Residue-by-residue listing for refined_3 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 ASP 1 t - - 178.9 - - - - - - - - 181.3 - 33.9 - 2 PRO 2 T - - - - - -67.4 - - - - - 181.1 - 38.2 - * * 3 ASN 3 T l - 177.0 - - - - - - - - 177.5 - 31.8 - 4 ALA 4 t b - - - - - - - - - - 179.7 -1.3 32.1 - 5 GLU 5 A - - -56.8 184.5 - - - - - - 181.4 -1.8 35.7 - 6 PHE 6 S B - 180.4 - - - - - - - - 175.7 - 33.2 - 7 ASP 7 B - 190.2 - - - - - - - - 183.0 -1.0 36.0 - * * 8 PRO 8 S - - - - - -72.5 - - - - - 179.7 - 36.8 - 9 ASP 9 S A - 181.7 - - - - - - - - 180.4 - 33.4 - 10 LEU 10 g B - - -66.8 - - - - - - - 179.2 - 34.0 - 11 PRO 11 G - - - - - -52.7 - - - - - 183.6 - 38.3 - * * * 12 GLY 12 G - - - - - - - - - - - 177.8 - - - 13 GLY 13 G - - - - - - - - - - - 186.1 -.8 - - * +* +* 14 GLY 14 G - - - - - - - - - - - 180.9 -.8 - - +* +* 15 LEU 15 g A - - -59.7 178.0 - - - - - - 181.1 -1.8 34.8 - 16 HIS 16 e b - - -48.0 - - - - - - - 183.1 -1.8 34.2 - * * 17 ARG 17 E B 50.6 - - 182.1 - - - - - - 174.3 -1.1 34.2 - * * 18 CYS 18 E B - 177.1 - - - - - - - - 184.5 -1.2 33.9 - * * 19 LEU 19 T A - 186.2 - - - - - - - - 177.8 -.7 35.1 - +* +* Residue-by-residue listing for refined_3 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 ALA 20 T A - - - - - - - - - - 180.9 - 33.6 - 21 CYS 21 T A - - -68.9 - - - - - - - 179.0 -1.1 30.6 - * * 22 ALA 22 T l - - - - - - - - - - 182.3 - 33.4 - 23 ARG 23 E B - 177.3 - 181.9 - - - - - - 178.5 -1.2 35.1 - * * 24 TYR 24 E B - - -58.7 - - - - - - - 180.9 - 36.7 - 25 PHE 25 e B - - -60.3 - - - - - - - 183.1 -2.9 34.7 - * * 26 ILE 26 S A 54.0 - - 178.6 - - - - - - 180.7 - 33.4 - 27 ASP 27 h B - - -59.5 - - - - - - - 176.9 - 34.7 - 28 SER 28 H A - 178.4 - - - -67.3 -31.0 - - - 178.9 - 34.2 - 29 THR 29 H A - - -48.1 - - -59.6 -44.4 - - - 178.6 - 36.1 - * * 30 ASN 30 H A - - -71.7 - - -66.0 -45.7 - - - 180.4 - 34.6 - 31 LEU 31 H A - 175.0 - - - -65.0 -46.7 - - - 178.4 -2.0 33.2 - 32 LYS 32 H A - 185.4 - 179.3 - -59.6 -43.2 - - - 177.7 -3.7 34.6 - ** ** 33 THR 33 H A - - -55.2 - - -63.0 -30.6 - - - 180.6 -2.2 34.8 - 34 HIS 34 H A - 165.7 - - - -63.1 -28.9 - - - 181.2 -1.3 32.2 - * * 35 PHE 35 h A - - -44.1 - - - - - - - 173.4 -1.0 32.0 - +* * * +* 36 ARG 36 T A - - -64.5 179.5 - - - - - - 178.1 -1.6 33.6 - 37 SER 37 h b - 180.3 - - - - - - - - 178.2 -.8 34.1 - +* +* 38 LYS 38 H A 53.7 - - 179.2 - -65.7 -28.8 - - - 178.6 -.8 32.9 - +* +* 39 ASP 39 H A - 175.3 - - - -59.7 -36.1 - - - 180.9 - 35.7 - 40 HIS 40 H A - 188.0 - - - -69.1 -56.3 - - - 185.6 -.5 38.3 - * ** * ** 41 LYS 41 H A - - -50.7 176.8 - -67.0 -28.3 - - - 169.6 -1.6 33.5 - * +* +* 42 LYS 42 H A - 171.7 - - - -60.9 -42.9 - - - 179.3 -2.3 36.4 - 43 ARG 43 H A - 184.9 - - - -63.9 -36.0 - - - 178.5 -1.4 34.3 - 44 LEU 44 H A - - -81.8 - - -69.8 -30.4 - - - 177.4 -1.8 33.7 - * * 45 LYS 45 H A - 182.5 - - - -62.1 -40.9 - - - 179.8 -1.4 33.7 - 46 GLN 46 H A 63.3 - - 181.0 - -78.7 -25.1 - - - 175.8 -1.5 30.9 - * * * 47 LEU 47 H A - - -87.7 - - -75.5 -24.5 - - - 177.4 -1.3 33.3 - * * * * 48 SER 48 h B - - -56.2 - - - - - - - 