Residue-by-residue listing for refined_10 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 - - 183.9 - - - - - - - - 181.0 - 35.0 - 2 ALA 2 b - - - - - - - - - - 179.8 - 34.5 - 3 GLU 3 B - - -71.2 - - - - - - - 178.7 - 33.7 - 4 VAL 4 t B - 182.5 - - - - - - - - 181.9 - 34.3 - 5 HIS 5 T b - - -63.1 - - - - - - - 177.8 - 31.6 - 6 ASN 6 T ~a - 179.6 - - - - - - - - 176.3 -1.5 34.6 - ** ** 7 GLN 7 e b - - -65.9 - - - - - - - 180.9 -.9 34.9 - * * 8 LEU 8 E B - - -64.5 - - - - - - - 183.4 -1.6 32.4 - 9 GLU 9 E B - - -57.0 179.9 - - - - - - 181.8 -1.6 34.0 - 10 ILE 10 E B - - -57.7 176.8 - - - - - - 170.9 -2.6 35.0 - +* +* 11 LYS 11 E B 57.1 - - 159.6 - - - - - - 180.5 -2.2 32.7 - 12 PHE 12 E B - - -58.8 - - - - - - - 181.3 - 34.9 - 13 ARG 13 E B - - -49.0 199.9 - - - - - - 179.2 -3.3 33.6 - * * +* +* 14 LEU 14 t B - - -68.8 - - - - - - - 181.2 -3.4 34.8 - +* +* 15 THR 15 T A 42.3 - - - - - - - - - 177.1 - 33.2 - * * 16 ASP 16 T A - - -70.9 - - - - - - - 180.3 - 33.7 - 17 GLY 17 t - - - - - - - - - - - 177.3 -1.5 - - 18 SER 18 B - - -56.0 - - - - - - - 179.7 - 36.2 - 19 ASP 19 B B 57.4 - - - - - - - - - 181.5 - 31.6 - 20 ILE 20 B - - -58.6 178.3 - - - - - - 182.2 -2.7 35.9 - 21 GLY 21 - - - - - - - - - - - 182.8 - - - Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 PRO 22 - - - - - -73.9 - - - - - 174.5 - 38.3 - * * 23 LYS 23 E B - - -76.7 - - - - - - - 182.1 -1.8 31.4 - 24 ALA 24 E B - - - - - - - - - - 180.3 - 32.7 - 25 PHE 25 E B - - -56.1 - - - - - - - 172.3 -3.7 37.2 - * ** ** 26 PRO 26 t - - - - - -65.2 - - - - - 177.7 - 39.9 - +* +* 27 ASP 27 T A 63.7 - - - - - - - - - 177.6 - 33.0 - 28 ALA 28 T A - - - - - - - - - - 177.6 - 34.0 - 29 THR 29 t B - - -54.4 - - - - - - - 181.5 -1.7 35.0 - 30 THR 30 h B 61.2 - - - - - - - - - 178.8 - 34.4 - 31 VAL 31 H A - 179.2 - - - -66.2 -27.4 - - - 177.1 -3.3 33.2 - * +* +* 32 SER 32 H A - - -61.2 - - -60.1 -49.2 - - - 180.3 -1.2 33.9 - * * 33 ALA 33 H A - - - - - -74.9 -31.0 - - - 178.1 - 33.8 - 34 LEU 34 H A - 176.7 - - - -62.9 -48.5 - - - 179.6 -2.3 36.1 - 35 LYS 35 H A - 187.5 - - - -64.2 -43.8 - - - 180.6 -3.1 36.3 - * * 36 GLU 36 H A - 193.8 - - - -56.3 -40.2 - - - 178.1 -2.1 37.6 - * * 37 THR 37 H A - - -55.0 - - -63.2 -42.3 - - - 177.4 -2.1 34.0 - 38 VAL 38 H A - 178.6 - - - -60.1 -42.6 - - - 181.2 -1.6 34.5 - 39 ILE 39 H A - - -49.0 - - -62.7 -33.5 - - - 178.4 -2.3 34.3 - * * 40 SER 40 H A - 184.1 - - - -76.5 -40.2 - - - 181.9 -1.5 34.2 - 41 GLU 41 H A - - -67.0 - - -70.7 -40.0 - - - 178.1 -2.5 34.5 - 42 TRP 42 h B - 188.5 - - - - - - - - 178.8 -3.1 35.6 - * * 43 PRO 43 t - - - - - -51.3 - - - - - 179.4 - 38.7 - * * * 44 ARG 44 T A - - -63.1 185.1 - - - - - - 178.6 - 33.3 - 45 GLU 45 T A - - -60.7 173.1 - - - - - - 174.6 - 34.0 - 46 LYS 46 t B - - -75.6 176.0 - - - - - - 181.4 -1.8 35.0 - 47 GLU 47 B - 183.2 - 172.2 - - - - - - 184.6 - 32.2 - 48 ASN 48 S l - - -72.8 - - - - - - - 172.2 -.5 30.1 - * ** * ** 49 GLY 49 S - - - - - - - - - - - 174.1 - - - * * 50 PRO 50 - - - - - -97.1 - - - - - 174.6 - 41.3 - +** ** +** 51 LYS 51 ~a - 180.2 - - - - - - - - 179.5 - 32.1 - ** ** 52 THR 52 t B 53.0 - - - - - - - - - 178.7 - 33.0 - 53 VAL 53 T A - 181.1 - - - - - - - - 180.3 - 35.8 - 54 LYS 54 T A - 174.9 - 188.2 - - - - - - 188.9 - 37.1 - +* +* 55 GLU 55 T A - - -57.6 - - - - - - - 183.7 - 34.6 - 56 VAL 56 t B - 179.9 - - - - - - - - 181.5 -1.6 33.9 - 57 LYS 57 E B - - -62.1 179.5 - - - - - - 180.7 -2.0 34.2 - 58 LEU 58 E B - 190.4 - - - - - - - - 182.8 - 34.8 - 59 ILE 59 E B - - -65.4 185.4 - - - - - - 174.5 -3.1 33.7 - * * 60 SER 60 E B 58.8 - - - - - - - - - 179.3 -1.9 34.9 - 61 ALA 61 T l - - - - - - - - - - 180.4 - 32.9 - 62 GLY 62 T - - - - - - - - - - - 180.3 - - - Residue-by-residue listing for refined_10 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 - - -84.6 - - - - - - - 178.8 -2.1 35.1 - * * 64 VAL 64 E B - 182.6 - - - - - - - - 179.9 - 34.8 - 65 LEU 65 e B - - -70.3 - - - - - - - 181.5 -2.7 31.3 - 66 GLU 66 t B - 203.5 - - - - - - - - 189.4 -.8 36.2 - * +* +* +* 67 ASN 67 T A 74.6 - - - - - - - - - 182.2 - 31.8 - 68 SER 68 T A - - -53.2 - - - - - - - 178.9 - 34.4 - 69 LYS 69 t B - - -73.0 - - - - - - - 176.6 -2.0 34.5 - 70 THR 70 h B - - -41.9 - - - - - - - 180.5 - 36.2 - +* +* 71 VAL 71 H A - 178.6 - - - -63.2 -40.7 - - - 178.4 -2.7 33.8 - 72 LYS 72 H A - 180.4 - 181.0 - -52.8 -33.2 - - - 185.1 -2.7 35.6 - * * 73 ASP 73 H A - 185.3 - - - -67.1 -32.9 - - - 179.1 -.7 32.8 - +* +* 74 TYR 74 H A - - -71.7 - - -99.2 -13.7 - - - 184.2 -1.1 33.7 - +** ** * +** 75 ARG 75 h B - 188.2 - 181.8 - - - - - - 176.4 -1.5 35.3 - 76 SER 76 B - - -56.0 - - - - - - - 176.9 - 36.0 - 77 PRO 77 S - - - - - -73.4 - - - - - 179.6 - 39.2 - +* +* 78 VAL 78 S XX - 173.5 - - - - - - - - 179.0 - 31.2 - **** **** 79 SER 79 b - - -59.0 - - - - - - - 181.1 -2.0 33.8 - 80 ASN 80 a - - -62.2 - - - - - - - 179.0 -1.1 34.7 - * * 81 LEU 81 B - - -62.3 177.0 - - - - - - 180.8 - 36.2 - 82 ALA 82 S b - - - - - - - - - - 182.0 - 33.0 - 83 GLY 83 S - - - - - - - - - - - 178.8 -1.1 - - * * 84 ALA 84 E B - - - - - - - - - - 183.5 -.6 34.7 - +* +* 85 VAL 85 E B - 185.7 - - - - - - - - 178.1 -.6 33.4 - +* +* 86 THR 86 E B - - -55.8 - - - - - - - 176.8 -3.4 36.0 - +* +* 87 THR 87 E B - - -66.6 - - - - - - - 182.2 - 34.3 - 88 MET 88 E B - 180.3 - 173.9 - - - - - - 184.2 -2.6 34.5 - 89 HIS 89 E B - - -63.9 - - - - - - - 176.8 -2.3 33.3 - 90 VAL 90 E B - 179.7 - - - - - - - - 182.7 -1.5 33.8 - 91 ILE 91 E B - - -65.0 - - - - - - - 181.8 -2.9 34.4 - * * 92 ILE 92 B - - -60.7 - - - - - - - 174.9 -.7 34.4 - +* +* 93 GLN 93 B - - -67.0 - - - - - - - 182.7 -.8 33.9 - +* +* 94 ALA 94 B - - - - - - - - - - 180.1 -.6 34.7 - +* +* 95 PRO 95 - - - - - -82.1 - - - - - 178.5 - 38.9 - * * * 96 VAL 96 B - 183.2 - - - - - - - - 182.7 - 33.9 - 97 THR 97 B - 181.6 - - - - - - - - 180.1 -.9 34.3 - +* +* 98 GLU 98 B - 182.6 - 177.6 - - - - - - 181.9 - 35.0 - 99 LYS 99 B - 182.6 - 171.9 - - - - - - 185.9 - 31.2 - * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 GLU 100 B - 178.2 - 182.1 - - - - - - 178.5 - 36.6 - 101 LYS 101 - - 179.6 - 182.8 - - - - - - - - 32.