Residue-by-residue listing for refined_1 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 - - 180.7 - - - - - - - - 180.1 - 34.2 - 2 ALA 2 l - - - - - - - - - - 186.0 - 33.1 - * * 3 ASP 3 l - 183.1 - - - - - - - - 184.0 - 29.8 - * * 4 THR 4 A - - -54.0 - - - - - - - 180.8 - 34.0 - 5 GLY 5 S - - - - - - - - - - - 177.6 - - - 6 GLU 6 l - 182.4 - 175.7 - - - - - - 180.1 -2.4 30.5 - 7 VAL 7 E B - - -64.1 - - - - - - - 180.7 -2.3 33.9 - 8 GLN 8 E B 53.3 - - 181.2 - - - - - - 177.3 - 33.8 - 9 PHE 9 E B - 180.0 - - - - - - - - 179.9 -2.0 35.1 - 10 MET 10 E B 60.4 - - 176.7 - - - - - - 183.2 - 31.6 - 11 LYS 11 E B - 183.2 - - - - - - - - 174.4 -2.5 34.8 - 12 PRO 12 E - - - - - -84.8 - - - - - 183.5 - 39.7 - +* +* +* 13 PHE 13 e B 55.4 - - - - - - - - - 179.9 -.8 31.7 - +* +* 14 ILE 14 h B - - -58.3 176.8 - - - - - - 186.0 - 35.1 - * * 15 SER 15 H A - - -50.9 - - -52.6 -30.4 - - - 180.5 -.6 36.3 - * * +* +* 16 GLU 16 H A - 182.1 - 181.8 - -60.6 -36.7 - - - 185.4 - 36.8 - 17 LYS 17 H a - - -59.0 174.6 - -110.6 -37.7 - - - 181.8 -2.1 33.0 - +*** +*** 18 SER 18 H A 58.7 - - - - -74.7 -2.8 - - - 173.6 -3.5 32.7 - *** * +* *** 19 SER 19 h A 47.5 - - - - - - - - - 180.2 -.8 33.3 - * +* +* Residue-by-residue listing for refined_1 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 LYS 20 T a - 182.5 - - - - - - - - 181.8 -1.8 33.9 - 21 SER 21 t B 51.1 - - - - - - - - - 180.4 -1.9 34.6 - 22 LEU 22 E B - 190.5 - 170.2 - - - - - - 183.7 -3.3 31.9 - +* +* 23 GLU 23 E B - 197.6 - - - - - - - - 184.2 -.7 36.2 - +* +* 24 ILE 24 e B - - -63.5 - - - - - - - 177.1 -.9 34.3 - * * 25 PRO 25 h - - - - - -61.2 - - - - - 182.7 - 39.1 - * * 26 LEU 26 H A - - -62.3 180.9 - -63.6 -26.3 - - - 177.3 - 31.5 - * * 27 GLY 27 H - - - - - - -70.4 -30.8 - - - 177.5 - - - 28 PHE 28 H A - 185.8 - - - -77.1 -39.6 - - - 179.2 -.9 37.1 - +* +* 29 ASN 29 H A - 176.4 - - - -63.9 -47.6 - - - 183.0 -2.5 37.3 - 30 GLU 30 h A - 183.2 - 179.0 - - - - - - 180.1 -3.2 34.8 - +* +* 31 TYR 31 T A - 180.4 - - - - - - - - 178.8 - 33.5 - 32 PHE 32 t b 65.2 - - - - - - - - - 167.4 -1.2 32.1 - ** * ** 33 PRO 33 - - - - - -81.4 - - - - - 187.6 - 39.0 - * * * * 34 ALA 34 B - - - - - - - - - - 171.8 - 34.7 - * * 35 PRO 35 - - - - - -67.6 - - - - - 183.2 - 38.9 - * * 36 PHE 36 B 53.6 - - - - - - - - - 177.2 - 32.0 - 37 PRO 37 - - - - - -88.3 - - - - - 179.9 - 39.1 - ** * ** 38 ILE 38 S A - - -60.0 - - - - - - - 176.9 - 32.1 - 39 THR 39 B 49.6 - - - - - - - - - 180.6 - 32.0 - 40 VAL 40 E B - 175.4 - - - - - - - - 181.4 -3.3 36.4 - +* +* 41 ASP 41 E B - - -71.2 - - - - - - - 174.4 - 32.8 - 42 LEU 42 E B - - -59.0 182.0 - - - - - - 183.6 -2.9 35.5 - * * 43 LEU 43 E B - - -62.4 - - - - - - - 174.2 -3.0 34.2 - * * 44 ASP 44 e B - 169.8 - - - - - - - - 184.1 -3.1 34.8 - * * 45 TYR 45 T A - 184.3 - - - - - - - - 181.5 - 34.4 - 46 SER 46 T A - 183.3 - - - - - - - - 175.4 - 33.2 - 47 GLY 47 t - - - - - - - - - - - 180.5 -1.9 - - 