180.6 -1.4 35.4 - 49 VAL 49 S a - 180.7 - - - - - - - - 177.9 - 33.2 - 50 GLU 50 b - 187.7 - - - - - - - - 173.8 - 33.0 - * * 51 PRO 51 S - - - - - -96.7 - - - - - 182.5 - 38.9 - +** * +** 52 TYR 52 S l - - -62.3 - - - - - - - 177.8 - 32.0 - 53 SER 53 b - 188.7 - - - - - - - - 178.4 - 34.7 - 54 GLN 54 S XX - 182.6 - 179.0 - - - - - - 181.4 - 31.5 - **** **** 55 GLU 55 S l - - -63.4 184.0 - - - - - - 183.1 - 31.7 - 56 GLU 56 S a - - -60.3 183.0 - - - - - - 190.2 - 34.4 - +* +* 57 ALA 57 S a - - - - - - - - - - 178.5 - 32.7 - 58 GLU 58 S A 59.5 - - - - - - - - - 174.4 - 31.7 - Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 ARG 59 B - 185.8 - - - - - - - - 183.3 - 34.3 - 60 ALA 60 S a - - - - - - - - - - 180.9 -1.0 34.8 - * * 61 ALA 61 S l - - - - - - - - - - 180.6 - 30.7 - 62 GLY 62 - - - - - - - - - - - 181.7 - - - 63 MET 63 S B - 179.6 - 182.8 - - - - - - 177.3 - 34.9 - 64 GLY 64 S - - - - - - - - - - - 182.2 - - - 65 SER 65 l - - -57.5 - - - - - - - 178.9 -2.4 31.6 - 66 TYR 66 B - - -66.8 - - - - - - - 180.4 - 34.7 - 67 VAL 67 - 51.7 - - - - - - - - - - - 31.4 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +** * * +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 55.5 180.9 -61.3 180.7 -72.3 -65.6 -36.5 - - - 179.7 -1.5 34.1 Standard deviations: 4.9 5.8 10.3 2.4 18.3 5.4 9.0 - - - 3.2 .7 1.9 Numbers of values: 6 24 22 14 4 17 17 0 0 0 66 32 62 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_3 Page 4 ---------------------------------------- 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 ASP 1 - 1.225 1.525 1.540 1.471 - 118.16 120.03 111.34 109.56 110.08 121.75 2 PRO 2 1.350 1.242 1.523 1.526 1.467 122.57 115.23 120.97 110.35 112.93 103.95 123.79 * * * 3 ASN 3 1.330 1.236 1.553 1.546 1.460 124.65 116.07 122.09 114.65 111.89 108.97 121.74 * +* ** ** 4 ALA 4 1.323 1.234 1.501 1.522 1.429 121.20 113.70 121.94 111.79 108.68 112.71 124.05 * +* * +* +* 5 GLU 5 1.303 1.232 1.499 1.510 1.429 123.76 115.62 121.15 108.47 110.48 110.19 123.23 +* * * +* * +* 6 PHE 6 1.305 1.235 1.507 1.537 1.418 120.70 115.70 120.95 111.06 110.10 111.60 123.31 +* ** ** 7 ASP 7 1.298 1.222 1.516 1.518 1.432 121.39 119.29 119.50 108.78 107.30 110.24 121.19 ** * +* * * ** 8 PRO 8 1.333 1.244 1.536 1.535 1.457 121.82 117.99 119.85 111.20 114.91 104.65 122.15 * +* +* 9 ASP 9 1.319 1.244 1.515 1.538 1.460 120.30 115.59 121.43 110.60 109.81 111.59 122.95 10 LEU 10 1.310 1.223 1.525 1.554 1.444 122.01 117.93 120.08 109.42 109.70 112.22 121.98 * * * * 11 PRO 11 1.349 1.246 1.523 1.524 1.473 122.86 115.56 121.20 110.74 111.88 103.46 123.22 12 GLY 12 1.313 1.239 1.501 - 1.433 120.95 114.93 121.26 - 110.95 - 123.69 * * * Residue-by-residue listing for refined_3 Page 5 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 GLY 13 1.324 1.225 1.497 - 1.436 122.55 116.25 120.62 - 113.03 - 123.13 * * * 14 GLY 14 1.320 1.224 1.512 - 1.439 120.92 115.49 121.48 - 110.46 - 123.03 15 LEU 15 1.313 1.217 1.508 1.525 1.427 122.44 116.27 121.24 110.57 110.32 109.55 122.48 * +* +* 16 HIS 16 1.301 1.230 