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * +* * +** +** ** +* ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.5 182.8 -62.6 179.1 -73.8 -66.7 -37.3 - - - 179.8 -1.9 34.5 Standard deviations: 9.2 5.8 8.3 7.9 15.5 11.0 9.0 - - - 3.1 .9 1.9 Numbers of values: 8 32 42 20 6 15 15 0 0 0 100 53 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_10 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 - 1.239 1.527 1.538 1.455 - 115.98 120.46 110.84 108.99 109.20 123.49 2 ALA 2 1.333 1.235 1.517 1.519 1.462 123.86 116.28 120.32 109.31 109.81 111.09 123.40 * * 3 GLU 3 1.308 1.238 1.519 1.540 1.436 122.83 116.09 120.83 109.77 111.30 111.65 123.08 * * * 4 VAL 4 1.313 1.240 1.525 1.553 1.446 121.78 116.27 121.06 109.64 109.25 111.58 122.68 * * 5 HIS 5 1.300 1.227 1.512 1.539 1.439 121.96 114.17 122.03 112.15 111.10 112.18 123.69 ** * * ** 6 ASN 6 1.299 1.225 1.503 1.538 1.452 124.08 114.63 121.40 109.92 107.27 111.39 123.94 ** * * * ** 7 GLN 7 1.327 1.242 1.521 1.545 1.447 123.11 117.09 120.67 109.19 109.25 111.08 122.24 8 LEU 8 1.301 1.215 1.509 1.535 1.433 119.84 116.57 120.88 111.32 110.07 112.37 122.54 +* * * * +* 9 GLU 9 1.291 1.206 1.487 1.511 1.423 121.09 116.25 121.10 110.20 109.52 111.38 122.65 +** * +* +* +** 10 ILE 10 1.267 1.243 1.494 1.561 1.426 121.04 115.60 120.82 108.95 109.68 111.52 123.53 **** * +* **** 11 LYS 11 1.289 1.249 1.507 1.538 1.414 120.97 116.37 120.41 109.63 107.82 114.51 123.21 +** ** * ** +** 12 PHE 12 1.287 1.226 1.503 1.526 1.432 121.17 116.98 120.30 110.28 108.76 110.24 122.69 +** * * +** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 ARG 13 1.307 1.240 1.503 1.516 1.418 120.77 115.20 121.07 110.03 110.50 111.78 123.72 +* * ** ** 14 LEU 14 1.291 1.242 1.514 1.536 1.427 123.16 115.78 120.91 109.73 110.62 110.46 123.28 +** +* +** 15 THR 15 1.313 1.235 1.543 1.535 1.444 123.06 116.06 121.13 111.84 112.77 109.62 122.80 * * * * 16 ASP 16 1.323 1.227 1.514 1.531 1.478 122.43 116.46 120.80 109.03 111.94 111.80 122.73 * * 17 GLY 17 1.315 1.234 1.505 - 1.450 120.63 115.34 121.24 - 111.57 - 123.42 * * 18 SER 18 1.301 1.231 1.510 1.523 1.424 122.51 117.74 119.84 110.06 107.60 108.69 122.38 ** +* * * ** 19 ASP 19 1.300 1.235 1.489 1.531 1.410 120.39 114.57 121.35 111.68 112.36 112.39 124.08 ** +* +** * +** 20 ILE 20 1.294 1.240 1.514 1.569 1.426 123.34 115.95 119.72 109.79 107.43 110.07 124.32 +** * +* * +** 21 GLY 21 1.332 1.245 1.520 - 1.455 122.73 117.71 120.29 - 113.23 - 