48 ARG 48 e B - - -75.8 - - - - - - - 175.9 - 31.1 - 49 SER 49 E B 57.2 - - - - - - - - - 176.9 - 33.3 - 50 TRP 50 E B - - -62.3 - - - - - - - 177.6 -2.6 34.8 - 51 THR 51 E B - - -57.1 - - - - - - - 184.8 - 33.5 - 52 VAL 52 E B - - -60.7 - - - - - - - 179.3 -2.9 34.1 - * * 53 ARG 53 e B - 185.7 - 171.6 - - - - - - 179.4 -2.2 34.9 - 54 MET 54 E B - 182.8 - 179.8 - - - - - - 186.2 -.6 34.2 - * +* +* 55 LYS 55 E B - 184.6 - 182.6 - - - - - - 169.9 -3.0 36.4 - +* * +* 56 LYS 56 E B - - -81.3 - - - - - - - 183.7 - 36.0 - Residue-by-residue listing for refined_1 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 ARG 57 E B 46.9 - - 173.2 - - - - - - 183.8 -3.2 32.1 - * +* +* 58 GLY 58 T - - - - - - - - - - - 176.4 - - - 59 GLU 59 T A - - -59.4 176.4 - - - - - - 187.7 -.8 34.9 - * +* +* 60 LYS 60 E B 60.5 - - 179.3 - - - - - - 179.4 -1.5 33.3 - 61 VAL 61 E B - 183.2 - - - - - - - - 169.8 - 36.5 - +* +* 62 PHE 62 E B - - -83.3 - - - - - - - 174.7 -2.5 33.8 - * * 63 LEU 63 E B - 192.3 - 172.2 - - - - - - 193.9 -2.5 34.1 - ** ** 64 THR 64 e b - - -40.9 - - - - - - - 184.7 -2.5 35.8 - +* +* 65 VAL 65 T B - - -63.8 - - - - - - - 187.3 - 32.6 - * * 66 GLY 66 h - - - - - - - - - - - 172.8 - - - * * 67 TRP 67 H A - 167.4 - - - -58.6 -27.2 - - - 184.6 -1.8 36.8 - * * 68 GLU 68 H A - 193.1 - 186.8 - -63.8 -29.3 - - - 178.2 - 34.7 - 69 ASN 69 H A - - -64.2 - - -65.1 -39.7 - - - 182.3 -1.4 34.0 - 70 PHE 70 H A - 180.4 - - - -74.0 -45.8 - - - 181.6 -.7 34.0 - +* +* 71 VAL 71 H A 73.2 - - - - -61.7 -44.0 - - - 178.4 -2.6 33.2 - 72 LYS 72 H A - - -68.7 177.2 - -71.7 -36.8 - - - 186.4 -2.3 32.7 - * * 73 ASP 73 H A - 184.3 - - - -66.5 -40.6 - - - 180.6 -2.0 33.3 - 74 ASN 74 H A - 182.6 - - - -96.8 -12.3 - - - 189.9 -1.8 35.4 - +** ** +* +** 75 ASN 75 h l - 183.6 - - - - - - - - 184.7 -.8 31.8 - +* +* 76 LEU 76 t B 51.2 - - - - - - - - - 181.2 -1.8 29.9 - * * 77 GLU 77 t B 54.6 - - 185.0 - - - - - - 183.6 - 32.5 - 78 ASP 78 T B 67.1 - - - - - - - - - 183.7 - 33.9 - 79 GLY 79 T - - - - - - - - - - - 174.8 - - - 80 LYS 80 e B - - -63.0 179.9 - - - - - - 182.1 -1.2 34.7 - * * 81 TYR 81 E B - - -56.3 - - - - - - - 181.9 -.6 35.5 - +* +* 82 LEU 82 E B 50.6 - - - - - - - - - 179.1 -1.7 30.5 - 83 GLN 83 E B - - -64.6 174.8 - - - - - - 174.3 -3.2 36.6 - +* +* 84 PHE 84 E B - - -61.3 - - - - - - - 173.8 -3.7 35.8 - * ** ** 85 ILE 85 E B - - -59.2 179.5 - - - - - - 180.0 -2.2 33.1 - 86 TYR 86 E B - - -51.0 - - - - - - - 172.0 -3.5 38.6 - * * ** * ** 87 ASP 87 e a 59.3 - - - - - - - - - 171.3 -.5 29.8 - +* ** * ** 88 ARG 88 S a - - -65.7 - - - - - - - 180.7 - 34.3 - 89 ASP 89 S B - 179.1 - - - - - - - - 181.5 - 34.6 - 90 ARG 90 S a - - -57.0 - - - - - - - 175.2 - 33.7 - 91 THR 91 e B - 194.0 - - - - - - - - 187.1 - 34.1 - * * 92 PHE 92 E B - - -55.0 - - - - - - - 176.3 -2.5 34.5 - Residue-by-residue listing for refined_1 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 - - -54.4 - - - - - - - 