Residue-by-residue listing for refined_1 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 - - 173.2 - - - - - - - - 176.5 - 34.1 - 2 GLY 2 - - - - - - - - - - - 181.2 - - - 3 HIS 3 S b - 187.0 - - - - - - - - 179.3 - 32.9 - 4 HIS 4 S a - - -70.1 - - - - - - - 177.9 -2.2 33.4 - 5 HIS 5 S b - - -65.6 - - - - - - - 174.0 - 35.4 - * * 6 HIS 6 S B 59.8 - - - - - - - - - 181.8 - 32.5 - 7 HIS 7 S b - 184.0 - - - - - - - - 184.0 - 33.7 - 8 HIS 8 B 69.9 - - - - - - - - - 175.4 - 36.2 - 9 LEU 9 B 66.6 - - 175.9 - - - - - - 179.6 - 31.9 - 10 GLU 10 B - 192.6 - - - - - - - - 183.6 - 35.3 - 11 MET 11 S B 64.2 - - - - - - - - - 176.5 - 35.1 - 12 ALA 12 b - - - - - - - - - - 181.2 - 33.4 - 13 SER 13 B 51.6 - - - - - - - - - 178.8 -1.7 35.7 - 14 GLU 14 S b - - -74.6 - - - - - - - 177.0 - 32.5 - 15 GLU 15 S b - - -60.1 176.1 - - - - - - 183.2 -1.9 35.6 - 16 GLY 16 S - - - - - - - - - - - 179.8 -1.8 - - 17 GLN 17 B 56.3 - - 186.0 - - - - - - 184.0 - 31.9 - 18 VAL 18 B 64.8 - - - - - - - - - 180.3 - 35.2 - 19 ILE 19 E B - - -56.8 177.2 - - - - - - 179.2 -2.8 35.2 - * * 20 ALA 20 E B - - - - - - - - - - 182.0 -.8 33.8 - +* +* 21 CYS 21 E B - - -51.7 - - - - - - - 175.0 -2.3 36.0 - * * 22 HIS 22 A - - -65.4 - - - - - - - 184.0 - 33.9 - 23 THR 23 h B 57.0 - - - - - - - - - 176.7 - 35.5 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 24 VAL 24 H A 64.1 - - - - -72.4 -22.6 - - - 179.0 - 32.8 - * * 25 GLU 25 H A - 187.8 - - - -62.4 -51.3 - - - 179.0 - 35.0 - * * 26 THR 26 H A - - -54.0 - - -63.9 -43.0 - - - 178.2 - 34.4 - 27 TRP 27 H A - 174.4 - - - -55.3 -54.5 - - - 180.0 -1.8 34.4 - * * 28 ASN 28 H A - 181.4 - - - -59.3 -43.2 - - - 180.6 -3.3 35.3 - +* +* 29 GLU 29 H A - 181.5 - - - -61.3 -45.7 - - - 182.1 -2.5 35.1 - 30 GLN 30 H A - - -65.3 - - -70.1 -35.9 - - - 174.1 -2.7 32.4 - * * 31 LEU 31 H A - - -66.8 180.5 - -63.3 -42.2 - - - 174.4 -2.2 35.1 - 32 GLN 32 H A - 170.5 - 175.7 - -58.3 -44.4 - - - 176.8 -2.3 33.0 - 33 LYS 33 H A - - -70.7 - - -67.4 -35.9 - - - 176.9 -2.4 30.4 - * * 34 ALA 34 H A - - - - - -67.6 -37.7 - - - 180.8 -2.6 33.9 - 35 ASN 35 H A - 188.4 - - - -71.2 -54.5 - - - 181.8 -2.7 37.3 - * * 36 GLU 36 H A - 177.7 - 182.8 - -59.5 -43.8 - - - 186.2 -3.6 35.7 - * ** ** 37 SER 37 H A - - -54.2 - - -94.0 -7.1 - - - 182.4 -2.3 34.9 - ** +** +** 38 LYS 38 h l - - -79.4 174.3 - - - - - - 176.7 -.8 31.1 - +* +* 39 THR 39 B - - -48.4 - - - - - - - 181.7 -.5 35.5 - * ** ** 40 LEU 40 E B - 182.4 - 168.6 - - - - - - 185.2 -.9 34.0 - * * 41 VAL 41 E B 59.8 - - - - - - - - - 176.9 -.9 33.1 - +* +* 42 VAL 42 E B - 181.1 - - - - - - - - 183.4 -3.2 34.4 - +* +* 43 VAL 43 E B - 184.8 - - - - - - - - 175.5 -3.2 34.1 - +* +* 44 ASP 44 E B - 163.1 - - - - - - - - 174.6 -3.4 35.5 - * +* +* 45 PHE 45 E B - - -63.7 - - - - - - - 179.0 -3.1 36.5 - * * 46 THR 46 E B - 187.9 - - - - - - - - 178.4 -2.4 33.0 - 47 ALA 47 t B - - - - - - - - - - 178.4 - 34.6 - 48 SER 48 T A - - -56.4 - - - - - - - 183.1 - 34.7 - 49 TRP 49 T A 55.0 - - - - - - - - - 179.6 - 31.4 - 50 CYS 50 h B 47.0 - - - - - - - -120.6 2.8 186.1 -.8 30.0 - * *** *7.8* * +* * *7.8* 51 GLY 51 H - - - - - - -58.4 -67.3 - - - 182.1 -.5 - - ** ** ** 52 PRO 52 H - - - - - -57.0 -57.0 -30.2 - - - 180.0 - 38.2 - * * 53 CYS 53 H A - - -48.4 156.6 - -65.7 -37.3 - -120.6 2.8 178.3 - 36.5 - * * *** *7.8* *7.8* 54 ARG 54 H A - 179.7 - 181.5 - -68.7 -29.3 - - - 180.3 -1.2 34.3 - * * 55 PHE 55 H A - 180.3 - - - -73.8 -29.3 - - - 182.2 -1.1 34.5 - * * 56 ILE 56 H A - 191.1 - - - -87.7 -18.4 - - - 180.5 -1.3 33.2 - +* +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 H A - - - - - -52.5 -49.4 - - - 179.3 -1.1 32.3 - * * * 58 PRO 58 H - - - - - -60.6 -60.6 -27.8 - - - 179.7 - 38.5 - * * * 59 PHE 59 H A - 181.1 - - - -73.2 -36.8 - - - 178.1 -.7 32.5 - +* +* 60 PHE 60 H A - 187.5 - - - -66.9 -33.7 - - - 176.2 -1.5 33.9 - 61 ALA 61 H A - - - - - -70.4 -29.2 - - - 178.1 -1.8 33.9 - 62 ASP 62 H A - 184.6 - - - -73.4 -39.2 - - - 173.9 -1.2 35.3 - * * * 63 LEU 63 H A - - -69.2 179.9 - -58.1 -40.5 - - - 176.9 -2.3 35.0 - 64 ALA 64 H A - - - - - -61.9 -32.2 - - - 178.6 -1.7 33.5 - 65 LYS 65 H A - 185.5 - 188.0 - -72.8 -32.3 - - - 185.6 -.9 36.3 - +* +* 66 LYS 66 H A - 179.9 - 174.6 - -82.0 -40.3 - - - 182.2 -1.4 33.0 - * * 67 LEU 67 h B - - -63.3 176.5 - - - - - - 183.2 -2.6 31.5 - 68 PRO 68 T - - - - - -71.2 - - - - - 187.6 - 38.7 - * * * 69 ASN 69 e a - 196.2 - - - - - - - - 176.9 - 35.2 - 70 VAL 70 E B - 175.9 - - - - - - - - 178.1 -.7 33.6 - +* +* 71 LEU 71 E B - - -65.2 177.9 - - - - - - 178.1 -3.0 35.3 - * * 72 PHE 72 E B - - -61.4 - - - - - - - 179.6 -.5 34.5 - ** ** 73 LEU 73 E B - - -73.0 - - - - - - - 180.5 -2.2 32.6 - 74 LYS 74 E B - 192.6 - - - - - - - - 180.6 -3.2 36.0 - +* +* 75 VAL 75 E B - 180.4 - - - - - - - - 179.7 -3.6 34.5 - ** ** 76 ASP 76 E B - 184.7 - - - - - - - - 184.3 -.7 33.9 - +* +* 77 THR 77 e A 52.1 - - - - - - - - - 176.4 -2.1 32.0 - 78 ASP 78 T A - 184.6 - - - - - - - - 175.4 - 34.8 - 79 GLU 79 T A - - -63.5 - - - - - - - 181.9 - 35.9 - 80 LEU 80 h b - - -70.3 - - - - - - - 180.3 -3.0 33.5 - * * 81 LYS 81 H A - - -61.1 177.3 - -68.5 -38.6 - - - 180.2 -1.4 33.7 - 82 SER 82 H A - - -56.1 - - -62.5 -38.1 - - - 179.8 - 34.5 - 83 VAL 83 H A - 178.2 - - - -69.3 -39.8 - - - 177.4 - 33.5 - 84 ALA 84 H A - - - - - -62.2 -40.5 - - - 178.6 -1.7 33.8 - 85 SER 85 H A - - -55.2 - - -66.9 -34.2 - - - 183.8 -2.3 35.6 - 86 ASP 86 H A - 183.0 - - - -73.5 -36.8 - - - 180.1 -1.8 33.7 - 87 TRP 87 h A - - -59.4 - - - - - - - 178.7 -2.2 32.9 - 88 ALA 88 T L - - - - - - - - - - 181.8 - 33.0 - 89 ILE 89 t B - - -55.4 176.7 - - - - - - 178.0 -3.3 34.5 - +* +* 90 GLN 90 A - 180.2 - 177.2 - - - - - - 180.6 -.9 34.5 - * * 91 ALA 91 S B - - - - - - - - - - 176.6 - 33.7 - 92 MET 92 S B - - -73.3 - - - - - - - .7 -.6 34.0 - +* +* 93 PRO 93 e cis - - - - - -92.3 - - - - - 174.4 - 39.8 - ** +* ** 94 THR 94 E B - - -58.0 - - - - - - - 177.7 -3.5 35.1 - +* +* Residue-by-residue listing for refined_1 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 PHE 95 E B - - -61.6 - - - - - - - 183.0 -3.4 35.8 - +* +* 96 MET 96 E B - 179.3 - 177.8 - - - - - - 