Residue-by-residue listing for refined_3 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 - - - -63.4 - - - - - - - 182.6 - 34.5 - 2 GLY 2 - - - - - - - - - - - 174.1 - - - * * 3 HIS 3 B - - -56.8 - - - - - - - 178.6 - 35.5 - 4 HIS 4 S A 63.3 - - - - - - - - - 166.4 - 26.2 - ** ** ** 5 HIS 5 S B - - -74.0 - - - - - - - 184.2 - 34.1 - 6 HIS 6 B - 185.3 - - - - - - - - 181.1 -.9 35.3 - * * 7 HIS 7 B - - -69.5 - - - - - - - 181.0 - 32.0 - 8 HIS 8 B - - -62.2 - - - - - - - 176.7 - 33.3 - 9 LEU 9 B 47.9 - - - - - - - - - 178.9 - 32.6 - * * 10 GLU 10 B - - -61.8 184.9 - - - - - - 176.8 - 33.6 - 11 MET 11 B - - -63.9 183.3 - - - - - - 179.5 - 32.7 - 12 ALA 12 B - - - - - - - - - - 181.2 -1.0 34.1 - * * 13 SER 13 b - 181.9 - - - - - - - - 172.9 - 35.6 - * * 14 GLU 14 S b - 187.3 - 181.7 - - - - - - 190.7 - 33.7 - +* +* 15 GLU 15 B 52.0 - - 186.9 - - - - - - 182.4 -1.8 35.1 - 16 GLY 16 S - - - - - - - - - - - 186.8 -1.8 - - * * 17 GLN 17 e B 61.8 - - 177.8 - - - - - - 171.7 - 31.8 - * * 18 VAL 18 E B - 180.6 - - - - - - - - 182.0 - 35.1 - Residue-by-residue listing for refined_3 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 ILE 19 E B - - -64.0 182.3 - - - - - - 179.7 -2.8 31.5 - * * 20 ALA 20 E B - - - - - - - - - - 179.1 -.7 34.2 - +* +* 21 CYS 21 E B - - -52.2 - - - - - - - 179.7 -1.2 35.7 - * * 22 HIS 22 A - - -64.6 - - - - - - - 182.6 -.7 33.9 - +* +* 23 THR 23 h B 55.1 - - - - - - - - - 176.0 - 35.8 - 24 VAL 24 H A - 181.8 - - - -76.3 -23.5 - - - 179.7 - 34.3 - * * 25 GLU 25 H A - 189.9 - - - -61.8 -50.5 - - - 176.9 - 35.2 - 26 THR 26 H A - - -56.0 - - -65.3 -43.1 - - - 178.4 - 34.5 - 27 TRP 27 H A - 171.9 - - - -53.1 -50.3 - - - 180.0 -1.7 35.8 - * * 28 ASN 28 H A - 183.9 - - - -61.5 -43.7 - - - 182.2 -3.3 35.8 - +* +* 29 GLU 29 H A - 183.4 - 177.7 - -63.8 -47.3 - - - 180.7 -2.0 34.5 - 30 GLN 30 H A - - -66.7 - - -60.3 -40.5 - - - 180.0 -3.0 34.7 - * * 31 LEU 31 H A - - -66.8 180.4 - -72.0 -45.1 - - - 176.8 -2.0 33.7 - 32 GLN 32 H A - 181.3 - - - -59.4 -40.2 - - - 177.2 -2.7 33.7 - 33 LYS 33 H A - 180.0 - 180.9 - -58.4 -49.2 - - - 182.7 -3.0 35.3 - * * 34 ALA 34 H A - - - - - -76.3 -38.4 - - - 181.9 -2.2 33.5 - 35 ASN 35 H A - 191.7 - - - -60.7 -53.3 - - - 182.1 -3.5 36.5 - * ** ** 36 GLU 36 H A - 179.1 - 184.2 - -68.7 -44.8 - - - 186.4 -2.5 35.0 - * * 37 SER 37 H A - - -54.0 - - -83.0 -7.7 - - - 180.3 -1.9 34.3 - * +** +** 38 LYS 38 h l - - -77.3 173.0 - - - - - - 172.5 -1.2 30.3 - * * * * 39 THR 39 e