Residue-by-residue listing for refined_5 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 - - 178.1 - 178.4 - - - - - - 179.8 - 33.8 - 2 ALA 2 B - - - - - - - - - - 177.9 - 34.2 - 3 ASP 3 B - 176.8 - - - - - - - - 179.3 - 34.1 - 4 THR 4 A - - -50.7 - - - - - - - 177.6 -.5 34.5 - * ** ** 5 GLY 5 - - - - - - - - - - - 179.4 - - - 6 GLU 6 B - 180.2 - 185.1 - - - - - - 176.5 -1.9 34.8 - 7 VAL 7 E B - - -64.9 - - - - - - - 180.0 -2.9 33.4 - * * 8 GLN 8 E B 55.4 - - 183.4 - - - - - - 179.4 - 34.2 - 9 PHE 9 E B - 192.2 - - - - - - - - 181.3 -2.0 34.8 - 10 MET 10 E B 61.9 - - 179.0 - - - - - - 182.1 - 33.1 - 11 LYS 11 E B - - -81.5 - - - - - - - 166.5 -2.8 34.1 - ** * ** 12 PRO 12 E - - - - - -80.4 - - - - - 184.8 - 39.0 - * * * 13 PHE 13 e B 57.2 - - - - - - - - - 180.5 -.6 33.1 - +* +* 14 ILE 14 h B - - -58.8 177.6 - - - - - - 186.0 - 34.8 - * * 15 SER 15 H A - 186.4 - - - -55.1 -29.2 - - - 179.6 -.6 32.8 - +* +* 16 GLU 16 H A - 178.0 - 184.6 - -59.7 -44.1 - - - 183.3 - 35.5 - 17 LYS 17 H A - 184.5 - 186.1 - -92.8 -40.6 - - - 184.8 -1.2 35.3 - ** * ** 18 SER 18 H A - - -55.1 - - -75.2 -1.4 - - - 172.7 -3.4 32.6 - *** * +* *** Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 19 SER 19 h A - - -69.6 - - - - - - - 181.5 -.9 31.5 - * * 20 LYS 20 T a 59.5 - - 181.9 - - - - - - 183.2 -1.8 33.2 - 21 SER 21 t B 54.6 - - - - - - - - - 180.2 -2.8 34.1 - 22 LEU 22 E B - 183.0 - 163.5 - - - - - - 182.8 -2.2 31.7 - 23 GLU 23 E B 53.9 - - 175.5 - - - - - - 174.6 - 35.6 - 24 ILE 24 e B - - -59.6 - - - - - - - 182.5 -1.0 33.0 - * * 25 PRO 25 h - - - - - -53.3 - - - - - 184.6 - 38.8 - * * * 26 LEU 26 H A - 182.7 - - - -52.6 -46.8 - - - 182.0 - 34.5 - * * 27 GLY 27 H - - - - - - -65.8 -22.3 - - - 180.1 - - - +* +* 28 PHE 28 H A - 184.3 - - - -86.5 -35.7 - - - 178.9 -1.4 34.1 - +* +* 29 ASN 29 H A - - -55.3 - - -69.1 -36.3 - - - 177.2 -2.0 34.0 - 30 GLU 30 h A - 178.1 - 186.7 - - - - - - 185.4 -2.4 37.0 - 31 TYR 31 T A - 180.5 - - - - - - - - 181.5 - 34.4 - 32 PHE 32 t B 67.5 - - - - - - - - - 167.5 -1.0 31.1 - ** * ** 33 PRO 33 - - - - - -81.4 - - - - - 186.7 - 38.8 - * * * * 34 ALA 34 B - - - - - - - - - - 176.0 - 34.9 - 35 PRO 35 - - - - - -60.8 - - - - - 185.7 - 38.1 - * * 36 PHE 36 B - 182.4 - - - - - - - - 178.7 - 34.4 - 37 PRO 37 - - - - - -95.0 - - - - - 174.6 - 39.8 - +** +* +** 38 ILE 38 e A - - -58.4 - - - - - - - 178.9 - 34.0 - 39 THR 39 E B 50.4 - - - - - - - - - 178.1 - 34.2 - 40 VAL 40 E B 61.0 - - - - - - - - - 188.7 -3.1 33.3 - +* * +* 41 ASP 41 E B - 186.4 - - - - - - - - 178.8 -2.4 34.5 - 42 LEU 42 E B - - -59.1 - - - - - - - 178.0 -3.3 36.2 - +* +* 43 LEU 43 E B - - -64.8 - - - - - - - 180.6 -3.3 33.5 - +* +* 44 ASP 44 e B - 169.4 - - - - - - - - 182.8 -2.8 34.9 - * * 45 TYR 45 T A - 185.0 - - - - - - - - 185.1 - 35.2 - 46 SER 46 T A - - -54.9 - - - - - - - 177.9 - 34.1 - 47 GLY 47 t - - - - - - - - - - - 179.0 -2.1 - - 48 ARG 48 e B - - -62.5 - - - - - - - 178.4 - 33.8 - 49 SER 49 E B 51.3 - - - - - - - - - 181.0 - 31.8 - 50 TRP 50 E B - - -71.9 - - - - - - - 177.4 -1.9 33.9 - 51 THR 51 E B - - -53.8 - - - - - - - 181.2 - 34.8 - 52 VAL 52 E B 62.3 - - - - - - - - - 178.4 -3.3 33.4 - +* +* 53 ARG 53 E B - - -67.1 177.5 - - - - - - 187.9 -1.4 33.5 - * * 54 MET 54 E B - 179.4 - 179.9 - - - - - - 181.2 -1.0 36.2 - * * 55 LYS 55 E B - - -74.7 - - - - - - - 179.5 -2.3 31.5 - 56 LYS 56 E B - 176.8 - 174.0 - - - - - - 177.7 - 33.9 - 57 ARG 57 E b 61.5 - - 177.5 - - - - - - 177.5 -3.4 32.0 - +* +* Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 GLY 58 T - - - - - - - - - - - 186.3 - - - * * 59 GLU 59 T A - - -55.6 - - - - - - - 184.0 - 35.4 - 60 LYS 60 E B - 185.5 - 183.7 - - - - - - 173.6 -2.3 34.5 - * * 61 VAL 61 E B - 180.2 - - - - - - - - 176.7 - 35.1 - 62 PHE 62 E B 60.6 - - - - - - - - - 184.5 -2.9 31.9 - * * 63 LEU 63 E B - 196.5 - - - - - - - - 186.6 -2.6 35.5 - * * 64 THR 64 e b 53.7 - - - - - - - - - 185.1 -2.2 33.9 - 65 VAL 65 T B - 182.3 - - - - - - - - 187.2 - 33.3 - * * 66 GLY 66 h - - - - - - - - - - - 175.4 - - - 67 TRP 67 H A - 167.4 - - - -62.8 -29.4 - - - 182.2 -1.5 35.1 - 68 GLU 68 H A 45.7 - - - - -64.5 -26.0 - - - 175.0 - 26.2 - * * ** ** 69 ASN 69 H A - - -61.3 - - -66.3 -46.6 - - - 186.9 -1.1 35.4 - * * * 70 PHE 70 H A - 178.8 - - - -72.9 -45.3 - - - 183.8 -.9 35.0 - +* +* 71 VAL 71 H A 74.0 - - - - -64.8 -43.8 - - - 178.9 -3.1 33.2 - * * 72 LYS 72 H A - - -60.1 - - -72.7 -38.9 - - - 184.8 -1.5 30.7 - 73 ASP 73 H A - 189.5 - - - -68.4 -40.4 - - - 181.5 -2.5 33.5 - 74 ASN 74 h A - 189.2 - - - - - - - - 182.2 -2.4 34.3 - 75 ASN 75 T l - 188.5 - - - - - - - - 181.7 - 30.9 - 76 LEU 76 t B - - -61.3 178.1 - - - - - - 177.7 -3.2 34.5 - +* +* 77 GLU 77 t B - - -55.4 179.0 - - - - - - 177.1 -.7 35.5 - +* +* 78 ASP 78 T B 47.9 - - - - - - - - - 183.3 - 31.1 - * * 79 GLY 79 T - - - - - - - - - - - 174.2 - - - * * 80 LYS 80 e B - - -67.6 186.7 - - - - - - 183.2 -1.6 32.5 - 81 TYR 81 E B - - -55.2 - - - - - - - 181.9 - 35.0 - 82 LEU 82 E B 46.5 - - - - - - - - - 178.6 -1.5 30.7 - * * 83 GLN 83 E B - 177.2 - 181.8 - - - - - - 178.2 -3.1 35.1 - * * 84 PHE 84 E B - - -66.5 - - - - - - - 172.2 -3.0 34.9 - * * * 85 ILE 85 E B - - -64.0 - - - - - - - 179.4 -2.3 33.7 - 86 TYR 86 E B - 178.9 - - - - - - - - 186.9 -3.6 35.8 - * ** ** 87 ASP 87 e A - 187.5 - - - - - - - - 180.6 -1.5 34.7 - 88 ARG 88 S ~l - 189.4 - - - - - - - - 179.7 - 32.0 - ** ** 89 ASP 89 S b - 192.9 - - - - - - - - 183.5 - 36.2 - 90 ARG 90 e a - - -63.6 178.4 - - - - - - 178.1 - 34.7 - 91 THR 91 E B 57.0 - - - - - - - - - 173.2 - 35.3 - * * 92 PHE 92 E B - - -74.5 - - - - - - - 175.1 -2.7 34.6 - 93 TYR 93 E B - - -58.4 - - - - - - - 186.3 -2.5 33.7 - * * 94 VAL 94 E B - 187.9 - - - - - - - - 177.7 -2.0 34.5 - Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 95 ILE 95 E B - - -62.8 - - - - - - - 176.9 -3.0 34.5 - * * 96 ILE 96 E B - - -69.5 - - - - - - - 182.8 -.5 33.5 - +* +* 97 TYR 97 e B - - -68.6 - - - - - - - 181.3 -3.2 34.1 - +* +* 98 GLY 98 S - - - - - - - - - - - 181.7 - - - 99 HIS 99 l 65.0 - - - - - - - - - 182.1 -.9 28.0 - +* +* +* 100 ASN 100 b - 185.2 - - - - - - - - 178.6 - 34.3 - 101 MET 101 b - 192.6 - - - - - - - - 179.6 -1.0 34.1 - * * 102 CYS 102 - - 184.9 - - - - - - - - - - 34.