Residue-by-residue listing for refined_2 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 - - 190.0 - - - - - - - - 180.7 - 34.8 - 2 ALA 2 b - - - - - - - - - - 174.3 - 35.1 - 3 GLU 3 b - - -59.3 177.3 - - - - - - 184.8 - 33.6 - 4 VAL 4 B - 185.0 - - - - - - - - 174.6 -1.8 34.4 - 5 HIS 5 S a - - -64.1 - - - - - - - 174.4 -.6 33.5 - +* +* 6 ASN 6 S b 59.5 - - - - - - - - - 174.8 - 30.5 - 7 GLN 7 B 47.1 - - 183.6 - - - - - - 191.6 - 31.4 - * +* +* 8 LEU 8 E B - - -67.9 - - - - - - - 181.5 -1.6 33.0 - 9 GLU 9 E B - - -55.7 181.4 - - - - - - 182.1 - 34.0 - 10 ILE 10 E B - - -55.6 178.7 - - - - - - 173.7 -2.7 35.2 - * * 11 LYS 11 E B 61.7 - - 174.8 - - - - - - 183.6 -3.1 32.9 - * * 12 PHE 12 E B - - -58.4 - - - - - - - 176.7 -.7 35.4 - +* +* 13 ARG 13 E B - 181.8 - 175.1 - - - - - - 183.9 -3.0 32.8 - * * 14 LEU 14 E B - - -60.0 - - - - - - - 181.7 -2.7 34.2 - 15 THR 15 e A - - -44.2 - - - - - - - 181.3 -.6 35.5 - +* +* +* 16 ASP 16 T A - - -67.0 - - - - - - - 179.1 - 34.2 - 17 GLY 17 t - - - - - - - - - - - 178.0 -1.5 - - 18 SER 18 e B - - -51.8 - - - - - - - 179.9 - 36.4 - 19 ASP 19 E B 64.7 - - - - - - - - - 178.6 - 34.0 - 20 ILE 20 E B - - -60.4 178.2 - - - - - - 182.7 -3.3 34.8 - +* +* Residue-by-residue listing for refined_2 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 - - - - - - - - - - - 181.2 - - - 22 PRO 22 E - - - - - -66.1 - - - - - 178.7 - 37.8 - * * 23 LYS 23 E B - 195.6 - - - - - - - - 182.6 -2.1 35.2 - 24 ALA 24 E B - - - - - - - - - - 180.1 - 32.4 - 25 PHE 25 E B - - -54.5 - - - - - - - 170.0 -3.6 37.8 - +* ** * ** 26 PRO 26 t - - - - - -65.1 - - - - - 180.2 - 40.1 - +* +* 27 ASP 27 T A 64.5 - - - - - - - - - 175.1 - 31.2 - 28 ALA 28 T A - - - - - - - - - - 181.2 - 33.8 - 29 THR 29 t B - 194.5 - - - - - - - - 175.7 -2.2 32.9 - 30 THR 30 h B 54.8 - - - - - - - - - 176.1 - 35.0 - 31 VAL 31 H A - 180.6 - - - -66.0 -26.1 - - - 175.6 -3.4 33.7 - * +* +* 32 SER 32 H A - 181.9 - - - -59.8 -50.6 - - - 180.2 -1.2 35.0 - * * 33 ALA 33 H A - - - - - -66.4 -32.4 - - - 177.8 - 33.6 - 34 LEU 34 H A - 169.8 - - - -62.3 -50.5 - - - 181.0 -1.9 35.7 - 35 LYS 35 H A - 190.9 - 185.6 - -72.0 -42.5 - - - 177.5 -2.9 34.6 - * * 36 GLU 36 H A - - -72.9 - - -56.7 -30.6 - - - 175.2 -3.3 33.4 - +* +* 37 THR 37 H A - - -60.4 - - -65.0 -44.2 - - - 180.6 -1.6 32.9 - 38 VAL 38 H A 75.3 - - - - -68.7 -36.0 - - - 178.0 -1.3 32.3 - * * 39 ILE 39 H A - - -52.9 - - -63.3 -38.1 - - - 179.6 -2.6 34.1 - 40 SER 40 H A - - -57.2 - - -72.9 -39.8 - - - 179.0 -2.0 34.2 - 41 GLU 41 H A - - -69.3 - - -66.0 -34.7 - - - 181.1 -2.5 34.8 - 42 TRP 42 h B - 198.2 - - - - - - - - 184.2 -2.3 35.5 - 43 PRO 43 t - - - - - -54.9 - - - - - 175.5 - 38.9 - * * 44 ARG 44 T A 57.1 - - - - - - - - - 178.1 - 31.9 - 45 GLU 45 T A - 177.5 - 178.9 - - - - - - 181.9 - 35.6 - 46 LYS 46 t B - 185.7 - - - - - - - - 173.6 -.6 35.8 - * +* +* 47 GLU 