Residue-by-residue listing for refined_8 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 - - - -63.9 181.4 - - - - - - 185.0 - 32.8 - 2 GLY 2 - - - - - - - - - - - 175.3 - - - 3 HIS 3 b - - -65.5 - - - - - - - 181.6 -.8 30.4 - +* * +* 4 HIS 4 a - 180.6 - - - - - - - - 181.8 - 34.6 - 5 HIS 5 B - - -61.7 - - - - - - - 181.0 - 33.4 - 6 HIS 6 B - - -61.2 - - - - - - - 181.6 -.7 33.5 - +* +* 7 HIS 7 B - - -63.8 - - - - - - - 176.3 - 33.7 - 8 HIS 8 b 59.1 - - - - - - - - - 180.3 -.5 30.8 - +* +* 9 LEU 9 b 64.8 - - 173.7 - - - - - - 178.5 - 33.4 - 10 GLU 10 B - 184.2 - - - - - - - - 181.4 - 34.0 - 11 MET 11 B - - -60.8 - - - - - - - 184.6 -1.2 33.1 - * * 12 ALA 12 S l - - - - - - - - - - 184.8 - 33.4 - 13 SER 13 B - - -58.5 - - - - - - - 179.2 - 35.6 - 14 GLU 14 S b - - -64.1 - - - - - - - 180.9 - 33.5 - 15 GLU 15 S b 52.7 - - 178.6 - - - - - - 188.6 -1.4 33.9 - * * 16 GLY 16 S - - - - - - - - - - - 174.5 -1.1 - - * * 17 GLN 17 B - - -55.4 - - - - - - - 180.0 - 33.1 - 18 VAL 18 B - 184.9 - - - - - - - - 182.5 - 35.1 - 19 ILE 19 E B - - -61.0 - - - - - - - 179.3 -3.2 33.0 - +* +* 20 ALA 20 E B - - - - - - - - - - 180.9 -.7 34.0 - +* +* Residue-by-residue listing for refined_8 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 CYS 21 E B - - -52.0 - - - - - - - 174.8 -2.7 35.2 - 22 HIS 22 S A - - -63.5 - - - - - - - 183.4 -.6 34.9 - +* +* 23 THR 23 h B 54.1 - - - - - - - - - 177.5 - 35.5 - 24 VAL 24 H A 61.6 - - - - -74.9 -22.2 - - - 176.7 - 31.8 - +* +* 25 GLU 25 H A - - -74.8 - - -61.3 -51.0 - - - 177.7 - 34.6 - * * 26 THR 26 H A - - -61.2 - - -60.9 -43.2 - - - 176.2 - 33.5 - 27 TRP 27 H A - 167.1 - - - -53.7 -55.0 - - - 181.0 -1.5 35.0 - * * 28 ASN 28 H A - 183.4 - - - -63.2 -43.9 - - - 181.9 -3.2 35.5 - * * 29 GLU 29 H A - 183.2 - - - -59.2 -48.0 - - - 182.0 -3.0 34.6 - * * 30 GLN 30 H A - - -69.9 - - -64.3 -39.6 - - - 180.2 -2.8 33.2 - * * 31 LEU 31 H A - - -65.8 180.7 - -70.8 -45.8 - - - 177.6 -1.8 34.2 - 32 GLN 32 H A - 179.4 - 177.6 - -61.2 -43.5 - - - 177.6 -2.8 33.5 - * * 33 LYS 33 H A - 179.6 - 179.9 - -60.7 -42.7 - - - 180.1 -3.0 34.8 - * * 34 ALA 34 H A - - - - - -70.6 -43.2 - - - 181.1 -2.3 33.5 - 35 ASN 35 H A - 185.9 - - - -62.9 -52.7 - - - 181.8 -3.3 36.2 - * +* +* 36 GLU 36 H A - 181.8 - 185.5 - -58.1 -43.1 - - - 182.0 -3.2 35.8 - +* +* 37 SER 37 H A - - -53.5 - - -87.1 -1.6 - - - 181.6 -1.9 34.8 - +* *** *** 38 LYS 38 h L - 191.4 - 186.1 - - - - - - 180.8 -1.1 32.6 - * * 39 THR 39 t B - - -48.1 - - - - - - - 178.9 -2.8 35.4 - * * * 40 LEU 40 e B - 168.5 - - - - - - - - 179.1 - 35.6 - 41 VAL 41 E B 63.2 - - - - - - - - - 178.4 -1.2 32.8 - * * 42 VAL 42 E B - 183.2 - - - - - - - - 184.6 -2.7 33.1 - 43 VAL 43 E B - 177.4 - - - - - - - - 174.0 -2.8 35.3 - * * * 44 ASP 44 E B - 164.7 - - - - - - - - 174.8 -2.5 34.6 - * * 45 PHE 45 E B - - -63.9 - - - - - - - 185.3 -2.8 35.6 - * * 46 THR 46 E B - - -73.0 - - - - - - - 174.4 -2.7 35.2 - 47 ALA 47 t B - - - - - - - - - - 183.6 - 