188.1 -1.9 35.3 - * * 94 VAL 94 E B - 181.3 - - - - - - - - 174.3 -2.7 33.7 - 95 ILE 95 E B - - -64.9 - - - - - - - 185.8 -1.7 33.7 - 96 ILE 96 E B - 185.7 - 175.4 - - - - - - 175.0 - 32.9 - 97 TYR 97 E B - - -66.9 - - - - - - - 187.2 -3.7 35.1 - * ** ** 98 GLY 98 S - - - - - - - - - - - 190.0 - - - +* +* 99 HIS 99 B - - -56.7 - - - - - - - 178.8 - 32.7 - 100 ASN 100 B - 177.7 - - - - - - - - 180.3 - 36.0 - 101 MET 101 A - 180.4 - - - - - - - - 180.3 - 33.4 - 102 CYS 102 - - 183.2 - - - - - - - - - - 34.3 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* ** +*** *** ** ** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.4 182.9 -61.6 178.0 -76.6 -70.7 -33.0 - - - 180.3 -2.1 34.2 * * Standard deviations: 7.1 6.0 8.1 4.2 11.7 14.6 11.9 - - - 4.9 .9 2.1 Numbers of values: 18 35 35 24 5 16 16 0 0 0 101 56 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_1 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 - 1.238 1.510 1.534 1.467 - 115.89 120.25 110.42 109.86 110.56 123.83 2 ALA 2 1.346 1.240 1.531 1.532 1.477 124.31 115.41 120.42 110.91 111.68 110.83 124.10 * * * * 3 ASP 3 1.342 1.236 1.515 1.534 1.467 125.03 115.20 121.54 112.47 111.45 113.99 123.18 +* * ** ** 4 THR 4 1.309 1.240 1.523 1.540 1.439 121.95 115.29 121.25 110.84 110.87 110.22 123.43 * * 5 GLY 5 1.291 1.229 1.492 - 1.427 121.74 115.77 119.63 - 111.13 - 124.58 +** * * +** 6 GLU 6 1.322 1.240 1.533 1.531 1.461 124.54 115.05 122.16 112.53 113.26 112.18 122.76 +* * +* 7 VAL 7 1.299 1.228 1.511 1.560 1.446 122.64 117.54 119.92 110.07 109.06 112.08 122.54 ** ** 8 GLN 8 1.303 1.238 1.517 1.514 1.415 121.33 115.54 121.15 111.30 111.75 109.80 123.28 +* ** ** 9 PHE 9 1.301 1.218 1.517 1.543 1.453 123.03 117.95 119.63 111.03 108.13 109.32 122.42 ** * ** 10 MET 10 1.309 1.243 1.509 1.540 1.457 120.17 115.87 121.00 111.17 111.40 113.01 123.13 * * * 11 LYS 11 1.310 1.236 1.542 1.572 1.434 121.43 117.77 120.40 112.98 110.07 107.62 121.78 * ** * +* +* ** 12 PRO 12 1.350 1.231 1.523 1.543 1.462 122.82 117.06 120.50 109.23 110.08 103.65 122.44 Residue-by-residue listing for refined_1 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 1.297 1.235 1.519 1.543 1.446 121.19 116.22 120.61 112.50 112.04 111.31 123.10 ** * ** 14 ILE 14 1.319 1.232 1.523 1.554 1.449 121.90 116.44 119.64 109.31 108.49 111.09 123.85 15 SER 15 1.335 1.216 1.535 1.516 1.479 124.72 115.83 120.89 108.75 112.88 108.00 123.27 * +* * +* 16 GLU 16 1.304 1.226 1.513 1.520 1.450 124.01 115.34 121.55 109.15 110.69 107.82 123.11 +* * +* +* 17 LYS 17 1.305 1.232 1.511 1.522 1.432 121.31 116.87 120.35 112.84 112.23 109.07 122.71 +* * * +* 18 SER 18 1.326 1.215 1.522 1.528 1.447 121.35 116.89 120.53 111.36 111.70 111.18 122.57 19 SER 19 1.316 1.239 1.537 1.528 1.439 121.03 116.62 120.88 111.82 111.09 109.98 122.50 * * 20 LYS 20 1.332 1.234 1.536 1.542 1.455 120.54 116.25 120.89 110.63 111.57 110.21 122.86 21 SER 21 1.305 1.232 1.525 