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +** ** *** ** ** ** *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.3 183.3 -62.7 179.9 -74.2 -68.6 -35.1 - - - 180.3 -2.1 34.1 Standard deviations: 7.2 6.3 7.1 5.3 16.9 10.6 12.1 - - - 4.1 .9 2.0 Numbers of values: 20 36 32 21 5 15 15 0 0 0 101 58 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_5 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 - 1.235 1.515 1.539 1.465 - 116.41 120.46 110.47 110.54 110.89 123.12 2 ALA 2 1.319 1.240 1.512 1.528 1.446 122.10 116.30 120.54 110.26 110.08 110.65 123.15 3 ASP 3 1.312 1.242 1.504 1.533 1.452 121.70 116.24 120.31 109.82 109.69 111.50 123.43 * * 4 THR 4 1.312 1.241 1.530 1.540 1.434 121.72 115.44 121.00 110.51 109.21 110.40 123.52 * * * 5 GLY 5 1.313 1.235 1.474 - 1.441 121.66 113.40 121.76 - 112.90 - 124.85 * ** * * ** 6 GLU 6 1.265 1.247 1.516 1.521 1.427 124.00 115.47 121.04 109.77 110.10 110.34 123.46 *4.5* +* * *4.5* 7 VAL 7 1.294 1.228 1.513 1.567 1.431 122.47 116.79 120.72 110.33 108.75 112.72 122.47 ** * * ** 8 GLN 8 1.288 1.237 1.501 1.527 1.414 121.23 116.84 120.41 111.61 109.65 109.70 122.74 +** * ** +** 9 PHE 9 1.300 1.233 1.523 1.545 1.440 120.49 116.84 120.09 111.38 108.76 109.27 123.07 ** ** 10 MET 10 1.312 1.241 1.517 1.534 1.459 121.54 115.91 120.91 110.33 111.33 111.78 123.17 * * 11 LYS 11 1.313 1.237 1.515 1.542 1.447 122.24 116.62 121.10 109.04 113.65 111.08 122.24 * * 12 PRO 12 1.338 1.241 1.525 1.544 1.443 122.41 116.87 120.49 110.18 107.50 104.27 122.65 +* +* * +* Residue-by-residue listing for refined_5 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 13 PHE 13 1.288 1.232 1.514 1.546 1.435 121.25 116.15 120.70 112.16 111.01 110.31 123.13 +** * * +** 14 ILE 14 1.307 1.234 1.513 1.558 1.437 121.92 116.96 119.67 110.17 107.72 111.11 123.37 +* * * +* 15 SER 15 1.332 1.215 1.543 1.545 1.468 122.62 116.90 120.49 111.36 112.10 110.71 122.54 16 GLU 16 1.320 1.237 1.530 1.531 1.459 122.62 115.95 121.17 109.07 110.80 109.71 122.85 17 LYS 17 1.310 1.241 1.510 1.533 1.440 121.16 115.36 121.14 110.06 109.83 109.48 123.43 * * 18 SER 18 1.312 1.209 1.530 1.520 1.431 122.50 117.77 120.11 112.48 113.06 109.60 122.11 * * * * * 19 SER 19 1.329 1.231 1.527 1.539 1.462 119.67 116.74 120.58 110.86 111.31 113.39 122.67 * +* +* 20 LYS 20 1.329 1.227 1.531 1.530 1.443 120.60 117.21 120.26 111.13 113.07 110.18 122.52 21 SER 21 1.318 1.235 1.536 1.540 1.455 120.72 116.84 120.57 111.31 111.84 109.24 122.60 22 LEU 22 1.319 1.239 1.528 1.558 1.444 121.11 114.70 121.25 