Residue-by-residue listing for refined_1 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLU 1 - - - -56.7 - - - - - - - 178.0 - 34.6 - 2 ALA 2 A - - - - - - - - - - 179.2 - 32.8 - 3 GLU 3 B - 181.2 - 177.7 - - - - - - 182.0 - 32.3 - 4 VAL 4 S b - 188.7 - - - - - - - - 166.9 -.5 37.3 - ** ** ** 5 HIS 5 S b - 185.2 - - - - - - - - 189.4 - 33.2 - +* +* 6 ASN 6 B - - -72.1 - - - - - - - 179.2 -1.7 31.1 - 7 GLN 7 b - - -62.2 171.7 - - - - - - 171.4 - 37.6 - * * * 8 LEU 8 E B 54.7 - - 164.6 - - - - - - 179.9 -2.1 29.0 - * * 9 GLU 9 E B - - -62.2 - - - - - - - 183.8 -1.8 31.8 - 10 ILE 10 E B - - -57.8 179.3 - - - - - - 174.9 -2.2 35.2 - 11 LYS 11 E B 64.8 - - - - - - - - - 185.6 -2.4 29.9 - * * 12 PHE 12 E B - - -55.6 - - - - - - - 183.0 -.6 34.9 - +* +* 13 ARG 13 E B - 185.1 - 180.5 - - - - - - 177.1 -3.5 35.5 - ** ** 14 LEU 14 E B - - -72.2 175.7 - - - - - - 177.3 -3.7 35.0 - ** ** 15 THR 15 e A - 186.4 - - - - - - - - 178.6 -1.2 34.6 - * * 16 ASP 16 T A - - -60.2 - - - - - - - 179.1 - 34.9 - 17 GLY 17 t - - - - - - - - - - - 179.0 -2.0 - - 18 SER 18 e B - - -54.9 - - - - - - - 181.4 - 35.8 - 19 ASP 19 E B 64.3 - - - - - - - - - 182.1 - 31.8 - Residue-by-residue listing for refined_1 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 ILE 20 E B - - -57.6 177.5 - - - - - - 181.7 -3.2 35.7 - +* +* 21 GLY 21 E - - - - - - - - - - - 183.7 - - - 22 PRO 22 E - - - - - -75.3 - - - - - 177.5 - 38.5 - * * 23 LYS 23 E B - - -75.0 - - - - - - - 182.4 -2.4 34.4 - 24 ALA 24 E B - - - - - - - - - - 179.2 - 34.1 - 25 PHE 25 E B - - -52.5 - - - - - - - 170.4 -2.7 36.3 - +* +* 26 PRO 26 t - - - - - -66.5 - - - - - 178.5 - 40.0 - +* +* 27 ASP 27 T A 67.0 - - - - - - - - - 177.0 - 32.9 - 28 ALA 28 T A - - - - - - - - - - 174.8 - 34.1 - 29 THR 29 t B - - -56.9 - - - - - - - 177.0 -2.1 35.3 - 30 THR 30 h B 54.7 - - - - - - - - - 180.2 - 34.9 - 31 VAL 31 H A - 182.9 - - - -63.6 -26.6 - - - 176.6 -3.5 33.3 - * +* +* 32 SER 32 H A 48.8 - - - - -62.3 -49.9 - - - 180.2 -.9 33.5 - +* +* 33 ALA 33 H A - - - - - -71.5 -28.6 - - - 176.9 - 33.5 - 34 LEU 34 H A - 169.8 - - - -67.1 -46.6 - - - 179.5 -2.1 35.3 - 35 LYS 35 H A - 188.9 - 179.1 - -72.3 -37.8 - - - 174.7 -2.9 33.3 - * * 36 GLU 36 H A - - -72.9 - - -56.9 -29.0 - - - 175.8 -2.8 32.8 - * * 37 THR 37 H A - - -59.3 - - -67.8 -39.9 - - - 178.4 -1.1 33.1 - * * 38 VAL 38 H A 70.8 - - - - -70.4 -36.3 - - - 177.3 -1.1 31.6 - * * 39 ILE 39 H A - - -58.2 - - -60.7 -39.7 - - - 179.4 -2.7 34.5 - 40 SER 40 H A - - -59.2 - - -65.2 -31.9 - - - 180.7 -2.1 34.1 - 41 GLU 41 H A - - -62.8 - - -90.6 -10.1 - - - 184.4 -1.2 36.0 - ** +** * +** 42 TRP 42 h B - 191.7 - - - - - - - - 174.8 -.9 36.1 - +* +* 43 PRO 43 t - - - - - -69.7 - - - - - 179.7 - 39.2 - +* +* 44 ARG 44 T A - - -52.5 180.5 - - - - - - 176.7 -.7 33.6 - +* +* 45 GLU 45 T A 61.2 - - 176.2 - - - - - - 182.3 - 36.4 - 46 LYS 46 t b - 193.1 - 180.8 - - - - - - 180.8 -1.9 34.3 - 47 GLU 47 T B - - -60.2 178.1 - - - - - - 183.0 -.7 33.5 - +* +* 48 ASN 48 T l - - -59.7 - - - - - - - 179.8 - 33.0 - 49 GLY 49 t - - - - - - - - - - - 178.7 -1.0 - - * * 50 PRO 50 - - - - - -69.2 - - - - - 178.2 - 39.4 - +* +* 51 LYS 51 a - - -54.0 176.4 - - - - - - 185.0 - 36.7 - 52 THR 52 t B 53.3 - - - - - - - - - 181.7 - 34.1 - 53 VAL 53 T A 60.3 - - - - - - - - - 183.7 - 34.5 - 54 LYS 54 T A 61.5 - - 176.8 - - - - - - 185.4 - 33.7 - 55 GLU 55 e A - - -60.2 168.2 - - - - - - 182.5 -2.0 35.1 - 56 VAL 56 E B - 181.7 - - - - - - - - 172.3 -1.0 35.7 - * * * 57 LYS 57 E B - - -87.0 - - - - - - - 183.8 -2.0 32.5 - * * Residue-by-residue listing for refined_1 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 58 LEU 58 E B - 200.2 - - - - - - - - 177.6 -.8 36.1 - +* +* 59 ILE 59 E B - - -62.1 180.6 - - - - - - 180.2 -.8 34.5 - +* +* 60 SER 60 E B 55.8 - - - - - - - - - 183.1 -2.4 34.8 - 61 ALA 61 e XX - - - - - - - - - - 178.5 -3.2 31.3 - **** +* **** 62 GLY 62 T - - - - - - - - - - - 181.5 -2.3 - - 63 LYS 63 E B - 199.8 - - - - - - - - 181.2 -1.9 35.2 - 64 VAL 64 E B 61.3 - - - - - - - - - 179.5 - 33.0 - 65 LEU 65 E B 53.9 - - 173.7 - - - - - - 183.7 -2.7 33.1 - 66 GLU 66 t B - 190.8 - 175.8 - - - - - - 189.4 - 31.7 - +* +* 67 ASN 67 T A - 186.0 - - - - - - - - 186.2 - 37.2 - * * 68 SER 68 T A - - -60.0 - - - - - - - 176.9 - 31.8 - 69 LYS 69 t B 55.2 - - 173.1 - - - - - - 178.1 -1.9 30.2 - * * 70 THR 70 B B - - -49.1 - - - - - - - 178.2 - 37.2 - * * 71 VAL 71 G A - 180.1 - - - - - - - - 177.1 -2.5 33.8 - 72 LYS 72 G A - 182.2 - 179.7 - - - - - - 178.5 -1.7 34.9 - 73 ASP 73 G A - 179.2 - - - - - - - - 180.4 -.6 34.5 - +* +* 74 TYR 74 G A - - -66.6 - - - - - - - 179.2 -1.6 34.0 - 75 ARG 75 g B - - -80.2 - - - - - - - 179.3 -1.3 32.5 - 76 SER 76 t B - - -59.9 - - - - - - - 176.6 - 35.5 - 77 PRO 77 T - - - - - -57.3 - - - - - 185.1 - 38.3 - * * 78 VAL 78 T l 81.5 - - - - - - - - - 180.5 - 30.0 - * * * 79 SER 79 T l - - -60.3 - - - - - - - 176.4 - 31.7 - 80 ASN 80 t B - 182.7 - - - - - - - - 189.4 -1.3 32.4 - +* * +* 81 LEU 81 B - - -54.7 180.1 - - - - - - 179.5 - 35.3 - 82 ALA 82 S b - - - - - - - - - - 179.2 - 33.4 - 83 GLY 83 - - - - - - - - - - - 183.0 -.7 - - +* +* 84 ALA 84 e B - - - - - - - - - - 173.9 - 34.6 - * * 85 VAL 85 E B - 181.3 - - - - - - - - 184.0 - 34.7 - 86 THR 86 E B - - -56.2 - - - - - - - 177.1 -3.0 34.4 - * * 87 THR 87 E B - - -62.9 - - - - - - - 176.9 - 33.4 - 88 MET 88 E B - 175.1 - - - - - - - - 179.4 -3.3 34.2 - +* +* 89 HIS 89 E B - - -63.1 - - - - - - - 185.1 -3.2 33.6 - +* +* 90 VAL 90 E B - 187.7 - - - - - - - - 182.4 -2.8 34.3 - * * 91 ILE 91 E B - - -64.6 - - - - - - - 181.5 -1.2 34.5 - * * 92 ILE 92 E B - - -67.2 - - - - - - - 176.8 -.6 34.1 - +* +* 93 GLN 93 e B - - -64.5 176.4 - - - - - - 183.6 -1.1 33.7 - * * Residue-by-residue listing for refined_1 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 