1.546 1.440 122.33 118.03 120.09 111.49 109.53 109.32 121.87 +* +* 22 LEU 22 1.305 1.245 1.510 1.562 1.429 119.95 114.12 121.60 113.74 107.82 111.89 124.25 +* +* * * +* * +* 23 GLU 23 1.298 1.242 1.540 1.542 1.434 124.23 116.06 120.73 112.31 108.02 106.35 123.20 ** * * * * ** ** 24 ILE 24 1.309 1.237 1.535 1.557 1.448 122.50 117.35 120.57 109.90 111.59 110.71 122.09 * * 25 PRO 25 1.355 1.245 1.530 1.538 1.466 122.61 116.73 120.71 109.73 110.60 103.80 122.55 26 LEU 26 1.310 1.210 1.529 1.531 1.452 121.58 117.00 120.24 111.88 112.40 111.96 122.73 * * * 27 GLY 27 1.325 1.222 1.524 - 1.457 121.24 115.62 121.21 - 111.61 - 123.17 28 PHE 28 1.314 1.219 1.534 1.552 1.466 123.54 114.56 121.94 110.65 106.68 106.88 123.47 * * * +* ** ** 29 ASN 29 1.321 1.234 1.533 1.527 1.468 123.93 115.44 121.09 107.81 111.49 108.05 123.45 * * * * 30 GLU 30 1.322 1.236 1.512 1.533 1.460 123.48 115.39 121.46 110.75 110.41 109.20 123.11 31 TYR 31 1.310 1.232 1.526 1.538 1.423 121.69 117.36 120.29 111.91 110.28 110.21 122.30 * +* +* 32 PHE 32 1.331 1.241 1.534 1.554 1.442 119.61 117.43 121.58 110.71 113.70 112.05 120.92 * * * * 33 PRO 33 1.329 1.237 1.509 1.517 1.441 121.76 116.80 120.52 109.54 107.75 104.59 122.67 +* +* * +* 34 ALA 34 1.276 1.240 1.507 1.531 1.443 120.44 117.79 120.01 110.09 111.48 109.85 122.20 +*** +*** 35 PRO 35 1.342 1.245 1.520 1.536 1.449 121.61 117.22 119.83 109.71 108.00 104.67 122.94 * +* +* +* 36 PHE 36 1.314 1.237 1.532 1.541 1.405 121.72 116.76 121.20 113.20 112.16 110.35 121.97 * +** +* +** 37 PRO 37 1.333 1.235 1.520 1.529 1.441 122.77 117.30 120.63 110.75 110.18 102.98 122.05 +* +* 38 ILE 38 1.296 1.222 1.519 1.555 1.438 119.95 116.73 120.85 111.96 109.87 112.42 122.39 ** * * ** 39 THR 39 1.309 1.229 1.525 1.548 1.435 120.77 114.76 121.21 111.08 111.69 112.58 124.01 * * * 40 VAL 40 1.306 1.221 1.528 1.574 1.449 126.35 118.60 119.47 109.92 106.34 109.28 121.92 +* * +** * +* * +** 41 ASP 41 1.302 1.246 1.504 1.527 1.451 120.43 114.69 121.19 109.68 113.35 112.05 124.12 +* * +* 42 LEU 42 1.316 1.233 1.513 1.541 1.442 123.61 117.00 120.11 108.64 107.02 111.45 122.89 * * * Residue-by-residue listing for refined_1 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 1.300 1.243 1.497 1.551 1.438 121.31 113.77 121.73 107.94 111.59 112.84 124.50 ** * * * * * * ** 44 ASP 44 1.286 1.241 1.512 1.524 1.424 124.40 115.66 120.68 110.68 108.51 109.98 123.67 *** +* +* *** 45 TYR 45 1.304 1.224 1.535 1.538 1.456 123.71 117.22 120.54 111.08 112.22 108.89 122.22 +* * +* 46 SER 46 1.312 1.236 1.542 1.534 1.437 120.66 117.19 120.37 111.80 111.16 110.18 122.44 * * * 47 GLY 47 1.330 1.236 1.510 - 1.451 119.88 117.36 120.02 - 114.26 - 122.63 48 ARG 48 1.319 1.229 1.499 1.542 1.467 120.58 115.08 121.31 109.66 112.92 114.56 123.59 * ** ** 49 SER 49 1.293 1.240 1.523 1.538 1.429 122.08 115.81 120.92 111.19 110.55 111.03 123.24 +** +* +** 50 TRP 50 1.303 1.234 1.498 1.542 1.451 122.28 