34.8 - +* * +* 64 THR 64 e b 52.3 - - - - - - - - - 186.2 -1.1 33.8 - * * * 65 VAL 65 T B 62.8 - - - - - - - - - 187.0 - 32.1 - * * 66 GLY 66 T - - - - - - - - - - - 172.0 - - - * * 67 TRP 67 h A - 156.2 - - - - - - - - 181.1 -1.4 35.3 - +* +* 68 GLU 68 H A - 190.8 - - - -53.3 -31.4 - - - 180.1 - 35.1 - * * 69 ASN 69 H A - - -61.4 - - -67.3 -30.6 - - - 181.5 -1.5 33.3 - 70 PHE 70 H A - 180.1 - - - -73.5 -53.0 - - - 181.7 -1.8 34.8 - * * 71 VAL 71 H A - 166.5 - - - -63.6 -39.1 - - - 174.8 -1.5 28.6 - * +* +* 72 LYS 72 H A 63.3 - - 184.2 - -71.4 -39.0 - - - 184.2 -2.5 30.0 - * * 73 ASP 73 H A - 178.4 - - - -77.6 -40.7 - - - 181.6 -2.1 32.7 - * * 74 ASN 74 H A - 191.4 - - - -84.9 -20.9 - - - 179.5 -3.4 34.6 - +* +* +* +* 75 ASN 75 h l - 189.4 - - - - - - - - 181.2 -.8 31.4 - +* +* 76 LEU 76 t B 50.3 - - - - - - - - - 180.0 -.7 31.4 - +* +* 77 GLU 77 t B 60.9 - - 182.6 - - - - - - 182.4 - 32.5 - 78 ASP 78 T B 62.7 - - - - - - - - - 184.5 - 32.5 - 79 GLY 79 T - - - - - - - - - - - 172.6 - - - * * 80 LYS 80 t B - - -62.2 180.4 - - - - - - 183.9 -1.4 34.5 - 81 TYR 81 E B - - -63.1 - - - - - - - 184.8 -.5 32.1 - ** ** 82 LEU 82 E B - - -53.8 181.9 - - - - - - 173.5 -.8 36.2 - * +* +* 83 GLN 83 E B - 191.1 - 174.1 - - - - - - 182.2 -2.9 35.3 - * * 84 PHE 84 E B - - -57.0 - - - - - - - 174.9 -3.5 35.9 - +* +* 85 ILE 85 E B - - -55.9 177.1 - - - - - - 187.4 -3.2 34.8 - * +* +* 86 TYR 86 E B - 177.0 - - - - - - - - 168.8 -3.0 33.9 - +* * +* 87 ASP 87 e B - 173.4 - - - - - - - - 183.0 -.8 32.9 - +* +* 88 ARG 88 S b - - -72.5 - - - - - - - 183.9 - 32.9 - 89 ASP 89 S ~b - 188.6 - - - - - - - - 183.2 -.8 35.6 - ** +* ** 90 ARG 90 e a - 190.2 - 183.6 - - - - - - 186.4 - 37.2 - * * 91 THR 91 E B - - -53.3 - - - - - - - 176.7 - 35.8 - 92 PHE 92 E B - - -67.1 - - - - - - - 174.8 -2.8 35.3 - 93 TYR 93 E B - - -60.9 - - - - - - - 184.6 -3.0 34.2 - * * Residue-by-residue listing for refined_19 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 - - -62.4 - - - - - - - 175.0 -3.0 33.1 - * * 95 ILE 95 E B - 181.5 - 177.3 - - - - - - 180.3 -1.9 32.8 - 96 ILE 96 E B 59.5 - - 176.3 - - - - - - 175.0 - 34.7 - 97 TYR 97 E B - - -72.6 - - - - - - - 181.9 -3.0 34.2 - * * 98 GLY 98 - - - - - - - - - - - 179.9 -.8 - - +* +* 99 HIS 99 l - 182.1 - - - - - - - - 185.0 - 32.2 - 100 ASN 100 S ~a - 180.8 - - - - - - - - 171.9 - 35.1 - ** * ** 101 MET 101 b - 177.4 - 181.1 - - - - - - 180.7 - 33.0 - 102 CYS 102 - - - -56.2 - - - - - - - - - 34.8 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* ** +* +* +* ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.2 182.2 -62.1 179.6 -63.6 -69.4 -35.2 - - - 179.8 -2.1 34.3 Standard deviations: 4.4 7.4 6.2 4.3 15.6 8.6 8.7 - - - 4.3 .9 1.9 Numbers of values: 17 41 30 29 5 13 13 0 0 0 101 53 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_19 