Residue-by-residue listing for refined_3 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 - - 177.9 - - - - - - - - 178.6 - 34.2 - 2 ALA 2 b - - - - - - - - - - 178.1 - 33.6 - 3 ASP 3 b - 179.7 - - - - - - - - 174.3 - 32.3 - 4 THR 4 A - - -57.7 - - - - - - - 177.5 - 33.8 - 5 GLY 5 - - - - - - - - - - - 178.3 - - - 6 GLU 6 b - 182.9 - 185.6 - - - - - - 175.8 - 35.1 - 7 VAL 7 E B - - -60.1 - - - - - - - 182.6 -2.6 32.2 - 8 GLN 8 E B - 182.6 - 181.1 - - - - - - 177.6 - 35.7 - 9 PHE 9 E B 59.9 - - - - - - - - - 185.4 -2.3 31.1 - 10 MET 10 E B 57.2 - - 190.0 - - - - - - 181.2 - 34.8 - 11 LYS 11 E B - - -64.2 180.5 - - - - - - 169.4 -2.7 35.5 - +* +* 12 PRO 12 E - - - - - -74.8 - - - - - 179.3 - 38.7 - * * 13 PHE 13 e B - 181.9 - - - - - - - - 177.9 -2.4 35.0 - 14 ILE 14 t B - - -65.6 - - - - - - - 183.6 - 34.4 - 15 SER 15 T A - 183.9 - - - - - - - - 180.8 -.7 34.3 - +* +* 16 GLU 16 T A - 185.1 - 174.8 - - - - - - 183.3 - 34.7 - 17 LYS 17 T a - 190.4 - 190.7 - - - - - - 187.5 -.8 33.9 - * +* +* 18 SER 18 T A - - -52.9 - - - - - - - 176.0 -2.6 33.4 - 19 SER 19 T A - - -59.1 - - - - - - - 179.6 - 31.0 - 20 LYS 20 T a 60.8 - - 182.8 - - - - - - 180.1 -1.6 33.1 - 21 SER 21 t B - - -56.1 - - - - - - - 180.0 -1.7 35.0 - 22 LEU 22 E B - 193.8 - 177.6 - - - - - - 182.8 -2.5 34.9 - 23 GLU 23 E B 47.5 - - 172.7 - - - - - - 173.9 - 34.1 - * * * Residue-by-residue listing for refined_3 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 - - -63.2 180.2 - - - - - - 182.0 -2.6 33.3 - 25 PRO 25 h - - - - - -62.6 - - - - - 181.7 - 38.1 - * * 26 LEU 26 H A - 189.2 - 170.4 - -52.6 -40.1 - - - 180.3 - 34.6 - * * 27 GLY 27 H - - - - - - -59.2 -35.2 - - - 180.8 - - - 28 PHE 28 H A - - -60.7 - - -86.8 -23.3 - - - 176.5 -1.2 33.5 - +* * * +* 29 ASN 29 H A - 178.5 - - - -59.9 -46.4 - - - 180.4 -1.6 35.2 - 30 GLU 30 H A - 192.6 - - - -72.7 -32.5 - - - 184.0 -2.0 35.2 - 31 TYR 31 H A - 183.6 - - - -68.3 -27.2 - - - 176.6 -1.0 32.7 - * * * 32 PHE 32 h b 56.0 - - - - - - - - - 173.5 -1.5 29.9 - * * * 33 PRO 33 - - - - - -77.8 - - - - - 180.3 - 38.8 - * * * 34 ALA 34 B - - - - - - - - - - 173.9 - 35.0 - * * 35 PRO 35 - - - - - -63.1 - - - - - 186.0 - 38.7 - * * * 36 PHE 36 B 48.1 - - - - - - - - - 182.5 - 32.1 - * * 37 PRO 37 - - - - - -98.0 - - - - - 174.6 - 40.3 - +** +* +** 38 ILE 38 S A - - -59.1 - - - - - - - 177.6 - 33.1 - 39 THR 39 B 50.1 - - - - - - - - - 178.9 - 32.9 - 40 VAL 40 E B - 180.8 - - - - - - - - 178.5 -3.0 36.4 - * * 41 ASP 41 E B - - -67.0 - - - - - - - 177.9 -1.4 31.7 - 42 LEU 42 E B - - -59.9 173.8 - - - - - - 179.7 -3.8 37.1 - ** ** 43 LEU 43 E B - - -67.9 - - - - - - - 178.7 -2.7 32.7 - 44 ASP 44 e B - 190.5 - - - - - - - - 177.3 -1.5 36.8 - 45 TYR 45 S A - - -71.0 - - - - - - - 171.0 - 31.4 - +* +* 46 SER 46 S b - 186.1 - - - - - - - - 183.4 - 34.4 - 47 GLY 47 S - - - - - - - - - - - 182.4 - - - 48 ARG 48 e B - - -62.1 180.8 - - - - - - 179.6 - 