Residue-by-residue listing for refined_6 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 - - 180.0 - 180.2 - - - - - - 176.5 - 34.2 - 2 ALA 2 B - - - - - - - - - - 183.0 - 33.4 - 3 ASP 3 B - 182.0 - - - - - - - - 175.1 - 34.5 - 4 THR 4 S a - - -58.0 - - - - - - - 176.9 - 32.9 - 5 GLY 5 S - - - - - - - - - - - 177.1 - - - 6 GLU 6 b - 184.3 - 187.8 - - - - - - 173.6 - 33.1 - * * 7 VAL 7 E B - - -63.1 - - - - - - - 184.2 -2.0 32.6 - 8 GLN 8 E B 53.8 - - 183.6 - - - - - - 181.6 - 34.3 - 9 PHE 9 E B - 182.3 - - - - - - - - 178.9 -1.9 35.2 - 10 MET 10 E B 60.8 - - 179.8 - - - - - - 183.6 - 33.6 - 11 LYS 11 E B - 198.1 - - - - - - - - 177.5 -1.2 35.9 - * * 12 PRO 12 E - - - - - -63.3 - - - - - 182.1 - 38.3 - * * 13 PHE 13 e B - 182.6 - - - - - - - - 178.4 -.7 36.7 - +* +* 14 ILE 14 h B - - -58.1 - - - - - - - 185.7 - 35.4 - 15 SER 15 H A - - -59.1 - - -53.5 -31.9 - - - 184.1 -.5 34.8 - ** ** 16 GLU 16 H A - 189.5 - 178.5 - -60.7 -40.9 - - - 178.6 - 34.5 - 17 LYS 17 H a - - -63.9 189.1 - -100.8 -40.4 - - - 187.4 -1.4 33.8 - +** * +** 18 SER 18 H A - - -55.0 - - -70.8 3.5 - - - 166.9 -3.3 31.6 - +*** ** +* +*** 19 SER 19 h A - - -62.7 - - - - - - - 178.5 -.8 33.7 - +* +* 20 LYS 20 T a - - -71.1 177.6 - - - - - - 181.3 -2.7 31.5 - Residue-by-residue listing for refined_6 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 49.5 - - - - - - - - - 180.1 -3.2 33.8 - +* +* 22 LEU 22 E B - 183.3 - 163.3 - - - - - - 181.0 -3.2 31.8 - +* +* 23 GLU 23 E B 51.9 - - 168.6 - - - - - - 176.0 - 34.8 - 24 ILE 24 E B - - -62.5 - - - - - - - 178.1 -2.7 35.1 - 25 PRO 25 h - - - - - -61.4 - - - - - 180.4 - 38.9 - * * 26 LEU 26 H A - 187.5 - 170.6 - -54.5 -42.2 - - - 181.8 - 35.1 - 27 GLY 27 H - - - - - - -58.7 -30.4 - - - 180.8 - - - 28 PHE 28 H A - 185.9 - - - -86.5 -25.4 - - - 175.5 -1.1 33.1 - +* * * +* 29 ASN 29 H A - 184.4 - - - -73.9 -37.2 - - - 176.8 -1.4 34.4 - 30 GLU 30 H A - 177.7 - 186.1 - -63.4 -27.4 - - - 182.5 -2.8 36.0 - * * 31 TYR 31 H A - 186.3 - - - -70.0 -27.2 - - - 178.8 -.5 33.8 - * ** ** 32 PHE 32 h b 67.9 - - - - - - - - - 168.7 -.9 32.5 - +* * +* 33 PRO 33 - - - - - -77.7 - - - - - 186.9 - 38.4 - * * * * 34 ALA 34 B - - - - - - - - - - 175.2 - 35.0 - 35 PRO 35 - - - - - -56.3 - - - - - 186.8 - 38.7 - * * * 36 PHE 36 B - 187.4 - - - - - - - - 177.8 - 35.4 - 37 PRO 37 - - - - - -93.0 - - - - - 176.5 - 39.0 - ** * ** 38 ILE 38 e a - - -55.9 - - - - - - - 178.3 - 32.8 - 39 THR 39 E B 49.0 - - - - - - - - - 180.1 - 31.9 - 40 VAL 40 E B - 174.8 - - - - - - - - 182.6 -3.1 35.2 - * * 41 ASP 41 E B - - -65.4 - - - - - - - 176.4 -2.5 33.3 - 42 LEU 42 E B - - -57.2 - - - - - - - 182.7 -2.7 35.5 - 43 LEU 43 E B - - -65.2 - - - - - - - 175.9 -3.5 34.5 - +* +* 44 ASP 44 e B - 182.5 - - - - - - - - 181.8 -2.7 35.8 - 45 TYR 45 T A 47.3 - - - - - - - - - 178.0 - 30.2 - * * * 46 SER 46 T A - 184.0 - - - - - - - - 178.1 - 33.5 - 47 GLY 47 t - - - - - - - - - - - 181.8 -2.4 - - 48 ARG 48 e B - 185.1 - 169.7 - - - - - - 