B - - -48.7 - - - - - - - 181.1 -1.0 36.3 - * * * 40 LEU 40 E B - 182.9 - 167.3 - - - - - - 185.3 -1.2 33.7 - * * 41 VAL 41 E B 58.8 - - - - - - - - - 179.6 -1.1 33.3 - * * 42 VAL 42 E B 64.1 - - - - - - - - - 181.1 -3.1 33.8 - * * 43 VAL 43 E B - 183.2 - - - - - - - - 176.6 -2.9 33.9 - * * 44 ASP 44 E B - 175.8 - - - - - - - - 176.4 -2.3 36.3 - 45 PHE 45 E B - - -63.8 - - - - - - - 183.8 -3.0 35.4 - * * 46 THR 46 E B - - -69.2 - - - - - - - 175.7 -2.4 36.0 - 47 ALA 47 t B - - - - - - - - - - 182.7 - 34.2 - 48 SER 48 T A - 183.1 - - - - - - - - 181.9 - 33.6 - 49 TRP 49 T A 57.5 - - - - - - - - - 182.6 - 32.6 - 50 CYS 50 h B - 177.8 - 212.5 - - - 61.6 - 2.0 181.4 -2.5 34.1 - +* ** ** 51 GLY 51 H - - - - - - -71.7 -66.0 - - - 179.9 - - - ** ** 52 PRO 52 H - - - - - -53.7 -53.7 -35.4 - - - 179.7 - 38.9 - * * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 53 CYS 53 H A - - -51.2 - - -65.3 -39.8 61.6 - 2.0 180.2 - 36.0 - * ** ** 54 ARG 54 H A - 191.2 - - - -71.6 -31.9 - - - 177.9 -1.1 34.4 - * * 55 PHE 55 H A - 174.6 - - - -68.1 -36.6 - - - 185.1 -2.0 34.6 - 56 ILE 56 H A - 191.2 - - - -87.6 -21.8 - - - 182.1 -1.9 33.9 - +* +* +* 57 ALA 57 H A - - - - - -50.7 -49.2 - - - 180.4 -1.6 31.5 - * * 58 PRO 58 H - - - - - -57.9 -57.9 -29.0 - - - 180.9 - 38.8 - * * 59 PHE 59 H A - 183.8 - - - -79.8 -40.6 - - - 176.4 -1.0 32.6 - * * * 60 PHE 60 H A - 180.7 - - - -61.3 -33.7 - - - 177.0 -1.9 34.7 - 61 ALA 61 H A - - - - - -66.3 -28.1 - - - 178.6 -2.2 33.8 - 62 ASP 62 H A - 186.8 - - - -72.3 -44.2 - - - 174.3 -.8 35.1 - +* +* 63 LEU 63 H A - - -85.3 - - -54.5 -43.4 - - - 178.3 -1.8 34.2 - * * 64 ALA 64 H A - - - - - -60.6 -37.9 - - - 179.9 -2.0 33.9 - 65 LYS 65 H A - 177.8 - 184.5 - -71.6 -33.7 - - - 183.1 -1.3 35.4 - 66 LYS 66 H A - 177.9 - - - -76.3 -38.0 - - - 184.8 -2.0 34.5 - 67 LEU 67 h B - - -65.4 171.5 - - - - - - 175.7 -2.5 32.8 - 68 PRO 68 T - - - - - -79.8 - - - - - 182.5 - 39.8 - * +* +* 69 ASN 69 e A 59.8 - - - - - - - - - 178.9 - 35.0 - 70 VAL 70 E B - 177.2 - - - - - - - - 178.8 -.5 33.8 - +* +* 71 LEU 71 E B - 183.0 - - - - - - - - 182.0 -3.0 34.9 - * * 72 PHE 72 E B - - -61.2 - - - - - - - 180.5 -1.0 35.4 - * * 73 LEU 73 E B - - -75.0 - - - - - - - 176.6 -2.0 34.0 - 74 LYS 74 E B - 177.6 - - - - - - - - 178.9 -2.4 35.6 - 75 VAL 75 E B - 179.0 - - - - - - - - 180.2 -3.5 33.5 - +* +* 76 ASP 76 E B - 188.3 - - - - - - - - 183.8 -.6 33.3 - +* +* 77 THR 77 e A 45.3 - - - - - - - - - 178.8 -.8 33.2 - * +* +* 78 