Residue-by-residue listing for refined_7 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 GLU 1 - - - -68.4 - - - - - - - 178.4 - 32.2 - 2 ALA 2 L - - - - - - - - - - 181.8 - 32.3 - 3 GLU 3 S B 64.8 - - - - - - - - - 175.7 - 33.5 - 4 VAL 4 B - 185.6 - - - - - - - - 180.7 - 34.7 - 5 HIS 5 B 60.5 - - - - - - - - - 186.4 -1.1 31.3 - * * * 6 ASN 6 S ~b - 178.6 - - - - - - - - 176.1 - 35.8 - ** ** 7 GLN 7 S b 52.8 - - 197.1 - - - - - - 184.6 - 35.6 - * * 8 LEU 8 E B - - -73.3 - - - - - - - 181.5 -1.3 30.3 - * * 9 GLU 9 E B - - -66.6 - - - - - - - 178.3 -.9 33.7 - * * 10 ILE 10 E B - - -61.5 178.4 - - - - - - 174.1 -2.6 35.3 - * * 11 LYS 11 E B 64.1 - - 177.4 - - - - - - 182.5 -2.5 32.3 - 12 PHE 12 E B - - -56.9 - - - - - - - 176.4 -.7 35.3 - +* +* 13 ARG 13 E B - 176.5 - 175.3 - - - - - - 179.2 -3.0 32.0 - * * 14 LEU 14 E B - - -59.6 - - - - - - - 180.5 -2.6 34.4 - 15 THR 15 e A - 188.0 - - - - - - - - 179.2 -1.4 34.2 - 16 ASP 16 T A - - -62.8 - - - - - - - 178.9 - 35.0 - 17 GLY 17 t - - - - - - - - - - - 178.6 -2.2 - - 18 SER 18 e B - - -54.5 - - - - - - - 181.2 - 35.2 - 19 ASP 19 E B - - -64.5 - - - - - - - 174.3 - 35.9 - 20 ILE 20 E B - - -59.2 179.3 - - - - - - 182.9 -2.2 34.7 - Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 GLY 21 E - - - - - - - - - - - 182.2 - - - 22 PRO 22 E - - - - - -59.9 - - - - - 181.4 - 37.7 - * * 23 LYS 23 E B - 187.2 - 181.9 - - - - - - 181.6 -2.4 36.0 - 24 ALA 24 E B - - - - - - - - - - 180.7 - 33.9 - 25 PHE 25 E B - - -58.2 - - - - - - - 169.5 -3.4 36.5 - +* +* +* 26 PRO 26 t - - - - - -66.1 - - - - - 176.2 - 40.6 - +* +* 27 ASP 27 T A - - -60.7 - - - - - - - 179.3 - 34.4 - 28 ALA 28 T A - - - - - - - - - - 176.0 - 34.0 - 29 THR 29 t B - - -56.3 - - - - - - - 179.6 -2.1 35.4 - 30 THR 30 h B 60.6 - - - - - - - - - 177.4 - 34.3 - 31 VAL 31 H A - 178.4 - - - -69.3 -26.9 - - - 175.3 -3.3 33.2 - * +* +* 32 SER 32 H A - 181.7 - - - -62.6 -49.6 - - - 179.7 -1.4 34.2 - 33 ALA 33 H A - - - - - -68.2 -28.1 - - - 176.6 - 33.6 - * * 34 LEU 34 H A - 178.7 - - - -64.9 -44.8 - - - 175.9 -1.8 35.9 - 35 LYS 35 H A - - -72.9 - - -68.5 -39.8 - - - 177.1 -2.5 33.2 - 36 GLU 36 H A - - -61.6 - - -56.8 -41.9 - - - 177.1 -2.7 34.8 - 37 THR 37 H A - - -58.6 - - -61.9 -40.9 - - - 177.9 -2.2 34.0 - 38 VAL 38 H A - 175.3 - - - -61.4 -50.7 - - - 181.1 -1.5 34.3 - 39 ILE 39 H A - - -55.6 177.0 - -57.6 -33.9 - - - 180.6 -2.9 34.9 - * * 40 SER 40 H A - - -55.5 - - -75.2 -37.9 - - - 182.2 -1.7 34.3 - 41 GLU 41 H A - - -61.7 - - -84.1 -27.3 - - - 182.0 -2.0 34.9 - +* * +* 42 TRP 42 h B - 193.6 - - - - - - - - 180.2 -2.8 34.8 - * * 43 PRO 43 t - - - - - -52.4 - - - - - 177.6 - 39.0 - * * * 44 ARG 44 T A - 177.7 - 177.0 - - - - - - 180.0 - 35.1 - 45 GLU 45 T A 61.1 - - 186.9 - - - - - - 184.9 - 36.4 - 46 LYS 46 t b 82.3 - - - - - - - - - 177.1 -1.1 34.8 - * * * 47 GLU 47 b - - -61.0 - - - - - - - 172.3 - 36.6 - * * 48 ASN 48 S b - - -70.5 - - - - - - - 179.1 - 31.7 - 49 GLY 49 S - - - - - - - - - - - 181.3 -2.7 - - 50 PRO 50 - - - - - -58.6 - - - - - 178.1 - 40.0 - +* +* 51 LYS 51 a - 182.5 - 185.3 - - - - - - 186.3 - 34.9 - * * 52 THR 52 t B 49.6 - - - - - - - - - 185.6 - 32.7 - 53 VAL 53 T A 55.5 - - - - - - - - - 184.3 - 32.8 - 54 LYS 54 T A - 191.9 - - - - - - - - 181.6 - 33.2 - 55 GLU 55 e A - - -52.4 - - - - - - - 180.4 -.6 34.3 - +* +* 56 VAL 56 E B - 179.9 - - - - - - - - 176.2 -2.0 35.7 - 57 LYS 57 E B - - -73.3 - - - - - - - 183.9 -1.5 33.0 - 58 LEU 58 E B - 192.3 - - - - - - - - 179.0 -.6 35.2 - +* +* 59 ILE 59 E B - - -64.5 182.4 - - - - - - 178.7 -3.1 33.5 - * * 60 SER 60 E B - 182.6 - - - - - - - - 177.8 -3.0 34.7 - * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 61 ALA 61 T l - - - - - - - - - - 180.0 - 32.8 - 62 GLY 62 T - - - - - - - - - - - 180.0 - - - 63 LYS 63 E B - - -72.2 - - - - - - - 175.3 -1.7 36.0 - 64 VAL 64 E B 59.4 - - - - - - - - - 186.4 - 31.9 - * * 65 LEU 65 e B - - -55.6 188.4 - - - - - - 179.2 -2.8 33.5 - 66 GLU 66 t B - 197.2 - - - - - - - - 189.1 - 36.1 - +* +* 67 ASN 67 T A 75.1 - - - - - - - - - 181.1 - 29.5 - * * 68 SER 68 T A - - -50.7 - - - - - - - 177.1 - 33.7 - * * 69 LYS 69 t B - - -78.9 - - - - - - - 177.5 -2.0 34.1 - 70 THR 70 B B - - -39.0 - - - - - - - 181.4 - 36.0 - +* +* 71 VAL 71 G A - 179.4 - - - - - - - - 179.1 -3.4 32.9 - +* +* 72 LYS 72 G A - 184.3 - 180.6 - - - - - - 181.8 -2.4 34.2 - 73 ASP 73 G A - 184.9 - - - - - - - - 182.6 -.6 34.8 - +* +* 74 TYR 74 G A - - -62.1 - - - - - - - 179.6 -1.1 34.3 - * * 75 ARG 75 g B - - -102.5 - - - - - - - 172.4 -.7 35.5 - ** * +* ** 76 SER 76 B - 182.8 - - - - - - - - 182.6 -.7 34.9 - +* +* 77 PRO 77 - - - - - -91.7 - - - - - 175.0 - 39.2 - ** +* ** 78 VAL 78 S A 62.8 - - - - - - - - - 178.3 - 32.8 - 79 SER 79 S B - 181.7 - - - - - - - - 182.0 - 35.4 - 80 ASN 80 S A - - -64.8 - - - - - - - 175.3 - 32.2 - 81 LEU 81 S B - - -59.2 180.2 - - - - - - 182.6 - 36.7 - 82 ALA 82 b - - - - - - - - - - 176.0 - 34.7 - 83 GLY 83 S - - - - - - - - - - - 180.6 - - - 84 ALA 84 e B - - - - - - - - - - 176.3 -2.1 35.1 - 85 VAL 85 E B - 181.9 - - - - - - - - 180.5 - 34.6 - 86 THR 86 E B - - -54.3 - - - - - - - 180.4 -2.7 33.9 - 87 THR 87 E B - - -54.2 - - - - - - - 175.8 - 34.9 - 88 MET 88 E B - - -81.9 - - - - - - - 184.2 -2.4 32.6 - * * 89 HIS 89 E B - - -60.5 - - - - - - - 180.3 -2.5 33.6 - 90 VAL 90 E B - 182.5 - - - - - - - - 181.2 -3.0 33.7 - * * 91 ILE 91 E B - - -63.8 - - - - - - - 185.4 -3.2 35.1 - +* +* 92 ILE 92 E B - - -61.3 - - - - - - - 168.9 -.6 33.7 - +* +* +* 93 GLN 93 e B - - -65.7 180.1 - - - - - - 191.7 -1.0 33.3 - ** * ** 94 ALA 94 B - - - - - - - - - - 166.7 -.6 35.7 - ** +* ** 95 PRO 95 - - - - - -63.2 - - - - - 191.8 - 39.2 - ** +* ** 96 VAL 96 B 60.4 - - - - - - - - - 168.4 -.6 33.0 - ** +* ** 97 THR 