Residue-by-residue listing for refined_11 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 - - - -65.9 - - - - - - - 172.3 - 35.2 - * * 2 ALA 2 b - - - - - - - - - - 190.0 - 34.2 - +* +* 3 GLU 3 S ~l - 178.2 - 184.1 - - - - - - 175.4 -1.2 32.0 - ** * ** 4 VAL 4 t b 55.0 - - - - - - - - - 188.4 - 28.6 - * +* +* 5 HIS 5 T A - 200.1 - - - - - - - - 174.5 -1.7 34.2 - 6 ASN 6 T A - - -64.2 - - - - - - - 179.4 - 34.2 - 7 GLN 7 t B - - -61.7 174.7 - - - - - - 178.8 -1.3 35.8 - 8 LEU 8 E B 55.7 - - 163.8 - - - - - - 182.1 -2.3 31.5 - 9 GLU 9 E B - - -57.8 178.5 - - - - - - 180.4 -1.0 34.3 - * * 10 ILE 10 E B - - -55.4 177.5 - - - - - - 172.4 -2.7 35.2 - * * 11 LYS 11 E B 59.6 - - 160.1 - - - - - - 182.0 -2.8 33.1 - 12 PHE 12 E B - - -51.5 - - - - - - - 184.2 -.6 34.7 - * +* +* 13 ARG 13 E B - 197.1 - - - - - - - - 180.6 -3.6 33.5 - ** ** 14 LEU 14 E B - - -71.9 - - - - - - - 176.6 -2.7 36.6 - 15 THR 15 e A - - -55.0 - - - - - - - 179.5 -1.4 35.2 - 16 ASP 16 T A - - -57.4 - - - - - - - 178.9 - 34.7 - 17 GLY 17 t - - - - - - - - - - - 176.9 -2.0 - - 18 SER 18 e B - 182.2 - - - - - - - - 176.7 - 35.3 - 19 ASP 19 E B 60.0 - - - - - - - - - 178.7 - 33.2 - 20 ILE 20 E B - - -58.3 179.4 - - - - - - 182.3 -2.4 35.1 - Residue-by-residue listing for refined_11 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 - - - - - - - - - - - 183.2 - - - 22 PRO 22 E - - - - - -74.6 - - - - - 177.1 - 38.3 - * * 23 LYS 23 E B - - -74.0 - - - - - - - 177.8 -2.2 34.1 - 24 ALA 24 E B - - - - - - - - - - 179.5 - 33.1 - 25 PHE 25 E B - - -57.8 - - - - - - - 171.9 -3.5 36.4 - * +* +* 26 PRO 26 t - - - - - -65.7 - - - - - 177.9 - 40.0 - +* +* 27 ASP 27 T A 53.2 - - - - - - - - - 179.3 - 31.5 - 28 ALA 28 T A - - - - - - - - - - 177.1 - 33.9 - 29 THR 29 t B - - -54.0 - - - - - - - 178.5 -1.8 35.8 - 30 THR 30 h B 52.3 - - - - - - - - - 176.5 - 33.6 - 31 VAL 31 H A - 174.1 - - - -65.4 -26.5 - - - 172.1 -3.4 31.9 - * * +* +* 32 SER 32 H A - - -59.6 - - -57.9 -49.6 - - - 180.5 -1.9 34.7 - 33 ALA 33 H A - - - - - -68.2 -29.0 - - - 177.0 - 33.5 - 34 LEU 34 H A - 174.9 - - - -63.8 -48.2 - - - 178.3 -1.8 35.5 - 35 LYS 35 H A - - -62.6 174.4 - -69.8 -36.7 - - - 176.3 -2.7 33.3 - 36 GLU 36 H A - - -67.8 - - -63.7 -32.2 - - - 175.5 -2.7 33.3 - 37 THR 37 H A - - -58.5 - - -65.8 -37.1 - - - 174.8 -1.8 33.5 - 38 VAL 38 H A - 180.7 - - - -59.4 -47.7 - - - 180.9 -1.3 35.8 - 39 ILE 39 H A - - -53.7 - - -63.8 -34.5 - - - 179.5 -2.3 34.4 - 40 SER 40 H A - - -56.7 - - -66.8 -35.3 - - - 180.6 -2.2 34.3 - 41 GLU 41 h A - - -65.3 - - - - - - - 181.8 -1.7 35.9 - 42 TRP 42 t B - 199.2 - - - - - - - - 174.3 -.5 36.5 - ** ** 43 PRO 43 t - - - - - -71.6 - - - - - 176.3 - 38.9 - * * 44 ARG 44 T A - - -67.2 - - - - - - - 177.1 -.8 32.0 - +* +* 45 GLU 45 T A 60.1 - - 173.9 - - - - - - 181.1 - 35.0 - 46 LYS 46 t b - 179.4 - - - - - - - - 173.4 -1.0 35.0 - * * * 47 