47 B - - -58.9 - - - - - - - 186.7 - 34.2 - * * 48 ASN 48 S b - - -77.2 - - - - - - - 166.4 - 27.6 - ** +* ** 49 GLY 49 S - - - - - - - - - - - 162.4 -2.4 - - *** *** 50 PRO 50 S - - - - - -61.2 - - - - - 184.4 - 39.7 - +* +* 51 LYS 51 a - 187.8 - 180.4 - - - - - - 179.7 -1.3 34.6 - 52 THR 52 t B 57.7 - - - - - - - - - 176.2 - 34.9 - 53 VAL 53 T A 61.8 - - - - - - - - - 179.4 - 34.2 - 54 LYS 54 T A - 177.5 - 185.1 - - - - - - 185.4 - 35.7 - 55 GLU 55 T A - - -58.1 - - - - - - - 181.6 - 33.3 - 56 VAL 56 t B - 179.0 - - - - - - - - 175.3 -1.9 35.0 - 57 LYS 57 E B - - -74.0 179.8 - - - - - - 183.7 -1.7 32.2 - 58 LEU 58 E B - 199.9 - - - - - - - - 183.4 - 35.4 - 59 ILE 59 E B - - -66.0 184.2 - - - - - - 176.3 -3.4 33.5 - +* +* 60 SER 60 E B - 184.1 - - - - - - - - 180.2 -2.5 34.6 - 61 ALA 61 T l - - - - - - - - - - 180.2 - 33.0 - 62 GLY 62 T - - - - - - - - - - - 181.6 - - - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 63 LYS 63 E B - 186.4 - 188.3 - - - - - - 179.5 -1.1 36.2 - * * 64 VAL 64 E B - 182.6 - - - - - - - - 176.4 - 34.9 - 65 LEU 65 e B 42.5 - - 167.3 - - - - - - 185.9 -2.5 28.2 - * * +* +* 66 GLU 66 t B - - -60.7 170.6 - - - - - - 182.3 -.8 35.0 - +* +* 67 ASN 67 T A 61.8 - - - - - - - - - 180.8 - 34.0 - 68 SER 68 T A 50.0 - - - - - - - - - 179.5 - 33.0 - 69 LYS 69 t B - - -63.5 175.7 - - - - - - 174.4 -2.2 35.5 - 70 THR 70 h B 54.7 - - - - - - - - - 178.6 - 35.6 - 71 VAL 71 H A - 181.4 - - - -65.3 -35.1 - - - 174.0 -2.7 31.5 - * * 72 LYS 72 H A - - -94.2 - - -55.6 -39.0 - - - 181.0 -1.1 33.5 - +* * +* 73 ASP 73 H A - 185.9 - - - -75.2 -24.5 - - - 180.9 - 34.6 - * * 74 TYR 74 H A - 190.5 - - - -85.6 -20.3 - - - 179.2 -1.3 36.4 - +* +* * +* 75 ARG 75 h B - - -75.3 - - - - - - - 170.3 -1.3 38.1 - +* * +* 76 SER 76 B - - -62.3 - - - - - - - 179.1 - 35.8 - 77 PRO 77 - - - - - -63.1 - - - - - 180.9 - 38.4 - * * 78 VAL 78 a 63.5 - - - - - - - - - 179.8 - 33.6 - 79 SER 79 S L - 182.9 - - - - - - - - 182.0 - 33.4 - 80 ASN 80 B - 183.2 - - - - - - - - 178.4 - 34.9 - 81 LEU 81 b - - -70.4 - - - - - - - 180.7 - 36.1 - 82 ALA 82 b - - - - - - - - - - 179.3 - 33.9 - 83 GLY 83 - - - - - - - - - - - 176.9 - - - 84 ALA 84 S B - - - - - - - - - - 178.2 -1.0 34.6 - * * 85 VAL 85 B - 183.5 - - - - - - - - 183.0 - 34.4 - 86 THR 86 E B - - -52.2 - - - - - - - 179.5 -2.8 35.1 - * * 87 THR 87 E B - - -53.1 - - - - - - - 180.2 -.7 34.7 - +* +* 88 MET 88 E B - - -64.7 181.8 - - - - - - 184.7 -2.7 32.4 - 89 HIS 89 E B - - -62.7 - - - - - - - 176.5 -3.0 33.7 - * * 90 VAL 90 E B - 182.0 - - - - - - - - 182.6 -3.3 34.5 - +* +* 91 ILE 91 E B - - -63.1 - - - - - - - 182.8 -3.1 34.9 - * * 92 ILE 92 B - - -54.7 - - - - - - - 172.4 -.6 35.4 - * +* +* 93 GLN 93 B - - -66.5 - - - - - - - 179.5 -1.1 34.4 - * * 94 ALA 94 B - - - - - - - - - - 175.8 -.8 34.3 - +* +* 95 PRO 95 - - - - - -60.1 - - - - - 179.7 - 39.2 - +* +* 