94 ALA 94 B - - - - - - - - - - 177.6 -.5 34.1 - +* +* 95 PRO 95 - - - - - -73.0 - - - - - 178.9 - 39.3 - +* +* 96 VAL 96 S A 63.6 - - - - - - - - - 178.1 - 33.9 - 97 THR 97 b - - -50.0 - - - - - - - 175.3 - 35.0 - * * 98 GLU 98 B 56.3 - - - - - - - - - 183.1 -.7 30.7 - +* +* 99 LYS 99 B - - -58.2 180.5 - - - - - - 185.3 -.8 32.7 - +* +* 100 GLU 100 B - - -53.0 179.0 - - - - - - 178.6 - 35.6 - 101 LYS 101 - - 185.9 - 186.3 - - - - - - - -.8 34.0 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * ** +** ** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.5 185.5 -61.3 177.1 -68.5 -68.1 -34.2 - - - 179.8 -1.8 34.3 Standard deviations: 7.7 7.0 7.9 4.4 6.3 8.8 10.9 - - - 3.8 .9 2.1 Numbers of values: 18 23 41 25 6 11 11 0 0 0 100 59 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_1 Page 5 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLU 1 - 1.229 1.511 1.552 1.463 - 116.57 120.50 108.15 109.08 112.66 122.90 * * * * 2 ALA 2 1.316 1.229 1.505 1.515 1.456 122.16 113.23 122.58 111.94 108.89 111.26 124.11 * * * 3 GLU 3 1.278 1.247 1.510 1.516 1.417 124.09 113.92 121.94 111.47 109.26 112.47 124.06 +*** ** * * * +*** 4 VAL 4 1.288 1.240 1.525 1.599 1.445 125.30 119.85 118.63 109.21 102.45 109.63 121.49 +** ** +* +* * *** * *** 5 HIS 5 1.306 1.232 1.524 1.533 1.434 118.49 115.23 121.01 111.11 105.10 112.90 123.62 +* * +* ** * ** 6 ASN 6 1.306 1.240 1.501 1.539 1.451 122.97 113.13 122.30 111.08 115.41 112.17 124.56 +* * +* +* +* 7 GLN 7 1.296 1.245 1.508 1.526 1.416 126.28 119.06 119.43 110.04 104.14 107.29 121.49 ** ** +** * +** +* +** 8 LEU 8 1.290 1.230 1.508 1.548 1.422 117.19 116.25 120.85 112.81 110.55 115.39 122.90 +** +* +** * +** +** 9 GLU 9 1.310 1.232 1.497 1.549 1.425 120.15 115.17 121.45 109.90 109.44 115.03 123.38 * * +* +** +** 10 ILE 10 1.287 1.241 1.515 1.566 1.429 122.54 116.36 120.54 109.71 109.85 110.37 123.06 *** +* *** 11 LYS 11 1.309 1.238 1.513 1.566 1.429 121.03 116.36 120.43 114.46 109.60 113.24 123.20 * +* +* ** +* ** Residue-by-residue listing for refined_1 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 PHE 12 1.297 1.223 1.524 1.532 1.447 121.91 116.77 120.34 110.68 110.06 109.21 122.88 ** ** 13 ARG 13 1.311 1.223 1.527 1.544 1.450 122.76 116.53 120.46 109.74 110.66 109.32 123.01 * * 14 LEU 14 1.310 1.236 1.504 1.536 1.452 122.70 115.31 120.77 108.39 111.20 111.18 123.86 * * * 15 THR 15 1.321 1.224 1.546 1.561 1.456 123.19 115.00 121.89 110.58 110.12 109.89 123.11 * * 16 ASP 16 1.319 1.233 1.523 1.532 1.462 123.56 116.64 120.71 108.99 111.42 110.48 122.65 * * 17 GLY 17 1.319 1.237 1.515 - 1.447 120.51 116.61 120.63 - 112.94 - 122.77 18 SER 18 1.311 1.224 1.523 1.535 1.450 121.72 117.65 120.02 109.75 108.79 109.27 122.33 * * 19 ASP 19 1.307 1.231 1.511 1.535 1.432 120.62 114.51 121.47 111.34 112.77 112.14 124.02 +* * +* 20 ILE 20 1.306 1.234 1.529 1.567 1.450 124.96 116.57 119.57 109.50 