Residue-by-residue listing for refined_14 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 - - 186.8 - - - - - - - - 177.7 - 35.0 - 2 PRO 2 - - - - - -55.7 - - - - - 180.3 - 39.2 - +* +* 3 ASN 3 S A - 187.5 - - - - - - - - 178.2 - 34.7 - 4 ALA 4 ~l - - - - - - - - - - 174.8 - 29.3 - ** * ** 5 GLU 5 A - - -60.8 175.2 - - - - - - 177.6 - 35.2 - 6 PHE 6 B - 170.6 - - - - - - - - 175.1 - 35.2 - 7 ASP 7 B - 189.6 - - - - - - - - 178.2 -1.5 36.2 - 8 PRO 8 S - - - - - -62.0 - - - - - 179.1 - 37.5 - * * 9 ASP 9 S A - 183.9 - - - - - - - - 177.7 - 33.0 - 10 LEU 10 t b 45.4 - - - - - - - - - 192.5 - 26.8 - * ** ** ** 11 PRO 11 T - - - - - -69.9 - - - - - 174.0 - 36.1 - * * 12 GLY 12 T - - - - - - - - - - - 184.6 - - - 13 GLY 13 T - - - - - - - - - - - 185.1 -1.4 - - 14 GLY 14 T - - - - - - - - - - - 182.3 - - - 15 LEU 15 T A 49.9 - - - - - - - - - 174.9 -.8 30.4 - +* * +* 16 HIS 16 t b - - -57.2 - - - - - - - 178.4 -2.3 32.0 - 17 ARG 17 B B - - -61.4 181.7 - - - - - - 169.1 -1.6 36.1 - +* +* 18 CYS 18 t B - 172.2 - - - - - - - - 185.1 -1.0 34.2 - * * 19 LEU 19 T A - - -59.6 178.4 - - - - - - 178.2 -.7 34.6 - +* +* Residue-by-residue listing for refined_14 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 - - - - - - - - - - 184.9 - 34.0 - 21 CYS 21 T a - - -62.1 - - - - - - - 176.9 -1.7 31.2 - 22 ALA 22 t l - - - - - - - - - - 180.8 -1.8 33.0 - 23 ARG 23 B - 176.0 - 181.8 - - - - - - 180.8 - 34.9 - 24 TYR 24 B B - - -55.1 - - - - - - - 178.3 - 37.7 - * * 25 PHE 25 B - - -58.1 - - - - - - - 186.4 -2.6 35.0 - * * 26 ILE 26 S A 61.2 - - 176.0 - - - - - - 181.8 - 33.8 - 27 ASP 27 h B - 174.8 - - - - - - - - 181.9 - 33.8 - 28 SER 28 H A 56.8 - - - - -57.7 -36.4 - - - 181.1 - 34.5 - 29 THR 29 H A - - -51.1 - - -60.0 -41.6 - - - 178.4 - 34.7 - * * 30 ASN 30 H A - - -70.7 - - -64.7 -47.8 - - - 179.5 -.5 35.0 - ** ** 31 LEU 31 H A - 173.1 - - - -61.8 -48.1 - - - 177.9 -2.0 32.7 - 32 LYS 32 H A - - -63.5 174.3 - -62.0 -40.0 - - - 176.7 -3.6 32.7 - ** ** 33 THR 33 H A - - -59.3 - - -62.7 -32.9 - - - 176.7 -2.5 33.3 - 34 HIS 34 H A - 164.2 - - - -59.4 -28.9 - - - 179.7 -1.7 32.3 - * * 35 PHE 35 h A - - -44.2 - - - - - - - 179.3 -1.1 33.4 - * * * 36 ARG 36 T A - - -61.5 179.5 - - - - - - 173.5 -1.7 31.8 - * * 37 SER 37 h B - - -56.5 - - - - - - - 186.8 -.5 35.1 - * +* +* 38 LYS 38 H A 59.9 - - 183.9 - -60.7 -36.7 - - - 181.8 -.7 32.4 - +* +* 39 ASP 39 H A - 175.7 - - - -56.3 -37.6 - - - 183.9 - 35.1 - 40 HIS 40 H A - 185.3 - - - -65.9 -56.5 - - - 185.8 -.8 36.2 - +* * +* +* 41 LYS 41 H A - - -53.5 179.6 - -68.8 -29.4 - - - 171.5 -1.1 33.3 - * * * 42 LYS 42 H A - 170.1 - - - -61.1 -45.5 - - - 181.8 -2.2 35.6 - 43 ARG 43 H A - 196.3 - - - -63.6 -36.9 - - - 178.5 -2.2 34.2 - 44 LEU 44 H A - - -84.6 - - -70.4 -36.6 - - - 177.4 -2.2 33.1 - * * 45 LYS 45 H A - 185.2 - 170.5 - -67.3 -26.6 - - - 174.5 -2.2 31.5 - * * 46 GLN 46 H A - 183.0 - 185.8 - -74.3 -41.6 - - - 178.8 -1.4 34.8 - 47 LEU 47 H A - - -61.4 