32.1 - 49 SER 49 E B 54.2 - - - - - - - - - 179.4 - 34.3 - 50 TRP 50 E B - - -67.9 - - - - - - - 176.0 -2.7 34.0 - 51 THR 51 E B - - -56.2 - - - - - - - 184.1 - 34.4 - 52 VAL 52 E B 64.4 - - - - - - - - - 176.8 -3.6 34.4 - ** ** 53 ARG 53 e B - 186.0 - 176.9 - - - - - - 185.4 -2.1 36.9 - 54 MET 54 E B - 182.3 - - - - - - - - 183.1 -.6 34.2 - +* +* 55 LYS 55 E B - - -69.4 180.4 - - - - - - 170.1 -2.0 35.2 - +* +* 56 LYS 56 E B - - -60.1 - - - - - - - 187.1 - 37.3 - * * 57 ARG 57 E b - 184.3 - 180.9 - - - - - - 178.4 -2.5 33.9 - 58 GLY 58 T - - - - - - - - - - - 181.2 - - - 59 GLU 59 T A 63.0 - - - - - - - - - 184.3 -.6 34.4 - +* +* 60 LYS 60 E B - - -58.1 - - - - - - - 174.8 -2.0 36.0 - 61 VAL 61 E B - 177.5 - - - - - - - - 180.3 -1.5 33.8 - Residue-by-residue listing for refined_3 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 - - -65.0 - - - - - - - 170.9 -1.5 34.1 - +* +* 63 LEU 63 E B - - -65.5 - - - - - - - 184.7 -2.4 33.1 - 64 THR 64 e ~b 56.1 - - - - - - - - - 183.9 -1.9 34.4 - ** ** 65 VAL 65 T B - - -63.7 - - - - - - - 187.2 - 32.5 - * * 66 GLY 66 h - - - - - - - - - - - 172.7 - - - * * 67 TRP 67 H A - 169.3 - - - -65.7 -25.1 - - - 180.2 -1.9 34.7 - * * 68 GLU 68 H A - 179.4 - 179.9 - -66.6 -31.4 - - - 177.7 - 33.0 - 69 ASN 69 H A - - -62.7 - - -67.7 -41.4 - - - 182.6 -.7 34.7 - +* +* 70 PHE 70 H A - 182.2 - - - -70.5 -45.4 - - - 181.5 -1.2 35.4 - * * 71 VAL 71 H A 72.9 - - - - -62.3 -40.3 - - - 176.0 -3.2 33.4 - +* +* 72 LYS 72 H A - - -63.6 182.8 - -71.5 -44.9 - - - 181.7 -1.8 31.4 - 73 ASP 73 H A - - -85.5 - - -67.1 -41.7 - - - 180.9 -3.0 32.3 - * * * 74 ASN 74 H A - - -66.4 - - -89.2 -9.1 - - - 181.9 -3.3 33.0 - ** +** +* +** 75 ASN 75 h l - 181.1 - - - - - - - - 182.2 -.5 32.7 - ** ** 76 LEU 76 t B - - -57.8 176.0 - - - - - - 177.2 -2.0 35.0 - 77 GLU 77 t B - - -59.9 181.9 - - - - - - 183.5 -.6 33.5 - +* +* 78 ASP 78 T B - 190.8 - - - - - - - - 177.4 - 35.1 - 79 GLY 79 T - - - - - - - - - - - 180.3 -1.2 - - * * 80 LYS 80 e B - - -63.2 184.0 - - - - - - 188.9 -1.5 30.6 - +* +* 81 TYR 81 E B - 195.7 - - - - - - - - 184.8 - 34.8 - 82 LEU 82 E B - - -58.1 175.4 - - - - - - 169.9 -2.5 36.3 - +* +* 83 GLN 83 E B - - -67.0 200.5 - - - - - - 180.6 -2.0 31.9 - * * 84 PHE 84 E B - - -55.1 - - - - - - - 177.6 -3.0 34.6 - * * 85 ILE 85 E B - - -56.5 177.1 - - - - - - 180.0 -2.0 34.6 - 86 TYR 86 E B - 193.6 - - - - - - - - 181.8 -3.4 35.4 - +* +* 87 ASP 87 e A - - -64.8 - - - - - - - 186.6 -.9 35.1 - * * * 88 ARG 88 S l - - -75.9 171.5 - - - - - - 179.5 - 31.5 - 89 ASP 89 S b - 183.0 - - - - - - - - 176.5 - 36.6 - 90 ARG 90 e a - 183.7 - 167.2 - - - - - - 182.1 - 34.4 - 91 THR 91 E B - - -55.4 - - - - - - - 176.0 - 36.0 - 92 PHE 92 E B - - -73.9 - - - - - - - 177.1 -2.6 34.5 - 93 TYR 93 E B - - -53.1 - - - - - - - 184.2 -1.6 35.8 - 94 VAL 94 E B - 183.9 - - - - - - - - 176.7 -2.3 34.2 - 95 ILE 95 E B - - -61.9 - - - - - - - 178.9 -3.1 