96 VAL 96 b 56.4 - - - - - - - - - 186.6 - 32.1 - * * 97 THR 97 S b - - -46.6 - - - - - - - 177.8 - 32.3 - * * 98 GLU 98 S b - 183.4 - - - - - - - - 185.1 -2.1 34.0 - Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 LYS 99 b - 181.6 - 178.1 - - - - - - 177.1 - 32.0 - 100 GLU 100 B - - -66.6 - - - - - - - 178.7 -1.4 35.4 - 101 LYS 101 - - - -62.4 182.3 - - - - - - - - 32.8 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* +* +* *** ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.3 185.1 -62.2 179.4 -61.7 -66.7 -36.3 - - - 179.2 -2.0 34.4 Standard deviations: 7.8 6.6 9.2 5.1 4.0 7.6 8.8 - - - 4.2 .9 2.0 Numbers of values: 16 28 38 20 6 15 15 0 0 0 100 52 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_2 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 - 1.238 1.515 1.554 1.456 - 116.02 120.40 111.84 107.42 109.31 123.54 * * * 2 ALA 2 1.320 1.244 1.497 1.528 1.443 123.43 116.27 120.28 109.01 108.88 111.07 123.45 * * 3 GLU 3 1.307 1.236 1.516 1.528 1.416 122.07 115.20 121.37 111.25 108.14 111.31 123.27 +* ** * ** 4 VAL 4 1.304 1.230 1.495 1.540 1.426 122.24 113.64 122.18 108.46 110.85 112.36 124.17 +* * +* * +* 5 HIS 5 1.263 1.224 1.499 1.543 1.436 124.23 115.39 121.21 111.21 106.49 112.20 123.37 *4.7* * * * +* * *4.7* 6 ASN 6 1.319 1.233 1.527 1.561 1.440 122.08 115.32 121.91 112.44 111.09 113.57 122.60 +* * +* +* 7 GLN 7 1.307 1.228 1.500 1.527 1.404 123.67 116.79 119.70 114.24 107.73 111.97 123.50 +* * +** * ** * +** 8 LEU 8 1.295 1.224 1.506 1.542 1.450 121.32 115.82 121.25 110.21 112.49 111.74 122.93 ** ** 9 GLU 9 1.302 1.252 1.503 1.510 1.425 121.46 114.33 121.85 109.96 109.75 111.44 123.82 +* * * +* +* 10 ILE 10 1.286 1.235 1.500 1.566 1.428 122.88 115.67 120.76 108.64 109.11 111.74 123.52 *** * +* *** 11 LYS 11 1.290 1.247 1.512 1.534 1.428 121.83 116.11 120.72 110.76 108.36 112.80 123.17 +** +* * * +** Residue-by-residue listing for refined_2 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 1.291 1.223 1.504 1.525 1.437 121.40 116.91 120.30 109.13 110.09 110.16 122.79 +** * * +** 13 ARG 13 1.298 1.225 1.512 1.525 1.434 120.92 115.69 120.83 111.59 109.60 111.56 123.49 ** * ** 14 LEU 14 1.305 1.240 1.512 1.545 1.444 123.33 115.20 121.46 109.66 111.18 111.24 123.33 +* +* 15 THR 15 1.311 1.222 1.543 1.514 1.435 122.96 115.89 121.22 109.44 111.07 109.11 122.83 * * * * 16 ASP 16 1.327 1.230 1.508 1.530 1.467 122.72 116.95 120.28 109.10 112.43 111.02 122.76 17 GLY 17 1.316 1.226 1.507 - 1.453 120.18 115.54 121.09 - 111.95 - 123.36 18 SER 18 1.300 1.230 1.524 1.522 1.433 122.74 118.51 119.46 110.27 107.27 108.07 122.01 ** * * * * ** 19 ASP 19 1.309 1.235 1.511 1.525 1.431 120.61 115.15 121.08 110.02 111.22 110.91 123.77 * * * 20 ILE 20 1.301 1.236 1.529 1.564 1.442 124.04 116.46 119.78 110.43 108.04 110.70 123.74 ** * * ** 21 GLY 21 1.328 1.243 1.529 - 1.457 122.58 117.05 