113.89 110.61 110.60 124.04 * +* +* 23 GLU 23 1.316 1.242 1.544 1.541 1.450 124.41 116.65 121.12 109.71 112.10 108.59 122.23 +* * +* 24 ILE 24 1.313 1.241 1.547 1.590 1.444 120.84 118.36 119.62 110.17 107.48 113.95 121.98 * * +* * * * +* 25 PRO 25 1.361 1.237 1.528 1.522 1.487 123.52 115.37 120.82 109.90 113.53 103.19 123.75 * * * * * 26 LEU 26 1.332 1.235 1.530 1.536 1.465 124.38 116.05 120.59 110.09 112.25 109.64 123.30 * * 27 GLY 27 1.323 1.231 1.513 - 1.454 121.59 116.18 120.81 - 113.26 - 123.00 28 PHE 28 1.306 1.215 1.527 1.541 1.437 122.01 117.26 120.23 112.04 109.26 109.45 122.45 +* * * +* 29 ASN 29 1.345 1.232 1.506 1.531 1.482 120.69 114.97 121.19 107.27 109.76 113.89 123.83 * * * +* +* 30 GLU 30 1.327 1.236 1.530 1.535 1.466 124.02 114.32 121.95 109.00 109.63 107.88 123.67 * +* +* 31 TYR 31 1.305 1.232 1.544 1.535 1.430 124.03 118.51 120.02 111.87 112.89 107.92 121.46 +* * * * +* +* 32 PHE 32 1.328 1.242 1.538 1.567 1.456 118.34 117.21 121.40 111.25 113.98 112.65 121.29 +* +* * * +* 33 PRO 33 1.337 1.246 1.512 1.523 1.437 122.04 116.38 120.83 109.72 108.25 104.77 122.78 +* * +* +* 34 ALA 34 1.273 1.238 1.503 1.531 1.438 121.34 117.79 119.77 110.27 110.03 109.80 122.43 **** * * **** 35 PRO 35 1.343 1.239 1.516 1.534 1.451 122.21 116.16 120.08 110.85 109.70 104.42 123.76 * * * * 36 PHE 36 1.315 1.238 1.525 1.540 1.452 122.53 116.95 120.68 110.66 110.97 109.73 122.33 37 PRO 37 1.337 1.234 1.522 1.528 1.436 123.08 116.05 121.34 109.88 111.70 102.59 122.56 ** ** 38 ILE 38 1.292 1.232 1.516 1.555 1.433 120.84 115.55 121.28 110.29 107.77 112.04 123.13 +** * * +** 39 THR 39 1.314 1.242 1.531 1.546 1.430 122.42 115.23 121.18 109.88 111.25 110.86 123.59 * * * 40 VAL 40 1.304 1.238 1.547 1.571 1.438 124.20 118.97 119.14 113.26 106.57 110.45 121.88 +* * * * * * +* +* +* 41 ASP 41 1.320 1.245 1.537 1.541 1.471 120.17 115.67 120.84 111.04 112.47 108.69 123.49 * * 42 LEU 42 1.327 1.234 1.499 1.561 1.458 123.16 116.58 120.33 105.66 108.30 113.22 123.08 * +* ** * +* ** Residue-by-residue listing for refined_5 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 1.294 1.243 1.515 1.550 1.431 121.20 115.16 120.95 110.13 109.71 112.22 123.89 ** * * * ** 44 ASP 44 1.304 1.241 1.514 1.535 1.449 123.74 114.58 120.98 110.60 111.00 109.11 124.44 +* * +* 45 TYR 45 1.313 1.235 1.545 1.546 1.460 125.73 117.11 120.41 110.26 112.92 108.47 122.44 * ** * ** 46 SER 46 1.322 1.235 1.533 1.517 1.456 121.40 116.73 120.88 110.53 112.22 109.67 122.39 47 GLY 47 1.317 1.229 1.502 - 1.444 120.28 116.36 120.82 - 112.47 - 122.82 48 ARG 48 1.309 1.229 1.523 1.534 1.443 121.36 117.15 120.26 110.83 109.46 110.94 122.54 * * 49 SER 49 1.305 1.239 1.521 1.541 1.433 121.03 115.53 120.89 112.93 111.50 111.05 123.54 +* * * +* 50 TRP 50 1.306 1.212 1.504 1.543 1.460 122.98 116.23 120.74 109.34 111.06 111.87 123.03 +* +* 51 THR 51 1.298 1.242 1.539 1.535 1.431 121.71 115.94 120.92 110.04 109.54 