Residue-by-residue listing for refined_4 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 - - - -57.6 180.7 - - - - - - 180.6 - 34.7 - 2 ALA 2 L - - - - - - - - - - 184.9 - 33.1 - 3 GLU 3 B - 181.5 - 184.5 - - - - - - 177.7 - 35.5 - 4 VAL 4 t B - 186.5 - - - - - - - - 186.3 -.5 34.0 - * ** ** 5 HIS 5 T A - 190.9 - - - - - - - - 175.7 - 33.8 - 6 ASN 6 T A - 191.3 - - - - - - - - 176.5 - 35.1 - 7 GLN 7 t b - - -72.9 - - - - - - - 180.8 -1.3 34.1 - 8 LEU 8 E B - - -58.3 - - - - - - - 180.4 -2.1 35.0 - 9 GLU 9 E B - - -58.8 184.9 - - - - - - 182.1 -.6 32.0 - +* +* 10 ILE 10 E B - - -56.5 176.9 - - - - - - 173.2 -2.4 35.7 - * * 11 LYS 11 E B 61.2 - - 158.3 - - - - - - 182.1 -2.6 32.0 - * * 12 PHE 12 E B - - -55.9 - - - - - - - 181.2 -.6 35.3 - +* +* 13 ARG 13 E B - 184.9 - 176.3 - - - - - - 179.6 -3.1 33.2 - * * 14 LEU 14 E B - - -68.0 - - - - - - - 179.9 -3.5 35.3 - +* +* 15 THR 15 e A 44.9 - - - - - - - - - 178.2 -1.3 34.5 - * * * 16 ASP 16 T A - - -64.7 - - - - - - - 179.0 - 33.5 - 17 GLY 17 t - - - - - - - - - - - 178.7 -1.9 - - 18 SER 18 e B - - -56.1 - - - - - - - 177.1 - 36.7 - 19 ASP 19 E B 70.0 - - - - - - - - - 179.2 -.6 32.9 - +* +* Residue-by-residue listing for refined_4 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 ILE 20 E B - - -56.6 178.6 - - - - - - 179.6 -2.9 35.6 - * * 21 GLY 21 E - - - - - - - - - - - 184.5 - - - 22 PRO 22 E - - - - - -67.0 - - - - - 181.5 - 37.0 - 23 LYS 23 E B - - -45.7 - - - - - - - 182.2 -2.8 36.3 - * * * 24 ALA 24 E B - - - - - - - - - - 180.5 - 33.3 - 25 PHE 25 E B - - -55.6 - - - - - - - 170.4 -3.3 36.0 - +* +* +* 26 PRO 26 t - - - - - -59.7 - - - - - 178.4 - 39.9 - +* +* 27 ASP 27 T A 61.3 - - - - - - - - - 181.5 - 34.2 - 28 ALA 28 T A - - - - - - - - - - 177.0 - 33.5 - 29 THR 29 t B - - -61.4 - - - - - - - 183.5 -2.2 33.5 - 30 THR 30 h B 57.8 - - - - - - - - - 175.6 - 33.9 - 31 VAL 31 H A - 178.4 - - - -67.1 -26.4 - - - 175.1 -3.3 33.6 - * +* +* 32 SER 32 H A - 186.3 - - - -65.7 -46.8 - - - 178.3 -2.0 34.3 - 33 ALA 33 H A - - - - - -69.7 -25.7 - - - 175.2 - 33.2 - * * 34 LEU 34 H A - 177.4 - - - -65.0 -48.0 - - - 172.3 -1.6 35.7 - * * 35 LYS 35 H A - - -81.2 161.8 - -58.8 -47.0 - - - 178.6 -2.5 34.7 - 36 GLU 36 H A - - -65.9 - - -56.9 -36.8 - - - 177.6 -2.8 34.2 - * * 37 THR 37 H A - - -58.6 - - -63.0 -41.0 - - - 176.2 -2.0 33.3 - 38 VAL 38 H A - 183.4 - - - -60.5 -49.1 - - - 180.3 -1.5 35.1 - 39 ILE 39 H A - - -51.6 - - -58.6 -33.2 - - - 180.4 -2.6 34.8 - * * 40 SER 40 H A - - -58.1 - - -74.2 -36.7 - - - 181.8 -2.0 34.1 - 41 GLU 41 H A - - -59.7 - - -86.5 -28.2 - - - 183.0 -1.9 35.5 - +* +* 42 TRP 42 h B - 194.4 - - - - - - - - 178.5 -2.8 36.0 - * * 43 PRO 43 t - - - - - -61.9 - - - - - 178.6 - 38.6 - * * 44 ARG 44 T A - - -59.0 173.4 - - - - - - 180.4 - 35.3 - 45 GLU 45 T A - 183.2 - - - - - - - - 179.7 - 34.8 - 46 LYS 46 t B - 192.5 - 179.4 - - - - - - 175.7 -1.1 34.7 - * * 47 GLU 47 b - 179.8 - 184.3 - - - - - - 179.4 - 35.5 - 48 ASN 48 S b - - -71.1 - - - - - - - 170.3 - 29.9 - +* * +* 49 GLY 49 S - - - - - - - - - - - 171.4 -2.6 - - * * 50 PRO 50 S - - - - - -70.3 - - - - - 180.0 - 38.5 - * * 51 LYS 51 ~a - 180.0 - 179.2 - - - - - - 176.7 - 34.8 - ** ** 52 THR 52 t B 49.9 - - - - - - - - - 194.0 - 27.7 - ** +* ** 53 VAL 53 T A 61.3 - - - - - - - - - 185.8 - 34.1 - * * 54 LYS 54 T A - - -54.4 179.9 - - - - - - 187.3 - 35.0 - * * 55 GLU 55 e A 58.8 - - - - - - - - - 179.5 - 30.9 - Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 VAL 56 E B 58.1 - - - - - - - - - 180.6 -.6 32.3 - +* +* 57 LYS 57 E B - - -66.0 184.1 - - - - - - 177.8 -2.4 34.2 - 58 LEU 58 E B - 194.0 - - - - - - - - 188.9 - 34.7 - +* +* 59 ILE 59 E B - - -67.0 176.4 - - - - - - 178.0 -3.3 34.0 - +* +* 60 SER 60 E B - 189.1 - - - - - - - - 184.5 -2.4 34.2 - 61 ALA 61 T l - - - - - - - - - - 181.8 - 32.3 - 62 GLY 62 T - - - - - - - - - - - 183.8 - - - 63 LYS 63 E B - - -64.5 177.3 - - - - - - 175.9 -1.5 36.7 - 64 VAL 64 E B - 182.5 - - - - - - - - 180.4 - 35.5 - 65 LEU 65 e B 39.2 - - 164.1 - - - - - - 180.9 -1.9 28.2 - +* +* +* 66 GLU 66 t B - 177.5 - 174.3 - - - - - - 183.3 - 34.1 - 67 ASN 67 T A 63.9 - - - - - - - - - 181.9 - 33.4 - 68 SER 68 T A - - -56.4 - - - - - - - 179.0 - 33.1 - 69 LYS 69 t B - - -64.1 182.1 - - - - - - 182.2 -1.8 33.1 - 70 THR 70 B B - - -33.1 - - - - - - - 178.4 - 36.2 - ** ** 71 VAL 71 T A - 177.9 - - - - - - - - 177.2 -2.7 34.0 - 72 LYS 72 T A - 184.6 - 177.6 - - - - - - 181.8 -2.7 36.7 - 73 ASP 73 T A - - -65.2 - - - - - - - 182.3 - 35.1 - 74 TYR 74 T A - 192.1 - - - - - - - - 176.6 -1.2 33.3 - * * 75 ARG 75 t b - - -68.3 - - - - - - - 179.6 -1.4 35.0 - 76 SER 76 t B - - -57.7 - - - - - - - 181.2 - 35.2 - 77 PRO 77 T - - - - - -39.2 - - - - - 184.5 - 38.1 - ** * ** 78 VAL 78 T l 79.9 - - - - - - - - - 177.9 - 28.8 - * * * 79 SER 79 T ~l - - -53.7 - - - - - - - 176.9 -2.0 32.1 - ** ** 80 ASN 80 t b 58.2 - - - - - - - - - 180.8 -.6 32.0 - +* +* 81 LEU 81 B - - -55.6 183.9 - - - - - - 184.0 -1.2 35.7 - * * 82 ALA 82 b - - - - - - - - - - 175.2 - 35.1 - 83 GLY 83 S - - - - - - - - - - - 177.6 - - - 84 ALA 84 S B - - - - - - - - - - 185.2 - 34.3 - 85 VAL 85 B - 182.0 - - - - - - - - 179.6 - 34.5 - 86 THR 86 E B - - -53.3 - - - - - - - 179.0 -2.8 35.9 - * * 87 THR 87 E B - - -58.7 - - - - - - - 178.9 - 34.3 - 88 MET 88 E B - - -65.9 179.1 - - - - - - 183.4 -2.6 32.3 - 89 HIS 89 E B - - -64.8 - - - - - - - 177.1 -2.5 33.8 - 90 VAL 90 E B - 176.5 - - - - - - - - 178.2 -2.5 33.0 - 91 ILE 91 E B - - -74.2 188.0 - - - - - - 183.8 -2.0 31.5 - 92 ILE 92 E B - - -53.7 - - - - - - - 177.7 -.5 36.8 - ** ** 93 GLN 93 e B - 183.9 - 179.9 - - - - - - 178.2 -1.9 33.3 - 94 ALA 94 B - - - - - - - - - - 179.1 -.9 34.7 - * * 95 PRO 95 - - - - - -57.4 - - - - - 183.8 - 38.4 - * * 96 VAL 96 S A 60.7 - - - - - - - - - 176.7 - 32.3 - 97 THR 97 S b - - -59.5 - - - - - - - 181.1 - 32.7 - Residue-by-residue listing for refined_4 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 GLU 98 B - 185.1 - - - - - - - - 181.1 - 35.0 - 99 LYS 99 B 57.8 - - 163.0 - - - - - - 170.6 - 35.1 - +* +* 100 GLU 100 B - - -65.5 179.7 - - - - - - 183.4 - 34.6 - 101 LYS 101 - 57.3 - - 166.1 - - - - - - - - 29.2 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* ** * ** +* * ** ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.8 184.6 -60.4 176.8 -59.2 -66.0 -38.1 - - - 179.7 -2.0 34.3 Standard deviations: 9.2 5.5 8.1 7.7 10.9 8.5 8.9 - - - 3.8 .8 2.1 Numbers of values: 16 25 41 27 6 11 11 0 0 0 100 51 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_4 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 - 1.240 1.523 1.540 1.461 - 116.42 120.04 110.22 108.99 110.36 123.48 2 ALA 2 1.351 1.243 1.524 1.524 1.484 123.18 114.06 122.14 111.58 109.94 110.61 123.71 +* * * +* 3 GLU 3 1.293 1.230 1.522 1.522 1.411 123.98 116.41 120.69 110.40 109.93 108.89 122.82 +** ** * +** 4 VAL 4 1.305 1.234 1.523 1.558 1.441 121.53 116.69 120.44 109.96 107.85 112.24 122.86 +* * +* 5 HIS 5 1.313 1.233 1.539 1.545 1.468 122.52 115.02 122.10 112.55 110.29 108.89 122.88 * * * 6 ASN 6 1.311 1.235 1.532 1.550 1.451 122.67 115.14 121.62 111.46 106.86 109.22 123.21 * +* +* 7 GLN 7 1.326 1.236 1.514 1.544 1.438 122.52 117.09 120.22 110.12 108.84 111.55 122.69 * * 8 LEU 8 1.307 1.224 1.509 1.534 1.443 120.46 117.43 120.39 108.38 108.84 111.93 122.17 +* +* 9 GLU 9 1.291 1.234 1.506 1.519 1.429 119.78 115.51 121.50 110.73 110.64 113.12 122.98 +** +* * +* +** 10 ILE 10 1.294 1.233 1.517 1.568 1.439 122.20 116.88 120.25 108.91 109.27 110.64 122.84 +** * * +** 11 LYS 11 1.309 1.248 1.508 1.537 1.441 120.51 115.89 120.73 109.37 109.51 115.02 123.38 * +** +** Residue-by-residue listing for refined_4 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 PHE 12 1.297 1.221 1.509 1.522 1.436 121.82 117.15 120.17 109.92 109.44 109.62 122.68 ** * ** 13 ARG 13 1.307 1.237 1.517 1.535 1.442 120.80 115.33 121.14 111.51 110.60 110.73 123.52 +* +* 14 LEU 14 1.304 1.242 1.514 1.554 1.447 123.50 116.04 120.54 108.51 109.54 111.32 123.37 +* * * +* 15 THR 15 1.310 1.232 1.541 1.528 1.451 123.33 116.53 121.01 110.42 112.76 109.18 122.46 * * * 16 ASP 16 1.321 1.239 1.524 1.534 1.468 122.06 116.81 120.60 109.48 111.84 111.79 122.59 17 GLY 17 1.323 1.237 1.511 - 1.456 120.69 115.75 121.37 - 112.35 - 122.88 18 SER 18 1.290 1.219 1.511 1.523 1.428 121.85 118.13 119.68 109.37 108.36 108.50 122.17 +** +* * * +** 19 ASP 19 1.305 1.232 1.497 1.533 1.419 120.00 115.37 120.71 110.76 109.73 112.51 123.88 +* * ** * ** 20 ILE 20 1.291 1.238 1.519 1.565 1.435 123.47 116.68 119.32 109.48 107.60 110.60 123.96 +** * * +** 21 GLY 21 1.333 1.241 1.518 - 1.450 122.07 118.31 119.68 - 112.18 - 