116.77 120.29 108.70 108.70 111.96 122.93 +* * +* 51 THR 51 1.290 1.237 1.534 1.534 1.420 120.83 115.43 121.47 111.84 109.01 110.58 123.09 +** ** * +** 52 VAL 52 1.301 1.207 1.515 1.552 1.440 123.40 117.35 120.50 109.75 110.49 111.52 122.13 ** * ** 53 ARG 53 1.293 1.215 1.516 1.528 1.442 120.80 116.96 120.51 110.64 109.41 109.55 122.52 +** +** 54 MET 54 1.305 1.223 1.504 1.529 1.460 121.06 117.10 120.31 110.24 108.39 111.29 122.59 +* * * +* 55 LYS 55 1.298 1.233 1.513 1.511 1.423 120.76 115.26 121.09 109.73 112.02 107.51 123.64 ** +* +* ** 56 LYS 56 1.304 1.228 1.480 1.507 1.437 122.80 115.34 120.78 107.56 105.56 111.74 123.87 +* ** * * * ** ** 57 ARG 57 1.242 1.241 1.493 1.533 1.427 122.95 115.03 121.59 112.16 110.87 111.80 123.38 *6.2* +* +* * *6.2* 58 GLY 58 1.292 1.236 1.478 - 1.411 120.58 115.98 120.57 - 108.88 - 123.45 +** ** +** * +** 59 GLU 59 1.286 1.219 1.519 1.519 1.431 121.52 116.53 120.57 109.88 110.00 110.01 122.89 *** * *** 60 LYS 60 1.331 1.233 1.532 1.522 1.447 121.73 115.09 121.59 110.38 113.90 110.43 123.31 61 VAL 61 1.321 1.234 1.531 1.571 1.449 123.20 115.51 120.79 106.95 109.54 111.19 123.68 * * 62 PHE 62 1.299 1.241 1.481 1.522 1.438 124.17 115.99 120.87 108.97 109.11 113.00 123.13 ** ** * * * ** 63 LEU 63 1.288 1.212 1.519 1.547 1.420 120.39 115.46 121.12 114.11 103.21 109.37 123.36 +** +* ** +** +** 64 THR 64 1.294 1.236 1.567 1.558 1.442 123.13 116.82 120.44 112.15 110.91 106.34 122.73 +** ** * *** *** 65 VAL 65 1.334 1.225 1.510 1.551 1.459 124.20 115.38 121.60 110.46 111.91 112.27 122.97 * * 66 GLY 66 1.287 1.229 1.476 - 1.415 120.75 114.46 121.26 - 108.67 - 124.25 *** ** ** * *** 67 TRP 67 1.331 1.239 1.505 1.533 1.456 123.80 113.75 122.06 108.91 109.00 108.63 124.10 * * * * 68 GLU 68 1.303 1.217 1.543 1.511 1.423 122.80 116.25 121.10 110.93 109.85 109.19 122.59 +* +* +* 69 ASN 69 1.331 1.211 1.505 1.545 1.465 122.02 115.42 120.98 109.19 109.93 112.14 123.57 * * 70 PHE 70 1.303 1.238 1.523 1.543 1.442 123.66 116.20 120.42 111.61 110.65 109.64 123.36 +* * +* Residue-by-residue listing for refined_1 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 1.342 1.230 1.520 1.587 1.463 121.56 114.79 121.37 110.60 109.45 112.48 123.84 +* +* 72 LYS 72 1.313 1.226 1.521 1.528 1.450 123.18 117.59 119.74 110.17 113.64 111.54 122.68 * * 73 ASP 73 1.334 1.239 1.512 1.530 1.487 120.40 116.19 120.85 109.70 112.87 111.44 122.94 +* +* 74 ASN 74 1.295 1.230 1.516 1.550 1.449 120.70 115.28 120.69 109.98 109.40 109.72 123.91 ** * ** 75 ASN 75 1.337 1.243 1.518 1.551 1.472 123.18 115.12 121.81 112.10 108.22 113.00 122.89 * * * * * 76 LEU 76 1.301 1.239 1.507 1.551 1.420 121.00 114.78 121.32 114.46 113.07 111.47 123.87 ** * +* ** ** 77 GLU 77 1.295 1.248 1.512 1.533 1.436 123.72 115.69 120.19 112.08 110.34 111.40 124.12 ** * * * ** 78 ASP 78 1.324 1.243 1.520 1.549 1.468 123.74 115.31 121.41 109.65 110.99 111.58 123.24 * * 79 GLY 79 1.300 1.238 1.503 - 1.436 