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 MET 1 - - 179.6 - 180.7 - - - - - - 180.0 - 34.4 - 2 ALA 2 b - - - - - - - - - - 177.1 - 32.5 - 3 ASP 3 b - 180.4 - - - - - - - - 175.6 - 32.8 - 4 THR 4 A - - -52.7 - - - - - - - 178.7 - 34.7 - 5 GLY 5 - - - - - - - - - - - 176.2 - - - 6 GLU 6 S B 57.8 - - - - - - - - - 186.4 - 32.4 - * * 7 VAL 7 E B - - -62.9 - - - - - - - 176.0 -1.6 32.4 - 8 GLN 8 E B 58.9 - - 178.3 - - - - - - 180.2 - 34.7 - 9 PHE 9 E B 50.6 - - - - - - - - - 179.7 -2.1 33.7 - 10 MET 10 E B 59.3 - - 176.9 - - - - - - 177.7 - 33.1 - 11 LYS 11 E B 48.3 - - - - - - - - - 176.2 -1.2 31.3 - * * * 12 PRO 12 - - - - - -70.4 - - - - - 180.4 - 38.6 - * * 13 PHE 13 B 57.3 - - - - - - - - - 180.0 - 33.8 - 14 ILE 14 h B - - -59.4 180.8 - - - - - - 186.2 - 33.4 - * * 15 SER 15 H A - 186.5 - - - -64.2 -11.9 - - - 174.4 -.6 32.8 - ** +* ** 16 GLU 16 H A - 181.6 - 186.1 - -60.7 -37.4 - - - 180.7 - 36.9 - 17 LYS 17 H a - 187.0 - - - -110.9 -41.3 - - - 186.1 -2.3 34.9 - +*** * +*** 18 SER 18 H A - 182.5 - - - -63.8 -9.7 - - - 176.9 -3.3 33.3 - +** +* +** 19 SER 19 h A 48.8 - - - - - - - - - 182.2 -.8 33.5 - +* +* 20 LYS 20 T a - 184.1 - 179.8 - - - - - - 181.0 -2.6 34.9 - 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 SER 21 t B - - -57.4 - - - - - - - 180.6 -2.8 35.2 - * * 22 LEU 22 E B - 183.9 - - - - - - - - 178.7 -2.5 35.1 - 23 GLU 23 E B 68.3 - - - - - - - - - 179.6 - 31.5 - 24 ILE 24 e B - - -62.9 - - - - - - - 177.6 -1.6 33.3 - 25 PRO 25 t - - - - - -70.7 - - - - - 180.8 - 39.3 - +* +* 26 LEU 26 T A - - -68.1 - - - - - - - 175.2 - 30.7 - 27 GLY 27 g - - - - - - - - - - - 180.2 - - - 28 PHE 28 G A - 180.8 - - - - - - - - 182.5 -.8 34.9 - +* +* 29 ASN 29 G A - 183.8 - - - - - - - - 181.6 -1.0 34.0 - * * 30 GLU 30 G A - 190.0 - - - - - - - - 180.1 -.6 33.2 - +* +* 31 TYR 31 G A - - -58.9 - - - - - - - 184.6 -1.3 35.0 - 32 PHE 32 g B - 195.6 - - - - - - - - 182.2 -.9 35.9 - +* +* 33 PRO 33 - - - - - -63.7 - - - - - 178.6 - 38.0 - * * 34 ALA 34 S A - - - - - - - - - - 176.1 - 32.6 - 35 PRO 35 S - - - - - -70.1 - - - - - 179.5 - 38.8 - * * 36 PHE 36 B - - -62.5 - - - - - - - 176.2 - 35.4 - 37 PRO 37 - - - - - -83.2 - - - - - 180.7 - 38.6 - +* * +* 38 ILE 38 e a - - -57.3 - - - - - - - 179.0 - 32.6 - 39 THR 39 E B 47.7 - - - - - - - - - 175.1 - 34.2 - * * 40 VAL 40 E B - 178.1 - - - - - - - - 180.6 -2.9 35.1 - * * 41 ASP 41 E B - - -74.1 - - - - - - - 179.5 -2.7 31.8 - 42 LEU 42 E B - - -60.2 180.2 - - - - - - 178.8 -2.7 34.7 - 43 LEU 43 E B - - -59.0 180.6 - - - - - - 175.9 -2.5 35.2 - 44 ASP 44 E B - 169.1 - - - - - - - - 184.0 -.8 33.2 - +* +* 45 TYR 45 e XX - - -57.8 - - - - - - - 181.7 -.6 30.6 - **** +* **** 46 SER 46 S B - - -58.7 - - - - - - - 172.3 -.9 35.7 - * +* +* 47 GLY 47 S - - - - - - - - - - - 185.0 - - - 48 ARG 48 e B - 182.4 - - - - - - - - 180.0 -2.1 33.2 - 49 SER 49 E B - - -55.0 - - - - - - - 177.5 - 36.3 - 50 TRP 50 E B - - -57.0 - - - - - - - 176.2 -2.3 36.8 - 51 THR 51 E B - - -57.1 - - - - - - - 184.8 - 34.0 - 52 VAL 52 E B - - -57.5 - - - - - - - 175.7 -3.1 34.0 - * * 53 ARG 53 E B - - -62.0 190.7 - - - - - - 184.5 -3.0 31.3 - * * 54 MET 54 E B - - -62.1 - - - - - - - 178.4 -1.7 36.0 - 55 LYS 55 E B - - -62.0 178.7 - - - - - - 173.5 -2.3 34.9 - * * 56 LYS 56 E B - - -57.5 183.4 - - - - - - 182.1 - 35.2 - 57 ARG 57 e B - 186.1 - - - - - - - - 178.7 -1.0 34.4 - * * 58 GLY 58 S - - - - - - - - - - - 184.4 - - - 59 GLU 59 S A - - -57.7 - - - - - - - 181.2 - 34.7 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 60 LYS 60 e B - 186.3 - 179.6 - - - - - - 179.6 - 34.9 - 61 VAL 61 E B - 183.0 - - - - - - - - 178.5 - 34.9 - 62 PHE 62 E B - - -67.9 - - - - - - - 175.6 -2.7 33.1 - 63 LEU 63 E B - 191.8 - 171.6 - - - - - - 194.4 -1.9 35.3 - ** ** 64 THR 64 e a 52.6 - - - - - - - - - 184.8 -1.5 33.5 - 65 VAL 65 T B 55.8 - - - - - - - - - 184.4 - 32.8 - 66 GLY 66 h - - - - - - - - - - - 176.2 - - - 67 TRP 67 H A - 174.7 - - - -65.0 -28.5 - - - 182.9 -.6 36.6 - +* +* 68 GLU 68 H A - 191.7 - 175.2 - -68.3 -28.4 - - - 175.1 - 32.6 - 69 ASN 69 H A - - -62.1 - - -71.5 -35.2 - - - 181.6 -.7 34.2 - +* +* 70 PHE 70 H A - 182.0 - - - -74.4 -45.6 - - - 180.0 -1.1 33.0 - * * 71 VAL 71 H A 70.1 - - - - -63.8 -40.9 - - - 177.6 -3.5 33.2 - +* +* 72 LYS 72 H A - - -64.1 - - -71.1 -33.5 - - - 184.6 -1.8 32.3 - 73 ASP 73 H A - 190.3 - - - -76.2 -41.5 - - - 181.4 -1.6 33.1 - 74 ASN 74 H A - - -66.7 - - -107.6 14.6 - - - 178.8 -2.6 31.6 - +*** *4.8* *4.8* 75 ASN 75 h XX - 182.8 - - - - - - - - 176.1 -.5 31.3 - **** ** **** 76 LEU 76 l - - -76.4 - - - - - - - 177.1 -2.2 27.8 - +* +* 77 GLU 77 t B - 183.0 - 180.6 - - - - - - 179.3 - 33.4 - 78 ASP 78 T B - 175.7 - - - - - - - - 184.4 - 34.4 - 79 GLY 79 T - - - - - - - - - - - 174.9 - - - 80 LYS 80 t B - - -55.6 - - - - - - - 182.4 -2.2 34.6 - 81 TYR 81 e B - - -57.7 - - - - - - - 181.9 - 33.9 - 82 LEU 82 E B - - -58.2 179.5 - - - - - - 173.7 -.6 36.6 - * +* +* 83 GLN 83 E B - 189.0 - 183.1 - - - - - - 180.1 -1.5 35.2 - 84 PHE 84 E B - - -65.1 - - - - - - - 178.9 -3.2 34.5 - +* +* 85 ILE 85 E B - - -56.3 178.7 - - - - - - 180.1 -2.0 33.9 - 86 TYR 86 E B - 176.6 - - - - - - - - 181.8 -3.4 34.3 - +* +* 87 ASP 87 S a 65.7 - - - - - - - - - 182.3 -.6 35.0 - +* +* 88 ARG 88 S l - - -60.5 - - - - - - - 180.3 - 31.9 - 89 ASP 89 S b - 189.9 - - - - - - - - 178.8 - 35.4 - 90 ARG 90 e A 38.3 - - - - - - - - - 177.1 - 32.1 - +* +* 91 THR 91 E B - - -57.2 - - - - - - - 177.7 - 34.6 - 92 PHE 92 E B - - -66.8 - - - - - - - 176.6 -2.8 34.7 - 93 TYR 93 E B - 180.4 - - - - - - - - 180.8 -1.1 33.7 - * * 94 VAL 94 E B - 185.0 - - - - - - - - 175.1 -3.0 35.7 - * * 95 ILE 95 E B - 181.9 - 179.8 - - - - - - 179.6 -1.3 33.1 - * * 96 ILE 96 E B - - -51.1 - - - - - - - 176.5 - 36.9 - * * 97 TYR 97 e