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 - 1.237 1.518 1.538 1.462 - 115.51 120.92 110.40 110.63 110.91 123.54 2 ALA 2 1.314 1.236 1.510 1.529 1.444 123.60 117.10 119.90 110.07 108.19 110.71 122.99 * * * * 3 ASP 3 1.313 1.233 1.507 1.535 1.452 121.34 116.00 120.25 110.50 109.11 111.25 123.72 * * 4 THR 4 1.305 1.237 1.533 1.544 1.433 122.86 115.86 121.23 110.78 110.82 109.10 122.78 +* * * +* 5 GLY 5 1.292 1.245 1.503 - 1.432 120.26 116.21 119.87 - 110.73 - 123.92 +** * +** 6 GLU 6 1.320 1.237 1.526 1.548 1.457 123.41 117.37 120.07 110.94 107.34 109.49 122.49 * * 7 VAL 7 1.320 1.231 1.522 1.567 1.459 120.79 115.57 121.09 109.95 112.01 112.72 123.34 * * 8 GLN 8 1.306 1.243 1.516 1.544 1.433 123.06 116.11 120.59 107.39 109.49 111.76 123.30 +* * * +* 9 PHE 9 1.298 1.227 1.530 1.544 1.437 122.89 117.21 120.19 111.00 108.15 109.89 122.61 ** * * ** 10 MET 10 1.304 1.231 1.513 1.540 1.452 121.82 116.94 120.18 110.40 109.22 110.44 122.87 +* +* 11 LYS 11 1.318 1.239 1.527 1.532 1.444 121.10 117.93 119.54 108.68 109.36 109.44 122.50 12 PRO 12 1.359 1.245 1.537 1.529 1.470 123.04 116.35 120.98 109.44 111.62 103.44 122.67 * * Residue-by-residue listing for refined_19 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 1.305 1.236 1.533 1.542 1.438 122.30 117.15 120.01 111.15 109.12 108.42 122.81 +* * * +* 14 ILE 14 1.337 1.240 1.519 1.559 1.447 122.19 116.22 119.97 109.74 107.65 111.89 123.78 * * 15 SER 15 1.331 1.220 1.537 1.543 1.465 123.94 116.59 120.79 111.26 112.33 109.45 122.60 * * 16 GLU 16 1.317 1.231 1.517 1.531 1.440 121.64 117.26 120.53 109.66 110.12 111.56 122.17 17 LYS 17 1.325 1.235 1.515 1.528 1.440 118.40 116.46 120.73 111.21 110.22 111.64 122.75 +* +* 18 SER 18 1.331 1.218 1.524 1.521 1.447 121.37 116.36 120.93 111.23 111.38 110.66 122.70 19 SER 19 1.308 1.233 1.532 1.526 1.437 121.80 115.28 121.42 110.48 109.62 108.79 123.28 * * * * 20 LYS 20 1.322 1.229 1.528 1.538 1.445 122.29 116.98 120.35 110.50 112.38 109.51 122.67 21 SER 21 1.325 1.233 1.524 1.539 1.444 120.79 116.63 120.63 109.89 111.64 108.58 122.74 * * 22 LEU 22 1.310 1.233 1.496 1.531 1.448 121.29 115.22 120.99 108.87 110.74 113.42 123.78 * * +* +* 23 GLU 23 1.298 1.225 1.503 1.515 1.434 122.50 116.85 120.46 108.56 109.40 109.27 122.65 ** * * ** 24 ILE 24 1.281 1.243 1.522 1.551 1.416 120.62 116.77 120.33 113.11 106.89 112.06 122.82 *** ** +* +* *** 25 PRO 25 1.352 1.240 1.521 1.525 1.467 123.62 114.94 121.46 110.40 114.63 103.69 123.59 * * * * 26 LEU 26 1.319 1.215 1.526 1.563 1.446 123.42 116.14 120.82 112.26 108.13 108.75 122.99 +* * * * +* 27 GLY 27 1.332 1.230 1.521 - 1.454 121.38 116.08 120.67 - 112.31 - 123.25 28 PHE 28 1.319 1.225 1.526 1.544 1.461 122.63 115.18 121.45 111.64 107.63 108.57 123.34 * * * 29 ASN 29 1.325 