GLU 47 S B - - -52.1 179.1 - - - - - - 186.2 - 35.2 - * * 48 ASN 48 S l - 176.3 - - - - - - - - 177.5 - 30.6 - 49 GLY 49 S - - - - - - - - - - - 179.2 - - - 50 PRO 50 - - - - - -48.5 - - - - - 177.0 - 39.6 - +* +* +* 51 LYS 51 A - - -60.5 181.0 - - - - - - 180.7 - 33.2 - 52 THR 52 g B 60.3 - - - - - - - - - 179.5 - 33.3 - 53 VAL 53 G A 51.2 - - - - - - - - - 181.3 - 33.6 - 54 LYS 54 G A - 177.6 - 184.7 - - - - - - 187.2 - 35.7 - * * 55 GLU 55 e A 57.2 - - 199.7 - - - - - - 179.0 -.7 32.7 - * +* +* 56 VAL 56 E B - 177.5 - - - - - - - - 177.0 -1.3 34.7 - * * 57 LYS 57 E B - - -64.1 179.9 - - - - - - 184.1 -1.6 33.6 - 58 LEU 58 E B - 190.8 - - - - - - - - 183.2 -.5 34.7 - ** ** 59 ILE 59 E B - - -60.6 180.1 - - - - - - 177.4 -3.2 35.3 - * * 60 SER 60 E B 53.8 - - - - - - - - - 180.4 -2.9 33.2 - * * 61 ALA 61 T l - - - - - - - - - - 181.0 - 32.3 - Residue-by-residue listing for refined_11 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 62 GLY 62 T - - - - - - - - - - - 181.1 - - - 63 LYS 63 E B - 182.0 - 176.5 - - - - - - 179.3 -1.3 34.4 - 64 VAL 64 E B 60.0 - - - - - - - - - 184.5 - 32.7 - 65 LEU 65 e B - - -58.4 188.0 - - - - - - 174.9 -2.8 34.1 - * * 66 GLU 66 t B - 170.7 - - - - - - - - 183.4 - 34.6 - 67 ASN 67 T A 60.5 - - - - - - - - - 182.5 -.6 29.8 - +* * +* 68 SER 68 T A - - -49.6 - - - - - - - 180.2 - 34.3 - * * 69 LYS 69 t B - - -61.1 181.4 - - - - - - 178.8 -1.9 34.9 - 70 THR 70 B B 57.4 - - - - - - - - - 176.6 - 34.8 - 71 VAL 71 g A - 179.5 - - - - - - - - 177.9 -2.6 34.0 - 72 LYS 72 G A - 189.4 - - - - - - - - 179.7 -2.8 34.9 - * * 73 ASP 73 G A - - -71.8 - - - - - - - 179.2 - 33.5 - 74 TYR 74 G A - - -63.6 - - - - - - - 181.9 -1.2 35.2 - * * 75 ARG 75 g B - 179.4 - - - - - - - - 176.8 -.8 37.1 - +* +* 76 SER 76 B 46.5 - - - - - - - - - 181.4 -.8 33.5 - * +* +* 77 PRO 77 - - - - - -62.8 - - - - - 179.8 - 38.3 - * * 78 VAL 78 A 64.9 - - - - - - - - - 181.6 - 34.2 - 79 SER 79 S XX - - -57.6 - - - - - - - 182.8 - 31.4 - **** **** 80 ASN 80 S ~p - 191.0 - - - - - - - - 178.5 - 33.0 - ** ** 81 LEU 81 B 64.2 - - 168.8 - - - - - - 182.3 - 33.2 - 82 ALA 82 b - - - - - - - - - - 180.0 - 33.6 - 83 GLY 83 - - - - - - - - - - - 180.0 - - - 84 ALA 84 e B - - - - - - - - - - 181.0 - 33.7 - 85 VAL 85 E B 58.6 - - - - - - - - - 181.3 - 32.0 - 86 THR 86 E B - - -50.6 - - - - - - - 179.3 -3.5 36.2 - * +* +* 87 THR 87 E B - - -55.0 - - - - - - - 178.9 -.5 35.8 - ** ** 88 MET 88 E B - - -65.5 181.8 - - - - - - 185.2 -2.4 31.9 - 89 HIS 89 E B - 184.0 - - - - - - - - 181.0 -2.2 35.6 - 90 VAL 90 E B 70.1 - - - - - - - - - 178.1 -2.7 32.9 - 91 ILE 91 E B - - -68.1 183.5 - - - - - - 183.6 -2.5 33.1 - 92 ILE 92 E B - - -59.1 - - - - - - - 180.0 -.6 34.8 - +* +* 93 GLN 93 e B - - -69.8 171.9 - - - - - - 180.0 -.8 34.5 - +* +* 94 ALA 94 B - - - - - - - - - - 181.7 - 33.9 - 95 PRO 95 - - - - - -66.6 - - - - - 176.7 - 39.5 - +* +* 96 VAL 96 S B - 181.1 - - - - - - - - 187.1 - 34.1 - * * 97 THR 97 S l - - -59.0 - - - - - - - 181.9 -.5 32.2 - ** ** 98 GLU 98 B 60.2 - - - - - - - - - 180.1 - 33.0 - 99 LYS 99 ~l - 177.5 - 177.3 - - - - - - 181.6 -.7 31.9 - ** +* ** 100 GLU 100 A - 186.0 - 180.6 - - - - - - 180.7 - 34.1 - Residue-by-residue listing for refined_11 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 - - 189.9 - - - - - - - - - - 33.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * +* * +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.1 183.3 -60.6 178.4 -65.0 -64.5 -37.7 - - - 179.6 -1.8 34.3 Standard deviations: 5.3 8.0 6.2 7.9 9.1 3.7 8.2 - - - 3.4 .9 1.9 Numbers of values: 20 24 38 24 6 10 10 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_11 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 - 1.230 1.512 1.536 1.461 - 116.55 120.55 108.36 111.27 110.88 122.90 2 ALA 2 1.315 1.237 1.510 1.521 1.442 121.38 115.27 120.27 111.08 106.39 110.99 124.40 * +* +* 3 GLU 3 1.324 1.253 1.520 1.544 1.456 124.54 116.54 121.20 109.89 109.35 114.56 122.21 * +* ** ** 4 VAL 4 1.306 1.230 1.503 1.533 1.421 119.71 112.82 123.35 114.01 110.24 114.76 123.83 +* * +* * +* * ** +* ** 5 HIS 5 1.275 1.226 1.527 1.543 1.447 123.49 115.36 121.38 112.19 109.68 108.95 123.27 +*** * +*** 6 ASN 6 1.333 1.235 1.513 1.549 1.461 122.31 115.50 121.49 109.15 109.09 112.29 123.01 * * 7 GLN 7 1.315 1.237 1.508 1.514 1.419 122.82 116.48 120.38 109.92 108.47 109.19 123.14 ** ** 8 LEU 8 1.293 1.226 1.510 1.551 1.436 121.19 117.35 120.39 111.28 110.14 113.74 122.26 +** * * +* +** 9 GLU 9 1.309 1.217 1.489 1.519 1.432 119.99 115.98 120.96 109.11 109.43 112.01 123.03 * +* * +* 10 ILE 10 1.287 1.241 1.510 1.568 1.433 121.72 115.90 120.63 108.92 109.51 111.39 123.42 +** * * +** 11 LYS 11 1.298 1.246 1.507 1.532 1.425 121.76 116.46 120.50 109.26 107.97 114.13 123.04 ** +* * ** ** Residue-by-residue listing for refined_11 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 1.290 1.229 1.503 1.525 1.435 121.05 116.50 120.36 111.34 108.54 109.47 123.12 +** * * +** 13 ARG 13 1.304 1.239 1.523 1.548 1.428 121.39 114.40 121.66 113.01 109.38 109.56 123.93 +* +* +* +* 14 LEU 14 1.301 1.240 1.503 1.566 1.451 124.87 114.95 121.30 107.32 110.18 110.60 123.65 ** * +* +* * ** 15 THR 15 1.295 1.224 1.555 1.519 1.426 123.11 115.59 121.76 110.32 109.74 109.07 122.58 ** * +* * ** 16 ASP 16 1.331 1.230 1.527 1.533 1.464 122.80 116.17 121.00 109.26 110.93 110.56 122.83 17 GLY 17 1.323 1.230 1.517 - 1.457 121.37 116.31 120.85 - 112.85 - 122.83 18 SER 18 1.306 1.216 1.517 1.545 1.442 121.83 118.01 119.70 110.46 107.80 109.78 122.27 +* * +* 19 ASP 19 1.296 1.233 1.495 1.537 1.418 121.49 115.90 120.68 110.93 109.70 112.04 123.41 ** * ** ** 20 ILE 20 1.290 1.234 1.516 1.566 1.441 122.78 116.58 119.28 109.83 107.43 111.12 124.11 +** * +** 21 GLY 21 