34.4 - 48 SER 48 T A - 185.5 - - - - - - - - 181.9 - 33.2 - 49 TRP 49 T A 56.4 - - - - - - - - - 179.0 - 30.9 - 50 CYS 50 h B 46.9 - - - - - - - -119.7 2.8 186.3 -1.1 29.3 - * *** *7.8* * * * *7.8* 51 GLY 51 H - - - - - - -55.0 -66.1 - - - 181.7 -.6 - - ** +* ** 52 PRO 52 H - - - - - -56.0 -56.0 -30.5 - - - 181.7 - 39.0 - * * 53 CYS 53 H A - - -44.6 154.1 - -71.2 -41.0 - -119.7 2.8 178.1 - 36.2 - * * *** *7.8* *7.8* 54 ARG 54 H A - 183.0 - 186.4 - -70.5 -34.9 - - - 181.4 -2.0 35.1 - Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 55 PHE 55 H A - 180.1 - - - -72.6 -27.9 - - - 182.5 -2.4 33.9 - * * 56 ILE 56 H A - 192.0 - - - -86.9 -20.4 - - - 180.8 -1.6 33.8 - +* +* +* 57 ALA 57 H A - - - - - -54.7 -46.3 - - - 178.5 -1.1 31.8 - * * 58 PRO 58 H - - - - - -51.7 -51.7 -36.9 - - - 181.2 - 39.0 - * * * * 59 PHE 59 H A - 183.6 - - - -76.6 -30.2 - - - 178.3 -.8 32.8 - +* +* 60 PHE 60 H A - 186.5 - - - -71.1 -33.8 - - - 175.1 -1.3 34.2 - 61 ALA 61 H A - - - - - -71.8 -29.9 - - - 177.5 -2.3 34.1 - 62 ASP 62 H A - 188.1 - - - -68.9 -43.4 - - - 175.8 -1.3 35.6 - * * 63 LEU 63 H A - - -71.9 180.4 - -53.7 -41.4 - - - 178.6 -2.4 34.7 - 64 ALA 64 H A - - - - - -64.2 -32.3 - - - 179.2 -1.4 33.9 - 65 LYS 65 H A - 183.3 - 176.5 - -79.9 -30.6 - - - 179.2 -.9 33.8 - * * * 66 LYS 66 H A - - -65.2 - - -73.8 -40.2 - - - 176.9 -2.0 32.7 - 67 LEU 67 h b - - -66.6 - - - - - - - 183.9 -2.6 33.6 - 68 PRO 68 T - - - - - -72.7 - - - - - 179.8 - 38.5 - * * 69 ASN 69 T A - - -66.2 - - - - - - - 182.4 - 34.1 - 70 VAL 70 t B - 179.8 - - - - - - - - 179.7 -1.3 34.4 - * * 71 LEU 71 E B - - -68.7 - - - - - - - 177.8 -1.7 33.8 - 72 PHE 72 E B - - -61.9 - - - - - - - 182.7 -.6 34.5 - +* +* 73 LEU 73 E B - - -75.7 - - - - - - - 172.2 -2.6 34.1 - * * 74 LYS 74 E B - - -71.2 - - - - - - - 177.6 -2.5 36.5 - 75 VAL 75 E B - 179.1 - - - - - - - - 180.3 -3.4 35.1 - +* +* 76 ASP 76 E B - 190.1 - - - - - - - - 184.2 -1.1 33.5 - * * 77 THR 77 e A 45.1 - - - - - - - - - 177.6 -1.5 33.9 - * * 78 ASP 78 T A - 192.2 - - - - - - - - 173.6 - 33.3 - * * 79 GLU 79 T A - - -68.6 183.8 - - - - - - 183.1 - 35.3 - 80 LEU 80 h a - - -63.8 178.7 - - - - - - 181.7 -3.4 36.0 - +* +* 81 LYS 81 H A 50.1 - - - - -61.0 -30.0 - - - 179.0 -1.1 29.1 - * * * 82 SER 82 H A - - -57.5 - - -77.8 -26.9 - - - 176.5 - 32.9 - * * * 83 VAL 83 H A - 180.6 - - - -72.0 -39.2 - - - 177.2 -.6 34.6 - +* +* 84 ALA 84 H A - - - - - -59.5 -47.1 - - - 178.9 -2.2 34.2 - 85 SER 85 H A - - -56.5 - - -63.6 -37.0 - - - 180.6 -1.9 34.4 - 86 ASP 86 H A - 182.4 - - - -63.0 -37.6 - - - 180.1 -1.8 34.8 - 87 TRP 87 h A - - -69.6 - - - - - - - 176.4 -2.0 31.8 - 88 ALA 88 T l - - - - - - - - - - 179.0 -1.4 33.1 - 89 ILE 89 t B - - -57.7 - - - - - - - 182.9 -3.0 33.7 - * * 90 GLN 90 A - - -58.9 179.6 - - - - - - 180.3 -.9 35.0 - +* +* Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 91 ALA 91 S B - - - - - - - - - - 180.4 - 34.0 - 92 MET 92 S B - - -62.1 177.6 - - - - - - -1.2 - 35.6 - 93 