184.1 -3.0 33.8 - * * 97 PHE 97 E B - - -63.3 - - - - - - - 178.9 -3.2 37.0 - +* +* 98 LEU 98 E B - - -53.6 - - - - - - - 173.6 -3.1 35.3 - * * * 99 LYS 99 E B - 170.3 - 180.1 - - - - - - 179.8 -3.2 33.3 - +* +* 100 GLU 100 T l - - -60.9 165.9 - - - - - - 183.2 - 34.2 - 101 GLY 101 T - - - - - - - - - - - 179.4 - - - 102 LYS 102 E B - - -57.9 179.9 - - - - - - 184.5 -2.0 34.4 - 103 ILE 103 E B - - -59.4 169.7 - - - - - - 175.4 - 35.5 - 104 LEU 104 E a - - -66.8 183.0 - - - - - - 183.4 -2.0 33.3 - 105 ASP 105 E B 58.4 - - - - - - - - - 180.2 -1.8 32.0 - 106 LYS 106 E B 55.3 - - - - - - - - - 179.8 - 31.4 - 107 VAL 107 E B - 180.2 - - - - - - - - 179.7 -3.0 34.9 - * * 108 VAL 108 E B 64.1 - - - - - - - - - 179.5 - 33.2 - 109 GLY 109 e - - - - - - - - - - - 179.8 -3.3 - - +* +* 110 ALA 110 B - - - - - - - - - - 179.6 - 34.0 - 111 LYS 111 h B - - -62.3 183.0 - - - - - - 181.7 -.9 35.4 - * * 112 LYS 112 H A - 186.6 - - - -69.5 -51.5 - - - 184.3 - 34.2 - * * 113 ASP 113 H A - - -61.4 - - -73.4 -49.8 - - - 186.9 - 34.2 - * * 114 GLU 114 H A - 185.7 - 173.2 - -67.8 -34.7 - - - 178.5 - 31.4 - 115 LEU 115 H A - 184.3 - - - -63.5 -51.5 - - - 179.1 -1.1 34.9 - * * * 116 GLN 116 H A - - -64.1 176.8 - -61.4 -33.0 - - - 175.9 -1.3 32.4 - 117 SER 117 H A - - -59.6 - - -67.3 -37.7 - - - 179.0 -2.2 34.1 - 118 THR 118 H A - - -52.1 - - -71.2 -29.8 - - - 174.6 -2.2 33.7 - 119 ILE 119 H A - - -58.3 - - -64.7 -50.9 - - - 178.5 -1.8 33.9 - * * 120 ALA 120 H A - - - - - -62.5 -31.3 - - - 177.1 -2.4 34.0 - 121 LYS 121 H A - 184.1 - 171.9 - -59.1 -40.8 - - - 176.8 -1.9 36.1 - 122 HIS 122 H A - - -75.3 - - -82.0 -32.5 - - - 179.6 -1.4 33.2 - * * 123 LEU 123 h b - - -83.6 - - - - - - - 178.8 -2.2 33.0 - * * 124 ALA 124 - - - - - - - - - - - - -1.4 34.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * * ** ** +** *** *7.8* * ** +* *7.8* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.1 182.3 -62.5 176.7 -70.3 -67.1 -38.4 - -120.6 2.8 179.7 -2.0 34.2 *** *7.8* *7.8* Standard deviations: 6.2 6.4 7.8 6.2 15.9 8.2 10.3 - .0 .0 3.1 .9 1.6 Numbers of values: 16 40 46 29 4 47 47 0 2 2 122 81 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_1 Page 5 ---------------------------------------- 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_1 Page 6 ---------------------------------------- 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 1.505 1.538 1.462 - 115.63 120.96 110.20 111.03 110.63 123.39 2 GLY 2 1.302 1.248 1.495 - 1.422 121.41 116.50 120.48 - 109.92 - 123.01 +* * +* +* 3 HIS 3 1.305 1.229 1.530 1.546 1.441 121.73 115.00 121.68 111.97 110.03 111.01 123.11 +* +* 4 HIS 4 1.317 1.232 1.516 1.544 1.460 123.08 115.79 120.93 110.41 110.74 111.57 123.27 5 HIS 5 1.317 1.232 1.512 1.549 1.466 123.17 117.47 119.74 108.27 107.72 111.74 122.79 * * 6 HIS 6 1.324 1.245 1.526 1.560 1.460 120.79 117.01 119.57 111.30 109.09 112.65 123.43 * * * 7 HIS 7 1.320 1.222 1.530 1.537 1.468 122.57 115.64 121.29 111.26 110.45 110.18 123.06 8 HIS 8 1.304 1.237 1.516 1.555 1.446 122.63 116.75 119.99 108.90 108.85 109.75 