108.29 110.07 123.78 +* +* * +* 21 GLY 21 1.337 1.241 1.528 - 1.471 123.63 117.29 120.40 - 114.29 - 122.31 * +* +* 22 PRO 22 1.347 1.243 1.525 1.526 1.466 123.46 114.84 121.70 109.91 114.61 103.57 123.46 * * * * 23 LYS 23 1.307 1.216 1.487 1.535 1.458 123.59 117.20 119.48 108.07 108.34 113.17 123.29 +* +* * * * +* +* 24 ALA 24 1.298 1.247 1.509 1.523 1.450 120.58 116.27 120.61 110.50 110.25 110.56 123.11 ** ** 25 PHE 25 1.311 1.225 1.510 1.535 1.434 121.47 117.99 120.40 107.41 109.21 110.92 121.53 * * * * 26 PRO 26 1.314 1.230 1.529 1.529 1.458 122.15 117.98 119.84 108.72 109.59 103.57 122.17 +* +* 27 ASP 27 1.326 1.211 1.530 1.535 1.476 120.79 116.01 121.32 110.25 110.27 112.32 122.62 * * * 28 ALA 28 1.316 1.231 1.537 1.517 1.454 122.28 116.55 120.94 110.34 110.87 110.28 122.51 29 THR 29 1.318 1.238 1.526 1.543 1.451 121.83 116.49 120.64 108.60 109.56 110.98 122.84 30 THR 30 1.304 1.245 1.526 1.541 1.432 121.57 116.98 120.24 110.03 109.40 110.32 122.78 +* * +* 31 VAL 31 1.321 1.228 1.526 1.549 1.456 121.82 116.17 121.00 110.43 109.99 111.90 122.82 32 SER 32 1.320 1.218 1.532 1.525 1.434 121.60 117.05 120.24 111.90 111.21 109.65 122.56 * * 33 ALA 33 1.329 1.239 1.524 1.518 1.464 121.62 115.73 121.04 110.83 110.60 110.71 123.23 34 LEU 34 1.318 1.230 1.531 1.532 1.418 123.35 116.24 121.05 111.95 109.70 107.72 122.68 ** +* ** 35 LYS 35 1.314 1.204 1.520 1.514 1.445 121.26 117.38 120.38 110.75 110.20 111.20 122.24 * * * 36 GLU 36 1.314 1.228 1.529 1.518 1.462 120.98 116.32 120.91 110.97 111.07 111.37 122.75 * * 37 THR 37 1.319 1.232 1.546 1.544 1.435 121.42 117.65 120.16 110.90 110.37 111.58 122.15 * * * 38 VAL 38 1.349 1.205 1.515 1.586 1.465 119.81 115.55 120.63 110.61 108.92 114.87 123.77 * * +* * +* +* 39 ILE 39 1.331 1.222 1.528 1.567 1.472 123.15 115.84 121.29 109.03 110.00 111.71 122.85 40 SER 40 1.316 1.226 1.537 1.530 1.450 122.23 116.20 120.88 110.72 111.22 109.85 122.90 41 GLU 41 1.318 1.234 1.528 1.523 1.440 122.80 115.66 121.03 109.64 110.83 108.43 123.31 * * 42 TRP 42 1.304 1.236 1.518 1.536 1.433 122.60 117.58 120.61 109.75 109.54 108.76 121.77 +* * * +* Residue-by-residue listing for refined_1 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 43 PRO 43 1.327 1.217 1.520 1.542 1.440 121.85 117.04 120.63 109.81 109.55 104.07 122.32 +* +* 44 ARG 44 1.313 1.230 1.528 1.526 1.470 121.39 114.56 121.88 111.16 109.35 110.68 123.55 * * 45 GLU 45 1.324 1.239 1.535 1.526 1.450 124.30 116.92 119.85 107.92 111.21 109.35 123.21 * * * 46 LYS 46 1.345 1.237 1.508 1.535 1.454 121.89 115.62 120.97 109.55 109.30 111.56 123.38 * * 47 GLU 47 1.298 1.233 1.502 1.510 1.417 121.96 115.55 120.29 111.54 109.97 110.54 124.15 ** * * ** ** 48 ASN 48 1.326 1.236 1.523 1.554 1.476 123.84 115.52 121.75 110.66 109.26 112.31 122.72 * * * * 49 GLY 49 1.317 1.244 1.504 - 1.419 121.05 117.43 120.21 - 111.88 - 122.35 ** ** 50 PRO 50 1.331 1.236 1.518 1.534 