120.52 - 114.25 - 122.43 * * 22 PRO 22 1.346 1.245 1.526 1.533 1.459 123.43 115.02 121.52 110.40 113.61 104.47 123.46 * * * * 23 LYS 23 1.303 1.223 1.531 1.574 1.441 123.37 119.14 118.78 113.39 104.64 108.01 122.04 +* ** * * +* ** * ** 24 ALA 24 1.311 1.229 1.515 1.531 1.462 119.91 115.95 120.73 111.36 111.20 111.64 123.29 * * 25 PHE 25 1.307 1.233 1.506 1.546 1.451 123.56 118.92 119.79 104.89 107.64 111.43 121.27 +* * * +** * * +** 26 PRO 26 1.317 1.216 1.514 1.532 1.449 121.08 117.69 120.12 108.89 108.30 103.64 122.19 +* * * +* 27 ASP 27 1.300 1.193 1.523 1.530 1.460 121.17 116.12 121.94 112.37 110.86 112.43 121.94 ** +* * * ** 28 ALA 28 1.291 1.232 1.549 1.519 1.456 121.48 117.02 120.36 110.31 111.55 110.40 122.61 +** * +** 29 THR 29 1.331 1.250 1.532 1.576 1.465 122.06 116.22 120.79 109.73 110.71 113.12 122.88 * * 30 THR 30 1.319 1.248 1.526 1.540 1.434 121.61 116.39 120.79 108.80 110.10 111.12 122.82 * * 31 VAL 31 1.317 1.234 1.529 1.548 1.448 121.57 115.43 121.42 110.61 108.58 111.71 123.14 32 SER 32 1.329 1.217 1.529 1.537 1.437 121.88 116.95 120.02 110.33 109.31 109.80 122.85 * * 33 ALA 33 1.339 1.230 1.521 1.519 1.462 121.85 115.88 120.82 110.67 110.80 110.67 123.30 34 LEU 34 1.320 1.235 1.532 1.533 1.423 123.57 115.93 121.14 111.64 110.07 107.25 122.88 +* * +* +* 35 LYS 35 1.315 1.201 1.524 1.517 1.444 121.65 116.94 120.61 110.16 109.74 110.10 122.45 * * * 36 GLU 36 1.316 1.230 1.526 1.521 1.469 121.90 116.75 120.51 110.87 111.38 110.46 122.73 37 THR 37 1.324 1.228 1.542 1.554 1.439 121.01 117.39 120.09 111.02 110.11 112.00 122.40 38 VAL 38 1.345 1.224 1.523 1.585 1.466 120.56 115.28 121.17 110.44 109.33 113.88 123.52 * +* * +* 39 ILE 39 1.324 1.228 1.538 1.575 1.463 122.41 116.26 121.02 109.47 109.50 112.16 122.71 * * 40 SER 40 1.328 1.234 1.536 1.532 1.451 121.77 116.53 120.43 110.32 110.94 110.32 123.03 41 GLU 41 1.335 1.238 1.508 1.518 1.442 123.06 115.50 120.54 109.81 111.79 109.66 123.95 42 TRP 42 1.314 1.236 1.526 1.522 1.437 123.02 117.39 120.07 110.83 108.55 108.65 122.52 * * * * 43 PRO 43 1.338 1.235 1.529 1.533 1.464 123.01 116.20 120.86 109.35 113.50 103.86 122.93 Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ARG 44 1.328 1.223 1.522 1.568 1.462 122.04 114.30 121.84 112.85 109.60 111.79 123.85 +* * +* 45 GLU 45 1.322 1.227 1.529 1.531 1.438 124.23 116.14 120.89 110.77 110.26 108.15 122.95 * * * * 46 LYS 46 1.322 1.238 1.520 1.546 1.443 121.91 116.63 120.04 109.09 108.98 110.10 123.27 47 GLU 47 1.323 1.252 1.525 1.546 1.449 122.48 116.16 120.94 109.41 108.65 112.18 122.90 * * 48 ASN 48 1.293 1.240 1.489 1.546 1.420 121.99 114.11 121.58 112.30 114.81 115.48 124.06 +** +* +* * * * +** +** 49 GLY 49 1.303 1.232 1.496 - 1.429 121.06 116.88 120.90 - 105.35 - 122.22 +* * * ** ** 50 PRO 50 1.332 1.237 1.527 1.526 1.449 122.38 115.83 121.05 109.83 109.18 103.05 123.01 * * * 51 LYS 51 