1.340 1.242 1.524 - 1.461 122.57 117.63 120.06 - 113.40 - 122.31 * * 22 PRO 22 1.342 1.240 1.519 1.525 1.454 123.00 114.93 121.72 110.18 113.79 103.84 123.35 * * 23 LYS 23 1.298 1.216 1.479 1.544 1.462 123.18 116.78 119.63 107.48 108.52 114.29 123.58 ** ** * ** ** 24 ALA 24 1.293 1.240 1.512 1.527 1.439 120.91 115.93 120.95 111.29 109.07 111.58 123.06 +** +** 25 PHE 25 1.295 1.227 1.497 1.539 1.431 122.40 118.58 120.03 107.11 108.19 111.35 121.33 ** * * * +* * * ** 26 PRO 26 1.313 1.237 1.518 1.526 1.448 121.12 116.95 120.24 108.54 109.32 103.90 122.81 +* * +* 27 ASP 27 1.298 1.217 1.525 1.535 1.455 121.44 116.11 121.33 111.77 111.75 112.25 122.44 ** * ** 28 ALA 28 1.302 1.229 1.535 1.521 1.458 121.49 116.31 120.92 110.48 111.09 110.32 122.77 +* +* 29 THR 29 1.320 1.243 1.533 1.545 1.449 122.11 116.91 120.43 109.21 109.09 109.77 122.65 * * 30 THR 30 1.309 1.241 1.516 1.536 1.426 120.95 116.17 120.91 109.97 110.97 111.74 122.92 * +* +* 31 VAL 31 1.309 1.231 1.546 1.556 1.436 122.01 116.77 120.83 113.20 109.73 111.41 122.39 * * +* +* 32 SER 32 1.344 1.222 1.526 1.537 1.459 121.36 116.34 120.53 109.33 109.31 111.05 123.04 * * 33 ALA 33 1.334 1.227 1.525 1.515 1.456 122.03 116.06 120.99 110.82 110.94 110.62 122.95 34 LEU 34 1.322 1.231 1.537 1.534 1.417 123.33 115.82 121.02 112.15 108.85 107.35 123.08 ** * +* ** 35 LYS 35 1.324 1.214 1.523 1.518 1.452 122.33 116.86 120.47 111.31 111.35 110.25 122.67 36 GLU 36 1.316 1.226 1.527 1.527 1.459 121.89 116.84 120.66 111.11 110.93 110.69 122.49 37 THR 37 1.326 1.236 1.545 1.552 1.451 121.27 115.71 121.01 110.85 108.98 111.54 123.25 38 VAL 38 1.337 1.221 1.525 1.568 1.467 122.72 115.02 121.21 108.23 108.38 111.16 123.72 * * * 39 ILE 39 1.329 1.225 1.536 1.567 1.464 123.75 116.27 121.05 110.07 110.85 110.62 122.66 * * 40 SER 40 1.313 1.238 1.537 1.529 1.453 122.23 115.91 120.95 110.81 110.80 109.67 123.09 * * 41 GLU 41 1.321 1.233 1.523 1.509 1.434 123.21 115.93 120.89 109.63 111.64 108.31 123.17 * * * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 TRP 42 1.297 1.236 1.523 1.532 1.439 122.28 118.68 120.08 109.25 108.29 108.89 121.15 ** * * * ** 43 PRO 43 1.322 1.218 1.540 1.542 1.453 121.64 117.17 120.44 109.48 111.69 104.26 122.39 * * * 44 ARG 44 1.327 1.229 1.510 1.545 1.472 121.43 115.25 121.40 109.73 109.70 114.45 123.29 ** ** 45 GLU 45 1.322 1.240 1.533 1.529 1.456 122.77 115.74 120.47 108.94 110.60 110.55 123.79 46 LYS 46 1.337 1.236 1.512 1.538 1.441 123.13 115.89 121.03 109.16 111.27 110.53 123.07 47 GLU 47 1.304 1.239 1.496 1.495 1.406 120.79 115.74 120.09 108.84 105.68 111.76 124.17 +* * +* +** +* +** 48 ASN 48 1.286 1.240 1.541 1.558 1.452 122.86 114.52 122.14 113.86 110.53 112.09 123.07 *** * +* *** 49 GLY 49 1.316 1.230 1.502 - 1.410 123.42 118.34 118.61 - 107.98 - 122.97 +** +* * +* +** 50 PRO 50 1.334 1.225 1.529 1.511 1.476 123.90 116.25 121.40 