PRO 93 e cis - - - - - -89.0 - - - - - 177.2 - 39.6 - ** +* ** 94 THR 94 E B - - -59.0 - - - - - - - 181.4 -1.8 34.1 - 95 PHE 95 E B - - -63.0 - - - - - - - 177.5 -2.5 35.9 - 96 MET 96 E B - 176.9 - 176.4 - - - - - - 179.4 -3.3 33.5 - +* +* 97 PHE 97 E B - - -67.3 - - - - - - - 177.1 -3.4 36.5 - +* +* 98 LEU 98 E B 58.6 - - 169.1 - - - - - - 187.6 -1.5 32.3 - * * 99 LYS 99 E B - 180.6 - 172.0 - - - - - - 173.2 -3.2 33.9 - * +* +* 100 GLU 100 T l - - -58.0 176.5 - - - - - - 180.5 -.5 33.5 - ** ** 101 GLY 101 T - - - - - - - - - - - 175.7 - - - 102 LYS 102 E B - 181.3 - - - - - - - - 179.4 -1.4 35.7 - 103 ILE 103 E B - - -62.2 177.3 - - - - - - 181.0 - 32.5 - 104 LEU 104 E a - - -60.2 182.2 - - - - - - 185.0 -1.9 34.0 - 105 ASP 105 E B 60.6 - - - - - - - - - 175.3 -2.2 33.3 - 106 LYS 106 E B - - -57.9 192.3 - - - - - - 174.6 - 34.7 - 107 VAL 107 E B 61.9 - - - - - - - - - 182.7 -2.5 33.1 - 108 VAL 108 E B 60.8 - - - - - - - - - 178.6 - 33.5 - 109 GLY 109 e - - - - - - - - - - - 179.7 -2.7 - - 110 ALA 110 B - - - - - - - - - - 174.2 - 34.2 - 111 LYS 111 h B - - -67.1 175.1 - - - - - - 182.6 -1.0 35.2 - * * 112 LYS 112 H A - 187.5 - 175.7 - -62.7 -39.8 - - - 179.0 - 34.3 - 113 ASP 113 H A - 176.5 - - - -72.5 -35.8 - - - 184.6 - 34.3 - 114 GLU 114 H A - 192.9 - - - -69.8 -36.9 - - - 178.6 - 34.8 - 115 LEU 115 H A - 187.4 - - - -63.7 -46.1 - - - 177.4 -2.1 34.7 - 116 GLN 116 H A - - -58.5 - - -59.7 -37.0 - - - 179.4 -1.4 34.0 - 117 SER 117 H A - - -56.7 - - -67.9 -34.9 - - - 178.8 -2.1 34.2 - 118 THR 118 H A - - -53.1 - - -71.7 -35.0 - - - 176.2 -2.1 33.7 - 119 ILE 119 H A - - -57.9 176.9 - -67.6 -39.1 - - - 177.4 -2.2 33.4 - 120 ALA 120 H A - - - - - -67.9 -31.8 - - - 175.2 -2.3 33.3 - 121 LYS 121 H A - 185.5 - 192.3 - -58.5 -44.2 - - - 180.3 -1.8 37.2 - 122 HIS 122 H A - - -75.4 - - -75.6 -24.0 - - - 181.1 -1.7 33.9 - * * 123 LEU 123 h b - 197.3 - 172.7 - - - - - - 178.7 -1.2 34.5 - * * 124 ALA 124 - - - - - - - - - - - - -1.2 34.3 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * * ** +* *** *** *7.8* * ** +* *7.8* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.9 182.8 -62.5 178.5 -67.4 -66.4 -38.0 - -119.7 2.8 179.6 -1.9 34.2 *** *7.8* *7.8* Standard deviations: 6.2 6.8 6.7 7.3 17.1 8.3 10.3 - .0 .0 3.1 .8 1.6 Numbers of values: 14 38 50 28 4 47 47 0 2 2 122 85 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_8 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_8 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 - 1.237 1.509 1.535 1.455 - 116.96 120.20 111.68 109.68 111.54 122.84 2 GLY 2 1.314 1.230 1.511 - 1.440 120.79 117.22 120.53 - 114.03 - 122.25 * * 3 HIS 3 1.308 1.235 1.513 1.545 1.445 120.49 114.90 121.73 112.24 110.73 113.98 123.25 * * ** ** 4 HIS 4 1.313 1.231 1.539 1.565 1.454 122.84 116.17 121.49 112.12 109.52 108.74 122.30 * +* * * +* 5 HIS 5 1.324 1.227 1.508 1.542 1.460 121.09 116.36 120.78 109.80 109.72 112.53 122.84 * * 6 HIS 6 1.302 1.235 1.503 1.532 1.443 