122.00 * * 22 PRO 22 1.338 1.243 1.523 1.528 1.448 122.55 114.71 121.92 109.98 113.87 104.17 123.38 * * * * 23 LYS 23 1.298 1.212 1.490 1.558 1.473 123.39 118.04 119.07 110.37 108.75 115.31 122.88 ** +* * * +** +** 24 ALA 24 1.309 1.238 1.518 1.519 1.449 120.03 115.45 121.10 111.29 111.32 111.20 123.44 * * 25 PHE 25 1.304 1.238 1.504 1.543 1.440 123.68 118.48 120.13 105.99 107.50 111.41 121.34 +* * * ** * * ** 26 PRO 26 1.310 1.238 1.526 1.526 1.446 121.04 116.98 120.42 108.62 109.94 103.79 122.59 +* * +* 27 ASP 27 1.309 1.230 1.524 1.533 1.461 121.72 115.05 121.59 110.93 109.98 111.76 123.34 * * 28 ALA 28 1.319 1.245 1.542 1.523 1.453 123.18 116.61 120.69 110.56 111.21 110.15 122.71 29 THR 29 1.324 1.240 1.531 1.545 1.455 122.02 116.94 120.42 109.52 109.13 110.54 122.63 30 THR 30 1.304 1.244 1.521 1.528 1.425 121.12 116.34 120.75 109.54 110.62 111.11 122.90 +* +* +* 31 VAL 31 1.318 1.228 1.528 1.547 1.447 121.84 116.30 120.71 110.87 110.22 111.64 122.96 32 SER 32 1.329 1.232 1.537 1.533 1.449 121.39 116.31 120.60 110.65 110.05 110.61 123.00 33 ALA 33 1.328 1.232 1.532 1.520 1.457 121.71 116.64 120.81 110.75 110.76 110.29 122.55 34 LEU 34 1.324 1.234 1.532 1.522 1.424 123.15 115.42 121.21 110.78 109.39 107.54 123.33 +* +* +* 35 LYS 35 1.324 1.220 1.520 1.518 1.451 122.83 115.19 120.97 108.05 109.51 109.71 123.84 * * 36 GLU 36 1.325 1.240 1.542 1.525 1.437 125.16 115.72 121.10 111.61 109.23 104.33 123.14 * +* +*** +*** 37 THR 37 1.323 1.225 1.540 1.542 1.438 122.02 116.57 120.47 110.56 109.99 110.75 122.92 * * 38 VAL 38 1.337 1.221 1.526 1.563 1.470 122.33 115.74 120.75 108.77 109.93 111.90 123.48 39 ILE 39 1.327 1.214 1.539 1.571 1.466 122.52 116.27 121.02 109.33 110.01 111.65 122.70 * * 40 SER 40 1.325 1.246 1.551 1.543 1.452 121.60 116.17 120.75 111.02 110.93 109.59 123.07 * * 41 GLU 41 1.334 1.235 1.512 1.516 1.439 123.34 116.30 120.80 110.41 112.14 109.39 122.89 42 TRP 42 1.299 1.223 1.514 1.535 1.427 121.35 118.18 119.72 110.15 107.08 109.82 122.05 ** +* * ** 43 PRO 43 1.339 1.236 1.534 1.524 1.459 122.43 115.81 120.92 110.25 112.86 103.36 123.27 44 ARG 44 1.332 1.230 1.515 1.524 1.468 123.22 115.20 121.34 110.03 111.33 111.66 123.43 Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 GLU 45 1.316 1.233 1.536 1.514 1.448 123.06 116.19 120.94 111.87 111.03 108.86 122.87 46 LYS 46 1.329 1.231 1.512 1.516 1.426 122.53 116.62 120.85 110.14 109.77 109.80 122.53 +* +* 47 GLU 47 1.295 1.227 1.508 1.532 1.415 121.25 116.02 120.25 113.86 109.28 110.57 123.69 ** ** +* ** 48 ASN 48 1.320 1.221 1.510 1.545 1.488 123.59 114.96 121.52 112.29 111.83 113.61 123.51 +* * * +* +* 49 GLY 49 1.294 1.223 1.497 - 1.420 122.48 117.60 120.67 - 107.10 - 121.70 +** * +* * +* +** 50 PRO 50 1.327 1.249 1.530 1.515 1.439 122.53 115.98 120.71 109.09 109.84 101.07 123.30 +* +* +* 51 LYS 51 1.309 1.214 1.513 1.553 1.436 