121.44 115.20 121.44 - 109.79 - 123.35 ** ** 80 LYS 80 1.315 1.238 1.522 1.531 1.441 122.33 116.96 120.22 109.61 107.98 111.18 122.82 * * * 81 TYR 81 1.304 1.217 1.496 1.537 1.447 121.62 117.99 119.59 109.67 107.78 110.28 122.42 +* * * +* 82 LEU 82 1.296 1.239 1.519 1.550 1.440 119.95 115.12 121.00 113.50 113.38 111.37 123.87 ** +* ** 83 GLN 83 1.308 1.236 1.506 1.527 1.442 123.96 115.99 120.41 107.35 109.70 110.26 123.60 +* * * +* 84 PHE 84 1.298 1.241 1.503 1.535 1.432 122.47 116.86 120.28 107.31 108.07 112.02 122.82 ** * * * * ** 85 ILE 85 1.293 1.235 1.515 1.556 1.433 120.28 115.68 120.58 110.54 108.10 112.99 123.69 +** * * +** 86 TYR 86 1.297 1.236 1.508 1.545 1.445 123.01 118.62 119.18 104.64 107.26 110.45 122.19 ** * +** * +** 87 ASP 87 1.312 1.236 1.538 1.580 1.453 118.40 116.01 120.53 113.89 108.37 114.29 123.45 * ** +* +* * ** ** 88 ARG 88 1.307 1.225 1.504 1.536 1.457 125.47 115.63 121.01 108.59 107.99 112.88 123.34 +* ** * * ** 89 ASP 89 1.327 1.237 1.508 1.549 1.403 122.99 115.34 121.71 111.86 109.09 109.38 122.95 +** +** 90 ARG 90 1.260 1.215 1.518 1.533 1.443 123.30 115.97 121.19 111.38 110.17 110.39 122.81 *4.9* *4.9* 91 THR 91 1.308 1.241 1.538 1.568 1.431 121.39 117.73 120.25 111.95 105.67 110.96 121.93 * * * * +* +* 92 PHE 92 1.305 1.219 1.503 1.530 1.443 119.66 116.03 120.95 109.54 111.56 110.62 123.02 +* * * +* 93 TYR 93 1.297 1.235 1.515 1.542 1.445 122.33 117.13 119.75 110.61 105.79 110.04 123.10 ** +* ** 94 VAL 94 1.315 1.242 1.527 1.559 1.453 120.91 115.25 121.28 109.53 112.83 111.41 123.47 * * 95 ILE 95 1.312 1.230 1.525 1.582 1.456 123.19 117.88 119.82 109.81 106.76 113.42 122.27 * +* +* * +* 96 ILE 96 1.308 1.240 1.549 1.567 1.446 120.29 115.59 121.19 111.83 113.01 110.18 123.21 * * * * 97 TYR 97 1.332 1.238 1.513 1.538 1.456 123.12 116.76 120.34 108.35 108.15 111.90 122.86 * * Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 GLY 98 1.309 1.233 1.493 - 1.436 120.00 114.92 120.93 - 107.16 - 124.15 * * +* +* 99 HIS 99 1.314 1.245 1.512 1.538 1.453 123.08 114.23 121.31 110.28 113.30 111.66 124.46 * * 100 ASN 100 1.312 1.233 1.522 1.542 1.449 124.50 116.66 120.44 109.90 109.78 108.70 122.88 * +* * +* 101 MET 101 1.311 1.235 1.518 1.558 1.457 121.53 115.63 121.25 112.23 109.85 110.21 123.10 * * * * 102 CYS 102 1.302 - 1.516 1.537 1.428 122.41 - - 111.36 108.40 110.24 - +* +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *6.2* * ** ** +** +** * +** +** *** * *6.2* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 1.242 1.346 1.308 .017 *6.2* * * C-N (Pro) 1.341 .016 5 1.329 1.355 1.342 .010 C-O C-O 1.231 .020 101 1.207 1.248 1.233 .009 * CA-C CH1E-C (except Gly) 1.525 .021 95 1.480 1.567 1.519 .014 ** ** CH2G*-C (Gly) 1.516 .018 7 1.476 1.524 1.497 .016 ** * CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.531 1.532 1.532 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.534 1.587 1.560 .013 +* CH1E-CH2E (the rest) 