1.459 123.32 115.82 120.90 109.22 111.88 103.72 123.27 51 LYS 51 1.309 1.224 1.521 1.529 1.440 122.36 115.69 121.22 108.09 109.30 109.42 123.09 * * * 52 THR 52 1.325 1.247 1.547 1.542 1.439 122.24 114.06 121.79 109.69 113.80 110.24 124.15 * * * * 53 VAL 53 1.334 1.234 1.547 1.577 1.474 126.94 117.30 120.51 109.85 113.93 109.59 122.16 * * +** * +** 54 LYS 54 1.319 1.232 1.530 1.540 1.458 121.29 116.59 120.57 109.94 112.04 111.05 122.83 55 GLU 55 1.310 1.234 1.536 1.519 1.462 121.96 116.16 121.10 110.44 111.91 108.31 122.73 * * * 56 VAL 56 1.308 1.227 1.526 1.565 1.455 121.88 116.80 120.43 108.33 110.32 110.74 122.74 * * 57 LYS 57 1.311 1.233 1.518 1.542 1.454 122.07 116.73 120.28 111.40 109.30 112.28 122.98 * * * 58 LEU 58 1.319 1.234 1.535 1.569 1.444 121.38 116.51 120.57 110.62 107.66 108.62 122.91 +* * * +* 59 ILE 59 1.312 1.222 1.513 1.567 1.448 122.25 116.73 120.62 109.77 108.67 111.71 122.65 * * * 60 SER 60 1.297 1.238 1.505 1.532 1.432 121.39 116.13 119.70 111.05 108.50 109.76 124.14 ** * ** 61 ALA 61 1.336 1.227 1.508 1.539 1.467 124.11 114.23 121.57 112.18 111.07 112.45 124.16 * * * * 62 GLY 62 1.261 1.233 1.512 - 1.438 123.29 116.24 120.88 - 110.83 - 122.87 *4.9* +* *4.9* 63 LYS 63 1.323 1.235 1.537 1.556 1.444 121.76 116.76 120.17 111.75 107.49 108.75 123.04 * * * * 64 VAL 64 1.323 1.236 1.541 1.572 1.463 122.20 115.90 121.36 110.62 111.73 111.71 122.74 * * 65 LEU 65 1.308 1.228 1.510 1.555 1.426 123.68 117.87 119.81 111.78 108.82 111.67 122.30 * * +* * +* 66 GLU 66 1.315 1.230 1.554 1.551 1.439 119.62 115.11 120.93 113.58 111.82 110.36 123.93 * * * * * +* +* 67 ASN 67 1.322 1.231 1.537 1.540 1.476 127.69 117.19 120.05 108.72 114.69 106.61 122.75 *** * ** *** 68 SER 68 1.315 1.238 1.548 1.520 1.461 122.30 118.73 119.88 111.84 116.02 109.82 121.38 * * * +* * +* 69 LYS 69 1.317 1.227 1.518 1.516 1.426 119.69 114.83 121.48 111.68 113.65 113.27 123.66 +* * +* +* 70 THR 70 1.302 1.231 1.551 1.544 1.438 124.18 118.12 119.75 109.47 107.63 107.64 122.13 +* * * * * ** ** 71 VAL 71 1.329 1.235 1.540 1.563 1.476 121.41 114.34 121.96 110.26 109.14 111.63 123.68 Residue-by-residue listing for refined_1 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.324 1.226 1.533 1.535 1.458 125.33 115.68 120.98 110.98 110.49 108.79 123.33 ** * ** 73 ASP 73 1.331 1.230 1.538 1.545 1.472 123.46 116.23 120.99 110.76 110.74 109.47 122.70 74 TYR 74 1.323 1.230 1.520 1.521 1.446 122.24 117.18 120.47 109.82 112.31 110.54 122.35 75 ARG 75 1.311 1.232 1.510 1.520 1.419 121.44 115.17 121.06 111.18 112.01 111.64 123.77 * ** ** 76 SER 76 1.308 1.251 1.532 1.525 1.434 123.30 116.96 120.24 110.23 111.43 108.45 122.79 +* * * +* 77 PRO 77 1.364 1.228 1.535 1.539 1.471 123.34 115.83 120.00 110.44 111.80 103.97 124.17 * +* +* 78 VAL 78 1.344 1.243 1.538 1.594 1.499 126.94 114.11 121.96 111.87 110.03 115.21 123.85 * ** ** +** * * ** +** 79 SER 79 1.326 1.246 1.523 1.536 