121.18 116.10 120.77 110.55 110.12 111.46 123.12 +* * +* 7 HIS 7 1.305 1.238 1.500 1.537 1.444 121.40 115.66 120.94 110.02 110.72 111.65 123.38 +* * +* 8 HIS 8 1.302 1.238 1.520 1.559 1.441 122.09 114.72 121.85 112.86 109.95 113.18 123.27 +* * * +* +* 9 LEU 9 1.306 1.229 1.512 1.575 1.442 123.43 116.87 120.43 110.10 108.76 112.99 122.67 +* ** * ** 10 GLU 10 1.296 1.227 1.521 1.544 1.435 120.74 116.03 121.15 111.58 107.59 110.63 122.68 ** * * ** 11 MET 11 1.309 1.235 1.507 1.533 1.450 121.76 116.85 119.61 111.20 109.60 111.54 123.53 * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.341 1.239 1.522 1.536 1.477 123.17 114.01 122.22 111.52 108.31 111.06 123.71 * * * * 13 SER 13 1.312 1.243 1.502 1.513 1.420 123.94 115.26 121.14 110.05 111.36 108.68 123.59 * * +* * * +* 14 GLU 14 1.300 1.228 1.522 1.533 1.394 122.40 114.23 121.64 112.08 108.96 110.56 123.96 ** *** * *** 15 GLU 15 1.299 1.237 1.518 1.552 1.437 124.92 116.27 121.27 112.13 107.18 110.52 122.42 ** * * +* * * ** 16 GLY 16 1.297 1.234 1.518 - 1.437 119.92 116.26 120.95 - 110.74 - 122.78 ** ** 17 GLN 17 1.324 1.233 1.496 1.531 1.438 121.71 115.78 120.75 108.29 109.16 114.67 123.47 * * ** ** 18 VAL 18 1.291 1.232 1.526 1.553 1.433 122.59 118.06 119.70 110.47 107.35 110.33 122.20 +** * * +** 19 ILE 19 1.316 1.227 1.522 1.570 1.448 120.86 116.75 120.79 109.75 110.38 113.14 122.46 * * 20 ALA 20 1.308 1.232 1.499 1.511 1.443 121.13 116.46 120.76 110.31 109.52 111.09 122.78 +* * +* 21 CYS 21 1.296 1.233 1.513 1.502 1.405 120.99 115.73 120.95 109.87 109.76 109.69 123.27 ** * +** +** 22 HIS 22 1.302 1.232 1.499 1.531 1.449 121.91 114.98 121.55 108.72 108.04 111.88 123.47 +* * * +* 23 THR 23 1.316 1.247 1.501 1.559 1.429 122.62 116.58 120.18 108.60 108.44 111.40 123.24 * +* +* 24 VAL 24 1.309 1.224 1.543 1.570 1.438 120.91 115.83 121.29 112.59 109.38 112.45 122.85 * * * +* +* 25 GLU 25 1.337 1.230 1.521 1.516 1.425 123.48 116.82 119.99 110.12 111.14 109.88 123.19 +* +* 26 THR 26 1.337 1.230 1.533 1.554 1.459 121.61 115.37 120.92 110.93 110.09 111.17 123.69 27 TRP 27 1.322 1.239 1.542 1.540 1.458 123.31 115.62 121.03 111.32 111.48 107.99 123.32 * * 28 ASN 28 1.318 1.237 1.525 1.534 1.462 123.12 115.46 120.96 109.37 110.68 109.44 123.56 29 GLU 29 1.326 1.215 1.518 1.537 1.456 123.07 116.99 120.11 110.32 110.94 109.81 122.84 30 GLN 30 1.326 1.227 1.514 1.487 1.421 121.89 117.39 120.21 110.81 113.41 110.09 122.40 ** +* ** 31 LEU 31 1.316 1.227 1.498 1.481 1.412 121.15 116.20 120.20 110.47 111.36 109.82 123.61 * ** ** ** 32 GLN 32 1.312 1.217 1.510 1.527 1.443 122.03 115.87 120.48 111.56 110.01 110.44 123.62 * * 33 LYS 33 1.312 1.240 1.531 1.526 1.446 122.87 116.83 120.44 110.54 110.67 109.34 122.72 * * 34 ALA 34 1.337 1.214 1.521 1.521 1.446 120.93 116.24 120.69 110.79 110.75 110.81 123.05 35 ASN 35 1.316 1.230 1.494 1.512 1.466 122.76 114.50 121.22 107.81 110.41 109.98 124.28 * * * 36 GLU 36 1.306 1.234 1.537 1.528 1.467 123.34 116.63 120.66 