ASP 78 T A - 188.8 - - - - - - - - 173.9 - 33.9 - * * 79 GLU 79 T A - - -70.9 - - - - - - - 181.7 - 35.3 - 80 LEU 80 h b - - -70.0 - - - - - - - 181.2 -3.4 33.2 - +* +* 81 LYS 81 H A - - -53.2 182.9 - -67.9 -40.5 - - - 181.8 -2.0 35.3 - 82 SER 82 H A - - -54.2 - - -62.9 -38.2 - - - 179.3 - 33.9 - 83 VAL 83 H A - 179.9 - - - -67.8 -43.3 - - - 177.9 - 33.3 - 84 ALA 84 H A - - - - - -64.2 -40.8 - - - 179.1 -1.7 34.2 - 85 SER 85 H A - 181.1 - - - -63.3 -45.1 - - - 181.8 -2.9 34.2 - * * 86 ASP 86 H A - 181.4 - - - -64.2 -37.1 - - - 181.1 -2.7 34.5 - 87 TRP 87 h A - - -67.9 - - - - - - - 177.7 -2.0 32.6 - 88 ALA 88 T l - - - - - - - - - - 182.8 -1.1 33.4 - * * 89 ILE 89 t B - - -56.9 178.4 - - - - - - 177.9 -2.7 35.0 - Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 90 GLN 90 a - 182.2 - 180.1 - - - - - - 180.9 -.8 33.7 - +* +* 91 ALA 91 S B - - - - - - - - - - 179.8 - 33.5 - 92 MET 92 S B - - -57.0 177.9 - - - - - - -2.0 -.6 35.8 - +* +* 93 PRO 93 e cis - - - - - -90.2 - - - - - 175.0 - 39.6 - ** +* ** 94 THR 94 E B - - -60.6 - - - - - - - 177.3 -1.6 34.2 - 95 PHE 95 E B - - -61.7 - - - - - - - 179.4 -3.1 36.2 - * * 96 MET 96 E B - 179.8 - - - - - - - - 181.9 -3.2 34.3 - +* +* 97 PHE 97 E B - - -68.7 - - - - - - - 178.8 -2.8 36.1 - * * 98 LEU 98 E B 59.7 - - 169.1 - - - - - - 183.2 -2.0 31.5 - 99 LYS 99 E B - 170.8 - 180.6 - - - - - - 178.3 -3.4 34.1 - +* +* 100 GLU 100 e l - - -55.3 165.0 - - - - - - 182.9 -.7 35.6 - +* +* 101 GLY 101 T - - - - - - - - - - - 175.0 - - - 102 LYS 102 E B - - -72.4 - - - - - - - 183.5 -2.7 33.3 - 103 ILE 103 E B - - -59.1 177.8 - - - - - - 179.8 - 33.6 - 104 LEU 104 E a - - -61.5 180.5 - - - - - - 184.6 -2.0 35.3 - 105 ASP 105 E B 62.4 - - - - - - - - - 180.1 -2.0 33.4 - 106 LYS 106 E B 58.3 - - 177.7 - - - - - - 177.2 - 34.4 - 107 VAL 107 E B - 181.0 - - - - - - - - 177.2 -3.1 34.8 - * * 108 VAL 108 E B 59.9 - - - - - - - - - 181.5 - 32.8 - 109 GLY 109 e - - - - - - - - - - - 181.5 -2.7 - - 110 ALA 110 B - - - - - - - - - - 173.2 - 34.0 - * * 111 LYS 111 h B - - -62.8 183.7 - - - - - - 185.6 -1.0 34.2 - * * 112 LYS 112 H A - 186.8 - 176.0 - -66.5 -33.6 - - - 179.2 - 33.5 - 113 ASP 113 H A - 174.4 - - - -65.0 -48.2 - - - 178.3 - 33.6 - 114 GLU 114 H A - - -68.8 189.0 - -71.8 -29.4 - - - 178.1 - 31.2 - 115 LEU 115 H A - 186.1 - - - -60.8 -42.5 - - - 177.4 -2.2 35.3 - 116 GLN 116 H A - - -55.8 - - -54.0 -44.5 - - - 181.4 -1.9 35.0 - 117 SER 117 H A - - -55.2 - - -68.3 -32.6 - - - 178.1 -1.1 34.5 - * * 118 THR 118 H A - - -53.0 - - -70.0 -34.2 - - - 175.9 -1.9 34.4 - 119 ILE 119 H A - - -59.0 177.5 - -65.2 -45.0 - - - 179.4 -2.2 34.1 - 120 ALA 120 H A - - - - - -64.0 -31.4 - - - 178.4 -2.3 33.7 - 121 LYS 121 H A - 194.6 - 179.0 - -63.4 -35.4 - - - 178.4 -1.8 36.6 - 122 HIS 122 H A - - -74.4 - - -87.3 -30.8 - - - 181.3 -1.2 33.8 - +* * +* 123 LEU 123 h b - 190.6 - 166.4 - - - - - - 179.7 -2.3 34.9 - 124 ALA 124 - - - - - - - - - - - - - 34.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * +* ** +* +** ** ** ** ** +** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 Page 5 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.6 182.4 -63.0 179.7 -70.4 -66.3 -39.1 61.6 - 2.0 179.7 -2.0 34.3 ** ** Standard deviations: 5.7 5.4 7.9 8.5 17.5 8.3 9.4 .0 - .0 3.3 .8 1.7 Numbers of values: 14 44 44 31 4 47 47 2 0 2 122 82 119 0 Number of cis-peptides (labelled cis): 1 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_3 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 - 1.233 1.502 1.531 1.465 - 116.71 120.63 109.39 108.80 111.55 122.67 * * 2 GLY 2 1.297 1.233 1.492 - 1.415 119.98 115.91 120.67 - 112.27 - 123.39 ** * ** ** 3 HIS 3 1.302 1.235 1.517 1.547 1.445 121.77 119.26 118.82 109.19 105.57 111.25 121.92 +* +* * ** ** 4 HIS 4 1.331 1.219 1.526 1.560 1.466 117.94 115.71 121.18 114.60 111.74 116.31 123.11 * ** ** *** *** 5 HIS 5 1.325 1.232 1.513 1.539 1.456 121.92 116.75 120.45 108.98 106.95 113.05 122.75 +* +* +* 6 HIS 6 1.298 1.227 1.514 1.558 1.451 121.62 117.24 119.99 111.44 108.41 108.75 122.77 ** * * ** 7 HIS 7 1.320 1.223 1.508 1.540 1.463 120.63 116.84 120.28 110.91 110.82 112.96 122.88 * * 8 HIS 8 1.314 1.246 1.516 1.533 1.460 121.37 115.29 121.50 109.49 111.60 112.22 123.17 * * * 9 LEU 9 1.293 1.232 1.511 1.557 1.435 122.61 117.96 119.59 113.46 109.15 110.52 122.45 +** * * +* +** 10 GLU 10 1.301 1.242 1.500 1.522 1.440 119.81 116.43 120.59 109.54 109.92 112.30 122.96 +* * * * +* 11 MET 11 1.309 1.234 1.502 1.531 1.434 120.39 115.71 120.89 110.46 109.37 112.99 123.35 * * * * * Residue-by-residue listing for refined_3 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 1.302 1.232 1.502 1.520 1.427 121.71 116.14 120.71 110.95 109.00 110.64 123.15 +* * +* +* 13 SER 13 1.285 1.253 1.526 1.553 1.426 122.05 117.67 120.26 111.52 107.57 108.48 122.04 *** * * +* * * *** 14 GLU 14 1.299 1.223 1.526 1.526 1.428 120.22 114.80 121.79 112.17 105.26 111.01 123.23 ** +* * ** ** 15 GLU 15 