1.503 1.528 1.445 120.53 116.20 120.95 109.25 108.53 112.30 122.76 +* * * +* 17 ARG 17 1.294 1.223 1.496 1.526 1.427 121.11 115.59 121.31 110.29 112.27 110.16 123.08 +** * +* +** 18 CYS 18 1.296 1.240 1.504 1.542 1.435 120.86 116.08 120.45 111.13 106.90 111.52 123.46 ** * * +* ** 19 LEU 19 1.305 1.226 1.508 1.514 1.437 122.65 115.01 121.31 110.74 109.56 109.06 123.63 +* * +* 20 ALA 20 1.310 1.224 1.535 1.521 1.452 122.64 117.14 120.73 110.62 111.38 110.51 122.12 * * 21 CYS 21 1.331 1.230 1.484 1.535 1.449 120.53 115.39 120.35 112.35 112.45 112.86 124.26 +* * * +* 22 ALA 22 1.331 1.233 1.537 1.518 1.455 123.59 115.17 121.64 111.25 110.99 110.31 123.11 * * 23 ARG 23 1.308 1.246 1.507 1.537 1.434 122.97 115.67 120.58 110.64 109.17 109.56 123.74 * * * 24 TYR 24 1.294 1.235 1.513 1.512 1.404 123.32 116.98 120.17 109.35 107.95 108.60 122.84 +** +** * * +** 25 PHE 25 1.303 1.218 1.497 1.531 1.443 121.63 116.03 120.27 109.48 108.88 111.32 123.69 +* * +* 26 ILE 26 1.305 1.228 1.539 1.536 1.424 123.50 117.57 120.52 111.09 113.25 110.03 121.88 +* +* +* 27 ASP 27 1.323 1.239 1.481 1.541 1.458 120.04 115.74 120.47 107.51 109.68 113.10 123.77 ** * +* ** 28 SER 28 1.313 1.194 1.511 1.545 1.438 122.26 116.15 120.45 111.36 108.44 110.43 123.31 * +* * +* 29 THR 29 1.324 1.238 1.548 1.520 1.440 122.89 115.92 121.05 109.64 110.37 108.29 122.98 * +* +* 30 ASN 30 1.332 1.231 1.515 1.539 1.441 122.90 115.12 121.26 110.44 110.44 109.95 123.59 31 LEU 31 1.306 1.227 1.543 1.556 1.443 123.17 115.67 121.09 113.95 111.46 108.09 123.24 +* * ** * ** 32 LYS 32 1.294 1.240 1.534 1.532 1.470 123.65 116.49 120.54 110.66 111.17 109.21 122.96 ** * ** 33 THR 33 1.338 1.227 1.535 1.544 1.465 122.11 114.99 121.68 109.13 109.82 110.93 123.30 34 HIS 34 1.311 1.228 1.546 1.556 1.442 123.89 119.20 119.67 112.60 113.53 110.11 121.13 * * * +* * * +* 35 PHE 35 1.331 1.216 1.520 1.522 1.463 117.18 117.25 120.56 109.01 111.14 114.46 122.19 +** ** +** 36 ARG 36 1.325 1.241 1.523 1.531 1.468 119.88 114.70 121.62 109.73 108.70 112.32 123.67 * * * 37 SER 37 1.324 1.244 1.518 1.535 1.423 123.61 115.44 121.39 110.87 110.41 110.32 123.16 +* * +* 38 LYS 38 1.320 1.205 1.509 1.532 1.444 122.11 115.88 120.30 111.45 110.40 111.29 123.75 * * 39 ASP 39 1.332 1.237 1.524 1.528 1.471 123.64 114.68 121.68 109.15 110.92 109.14 123.64 * * 40 HIS 40 1.301 1.209 1.464 1.502 1.455 123.67 113.60 121.89 106.50 110.08 108.29 124.51 +* * +** * * * +* * +** 41 LYS 41 1.266 1.221 1.539 1.508 1.403 123.42 114.90 121.47 115.57 108.81 106.69 123.62 **** * +** +** ** **** Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 LYS 42 1.327 1.233 1.538 1.527 1.455 124.30 116.97 120.64 108.10 110.25 109.35 122.39 * * * 43 ARG 43 1.339 1.214 1.527 1.540 1.458 120.75 115.24 121.84 110.43 108.44 110.87 122.85 44 LEU 44 1.301 1.228 1.528 1.532 1.441 122.82 115.40 121.21 111.61 110.64 109.91 123.37 +* +* 45 LYS 45 1.313 1.231 1.542 1.575 1.459 124.01 117.03 120.31 113.53 109.82 108.50 122.62 * ** * +* * ** 46 GLN 46 1.338 1.240 1.538 1.541 1.469 120.72 116.81 120.61 