110.30 123.13 ** * ** 52 VAL 52 1.306 1.225 1.525 1.567 1.444 122.97 116.60 120.54 110.70 109.64 111.96 122.82 +* * +* 53 ARG 53 1.296 1.228 1.523 1.520 1.428 122.12 115.70 121.06 113.00 109.52 109.17 123.22 ** +* +* ** 54 MET 54 1.311 1.215 1.513 1.536 1.456 122.77 117.18 120.28 110.23 110.29 107.81 122.54 * +* +* 55 LYS 55 1.317 1.231 1.520 1.551 1.454 120.58 115.13 121.50 110.75 112.52 113.14 123.37 * +* +* 56 LYS 56 1.316 1.232 1.487 1.527 1.446 123.23 114.85 121.21 109.92 110.38 111.57 123.94 +* +* 57 ARG 57 1.272 1.235 1.527 1.546 1.429 122.80 115.35 121.56 112.03 109.83 112.44 122.94 **** +* * * **** 58 GLY 58 1.310 1.247 1.518 - 1.443 121.54 115.51 120.98 - 113.35 - 123.39 * * 59 GLU 59 1.318 1.221 1.521 1.555 1.447 122.51 117.89 120.03 107.12 111.07 112.03 122.08 * +* +* 60 LYS 60 1.321 1.235 1.528 1.538 1.447 119.60 115.43 121.41 110.16 112.23 109.79 123.13 * * 61 VAL 61 1.310 1.232 1.506 1.561 1.432 123.41 116.53 120.33 108.11 107.21 112.87 123.12 * * * * 62 PHE 62 1.286 1.246 1.504 1.551 1.420 121.30 115.91 120.93 113.31 108.18 112.14 123.10 *** * * +* +* * *** 63 LEU 63 1.292 1.234 1.520 1.518 1.427 121.08 116.81 119.96 110.87 107.97 108.78 123.23 +** +* * * +** 64 THR 64 1.310 1.247 1.553 1.547 1.444 122.29 115.90 120.86 111.41 112.60 109.13 123.24 * * * * * 65 VAL 65 1.349 1.241 1.526 1.566 1.469 123.79 115.54 121.17 110.68 110.87 111.54 123.29 * * * 66 GLY 66 1.306 1.236 1.481 - 1.418 121.67 114.00 121.62 - 108.44 - 124.35 +* +* ** * * ** 67 TRP 67 1.327 1.235 1.501 1.546 1.444 123.68 114.92 121.48 110.60 109.11 109.69 123.51 * * * 68 GLU 68 1.311 1.219 1.539 1.550 1.429 121.12 116.76 120.61 115.93 113.79 113.89 122.62 * +* *** +* *** 69 ASN 69 1.330 1.209 1.506 1.544 1.476 121.67 114.61 121.59 106.63 109.41 112.77 123.75 * +* * +* 70 PHE 70 1.300 1.239 1.505 1.544 1.438 123.97 115.85 120.52 110.49 110.81 109.40 123.62 ** * * ** Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.324 1.226 1.517 1.576 1.446 121.28 115.69 121.33 111.21 109.31 111.93 122.98 * * 72 LYS 72 1.314 1.230 1.519 1.533 1.434 121.02 117.60 119.90 112.37 112.68 112.52 122.48 * * * * * 73 ASP 73 1.343 1.240 1.523 1.531 1.484 119.82 116.76 120.66 109.16 111.87 112.01 122.53 * * * 74 ASN 74 1.324 1.228 1.534 1.548 1.462 120.69 114.84 121.36 110.51 109.56 110.52 123.78 75 ASN 75 1.325 1.253 1.522 1.534 1.465 125.08 114.25 122.48 111.88 111.05 113.25 123.14 * +* +* +* 76 LEU 76 1.290 1.231 1.501 1.526 1.417 122.39 115.34 121.32 110.56 110.00 110.29 123.32 +** * ** +** 77 GLU 77 1.290 1.249 1.508 1.541 1.427 122.74 117.48 119.54 110.13 106.35 110.27 122.98 +** +* +* +** 78 ASP 78 1.303 1.230 1.514 1.536 1.447 120.60 114.80 121.67 112.64 110.80 112.42 123.45 +* * * +* 79 GLY 79 1.304 1.231 1.501 - 1.433 122.07 115.31 121.38 - 109.61 - 123.31 +* * +* 80 LYS 80 1.313 1.231 1.516 1.543 1.444 121.73 117.25 120.03 111.44 109.04 112.55 122.73 * * * 81 TYR 81 1.313 1.238 1.499 