122.00 22 PRO 22 1.342 1.247 1.518 1.531 1.449 122.23 115.04 121.31 110.82 112.80 105.35 123.65 * * ** * ** 23 LYS 23 1.300 1.224 1.464 1.516 1.442 123.25 115.94 120.21 106.14 105.88 112.84 123.82 ** +** ** +* * +** 24 ALA 24 1.247 1.233 1.508 1.519 1.449 120.49 116.49 120.77 111.06 109.73 111.17 122.73 *5.9* *5.9* 25 PHE 25 1.305 1.237 1.503 1.530 1.435 121.65 117.44 120.67 107.78 110.18 110.74 121.81 +* * * * +* 26 PRO 26 1.316 1.236 1.523 1.523 1.451 122.11 116.29 120.65 108.75 110.45 103.58 123.06 +* * +* 27 ASP 27 1.310 1.228 1.528 1.536 1.463 122.41 116.21 120.77 109.96 111.14 110.65 122.96 * * 28 ALA 28 1.325 1.227 1.531 1.510 1.449 122.26 117.22 120.36 110.65 112.34 110.31 122.41 29 THR 29 1.315 1.237 1.531 1.547 1.439 121.05 116.73 120.70 111.90 108.94 110.56 122.53 * * 30 THR 30 1.304 1.232 1.524 1.539 1.430 121.26 115.68 121.15 109.61 112.19 111.26 123.17 +* * +* 31 VAL 31 1.322 1.234 1.539 1.560 1.454 122.68 115.75 121.53 111.32 108.83 111.14 122.71 * * 32 SER 32 1.323 1.220 1.523 1.540 1.440 121.95 116.31 120.65 110.78 108.53 110.66 122.98 33 ALA 33 1.332 1.229 1.531 1.512 1.453 121.75 116.07 120.99 111.29 110.61 110.59 122.94 34 LEU 34 1.321 1.235 1.542 1.527 1.419 123.57 115.62 121.02 112.41 107.79 107.07 123.32 ** * * * ** ** 35 LYS 35 1.338 1.221 1.521 1.530 1.467 122.99 116.41 120.33 109.64 110.65 110.32 123.26 36 GLU 36 1.332 1.222 1.514 1.522 1.461 122.75 116.86 120.37 109.45 111.40 110.91 122.77 37 THR 37 1.321 1.230 1.535 1.546 1.442 121.44 116.25 120.56 110.95 109.84 111.45 123.13 38 VAL 38 1.334 1.213 1.523 1.558 1.459 122.02 115.27 120.94 108.37 108.43 111.97 123.71 39 ILE 39 1.331 1.230 1.542 1.576 1.477 124.06 115.65 121.83 109.59 110.46 110.54 122.52 * * * * 40 SER 40 1.310 1.238 1.535 1.524 1.442 122.53 116.93 120.55 110.68 112.26 109.62 122.52 * * 41 GLU 41 1.318 1.242 1.534 1.521 1.434 122.03 115.72 120.94 109.95 111.27 108.70 123.34 * * * 42 TRP 42 1.312 1.239 1.534 1.538 1.449 123.42 118.14 120.01 110.39 109.34 108.21 121.79 * * * 43 PRO 43 1.343 1.228 1.530 1.532 1.461 122.45 115.52 121.28 109.83 112.53 104.08 123.20 44 ARG 44 1.308 1.224 1.528 1.523 1.456 123.13 115.03 121.63 109.90 109.46 109.36 123.34 * * Residue-by-residue listing for refined_4 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 1.322 1.240 1.554 1.547 1.455 123.41 116.73 121.40 111.32 110.51 108.60 121.87 * * * 46 LYS 46 1.318 1.236 1.546 1.541 1.456 121.16 116.22 120.48 110.02 110.04 110.18 123.29 47 GLU 47 1.332 1.237 1.564 1.553 1.461 124.20 116.63 120.37 111.09 110.14 107.88 123.00 +* * * +* +* 48 ASN 48 1.335 1.234 1.506 1.531 1.455 125.28 112.87 122.43 111.30 114.71 113.50 124.47 +* +* * +* +* 49 GLY 49 1.259 1.240 1.492 - 1.418 124.57 119.22 119.34 - 107.09 - 121.45 *5.0* * ** ** * +* *5.0* 50 PRO 50 1.317 1.239 1.514 1.529 1.438 121.28 115.93 120.51 110.20 108.98 104.63 123.54 +* +* * * * +* 51 LYS 51 