122.61 116.71 120.57 112.38 109.09 112.30 122.69 * * * * * * 52 THR 52 1.296 1.240 1.520 1.526 1.433 122.12 115.81 120.13 110.46 111.27 111.76 124.05 ** * ** 53 VAL 53 1.333 1.236 1.547 1.568 1.476 124.39 114.78 121.47 109.13 110.56 109.47 123.74 * * * * * 54 LYS 54 1.314 1.238 1.541 1.529 1.460 124.73 116.09 120.76 108.65 112.60 107.21 123.15 * +* +* +* 55 GLU 55 1.319 1.236 1.528 1.526 1.466 122.37 116.87 120.65 109.48 113.19 109.67 122.47 56 VAL 56 1.303 1.223 1.526 1.559 1.454 121.20 116.90 120.37 110.59 109.91 111.09 122.71 +* +* 57 LYS 57 1.323 1.235 1.520 1.518 1.444 121.87 115.72 121.09 110.33 111.30 110.13 123.19 58 LEU 58 1.306 1.242 1.549 1.564 1.443 122.65 116.87 120.18 112.87 108.05 108.02 122.95 +* * +* * * * +* 59 ILE 59 1.334 1.233 1.538 1.574 1.466 122.68 115.62 121.65 109.77 112.24 111.39 122.71 * * 60 SER 60 1.307 1.237 1.513 1.531 1.432 122.73 116.92 119.47 110.48 107.58 110.36 123.52 +* * * +* 61 ALA 61 1.333 1.234 1.535 1.531 1.479 123.42 115.46 121.58 111.28 111.12 110.88 122.93 * * 62 GLY 62 1.317 1.228 1.515 - 1.442 121.57 116.86 120.51 - 112.66 - 122.63 63 LYS 63 1.326 1.229 1.506 1.540 1.433 122.56 116.49 120.10 108.92 109.21 111.24 123.41 * * 64 VAL 64 1.303 1.242 1.511 1.555 1.441 122.03 116.34 120.88 108.95 108.37 111.93 122.76 +* * +* 65 LEU 65 1.294 1.232 1.506 1.533 1.411 120.87 114.46 121.36 112.61 110.78 112.49 124.15 +** ** * * +** 66 GLU 66 1.305 1.230 1.544 1.544 1.437 123.67 118.21 119.52 112.54 106.18 106.41 122.26 +* * * * * +* ** ** 67 ASN 67 1.325 1.237 1.524 1.553 1.479 121.40 116.86 120.28 110.42 112.99 112.81 122.82 * * * * 68 SER 68 1.320 1.239 1.543 1.526 1.453 121.76 116.15 121.24 110.93 111.25 109.14 122.61 69 LYS 69 1.317 1.236 1.511 1.521 1.434 122.70 115.24 121.39 109.75 111.68 110.33 123.36 * * 70 THR 70 1.298 1.239 1.536 1.535 1.426 122.36 118.27 119.20 109.25 106.51 109.67 122.53 ** +* * +* * ** 71 VAL 71 1.333 1.232 1.530 1.562 1.477 120.97 114.46 121.65 109.77 109.54 111.96 123.86 72 LYS 72 1.316 1.228 1.541 1.527 1.454 124.93 116.95 120.27 109.57 112.63 108.50 122.78 +* * +* 73 ASP 73 1.331 1.228 1.519 1.532 1.474 121.42 116.60 120.87 110.58 111.99 111.49 122.52 74 TYR 74 1.314 1.237 1.517 1.523 1.443 120.94 116.39 120.64 109.53 111.67 111.51 122.96 * * 75 ARG 75 1.314 1.236 1.523 1.518 1.412 122.14 115.72 120.96 109.65 111.24 109.49 123.32 * ** ** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 76 SER 76 1.301 1.237 1.546 1.524 1.421 122.39 118.63 119.78 110.45 108.89 108.07 121.55 +* +* * * +* 77 PRO 77 1.349 1.245 1.545 1.547 1.473 122.64 116.54 120.71 110.02 111.21 103.22 122.75 78 VAL 78 1.337 1.241 1.528 1.533 1.464 124.65 115.67 121.04 112.40 112.91 111.58 123.28 +* * +* 79 SER 79 1.285 1.235 1.532 1.530 1.443 122.84 115.81 121.10 110.83 110.53 110.51 123.05 *** *** 80 ASN 80 1.319 1.231 1.515 1.541 1.456 122.39 116.63 120.89 