Residue-by-residue listing for refined_10 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 - - - -61.3 176.2 - - - - - - 182.1 - 34.7 - 2 ALA 2 l - - - - - - - - - - 185.7 - 31.5 - 3 GLU 3 B - - -65.1 167.7 - - - - - - 180.9 - 34.3 - 4 VAL 4 B 61.0 - - - - - - - - - 181.6 - 33.0 - 5 HIS 5 b 48.7 - - - - - - - - - 178.3 - 30.9 - 6 ASN 6 S a - 182.3 - - - - - - - - 168.4 - 34.7 - ** ** 7 GLN 7 S B - - -50.2 - - - - - - - 177.3 - 36.4 - * * 8 LEU 8 E B 59.3 - - 168.5 - - - - - - 180.4 -2.2 30.6 - 9 GLU 9 E B - - -49.4 - - - - - - - 180.4 -.5 33.7 - * ** ** 10 ILE 10 E B - - -61.0 178.3 - - - - - - 174.0 -3.0 34.7 - * * * 11 LYS 11 E B 59.8 - - 177.7 - - - - - - 183.8 -2.7 32.1 - 12 PHE 12 E B - - -54.6 - - - - - - - 178.5 - 35.2 - 13 ARG 13 E B - 175.6 - 171.7 - - - - - - 182.9 -3.5 32.2 - +* +* 14 LEU 14 t B - - -60.4 178.8 - - - - - - 173.8 -3.6 36.6 - * ** ** 15 THR 15 T A 48.8 - - - - - - - - - 179.3 - 35.5 - 16 ASP 16 T A - 177.5 - - - - - - - - 181.2 - 36.1 - 17 GLY 17 t - - - - - - - - - - - 176.8 -1.1 - - * * 18 SER 18 B - - -60.7 - - - - - - - 184.6 - 34.5 - 19 ASP 19 B B 58.0 - - - - - - - - - 176.1 - 33.2 - 20 ILE 20 B - - -58.7 178.0 - - - - - - 181.4 -1.9 35.3 - 21 GLY 21 - - - - - - - - - - - 184.4 - - - Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 PRO 22 - - - - - -60.0 - - - - - 178.0 - 38.1 - * * 23 LYS 23 E B - 175.8 - 182.7 - - - - - - 179.5 -2.4 35.8 - 24 ALA 24 E B - - - - - - - - - - 179.6 - 33.9 - 25 PHE 25 E B - - -56.8 - - - - - - - 176.0 -3.4 36.3 - +* +* 26 PRO 26 t - - - - - -66.3 - - - - - 179.7 - 39.2 - +* +* 27 ASP 27 T A 59.7 - - - - - - - - - 182.5 - 32.6 - 28 ALA 28 T A - - - - - - - - - - 177.5 - 33.3 - 29 THR 29 t B - 195.1 - - - - - - - - 182.9 -2.2 31.3 - 30 THR 30 h B 50.7 - - - - - - - - - 178.9 - 33.9 - 31 VAL 31 H A - 180.4 - - - -63.9 -26.4 - - - 176.8 -3.0 33.7 - * * * 32 SER 32 H A 56.4 - - - - -60.6 -46.7 - - - 179.4 -1.7 33.8 - 33 ALA 33 H A - - - - - -70.0 -29.1 - - - 175.8 - 34.0 - 34 LEU 34 H A - 171.0 - - - -64.6 -44.2 - - - 176.2 -1.5 35.3 - 35 LYS 35 H A - - -69.2 179.6 - -69.0 -30.8 - - - 176.3 -2.5 31.3 - 36 GLU 36 H A - - -64.4 - - -58.1 -38.4 - - - 176.8 -1.7 33.1 - 37 THR 37 H A - - -62.2 - - -69.4 -45.9 - - - 182.0 -1.4 32.5 - 38 VAL 38 H A 67.3 - - - - -61.1 -40.3 - - - 176.9 -1.7 31.5 - 39 ILE 39 H A - - -60.9 174.8 - -63.5 -44.8 - - - 182.3 -2.7 35.2 - 40 SER 40 H A - - -59.7 - - -68.0 -30.2 - - - 180.0 -1.9 33.3 - 41 GLU 41 h A - - -67.3 - - - - - - - 182.4 -2.2 35.6 - 42 TRP 42 t B - 198.2 - - - - - - - - 173.3 -.9 35.2 - * * * 43 PRO 43 t - - - - - -57.7 - - - - - 181.7 - 38.5 - * * 44 ARG 44 T A - - -55.1 176.0 - - - - - - 178.6 -.6 34.2 - +* +* 45 GLU 45 T A - 183.4 - 181.8 - - - - - - 181.3 - 35.0 - 46 LYS 46 t B - 192.6 - - - - - - - - 176.8 -1.3 35.2 - * * 47 GLU 47 S B - - -62.7 - - - - - - - 183.7 -.5 33.5 - ** ** 48 ASN 48 S l - - -61.0 - - - - - - - 179.7 - 31.7 - 49 GLY 49 S - - - - - - - - - - - 180.2 - - - 50 PRO 50 S - - - - - -58.7 - - - - - 180.6 - 40.3 - +* +* 51 LYS 51 S A - 171.4 - - - - - - - - 175.1 -3.2 31.2 - +* +* 52 THR 52 g B 57.3 - - - - - - - - - 183.1 - 33.4 - 53 VAL 53 G A 57.6 - - - - - - - - - 177.7 - 31.3 - 54 LYS 54 G A - - -69.5 - - - - - - - 184.1 - 33.9 - 55 GLU 55 e A - - -56.8 174.6 - - - - - - 182.8 -1.4 34.5 - 56 VAL 56 E B 58.6 - - - - - - - - - 172.9 -1.2 33.0 - * * * 57 LYS 57 E B - - -78.0 - - - - - - - 181.6 -1.5 33.0 - 58 LEU 58 E B - 191.9 - - - - - - - - 183.8 - 35.0 - 59 ILE 59 E B - - -60.4 180.5 - - - - - - 176.8 -3.0 35.3 - * * 60 SER 60 E B 59.2 - - - - - - - - - 177.1 -2.7 34.3 - 61 ALA 61 T l - - - - - - - - - - 179.0 - 32.9 - 62 GLY 62 T - - - - - - - - - - - 180.7 - - - 63 LYS 63 E B - 178.2 - 185.3 - - - - - - 175.6 -1.7 34.5 - 64 VAL 64 E B 61.9 - - - - - - - - - 182.5 - 33.1 - Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 65 LEU 65 e B - - -68.1 - - - - - - - 180.5 -2.9 32.4 - * * 66 GLU 66 t B - 192.9 - - - - - - - - 188.3 - 34.3 - * * 67 ASN 67 T A 58.0 - - - - - - - - - 183.4 -.6 32.4 - +* +* 68 SER 68 T A - 187.1 - - - - - - - - 177.8 - 32.8 - 69 LYS 69 t B - - -68.0 - - - - - - - 177.9 -2.4 33.1 - 70 THR 70 h B 54.6 - - - - - - - - - 175.9 - 36.0 - 71 VAL 71 H A - 181.4 - - - -64.8 -31.3 - - - 177.9 -2.9 34.2 - * * 72 LYS 72 H A - 182.0 - 177.5 - -56.0 -33.5 - - - 182.2 -2.6 35.7 - 73 ASP 73 H A - 184.7 - - - -71.4 -27.8 - - - 180.9 -.8 34.0 - * +* +* 74 TYR 74 H A - - -65.5 - - -95.2 -26.4 - - - 178.0 -1.0 34.2 - +** * * +** 75 ARG 75 h B - 186.6 - 190.7 - - - - - - 177.0 -2.3 36.9 - 76 SER 76 t B - - -55.9 - - - - - - - 183.0 - 35.7 - 77 PRO 77 T - - - - - -41.9 - - - - - 182.1 - 38.6 - ** * ** 78 VAL 78 T A - 189.6 - - - - - - - - 185.6 - 35.0 - 79 SER 79 t l - - -56.4 - - - - - - - 183.9 -.5 32.0 - ** ** 80 ASN 80 S A - 182.2 - - - - - - - - 177.9 - 33.5 - 81 LEU 81 S B - - -66.8 - - - - - - - 182.9 - 34.7 - 82 ALA 82 b - - - - - - - - - - 181.0 - 35.5 - 83 GLY 83 S - - - - - - - - - - - 180.1 - - - 84 ALA 84 B - - - - - - - - - - 177.0 -2.3 34.6 - 85 VAL 85 B - 178.6 - - - - - - - - 186.7 - 34.4 - * * 86 THR 86 E B - - -45.5 - - - - - - - 182.7 -3.4 34.8 - * +* +* 87 THR 87 E B - - -50.2 - - - - - - - 176.0 -.5 35.2 - * ** ** 88 MET 88 E B - - -82.6 - - - - - - - 182.1 -2.8 33.0 - * * * 89 HIS 89 E B - 188.6 - - - - - - - - 180.6 -3.4 34.8 - +* +* 90 VAL 90 E B 65.7 - - - - - - - - - 177.8 -2.7 33.8 - 91 ILE 91 E B - - -65.2 - - - - - - - 185.2 -2.7 34.5 - 92 ILE 92 E B - - -55.1 - - - - - - - 178.9 -.6 35.6 - +* +* 93 GLN 93 e B - - -59.3 182.3 - - - - - - 168.4 -1.0 36.1 - +* * +* 94 ALA 94 B - - - - - - - - - - 184.0 -.5 34.5 - ** ** 95 PRO 95 - - - - - -68.4 - - - - - 176.7 - 37.6 - * * 96 VAL 96 b - 184.5 - - - - - - - - 181.3 - 33.3 - 97 THR 97 S a - 185.1 - - - - - - - - 187.9 -1.2 35.3 - * * * 98 GLU 98 S l - 194.1 - - - - - - - - 186.6 - 31.7 - * * 99 LYS 99 S b - 179.4 - 179.8 - - - - - - 187.0 - 34.7 - * * 100 GLU 100 XX - 194.9 - - - - - - - - 171.1 - 32.6 - **** +* **** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 LYS 101 - - - -62.3 180.5 - - - - - - - -2.6 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** +** * ** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.9 184.5 -61.3 178.2 -58.8 -66.8 -35.4 - - - 179.9 -2.0 34.3 Standard deviations: 5.0 7.3 7.5 5.2 9.4 9.4 7.7 - - - 3.8 1.0 1.8 Numbers of values: 18 28 36 21 6 14 14 0 0 0 100 53 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_10 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 - 1.228 1.516 1.532 1.476 - 116.40 119.72 109.60 109.42 110.66 123.88 2 ALA 2 1.340 1.235 1.522 1.531 1.472 124.04 115.35 121.43 111.92 111.08 112.31 123.18 * * * 3 GLU 3 1.308 1.237 1.516 1.536 1.438 122.89 117.14 120.10 111.65 109.81 109.38 122.75 * * * 4 VAL 4 1.305 1.232 1.516 1.560 1.436 121.57 115.35 121.05 111.25 110.51 111.70 123.59 +* * +* 5 HIS 5 1.298 1.222 1.513 1.551 1.440 123.05 114.47 122.12 112.51 111.66 112.70 123.37 ** * * * ** 6 ASN 6 1.278 1.235 1.482 1.530 1.450 123.99 113.14 122.30 110.55 105.23 111.19 124.57 +*** ** * +* ** +*** 7 GLN 7 1.306 1.241 1.520 1.548 1.411 123.69 119.12 119.30 108.41 104.09 111.17 121.58 +* ** * * +** +** 8 LEU 8 1.287 1.230 1.508 1.554 1.437 118.20 117.23 120.39 111.82 110.14 114.42 122.38 +** * * +* ** +** 9 GLU 9 1.315 1.234 1.493 1.550 1.426 119.21 115.17 121.04 108.49 108.59 114.17 123.75 +* * +* * ** ** 10 ILE 10 1.290 1.240 1.503 1.565 1.425 122.86 115.80 120.74 109.64 109.20 111.44 123.39 +** * +* +** 11 LYS 11 1.294 1.243 1.504 1.528 1.432 121.49 116.15 120.59 111.63 109.36 112.73 123.25 ** * * * ** Residue-by-residue listing for refined_10 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 1.301 1.225 1.510 1.533 1.439 121.51 116.62 120.38 109.68 109.82 109.97 122.99 ** ** 13 ARG 13 1.304 1.243 1.515 1.538 1.440 121.63 114.93 121.24 112.24 110.24 111.63 123.83 +* * +* 14 LEU 14 1.309 1.235 1.514 1.542 1.444 123.77 115.30 121.36 106.95 111.24 110.33 123.25 * * +* +* 15 THR 15 1.313 1.225 1.539 1.533 1.437 122.88 115.00 121.65 110.26 109.26 109.10 123.32 * * * * 16 ASP 16 1.327 1.231 1.544 1.541 1.463 123.77 116.17 121.45 109.92 110.99 107.88 122.30 * +* +* 17 GLY 17 1.319 1.230 1.518 - 1.460 120.84 115.86 121.04 - 112.61 - 123.10 18 SER 18 1.308 1.226 1.519 1.530 1.441 122.36 117.85 119.87 111.37 108.49 109.70 122.27 +* +* 19 ASP 19 1.302 1.239 1.508 1.538 1.437 120.63 114.48 121.72 110.12 112.99 111.39 123.77 +* * +* 20 ILE 20 1.299 1.235 1.524 1.567 1.437 123.81 116.58 119.41 109.65 107.29 110.92 124.01 ** * * * * ** 21 GLY 21 1.331 1.249 1.516 - 1.454 122.50 117.14 120.05 - 113.00 - 122.81 * * 22 PRO 22 1.345 1.241 1.521 1.532 1.459 123.67 114.67 121.60 110.04 