97 B - - -54.0 - - - - - - - 196.2 - 35.6 - +** +** Residue-by-residue listing for refined_7 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 GLU 98 S b - 187.3 - 171.0 - - - - - - 174.8 -1.1 27.9 - * +* +* 99 LYS 99 ~b - 182.0 - 180.8 - - - - - - 185.5 -1.0 33.1 - ** * ** 100 GLU 100 a - 179.6 - - - - - - - - 180.4 - 35.0 - 101 LYS 101 - - 181.4 - 181.2 - - - - - - - - 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * ** * ** +* * +** +* +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 62.2 183.4 -62.7 181.1 -65.3 -66.4 -38.3 - - - 179.7 -1.9 34.5 Standard deviations: 8.6 5.4 10.2 5.7 13.7 8.0 8.5 - - - 4.6 .9 2.0 Numbers of values: 13 28 41 18 6 11 11 0 0 0 100 54 96 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_7 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 GLU 1 - 1.239 1.506 1.530 1.457 - 115.46 120.39 111.35 111.00 112.03 124.09 2 ALA 2 1.338 1.236 1.508 1.517 1.470 124.44 114.57 121.83 111.90 111.41 111.04 123.45 +* +* 3 GLU 3 1.283 1.248 1.498 1.553 1.409 122.41 116.39 120.45 110.01 109.54 112.75 123.15 *** * * +** * *** 4 VAL 4 1.300 1.243 1.503 1.518 1.428 120.57 114.50 121.74 107.98 107.86 112.94 123.73 ** * +* * ** 5 HIS 5 1.264 1.225 1.505 1.554 1.424 122.65 115.14 120.75 112.89 109.78 112.72 124.11 *4.7* * +* * * *4.7* 6 ASN 6 1.302 1.222 1.497 1.545 1.468 124.44 112.92 122.43 109.46 106.31 110.24 124.64 +* * +* +* +* * +* 7 GLN 7 1.314 1.229 1.528 1.527 1.439 125.03 117.96 119.98 112.38 108.97 106.84 122.05 * * +* * ** ** 8 LEU 8 1.299 1.217 1.501 1.531 1.452 119.93 116.24 120.91 111.47 113.00 113.73 122.84 ** * +* ** 9 GLU 9 1.305 1.243 1.514 1.539 1.431 120.92 114.62 121.86 108.44 111.08 113.05 123.52 +* * +* +* 10 ILE 10 1.294 1.240 1.507 1.570 1.440 123.21 116.18 120.47 108.69 108.53 111.72 123.32 ** * ** 11 LYS 11 1.296 1.249 1.508 1.538 1.435 121.10 116.23 120.64 111.06 108.79 113.23 123.12 ** * +* ** Residue-by-residue listing for refined_7 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 PHE 12 1.293 1.232 1.497 1.531 1.435 121.32 116.83 120.31 109.07 109.70 110.64 122.85 +** * * +** 13 ARG 13 1.298 1.237 1.500 1.529 1.426 120.28 115.20 121.26 111.18 110.25 113.06 123.53 ** * +* +* ** 14 LEU 14 1.298 1.241 1.521 1.547 1.421 122.31 116.85 120.48 110.19 108.98 111.17 122.67 ** +* ** 15 THR 15 1.314 1.223 1.539 1.547 1.465 122.49 115.37 121.41 110.28 110.97 110.38 123.21 * * 16 ASP 16 1.307 1.229 1.522 1.534 1.466 122.96 116.67 120.76 108.90 111.22 110.48 122.57 +* +* 17 GLY 17 1.323 1.230 1.510 - 1.447 120.56 116.46 120.84 - 112.72 - 122.70 18 SER 18 1.298 1.230 1.528 1.522 1.442 121.44 117.49 119.82 110.89 108.95 108.77 122.69 ** * ** 19 ASP 19 1.314 1.236 1.500 1.540 1.444 121.61 115.79 120.98 107.01 109.81 111.80 123.24 * * +* +* 20 ILE 20 1.288 1.242 1.513 1.564 1.434 122.41 116.26 119.30 109.97 106.57 111.78 124.41 +** * +* +** 21 GLY 21 1.334 