B - - -75.2 - - - - - - - 187.8 -2.5 31.7 - * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 GLY 98 S - - - - - - - - - - - 176.2 -.7 - - +* +* 99 HIS 99 b - 192.0 - - - - - - - - 181.7 -.6 34.5 - +* +* 100 ASN 100 b - 178.7 - - - - - - - - 179.8 - 34.4 - 101 MET 101 B - 190.3 - - - - - - - - 178.8 - 33.9 - 102 CYS 102 - - 180.6 - - - - - - - - - -.9 34.8 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* * +* +*** *4.8* ** ** +* *4.8* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 55.7 183.8 -61.1 180.2 -71.6 -74.8 -28.3 - - - 179.7 -1.8 34.1 Standard deviations: 8.8 5.6 5.8 4.0 7.1 16.8 17.6 - - - 3.5 .9 1.9 Numbers of values: 14 36 38 19 5 12 12 0 0 0 101 57 95 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 MET 1 - 1.226 1.510 1.539 1.459 - 116.90 120.34 110.09 109.53 110.82 122.74 2 ALA 2 1.312 1.242 1.505 1.523 1.445 121.07 115.14 121.06 110.88 111.16 112.13 123.69 * * * 3 ASP 3 1.314 1.238 1.501 1.533 1.446 122.77 115.78 121.15 109.60 110.96 113.09 123.03 * * +* +* 4 THR 4 1.303 1.229 1.547 1.552 1.436 121.78 115.14 121.73 111.23 108.18 109.75 123.08 +* * * * * +* 5 GLY 5 1.330 1.241 1.497 - 1.438 122.09 116.18 120.43 - 111.94 - 123.39 * * 6 GLU 6 1.305 1.234 1.516 1.566 1.434 121.82 116.43 121.23 112.25 107.90 112.57 122.31 +* +* * * * * +* 7 VAL 7 1.287 1.233 1.502 1.557 1.432 120.13 115.00 121.47 110.45 112.07 112.80 123.51 *** * * *** 8 GLN 8 1.289 1.243 1.505 1.535 1.415 122.31 116.23 120.41 110.58 107.63 110.75 123.34 +** ** * +** 9 PHE 9 1.290 1.227 1.504 1.552 1.436 122.45 117.02 120.44 111.50 109.55 110.82 122.53 +** * * * +** 10 MET 10 1.286 1.233 1.496 1.540 1.430 120.80 115.59 120.99 110.62 110.51 112.05 123.42 *** * * *** 11 LYS 11 1.298 1.229 1.507 1.582 1.427 122.37 117.97 120.23 113.59 109.89 112.21 121.69 ** +** +* +* * +** 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 PRO 12 1.327 1.241 1.507 1.527 1.443 121.72 116.11 120.74 109.98 109.69 104.57 123.13 +* * +* 13 PHE 13 1.276 1.240 1.504 1.539 1.425 121.72 116.78 120.53 111.71 108.83 110.48 122.66 +*** +* +*** 14 ILE 14 1.292 1.230 1.516 1.561 1.426 120.38 116.53 120.38 111.84 107.87 111.49 123.09 +** +* * * +** 15 SER 15 1.328 1.229 1.539 1.530 1.470 123.16 115.37 121.32 112.09 111.91 109.92 123.31 * * 16 GLU 16 1.308 1.238 1.532 1.528 1.442 124.04 115.80 121.52 109.30 108.50 108.02 122.67 +* * * +* 17 LYS 17 1.328 1.243 1.513 1.541 1.443 120.66 115.11 120.79 109.94 109.66 110.28 123.95 18 SER 18 1.333 1.223 1.526 1.534 1.457 123.99 117.41 120.09 111.10 112.99 110.07 122.49 * * 19 SER 19 1.314 1.240 1.540 1.525 1.448 121.01 115.81 121.61 111.82 110.86 109.66 122.58 * * 20 LYS 20 1.317 1.231 1.532 1.526 1.439 121.66 116.81 120.55 110.91 111.05 108.76 122.64 * * 21 SER 21 1.323 1.217 1.528 1.538 1.455 122.23 117.47 120.08 110.00 109.56 109.59 122.45 22 LEU 22 1.308 1.250 1.506 1.528 1.454 121.06 117.16 120.03 108.70 