114.36 104.20 123.73 * * * * * 23 LYS 23 1.297 1.220 1.515 1.539 1.441 124.01 117.88 119.45 110.02 107.16 109.48 122.66 ** * * ** 24 ALA 24 1.308 1.231 1.518 1.519 1.444 120.59 116.16 120.86 110.75 109.82 110.57 122.97 +* +* 25 PHE 25 1.301 1.227 1.498 1.535 1.443 122.69 118.50 119.87 107.49 107.57 111.22 121.59 +* * * * * +* 26 PRO 26 1.315 1.225 1.518 1.534 1.454 121.62 116.69 120.25 109.73 110.22 103.84 123.05 +* +* 27 ASP 27 1.309 1.230 1.529 1.550 1.465 122.37 116.51 120.82 110.93 111.91 111.62 122.54 * * * 28 ALA 28 1.314 1.237 1.537 1.517 1.446 121.36 118.45 120.01 110.46 113.02 110.49 121.54 * * * 29 THR 29 1.323 1.240 1.543 1.570 1.448 119.26 116.61 120.76 111.54 108.99 114.16 122.56 * * * +* +* 30 THR 30 1.309 1.240 1.532 1.544 1.443 121.84 115.74 121.24 109.97 112.27 110.83 123.02 * * 31 VAL 31 1.324 1.233 1.535 1.552 1.458 123.17 116.50 120.93 110.35 110.53 111.33 122.56 32 SER 32 1.321 1.227 1.537 1.533 1.443 121.20 115.87 120.77 111.68 109.97 109.89 123.24 33 ALA 33 1.333 1.235 1.524 1.516 1.461 122.92 115.86 120.74 110.72 110.62 110.13 123.40 34 LEU 34 1.324 1.240 1.538 1.533 1.423 123.51 115.87 121.29 112.19 109.19 107.58 122.80 +* * * +* +* 35 LYS 35 1.329 1.214 1.515 1.536 1.450 121.47 116.99 120.33 111.86 111.45 112.72 122.66 * * 36 GLU 36 1.315 1.232 1.524 1.519 1.449 121.30 116.43 120.78 111.00 110.92 111.10 122.77 37 THR 37 1.318 1.227 1.541 1.543 1.431 120.92 117.82 119.58 111.21 111.46 111.82 122.55 * * 38 VAL 38 1.346 1.218 1.535 1.576 1.475 120.75 115.81 120.65 111.37 110.94 113.27 123.49 * * * * * 39 ILE 39 1.320 1.231 1.538 1.559 1.474 122.78 115.83 121.54 108.81 110.44 110.57 122.61 40 SER 40 1.316 1.228 1.531 1.520 1.443 122.06 116.33 120.35 111.37 112.36 109.88 123.31 41 GLU 41 1.314 1.235 1.522 1.516 1.439 123.12 116.92 120.49 109.52 111.71 108.86 122.59 * * 42 TRP 42 1.305 1.240 1.518 1.539 1.439 121.02 118.19 119.62 109.95 109.09 109.97 122.06 +* +* Residue-by-residue listing for refined_10 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 PRO 43 1.351 1.227 1.529 1.532 1.451 122.39 115.54 121.46 110.29 110.91 104.05 122.98 * * 44 ARG 44 1.300 1.226 1.526 1.523 1.450 123.15 115.49 121.61 111.74 110.27 109.05 122.90 ** ** 45 GLU 45 1.312 1.238 1.555 1.541 1.452 123.19 116.76 121.48 111.29 110.01 108.36 121.75 * * * * 46 LYS 46 1.319 1.239 1.535 1.537 1.452 120.97 116.86 120.45 109.12 109.89 110.40 122.68 47 GLU 47 1.321 1.240 1.499 1.520 1.436 121.43 114.82 120.26 109.70 109.79 112.40 124.90 * * * * * 48 ASN 48 1.308 1.241 1.518 1.541 1.465 124.96 116.48 121.05 110.54 112.12 113.10 122.45 * +* +* +* 49 GLY 49 1.312 1.231 1.502 - 1.423 119.63 116.74 119.39 - 112.83 - 123.86 * +* +* 50 PRO 50 1.356 1.228 1.544 1.529 1.519 126.59 116.27 121.00 108.96 115.76 101.41 122.57 +*** +* * +*** 51 LYS 51 1.284 1.224 1.543 1.561 1.444 122.49 116.58 120.86 115.26 111.63 109.43 122.56 *** +* +** *** 