181.3 - -65.3 -35.4 - - - 181.0 -1.8 36.2 - 48 SER 48 h b - - -56.3 - - - - - - - 183.9 -2.5 34.4 - 49 VAL 49 A - 184.1 - - - - - - - - 182.6 - 34.7 - 50 GLU 50 b - - -54.2 - - - - - - - 178.6 - 35.2 - 51 PRO 51 - - - - - -79.5 - - - - - 183.4 - 38.2 - * * * 52 TYR 52 S ~p - - -66.0 - - - - - - - 178.7 -1.1 32.5 - ** * ** 53 SER 53 S B - 179.0 - - - - - - - - 181.1 - 34.7 - 54 GLN 54 g l - 185.1 - 179.4 - - - - - - 186.6 - 33.0 - * * 55 GLU 55 G l - - -69.5 - - - - - - - 183.2 - 29.9 - * * 56 GLU 56 G ~l 66.8 - - 185.4 - - - - - - 177.9 - 28.6 - ** +* ** Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 G l - - - - - - - - - - 178.1 -.5 31.3 - ** ** 58 GLU 58 g A - 189.8 - 170.4 - - - - - - 174.8 -.8 34.0 - +* +* 59 ARG 59 S b - - -67.6 - - - - - - - 183.2 - 35.0 - 60 ALA 60 S a - - - - - - - - - - 179.7 - 34.6 - 61 ALA 61 S a - - - - - - - - - - 177.9 - 34.0 - 62 GLY 62 - - - - - - - - - - - 178.1 - - - 63 MET 63 B 54.0 - - - - - - - - - 180.4 - 31.7 - 64 GLY 64 - - - - - - - - - - - 180.6 - - - 65 SER 65 B - 184.5 - - - - - - - - 180.1 - 34.8 - 66 TYR 66 B - 180.1 - - - - - - - - 179.8 - 33.9 - 67 VAL 67 - - 178.5 - - - - - - - - - - 33.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * * +* ** ** ** ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.3 180.7 -60.7 178.9 -66.8 -63.6 -38.7 - - - 179.8 -1.6 33.9 Standard deviations: 7.2 7.7 8.1 4.8 10.3 4.7 7.7 - - - 3.9 .8 2.2 Numbers of values: 7 23 22 15 4 17 17 0 0 0 66 31 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_14 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 - 1.235 1.520 1.545 1.462 - 118.30 119.27 110.20 108.21 110.16 122.33 * * * 2 PRO 2 1.361 1.246 1.540 1.538 1.482 123.68 114.72 122.42 109.53 114.47 102.95 122.86 * * * * * 3 ASN 3 1.312 1.235 1.542 1.531 1.472 123.41 115.19 121.13 109.87 110.80 109.85 123.68 * * 4 ALA 4 1.327 1.236 1.509 1.532 1.458 124.85 114.42 122.02 112.51 113.14 113.78 123.45 +* * ** ** 5 GLU 5 1.303 1.232 1.511 1.519 1.419 123.31 114.10 121.77 110.93 107.70 109.42 124.12 +* ** * * ** 6 PHE 6 1.316 1.232 1.519 1.541 1.433 124.20 115.91 120.82 110.59 110.90 108.89 123.27 * * * 7 ASP 7 1.303 1.225 1.511 1.523 1.450 121.91 119.73 119.07 108.02 106.40 110.75 121.17 +* +* * * +* * +* 8 PRO 8 1.331 1.238 1.538 1.527 1.461 121.79 117.88 119.91 110.92 114.07 104.06 122.20 9 ASP 9 1.322 1.228 1.516 1.520 1.466 120.05 115.52 121.58 110.93 110.50 111.40 122.88 10 LEU 10 1.306 1.230 1.526 1.576 1.427 122.62 115.87 122.15 115.94 111.24 114.82 121.98 +* ** +* *** +** *** 11 PRO 11 1.348 1.221 1.518 1.516 1.467 123.31 117.57 120.28 112.12 116.62 103.92 122.15 * +* +* 12 GLY 12 1.282 1.226 1.479 - 1.436 119.10 114.75 121.08 - 109.39 - 124.12 *** ** * *** Residue-by-residue listing for refined_14 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 1.337 1.227 1.493 - 1.443 122.47 114.68 121.66 - 109.99 - 123.66 * * * 14 GLY 14 1.335 1.219 1.531 - 1.465 122.22 116.53 121.03 - 113.10 - 122.44 15 LEU 15 1.304 1.230 1.521 1.536 1.424 122.39 117.15 120.66 114.93 113.30 110.12 122.18 +* +* +** +** 16 HIS 16 1.314 1.240 1.495 1.530 1.463 119.35 115.41 121.21 108.79 109.82 115.34 123.27 * * * +** +** 17 ARG 17 1.289 1.238 1.486 1.531 1.419 122.05 115.23 121.06 106.88 109.19 111.86 123.69 +** +* ** +* +** 18 CYS 18 1.279 1.240 1.490 1.536 1.414 121.07 115.85 120.31 111.26 105.03 111.57 123.83 +*** +* ** ** +*** 19 LEU 19 1.299 1.228 1.514 1.522 1.448 122.96 114.96 121.61 110.97 110.41 109.25 123.41 ** ** 20 ALA 20 1.299 1.230 1.536 1.517 1.442 122.91 117.89 119.82 110.03 112.28 110.24 122.30 ** ** 21 CYS 21 1.338 1.233 1.506 1.533 1.461 120.18 115.87 120.31 112.10 113.58 111.63 123.81 * * 22 ALA 22 1.329 1.235 1.546 1.531 1.466 123.70 116.34 121.01 111.11 112.34 110.55 122.59 * * * 23 ARG 23 1.309 1.240 1.513 1.542 1.444 122.27 116.08 120.31 110.29 109.08 110.19 123.61 * * 24 TYR 24 1.307 1.232 1.512 1.521 1.404 123.26 116.67 120.63 107.52 108.27 108.97 122.69 +* +** * * +** 25 PHE 25 1.292 1.220 1.494 1.521 1.439 120.94 117.05 119.60 110.12 107.07 110.58 123.34 +** * * * +** 26 ILE 26 1.307 1.224 1.536 1.530 1.426 122.24 116.90 120.69 110.01 113.14 110.54 122.40 +* +* +* 27 ASP 27 1.311 1.240 1.500 1.546 1.455 121.10 116.01 120.08 111.20 109.70 110.70 123.91 * * * 28 SER 28 1.318 1.203 1.523 1.531 1.441 123.42 117.43 119.64 110.94 111.53 109.10 122.86 * * 29 THR 29 1.334 1.232 1.535 1.531 1.459 122.06 115.71 120.99 109.65 110.51 110.35 123.26 30 ASN 30 1.328 1.230 1.512 1.535 1.442 123.16 115.01 121.43 110.42 109.81 109.54 123.51 31 LEU 31 1.308 1.228 1.540 1.559 1.443 122.88 116.11 120.83 114.15 111.34 108.78 123.06 * * ** * ** 32 LYS 32 1.298 1.233 1.536 1.533 1.467 122.62 116.87 120.30 111.61 111.73 110.75 122.81 ** ** 33 THR 33 1.339 1.236 1.531 1.542 1.462 121.69 115.27 121.42 110.47 110.14 111.66 123.27 34 HIS 34 1.315 1.231 1.554 1.557 1.443 122.98 118.60 120.18 112.50 112.75 110.33 121.22 * * * * * * 35 PHE 35 1.327 1.209 1.515 1.522 1.459 118.37 117.30 120.97 108.09 109.93 113.89 121.72 * +* * +* +* 36 ARG 36 1.311 1.234 1.520 1.519 1.453 120.39 114.60 121.79 112.75 110.41 111.27 123.61 * * * 37 SER 37 1.311 1.248 1.542 1.512 1.419 124.00 115.68 120.83 111.57 107.66 108.58 123.47 * ** * * * ** 38 LYS 38 1.324 1.235 1.531 1.535 1.463 123.44 116.71 119.98 111.50 113.76 110.53 123.27 39 ASP 39 1.332 1.233 1.516 1.531 1.482 123.05 114.97 121.46 108.88 111.90 110.05 123.54 * * 40 HIS 40 1.298 1.217 1.479 1.512 1.450 122.99 115.21 121.04 108.18 111.64 109.43 123.75 ** ** * ** 41 LYS 41 1.275 1.218 1.515 1.494 1.414 121.78 115.12 121.18 113.66 109.42 108.67 123.66 +*** +* ** +* * +*** 42 LYS 42 1.323 1.243 1.530 1.526 1.440 122.67 116.23 120.61 108.99 110.25 109.77 123.15 Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 ARG 43 1.342 1.224 1.536 1.553 1.449 121.88 115.68 121.16 112.99 108.18 108.70 123.06 * +* * * +* 44 LEU 44 1.314 1.223 1.516 1.522 1.450 