109.15 111.22 122.81 +* +* 23 GLU 23 1.314 1.243 1.525 1.551 1.421 119.55 116.06 121.20 111.78 109.79 113.45 122.69 * * +* * +* +* 24 ILE 24 1.308 1.237 1.524 1.555 1.435 121.40 117.15 120.46 110.67 110.38 111.73 122.36 +* * +* 25 PRO 25 1.343 1.237 1.520 1.541 1.455 122.50 116.98 120.54 109.42 110.34 104.01 122.47 26 LEU 26 1.310 1.228 1.521 1.543 1.452 120.99 116.57 120.66 112.06 111.53 113.31 122.75 * * +* +* 27 GLY 27 1.326 1.225 1.523 - 1.449 120.35 115.66 121.25 - 110.77 - 123.05 28 PHE 28 1.327 1.226 1.526 1.544 1.459 122.62 115.59 120.90 110.71 109.78 109.31 123.45 29 ASN 29 1.334 1.224 1.529 1.546 1.475 123.15 116.72 121.04 110.22 111.61 110.47 122.20 30 GLU 30 1.322 1.232 1.530 1.531 1.454 120.82 115.20 121.93 111.63 110.38 110.61 122.80 31 TYR 31 1.289 1.235 1.524 1.540 1.452 122.23 115.24 121.46 109.85 109.11 110.31 123.29 +** +** 32 PHE 32 1.312 1.238 1.544 1.535 1.434 122.96 118.77 119.65 111.45 108.34 107.44 121.56 * * * * +* +* 33 PRO 33 1.351 1.252 1.531 1.529 1.464 122.42 114.56 121.75 109.59 114.06 104.74 123.67 * +* +* * +* 34 ALA 34 1.316 1.225 1.542 1.522 1.451 123.68 120.15 119.11 111.09 112.07 111.19 120.75 * +* * +* 35 PRO 35 1.380 1.243 1.536 1.536 1.471 121.49 116.85 120.75 110.13 111.14 103.61 122.39 ** ** 36 PHE 36 1.309 1.240 1.526 1.527 1.426 121.61 118.09 120.28 109.49 110.24 109.80 121.61 * +* +* 37 PRO 37 1.337 1.240 1.523 1.529 1.445 121.97 116.95 120.62 110.91 109.96 103.51 122.41 * * 38 ILE 38 1.306 1.219 1.511 1.554 1.434 119.98 117.18 120.14 111.17 109.25 112.74 122.62 +* * +* 39 THR 39 1.311 1.240 1.518 1.545 1.435 120.56 114.54 121.24 109.37 111.83 111.32 124.23 * * * 40 VAL 40 1.306 1.228 1.526 1.575 1.445 125.29 118.12 119.85 109.51 105.90 111.84 122.00 +* * +* +* +* 41 ASP 41 1.297 1.238 1.499 1.527 1.454 120.22 115.38 121.20 111.06 112.43 112.34 123.42 ** * * ** 42 LEU 42 1.308 1.244 1.511 1.536 1.443 122.46 116.16 120.66 109.34 109.40 111.16 123.17 +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 LEU 43 1.304 1.203 1.505 1.535 1.444 121.74 116.01 120.14 108.86 109.54 110.89 123.85 +* * +* 44 ASP 44 1.297 1.240 1.502 1.536 1.461 124.34 115.55 119.98 110.56 108.78 112.34 124.47 ** * * * ** 45 TYR 45 1.324 1.243 1.536 1.544 1.468 125.12 116.65 120.78 110.76 112.75 113.96 122.54 +* ** ** 46 SER 46 1.325 1.240 1.521 1.549 1.446 123.37 116.16 120.47 108.74 109.42 110.51 123.32 47 GLY 47 1.311 1.230 1.510 - 1.440 121.25 116.59 120.46 - 114.72 - 122.94 * * 48 ARG 48 1.319 1.234 1.530 1.535 1.460 121.39 115.89 121.24 110.62 111.15 111.27 122.85 49 SER 49 1.309 1.226 1.531 1.521 1.437 122.26 116.60 120.46 109.59 109.91 108.29 122.91 * * * * 50 TRP 50 1.310 1.242 1.518 1.515 1.424 123.24 116.23 120.66 108.82 110.11 108.36 123.10 * +* * +* 51 THR 51 1.298 1.241 1.524 1.540 1.427 121.56 116.08 121.15 111.14 107.92 110.93 122.74 ** +* * ** 52 VAL 52 1.301 1.232 1.510 1.558 1.434 