34.6 - * * 96 ILE 96 E B - 175.6 - 180.1 - - - - - - 180.8 -.6 33.3 - +* +* 97 TYR 97 e B - - -65.8 - - - - - - - 179.9 -2.0 32.5 - Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 GLY 98 - - - - - - - - - - - 178.7 -.8 - - +* +* 99 HIS 99 S a - 180.7 - - - - - - - - 179.1 - 33.7 - 100 ASN 100 S B - 184.2 - - - - - - - - 180.2 - 34.4 - 101 MET 101 b - 178.1 - 179.6 - - - - - - 177.8 - 34.7 - 102 CYS 102 - - - -57.9 - - - - - - - - -.6 35.7 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * +** ** +** +* ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.5 183.9 -62.8 179.8 -75.3 -68.6 -34.6 - - - 179.6 -1.9 34.3 Standard deviations: 7.3 5.7 6.4 6.7 14.4 9.8 10.6 - - - 4.0 .9 1.8 Numbers of values: 12 34 42 28 5 14 14 0 0 0 101 59 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_3 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 1.502 1.535 1.462 - 116.42 120.42 109.92 109.96 111.11 123.16 * * 2 ALA 2 1.305 1.237 1.509 1.525 1.433 122.10 115.90 121.07 110.68 109.79 111.30 122.96 +* * +* 3 ASP 3 1.304 1.233 1.492 1.542 1.437 121.36 115.31 121.42 110.70 110.42 113.13 123.11 +* +* * +* +* 4 THR 4 1.289 1.235 1.500 1.541 1.418 121.17 115.01 121.25 111.51 107.12 111.39 123.60 +** * ** * * +** 5 GLY 5 1.297 1.235 1.497 - 1.415 120.35 115.35 120.83 - 113.48 - 123.81 ** * ** ** 6 GLU 6 1.312 1.234 1.522 1.535 1.437 123.15 116.90 120.50 109.19 108.96 110.91 122.52 * * * 7 VAL 7 1.312 1.234 1.517 1.571 1.449 121.31 116.81 120.66 110.93 109.00 113.63 122.51 * * * * 8 GLN 8 1.294 1.239 1.510 1.539 1.431 121.29 116.69 120.52 110.38 109.04 108.92 122.79 +** * +** 9 PHE 9 1.296 1.239 1.499 1.549 1.437 121.16 115.74 120.68 112.80 110.08 112.81 123.58 ** * * * * ** 10 MET 10 1.297 1.235 1.521 1.548 1.436 122.19 116.66 120.69 112.03 110.58 108.24 122.65 ** * * * ** 11 LYS 11 1.324 1.235 1.516 1.550 1.454 122.01 116.95 121.04 107.04 111.19 111.87 121.97 * +* +* Residue-by-residue listing for refined_3 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 1.326 1.238 1.535 1.530 1.450 122.31 117.22 120.30 110.62 109.09 103.74 122.39 * * * 13 PHE 13 1.303 1.242 1.542 1.539 1.451 121.23 117.11 120.22 110.59 110.15 109.15 122.67 +* +* 14 ILE 14 1.338 1.224 1.519 1.595 1.430 121.91 117.13 120.03 109.74 106.62 112.83 122.84 ** * +* ** 15 SER 15 1.326 1.233 1.531 1.533 1.473 122.49 115.50 121.62 110.06 111.36 110.17 122.87 16 GLU 16 1.291 1.226 1.518 1.514 1.421 122.68 117.49 120.30 111.02 110.77 109.06 122.20 +** +* +** 17 LYS 17 1.327 1.238 1.514 1.518 1.462 118.50 115.69 121.29 109.20 112.03 111.33 123.00 +* +* 18 SER 18 1.307 1.210 1.527 1.522 1.429 121.72 117.92 120.10 111.35 112.75 109.83 121.97 +* * +* +* 19 SER 19 1.319 1.235 1.538 1.518 1.451 119.33 116.70 121.18 112.32 111.71 112.17 122.12 * * * 20 LYS 20 1.323 1.231 1.516 1.524 1.448 120.44 116.81 120.79 110.82 112.32 110.90 122.39 21 SER 21 1.305 1.228 1.530 1.531 1.440 121.44 116.42 120.56 