1.541 1.447 121.50 117.12 119.78 110.00 108.21 110.60 123.10 * * * * 82 LEU 82 1.304 1.239 1.521 1.548 1.439 121.00 114.75 121.31 113.10 113.80 111.39 123.92 +* +* +* 83 GLN 83 1.306 1.238 1.518 1.534 1.436 123.92 116.30 120.49 109.88 109.23 110.07 123.21 +* * * +* 84 PHE 84 1.307 1.234 1.495 1.529 1.443 122.12 116.02 120.58 107.95 110.60 111.92 123.37 +* * * +* 85 ILE 85 1.295 1.239 1.521 1.579 1.429 121.53 116.06 120.52 109.54 107.09 113.79 123.41 ** * +* * * ** 86 TYR 86 1.301 1.220 1.511 1.548 1.439 122.58 116.14 120.83 111.23 106.98 108.60 123.02 +* +* * +* 87 ASP 87 1.304 1.226 1.533 1.544 1.470 121.73 115.12 121.97 111.85 110.37 108.22 122.90 +* * +* 88 ARG 88 1.327 1.236 1.548 1.558 1.489 125.08 116.11 121.14 111.33 111.28 112.20 122.73 * * +* +* +* 89 ASP 89 1.315 1.219 1.528 1.551 1.423 123.55 116.89 120.41 110.81 106.59 108.55 122.60 * +* * +* * +* 90 ARG 90 1.276 1.232 1.522 1.531 1.447 123.31 116.07 121.12 110.49 110.15 109.65 122.81 +*** +*** 91 THR 91 1.309 1.248 1.536 1.549 1.426 121.09 116.39 120.37 109.32 110.74 110.18 123.23 * +* +* 92 PHE 92 1.320 1.225 1.498 1.537 1.451 122.21 116.77 120.54 107.33 109.52 113.28 122.68 * * +* +* 93 TYR 93 1.284 1.234 1.508 1.527 1.436 120.64 116.64 120.26 111.89 106.99 110.79 123.03 *** * +* *** 94 VAL 94 1.307 1.231 1.520 1.549 1.443 120.83 116.00 120.86 109.20 110.85 111.38 123.13 +* +* 95 ILE 95 1.306 1.225 1.526 1.566 1.444 122.16 116.64 120.54 109.63 109.58 111.41 122.81 +* +* 96 ILE 96 1.310 1.245 1.527 1.597 1.456 121.88 116.43 120.34 110.45 108.22 112.74 123.23 * ** * ** 97 TYR 97 1.320 1.239 1.504 1.535 1.447 121.99 115.07 121.32 109.21 110.98 111.70 123.61 98 GLY 98 1.299 1.220 1.492 - 1.421 121.88 115.09 120.47 - 110.22 - 124.38 ** * +* ** Residue-by-residue listing for refined_5 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 HIS 99 1.329 1.230 1.528 1.569 1.468 124.77 115.05 122.22 113.93 112.56 114.49 122.63 +* +* ** ** ** 100 ASN 100 1.293 1.232 1.509 1.536 1.429 121.45 116.04 120.56 111.05 109.82 110.14 123.25 +** +* +** 101 MET 101 1.314 1.239 1.516 1.551 1.443 122.13 115.93 120.74 110.76 108.43 111.16 123.27 * * * 102 CYS 102 1.305 - 1.514 1.546 1.440 122.79 - - 111.00 107.96 111.14 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.5* * ** ** ** ** * *** +* ** * *4.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 1.265 1.349 1.310 .015 *4.5* * * C-N (Pro) 1.341 .016 5 1.337 1.361 1.343 .009 * C-O C-O 1.231 .020 101 1.209 1.253 1.234 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.487 1.553 1.521 .013 +* * CH2G*-C (Gly) 1.516 .018 7 1.474 1.518 1.497 .015 ** * CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.528 1.531 1.530 .001 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.535 1.597 1.562 .016 ** CH1E-CH2E (the rest) 1.530 .020 75 1.517 1.569 1.539 .011 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.414 1.489 1.446 .015 