123.22 +* * +* 9 LEU 9 1.307 1.233 1.518 1.564 1.442 121.19 116.28 120.45 111.35 109.19 113.61 123.22 +* +* +* +* 10 GLU 10 1.306 1.235 1.515 1.554 1.449 122.37 116.30 120.28 111.25 105.90 109.58 123.40 +* * +* +* 11 MET 11 1.297 1.240 1.503 1.557 1.434 122.76 116.87 119.86 109.75 108.32 110.94 123.27 ** * * * * ** 12 ALA 12 1.319 1.230 1.514 1.522 1.444 121.30 115.06 121.16 110.96 109.12 111.40 123.61 13 SER 13 1.298 1.240 1.515 1.526 1.426 123.47 116.63 120.32 110.86 110.50 107.99 123.05 ** +* * ** Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 14 GLU 14 1.316 1.237 1.512 1.527 1.428 122.17 114.57 121.49 111.42 111.60 111.51 123.74 +* +* 15 GLU 15 1.307 1.231 1.510 1.533 1.437 123.88 117.09 120.14 108.89 107.26 110.83 122.69 +* * * * +* 16 GLY 16 1.308 1.232 1.519 - 1.448 120.12 116.60 120.60 - 112.34 - 122.79 +* +* 17 GLN 17 1.322 1.233 1.496 1.527 1.446 121.50 114.37 121.37 111.33 111.50 112.48 124.26 * * * 18 VAL 18 1.287 1.233 1.544 1.548 1.437 123.84 117.80 120.27 110.81 110.62 108.65 121.90 +** * * +* +** 19 ILE 19 1.327 1.232 1.525 1.546 1.452 120.38 116.75 120.56 108.76 109.84 110.95 122.68 20 ALA 20 1.310 1.230 1.515 1.526 1.450 121.42 116.60 120.89 110.89 109.61 110.81 122.49 * * 21 CYS 21 1.299 1.231 1.513 1.507 1.418 121.17 116.34 120.65 109.01 110.00 109.36 122.99 ** * ** ** 22 HIS 22 1.308 1.226 1.502 1.539 1.456 121.41 115.89 121.11 109.48 109.18 112.30 122.98 +* * * +* 23 THR 23 1.319 1.249 1.510 1.552 1.440 121.48 116.29 120.39 108.31 109.78 111.13 123.32 24 VAL 24 1.319 1.224 1.538 1.571 1.441 121.51 116.18 120.87 111.30 109.34 112.28 122.93 * * 25 GLU 25 1.340 1.240 1.527 1.530 1.455 122.25 115.95 120.63 109.22 109.87 110.53 123.42 26 THR 26 1.337 1.227 1.533 1.550 1.452 121.73 115.73 120.69 109.90 109.67 111.00 123.55 27 TRP 27 1.330 1.232 1.538 1.545 1.462 123.10 115.77 120.86 111.46 111.00 108.95 123.35 28 ASN 28 1.321 1.238 1.530 1.532 1.466 123.44 115.52 120.93 109.82 111.01 109.06 123.53 29 GLU 29 1.327 1.228 1.528 1.537 1.466 123.17 116.40 120.97 109.71 110.82 109.68 122.62 30 GLN 30 1.317 1.225 1.507 1.476 1.411 121.78 117.01 120.29 112.21 113.26 109.78 122.69 +** ** * +** 31 LEU 31 1.317 1.227 1.511 1.489 1.417 121.83 115.30 121.02 110.10 109.74 109.32 123.67 ** ** ** 32 GLN 32 1.313 1.209 1.514 1.530 1.438 123.08 117.32 119.92 112.45 110.51 110.15 122.73 * * * * * 33 LYS 33 1.312 1.231 1.521 1.530 1.452 120.97 117.57 119.85 112.59 112.85 112.46 122.56 * * * * 34 ALA 34 1.325 1.231 1.523 1.519 1.451 120.55 115.22 121.17 110.61 109.69 110.65 123.58 35 ASN 35 1.318 1.230 1.511 1.526 1.455 123.27 114.65 121.32 107.99 109.95 108.41 124.02 * * * 36 GLU 36 1.311 1.237 1.533 1.538 1.477 123.98 116.65 120.90 108.83 112.90 108.96 122.44 * * * * 37 SER 37 1.303 1.231 1.523 1.507 1.427 120.73 117.01 119.82 110.39 112.93 108.54 123.16 +* * +* * +* 38 LYS 38 1.343 1.237 1.501 1.512 1.474 122.22 115.19 121.47 112.01 112.60 112.09 123.25 * * * 39 THR 39 1.300 1.242 1.515 1.527 1.401 121.33 116.04 121.14 109.60 106.57 110.71 122.80 ** +** +* +** 40 LEU 40 1.265 1.233 