1.530 .020 75 1.507 1.580 1.537 .013 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.403 1.487 1.445 .016 +** +* NH1-CH2G* (Gly) 1.451 .016 7 1.411 1.457 1.433 .016 +** * N-CH1E (Pro) 1.466 .015 5 1.441 1.466 1.452 .011 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 89 113.75 118.62 116.13 1.08 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.46 117.36 115.62 .86 CH1E-C-N (Pro) 116.9 1.5 5 116.73 117.30 117.02 .22 O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.92 124.58 123.11 .68 * O-C-N (Pro) 122.0 1.4 5 122.05 122.94 122.53 .29 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.40 126.35 122.23 1.55 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.88 121.74 120.80 .66 C-N-CH1E (Pro) 122.6 5.0 5 121.61 122.82 122.31 .52 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.18 122.16 120.77 .62 CH2G*-C-O (Gly) 120.8 2.1 7 119.63 121.44 120.72 .63 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.09 110.91 110.50 .41 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 106.95 112.15 110.47 1.24 * CH2E-CH1E-C (the rest) 110.1 1.9 75 104.64 114.46 110.59 1.77 +** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 103.21 113.90 110.14 2.16 +** NH1-CH2G*-C (Gly) 112.5 2.9 7 107.16 114.26 110.21 2.17 +* N-CH1E-C (Pro) 111.8 2.5 5 107.75 110.60 109.32 1.20 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.85 110.83 110.34 .49 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 106.34 113.42 111.21 1.59 *** * N-CH1E-CH2E (Pro) 103.0 1.1 5 102.98 104.67 103.94 .63 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.35 114.56 110.62 1.68 ** ** ------------------------------------------------------------------------------------------------------------- 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_1 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] 11 12.5% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% 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 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 101 4.9 6.0 3.0 -.4 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 2.1 3.1 1.6 -.7 Inside e. H-bond energy st dev 56 .9 .8 .2 .6 Inside f. Overall G-factor 102 -.1 -.4 .3 .9 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 18 7.1 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 35 6.0 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 35 8.1 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 88 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 24 4.2 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% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_1 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.50 Chi1-chi2 distribution -.30 Chi1 only .01 Chi3 & chi4 .63 Omega -.42 ------ -.27 ===== Main-chain covalent forces:- Main-chain bond lengths -.15 Main-chain bond angles .31 ------ .12 ===== OVERALL AVERAGE -.13 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.