1.250 1.513 - 1.457 122.67 116.95 120.10 - 113.63 - 122.95 * * 22 PRO 22 1.354 1.242 1.522 1.537 1.455 123.03 115.20 121.61 110.68 112.92 104.54 123.19 * * * 23 LYS 23 1.292 1.227 1.516 1.541 1.431 123.08 118.04 119.24 111.06 106.52 108.46 122.72 +** * +* * +** 24 ALA 24 1.301 1.242 1.529 1.532 1.448 120.83 116.53 120.52 111.59 110.08 109.81 122.91 ** ** 25 PHE 25 1.329 1.235 1.522 1.533 1.446 122.50 117.67 120.93 105.95 110.56 111.54 121.38 ** * ** 26 PRO 26 1.312 1.237 1.533 1.528 1.451 122.27 117.56 119.96 108.05 109.67 103.23 122.48 +* * * +* 27 ASP 27 1.316 1.231 1.537 1.542 1.474 121.73 115.43 121.58 109.53 109.50 111.19 122.96 28 ALA 28 1.331 1.228 1.541 1.518 1.455 122.96 117.18 120.39 110.24 112.32 110.05 122.43 29 THR 29 1.323 1.225 1.529 1.548 1.466 121.45 117.68 120.08 108.70 108.97 110.80 122.24 30 THR 30 1.306 1.236 1.521 1.529 1.429 120.47 116.67 120.49 109.70 110.53 111.06 122.84 +* +* +* 31 VAL 31 1.321 1.232 1.528 1.549 1.450 121.64 116.12 121.07 110.80 109.63 111.85 122.78 32 SER 32 1.323 1.220 1.527 1.540 1.437 121.13 116.39 120.58 110.77 108.84 110.71 122.94 * * 33 ALA 33 1.331 1.235 1.524 1.510 1.455 121.85 116.03 121.00 110.92 110.97 110.32 122.96 34 LEU 34 1.323 1.228 1.540 1.529 1.414 123.49 115.66 121.19 112.14 108.30 106.88 123.10 ** * * ** ** 35 LYS 35 1.328 1.220 1.516 1.520 1.452 122.41 117.15 119.71 110.22 111.76 111.51 123.14 36 GLU 36 1.336 1.236 1.522 1.529 1.462 121.93 115.36 121.30 109.22 109.58 110.85 123.33 37 THR 37 1.320 1.233 1.538 1.545 1.439 122.80 116.50 120.35 110.97 110.40 110.33 123.10 38 VAL 38 1.332 1.221 1.523 1.557 1.460 122.32 115.75 120.61 109.27 109.96 111.75 123.57 39 ILE 39 1.326 1.235 1.539 1.562 1.477 123.20 115.58 121.48 109.03 110.52 110.89 122.94 * * 40 SER 40 1.311 1.231 1.548 1.521 1.440 122.39 117.09 120.60 110.97 111.98 108.97 122.31 * * * 41 GLU 41 1.328 1.235 1.529 1.516 1.438 122.00 116.42 120.65 109.58 112.13 109.56 122.93 * * 42 TRP 42 1.311 1.239 1.526 1.538 1.443 121.81 117.71 119.99 111.29 108.68 109.26 122.23 * * 43 PRO 43 1.343 1.221 1.532 1.531 1.467 123.13 115.61 121.43 109.91 113.36 103.18 122.95 44 ARG 44 1.311 1.230 1.530 1.535 1.455 122.96 114.34 122.00 111.11 109.03 108.74 123.62 * * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 GLU 45 1.307 1.240 1.538 1.516 1.459 124.81 116.15 120.27 108.93 111.26 108.17 123.55 +* +* * +* 46 LYS 46 1.336 1.244 1.548 1.554 1.456 124.40 114.96 121.63 109.59 112.85 109.78 123.41 * * * * 47 GLU 47 1.312 1.252 1.527 1.562 1.444 124.52 115.58 121.56 108.22 109.51 109.73 122.86 * * +* +* +* 48 ASN 48 1.305 1.227 1.508 1.539 1.432 122.92 113.28 122.30 111.05 109.35 113.92 123.98 +* * * ** ** 49 GLY 49 1.280 1.238 1.507 - 1.416 123.80 117.50 119.72 - 110.88 - 122.78 *** ** +* *** 50 PRO 50 1.344 1.232 1.536 1.524 1.490 124.44 115.44 121.22 108.70 114.74 102.39 123.33 +* * +* 51 LYS 51 1.336 