109.21 111.27 108.87 122.68 +* +* 37 SER 37 1.309 1.240 1.545 1.513 1.442 121.41 116.04 120.50 110.99 111.60 108.35 123.46 * * * 38 LYS 38 1.345 1.220 1.554 1.517 1.439 125.04 115.59 122.33 112.42 110.45 110.45 121.99 * * * +* * +* 39 THR 39 1.295 1.236 1.533 1.525 1.432 122.37 115.05 121.17 108.90 109.75 110.40 123.76 ** * ** 40 LEU 40 1.288 1.245 1.552 1.552 1.456 124.18 117.19 120.31 110.45 110.08 108.48 122.48 +** * * * * +** Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 VAL 41 1.328 1.233 1.536 1.568 1.447 121.38 117.12 120.66 111.50 110.06 111.72 122.19 * * * 42 VAL 42 1.307 1.235 1.515 1.538 1.444 120.95 116.08 120.87 110.20 109.28 112.66 123.05 +* +* 43 VAL 43 1.304 1.224 1.524 1.549 1.443 121.89 115.90 120.60 108.67 112.10 110.32 123.50 +* +* 44 ASP 44 1.308 1.236 1.512 1.528 1.455 123.21 116.59 120.44 109.19 110.69 110.94 122.95 * * 45 PHE 45 1.310 1.241 1.524 1.528 1.423 121.67 116.03 120.35 109.86 108.18 109.69 123.57 * +* * +* 46 THR 46 1.317 1.229 1.528 1.563 1.447 122.94 115.57 121.23 109.92 111.35 109.53 123.20 * * 47 ALA 47 1.297 1.228 1.518 1.521 1.440 123.39 117.78 120.07 110.68 107.09 110.83 122.15 ** * ** 48 SER 48 1.301 1.234 1.542 1.543 1.446 120.83 116.78 120.75 111.50 111.26 110.56 122.43 +* +* 49 TRP 49 1.327 1.228 1.535 1.546 1.453 120.93 118.30 119.97 111.80 114.05 112.12 121.72 * * * 50 CYS 50 1.319 1.241 1.533 1.548 1.450 119.26 114.56 121.55 114.41 111.96 112.61 123.89 * ** * ** 51 GLY 51 1.332 1.227 1.526 - 1.464 124.00 119.07 119.47 - 115.84 - 121.46 ** * * ** 52 PRO 52 1.357 1.226 1.517 1.529 1.479 122.81 115.19 121.35 109.74 112.05 103.61 123.45 * * * 53 CYS 53 1.299 1.232 1.538 1.503 1.436 123.00 115.84 121.55 109.82 109.53 107.88 122.60 ** * * +* ** 54 ARG 54 1.324 1.235 1.533 1.539 1.454 121.99 115.46 121.23 109.42 109.51 110.38 123.30 55 PHE 55 1.322 1.237 1.540 1.543 1.459 123.14 117.24 120.63 110.95 112.33 109.67 122.11 56 ILE 56 1.319 1.238 1.548 1.577 1.460 120.50 115.27 121.43 110.71 109.76 111.15 123.22 * * * 57 ALA 57 1.334 1.227 1.559 1.526 1.464 123.34 120.36 118.82 111.22 114.39 111.11 120.82 +* ** * * * ** 58 PRO 58 1.383 1.230 1.531 1.524 1.479 122.49 116.83 120.61 109.75 113.24 103.18 122.55 +** +** 59 PHE 59 1.325 1.220 1.527 1.532 1.449 120.55 116.26 120.98 111.30 110.32 111.48 122.73 60 PHE 60 1.311 1.230 1.535 1.537 1.455 122.14 115.70 121.38 112.06 108.99 109.15 122.91 * * * 61 ALA 61 1.326 1.237 1.530 1.524 1.455 121.75 115.38 121.47 110.63 109.50 110.50 123.15 62 ASP 62 1.324 1.225 1.501 1.515 1.465 122.85 114.70 121.21 108.79 108.91 110.17 124.09 * * 63 LEU 63 1.318 1.233 1.529 1.530 1.436 124.15 116.01 120.56 110.93 111.37 108.94 123.40 * * * 64 ALA 64 1.324 1.231 1.524 1.520 1.460 122.75 115.92 121.27 110.47 111.30 110.35 122.78 65 LYS 65 1.315 1.236 1.538 1.536 1.446 121.78 115.93 121.29 111.92 110.31 109.50 122.77 * * 66 LYS 66 1.325 1.238 1.525 1.537 1.454 121.75 116.93 120.43 110.68 111.53 111.86 122.64 67 LEU 67 1.317 