1.289 1.227 1.496 1.539 1.442 122.65 114.68 121.68 110.32 107.59 110.72 123.63 +** * * +** 52 THR 52 1.306 1.237 1.563 1.541 1.412 122.80 115.56 121.02 114.97 112.98 113.48 123.40 +* +* ** +** * +** 53 VAL 53 1.310 1.247 1.549 1.565 1.468 125.89 117.53 120.09 110.11 115.34 109.30 122.38 * * ** * * ** 54 LYS 54 1.320 1.232 1.512 1.526 1.464 120.69 116.17 120.52 107.75 111.49 111.57 123.29 * * 55 GLU 55 1.319 1.240 1.526 1.538 1.466 120.56 117.06 120.92 110.64 113.92 113.29 122.02 +* +* 56 VAL 56 1.300 1.238 1.533 1.567 1.436 120.07 116.43 121.16 111.86 110.73 112.00 122.41 ** * * * ** 57 LYS 57 1.313 1.233 1.499 1.530 1.437 121.22 115.89 120.64 108.97 110.71 111.98 123.46 * * * * 58 LEU 58 1.308 1.243 1.518 1.553 1.422 121.57 116.30 120.31 112.89 104.34 109.40 123.35 +* * +* * ** ** 59 ILE 59 1.303 1.243 1.520 1.558 1.440 122.25 114.17 121.91 111.30 113.14 109.25 123.93 +* * * +* 60 SER 60 1.304 1.235 1.534 1.539 1.419 123.94 116.40 119.72 112.21 106.11 110.18 123.67 +* ** * * +* ** 61 ALA 61 1.339 1.239 1.527 1.530 1.484 124.84 115.13 121.73 111.35 110.16 112.02 123.10 * +* * +* 62 GLY 62 1.324 1.235 1.515 - 1.448 121.62 115.97 121.09 - 111.58 - 122.92 63 LYS 63 1.317 1.241 1.495 1.502 1.399 122.72 115.55 120.64 108.93 110.37 108.40 123.81 * * *** * *** 64 VAL 64 1.298 1.245 1.518 1.555 1.432 121.88 117.42 120.35 109.28 106.95 111.10 122.21 ** * +* ** 65 LEU 65 1.299 1.237 1.502 1.546 1.422 119.95 114.19 121.46 113.13 113.30 114.73 124.32 ** * +* * +* ** ** 66 GLU 66 1.316 1.234 1.523 1.528 1.439 123.92 115.48 120.98 111.73 111.28 109.04 123.53 * * * 67 ASN 67 1.324 1.227 1.526 1.549 1.469 123.44 116.62 120.68 110.21 112.59 111.09 122.69 68 SER 68 1.307 1.241 1.542 1.524 1.444 121.69 116.57 120.99 112.23 112.31 109.33 122.43 +* * +* 69 LYS 69 1.314 1.239 1.522 1.519 1.429 121.85 116.75 120.45 111.63 110.54 110.68 122.78 * +* +* 70 THR 70 1.307 1.235 1.539 1.531 1.441 121.10 117.78 119.58 108.51 109.04 109.76 122.64 +* * +* 71 VAL 71 1.347 1.235 1.528 1.568 1.476 121.06 114.29 121.67 109.84 108.98 111.96 124.03 * * * 72 LYS 72 1.315 1.234 1.533 1.523 1.452 124.95 115.87 121.08 110.07 110.53 106.87 123.00 * +* ** ** 73 ASP 73 1.328 1.226 1.516 1.526 1.450 123.02 116.72 120.56 108.26 111.90 110.80 122.72 74 TYR 74 1.320 1.235 1.543 1.543 1.448 121.10 116.24 121.48 111.56 110.59 110.47 122.27 Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 75 ARG 75 1.315 1.241 1.531 1.521 1.414 122.31 116.53 120.72 111.08 109.78 108.91 122.74 ** ** 76 SER 76 1.306 1.235 1.550 1.524 1.437 122.29 118.40 119.11 111.77 109.58 107.73 122.47 +* * * * +* +* 77 PRO 77 1.380 1.230 1.537 1.543 1.485 124.58 115.00 120.19 110.50 113.76 103.78 124.81 ** * * ** ** 78 VAL 78 1.352 1.245 1.532 1.579 1.506 128.66 114.02 121.86 111.96 111.07 116.08 124.08 +* * +** +*** * * +** +*** 79 SER 79 1.316 1.239 1.516 1.526 1.449 125.58 115.51 121.57 111.78 