52 THR 52 1.318 1.238 1.530 1.547 1.448 121.93 116.79 120.06 109.55 109.53 112.79 123.14 53 VAL 53 1.327 1.234 1.546 1.561 1.467 122.79 117.37 120.56 111.96 113.27 111.82 122.05 * * * 54 LYS 54 1.319 1.230 1.527 1.529 1.467 121.42 116.51 120.92 109.66 112.02 110.97 122.56 55 GLU 55 1.309 1.230 1.538 1.526 1.445 121.95 116.99 120.62 110.94 111.43 109.06 122.33 * * 56 VAL 56 1.321 1.234 1.550 1.571 1.452 120.82 116.09 121.38 110.79 112.90 111.04 122.49 * * * 57 LYS 57 1.323 1.238 1.507 1.548 1.462 122.23 116.21 120.32 109.18 109.07 113.99 123.47 ** ** 58 LEU 58 1.304 1.234 1.541 1.562 1.433 121.76 116.45 120.51 113.06 107.65 107.74 123.04 +* +* * +* * +* +* 59 ILE 59 1.327 1.224 1.527 1.571 1.469 123.05 116.70 120.69 109.07 110.57 110.40 122.59 * * 60 SER 60 1.307 1.243 1.511 1.524 1.429 121.85 116.25 119.67 110.35 109.15 110.77 123.97 +* +* +* 61 ALA 61 1.334 1.238 1.536 1.532 1.474 123.58 116.17 121.11 111.27 111.84 110.73 122.69 * * 62 GLY 62 1.317 1.235 1.515 - 1.436 120.88 117.47 120.07 - 113.33 - 122.46 63 LYS 63 1.319 1.235 1.510 1.544 1.452 121.22 116.38 120.14 109.26 109.99 111.39 123.46 64 VAL 64 1.316 1.245 1.534 1.574 1.444 121.50 116.41 120.92 111.19 108.74 112.21 122.63 * * 65 LEU 65 1.300 1.242 1.501 1.538 1.433 121.20 115.15 121.25 110.79 111.18 112.53 123.59 ** * * * ** 66 GLU 66 1.296 1.232 1.524 1.544 1.421 122.77 115.17 121.08 113.68 106.80 108.47 123.75 ** +* +* +* * ** 67 ASN 67 1.313 1.236 1.523 1.526 1.473 124.91 117.96 119.38 109.93 116.24 111.01 122.66 * +* +* +* 68 SER 68 1.315 1.239 1.539 1.531 1.446 120.83 117.15 120.39 111.86 111.90 110.30 122.47 * * 69 LYS 69 1.321 1.234 1.506 1.543 1.442 121.16 115.64 121.07 109.15 110.45 113.51 123.29 +* +* 70 THR 70 1.296 1.241 1.520 1.541 1.422 122.84 116.78 120.30 108.88 109.56 109.82 122.91 ** +* ** 71 VAL 71 1.321 1.230 1.539 1.556 1.456 121.20 114.70 121.62 110.16 108.53 111.34 123.63 72 LYS 72 1.326 1.230 1.534 1.535 1.462 125.19 116.54 120.57 110.25 111.38 108.12 122.87 +* * +* 73 ASP 73 1.323 1.245 1.531 1.533 1.468 121.85 115.99 121.26 110.30 111.26 110.39 122.74 Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 TYR 74 1.317 1.233 1.518 1.527 1.448 122.19 115.33 121.26 110.81 110.53 110.01 123.41 75 ARG 75 1.317 1.235 1.531 1.527 1.436 123.34 117.22 120.22 108.78 108.81 108.43 122.56 * * * 76 SER 76 1.311 1.234 1.542 1.507 1.430 121.58 117.72 119.61 110.31 109.10 108.36 122.65 * * * * * 77 PRO 77 1.353 1.237 1.517 1.520 1.484 124.35 115.34 121.24 110.28 114.62 102.85 123.40 * * * * 78 VAL 78 1.286 1.226 1.536 1.561 1.455 122.21 114.79 121.74 110.14 108.44 110.35 123.38 *** *** 79 SER 79 1.333 1.236 1.529 1.538 1.463 124.11 115.84 121.61 111.99 109.82 112.10 122.51 * * 80 ASN 80 1.316 1.229 1.509 1.540 1.452 121.52 115.95 121.19 111.28 110.02 110.76 122.84 81 LEU 81 1.310 1.240 1.522 1.517 1.390 122.58 116.70 120.64 111.01 109.40 109.63 122.66 * +*** +*** 82 ALA 82 1.302 1.249 1.515 1.519 1.406 122.05 115.21 121.18 110.97 109.23 108.54 123.61 +* +** * +** 83 GLY 83 1.299 1.229 1.506 - 1.444 122.73 115.32 121.50 - 111.32 - 123.16 ** * ** 84 ALA 84 1.293 1.238 1.510 1.520 1.433 123.03 116.49 120.49 110.40 109.73 110.17 123.02 +** * +** 85 VAL 85 1.301 1.243 1.514 1.555 1.431 121.32 116.13 120.81 110.17 107.26 111.78 123.06 ** * * ** 86 THR 86 1.292 1.232 1.518 1.538 1.416 121.63 116.26 120.94 110.98 108.40 109.87 122.71 +** ** +** 87 THR 87 1.295 1.235 1.527 1.531 1.416 120.80 115.87 120.93 109.75 110.76 109.72 123.19 ** ** * ** 88 MET 88 1.302 1.229 1.498 1.531 1.440 122.52 116.22 120.62 110.66 109.76 112.26 123.16 +* * * +* 89 HIS 89 1.296 1.235 1.510 1.532 1.431 121.83 115.90 120.88 110.50 108.84 110.06 123.22 ** * ** 90 VAL 90 1.288 1.234 1.511 1.557 1.437 121.41 114.76 121.53 110.80 109.83 111.18 123.65 +** * +** 91 ILE 91 1.280 1.244 1.512 1.531 1.420 123.22 115.10 121.04 111.33 108.50 109.86 123.85 *** +* * *** 92 ILE 92 1.304 1.237 1.523 1.555 1.437 122.76 116.73 120.47 109.06 110.28 110.17 122.80 +* * +* 93 GLN 93 1.315 1.229 1.489 1.511 1.438 121.22 115.59 120.71 105.97 110.64 112.03 123.69 +* * ** ** 94 ALA 94 1.275 1.238 1.519 1.518 1.418 121.66 118.40 119.99 111.11 105.49 110.83 121.54 +*** ** * ** +*** 95 PRO 95 1.326 1.245 1.511 1.523 1.445 122.00 115.00 121.83 110.40 112.98 104.86 123.16 * * +* +* 96 VAL 96 1.291 1.227 1.510 1.544 1.423 121.64 114.93 121.62 110.17 107.72 113.24 123.26 +** +* * * +** 97 THR 97 1.293 1.244 1.532 1.578 1.440 122.89 113.58 122.02 111.61 107.38 109.05 124.26 +** * * * * * +** 98 GLU 98 1.340 1.234 1.513 1.560 1.450 124.87 114.08 121.81 113.65 106.05 112.63 123.95 +* +* * +* +* * +* 99 LYS 99 1.308 1.254 1.502 1.534 1.437 124.46 115.68 119.79 110.12 107.35 111.06 124.53 +* * * * +* * +* 100 GLU 100 1.336 1.230 1.548 1.560 1.476 125.25 115.04 121.76 113.80 106.76 110.61 123.16 * * +* +* +* +* 101 LYS 101 1.303 - 1.513 1.524 1.419 124.09 - - 109.87 106.49 111.54 - +* ** * +* ** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 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: +*** * ** +* +*** +* +* +** +** ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 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 1.275 1.346 1.310 .014 +*** * * C-N (Pro) 1.341 .016 6 1.315 1.356 1.341 .015 +* C-O C-O 1.231 .020 100 1.214 1.254 1.234 .007 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.482 1.555 1.522 .014 ** * CH2G*-C (Gly) 1.516 .018 5 1.502 1.518 1.511 .006 CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.516 1.532 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.531 1.578 1.555 .014 * CH1E-CH2E (the rest) 1.530 .020 62 1.507 1.562 1.535 .012 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.390 1.476 1.443 .017 +*** NH1-CH2G* (Gly) 1.451 .016 5 1.423 1.460 1.444 .013 +* N-CH1E (Pro) 