1.299 1.229 1.521 1.534 1.434 121.54 116.34 120.63 111.46 110.17 108.95 123.03 ** * ** 52 THR 52 1.314 1.242 1.523 1.541 1.439 122.00 115.38 120.90 108.16 110.46 111.77 123.72 * * 53 VAL 53 1.319 1.232 1.552 1.569 1.460 124.42 115.96 121.34 110.73 110.48 110.27 122.70 * * +* +* 54 LYS 54 1.323 1.233 1.532 1.532 1.450 123.08 116.18 120.89 109.23 110.84 109.23 122.91 55 GLU 55 1.319 1.229 1.531 1.534 1.460 121.64 116.37 120.87 110.75 112.41 110.52 122.76 56 VAL 56 1.299 1.223 1.525 1.548 1.454 122.23 116.88 120.48 109.37 110.98 110.30 122.63 ** ** 57 LYS 57 1.313 1.234 1.515 1.520 1.442 122.37 116.38 120.61 111.92 110.70 111.66 123.00 * * 58 LEU 58 1.313 1.239 1.541 1.571 1.438 121.62 116.78 120.19 112.74 106.41 107.91 122.99 * ** * * +* +* ** 59 ILE 59 1.323 1.236 1.530 1.576 1.465 122.82 115.44 121.45 109.90 112.17 111.63 123.11 * * 60 SER 60 1.309 1.239 1.523 1.542 1.430 123.02 116.53 119.86 111.03 107.50 110.39 123.56 * * * * 61 ALA 61 1.338 1.236 1.540 1.535 1.477 123.65 116.03 121.02 111.21 111.25 110.78 122.91 * * * 62 GLY 62 1.331 1.241 1.518 - 1.454 121.11 116.17 121.03 - 112.30 - 122.79 63 LYS 63 1.313 1.235 1.515 1.531 1.438 122.21 117.18 119.90 109.69 107.91 109.04 122.91 * * * * 64 VAL 64 1.308 1.248 1.518 1.558 1.443 121.00 116.58 120.63 108.72 109.34 111.76 122.79 +* +* 65 LEU 65 1.307 1.230 1.488 1.550 1.409 120.76 113.77 121.86 113.92 110.49 115.60 124.33 +* +* +** * ** *** *** 66 GLU 66 1.289 1.230 1.506 1.502 1.427 124.29 114.87 121.21 111.36 112.20 107.76 123.90 +** * +* * +* +** 67 ASN 67 1.314 1.231 1.530 1.548 1.467 124.19 116.54 120.67 109.78 112.48 110.74 122.79 * * * 68 SER 68 1.309 1.230 1.535 1.525 1.434 122.23 116.77 120.89 112.42 112.75 109.29 122.34 * * * * 69 LYS 69 1.308 1.236 1.516 1.520 1.425 122.03 116.17 120.76 109.84 110.31 109.20 123.04 +* +* +* 70 THR 70 1.298 1.246 1.507 1.535 1.410 122.82 117.69 119.62 109.67 107.81 110.30 122.69 ** +** * +** 71 VAL 71 1.320 1.201 1.545 1.559 1.440 119.44 117.02 120.15 112.43 109.45 112.86 122.77 * * +* +* 72 LYS 72 1.346 1.224 1.529 1.538 1.480 122.89 117.07 120.24 108.90 112.65 111.97 122.69 * * * Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 ASP 73 1.329 1.234 1.521 1.541 1.480 121.76 114.58 121.94 109.95 109.87 110.42 123.47 * * 74 TYR 74 1.304 1.233 1.544 1.528 1.444 123.70 114.84 121.80 111.19 108.96 106.65 123.35 +* * ** ** 75 ARG 75 1.312 1.236 1.512 1.521 1.424 124.84 114.93 121.25 107.15 110.83 107.98 123.81 * +* +* +* * +* 76 SER 76 1.301 1.242 1.530 1.515 1.408 123.56 118.45 119.72 109.91 107.28 109.39 121.79 ** +** * * * +** 77 PRO 77 1.339 1.239 1.527 1.530 1.457 122.19 116.14 120.96 110.18 110.94 104.24 122.88 * * 78 VAL 78 1.304 1.235 1.535 1.564 1.458 121.81 115.07 121.68 111.28 110.35 110.70 123.24 +* +* 79 SER 79 1.321 1.243 1.540 1.558 1.468 123.76 115.53 121.78 111.96 110.14 110.17 122.61 * * * 80 ASN 