1.298 1.246 1.512 1.526 1.442 122.89 115.76 120.57 111.56 112.26 107.48 123.67 ** +* ** 16 GLY 16 1.333 1.226 1.503 - 1.434 121.37 116.71 120.52 - 111.26 - 122.77 * * 17 GLN 17 1.327 1.238 1.475 1.507 1.435 119.99 112.54 122.39 109.15 114.56 113.41 125.04 ** * * +* * +* * ** 18 VAL 18 1.270 1.235 1.522 1.555 1.429 123.93 118.28 119.50 109.62 106.20 111.50 122.22 **** +* * * +* **** 19 ILE 19 1.309 1.236 1.512 1.556 1.449 119.86 115.32 121.43 111.62 111.67 112.73 123.24 * * * * 20 ALA 20 1.302 1.223 1.506 1.518 1.428 122.16 116.32 120.77 110.43 110.10 110.55 122.90 +* +* +* 21 CYS 21 1.306 1.229 1.507 1.507 1.420 121.40 116.48 120.62 109.67 108.62 109.43 122.87 +* * ** ** 22 HIS 22 1.295 1.234 1.510 1.539 1.450 121.40 115.58 121.18 110.24 109.87 111.33 123.24 ** ** 23 THR 23 1.316 1.245 1.514 1.549 1.438 122.43 116.30 120.47 108.09 109.71 110.91 123.23 * * 24 VAL 24 1.319 1.218 1.527 1.554 1.443 122.00 115.59 121.43 109.71 108.35 111.86 122.96 * * 25 GLU 25 1.326 1.241 1.539 1.533 1.455 122.51 116.27 120.71 110.03 109.21 109.65 123.01 26 THR 26 1.335 1.224 1.538 1.542 1.454 121.52 115.68 120.61 109.77 109.82 110.85 123.67 27 TRP 27 1.332 1.235 1.533 1.541 1.470 123.85 115.19 121.33 110.87 110.79 107.42 123.46 * +* +* 28 ASN 28 1.308 1.238 1.521 1.532 1.452 123.58 115.40 120.92 109.46 110.62 108.97 123.67 * * * 29 GLU 29 1.320 1.223 1.516 1.523 1.448 122.84 116.18 120.44 110.60 110.74 109.62 123.36 30 GLN 30 1.324 1.237 1.509 1.493 1.424 123.13 116.42 120.76 109.98 112.30 109.34 122.81 +* +* +* 31 LEU 31 1.311 1.209 1.499 1.484 1.396 121.38 116.83 119.99 111.65 111.51 109.45 123.17 * * * ** *** *** 32 GLN 32 1.314 1.240 1.524 1.535 1.452 121.75 115.26 120.76 111.10 109.85 110.64 123.97 * * 33 LYS 33 1.313 1.236 1.529 1.532 1.448 123.60 116.68 120.47 110.20 110.61 108.90 122.82 * * * 34 ALA 34 1.328 1.226 1.525 1.512 1.452 120.96 116.02 120.61 110.77 111.79 110.28 123.36 35 ASN 35 1.319 1.233 1.500 1.531 1.467 123.21 114.60 121.57 107.93 109.97 109.73 123.83 * * * 36 GLU 36 1.309 1.231 1.530 1.523 1.458 121.77 117.27 120.15 108.79 112.82 110.05 122.54 * * 37 SER 37 1.322 1.236 1.525 1.517 1.451 120.97 116.29 120.50 110.48 112.35 109.44 123.21 38 LYS 38 1.338 1.234 1.502 1.505 1.455 122.65 114.80 121.74 113.37 112.94 111.62 123.42 * * +* +* 39 THR 39 1.292 1.242 1.520 1.528 1.410 122.10 116.84 120.78 108.64 105.62 110.52 122.36 +** +** +* +** 40 LEU 40 1.266 1.234 1.534 1.567 1.431 120.35 117.21 120.32 113.62 106.43 