109.94 110.18 109.87 123.03 +* +* 22 LEU 22 1.306 1.236 1.523 1.553 1.453 122.05 115.81 120.60 111.09 107.13 109.94 123.59 +* * * +* 23 GLU 23 1.297 1.240 1.539 1.532 1.443 122.96 115.97 121.11 110.62 113.29 109.44 122.91 ** ** 24 ILE 24 1.316 1.240 1.541 1.555 1.446 122.55 117.18 120.61 110.47 108.81 112.40 122.16 25 PRO 25 1.347 1.245 1.543 1.533 1.471 123.31 114.86 121.35 110.30 114.25 103.84 123.77 * * * 26 LEU 26 1.336 1.237 1.543 1.562 1.469 125.17 116.71 120.55 111.96 111.50 108.03 122.72 +* +* * +* 27 GLY 27 1.330 1.232 1.519 - 1.458 121.02 115.97 121.06 - 112.37 - 122.93 28 PHE 28 1.314 1.228 1.519 1.523 1.443 121.91 115.63 121.04 111.45 110.24 110.34 123.32 * * 29 ASN 29 1.323 1.230 1.524 1.543 1.461 122.52 115.51 120.95 109.72 109.51 110.02 123.48 30 GLU 30 1.319 1.232 1.549 1.560 1.456 122.75 116.03 121.28 111.95 109.05 107.99 122.58 * * * * 31 TYR 31 1.325 1.242 1.543 1.546 1.461 122.20 117.34 120.27 111.98 112.23 110.26 122.38 32 PHE 32 1.327 1.233 1.539 1.563 1.457 120.74 117.32 121.35 112.50 113.58 113.08 121.24 +* * +* * +* 33 PRO 33 1.344 1.248 1.534 1.543 1.454 123.04 116.07 121.11 110.08 110.70 103.95 122.80 34 ALA 34 1.300 1.234 1.507 1.529 1.439 122.33 119.24 119.23 110.24 108.28 110.16 121.46 ** * +* * ** 35 PRO 35 1.337 1.235 1.514 1.527 1.452 121.03 116.77 119.78 110.07 107.93 104.57 123.45 +* * * +* 36 PHE 36 1.310 1.235 1.532 1.540 1.416 122.81 116.31 121.41 113.51 112.14 109.90 122.23 * ** +* ** 37 PRO 37 1.340 1.239 1.523 1.519 1.440 123.83 115.81 121.48 109.47 113.00 101.92 122.64 +* +* 38 ILE 38 1.297 1.236 1.543 1.558 1.434 121.01 116.40 121.03 111.69 109.32 111.40 122.55 ** * * ** 39 THR 39 1.329 1.240 1.541 1.552 1.453 122.00 114.96 121.17 109.99 112.09 112.13 123.85 40 VAL 40 1.316 1.225 1.539 1.577 1.459 125.93 119.31 118.95 108.96 105.76 110.24 121.73 * ** +* * +* ** 41 ASP 41 1.316 1.242 1.514 1.539 1.464 119.91 114.50 121.51 110.18 112.53 113.35 123.99 +* +* 42 LEU 42 1.309 1.245 1.511 1.536 1.445 124.88 116.93 120.24 107.65 107.66 109.70 122.82 * +* * * +* Residue-by-residue listing for refined_3 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 1.295 1.245 1.515 1.551 1.437 121.01 115.10 121.11 110.77 111.19 112.23 123.79 ** * * * ** 44 ASP 44 1.310 1.233 1.526 1.553 1.454 123.00 117.07 120.12 108.71 107.16 109.36 122.81 * * * * 45 TYR 45 1.308 1.238 1.525 1.530 1.458 122.09 116.05 121.31 112.23 111.44 112.01 122.63 +* * +* 46 SER 46 1.311 1.233 1.542 1.549 1.425 121.72 118.48 120.00 111.90 106.03 110.14 121.51 * +* * +* +* 47 GLY 47 1.301 1.232 1.512 - 1.444 119.55 116.64 120.47 - 113.06 - 122.87 +* +* 48 ARG 48 1.313 1.244 1.525 1.505 1.440 121.68 115.95 120.75 112.03 112.48 110.77 123.30 * * * * 49 SER 49 1.314 1.241 1.531 1.531 1.442 122.91 116.49 120.62 111.04 110.09 109.73 122.86 * * 50 TRP 50 1.307 1.216 1.506 1.540 1.463 121.95 116.49 120.59 109.24 110.94 111.73 122.91 +* +* 51 THR 51 1.294 