109.14 114.80 102.47 122.34 * * 51 LYS 51 1.299 1.230 1.528 1.526 1.434 120.69 117.32 120.46 110.79 111.37 111.17 122.22 ** * ** 52 THR 52 1.327 1.227 1.540 1.544 1.453 120.71 115.47 121.39 109.02 112.73 112.25 123.14 53 VAL 53 1.324 1.241 1.540 1.578 1.470 124.59 115.66 121.00 111.05 111.67 110.52 123.30 * +* +* 54 LYS 54 1.323 1.228 1.527 1.531 1.461 123.19 116.10 121.26 108.90 111.77 109.35 122.61 55 GLU 55 1.299 1.237 1.536 1.526 1.454 120.97 115.99 121.14 113.37 112.55 108.66 122.82 ** +* * ** 56 VAL 56 1.319 1.219 1.524 1.558 1.454 122.22 116.92 120.28 109.29 109.70 111.29 122.78 57 LYS 57 1.315 1.241 1.532 1.529 1.438 122.00 116.30 120.53 111.93 109.77 109.92 123.16 * * 58 LEU 58 1.329 1.240 1.539 1.572 1.455 122.36 116.18 120.78 112.37 108.40 108.72 123.03 ** * * ** 59 ILE 59 1.317 1.219 1.522 1.559 1.451 122.93 116.35 120.99 109.74 110.47 109.84 122.65 60 SER 60 1.302 1.243 1.519 1.526 1.427 121.88 115.93 120.36 112.07 109.69 110.52 123.58 +* +* * +* 61 ALA 61 1.332 1.230 1.526 1.535 1.470 124.23 115.73 121.24 111.57 111.28 111.53 122.94 * * 62 GLY 62 1.313 1.232 1.517 - 1.443 121.33 116.69 120.69 - 112.44 - 122.61 * * 63 LYS 63 1.320 1.236 1.517 1.534 1.438 121.48 116.38 120.35 110.98 109.71 109.93 123.25 * * 64 VAL 64 1.321 1.245 1.524 1.569 1.454 121.43 116.75 120.48 111.69 109.10 112.16 122.75 * * * 65 LEU 65 1.311 1.244 1.500 1.514 1.419 120.50 114.65 121.14 109.31 112.21 111.21 124.21 * * ** ** 66 GLU 66 1.304 1.237 1.511 1.542 1.430 123.10 116.19 120.55 111.68 108.37 109.53 123.26 +* * * +* 67 ASN 67 1.326 1.227 1.523 1.564 1.452 121.74 116.12 120.93 112.67 113.18 113.27 122.88 +* * +* +* 68 SER 68 1.324 1.239 1.548 1.523 1.454 122.03 115.97 121.36 111.02 111.62 109.02 122.66 * * 69 LYS 69 1.305 1.232 1.519 1.516 1.427 123.23 116.82 120.60 110.21 109.80 109.78 122.56 +* +* +* 70 THR 70 1.300 1.241 1.509 1.542 1.405 121.91 116.74 120.30 109.83 109.29 110.94 122.96 ** +** +** 71 VAL 71 1.315 1.219 1.537 1.556 1.448 121.03 115.09 121.19 110.70 108.42 111.25 123.67 * * Residue-by-residue listing for refined_11 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.333 1.239 1.529 1.552 1.453 125.10 116.35 120.70 111.72 109.99 108.42 122.93 * +* * +* 73 ASP 73 1.328 1.225 1.526 1.537 1.446 122.51 116.66 120.49 110.32 111.81 111.16 122.84 74 TYR 74 1.324 1.241 1.537 1.523 1.447 122.47 115.97 121.19 109.45 111.01 109.62 122.84 75 ARG 75 1.314 1.230 1.506 1.505 1.422 123.73 116.19 120.85 110.27 109.54 106.54 122.90 * * +* * ** ** 76 SER 76 1.279 1.241 1.527 1.528 1.417 121.37 118.17 119.91 112.92 109.23 109.52 121.87 +*** ** * +*** 77 PRO 77 1.346 1.242 1.515 1.520 1.453 122.12 115.28 121.40 109.51 111.64 104.90 123.31 * +* +* 78 VAL 78 1.296 1.237 1.530 1.563 1.448 122.46 113.69 121.98 111.26 108.30 110.56 124.28 ** * * ** 79 SER 79 1.331 1.246 1.521 1.532 1.454 125.22 115.13 120.96 112.21 110.90 