1.222 1.531 1.545 1.435 121.74 117.85 120.53 109.92 109.68 112.25 121.60 * * * 68 PRO 68 1.348 1.230 1.538 1.533 1.472 122.62 117.67 120.44 110.30 114.34 103.24 121.89 * * 69 ASN 69 1.319 1.235 1.514 1.519 1.442 120.99 116.25 120.72 109.98 111.43 110.68 123.02 70 VAL 70 1.305 1.226 1.514 1.552 1.439 121.88 116.36 120.71 110.09 109.74 111.04 122.91 +* +* 71 LEU 71 1.309 1.231 1.514 1.538 1.416 121.69 115.87 121.05 110.42 110.41 111.25 123.06 * ** ** Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 PHE 72 1.298 1.237 1.508 1.523 1.442 122.18 116.35 120.56 109.82 108.74 111.15 123.08 ** ** 73 LEU 73 1.298 1.225 1.509 1.541 1.452 122.48 115.09 121.12 107.75 113.12 112.50 123.79 ** * * ** 74 LYS 74 1.313 1.239 1.507 1.528 1.411 123.77 116.76 120.48 108.77 107.08 109.89 122.74 * ** * * ** 75 VAL 75 1.280 1.235 1.488 1.553 1.425 121.01 116.31 120.24 109.72 107.46 111.34 123.44 *** +* +* * *** 76 ASP 76 1.309 1.225 1.488 1.508 1.430 120.23 115.38 121.03 110.51 108.05 112.17 123.55 * +* * * * +* 77 THR 77 1.284 1.226 1.519 1.517 1.428 123.08 117.54 120.13 110.85 113.47 109.40 122.32 *** +* * *** 78 ASP 78 1.313 1.231 1.512 1.511 1.440 119.68 115.25 121.27 111.06 108.10 111.69 123.48 * * * * 79 GLU 79 1.329 1.238 1.525 1.527 1.429 122.84 115.52 121.30 109.25 110.22 110.10 123.13 +* +* 80 LEU 80 1.314 1.236 1.531 1.518 1.423 124.06 115.77 121.22 110.50 110.82 107.60 122.94 * +* * +* +* 81 LYS 81 1.318 1.228 1.542 1.563 1.459 122.48 117.53 120.36 114.07 114.11 112.18 122.05 +* ** * ** 82 SER 82 1.322 1.236 1.530 1.518 1.446 120.57 115.96 121.01 111.74 110.25 110.80 123.00 83 VAL 83 1.331 1.232 1.524 1.558 1.459 121.81 115.13 121.48 109.38 108.26 111.73 123.37 * * 84 ALA 84 1.328 1.229 1.520 1.521 1.450 122.43 116.03 120.78 110.45 109.95 110.48 123.18 85 SER 85 1.323 1.235 1.533 1.520 1.446 122.17 116.44 120.51 110.55 111.39 109.56 123.03 86 ASP 86 1.331 1.235 1.527 1.542 1.469 122.04 115.94 121.20 110.04 110.41 109.96 122.75 87 TRP 87 1.313 1.234 1.527 1.523 1.444 122.10 116.03 120.44 112.02 112.96 111.06 123.53 * * * 88 ALA 88 1.342 1.238 1.531 1.532 1.476 123.74 116.09 120.97 111.01 112.14 110.58 122.89 * * 89 ILE 89 1.316 1.240 1.522 1.557 1.444 122.03 115.20 121.42 110.29 108.79 112.04 123.32 90 GLN 90 1.301 1.229 1.522 1.518 1.427 122.67 116.35 120.77 110.61 110.76 108.91 122.88 +* +* +* 91 ALA 91 1.312 1.237 1.520 1.522 1.443 121.75 116.39 120.71 110.86 110.08 110.24 122.88 * * 92 MET 92 1.313 1.240 1.522 1.525 1.442 122.52 118.42 120.09 109.28 109.66 109.71 121.49 * * * 93 PRO 93 1.334 1.240 1.522 1.522 1.460 123.87 116.18 120.96 109.86 111.52 102.64 122.83 94 THR 94 1.288 1.230 1.513 1.530 1.419 121.20 116.70 120.41 110.72 108.99 110.94 122.89 +** ** +** 95 PHE 95 1.310 1.226 1.501 1.523 1.413 121.41 116.61 120.27 109.12 108.76 109.94 123.11 * * ** ** 96 MET 96 1.294 1.239 1.496 1.533 1.430 121.61 114.68 121.35 110.55 109.36 111.85 123.98 +** * * +** 97 PHE 97 1.280 1.245 1.504 1.519 1.389 123.65 