1.216 1.530 1.534 1.463 122.95 115.64 121.37 110.12 110.71 110.00 122.99 30 GLU 30 1.317 1.237 1.530 1.536 1.458 123.61 115.64 121.36 109.87 110.35 108.91 123.00 * * 31 TYR 31 1.306 1.244 1.546 1.540 1.428 122.34 116.58 120.25 113.26 110.20 108.58 123.14 +* +* +* * +* 32 PHE 32 1.348 1.225 1.549 1.567 1.470 122.76 118.48 120.99 110.83 112.50 112.71 120.44 * * +* * * +* +* 33 PRO 33 1.339 1.247 1.512 1.514 1.425 121.37 115.20 121.46 110.19 111.31 104.69 123.34 +** * +* +** 34 ALA 34 1.284 1.240 1.506 1.533 1.438 122.76 119.01 118.86 110.23 108.13 109.59 122.06 *** * * * * *** 35 PRO 35 1.354 1.238 1.517 1.535 1.459 121.65 117.43 120.01 110.47 107.70 103.91 122.55 +* +* 36 PHE 36 1.300 1.230 1.524 1.519 1.407 120.64 116.73 121.15 112.58 113.63 111.17 122.07 ** +** * +** 37 PRO 37 1.333 1.242 1.526 1.535 1.456 122.52 116.50 120.59 110.24 110.36 103.50 122.90 38 ILE 38 1.320 1.235 1.522 1.555 1.453 121.19 116.49 120.57 111.35 110.21 112.01 122.90 * * 39 THR 39 1.312 1.222 1.522 1.550 1.432 121.14 115.87 120.59 111.10 110.36 111.99 123.53 * * * 40 VAL 40 1.305 1.252 1.517 1.572 1.447 124.24 117.13 120.10 110.07 108.04 110.50 122.76 +* * * * * +* 41 ASP 41 1.308 1.237 1.497 1.547 1.438 121.19 115.84 120.80 108.35 110.33 111.83 123.35 * * * * 42 LEU 42 1.309 1.236 1.494 1.541 1.434 121.39 116.45 120.48 108.69 106.86 112.69 123.02 * * * +* * +* Residue-by-residue listing for refined_19 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 LEU 43 1.284 1.231 1.493 1.552 1.433 121.03 115.12 120.90 109.53 110.36 112.56 123.97 *** +* * * * *** 44 ASP 44 1.289 1.237 1.507 1.548 1.441 122.88 117.60 119.55 109.29 105.05 109.49 122.84 +** ** +** 45 TYR 45 1.304 1.231 1.537 1.543 1.457 121.30 115.65 121.22 113.22 111.67 111.90 123.13 +* +* +* 46 SER 46 1.312 1.240 1.553 1.549 1.437 123.09 117.73 120.27 111.62 107.36 108.86 122.00 * * * * * 47 GLY 47 1.312 1.233 1.530 - 1.454 121.17 117.48 120.43 - 114.10 - 122.09 * * 48 ARG 48 1.316 1.239 1.519 1.522 1.454 121.20 113.95 121.95 110.80 114.63 113.29 124.10 * * +* +* 49 SER 49 1.307 1.238 1.531 1.535 1.430 124.79 117.84 120.07 110.67 107.96 108.57 122.06 +* * +* * * +* 50 TRP 50 1.308 1.245 1.527 1.539 1.463 120.43 115.54 121.01 109.93 112.16 111.24 123.43 +* +* 51 THR 51 1.322 1.240 1.531 1.546 1.452 123.12 116.32 120.86 109.07 108.41 110.61 122.82 52 VAL 52 1.308 1.215 1.530 1.561 1.450 121.89 117.33 119.78 110.16 110.00 109.76 122.87 * * * 53 ARG 53 1.320 1.229 1.522 1.531 1.454 122.25 117.38 120.08 108.39 108.37 110.07 122.53 * * 54 MET 54 1.304 1.225 1.504 1.526 1.463 122.03 117.55 120.10 110.15 109.45 109.44 122.35 +* +* 55 LYS 55 1.314 1.228 1.522 1.525 1.440 119.25 115.76 121.22 109.95 112.58 111.45 123.02 * * * 56 LYS 56 1.312 1.236 1.484 1.523 1.438 122.41 114.57 121.48 111.76 108.46 111.25 123.95 * +* * +* 57 ARG 57 1.267 1.236 1.512 1.557 1.421 122.21 115.23 121.36 113.02 108.28 108.12 123.34 **** * +* +* * * **** 58 GLY 58 1.301 1.247 1.510 - 1.423 120.90 115.49 121.06 - 111.87 - 123.40 ** +* ** 59 GLU 59 1.309 1.227 1.523 1.543 1.455 122.74 116.05 121.21 108.96 110.46 110.97 122.74 * * 60 LYS 60 1.304 1.239 1.514 1.528 1.415 122.24 116.67 120.70 111.34 109.48 110.53 122.60 +* ** ** 61 VAL 61 1.295 1.227 1.521 1.571 1.437 121.26 116.73 120.53 110.25 108.80 111.52 122.70 ** * * ** 62 PHE 62 1.299 1.240 1.493 1.533 1.430 121.90 116.17 121.03 109.32 109.52 112.33 122.77 ** +* * * ** 63 LEU 63 1.285 1.220 1.516 1.517 1.412 120.09 115.44 120.58 110.87 104.97 110.62 123.94 *** ** ** *** 64 THR 64 1.300 1.241 1.557 1.546 1.448 123.96 115.38 121.26 111.66 114.38 108.36 123.35 ** +* * * * +* ** 65 VAL 65 1.339 1.227 1.541 1.568 1.459 124.19 115.44 121.49 111.91 111.83 111.56 123.00 * * * * 66 GLY 66 1.306 1.229 1.485 - 1.439 121.71 113.69 122.09 - 107.69 - 124.18 +* +* * +* +* 67 TRP 67 1.327 1.237 1.536 1.550 1.450 124.06 113.86 122.14 111.00 109.37 108.70 123.93 * * * * 68 GLU 68 1.311 1.224 1.554 1.564 1.454 125.50 116.09 120.79 114.08 109.55 105.82 122.89 * * +* ** ** +** +** 69 ASN 69 1.338 1.211 1.514 1.548 1.469 123.33 116.83 120.29 109.32 112.00 112.37 122.87 * * * 70 PHE 70 1.310 1.225 1.495 1.543 1.450 122.41 115.84 120.83 109.62 108.91 111.06 123.31 * * * Residue-by-residue listing for refined_19 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 1.320 1.227 1.520 1.567 1.438 120.86 117.85 119.88 114.34 111.99 113.76 122.25 * ** * ** 72 LYS 72 1.328 1.230 1.543 1.543 1.458 118.37 117.81 120.19 111.96 112.44 113.73 121.99 +* +* +* 73 ASP 73 1.345 1.230 1.517 1.528 1.490 119.90 116.88 120.66 109.55 113.65 111.93 122.44 * +* * +* 74 ASN 74 1.305 1.232 1.527 1.553 1.452 120.68 113.99 121.50 112.43 107.71 108.79 124.30 +* * * * * * +* 75 ASN 75 1.333 1.239 1.520 1.537 1.468 125.81 115.59 121.33 111.67 112.36 112.30 123.04 ** * ** 76 LEU 76 1.310 1.239 1.519 1.563 1.441 122.07 115.56 120.76 112.79 111.87 111.72 123.68 * +* * +* 77 GLU 77 1.302 1.244 1.512 1.530 1.438 124.08 116.33 119.91 111.57 108.98 112.30 123.72 +* * * * +* 78 ASP 78 1.321 1.235 1.516 1.529 1.467 122.75 114.31 121.91 110.73 111.74 111.94 123.74 79 GLY 79 1.294 1.221 1.487 - 1.434 123.11 114.55 121.74 - 107.18 - 123.71 ** +* * * +* ** 80 LYS 80 1.314 1.238 1.516 1.536 1.436 122.45 117.47 119.89 110.69 106.85 110.99 122.63 * * +* +* 81 TYR 81 1.304 1.235 1.497 1.533 1.446 120.78 116.15 120.45 112.29 111.19 111.40 123.39 +* * * +* 82 LEU 82 1.311 1.244 1.506 1.534 1.440 121.55 115.81 120.75 107.76 110.56 110.27 123.43 * * * 83 GLN 83 1.301 1.238 1.509 1.517 1.427 121.83 116.61 120.17 109.30 106.27 111.09 123.20 +* +* +* +* 84 PHE 84 1.292 1.225 1.506 1.538 