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.418 1.454 1.436 .012 ** N-CH1E (Pro) 1.466 .015 5 1.436 1.487 1.451 .019 ** * * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_5 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 89 114.25 118.97 116.21 .97 * CH2G*-C-NH1 (Gly) 116.4 2.1 7 113.40 116.36 115.12 1.01 * CH1E-C-N (Pro) 116.9 1.5 5 115.37 116.87 116.17 .49 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.29 124.85 123.06 .60 * * O-C-N (Pro) 122.0 1.4 5 122.56 123.76 123.10 .54 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.34 125.73 122.10 1.36 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 7 120.28 122.07 121.53 .54 C-N-CH1E (Pro) 122.6 5.0 5 122.04 123.52 122.65 .56 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.14 122.48 120.75 .59 CH2G*-C-O (Gly) 120.8 2.1 7 120.47 121.76 121.12 .44 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.26 110.27 110.26 .01 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.11 113.26 110.27 1.04 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 105.66 115.93 110.67 1.66 ** *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 106.35 113.98 110.24 1.81 +* NH1-CH2G*-C (Gly) 112.5 2.9 7 108.44 113.35 111.46 1.85 * N-CH1E-C (Pro) 111.8 2.5 5 107.50 113.53 110.14 2.22 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.80 110.65 110.23 .43 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.13 113.95 111.60 1.26 * * N-CH1E-CH2E (Pro) 103.0 1.1 5 102.59 104.77 103.85 .82 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.81 114.49 110.76 1.63 +* ** ------------------------------------------------------------------------------------------------------------- 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_5 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] 78 88.6% Residues in additional allowed regions [a,b,l,p] 9 10.2% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.1% 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 88.6 83.8 10.0 .5 Inside b. Omega angle st dev 101 4.1 6.0 3.0 -.6 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 2.0 3.1 1.6 -.7 Inside e. H-bond energy st dev 58 .9 .8 .2 .5 Inside f. Overall G-factor 102 -.1 -.4 .3 1.1 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 20 7.2 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 36 6.3 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 32 7.1 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 88 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 21 5.3 20.4 5.0 -3.0 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% 88.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .91 3 Residue-by-residue listing for refined_5 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.44 Chi1-chi2 distribution -.37 Chi1 only -.21 Chi3 & chi4 .50 Omega -.15 ------ -.21 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .38 ------ .20 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.