181.6 - 34.1 - 49 SER 49 E B 57.7 - - - - - - - - - 179.1 - 33.3 - 50 TRP 50 E B - - -57.6 - - - - - - - 181.4 -1.9 34.6 - 51 THR 51 E B - - -52.9 - - - - - - - 180.2 - 35.0 - 52 VAL 52 E B - - -62.5 - - - - - - - 176.6 -3.3 33.1 - +* +* 53 ARG 53 E B - 183.4 - 179.6 - - - - - - 185.2 -1.6 35.5 - 54 MET 54 E B - 184.5 - - - - - - - - 185.3 -1.0 36.2 - * * 55 LYS 55 E B - 186.2 - 166.4 - - - - - - 179.2 -2.5 34.5 - 56 LYS 56 E B - - -50.2 - - - - - - - 180.5 - 37.9 - * * * 57 ARG 57 E B - - -59.7 184.7 - - - - - - 177.4 -2.9 33.8 - * * 58 GLY 58 T - - - - - - - - - - - 188.1 -.5 - - * ** ** Residue-by-residue listing for refined_6 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 59 GLU 59 T A - - -42.8 - - - - - - - 184.9 - 35.2 - +* +* 60 LYS 60 E B 54.4 - - - - - - - - - 180.4 -2.5 31.5 - 61 VAL 61 E B - 179.5 - - - - - - - - 176.2 -.6 34.9 - +* +* 62 PHE 62 E B - - -63.2 - - - - - - - 173.4 -2.5 34.3 - * * 63 LEU 63 E B - - -64.5 - - - - - - - 189.7 -2.5 34.1 - +* +* 64 THR 64 e a 57.7 - - - - - - - - - 185.8 -2.4 31.7 - 65 VAL 65 T B - 180.4 - - - - - - - - 178.9 - 33.7 - 66 GLY 66 h - - - - - - - - - - - 177.5 - - - 67 TRP 67 H A - 172.1 - - - -61.8 -23.6 - - - 183.9 -2.3 34.0 - * * 68 GLU 68 H A 61.7 - - 187.1 - -70.6 -26.8 - - - 177.9 - 31.8 - * * 69 ASN 69 H A - - -58.6 - - -66.5 -39.9 - - - 184.0 -1.3 35.6 - 70 PHE 70 H A - 183.2 - - - -71.7 -43.9 - - - 181.4 -1.0 35.6 - * * 71 VAL 71 H A 72.4 - - - - -66.2 -43.6 - - - 178.1 -2.5 32.7 - 72 LYS 72 H A 62.1 - - 177.4 - -71.6 -34.9 - - - 182.8 -2.2 30.6 - 73 ASP 73 H A - 186.6 - - - -77.6 -39.6 - - - 178.1 -2.3 31.6 - * * 74 ASN 74 H A - - -73.7 - - -89.4 -7.0 - - - 184.7 -2.9 33.0 - ** +** * +** 75 ASN 75 h l - - -62.1 - - - - - - - 183.7 -.8 30.1 - +* * +* 76 LEU 76 t B - - -61.3 181.6 - - - - - - 182.3 -1.4 33.0 - 77 GLU 77 t B 54.0 - - 181.8 - - - - - - 173.6 - 36.8 - * * 78 ASP 78 T B 60.8 - - - - - - - - - 180.3 - 33.6 - 79 GLY 79 T - - - - - - - - - - - 178.2 - - - 80 LYS 80 e B - - -74.5 180.0 - - - - - - 190.0 -.7 31.8 - +* +* +* 81 TYR 81 E B - - -61.0 - - - - - - - 179.3 - 34.2 - 82 LEU 82 E B 63.4 - - 176.2 - - - - - - 176.3 -.6 33.3 - +* +* 83 GLN 83 E B - - -60.3 195.9 - - - - - - 179.2 -2.6 33.3 - * * 84 PHE 84 E B - - -64.2 - - - - - - - 174.0 -3.1 35.5 - * * * 85 ILE 85 E B - - -55.4 178.0 - - - - - - 188.2 -2.7 34.1 - * * 86 TYR 86 E B - 184.0 - - - - - - - - 178.1 -3.7 35.8 - ** ** 87 ASP 87 e A - - -73.9 - - - - - - - 183.8 -2.4 35.2 - 88 ARG 88 S l - - -59.1 185.1 - - - - - - 179.8 - 32.2 - 89 ASP 89 S b - 193.7 - - - - - - - - 178.9 - 37.1 - 90 ARG 90 e a 59.3 - - 175.8 - - - - - - 183.5 - 35.0 - 91 THR 91 E B - - -54.0 - - - - - - - 171.8 - 35.6 - * * 92 PHE 92 E B - - -74.5 - - - - - - - 170.4 -1.7 35.6 - +* +* 93 TYR 93 E B - - -61.4 - - - - - - - 186.1 -2.6 33.5 - * * 94 VAL 94 E B - 186.6 - - - - - - - - 177.0 -1.6 34.4 - 95 ILE 95 E B - - -63.2 - - - - - - - 181.9 -2.1 34.0 - Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 