1.543 1.567 1.428 121.25 117.62 120.00 113.90 106.81 108.82 122.36 *4.6* +* +* ** +* *4.6* 41 VAL 41 1.310 1.232 1.536 1.565 1.444 120.88 115.86 121.06 111.36 112.17 110.71 123.06 * * * 42 VAL 42 1.312 1.240 1.519 1.541 1.441 123.03 116.84 120.65 109.24 108.10 112.10 122.50 * * * 43 VAL 43 1.302 1.238 1.525 1.551 1.439 120.95 114.93 121.08 109.22 111.49 111.70 123.98 +* * +* 44 ASP 44 1.305 1.237 1.512 1.539 1.449 124.57 116.91 120.53 109.55 110.22 109.59 122.48 +* +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 45 PHE 45 1.308 1.230 1.505 1.519 1.415 121.23 117.07 120.43 107.70 108.07 110.57 122.50 +* ** * * ** 46 THR 46 1.283 1.229 1.510 1.562 1.420 120.34 116.40 120.38 111.53 109.44 111.96 123.21 *** ** * *** 47 ALA 47 1.290 1.233 1.512 1.510 1.416 122.02 116.27 120.68 110.77 108.90 109.94 123.03 +** ** +** 48 SER 48 1.291 1.226 1.544 1.537 1.440 122.68 116.45 120.85 110.69 110.68 109.44 122.67 +** +** 49 TRP 49 1.332 1.229 1.537 1.548 1.460 121.95 118.12 120.00 111.42 114.52 111.64 121.88 * * 50 CYS 50 1.313 1.244 1.544 1.540 1.460 120.20 115.20 121.23 114.17 112.32 111.52 123.56 * ** ** 51 GLY 51 1.337 1.237 1.532 - 1.471 123.93 119.13 119.44 - 116.09 - 121.44 * +* * * +* 52 PRO 52 1.361 1.227 1.527 1.541 1.485 123.20 115.35 121.56 110.45 112.38 103.93 123.08 * * * * 53 CYS 53 1.306 1.217 1.533 1.500 1.449 123.06 115.85 121.58 109.21 109.90 107.99 122.55 +* +* * +* 54 ARG 54 1.309 1.227 1.538 1.530 1.450 122.14 115.82 121.16 111.27 109.91 109.49 123.00 * * 55 PHE 55 1.324 1.240 1.540 1.545 1.463 122.81 116.77 120.86 110.63 111.22 109.56 122.35 56 ILE 56 1.322 1.236 1.551 1.578 1.458 120.68 115.54 121.14 111.08 110.24 111.52 123.26 * * * 57 ALA 57 1.333 1.237 1.563 1.527 1.476 123.52 120.06 119.53 111.06 113.87 110.76 120.40 +* * +* +* +* 58 PRO 58 1.381 1.235 1.525 1.535 1.474 121.98 116.29 120.98 109.97 112.17 104.02 122.73 ** ** 59 PHE 59 1.318 1.221 1.522 1.538 1.446 121.10 116.40 120.74 111.30 110.31 112.01 122.83 60 PHE 60 1.319 1.231 1.532 1.536 1.458 121.61 115.65 121.43 111.71 109.02 109.99 122.89 61 ALA 61 1.321 1.232 1.539 1.518 1.455 121.88 115.78 121.46 111.01 110.07 110.09 122.74 62 ASP 62 1.325 1.236 1.504 1.507 1.469 122.59 114.39 121.54 109.19 109.28 109.96 124.07 * * 63 LEU 63 1.311 1.234 1.530 1.523 1.436 124.02 115.76 120.91 110.66 110.40 108.95 123.31 * * * * 64 ALA 64 1.327 1.225 1.530 1.525 1.458 122.87 115.96 121.17 110.76 110.93 110.71 122.87 65 LYS 65 1.318 1.229 1.530 1.537 1.458 122.58 115.44 121.44 108.43 109.74 109.51 123.12 66 LYS 66 1.311 1.221 1.519 1.532 1.439 121.87 117.71 119.86 111.50 112.86 110.25 122.43 * * 67 LEU 67 1.310 1.233 1.524 1.506 1.436 120.32 116.15 121.38 113.00 112.65 110.50 122.47 * * * +* +* 68 PRO 68 1.338 1.230 1.538 1.537 1.465 123.60 117.27 120.60 110.11 114.82 103.09 122.12 * * 69 ASN 69 1.312 1.239 1.533 1.539 1.457 121.16 115.41 122.08 111.40 109.33 108.25 122.52 * * * 70 VAL 70 1.307 1.232 1.521 1.566 1.447 122.52 116.51 120.52 110.34 109.20 112.19 122.92 +* +* 71 LEU 71 1.309 1.228 1.512 1.526 1.423 122.28 116.54 