123.00 116.56 120.52 110.92 112.16 110.75 122.92 * * 45 LYS 45 1.314 1.225 1.536 1.544 1.453 121.83 116.24 121.47 113.01 110.15 111.77 122.28 * +* +* 46 GLN 46 1.322 1.228 1.535 1.514 1.421 121.55 116.02 120.81 110.11 109.50 110.09 123.17 +* +* 47 LEU 47 1.331 1.236 1.516 1.505 1.436 123.05 115.43 121.77 108.63 110.67 109.06 122.80 * * * 48 SER 48 1.295 1.236 1.520 1.528 1.424 122.70 115.55 121.08 111.32 109.26 109.68 123.35 ** +* ** 49 VAL 49 1.318 1.233 1.535 1.569 1.457 122.80 115.42 120.63 110.19 110.54 110.23 123.92 * * 50 GLU 50 1.339 1.247 1.542 1.533 1.473 124.18 117.62 120.52 108.64 111.86 110.13 121.82 * * 51 PRO 51 1.346 1.244 1.521 1.545 1.445 122.73 115.75 120.58 110.66 110.88 104.50 123.64 * * * * 52 TYR 52 1.335 1.240 1.532 1.544 1.464 123.52 116.17 121.07 110.86 111.34 112.06 122.72 * * 53 SER 53 1.303 1.234 1.515 1.542 1.433 122.54 116.35 119.47 111.14 108.15 109.87 124.12 +* * * +* 54 GLN 54 1.346 1.225 1.543 1.556 1.479 124.01 114.94 121.89 112.22 109.47 110.60 123.09 * * * * * * 55 GLU 55 1.334 1.231 1.500 1.544 1.451 123.48 113.40 121.60 112.73 109.29 114.70 124.56 * * * ** ** 56 GLU 56 1.340 1.228 1.542 1.556 1.486 127.27 116.22 120.49 112.99 113.28 114.09 123.29 * * *** +* ** *** 57 ALA 57 1.345 1.230 1.512 1.516 1.474 125.42 114.16 122.09 112.64 111.63 111.50 123.71 * ** * * ** 58 GLU 58 1.291 1.229 1.529 1.530 1.427 123.50 112.78 123.32 113.83 106.47 108.65 123.90 +** +* * +* * +* +* * +** 59 ARG 59 1.313 1.228 1.507 1.541 1.431 125.93 116.14 120.62 109.72 106.25 111.52 123.07 * * ** +* ** 60 ALA 60 1.304 1.232 1.510 1.526 1.444 121.69 116.10 121.12 110.21 110.21 110.17 122.78 +* +* 61 ALA 61 1.312 1.240 1.505 1.524 1.443 121.06 114.83 121.13 111.02 109.30 110.58 124.04 * * 62 GLY 62 1.308 1.247 1.513 - 1.438 122.21 115.37 121.03 - 112.97 - 123.59 * * 63 MET 63 1.309 1.250 1.518 1.566 1.449 123.99 116.48 120.22 112.69 109.73 112.34 123.29 * +* * * * +* 64 GLY 64 1.306 1.235 1.504 - 1.433 121.25 116.39 120.70 - 111.50 - 122.90 +* * +* 65 SER 65 1.302 1.247 1.533 1.541 1.434 122.08 116.73 120.53 111.20 109.16 109.25 122.73 +* * +* 66 TYR 66 1.310 1.238 1.515 1.545 1.441 122.04 116.23 120.79 110.92 109.68 110.80 122.97 * * 67 VAL 67 1.299 - 1.515 1.556 1.439 121.99 - - 110.77 109.56 112.09 - ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** ** +** *** +* * *** ** +** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 1.275 1.346 1.314 .017 +*** * * C-N (Pro) 1.341 .016 4 1.331 1.361 1.346 .011 * C-O C-O 1.231 .020 66 1.203 1.250 1.232 .009 * CA-C CH1E-C (except Gly) 1.525 .021 62 1.479 1.554 1.521 .016 ** * CH2G*-C (Gly) 1.516 .018 5 1.479 1.531 1.504 .018 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 6 1.516 1.532 1.524 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 5 1.530 1.569 1.546 .015 * CH1E-CH2E (the rest) 1.530 .020 51 1.494 1.576 1.534 .016 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 58 1.404 1.486 1.446 .019 +** * NH1-CH2G* (Gly) 1.451 .016 5 1.433 1.465 1.443 .011 * N-CH1E (Pro) 1.466 .015 4 1.445 1.482 1.464 .013 * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 57 112.78 119.73 115.97 1.20 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.68 116.53 115.54 .79 CH1E-C-N (Pro) 116.9 1.5 4 114.72 117.88 116.48 1.30 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 62 121.17 124.56 123.14 .69 * O-C-N (Pro) 122.0 1.4 4 122.15 123.64 122.71 .60 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 57 118.37 127.27 122.63 1.49 +* *** C-NH1-CH2G* (Gly) 120.6 1.7 5 119.10 122.47 121.45 1.25 * C-N-CH1E (Pro) 122.6 5.0 4 121.79 123.68 122.88 .71 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 61 119.07 123.32 120.87 .79 * * CH2G*-C-O (Gly) 120.8 2.1 5 120.70 121.66 121.10 .31 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 6 110.03 112.64 111.26 1.01 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 5 109.65 110.77 110.22 .38 CH2E-CH1E-C (the rest) 110.1 1.9 51 106.88 115.94 111.00 1.88 +* *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 58 105.03 113.76 110.19 1.93 ** NH1-CH2G*-C (Gly) 112.5 2.9 5 109.39 113.10 111.39 1.51 * N-CH1E-C (Pro) 111.8 2.5 4 110.88 116.62 114.01 2.05 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 6 110.17 113.78 111.13 1.26 ** NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 5 110.23 112.09 110.97 .76 N-CH1E-CH2E (Pro) 103.0 1.1 4 102.95 104.50 103.86 .57 * NH1-CH1E-CH2E (the rest) 110.5 1.7 47 108.58 115.34 110.64 1.68 * +** ------------------------------------------------------------------------------------------------------------- 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_14 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] 41 73.2% Residues in additional allowed regions [a,b,l,p] 12 21.4% Residues in generously allowed regions [~a,~b,~l,~p] 3 5.4% Residues in disallowed regions [XX] 0 .0% ---- ------ 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 73.2 83.8 10.0 -1.1 WORSE b. Omega angle st dev 66 3.9 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 62 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 31 .8 .8 .2 -.3 Inside f. Overall G-factor 67 -.1 -.4 .3 1.0 Inside S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 7 7.2 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 23 7.7 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 22 8.1 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 52 9.5 18.2 4.8 -1.8 BETTER e. Chi-2 trans st dev 15 4.8 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% 73.2 2 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_14 Page 10 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.62 Chi1-chi2 distribution -.24 Chi1 only .26 Chi3 & chi4 .24 Omega -.17 ------ -.25 ===== Main-chain covalent forces:- Main-chain bond lengths -.01 Main-chain bond angles .27 ------ .16 ===== OVERALL AVERAGE -.10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.