96 ILE 96 E B - - -55.7 - - - - - - - 175.1 - 35.2 - 97 TYR 97 e B - - -59.4 - - - - - - - 186.4 -3.3 34.7 - * +* +* 98 GLY 98 S - - - - - - - - - - - 183.5 -.8 - - +* +* 99 HIS 99 b - 178.9 - - - - - - - - 175.4 - 32.2 - 100 ASN 100 S p - 199.1 - - - - - - - - 176.8 -1.5 34.3 - 101 MET 101 B - 191.2 - - - - - - - - 183.8 - 34.9 - 102 CYS 102 - 54.9 - - - - - - - - - - -.9 33.8 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* * ** +** +*** ** ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.7 184.6 -61.1 179.4 -70.3 -70.4 -31.1 - - - 180.0 -2.0 34.3 Standard deviations: 6.6 5.7 6.6 7.6 14.9 12.2 12.7 - - - 4.4 .9 1.8 Numbers of values: 18 32 38 25 5 18 18 0 0 0 101 59 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_6 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 - 1.232 1.504 1.536 1.454 - 115.79 120.82 109.94 109.84 111.17 123.38 2 ALA 2 1.298 1.247 1.505 1.523 1.431 122.54 115.49 121.30 111.42 107.94 111.48 123.06 ** * * ** 3 ASP 3 1.305 1.230 1.511 1.533 1.434 121.54 115.64 121.26 109.95 110.85 110.47 123.06 +* * +* 4 THR 4 1.293 1.229 1.515 1.550 1.444 122.55 115.49 121.37 111.32 108.87 112.16 123.10 +** * +** 5 GLY 5 1.295 1.229 1.474 - 1.422 120.93 114.20 121.81 - 112.39 - 123.97 ** ** +* * ** 6 GLU 6 1.258 1.241 1.515 1.542 1.437 122.85 115.98 121.20 109.70 110.23 112.94 122.67 *5.1* * * *5.1* 7 VAL 7 1.293 1.219 1.506 1.572 1.442 121.37 117.45 120.06 111.32 107.44 113.46 122.47 +** * * * * +** 8 GLN 8 1.289 1.233 1.507 1.516 1.418 121.13 116.10 120.57 111.78 110.85 108.84 123.33 +** ** +** 9 PHE 9 1.303 1.233 1.518 1.542 1.438 122.33 116.50 120.36 111.04 109.05 108.91 123.12 +* * +* 10 MET 10 1.306 1.240 1.514 1.545 1.448 122.11 117.34 120.11 111.40 108.41 111.18 122.54 +* +* 11 LYS 11 1.309 1.229 1.532 1.564 1.444 120.41 118.03 119.86 111.08 108.27 108.27 122.09 * +* * * +* Residue-by-residue listing for refined_6 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 1.353 1.248 1.539 1.530 1.470 122.64 114.95 121.65 110.25 112.78 103.81 123.38 * * 13 PHE 13 1.295 1.232 1.533 1.546 1.441 123.81 117.60 119.88 110.79 108.64 107.07 122.52 ** * ** ** 14 ILE 14 1.330 1.231 1.510 1.569 1.434 121.52 116.98 119.53 109.49 106.35 111.35 123.49 * * +* +* 15 SER 15 1.331 1.219 1.525 1.532 1.467 123.13 115.59 120.86 109.21 112.01 110.15 123.45 16 GLU 16 1.314 1.234 1.525 1.520 1.442 123.69 117.31 120.59 110.66 111.03 109.44 122.08 * * * 17 LYS 17 1.327 1.229 1.471 1.517 1.452 118.36 115.09 120.96 107.79 110.18 113.78 123.89 +** +* * +* +** 18 SER 18 1.314 1.218 1.526 1.518 1.425 122.37 117.34 119.96 113.15 113.40 110.13 122.69 * +* +* +* 19 SER 19 1.335 1.228 1.543 1.537 1.443 119.66 116.90 120.72 110.07 108.59 112.03 122.37 * * 20 LYS 20 1.347 1.213 1.520 1.528 1.459 120.52 118.20 119.60 110.49 114.03 112.54 122.20 * * * * 21 SER 21 1.316 1.228 1.526 1.521 1.446 120.61 116.24 121.72 110.66 112.94 109.78 122.04 22 LEU 22 1.291 1.234 1.519 1.560 1.443 121.03 115.34 