1.447 125.23 115.85 121.31 111.87 112.54 111.73 122.77 +* +* 80 ASN 80 1.323 1.242 1.526 1.539 1.453 120.91 115.79 120.46 112.41 108.79 111.59 123.74 * * 81 LEU 81 1.317 1.249 1.525 1.494 1.415 124.28 114.41 122.32 109.87 114.17 108.13 123.26 +* ** * * * ** 82 ALA 82 1.299 1.222 1.511 1.522 1.412 123.26 115.17 121.38 111.38 109.01 111.27 123.31 ** ** ** 83 GLY 83 1.294 1.224 1.489 - 1.434 121.46 115.15 121.43 - 109.66 - 123.39 ** * * ** 84 ALA 84 1.303 1.227 1.506 1.518 1.432 121.85 116.09 120.64 110.02 110.82 110.14 123.27 +* * +* 85 VAL 85 1.296 1.227 1.512 1.550 1.438 122.14 117.12 120.22 109.70 106.18 112.00 122.62 ** * +* ** 86 THR 86 1.292 1.239 1.524 1.546 1.435 121.01 115.96 121.08 110.44 111.24 110.15 122.95 +** * +** 87 THR 87 1.301 1.243 1.521 1.546 1.417 121.53 115.08 121.70 110.65 110.41 111.66 123.20 +* ** ** 88 MET 88 1.292 1.213 1.509 1.556 1.421 122.82 116.79 120.18 112.88 107.46 109.45 122.95 +** * +* * * +** 89 HIS 89 1.295 1.240 1.503 1.536 1.437 121.94 116.28 120.32 111.17 108.32 111.41 123.40 ** * * * ** 90 VAL 90 1.313 1.244 1.485 1.557 1.438 120.92 113.57 121.89 108.99 109.03 112.74 124.53 * +* * * +* 91 ILE 91 1.281 1.247 1.505 1.540 1.404 123.44 114.50 121.58 111.60 109.42 109.56 123.90 *** +** * * *** 92 ILE 92 1.293 1.238 1.510 1.582 1.420 123.08 115.74 120.92 109.74 109.05 112.45 123.29 +** +* ** +** 93 GLN 93 1.299 1.238 1.503 1.528 1.432 122.09 115.45 120.76 111.93 108.54 110.47 123.76 ** * * ** 94 ALA 94 1.312 1.248 1.521 1.528 1.445 122.63 117.01 120.64 110.55 111.40 110.12 122.35 * * 95 PRO 95 1.346 1.236 1.521 1.539 1.457 122.76 115.92 121.02 110.26 111.10 103.05 123.06 96 VAL 96 1.311 1.233 1.562 1.564 1.474 122.83 116.26 121.83 110.63 111.18 110.43 121.91 * +* +* 97 THR 97 1.308 1.236 1.538 1.547 1.421 121.54 116.61 120.56 109.51 109.49 110.76 122.63 * +* +* 98 GLU 98 1.315 1.248 1.523 1.564 1.444 121.33 115.08 121.31 112.52 109.88 113.70 123.55 +* * +* +* 99 LYS 99 1.319 1.236 1.520 1.529 1.436 123.06 115.54 121.19 112.08 111.51 110.54 123.27 * * * 100 GLU 100 1.302 1.237 1.525 1.529 1.439 122.47 117.04 120.54 109.95 110.55 108.85 122.42 +* * +* Residue-by-residue listing for refined_1 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 101 LYS 101 1.310 - 1.525 1.536 1.445 121.08 - - 110.61 108.76 111.12 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.9* * +* ** +** *** +* * ** *** +** +* *4.9* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 10 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 94 1.261 1.349 1.312 .014 *4.9* * * C-N (Pro) 1.341 .016 6 1.314 1.364 1.338 .016 +* * C-O C-O 1.231 .020 100 1.204 1.251 1.233 .009 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.485 1.562 1.523 .014 +* +* CH2G*-C (Gly) 1.516 .018 5 1.489 1.528 1.510 .013 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.515 1.539 1.523 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.540 1.599 