120.52 109.86 109.39 109.87 122.93 * +* +* 72 PHE 72 1.304 1.245 1.492 1.514 1.440 121.33 115.31 121.15 108.40 109.49 112.24 123.54 +* +* * +* 73 LEU 73 1.281 1.220 1.497 1.532 1.431 122.61 115.26 121.00 109.88 110.88 113.28 123.74 *** * * +* *** 74 LYS 74 1.292 1.233 1.518 1.566 1.426 123.43 115.98 120.87 113.38 105.70 106.65 123.10 +** +* +* +* +* ** +** Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 75 VAL 75 1.307 1.241 1.522 1.563 1.447 122.66 116.35 120.77 109.85 109.05 111.35 122.81 +* +* 76 ASP 76 1.307 1.236 1.518 1.520 1.448 121.56 116.57 120.30 111.20 108.84 110.48 123.10 +* +* 77 THR 77 1.311 1.240 1.540 1.543 1.453 122.42 117.02 120.41 111.47 113.98 111.15 122.56 * * * 78 ASP 78 1.323 1.232 1.506 1.516 1.461 121.03 114.39 121.89 110.09 107.98 110.41 123.72 * * 79 GLU 79 1.315 1.235 1.526 1.519 1.421 123.52 116.11 121.00 109.17 110.18 109.31 122.88 +* * +* 80 LEU 80 1.322 1.239 1.509 1.528 1.409 122.38 115.50 121.23 110.34 111.05 111.55 123.22 +** +** 81 LYS 81 1.304 1.232 1.515 1.521 1.446 122.07 115.88 120.61 110.88 110.70 110.49 123.48 +* +* 82 SER 82 1.324 1.237 1.527 1.513 1.450 122.59 115.87 120.94 110.54 111.20 109.34 123.15 83 VAL 83 1.324 1.231 1.528 1.559 1.451 122.01 115.90 121.11 111.39 109.53 111.07 122.92 * * 84 ALA 84 1.328 1.227 1.530 1.522 1.454 121.76 116.34 120.56 110.58 110.32 110.61 123.08 85 SER 85 1.323 1.236 1.539 1.529 1.453 122.34 116.06 121.18 109.45 110.85 109.12 122.74 86 ASP 86 1.326 1.235 1.516 1.529 1.457 121.73 116.56 120.62 110.48 111.85 110.51 122.79 87 TRP 87 1.315 1.239 1.524 1.521 1.441 121.18 116.30 120.24 110.62 112.03 111.35 123.46 88 ALA 88 1.345 1.251 1.535 1.531 1.477 123.52 115.22 121.60 111.47 111.20 110.50 123.18 * * * * 89 ILE 89 1.313 1.242 1.524 1.546 1.442 122.56 115.68 121.07 109.43 110.47 111.19 123.19 * * 90 GLN 90 1.306 1.243 1.530 1.539 1.444 122.36 115.90 121.41 110.95 109.70 109.76 122.69 +* +* 91 ALA 91 1.318 1.229 1.518 1.521 1.438 121.54 115.73 121.04 110.74 111.03 110.64 123.21 * * 92 MET 92 1.299 1.236 1.507 1.502 1.428 122.54 118.93 119.62 110.05 110.28 111.04 121.45 ** * +* * ** 93 PRO 93 1.335 1.228 1.532 1.528 1.455 123.99 116.23 121.15 110.07 112.37 102.02 122.58 94 THR 94 1.291 1.228 1.511 1.525 1.419 121.67 116.57 120.51 108.87 108.43 111.37 122.92 +** ** +** 95 PHE 95 1.294 1.228 1.494 1.517 1.403 121.84 116.40 120.52 110.22 107.40 109.46 123.07 ** * +** * +** 96 MET 96 1.285 1.229 1.507 1.521 1.432 121.32 114.87 121.36 112.47 109.93 109.18 123.77 *** * * *** 97 PHE 97 1.290 1.245 1.517 1.514 1.408 124.33 116.45 121.15 109.19 110.13 107.71 122.40 +** +** * +* +** 98 LEU 98 1.293 1.215 1.528 1.563 1.427 121.02 116.81 120.66 107.24 108.49 112.93 122.52 +** +* +* +* * +** 99 LYS 99 1.297 1.231 1.475 1.524 1.445 122.21 115.11 120.32 109.43 108.72 113.45 124.53 ** ** +* ** 100 GLU 100 1.322 1.234 1.539 1.532 1.457 124.02 115.93 121.22 109.48 110.14 111.32 122.86 * * 101 GLY 101 1.317 1.227 1.520 - 1.441 120.92 116.34 120.81 - 111.57 - 122.85 102 LYS 102 1.319 1.233 1.517 1.534 1.451 122.15 116.11 120.31 