121.61 116.33 120.81 109.78 110.95 111.59 122.82 ** * ** 53 ARG 53 1.301 1.249 1.503 1.527 1.425 120.90 115.21 121.12 111.64 110.59 113.35 123.66 +* * +* +* +* 54 MET 54 1.298 1.230 1.496 1.526 1.442 122.17 116.48 120.59 108.45 110.34 109.89 122.92 ** * ** 55 LYS 55 1.316 1.241 1.510 1.540 1.438 121.09 116.23 120.91 109.47 110.19 110.64 122.85 * * 56 LYS 56 1.306 1.232 1.492 1.508 1.430 121.10 116.13 120.79 107.94 106.94 112.31 123.06 +* +* * * * +* * +* 57 ARG 57 1.268 1.233 1.503 1.542 1.429 121.17 115.90 120.80 110.71 109.16 110.64 123.23 **** * +* **** 58 GLY 58 1.295 1.240 1.493 - 1.421 120.39 115.95 120.57 - 112.26 - 123.45 ** * +* ** 59 GLU 59 1.306 1.233 1.526 1.531 1.442 121.80 116.39 120.73 110.37 111.25 109.52 122.88 +* +* 60 LYS 60 1.309 1.238 1.530 1.538 1.442 121.89 116.27 120.63 110.84 109.51 109.31 123.09 * * 61 VAL 61 1.312 1.238 1.528 1.560 1.445 122.27 116.70 120.46 109.71 109.04 110.82 122.82 * * 62 PHE 62 1.311 1.246 1.513 1.538 1.443 121.77 115.07 121.46 110.44 111.31 111.84 123.46 * * 63 LEU 63 1.304 1.227 1.525 1.548 1.436 122.85 116.75 120.35 112.87 104.28 108.28 122.89 +* * * ** * ** 64 THR 64 1.308 1.226 1.538 1.538 1.450 120.77 116.33 121.13 110.57 115.92 109.25 122.53 * +* * +* 65 VAL 65 1.303 1.233 1.530 1.556 1.446 122.36 116.07 120.88 112.51 111.00 110.40 123.02 +* +* +* 66 GLY 66 1.321 1.230 1.490 - 1.446 121.92 113.88 122.03 - 109.33 - 124.07 * * * * 67 TRP 67 1.315 1.220 1.487 1.528 1.429 124.50 115.25 121.23 108.77 108.74 109.38 123.48 * +* +* +* +* 68 GLU 68 1.309 1.215 1.537 1.521 1.422 120.61 116.02 121.33 112.95 109.03 110.65 122.55 * +* +* +* 69 ASN 69 1.323 1.225 1.509 1.538 1.457 121.92 115.53 121.04 109.73 109.61 111.38 123.42 70 PHE 70 1.313 1.240 1.525 1.544 1.450 122.94 116.16 120.64 112.28 110.82 110.19 123.18 * * * 71 VAL 71 1.331 1.208 1.521 1.574 1.455 122.05 116.11 121.31 110.64 109.62 112.37 122.58 * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.305 1.230 1.513 1.532 1.443 120.78 117.65 120.08 110.59 112.00 112.38 122.26 +* * +* 73 ASP 73 1.333 1.236 1.536 1.535 1.470 118.51 117.47 120.19 109.97 112.64 111.46 122.31 +* +* 74 ASN 74 1.323 1.238 1.528 1.545 1.464 120.75 116.39 120.39 111.34 112.51 112.29 123.21 * * 75 ASN 75 1.335 1.236 1.520 1.536 1.501 124.75 115.25 120.77 111.26 112.70 112.48 123.97 ** +* * ** 76 LEU 76 1.309 1.237 1.520 1.522 1.497 123.41 117.19 120.82 110.63 116.58 115.41 121.85 * ** +* +** +** 77 GLU 77 1.277 1.245 1.516 1.523 1.432 119.70 115.38 120.36 111.46 109.35 110.96 124.25 +*** * * +*** 78 ASP 78 1.325 1.239 1.512 1.537 1.467 123.29 115.65 120.74 109.73 109.92 111.03 123.61 79 GLY 79 1.301 1.234 1.498 - 1.430 121.20 115.41 121.22 - 109.79 - 123.36 +* * * +* 80 LYS 80 1.319 1.234 1.521 1.542 1.444 121.91 117.82 119.80 110.10 107.14 111.27 122.38 * * 81 TYR 81 1.317 1.241 1.516 1.544 1.456 121.03 116.48 119.94 110.84 110.19 110.64 