120.91 113.29 110.08 111.36 123.74 +** * +* +** 23 GLU 23 1.315 1.234 1.538 1.540 1.449 123.29 116.37 120.93 109.72 111.57 109.97 122.69 24 ILE 24 1.308 1.238 1.526 1.559 1.450 122.19 118.34 119.70 109.11 108.48 111.32 121.93 * * * 25 PRO 25 1.348 1.247 1.529 1.535 1.462 122.46 115.61 120.85 109.80 111.77 103.80 123.54 * * 26 LEU 26 1.326 1.230 1.532 1.561 1.457 123.71 115.70 120.77 111.69 109.68 108.26 123.48 +* * * +* 27 GLY 27 1.326 1.236 1.525 - 1.456 122.01 117.04 120.22 - 114.10 - 122.74 28 PHE 28 1.324 1.221 1.532 1.540 1.454 121.08 117.01 120.93 112.04 110.01 110.55 122.05 * * 29 ASN 29 1.330 1.233 1.512 1.526 1.467 120.01 114.55 121.67 108.55 108.21 112.52 123.78 * * * 30 GLU 30 1.322 1.239 1.526 1.530 1.446 123.67 115.24 121.31 109.17 109.88 109.15 123.45 * * 31 TYR 31 1.314 1.237 1.536 1.537 1.435 122.81 117.24 120.33 111.62 111.20 109.61 122.41 * * * 32 PHE 32 1.333 1.235 1.544 1.567 1.449 119.87 117.95 121.28 110.67 112.50 112.06 120.68 +* * * +* 33 PRO 33 1.324 1.245 1.512 1.531 1.436 122.19 116.82 120.81 110.45 108.07 104.82 122.36 * ** * +* ** 34 ALA 34 1.280 1.235 1.499 1.532 1.439 120.39 117.45 119.59 110.15 110.27 109.77 122.93 *** * * *** 35 PRO 35 1.356 1.243 1.528 1.533 1.462 122.64 116.04 120.37 110.56 110.23 103.65 123.58 * * 36 PHE 36 1.305 1.234 1.539 1.534 1.448 122.88 118.19 120.30 110.37 111.12 108.51 121.48 +* * +* 37 PRO 37 1.337 1.235 1.530 1.536 1.444 122.92 116.88 120.77 110.43 111.50 103.19 122.29 * * 38 ILE 38 1.312 1.228 1.524 1.557 1.442 119.94 116.69 120.88 110.79 109.10 112.86 122.40 * * 39 THR 39 1.308 1.243 1.520 1.546 1.436 120.65 114.70 121.40 111.16 112.30 112.40 123.90 +* * +* 40 VAL 40 1.304 1.230 1.527 1.574 1.442 125.16 117.96 119.73 110.44 106.98 110.49 122.29 +* * +* +* +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 ASP 41 1.306 1.244 1.507 1.539 1.448 120.52 115.03 121.41 109.98 112.13 111.71 123.56 +* +* 42 LEU 42 1.313 1.238 1.487 1.557 1.443 122.67 116.40 120.26 107.22 106.01 113.36 123.34 * +* * +* +* +* +* 43 LEU 43 1.286 1.252 1.504 1.556 1.421 120.92 114.94 121.40 109.53 110.26 111.50 123.66 *** * * +* *** 44 ASP 44 1.295 1.239 1.500 1.534 1.441 122.58 115.97 120.35 108.87 107.80 110.47 123.68 ** * * ** 45 TYR 45 1.301 1.236 1.536 1.537 1.454 123.17 117.49 120.23 113.07 114.36 111.54 122.22 ** +* * ** 46 SER 46 1.322 1.232 1.552 1.549 1.452 121.23 116.68 121.13 111.41 110.40 110.41 122.19 * * 47 GLY 47 1.333 1.233 1.506 - 1.454 120.91 115.86 121.16 - 112.37 - 122.98 48 ARG 48 1.305 1.230 1.521 1.532 1.445 121.94 117.24 120.12 112.39 109.57 108.93 122.62 +* * +* 49 SER 49 1.311 1.240 1.523 1.532 1.441 120.69 115.60 121.08 111.32 112.01 110.35 123.30 * * 50 TRP 50 1.305 1.229 1.510 1.536 1.458 122.43 116.61 120.11 109.63 109.24 111.09 123.28 +* +* 51 THR 51 1.304 1.237 1.532 1.536 1.442 121.90 115.72 121.03 109.25 110.23 110.45 123.25 +* +* 52 VAL 52 1.304 1.230 1.498 1.549 1.442 123.22 115.51 121.17 108.68 110.86 113.90 123.31 +* * * +* 