110.75 109.20 110.23 123.57 103 ILE 103 1.309 1.228 1.511 1.548 1.461 123.46 116.08 120.71 108.55 111.82 110.27 123.21 * * 104 LEU 104 1.310 1.228 1.508 1.525 1.421 121.19 116.37 120.65 110.63 110.17 111.75 122.93 * +* +* 105 ASP 105 1.314 1.216 1.498 1.535 1.448 121.53 115.90 121.08 110.67 112.37 112.63 122.98 * * * * Residue-by-residue listing for refined_1 Page 10 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 106 LYS 106 1.303 1.230 1.527 1.570 1.446 121.88 116.38 120.47 113.36 111.32 111.45 123.14 +* ** +* ** 107 VAL 107 1.314 1.231 1.520 1.565 1.460 123.13 116.81 120.23 108.99 109.10 111.55 122.95 * * 108 VAL 108 1.312 1.238 1.541 1.564 1.440 121.38 116.30 120.99 111.11 110.44 111.41 122.68 * * 109 GLY 109 1.308 1.241 1.506 - 1.439 121.25 117.11 120.46 - 111.14 - 122.44 +* +* 110 ALA 110 1.312 1.238 1.509 1.525 1.432 119.83 115.44 121.47 110.95 109.09 110.73 123.08 * * * * 111 LYS 111 1.295 1.232 1.495 1.513 1.419 122.79 116.94 120.01 109.69 108.56 110.08 123.04 ** * ** ** 112 LYS 112 1.301 1.235 1.530 1.538 1.416 121.23 116.09 120.54 113.00 110.21 108.10 123.25 +* ** +* * ** 113 ASP 113 1.316 1.237 1.513 1.540 1.463 121.83 116.25 120.83 108.54 112.58 111.59 122.89 114 GLU 114 1.319 1.237 1.527 1.532 1.456 121.54 117.58 120.10 112.36 113.05 111.33 122.29 * * 115 LEU 115 1.327 1.226 1.506 1.515 1.461 120.25 114.61 121.45 108.82 108.83 111.27 123.90 116 GLN 116 1.308 1.239 1.526 1.521 1.456 122.96 116.48 120.48 112.25 111.90 110.35 123.02 * * * 117 SER 117 1.326 1.226 1.534 1.532 1.452 121.60 116.28 120.81 110.20 110.03 110.78 122.90 118 THR 118 1.325 1.238 1.540 1.540 1.449 122.24 116.14 121.27 111.04 109.77 110.69 122.58 119 ILE 119 1.324 1.224 1.527 1.558 1.451 121.16 116.02 120.69 109.75 108.56 112.29 123.20 120 ALA 120 1.331 1.213 1.528 1.511 1.467 122.47 115.33 121.18 110.44 110.69 110.19 123.50 121 LYS 121 1.314 1.216 1.519 1.501 1.453 124.26 115.40 121.61 110.56 110.02 107.19 122.99 * * * +* +* 122 HIS 122 1.299 1.235 1.528 1.519 1.439 121.94 116.92 120.65 110.42 112.15 111.09 122.42 ** * ** 123 LEU 123 1.307 1.236 1.516 1.515 1.407 122.43 115.44 121.40 111.64 112.33 110.34 123.13 +* +** +** 124 ALA 124 1.300 - 1.514 1.525 1.426 122.29 - - 111.43 108.51 110.42 - ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * ** +** +** +* +* ** +* ** +* *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 11 ---------------------------------------- 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 .014 119 1.265 1.345 1.312 .013 *4.6* * * C-N (Pro) 1.341 .016 4 1.335 1.381 1.354 .019 ** C-O C-O 1.231 .020 123 1.209 1.251 1.232 .007 * * CA-C CH1E-C (except Gly) 1.525 .021 119 1.475 1.563 1.521 .014 ** +* CH2G*-C (Gly) 1.516 .018 5 1.495 1.532 1.515 .013 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.531 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.578 1.553 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.476 1.570 1.530 .017 +** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.401 1.477 1.444 .017 +** * NH1-CH2G* (Gly) 1.451 .016 5 1.422 1.471 