80 1.308 1.235 1.516 1.544 1.451 122.06 116.21 120.48 109.82 109.55 110.42 123.30 +* +* 81 LEU 81 1.312 1.227 1.526 1.515 1.393 123.70 116.63 120.49 109.83 109.58 108.66 122.87 * *** * * *** 82 ALA 82 1.308 1.235 1.505 1.523 1.418 122.37 115.96 120.78 110.91 108.96 111.05 123.23 +* ** ** 83 GLY 83 1.303 1.232 1.510 - 1.449 121.89 115.65 121.06 - 112.31 - 123.23 +* +* 84 ALA 84 1.300 1.240 1.510 1.523 1.437 123.06 117.59 119.91 110.58 108.27 110.40 122.49 ** * * ** 85 VAL 85 1.303 1.242 1.512 1.553 1.442 120.25 116.47 120.85 109.42 107.53 112.36 122.67 +* * +* 86 THR 86 1.294 1.223 1.509 1.542 1.419 120.53 116.70 120.65 110.05 108.41 110.44 122.62 ** ** ** 87 THR 87 1.296 1.237 1.515 1.537 1.422 120.88 116.06 120.71 110.71 108.74 110.23 123.20 ** +* ** 88 MET 88 1.301 1.237 1.497 1.525 1.433 121.49 115.86 120.87 111.59 110.19 111.96 123.26 +* * * +* 89 HIS 89 1.298 1.229 1.496 1.536 1.437 121.55 115.17 121.32 109.97 111.11 111.56 123.51 ** * * ** 90 VAL 90 1.284 1.245 1.483 1.542 1.422 122.36 114.58 121.28 109.93 106.79 112.03 124.13 *** ** +* +* *** 91 ILE 91 1.271 1.245 1.494 1.530 1.408 122.89 114.76 121.44 111.07 108.93 109.69 123.79 **** * +** * **** 92 ILE 92 1.291 1.230 1.498 1.556 1.403 121.75 115.75 120.95 108.99 109.52 111.15 123.24 +** * +** +** 93 GLN 93 1.294 1.233 1.473 1.532 1.407 120.52 115.57 120.75 109.97 106.41 112.31 123.66 ** ** +** +* * +** 94 ALA 94 1.288 1.250 1.501 1.518 1.418 120.93 117.67 119.76 110.64 108.89 110.73 122.48 +** * ** +** 95 PRO 95 1.336 1.253 1.518 1.536 1.453 122.33 116.32 120.02 110.02 110.11 103.55 123.65 * * * 96 VAL 96 1.327 1.245 1.541 1.562 1.454 122.04 115.60 121.89 112.31 110.36 111.75 122.44 * * 97 THR 97 1.307 1.238 1.530 1.539 1.420 121.40 113.19 121.88 112.31 111.15 111.10 124.72 +* ** +* * * ** 98 GLU 98 1.319 1.235 1.512 1.544 1.447 126.84 116.19 120.73 110.55 105.48 112.25 122.93 +** ** * +** 99 LYS 99 1.306 1.236 1.525 1.533 1.426 121.80 115.09 121.14 112.11 112.74 111.07 123.74 +* +* * +* Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 GLU 100 1.315 1.243 1.517 1.534 1.445 123.48 116.57 120.67 109.29 109.72 110.10 122.76 * * 101 LYS 101 1.301 - 1.521 1.529 1.431 121.07 - - 111.71 110.32 111.21 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.7* +* ** ** *** +** +* * +** ** *** * *4.7* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 1.263 1.346 1.310 .015 *4.7* * * C-N (Pro) 1.341 .016 6 1.317 1.346 1.335 .009 +* C-O C-O 1.231 .020 100 1.193 1.253 1.234 .010 +* * CA-C CH1E-C (except Gly) 1.525 .021 96 1.473 1.552 1.519 .015 ** * CH2G*-C (Gly) 1.516 .018 5 1.496 1.529 1.512 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.518 1.535 1.525 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.514 1.585 1.553 .016 +* CH1E-CH2E (the rest) 1.530 .020 62 1.502 1.574 1.534 .014 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.393 