111.71 112.20 112.92 122.57 * * 47 LEU 47 1.333 1.235 1.513 1.522 1.450 121.84 115.52 121.30 110.65 111.02 111.20 123.18 48 SER 48 1.301 1.242 1.530 1.520 1.428 121.93 117.31 120.06 110.59 108.45 109.03 122.63 ** +* ** 49 VAL 49 1.317 1.245 1.521 1.548 1.450 120.92 116.56 120.41 110.61 110.03 111.89 123.01 50 GLU 50 1.325 1.231 1.545 1.545 1.446 120.96 117.76 120.85 110.65 111.73 111.41 121.20 * * 51 PRO 51 1.342 1.245 1.543 1.523 1.448 122.53 116.04 120.51 110.80 111.34 102.74 123.45 * * * 52 TYR 52 1.325 1.250 1.527 1.534 1.475 123.97 115.84 120.85 109.53 112.99 113.23 123.29 * +* +* 53 SER 53 1.310 1.236 1.520 1.535 1.440 122.67 115.85 120.25 109.90 109.31 110.67 123.87 * * 54 GLN 54 1.330 1.236 1.545 1.553 1.467 124.06 115.30 120.90 112.66 111.92 111.40 123.73 * * * * 55 GLU 55 1.333 1.229 1.502 1.535 1.458 125.59 115.55 121.16 111.66 110.08 112.96 123.15 * ** * ** 56 GLU 56 1.329 1.230 1.533 1.534 1.450 121.58 117.91 120.02 108.36 113.31 111.27 122.06 57 ALA 57 1.330 1.234 1.519 1.517 1.467 119.96 116.00 121.31 111.61 114.15 109.72 122.65 * * 58 GLU 58 1.269 1.230 1.503 1.558 1.459 121.53 115.55 121.35 111.91 108.82 113.41 123.08 **** * * +* **** 59 ARG 59 1.308 1.226 1.525 1.537 1.420 121.15 116.28 120.86 111.14 107.04 110.82 122.75 +* +* * +* 60 ALA 60 1.307 1.235 1.514 1.522 1.455 122.06 115.06 120.93 110.41 110.30 109.52 124.00 +* +* 61 ALA 61 1.324 1.239 1.521 1.535 1.457 124.24 114.85 121.74 112.44 111.23 112.91 123.32 * * +* +* 62 GLY 62 1.304 1.236 1.499 - 1.429 121.96 116.16 120.81 - 110.33 - 123.01 +* * +* 63 MET 63 1.303 1.242 1.511 1.529 1.436 122.06 116.15 120.59 109.61 110.03 110.43 123.22 +* * +* 64 GLY 64 1.308 1.235 1.512 - 1.442 121.27 115.91 120.06 - 112.90 - 124.02 +* +* 65 SER 65 1.327 1.238 1.533 1.539 1.460 124.33 115.57 121.73 111.90 111.58 112.08 122.62 * * 66 TYR 66 1.308 1.236 1.506 1.513 1.403 122.51 115.84 120.97 110.77 110.22 109.67 123.19 * +** +** 67 VAL 67 1.287 - 1.529 1.565 1.426 122.84 - - 113.13 110.43 112.10 - +** +* +* +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* +** ** +** +** +* +** +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 Page 7 ---------------------------------------- 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 62 1.266 1.339 1.314 .015 **** * C-N (Pro) 1.341 .016 4 1.333 1.350 1.343 .007 C-O C-O 1.231 .020 66 1.194 1.250 1.232 .010 +* CA-C CH1E-C (except Gly) 1.525 .021 62 1.464 1.553 1.521 .017 +** * CH2G*-C (Gly) 1.516 .018 5 1.497 1.512 1.504 .006 * CA-CB CH1E-CH3E (Ala) 1.521 .033 6 1.517 1.535 1.523 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 5 1.520 1.565 1.543 .015 CH1E-CH2E (the rest) 1.530 .020 51 1.502 1.575 1.533 .014 * ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 58 1.403 1.475 1.445 .018 +** NH1-CH2G* (Gly) 1.451 .016 5 1.429 1.442 1.436 .005 * N-CH1E (Pro) 1.466 .015 4 1.448 1.473 1.461 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 Page 8 ---------------------------------------- +-----------------+ | 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 57 113.60 