53 ARG 53 1.283 1.228 1.512 1.519 1.419 121.82 115.60 120.88 110.35 107.23 109.50 123.51 *** ** * *** 54 MET 54 1.296 1.227 1.501 1.548 1.447 122.69 116.58 120.43 111.90 106.90 107.31 122.97 ** * +* +* ** 55 LYS 55 1.304 1.238 1.520 1.518 1.421 120.42 115.63 121.06 111.79 112.06 108.24 123.31 +* +* * +* 56 LYS 56 1.321 1.239 1.518 1.531 1.437 122.98 116.97 120.43 106.78 105.93 109.49 122.59 * +* +* +* 57 ARG 57 1.284 1.244 1.505 1.541 1.445 121.14 115.10 121.01 109.14 110.32 112.47 123.89 *** * *** 58 GLY 58 1.306 1.230 1.504 - 1.432 122.46 115.37 121.32 - 115.00 - 123.27 +* * * +* 59 GLU 59 1.299 1.222 1.525 1.547 1.432 122.01 117.16 120.43 108.42 110.83 111.08 122.39 ** * ** 60 LYS 60 1.320 1.221 1.533 1.538 1.437 121.24 115.97 121.27 110.95 113.18 112.68 122.73 * * * 61 VAL 61 1.314 1.234 1.523 1.565 1.458 122.61 116.65 120.40 109.04 109.40 111.37 122.91 * * 62 PHE 62 1.311 1.238 1.513 1.538 1.436 121.82 116.03 120.62 109.27 109.92 111.78 123.32 * * * 63 LEU 63 1.307 1.225 1.499 1.561 1.453 121.97 117.08 120.22 109.93 105.60 112.99 122.66 +* * +* ** * ** 64 THR 64 1.298 1.226 1.537 1.549 1.431 119.97 115.40 121.29 111.46 115.44 110.98 123.26 ** * * +* ** 65 VAL 65 1.306 1.224 1.515 1.557 1.460 123.82 116.01 120.76 109.98 111.45 111.41 123.19 +* * +* 66 GLY 66 1.318 1.230 1.480 - 1.432 120.21 116.08 120.64 - 112.61 - 123.28 +* * +* 67 TRP 67 1.325 1.243 1.511 1.544 1.449 121.60 114.60 121.99 110.53 109.50 111.09 123.26 68 GLU 68 1.298 1.211 1.522 1.518 1.432 120.58 116.22 120.57 112.43 110.60 111.60 123.15 ** * * * ** Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 69 ASN 69 1.328 1.204 1.503 1.547 1.462 122.64 114.41 121.67 107.75 108.75 111.65 123.82 * * * * 70 PHE 70 1.299 1.232 1.509 1.543 1.435 124.46 116.11 120.80 110.63 109.62 108.79 123.09 ** * +* * ** 71 VAL 71 1.327 1.223 1.512 1.560 1.445 120.78 115.89 120.83 110.40 110.58 112.90 123.28 72 LYS 72 1.310 1.232 1.525 1.549 1.454 120.83 117.35 120.44 111.42 112.48 113.64 122.21 * +* +* 73 ASP 73 1.322 1.232 1.532 1.524 1.462 119.57 116.99 120.79 112.35 112.25 111.21 122.17 * * * 74 ASN 74 1.318 1.226 1.512 1.547 1.473 120.90 116.35 119.69 109.24 112.03 112.81 123.93 * * 75 ASN 75 1.338 1.237 1.517 1.511 1.434 124.59 115.36 121.69 112.48 112.32 113.12 122.89 * +* * +* +* 76 LEU 76 1.312 1.237 1.500 1.526 1.430 121.24 114.20 121.63 110.66 111.75 111.59 124.16 * * * * 77 GLU 77 1.291 1.246 1.491 1.509 1.431 123.96 115.09 120.59 107.95 109.48 109.30 124.31 +** +* * * * * +** 78 ASP 78 1.297 1.234 1.518 1.556 1.464 121.80 116.90 120.35 110.23 108.88 112.18 122.68 ** * ** 79 GLY 79 1.306 1.224 1.502 - 1.443 120.20 116.44 120.69 - 111.82 - 122.83 +* +* 80 LYS 80 1.320 1.234 1.516 1.536 1.457 121.22 117.53 120.00 112.50 110.05 111.87 122.47 * * 81 TYR 81 1.316 1.233 1.480 1.533 1.436 120.20 114.91 121.04 109.54 110.98 111.45 124.05 ** * ** 82 LEU 82 1.285 1.237 1.515 1.556 1.411 122.76 116.84 120.22 111.61 109.24 111.46 122.90 *** * ** *** 