109.62 122.45 **** +* * +* +* **** 41 VAL 41 1.300 1.232 1.529 1.566 1.439 121.12 116.15 120.92 111.95 111.10 110.30 122.90 ** * * ** Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.301 1.237 1.517 1.555 1.429 121.96 116.45 121.13 110.52 109.35 111.68 122.38 ** +* ** 43 VAL 43 1.288 1.235 1.511 1.538 1.425 120.32 115.24 120.84 109.36 110.65 112.12 123.91 +** +* +** 44 ASP 44 1.298 1.240 1.516 1.534 1.442 123.39 116.99 120.33 109.36 108.55 108.97 122.60 ** ** 45 PHE 45 1.305 1.237 1.518 1.523 1.419 121.08 116.04 120.41 109.81 108.89 109.81 123.50 +* ** ** 46 THR 46 1.307 1.207 1.513 1.552 1.443 122.90 116.12 120.78 109.08 110.22 109.58 123.10 +* * * +* 47 ALA 47 1.291 1.237 1.508 1.519 1.440 122.33 116.69 119.69 110.47 107.68 111.09 123.63 +** * +** 48 SER 48 1.315 1.233 1.553 1.543 1.471 123.24 117.41 120.33 110.87 113.29 109.71 122.24 * * 49 TRP 49 1.325 1.228 1.537 1.548 1.462 121.52 117.23 120.64 111.18 112.85 111.07 122.08 50 CYS 50 1.314 1.237 1.525 1.533 1.455 120.81 115.82 120.81 110.41 110.85 110.42 123.36 * * 51 GLY 51 1.324 1.233 1.525 - 1.458 121.93 118.56 119.69 - 113.54 - 121.75 * * 52 PRO 52 1.361 1.228 1.526 1.540 1.478 123.28 115.62 121.34 109.67 112.18 103.86 123.03 * * 53 CYS 53 1.310 1.222 1.536 1.513 1.448 122.63 116.01 121.43 109.14 110.01 108.92 122.54 * * 54 ARG 54 1.318 1.225 1.543 1.562 1.452 122.14 115.66 121.38 113.07 108.20 108.39 122.93 +* +* * * +* 55 PHE 55 1.322 1.240 1.543 1.553 1.468 123.36 116.79 120.65 110.26 111.85 109.54 122.55 * * 56 ILE 56 1.319 1.244 1.551 1.570 1.461 121.60 115.79 121.03 110.63 111.51 110.53 123.13 * * * 57 ALA 57 1.333 1.234 1.559 1.528 1.470 123.48 120.27 119.02 111.40 114.71 111.18 120.71 +* ** * * * ** 58 PRO 58 1.382 1.235 1.526 1.527 1.477 122.06 116.68 120.82 109.42 112.88 103.91 122.50 +** +** 59 PHE 59 1.315 1.217 1.525 1.532 1.438 120.73 116.48 120.60 112.11 110.00 111.22 122.89 * * * 60 PHE 60 1.324 1.234 1.538 1.545 1.476 122.64 115.57 121.49 111.34 109.30 109.00 122.92 61 ALA 61 1.323 1.235 1.540 1.521 1.454 122.31 116.65 120.72 110.53 111.08 110.46 122.63 62 ASP 62 1.331 1.235 1.499 1.519 1.475 121.91 114.41 121.50 108.84 108.46 111.03 124.09 * * 63 LEU 63 1.318 1.236 1.527 1.536 1.434 123.52 116.11 120.61 110.86 111.24 109.86 123.27 * * * 64 ALA 64 1.331 1.231 1.524 1.523 1.463 122.42 115.59 121.19 110.53 111.22 110.29 123.22 65 LYS 65 1.314 1.243 1.536 1.540 1.451 122.80 115.33 121.19 110.12 110.45 108.96 123.47 * * 66 LYS 66 1.315 1.232 