1.222 1.527 1.538 1.456 122.66 115.54 121.35 108.42 110.42 111.45 123.09 52 THR 52 1.315 1.242 1.540 1.528 1.431 122.62 114.81 121.37 111.83 113.97 109.85 123.82 * * * 53 VAL 53 1.334 1.234 1.541 1.575 1.467 124.98 117.57 119.92 110.30 114.53 111.17 122.51 * +* * +* 54 LYS 54 1.320 1.236 1.536 1.534 1.448 120.84 116.47 121.10 111.40 111.14 110.62 122.43 55 GLU 55 1.320 1.231 1.526 1.538 1.455 121.35 115.57 121.26 110.19 109.55 110.76 123.13 56 VAL 56 1.311 1.221 1.523 1.554 1.446 122.22 116.79 120.61 107.88 110.05 111.12 122.59 * * 57 LYS 57 1.309 1.234 1.517 1.544 1.441 121.65 116.50 120.48 111.43 109.06 111.80 123.01 * * 58 LEU 58 1.315 1.243 1.530 1.569 1.446 121.68 115.83 120.80 111.51 108.48 108.83 123.37 * +* +* 59 ILE 59 1.309 1.242 1.519 1.561 1.442 122.82 115.32 121.23 110.85 110.33 111.43 123.43 * * 60 SER 60 1.306 1.237 1.519 1.539 1.425 122.57 116.20 120.05 110.81 108.38 110.13 123.65 +* +* * +* 61 ALA 61 1.336 1.235 1.535 1.536 1.479 123.78 115.97 121.15 111.17 112.01 110.84 122.82 * * * 62 GLY 62 1.315 1.235 1.518 - 1.444 121.35 116.83 120.34 - 112.96 - 122.83 * * 63 LYS 63 1.324 1.236 1.511 1.540 1.419 122.83 117.01 119.95 108.29 109.67 110.56 123.04 ** ** 64 VAL 64 1.313 1.236 1.526 1.568 1.442 120.66 116.20 121.31 112.13 108.54 113.11 122.46 * * * * 65 LEU 65 1.297 1.239 1.521 1.518 1.422 120.81 115.26 121.00 110.97 112.21 110.22 123.73 ** +* ** 66 GLU 66 1.316 1.229 1.541 1.551 1.447 123.73 118.22 119.24 111.50 105.04 107.96 122.53 * * * ** * ** 67 ASN 67 1.333 1.228 1.532 1.562 1.480 121.25 118.28 119.61 111.04 114.82 114.22 122.10 +* * * * ** ** 68 SER 68 1.329 1.225 1.536 1.521 1.460 120.20 116.57 121.02 110.62 111.12 110.48 122.40 69 LYS 69 1.316 1.237 1.502 1.523 1.435 121.74 115.21 121.44 109.48 111.12 111.36 123.35 * * * 70 THR 70 1.284 1.238 1.530 1.531 1.417 121.87 118.12 119.42 109.60 106.32 109.84 122.46 *** ** +* *** 71 VAL 71 1.320 1.229 1.530 1.566 1.457 120.52 115.22 120.95 111.05 109.51 112.18 123.77 72 LYS 72 1.334 1.223 1.539 1.540 1.468 124.45 117.08 120.23 109.78 112.33 110.35 122.68 +* +* 73 ASP 73 1.334 1.233 1.526 1.538 1.480 122.09 115.76 121.31 109.36 110.58 110.36 122.88 * * 74 TYR 74 1.314 1.235 1.528 1.523 1.435 122.48 115.69 121.11 110.99 111.07 109.40 123.19 * * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 75 ARG 75 1.306 1.227 1.498 1.505 1.434 123.86 115.55 121.32 109.24 111.68 109.23 123.12 +* * * * * +* 76 SER 76 1.278 1.234 1.522 1.540 1.420 120.99 118.41 120.02 111.16 105.77 110.24 121.56 +*** ** * +* +*** 77 PRO 77 1.327 1.238 1.524 1.523 1.441 122.14 115.90 121.33 110.26 113.87 102.62 122.77 +* +* 78 VAL 78 1.323 1.228 1.520 1.571 1.460 121.50 112.86 122.42 111.43 108.15 112.51 124.60 * +* * * * +* 79 SER 79 1.287 1.242 1.512 1.541 1.419 126.51 118.37 118.42 110.94 104.10 110.13 123.20 *** ** +** * * +** *** 80 ASN 80 1.321 1.234 1.506 1.538 1.468 