123.58 82 LEU 82 1.330 1.240 1.511 1.541 1.460 122.55 116.23 120.38 106.80 109.97 110.74 123.38 +* +* 83 GLN 83 1.307 1.229 1.515 1.526 1.446 121.84 116.94 119.89 108.66 107.11 111.63 123.17 +* * +* 84 PHE 84 1.302 1.238 1.508 1.539 1.443 122.02 116.46 120.71 109.85 109.35 111.15 122.80 +* +* 85 ILE 85 1.299 1.241 1.525 1.552 1.440 121.13 116.08 120.63 110.29 109.49 111.53 123.27 ** ** 86 TYR 86 1.317 1.232 1.525 1.542 1.440 121.89 115.58 121.24 111.18 110.04 109.75 123.15 87 ASP 87 1.309 1.230 1.519 1.544 1.462 123.00 114.72 121.18 109.75 109.54 110.27 124.01 * * 88 ARG 88 1.332 1.239 1.506 1.561 1.482 125.01 116.89 120.14 108.29 110.77 115.71 122.95 +* * +* *** *** 89 ASP 89 1.318 1.238 1.526 1.553 1.420 122.01 116.28 120.37 111.08 107.16 109.37 123.34 * ** * ** 90 ARG 90 1.287 1.229 1.523 1.559 1.456 124.17 115.24 121.89 112.45 111.02 111.30 122.87 +** * * * +** 91 THR 91 1.298 1.235 1.526 1.546 1.425 122.31 116.21 120.52 110.30 109.25 110.59 123.23 ** +* ** 92 PHE 92 1.304 1.244 1.503 1.540 1.442 122.33 116.54 120.48 109.15 109.28 111.56 122.97 +* * +* 93 TYR 93 1.301 1.242 1.497 1.534 1.430 120.37 115.82 120.51 110.54 108.10 112.04 123.66 ** * * * ** 94 VAL 94 1.297 1.231 1.508 1.567 1.420 122.14 116.50 120.42 109.36 107.37 110.84 123.00 ** +* * ** 95 ILE 95 1.282 1.255 1.512 1.573 1.422 121.39 116.02 120.55 111.12 108.23 112.73 123.41 *** * * +* * *** 96 ILE 96 1.298 1.238 1.521 1.567 1.434 121.71 117.02 120.27 107.03 107.75 111.05 122.72 ** * * * ** 97 TYR 97 1.315 1.235 1.492 1.526 1.444 120.28 113.89 121.68 111.91 109.59 112.93 124.41 * +* * * +* 98 GLY 98 1.300 1.237 1.492 - 1.411 122.57 116.81 119.79 - 106.90 - 123.33 ** * ** * +* ** 99 HIS 99 1.308 1.229 1.507 1.539 1.447 122.08 116.73 119.44 110.71 107.58 110.70 123.81 * * * 100 ASN 100 1.333 1.248 1.518 1.530 1.486 122.39 116.08 120.59 108.65 111.53 111.32 123.33 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 MET 101 1.311 1.252 1.517 1.550 1.438 121.70 115.06 121.33 111.78 108.13 110.54 123.51 * * * * * * 102 CYS 102 1.299 - 1.515 1.533 1.425 122.94 - - 111.03 107.78 109.91 - ** +* * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* +** ** +* +* +* ** *** * **** ----------------------------------------------------------------------------------------------------------------------------------- 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 96 1.268 1.335 1.309 .014 **** * C-N (Pro) 1.341 .016 5 1.327 1.380 1.348 .018 ** C-O C-O 1.231 .020 101 1.203 1.255 1.235 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.487 1.547 1.518 .013 +* * CH2G*-C (Gly) 1.516 .018 7 1.490 1.523 1.500 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.522 1.523 1.523 .001 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.538 1.575 1.557 .011 * CH1E-CH2E (the rest) 1.530 .020 75 1.508 1.582 1.537 .011 * +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.415 