112.10 111.38 122.88 ** ** 80 ASN 80 1.305 1.236 1.516 1.557 1.442 121.67 115.67 121.79 111.87 109.86 112.60 122.45 +* * * +* 81 LEU 81 1.307 1.239 1.513 1.491 1.384 122.37 116.43 120.40 110.89 109.77 108.00 123.16 +* +* +*** * +*** 82 ALA 82 1.307 1.224 1.492 1.524 1.409 122.70 115.63 120.45 109.79 108.64 110.68 123.89 +* +* +** +** 83 GLY 83 1.297 1.224 1.509 - 1.445 121.57 114.87 121.39 - 110.20 - 123.73 ** ** 84 ALA 84 1.325 1.240 1.518 1.518 1.441 123.31 116.17 120.97 110.36 110.10 110.27 122.82 85 VAL 85 1.302 1.232 1.514 1.555 1.436 120.90 115.25 121.23 109.65 109.82 111.27 123.49 +* * +* 86 THR 86 1.300 1.232 1.541 1.550 1.434 123.18 117.57 120.18 109.91 108.36 109.24 122.22 ** * * * ** 87 THR 87 1.307 1.229 1.525 1.544 1.443 121.15 116.44 120.84 110.01 110.29 110.93 122.71 +* +* 88 MET 88 1.305 1.238 1.511 1.531 1.443 121.52 116.21 120.69 112.20 110.08 111.54 123.07 +* * +* 89 HIS 89 1.316 1.228 1.497 1.539 1.453 121.67 115.62 120.82 109.30 111.05 112.03 123.55 * * 90 VAL 90 1.293 1.238 1.491 1.554 1.433 121.95 114.43 121.62 110.47 109.51 112.89 123.93 +** +* * +** 91 ILE 91 1.278 1.245 1.502 1.545 1.405 122.21 114.16 121.61 113.24 110.22 111.93 124.21 +*** * +** * +* +*** 92 ILE 92 1.291 1.237 1.509 1.559 1.423 123.52 117.56 120.23 108.37 108.71 109.68 122.16 +** +* * * +** 93 GLN 93 1.308 1.232 1.495 1.525 1.406 118.44 114.90 121.58 110.75 108.61 112.35 123.51 +* * +** +* * +** 94 ALA 94 1.281 1.237 1.507 1.520 1.423 121.64 118.51 119.47 110.79 108.11 110.15 121.99 *** +* * * *** 95 PRO 95 1.342 1.246 1.527 1.524 1.458 121.96 116.41 120.36 110.45 110.30 104.02 123.23 96 VAL 96 1.320 1.234 1.542 1.567 1.464 122.39 116.35 121.44 111.60 111.54 111.71 122.20 * * * 97 THR 97 1.302 1.238 1.519 1.542 1.430 121.98 114.93 121.58 111.72 109.93 111.60 123.41 +* * * +* 98 GLU 98 1.303 1.240 1.517 1.539 1.432 122.76 116.72 119.94 111.02 107.88 109.65 123.33 +* * * +* 99 LYS 99 1.302 1.235 1.527 1.528 1.424 122.20 115.47 120.93 107.92 112.30 111.15 123.60 +* +* * +* 100 GLU 100 1.316 1.231 1.521 1.527 1.442 122.78 116.82 118.97 109.13 107.51 111.86 124.17 * * * 101 LYS 101 1.337 - 1.544 1.548 1.484 124.78 - - 111.68 113.95 114.25 - * +* ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.9* +** +* +*** +*** +* * +** ** +** ** *5.9* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 1.247 1.352 1.311 .017 *5.9* +* * C-N (Pro) 1.341 .016 6 1.316 1.380 1.340 .021 +* ** C-O C-O 1.231 .020 100 1.213 1.248 1.235 .007 CA-C CH1E-C (except Gly) 1.525 .021 96 1.464 1.564 1.522 .016 +** +* CH2G*-C (Gly) 1.516 .018 5 1.492 1.518 1.509 .009 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.510 1.530 1.520 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.528 1.579 1.555 .013 * CH1E-CH2E (the rest) 1.530 .020 62 1.491 1.557 1.532 .012 +* * N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.384 1.506 1.443 .020 +*** +** NH1-CH2G* (Gly) 1.451 .016 5 1.418 1.456 1.443 .013 ** N-CH1E (Pro) 1.466 .015 6 1.438 1.485 1.457 .014 +* * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 89 112.87 118.51 116.12 1.05 +* * CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.87 119.22 116.82 1.65 * CH1E-C-N (Pro) 116.9 1.5 6 115.00 116.41 115.70 .56 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.45 124.47 123.02 .64 O-C-N (Pro) 122.0 1.4 6 123.06 124.81 123.58 .58 ** * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.44 128.66 122.38 1.49 +* +*** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.69 124.57 122.10 1.31 ** C-N-CH1E (Pro) 122.6 5.0 6 121.28 124.58 122.44 1.02 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.97 122.43 120.80 .68 * CH2G*-C-O (Gly) 120.8 2.1 5 119.34 121.39 120.57 .88 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 109.79 111.58 110.86 .55 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.37 114.97 110.51 1.51 +** CH2E-CH1E-C (the rest) 110.1 1.9 62 106.14 113.13 110.39 1.37 ** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.34 115.34 110.10 1.90 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 107.09 112.35 110.68 1.94 +* N-CH1E-C (Pro) 111.8 2.5 6 108.98 113.76 111.47 1.67 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 110.15 112.02 110.73 .57 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.18 116.08 111.22 1.48 * +** N-CH1E-CH2E (Pro) 103.0 1.1 6 103.58 105.35 104.24 .59 ** * NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.87 115.02 110.58 1.86 ** +** ------------------------------------------------------------------------------------------------------------- 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_4 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] 9 10.2% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 6 ---- Total number of residues 101 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 88 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 100 3.8 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 2.1 3.1 1.6 -.7 Inside e. H-bond energy st dev 51 .8 .8 .2 .1 Inside f. Overall G-factor 101 .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 16 9.2 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 25 5.5 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 41 8.1 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 82 9.0 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 27 7.7 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 10.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_4 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.44 Chi1-chi2 distribution -.01 Chi1 only -.03 Chi3 & chi4 .22 Omega -.05 ------ -.12 ===== Main-chain covalent forces:- Main-chain bond lengths -.11 Main-chain bond angles .33 ------ .14 ===== OVERALL AVERAGE -.04 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.