83 GLN 83 1.308 1.239 1.491 1.530 1.439 120.65 115.27 120.75 108.44 109.45 114.14 123.97 +* +* ** ** 84 PHE 84 1.291 1.236 1.503 1.532 1.425 122.81 116.40 120.37 109.15 109.66 110.33 123.19 +** * +* +** 85 ILE 85 1.303 1.230 1.511 1.544 1.434 121.09 115.52 120.84 110.37 106.40 112.05 123.62 +* * +* +* 86 TYR 86 1.289 1.241 1.521 1.537 1.429 123.21 115.37 121.11 111.77 111.11 106.82 123.52 +** +* ** +** 87 ASP 87 1.323 1.233 1.499 1.529 1.478 123.36 115.74 120.31 107.67 111.67 111.25 123.94 * * * * 88 ARG 88 1.340 1.234 1.519 1.514 1.474 123.79 113.80 122.12 111.68 110.19 111.76 124.00 * * * 89 ASP 89 1.301 1.219 1.535 1.552 1.431 124.91 118.59 119.59 110.84 104.01 107.48 121.76 ** * * +* * +** +* +** 90 ARG 90 1.286 1.236 1.536 1.532 1.460 121.78 115.76 121.48 109.76 109.54 109.97 122.71 *** *** 91 THR 91 1.309 1.245 1.549 1.546 1.433 121.97 115.60 120.66 109.85 111.66 108.79 123.68 * * * +* +* 92 PHE 92 1.331 1.233 1.514 1.538 1.460 123.45 116.82 120.31 105.74 109.73 113.22 122.87 ** +* ** 93 TYR 93 1.298 1.232 1.510 1.533 1.449 121.50 116.76 120.45 110.75 107.06 112.24 122.75 ** * * ** 94 VAL 94 1.304 1.235 1.530 1.554 1.452 120.92 115.96 120.72 109.35 111.25 111.12 123.29 +* +* 95 ILE 95 1.321 1.228 1.535 1.589 1.461 122.94 117.26 119.85 108.82 108.25 113.44 122.88 +* * * +* 96 ILE 96 1.323 1.234 1.518 1.592 1.473 122.41 116.33 120.49 107.39 109.18 112.85 123.17 +* +* Residue-by-residue listing for refined_6 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 ----------------------------------------------------------------------------------------------------------------------------------- 97 TYR 97 1.312 1.238 1.507 1.531 1.441 121.72 115.77 120.64 110.15 107.40 111.02 123.58 * * * 98 GLY 98 1.300 1.238 1.503 - 1.426 121.11 116.17 120.47 - 108.82 - 123.33 ** +* * ** 99 HIS 99 1.316 1.239 1.532 1.545 1.454 122.14 114.81 120.88 111.68 112.74 111.18 124.26 100 ASN 100 1.332 1.241 1.555 1.563 1.473 124.72 117.63 120.47 111.68 109.52 109.36 121.88 * +* +* +* 101 MET 101 1.306 1.237 1.522 1.545 1.442 121.69 116.25 120.73 111.62 106.02 109.65 122.88 +* +* +* 102 CYS 102 1.304 - 1.521 1.533 1.435 121.84 - - 111.81 111.08 109.44 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.1* * +** +* ** +* * ** +** ** * *5.1* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 1.258 1.347 1.309 .015 *5.1* * * C-N (Pro) 1.341 .016 5 1.324 1.356 1.343 .012 * C-O C-O 1.231 .020 101 1.204 1.252 1.233 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.471 1.555 1.518 .015 +** * CH2G*-C (Gly) 1.516 .018 7 1.474 1.525 1.499 .016 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.523 1.532 1.527 .004 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.536 1.592 1.559 .015 +* CH1E-CH2E (the rest) 1.530 .020 75 1.509 1.567 1.537 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.411 1.478 1.445 .014 ** * NH1-CH2G* (Gly) 1.451 .016 7 1.422 1.456 1.438 .012 +* N-CH1E (Pro) 1.466 .015 5 1.436 1.470 1.455 .013 ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_6 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 89 113.80 118.59 116.26 1.03 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.20 117.04 115.88 .83 * CH1E-C-N (Pro) 116.9 1.5 5 114.95 116.88 116.06 .74 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.68 124.31 123.03 .67 * O-C-N (Pro) 122.0 1.4 5 122.29 123.58 123.03 .58 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.36 125.16 121.97 1.34 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 7 120.20 122.46 121.12 .79 * C-N-CH1E (Pro) 122.6 5.0 5 122.19 122.92 122.57 .24 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.53 122.12 120.70 .57 CH2G*-C-O (Gly) 120.8 2.1 7 120.22 121.81 120.90 .51 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.15 111.42 110.79 .64 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.39 111.46 109.90 1.08 * CH2E-CH1E-C (the rest) 110.1 1.9 75 105.74 113.29 110.40 1.52 ** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.01 115.44 109.95 2.09 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 108.82 115.00 112.45 1.81 * N-CH1E-C (Pro) 111.8 2.5 5 108.07 112.78 110.87 1.62 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.77 111.48 110.63 .86 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.79 113.90 111.85 1.25 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.19 104.82 103.85 .53 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.82 114.14 110.76 1.70 ** ** ------------------------------------------------------------------------------------------------------------- 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_6 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] 75 85.2% Residues in additional allowed regions [a,b,l,p] 13 14.8% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% 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 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 85.2 83.8 10.0 .1 Inside b. Omega angle st dev 101 4.4 6.0 3.0 -.5 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 59 .9 .8 .2 .6 Inside f. Overall G-factor 102 -.1 -.4 .3 .9 Inside S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 18 6.6 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 32 5.7 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 38 6.6 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 88 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 25 7.6 20.4 5.0 -2.6 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 85.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.7 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .92 3 Residue-by-residue listing for refined_6 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.55 Chi1-chi2 distribution -.44 Chi1 only .02 Chi3 & chi4 .31 Omega -.28 ------ -.31 ===== Main-chain covalent forces:- Main-chain bond lengths -.07 Main-chain bond angles .37 ------ .19 ===== OVERALL AVERAGE -.13 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.