1.466 .015 6 1.445 1.519 1.469 .026 * +*** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 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 89 113.14 119.12 116.18 1.08 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.32 117.47 116.51 .80 CH1E-C-N (Pro) 116.9 1.5 6 114.67 116.69 115.59 .70 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.54 124.90 123.02 .65 * O-C-N (Pro) 122.0 1.4 6 122.57 123.73 123.15 .36 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.20 125.25 122.29 1.32 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.63 122.73 121.32 1.15 * C-N-CH1E (Pro) 122.6 5.0 6 121.62 126.59 123.44 1.70 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 119.30 122.30 120.80 .68 CH2G*-C-O (Gly) 120.8 2.1 5 119.39 121.50 120.41 .76 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.40 111.92 110.95 .46 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.81 111.96 110.37 .89 * CH2E-CH1E-C (the rest) 110.1 1.9 62 105.97 115.26 110.57 1.59 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.09 116.24 109.81 1.94 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 5 111.32 113.33 112.62 .69 N-CH1E-C (Pro) 111.8 2.5 6 110.22 115.76 113.14 2.00 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 108.54 112.31 110.47 .97 * * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.05 114.16 111.14 1.27 * +* N-CH1E-CH2E (Pro) 103.0 1.1 6 101.41 104.86 103.53 1.12 * +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 107.58 114.42 110.72 1.67 +* ** ------------------------------------------------------------------------------------------------------------- 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_10 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] 76 86.4% 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] 1 1.1% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 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 86.4 83.8 10.0 .3 Inside b. Omega angle st dev 100 3.8 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 53 1.0 .8 .2 .7 Inside f. Overall G-factor 101 -.1 -.4 .3 1.0 Inside S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 5.0 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 28 7.3 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 36 7.5 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 82 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 21 5.2 20.4 5.0 -3.0 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% 86.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .95 3 Residue-by-residue listing for refined_10 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.61 Chi1-chi2 distribution -.27 Chi1 only -.24 Chi3 & chi4 .24 Omega -.11 ------ -.25 ===== Main-chain covalent forces:- Main-chain bond lengths -.03 Main-chain bond angles .36 ------ .19 ===== OVERALL AVERAGE -.09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.