119.29 116.06 1.13 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.93 116.25 115.75 .49 CH1E-C-N (Pro) 116.9 1.5 4 115.23 117.99 116.21 1.07 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 62 121.13 124.51 123.03 .73 * O-C-N (Pro) 122.0 1.4 4 122.15 123.79 123.15 .61 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 57 117.18 125.59 122.30 1.51 +** ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.92 122.55 121.53 .63 * C-N-CH1E (Pro) 122.6 5.0 4 121.82 122.86 122.45 .38 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 61 119.50 122.09 120.89 .60 CH2G*-C-O (Gly) 120.8 2.1 5 120.06 121.48 120.85 .50 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 6 110.41 112.44 111.35 .69 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 5 109.13 113.13 110.72 1.39 +* CH2E-CH1E-C (the rest) 110.1 1.9 51 106.50 115.57 110.68 1.67 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 58 106.90 114.15 110.32 1.58 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.33 113.03 111.53 1.19 N-CH1E-C (Pro) 111.8 2.5 4 111.34 114.91 112.76 1.37 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 6 109.52 112.91 110.95 1.36 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 5 108.29 112.10 110.65 1.39 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.74 104.65 103.70 .70 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 47 106.69 114.46 110.69 1.61 ** ** ------------------------------------------------------------------------------------------------------------- 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_3 Page 9 ---------------------------------------- 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] 40 71.4% Residues in additional allowed regions [a,b,l,p] 15 26.8% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 1 1.8% ---- ------ Number of non-glycine and non-proline residues 56 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 67 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 56 71.4 83.8 10.0 -1.2 WORSE b. Omega angle st dev 66 3.2 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 62 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 32 .7 .8 .2 -.7 Inside f. Overall G-factor 67 .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 6 4.9 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 24 5.8 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 22 10.3 17.5 4.9 -1.5 BETTER d. Chi-1 pooled st dev 52 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 14 2.4 20.4 5.0 -3.6 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% 71.4 2 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 11.7 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 3 Residue-by-residue listing for refined_3 Page 10 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.58 Chi1-chi2 distribution -.21 Chi1 only .02 Chi3 & chi4 .45 Omega .16 ------ -.11 ===== Main-chain covalent forces:- Main-chain bond lengths .01 Main-chain bond angles .35 ------ .21 ===== OVERALL AVERAGE .00 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.