1.480 1.440 .018 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.429 1.457 1.448 .010 * N-CH1E (Pro) 1.466 .015 6 1.449 1.464 1.455 .005 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 89 113.19 119.14 116.09 1.07 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.54 117.05 116.26 .62 CH1E-C-N (Pro) 116.9 1.5 6 115.02 117.69 116.20 .79 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.27 124.72 123.07 .58 * * O-C-N (Pro) 122.0 1.4 6 122.19 123.65 123.02 .47 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.44 126.84 122.30 1.21 * +** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.18 122.58 121.37 .81 * C-N-CH1E (Pro) 122.6 5.0 6 121.08 123.43 122.40 .73 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.78 122.18 120.80 .66 * CH2G*-C-O (Gly) 120.8 2.1 5 120.52 121.09 120.92 .21 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 109.01 111.36 110.59 .68 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.16 112.43 110.08 1.17 +* CH2E-CH1E-C (the rest) 110.1 1.9 62 104.89 114.24 110.60 1.51 +** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.64 114.81 109.77 1.78 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 105.35 114.25 111.23 3.05 ** N-CH1E-C (Pro) 111.8 2.5 6 108.30 113.61 110.94 2.02 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 110.40 111.64 110.84 .38 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.11 113.88 111.40 1.08 * * N-CH1E-CH2E (Pro) 103.0 1.1 6 103.05 104.47 103.80 .47 * NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.65 115.60 110.53 1.81 ** *** ------------------------------------------------------------------------------------------------------------- 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_2 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] 74 84.1% Residues in additional allowed regions [a,b,l,p] 14 15.9% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 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 84.1 83.8 10.0 .0 Inside b. Omega angle st dev 100 4.2 6.0 3.0 -.6 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 52 .9 .8 .2 .5 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 16 7.8 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 28 6.6 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 38 9.2 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 82 9.0 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 20 5.1 20.4 5.0 -3.1 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% 84.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .91 3 Residue-by-residue listing for refined_2 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.48 Chi1-chi2 distribution -.27 Chi1 only -.04 Chi3 & chi4 .32 Omega -.08 ------ -.18 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .38 ------ .17 ===== OVERALL AVERAGE -.06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.