112.33 123.90 +* * * +* 80 ASN 80 1.337 1.249 1.554 1.559 1.475 124.33 119.17 119.57 112.61 108.48 110.52 121.23 * * * * * * * 81 LEU 81 1.331 1.244 1.505 1.523 1.393 120.56 114.91 121.31 109.88 111.09 112.51 123.77 *** * *** 82 ALA 82 1.287 1.236 1.502 1.520 1.419 123.16 115.31 120.87 110.85 109.10 111.46 123.80 *** * ** *** 83 GLY 83 1.292 1.235 1.495 - 1.430 121.63 115.49 120.97 - 110.39 - 123.49 +** * * +** 84 ALA 84 1.296 1.240 1.508 1.516 1.439 122.77 117.28 119.96 111.00 109.20 110.85 122.76 ** ** 85 VAL 85 1.313 1.234 1.513 1.559 1.436 119.90 114.10 122.12 111.09 110.17 113.36 123.74 * * * * * 86 THR 86 1.280 1.241 1.518 1.536 1.414 123.49 115.93 120.84 109.46 108.71 109.24 123.21 +*** ** * +*** 87 THR 87 1.288 1.235 1.526 1.545 1.417 121.92 117.24 120.19 110.15 108.19 109.29 122.52 +** ** * * +** 88 MET 88 1.314 1.224 1.509 1.531 1.452 121.03 115.83 120.73 112.03 110.85 111.88 123.44 * * * 89 HIS 89 1.304 1.230 1.513 1.534 1.447 123.38 116.26 121.20 110.14 110.19 108.82 122.54 +* +* 90 VAL 90 1.284 1.242 1.504 1.560 1.437 120.18 114.73 121.53 111.08 110.65 111.99 123.70 *** * * *** 91 ILE 91 1.288 1.243 1.510 1.538 1.417 122.75 114.57 121.53 111.54 109.24 111.56 123.89 +** ** * +** 92 ILE 92 1.292 1.230 1.507 1.543 1.421 122.86 115.39 120.95 110.39 110.35 110.03 123.65 +** +* +** 93 GLN 93 1.301 1.229 1.496 1.528 1.427 123.52 115.61 120.42 111.10 108.54 110.15 123.90 +* * +* * +* 94 ALA 94 1.305 1.242 1.531 1.520 1.446 122.46 117.33 120.42 110.97 110.59 110.08 122.25 +* +* 95 PRO 95 1.337 1.243 1.536 1.531 1.475 123.36 115.77 121.22 109.42 113.18 102.81 123.02 96 VAL 96 1.322 1.240 1.513 1.544 1.441 121.94 115.54 120.33 110.05 107.88 111.93 124.14 * * 97 THR 97 1.317 1.237 1.533 1.538 1.425 123.90 114.99 122.09 112.42 109.42 111.73 122.79 +* * +* +* 98 GLU 98 1.305 1.232 1.524 1.554 1.427 122.25 115.86 120.37 111.31 110.63 111.45 123.76 +* * +* +* 99 LYS 99 1.336 1.237 1.526 1.542 1.471 123.80 115.92 121.43 111.66 111.87 111.85 122.62 * * 100 GLU 100 1.302 1.235 1.528 1.524 1.438 121.16 115.98 121.16 110.93 110.02 110.16 122.83 +* * +* Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 LYS 101 1.310 - 1.517 1.558 1.439 121.64 - - 113.22 108.57 110.31 - * * * +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** ** *** +* +* * ** +* ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 1.344 1.311 .016 +*** * * C-N (Pro) 1.341 .016 6 1.313 1.346 1.332 .011 +* C-O C-O 1.231 .020 100 1.214 1.253 1.234 .008 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.479 1.555 1.521 .014 ** * CH2G*-C (Gly) 1.516 .018 5 1.495 1.524 1.511 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.515 1.535 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.519 1.578 1.552 .014 * CH1E-CH2E (the rest) 1.530 .020 62 1.495 1.572 1.534 .015 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.393 1.475 1.441 .017 *** NH1-CH2G* (Gly) 1.451 .016 5 1.410 1.461 1.440 .019 +** N-CH1E (Pro) 1.466 .015 6 1.448 1.476 1.460 .011 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 89 112.82 119.17 116.06 1.00 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.49 118.34 116.89 1.00 CH1E-C-N (Pro) 116.9 1.5 6 114.93 117.17 116.06 .82 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.15 124.40 123.05 .63 * O-C-N (Pro) 122.0 1.4 6 122.34 123.35 122.87 .40 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.71 125.22 122.27 1.19 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 121.33 123.42 122.06 .81 +* C-N-CH1E (Pro) 122.6 5.0 6 121.12 123.90 122.52 .98 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 119.28 123.35 120.86 .62 * CH2G*-C-O (Gly) 120.8 2.1 5 118.61 120.97 120.24 .87 * CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.48 111.57 111.01 .31 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.23 114.01 110.51 1.30 ** CH2E-CH1E-C (the rest) 110.1 1.9 62 107.11 113.86 110.54 1.53 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.68 113.18 109.86 1.38 +* NH1-CH2G*-C (Gly) 112.5 2.9 5 107.98 113.40 111.41 1.99 +* N-CH1E-C (Pro) 111.8 2.5 6 109.32 114.80 112.40 1.77 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 110.08 111.58 110.93 .53 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.07 114.76 111.17 1.24 * +* N-CH1E-CH2E (Pro) 103.0 1.1 6 102.47 104.90 103.70 .83 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.54 114.56 110.67 1.73 ** ** ------------------------------------------------------------------------------------------------------------- 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_11 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] 7 8.0% Residues in generously allowed regions [~a,~b,~l,~p] 3 3.4% 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 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 100 3.4 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.9 3.1 1.6 -.7 Inside e. H-bond energy st dev 54 .9 .8 .2 .5 Inside f. Overall G-factor 101 .0 -.4 .3 1.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 20 5.3 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 24 8.0 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 38 6.2 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 82 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 24 7.9 20.4 5.0 -2.5 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 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .94 3 Residue-by-residue listing for refined_11 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.46 Chi1-chi2 distribution -.26 Chi1 only -.02 Chi3 & chi4 .30 Omega .09 ------ -.12 ===== Main-chain covalent forces:- Main-chain bond lengths -.07 Main-chain bond angles .39 ------ .20 ===== OVERALL AVERAGE -.01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.