120.99 115.88 121.12 110.52 111.19 112.80 122.99 * * 81 LEU 81 1.289 1.245 1.508 1.482 1.374 122.74 116.28 120.07 109.62 107.74 108.16 123.63 +** ** **** * * **** 82 ALA 82 1.309 1.232 1.501 1.536 1.435 123.56 116.07 120.49 109.25 108.94 111.53 123.44 * * * * * 83 GLY 83 1.303 1.230 1.517 - 1.451 122.21 115.05 121.60 - 111.00 - 123.34 +* +* 84 ALA 84 1.297 1.237 1.509 1.522 1.433 123.28 116.56 120.41 110.17 109.15 109.79 123.00 ** * ** 85 VAL 85 1.301 1.231 1.510 1.558 1.439 121.58 116.66 120.59 109.22 107.74 112.32 122.74 ** * ** 86 THR 86 1.289 1.232 1.523 1.546 1.429 120.72 116.87 120.51 111.10 109.01 110.92 122.56 +** +* +** 87 THR 87 1.307 1.242 1.526 1.544 1.431 120.55 116.20 120.65 109.08 110.31 110.98 123.15 +* * +* 88 MET 88 1.306 1.236 1.497 1.536 1.447 122.05 115.96 120.76 110.94 109.51 112.67 123.27 +* * * +* 89 HIS 89 1.305 1.236 1.499 1.536 1.441 121.33 115.53 121.00 110.87 110.31 111.11 123.44 +* * +* 90 VAL 90 1.296 1.244 1.501 1.545 1.431 121.89 114.13 121.82 110.10 109.81 112.00 124.05 ** * * * ** 91 ILE 91 1.281 1.249 1.495 1.531 1.411 123.53 114.66 121.54 110.93 108.42 109.56 123.80 *** * ** * * *** 92 ILE 92 1.292 1.228 1.505 1.555 1.408 121.84 114.80 121.52 110.14 111.50 111.68 123.58 +** +** +** 93 GLN 93 1.292 1.235 1.485 1.519 1.418 121.85 114.99 121.22 112.22 104.99 111.92 123.78 +** +* ** * ** +** 94 ALA 94 1.271 1.232 1.503 1.515 1.419 122.11 117.26 120.52 109.42 113.31 108.63 122.19 **** * ** * **** 95 PRO 95 1.344 1.244 1.495 1.506 1.442 121.60 116.32 120.92 108.98 106.06 104.88 122.75 * * +* ** +* ** 96 VAL 96 1.262 1.229 1.508 1.577 1.418 119.31 114.24 121.94 111.08 113.85 110.94 123.76 *4.8* * ** * *4.8* 97 THR 97 1.292 1.238 1.513 1.537 1.407 123.05 114.79 121.07 111.52 101.92 109.79 123.80 +** +** * *** * *** 98 GLU 98 1.312 1.226 1.518 1.524 1.431 122.57 111.98 122.68 115.12 116.15 111.34 125.31 * * ** * +** +* * +** 99 LYS 99 1.306 1.237 1.516 1.544 1.430 128.46 115.19 121.28 110.63 104.95 113.82 123.23 +* * +*** ** +* +*** 100 GLU 100 1.304 1.235 1.524 1.550 1.452 122.44 115.79 121.33 110.56 109.92 109.44 122.88 +* +* 101 LYS 101 1.305 - 1.510 1.531 1.430 122.32 - - 110.42 108.63 110.45 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.8* * +* ** **** +*** ** * +** *** ** * *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 94 1.262 1.338 1.309 .017 *4.8* * C-N (Pro) 1.341 .016 6 1.312 1.354 1.337 .014 +* C-O C-O 1.231 .020 100 1.217 1.252 1.234 .007 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.485 1.548 1.520 .014 +* * CH2G*-C (Gly) 1.516 .018 5 1.507 1.518 1.513 .004 CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.510 1.536 1.523 .009 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.518 1.577 1.551 .016 * CH1E-CH2E (the rest) 1.530 .020 62 1.482 1.569 1.534 .014 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.374 1.480 1.441 .019 **** * NH1-CH2G* (Gly) 1.451 .016 5 1.416 1.457 1.443 .014 ** N-CH1E (Pro) 1.466 .015 6 1.441 1.490 1.458 .017 +* +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 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 89 111.98 118.41 116.00 1.23 ** * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.05 117.50 116.56 .82 CH1E-C-N (Pro) 116.9 1.5 6 115.20 117.56 116.01 .78 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.38 125.31 123.12 .63 * * O-C-N (Pro) 122.0 1.4 6 122.48 123.33 122.91 .29 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.31 128.46 122.34 1.44 * +*** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.56 123.80 122.12 1.11 +* C-N-CH1E (Pro) 122.6 5.0 6 121.60 124.44 122.77 .91 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.42 122.68 120.85 .75 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.72 121.60 120.52 .65 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 109.25 111.90 110.58 .91 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 107.88 112.13 110.14 1.14 * CH2E-CH1E-C (the rest) 110.1 1.9 62 105.95 115.12 110.30 1.42 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 101.92 116.15 109.81 2.32 *** +* NH1-CH2G*-C (Gly) 112.5 2.9 5 110.88 113.63 112.24 1.10 N-CH1E-C (Pro) 111.8 2.5 6 106.06 114.74 111.77 3.00 ** * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 108.63 111.53 110.25 .84 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.56 113.11 111.27 .94 * N-CH1E-CH2E (Pro) 103.0 1.1 6 102.39 104.88 103.47 .93 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.84 114.22 110.71 1.72 ** ** ------------------------------------------------------------------------------------------------------------- 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_7 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] 9 10.2% 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 5 Number of proline residues 6 ---- Total number of residues 101 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 100 4.6 6.0 3.0 -.5 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 54 .9 .8 .2 .4 Inside f. Overall G-factor 101 -.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 13 8.6 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 28 5.4 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 41 10.2 17.5 4.9 -1.5 BETTER d. Chi-1 pooled st dev 82 8.7 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 18 5.7 20.4 5.0 -2.9 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 11.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_7 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.59 Chi1-chi2 distribution -.36 Chi1 only .09 Chi3 & chi4 .22 Omega -.20 ------ -.26 ===== Main-chain covalent forces:- Main-chain bond lengths -.17 Main-chain bond angles .33 ------ .12 ===== OVERALL AVERAGE -.13 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.