1.237 1.534 1.541 1.433 121.57 116.46 120.64 110.89 108.35 110.49 122.88 ** * * ** 52 VAL 52 1.305 1.217 1.529 1.561 1.438 122.41 116.12 120.93 110.35 110.64 110.54 122.94 +* * +* 53 ARG 53 1.290 1.224 1.530 1.535 1.442 122.74 117.82 119.85 111.30 105.93 106.64 122.33 +** +* ** +** 54 MET 54 1.315 1.225 1.496 1.558 1.471 121.62 116.67 120.01 111.66 109.41 109.87 123.31 * * * 55 LYS 55 1.317 1.239 1.500 1.495 1.416 121.36 114.67 121.44 108.27 113.29 110.13 123.89 * +* ** ** 56 LYS 56 1.302 1.235 1.505 1.507 1.423 123.34 116.83 120.43 108.22 103.88 109.31 122.71 +* * +* +** +** 57 ARG 57 1.263 1.238 1.514 1.538 1.444 120.67 115.41 121.12 110.99 111.76 110.01 123.45 *4.7* *4.7* 58 GLY 58 1.312 1.233 1.505 - 1.434 121.22 115.83 121.03 - 112.11 - 123.13 * * * 59 GLU 59 1.298 1.232 1.522 1.551 1.442 122.26 116.07 121.12 109.78 110.32 111.11 122.81 ** * ** 60 LYS 60 1.311 1.243 1.522 1.526 1.433 121.61 115.89 121.08 108.46 110.86 109.67 123.04 * * * 61 VAL 61 1.312 1.237 1.506 1.552 1.442 122.39 116.24 120.93 109.46 108.59 112.92 122.81 * * 62 PHE 62 1.298 1.244 1.496 1.544 1.434 120.81 115.68 121.02 108.94 111.06 112.16 123.28 ** * * ** 63 LEU 63 1.304 1.213 1.486 1.543 1.435 120.47 115.43 120.59 109.59 106.36 114.55 123.95 +* +* * +* ** ** 64 THR 64 1.283 1.241 1.555 1.550 1.436 123.55 116.73 120.65 111.77 111.77 108.49 122.62 *** * * * * +* *** 65 VAL 65 1.328 1.239 1.528 1.553 1.462 122.55 114.91 121.95 110.43 111.83 112.40 123.13 66 GLY 66 1.291 1.230 1.476 - 1.421 121.66 114.52 121.60 - 108.59 - 123.83 +** ** +* * +** 67 TRP 67 1.323 1.226 1.517 1.544 1.437 122.31 115.01 121.66 110.87 108.05 110.15 123.25 * * * 68 GLU 68 1.321 1.220 1.539 1.531 1.443 121.61 116.46 120.99 111.42 110.27 111.10 122.53 69 ASN 69 1.319 1.205 1.519 1.551 1.463 121.75 114.87 121.53 109.33 108.92 111.43 123.50 * * * 70 PHE 70 1.306 1.229 1.519 1.543 1.447 124.47 116.24 120.63 110.28 110.52 109.03 123.12 +* +* +* 71 VAL 71 1.329 1.234 1.516 1.561 1.449 121.65 115.12 121.27 110.60 109.70 111.94 123.61 Residue-by-residue listing for refined_3 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 1.313 1.242 1.527 1.529 1.445 121.72 117.39 120.00 111.46 112.10 112.65 122.60 * * * 73 ASP 73 1.343 1.231 1.507 1.538 1.479 120.49 117.35 119.98 108.79 113.60 113.42 122.59 * * +* +* 74 ASN 74 1.309 1.228 1.495 1.549 1.463 120.59 115.33 120.49 109.84 110.78 112.85 124.18 * * * * 75 ASN 75 1.333 1.236 1.520 1.524 1.465 124.13 115.91 121.79 111.01 110.89 111.67 122.24 * * 76 LEU 76 1.290 1.232 1.501 1.520 1.431 120.90 115.99 120.60 109.81 110.29 109.99 123.41 +** * * +** 77 GLU 77 1.307 1.250 1.514 1.528 1.438 122.32 116.14 120.10 110.94 108.83 111.49 123.76 +* * +* 78 ASP 78 1.319 1.241 1.520 1.534 1.466 122.87 116.41 120.67 109.01 110.88 110.35 122.90 79 GLY 79 1.307 1.225 1.500 - 1.436 119.99 117.08 120.30 - 112.94 - 122.61 +* +* 80 LYS 80 1.316 1.243 1.513 1.544 1.450 120.13 