108.77 110.25 111.50 122.48 81 LEU 81 1.320 1.239 1.522 1.490 1.402 122.53 115.49 121.47 109.34 110.97 108.28 123.03 +* +** * +** 82 ALA 82 1.291 1.233 1.498 1.522 1.406 122.75 114.78 121.53 111.76 108.67 111.60 123.55 +** * +** +** 83 GLY 83 1.292 1.229 1.507 - 1.434 121.13 116.04 120.87 - 110.84 - 123.06 +** * +** 84 ALA 84 1.312 1.224 1.501 1.521 1.451 121.78 117.07 119.92 110.12 108.43 110.60 123.01 * * * 85 VAL 85 1.301 1.232 1.522 1.552 1.438 120.82 115.24 121.29 109.80 110.56 112.40 123.44 +* * +* 86 THR 86 1.293 1.244 1.537 1.550 1.422 124.16 116.60 120.62 109.23 108.71 109.78 122.77 +** +* * * +** 87 THR 87 1.302 1.228 1.520 1.539 1.428 121.88 115.49 121.26 110.64 109.37 110.62 123.23 +* +* +* 88 MET 88 1.298 1.229 1.516 1.519 1.427 122.52 117.28 120.07 112.69 108.88 108.23 122.58 ** +* * * ** 89 HIS 89 1.311 1.233 1.507 1.536 1.445 121.03 115.19 121.43 110.48 112.06 111.23 123.37 * * 90 VAL 90 1.297 1.232 1.489 1.553 1.439 122.13 115.02 121.09 110.35 107.84 112.39 123.86 ** +* * * ** 91 ILE 91 1.278 1.250 1.500 1.530 1.408 122.43 114.41 121.72 111.33 109.87 109.81 123.87 +*** * +** * +*** 92 ILE 92 1.291 1.232 1.520 1.555 1.415 122.41 115.47 121.33 110.31 110.20 110.87 123.13 +** ** +** 93 GLN 93 1.298 1.224 1.490 1.538 1.429 122.32 115.50 120.38 110.86 107.27 111.73 124.08 ** +* +* * ** 94 ALA 94 1.302 1.242 1.518 1.513 1.441 122.43 117.48 120.41 110.21 110.83 109.67 122.11 +* +* 95 PRO 95 1.330 1.242 1.515 1.521 1.441 122.14 116.06 120.94 110.15 111.62 103.50 123.00 +* +* 96 VAL 96 1.302 1.238 1.520 1.545 1.435 121.48 116.11 121.15 110.01 108.75 112.09 122.73 +* * +* 97 THR 97 1.296 1.232 1.499 1.574 1.410 122.77 115.72 120.85 110.55 107.75 111.91 123.43 ** * * +** * +** 98 GLU 98 1.266 1.248 1.528 1.516 1.413 122.38 118.20 118.90 114.36 106.85 106.29 122.85 **** ** * ** +* ** **** 99 LYS 99 1.321 1.237 1.516 1.522 1.434 121.27 114.68 121.56 112.48 111.54 112.12 123.76 * * * 100 GLU 100 1.300 1.235 1.517 1.523 1.417 123.39 116.25 119.50 110.76 109.34 107.03 124.24 ** ** ** ** 101 LYS 101 1.336 - 1.535 1.541 1.471 123.55 - - 111.70 111.80 111.51 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +* +** +* * * ** +* +*** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 9 ---------------------------------------- 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 1.266 1.337 1.310 .016 **** * C-N (Pro) 1.341 .016 6 1.310 1.349 1.332 .012 +* C-O C-O 1.231 .020 100 1.206 1.250 1.234 .008 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.487 1.551 1.521 .015 +* * CH2G*-C (Gly) 1.516 .018 5 1.497 1.520 1.509 .008 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.513 1.531 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.526 1.574 1.551 .014 * CH1E-CH2E (the rest) 1.530 .020 62 1.490 1.564 1.530 .012 +* +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.402 1.488 