1.501 1.445 .017 ** ** NH1-CH2G* (Gly) 1.451 .016 7 1.411 1.449 1.433 .013 ** * N-CH1E (Pro) 1.466 .015 5 1.443 1.471 1.456 .011 +* ------------------------------------------------------------------------------------------------------------- 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 89 113.89 120.15 116.27 .95 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 113.88 116.81 115.78 .90 * CH1E-C-N (Pro) 116.9 1.5 5 114.56 116.98 116.29 .92 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.75 124.47 123.03 .62 * O-C-N (Pro) 122.0 1.4 5 122.39 123.67 122.82 .51 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.51 125.29 121.99 1.29 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 7 120.35 122.57 121.40 .78 * C-N-CH1E (Pro) 122.6 5.0 5 121.49 122.50 122.02 .39 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.11 121.93 120.71 .54 CH2G*-C-O (Gly) 120.8 2.1 7 119.79 122.03 120.82 .68 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.88 111.09 110.99 .10 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.03 112.51 110.37 1.16 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 106.80 113.59 110.45 1.26 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.28 116.58 109.89 1.88 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 106.90 114.72 110.81 2.30 +* N-CH1E-C (Pro) 111.8 2.5 5 109.69 114.06 111.04 1.59 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 111.19 112.13 111.66 .47 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.25 112.80 111.32 .96 * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.51 104.74 104.09 .50 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.44 115.71 110.98 1.57 +* *** ------------------------------------------------------------------------------------------------------------- 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] 12 13.6% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 2 2.3% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 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 101 3.5 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 57 .9 .8 .2 .5 Inside f. Overall G-factor 102 .0 -.4 .3 1.2 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 14 8.8 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 36 5.6 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 38 5.8 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 88 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 19 4.0 20.4 5.0 -3.3 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 8.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .95 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 -.59 Chi1-chi2 distribution -.11 Chi1 only -.07 Chi3 & chi4 .48 Omega .03 ------ -.14 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .40 ------ .21 ===== OVERALL AVERAGE -.02 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.