116.58 120.61 113.84 110.67 112.10 122.81 +* +* 81 TYR 81 1.308 1.247 1.506 1.532 1.429 120.60 116.39 120.00 111.23 109.09 109.33 123.61 * +* +* 82 LEU 82 1.318 1.239 1.524 1.538 1.437 121.67 116.15 120.98 108.29 111.35 109.40 122.84 * * 83 GLN 83 1.306 1.233 1.483 1.525 1.443 121.26 116.11 120.40 108.91 108.93 115.76 123.49 +* +* *** *** 84 PHE 84 1.291 1.240 1.505 1.529 1.423 121.37 115.89 120.78 110.47 109.23 110.40 123.27 +** +* +** 85 ILE 85 1.299 1.234 1.508 1.552 1.437 121.61 116.58 120.27 109.68 107.89 111.73 123.08 ** * * ** 86 TYR 86 1.296 1.226 1.535 1.536 1.429 121.39 117.22 120.72 111.94 108.38 107.84 122.05 ** +* * +* ** 87 ASP 87 1.312 1.213 1.524 1.550 1.488 121.26 117.73 119.57 107.25 111.95 111.73 122.70 * +* +* +* 88 ARG 88 1.357 1.230 1.526 1.518 1.495 122.78 113.92 121.84 111.55 111.41 112.25 124.21 +* +* * * +* 89 ASP 89 1.316 1.229 1.547 1.569 1.450 126.01 117.48 120.15 111.97 107.11 106.45 122.34 * +* ** * ** ** 90 ARG 90 1.298 1.226 1.543 1.541 1.436 123.87 114.53 122.70 113.66 107.02 108.04 122.73 ** * * * +* * * ** 91 THR 91 1.321 1.241 1.564 1.555 1.444 122.71 117.05 119.94 109.79 110.63 108.43 122.98 +* +* +* 92 PHE 92 1.351 1.234 1.526 1.543 1.481 122.70 115.86 120.88 107.22 111.19 112.81 123.26 +* * +* * +* 93 TYR 93 1.313 1.240 1.514 1.539 1.460 123.13 117.46 119.58 109.14 106.90 110.30 122.94 * +* +* 94 VAL 94 1.316 1.231 1.530 1.549 1.456 120.95 115.98 120.97 108.97 111.86 111.55 123.05 95 ILE 95 1.319 1.230 1.532 1.589 1.453 122.62 116.74 120.15 108.14 108.57 113.15 123.10 +* +* 96 ILE 96 1.312 1.233 1.520 1.573 1.459 122.39 116.01 120.89 110.60 110.00 112.08 123.10 * * * 97 TYR 97 1.309 1.237 1.507 1.526 1.443 121.38 114.83 121.37 111.72 111.81 111.10 123.80 * * 98 GLY 98 1.301 1.235 1.501 - 1.420 122.50 116.77 120.34 - 109.98 - 122.89 +* +* * +* 99 HIS 99 1.295 1.222 1.503 1.547 1.448 121.75 115.89 120.82 110.52 109.28 111.72 123.29 ** * ** Residue-by-residue listing for refined_3 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 1.303 1.237 1.508 1.540 1.436 121.33 116.10 120.11 110.76 108.36 110.68 123.75 +* * * +* 101 MET 101 1.307 1.240 1.518 1.524 1.452 123.46 115.60 120.83 110.41 111.07 109.51 123.49 +* +* 102 CYS 102 1.309 - 1.530 1.551 1.439 123.48 - - 109.21 107.89 110.37 - * * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.7* * ** ** ** ** +* * +* +** *** * *4.7* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 1.263 1.357 1.311 .014 *4.7* +* * C-N (Pro) 1.341 .016 5 1.326 1.347 1.339 .007 C-O C-O 1.231 .020 101 1.205 1.250 1.234 .008 * CA-C CH1E-C (except Gly) 1.525 .021 95 1.483 1.564 1.521 .015 +* +* CH2G*-C (Gly) 1.516 .018 7 1.476 1.519 1.501 .013 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.525 1.529 1.527 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.541 1.595 1.560 .015 ** CH1E-CH2E (the rest) 1.530 .020 75 1.495 1.569 1.537 .014 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.416 