116.21 121.09 109.49 109.06 108.67 122.70 +*** +*** * * +*** 98 LEU 98 1.285 1.216 1.496 1.562 1.412 121.12 117.80 119.60 112.03 106.87 113.43 122.59 *** * +* ** * +* +* *** 99 LYS 99 1.285 1.234 1.478 1.537 1.421 120.17 113.49 121.48 111.17 111.39 110.26 124.89 *** ** +* * * *** 100 GLU 100 1.320 1.243 1.542 1.517 1.440 124.71 115.42 121.36 111.71 111.52 109.57 123.11 +* +* 101 GLY 101 1.317 1.235 1.518 - 1.445 122.12 117.07 120.58 - 113.24 - 122.35 102 LYS 102 1.314 1.217 1.517 1.544 1.445 120.86 117.74 119.80 109.63 108.37 109.73 122.44 * * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 103 ILE 103 1.312 1.230 1.508 1.559 1.451 120.54 116.22 120.70 110.84 109.70 112.93 123.05 * * 104 LEU 104 1.310 1.232 1.504 1.521 1.417 121.06 117.06 120.42 110.21 110.60 111.04 122.49 * * ** ** 105 ASP 105 1.315 1.223 1.496 1.520 1.446 120.47 115.09 121.35 109.11 113.31 112.03 123.50 * * * 106 LYS 106 1.305 1.233 1.511 1.542 1.443 122.41 116.55 120.38 107.56 108.66 113.27 123.07 +* * +* +* 107 VAL 107 1.296 1.233 1.525 1.557 1.432 122.14 116.68 120.51 111.57 109.01 111.72 122.76 ** * * ** 108 VAL 108 1.310 1.246 1.537 1.564 1.445 121.60 115.98 120.80 111.07 111.24 110.72 123.19 * * 109 GLY 109 1.322 1.243 1.505 - 1.445 121.68 117.76 120.11 - 110.88 - 122.13 110 ALA 110 1.320 1.241 1.496 1.519 1.432 118.56 114.54 121.72 109.92 110.14 111.17 123.73 * * +* +* 111 LYS 111 1.287 1.240 1.496 1.496 1.411 124.18 117.50 119.35 109.89 107.61 110.25 123.14 *** * +* ** * * *** 112 LYS 112 1.300 1.232 1.540 1.526 1.439 121.63 115.46 121.39 112.38 109.90 108.31 123.04 ** * * * ** 113 ASP 113 1.318 1.232 1.530 1.531 1.459 122.55 116.75 120.81 109.67 112.10 110.37 122.42 114 GLU 114 1.323 1.232 1.512 1.514 1.467 121.57 116.22 120.86 108.97 109.95 110.83 122.92 115 LEU 115 1.321 1.226 1.504 1.508 1.443 120.95 115.02 121.23 109.49 108.83 111.00 123.73 * * 116 GLN 116 1.317 1.237 1.520 1.528 1.469 122.07 115.83 120.88 108.95 110.64 111.91 123.29 117 SER 117 1.321 1.223 1.529 1.528 1.446 121.89 116.03 121.02 110.70 109.88 110.24 122.92 118 THR 118 1.321 1.231 1.539 1.544 1.440 122.06 116.75 121.01 110.98 110.01 110.84 122.21 119 ILE 119 1.324 1.225 1.535 1.550 1.446 120.56 115.97 121.12 110.58 108.94 111.97 122.85 120 ALA 120 1.330 1.220 1.528 1.520 1.459 122.19 116.03 120.68 110.97 110.51 110.83 123.29 121 LYS 121 1.330 1.224 1.522 1.511 1.463 123.16 114.61 121.67 107.55 108.80 108.81 123.72 * * 122 HIS 122 1.318 1.225 1.517 1.527 1.446 123.40 116.98 119.92 109.82 112.89 110.67 123.08 123 LEU 123 1.326 1.241 1.533 1.533 1.435 122.41 115.42 120.87 111.77 110.00 108.90 123.67 * * 124 ALA 124 1.311 - 1.514 1.536 1.442 124.27 - - 110.50 107.89 111.06 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** ** ** +*** ** ** * ** +* ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 1.280 1.345 1.313 .013 +*** * * C-N (Pro) 1.341 .016 4 1.334 1.383 1.355 .018 +** C-O C-O 1.231 .020 123 1.214 1.247 1.232 