1.432 121.79 116.79 120.40 108.84 109.30 110.12 122.78 +** * +** 85 ILE 85 1.293 1.244 1.518 1.544 1.432 121.05 116.09 120.84 110.63 106.23 110.91 123.04 +** * +* +** 86 TYR 86 1.298 1.236 1.523 1.560 1.437 121.31 114.27 121.69 111.27 113.09 109.42 124.02 ** +* * ** 87 ASP 87 1.302 1.225 1.497 1.527 1.430 124.60 116.71 118.94 110.59 106.34 113.67 124.30 +* * * +* * +* +* +* 88 ARG 88 1.319 1.236 1.517 1.541 1.467 124.31 114.49 121.53 110.69 111.82 111.49 123.97 * * 89 ASP 89 1.304 1.232 1.528 1.568 1.423 124.79 117.50 119.94 111.28 104.71 109.62 122.53 +* +* +* +* ** ** 90 ARG 90 1.276 1.236 1.540 1.528 1.438 123.00 115.43 121.97 110.78 107.57 106.19 122.56 +*** * * +** +*** 91 THR 91 1.317 1.234 1.541 1.544 1.436 121.41 116.19 120.73 109.77 111.43 108.68 123.07 * +* +* 92 PHE 92 1.325 1.237 1.518 1.544 1.457 122.67 116.71 120.63 107.78 109.42 111.78 122.66 * * 93 TYR 93 1.300 1.227 1.508 1.531 1.444 121.47 116.97 120.48 110.38 107.58 111.34 122.53 ** * ** 94 VAL 94 1.298 1.240 1.516 1.557 1.434 120.77 115.39 121.35 110.11 112.14 112.09 123.21 ** * ** 95 ILE 95 1.298 1.235 1.519 1.574 1.435 122.72 116.39 120.64 111.27 108.33 112.76 122.90 ** * * * ** 96 ILE 96 1.297 1.235 1.507 1.550 1.410 122.17 116.37 120.62 109.55 109.86 111.25 122.99 ** +** +** 97 TYR 97 1.299 1.239 1.493 1.530 1.432 120.58 114.94 121.23 109.63 108.02 112.16 123.79 ** +* * * ** 98 GLY 98 1.290 1.229 1.488 - 1.410 122.11 116.09 119.76 - 109.44 - 124.09 +** +* +** * +** Residue-by-residue listing for refined_19 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 1.333 1.227 1.527 1.552 1.464 123.02 115.22 121.50 112.38 110.08 111.44 123.26 * * * 100 ASN 100 1.299 1.230 1.502 1.543 1.459 123.30 114.61 121.67 110.40 107.20 110.24 123.72 ** * * ** 101 MET 101 1.312 1.234 1.516 1.551 1.440 122.81 114.73 121.77 111.67 107.11 112.22 123.11 * * * * * 102 CYS 102 1.307 - 1.520 1.550 1.437 122.98 - - 110.35 107.72 110.70 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +* +** ** * * ** ** +** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 Page 10 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 96 1.267 1.348 1.310 .015 **** * * C-N (Pro) 1.341 .016 5 1.333 1.359 1.347 .010 * C-O C-O 1.231 .020 101 1.211 1.252 1.233 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.484 1.557 1.520 .014 +* +* CH2G*-C (Gly) 1.516 .018 7 1.485 1.530 1.503 .016 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.529 1.533 1.531 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.544 1.574 1.557 .010 * CH1E-CH2E (the rest) 1.530 .020 75 1.514 1.568 1.538 .012 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.407 1.490 1.444 .015 +** +* NH1-CH2G* (Gly) 1.451 .016 7 1.410 1.454 1.435 .015 +** N-CH1E (Pro) 1.466 .015 5 1.425 1.470 1.455 .016 +** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_19 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 89 113.86 119.01 116.22 1.04 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 113.69 117.48 115.66 1.14 * CH1E-C-N (Pro) 116.9 1.5 5 114.94 117.43 116.08 .91 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.44 124.30 123.06 .63 +* O-C-N (Pro) 122.0 1.4 5 122.55 123.59 123.01 .40 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.37 125.81 122.20 1.40 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 7 120.26 123.11 121.52 .85 * C-N-CH1E (Pro) 122.6 5.0 5 121.37 123.62 122.44 .84 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.86 122.14 120.73 .64 * CH2G*-C-O (Gly) 120.8 2.1 7 119.76 122.09 120.80 .82 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.07 110.23 110.15 .08 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 109.07 114.34 110.82 1.28 ** CH2E-CH1E-C (the rest) 110.1 1.9 75 107.39 114.08 110.53 1.35 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.71 114.63 109.67 2.14 ** * NH1-CH2G*-C (Gly) 112.5 2.9 7 107.18 114.10 110.47 2.34 +* N-CH1E-C (Pro) 111.8 2.5 5 107.70 114.63 111.12 2.23 +* * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.59 110.71 110.15 .56 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.36 113.76 111.20 1.43 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.44 104.69 103.85 .45 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 105.82 113.73 110.62 1.63 +** +* ------------------------------------------------------------------------------------------------------------- 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_19 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] 74 84.1% Residues in additional allowed regions [a,b,l,p] 12 13.6% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% 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 84.1 83.8 10.0 .0 Inside b. Omega angle st dev 101 4.3 6.0 3.0 -.6 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 53 .9 .8 .2 .3 Inside f. Overall G-factor 102 -.1 -.4 .3 1.0 Inside S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 17 4.4 18.1 6.5 -2.1 BETTER b. Chi-1 trans st dev 41 7.4 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 30 6.2 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 88 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 29 4.3 20.4 5.0 -3.2 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% 84.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 2 Residue-by-residue listing for refined_19 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.60 Chi1-chi2 distribution -.14 Chi1 only .12 Chi3 & chi4 .23 Omega -.24 ------ -.25 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .34 ------ .18 ===== OVERALL AVERAGE -.10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.