1.495 1.446 .015 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.415 1.458 1.433 .014 ** * N-CH1E (Pro) 1.466 .015 5 1.440 1.471 1.454 .010 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 89 113.92 119.31 116.31 .97 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.52 117.08 116.02 .83 CH1E-C-N (Pro) 116.9 1.5 5 114.86 117.22 116.15 .82 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.24 124.21 122.95 .59 * O-C-N (Pro) 122.0 1.4 5 122.39 123.77 123.01 .52 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.50 126.01 122.04 1.26 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.55 122.50 120.90 .94 * C-N-CH1E (Pro) 122.6 5.0 5 121.03 123.83 122.71 .97 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.95 122.70 120.74 .61 * * CH2G*-C-O (Gly) 120.8 2.1 7 120.30 121.60 120.81 .44 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.24 110.68 110.46 .22 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.14 111.77 110.22 .95 * CH2E-CH1E-C (the rest) 110.1 1.9 75 107.04 113.84 110.46 1.47 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 103.88 113.60 109.96 1.97 +** NH1-CH2G*-C (Gly) 112.5 2.9 7 108.59 113.48 111.79 1.68 * N-CH1E-C (Pro) 111.8 2.5 5 107.93 114.25 111.00 2.35 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 110.16 111.30 110.73 .57 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.43 113.63 111.54 1.41 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 101.92 104.57 103.61 .89 * NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.45 115.76 110.64 1.71 ** *** ------------------------------------------------------------------------------------------------------------- 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_3 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] 73 83.0% Residues in additional allowed regions [a,b,l,p] 14 15.9% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.1% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 88 83.0 83.8 10.0 -.1 Inside b. Omega angle st dev 101 4.0 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 59 .9 .8 .2 .3 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 12 7.3 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 34 5.7 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 42 6.4 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 88 7.2 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 28 6.7 20.4 5.0 -2.7 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% 83.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 3 Residue-by-residue listing for refined_3 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.51 Chi1-chi2 distribution -.17 Chi1 only -.15 Chi3 & chi4 .42 Omega -.13 ------ -.19 ===== Main-chain covalent forces:- Main-chain bond lengths -.02 Main-chain bond angles .38 ------ .21 ===== OVERALL AVERAGE -.05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.