1.441 .020 +** +* NH1-CH2G* (Gly) 1.451 .016 5 1.420 1.455 1.440 .012 +* N-CH1E (Pro) 1.466 .015 6 1.439 1.473 1.451 .012 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 10 ---------------------------------------- +-----------------+ | 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 89 114.17 118.63 116.15 .98 * * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.34 117.71 116.71 .91 CH1E-C-N (Pro) 116.9 1.5 6 114.71 116.98 116.01 .70 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.34 124.32 123.06 .59 * O-C-N (Pro) 122.0 1.4 6 122.59 123.38 123.05 .30 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.84 125.16 122.36 1.08 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.63 122.73 121.71 .79 * C-N-CH1E (Pro) 122.6 5.0 6 121.04 122.64 122.22 .55 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.90 122.03 120.76 .63 * CH2G*-C-O (Gly) 120.8 2.1 5 120.29 121.24 120.71 .32 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 109.31 111.76 110.66 .74 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.77 112.40 110.05 .88 * CH2E-CH1E-C (the rest) 110.1 1.9 62 105.99 114.36 110.51 1.39 ** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 106.18 113.19 110.00 1.63 +* NH1-CH2G*-C (Gly) 112.5 2.9 5 107.10 113.23 111.08 2.16 +* N-CH1E-C (Pro) 111.8 2.5 6 109.84 113.87 111.56 1.46 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.67 111.60 110.68 .59 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.47 112.40 111.12 .90 * N-CH1E-CH2E (Pro) 103.0 1.1 6 101.07 104.17 103.18 1.00 +* * NH1-CH1E-CH2E (the rest) 110.5 1.7 56 104.33 115.31 110.37 2.05 +*** +** ------------------------------------------------------------------------------------------------------------- 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_10 Page 11 ---------------------------------------- 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] 8 9.1% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% 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 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 53 .9 .8 .2 .3 Inside f. Overall G-factor 101 .0 -.4 .3 1.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 8 9.2 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 32 5.8 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 42 8.3 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 82 8.1 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 20 7.9 20.4 5.0 -2.5 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 3 Residue-by-residue listing for refined_10 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.52 Chi1-chi2 distribution -.12 Chi1 only .26 Chi3 & chi4 .30 Omega .16 ------ -.07 ===== Main-chain covalent forces:- Main-chain bond lengths -.12 Main-chain bond angles .40 ------ .19 ===== OVERALL AVERAGE .01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.