1.444 .016 +* * N-CH1E (Pro) 1.466 .015 4 1.455 1.485 1.470 .011 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 12 ---------------------------------------- +-----------------+ | 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 2.0 114 114.37 120.06 116.17 .89 +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.34 119.13 117.13 1.03 * CH1E-C-N (Pro) 116.9 1.5 4 115.35 117.27 116.28 .68 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.40 124.53 122.99 .55 +* O-C-N (Pro) 122.0 1.4 4 122.12 123.08 122.63 .34 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.83 124.57 122.11 1.00 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.12 123.93 121.53 1.28 +* C-N-CH1E (Pro) 122.6 5.0 4 121.98 123.99 123.19 .75 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.53 122.08 120.80 .53 CH2G*-C-O (Gly) 120.8 2.1 5 119.44 120.81 120.36 .48 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.44 111.47 110.90 .29 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.31 111.53 110.09 1.06 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.24 114.17 110.53 1.41 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.70 114.52 110.21 1.63 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.92 116.09 112.21 2.09 * N-CH1E-C (Pro) 111.8 2.5 4 112.17 114.82 112.93 1.09 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.94 111.40 110.57 .36 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.65 112.29 111.24 .78 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.02 104.02 103.27 .80 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.65 113.61 110.37 1.46 ** +* ------------------------------------------------------------------------------------------------------------- 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_1 Page 13 ---------------------------------------- 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] 100 88.5% Residues in additional allowed regions [a,b,l,p] 13 11.5% 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 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 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 113 88.5 83.8 10.0 .5 Inside b. Omega angle st dev 122 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.6 3.1 1.6 -.9 Inside e. H-bond energy st dev 81 .9 .8 .2 .5 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 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 6.2 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 40 6.4 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 46 7.8 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 29 6.2 20.4 5.0 -2.8 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% 88.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 3 Residue-by-residue listing for refined_1 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.18 Chi1-chi2 distribution -.22 Chi1 only -.02 Chi3 & chi4 .45 Omega .10 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths .02 Main-chain bond angles .47 ------ .28 ===== OVERALL AVERAGE .09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.