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.478 1.559 1.521 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.505 1.526 1.515 .007 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.511 1.536 1.524 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.517 1.577 1.553 .015 * CH1E-CH2E (the rest) 1.530 .020 84 1.481 1.575 1.529 .016 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.389 1.477 1.442 .016 +*** * NH1-CH2G* (Gly) 1.451 .016 5 1.437 1.464 1.446 .009 N-CH1E (Pro) 1.466 .015 4 1.460 1.479 1.472 .008 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 2.0 114 113.49 120.36 116.13 1.00 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.26 119.07 117.47 .93 * CH1E-C-N (Pro) 116.9 1.5 4 115.19 117.67 116.47 .90 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.82 124.89 122.99 .61 * * O-C-N (Pro) 122.0 1.4 4 121.89 123.45 122.68 .56 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.56 125.04 122.08 1.19 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.92 124.00 121.70 1.38 ** C-N-CH1E (Pro) 122.6 5.0 4 122.49 123.87 122.95 .54 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.82 122.33 120.82 .57 * CH2G*-C-O (Gly) 120.8 2.1 5 119.47 120.95 120.33 .50 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.92 111.52 110.72 .40 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.60 112.59 110.38 .95 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 107.55 114.41 110.44 1.33 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 106.87 114.39 110.12 1.57 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.74 115.84 112.95 1.94 * N-CH1E-C (Pro) 111.8 2.5 4 111.52 114.34 112.78 1.09 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.24 111.17 110.78 .30 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.40 113.14 111.32 .98 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.64 103.61 103.17 .35 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.60 114.67 110.56 1.47 +* ** ------------------------------------------------------------------------------------------------------------- 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_8 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 85 .8 .8 .2 .1 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 14 6.2 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 38 6.8 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 50 6.7 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 7.7 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 28 7.3 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% 88.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .85 2 Residue-by-residue listing for refined_8 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.15 Chi1-chi2 distribution -.09 Chi1 only -.04 Chi3 & chi4 .31 Omega .06 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths .03 Main-chain bond angles .45 ------ .28 ===== OVERALL AVERAGE .09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.