1.561 .017 ** CH1E-CH2E (the rest) 1.530 .020 62 1.494 1.569 1.535 .014 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.404 1.499 1.445 .018 +** ** NH1-CH2G* (Gly) 1.451 .016 5 1.419 1.471 1.442 .017 ** * N-CH1E (Pro) 1.466 .015 6 1.440 1.471 1.459 .010 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 11 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 89 113.13 119.85 116.11 1.21 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.15 117.43 116.54 .82 CH1E-C-N (Pro) 116.9 1.5 6 114.84 117.98 116.24 1.01 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.38 124.56 123.03 .67 * O-C-N (Pro) 122.0 1.4 6 122.17 124.17 123.07 .68 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.19 127.69 122.39 1.69 +** *** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.51 123.63 121.99 1.24 +* C-N-CH1E (Pro) 122.6 5.0 6 121.85 123.46 122.81 .62 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.63 122.58 120.81 .71 * * CH2G*-C-O (Gly) 120.8 2.1 5 120.21 121.43 120.71 .43 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.02 112.18 110.97 .73 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.33 111.87 109.99 .83 * CH2E-CH1E-C (the rest) 110.1 1.9 62 107.41 114.46 110.61 1.40 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 102.45 116.02 110.11 2.10 *** +* NH1-CH2G*-C (Gly) 112.5 2.9 5 109.66 114.29 111.92 1.61 N-CH1E-C (Pro) 111.8 2.5 6 109.55 114.61 111.42 1.71 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 110.12 112.45 110.85 .74 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 107.64 115.21 111.14 1.57 ** ** N-CH1E-CH2E (Pro) 103.0 1.1 6 103.05 104.07 103.66 .33 NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.61 115.39 110.65 1.86 ** +** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_1 Page 12 ---------------------------------------- R A M A C H A N D R A N P L O T S T A T I S T I C S Residues in most favoured regions [A,B,L] 77 87.5% Residues in additional allowed regions [a,b,l,p] 10 11.4% 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 87.5 83.8 10.0 .4 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 2.1 3.1 1.6 -.6 Inside e. H-bond energy st dev 59 .9 .8 .2 .6 Inside f. Overall G-factor 101 -.1 -.4 .3 1.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 7.7 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 23 7.0 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 41 7.9 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 82 8.7 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 25 4.4 20.4 5.0 -3.2 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for refined_1 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.63 Chi1-chi2 distribution -.24 Chi1 only -.02 Chi3 & chi4 .30 Omega -.03 ------ -.21 ===== Main-chain covalent forces:- Main-chain bond lengths -.02 Main-chain bond angles .31 ------ .18 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.