1.526 1.546 1.449 122.87 117.03 120.48 110.11 112.05 109.96 122.49 67 LEU 67 1.311 1.230 1.523 1.507 1.429 121.02 116.53 121.23 111.75 113.96 109.57 122.23 * * +* +* 68 PRO 68 1.339 1.230 1.538 1.534 1.470 123.13 115.47 121.51 109.71 111.35 102.53 123.02 69 ASN 69 1.321 1.226 1.521 1.531 1.444 123.50 116.23 120.98 110.40 111.35 109.11 122.79 * * 70 VAL 70 1.311 1.230 1.511 1.563 1.440 121.74 116.28 120.58 110.19 109.12 112.09 123.11 * * 71 LEU 71 1.298 1.229 1.525 1.537 1.437 121.98 116.70 120.48 111.05 108.58 109.50 122.81 ** * ** Residue-by-residue listing for refined_3 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 1.311 1.240 1.518 1.536 1.453 121.77 116.07 120.92 108.61 109.34 110.89 123.01 * * 73 LEU 73 1.291 1.219 1.503 1.543 1.452 122.94 115.37 120.82 108.15 111.56 112.82 123.81 +** * * * +** 74 LYS 74 1.308 1.234 1.523 1.547 1.444 123.59 116.96 120.83 109.85 107.73 109.82 122.20 * * * * 75 VAL 75 1.286 1.234 1.500 1.555 1.435 121.02 116.05 120.56 110.37 109.01 112.38 123.37 *** * * *** 76 ASP 76 1.312 1.224 1.498 1.513 1.431 120.83 115.75 120.80 110.68 109.09 111.92 123.43 * * * * 77 THR 77 1.293 1.237 1.528 1.522 1.436 123.06 117.55 120.13 111.11 114.21 109.68 122.32 +** * * * +** 78 ASP 78 1.322 1.230 1.498 1.522 1.453 120.08 114.51 121.54 110.08 107.64 112.06 123.95 * * * 79 GLU 79 1.313 1.233 1.520 1.513 1.418 123.39 116.59 120.66 110.10 110.50 109.10 122.72 * ** ** 80 LEU 80 1.321 1.238 1.510 1.534 1.411 122.46 114.96 121.54 110.96 110.72 111.48 123.46 ** ** 81 LYS 81 1.310 1.223 1.507 1.525 1.449 122.30 115.08 121.37 109.24 109.62 110.21 123.52 * * 82 SER 82 1.309 1.228 1.535 1.508 1.433 122.73 116.90 120.40 111.73 112.05 108.72 122.65 * * * * * 83 VAL 83 1.329 1.229 1.530 1.558 1.459 121.12 116.02 121.02 110.50 109.60 112.04 122.91 84 ALA 84 1.328 1.218 1.526 1.523 1.454 121.83 116.13 120.61 110.60 109.96 110.20 123.25 85 SER 85 1.321 1.230 1.536 1.544 1.446 122.69 116.58 120.59 110.97 110.96 109.78 122.82 86 ASP 86 1.326 1.239 1.526 1.537 1.467 122.06 116.08 121.07 109.83 111.27 110.28 122.81 87 TRP 87 1.313 1.231 1.538 1.528 1.440 122.03 116.66 120.06 111.55 112.93 110.60 123.28 * * 88 ALA 88 1.350 1.237 1.539 1.533 1.492 123.83 115.75 121.18 110.73 112.16 110.31 122.97 +* +* * +* 89 ILE 89 1.312 1.236 1.522 1.551 1.451 122.78 116.42 120.76 109.05 110.71 110.81 122.80 * * 90 GLN 90 1.304 1.237 1.529 1.535 1.444 121.23 116.26 121.05 110.81 110.05 110.95 122.67 +* +* 91 ALA 91 1.312 1.234 1.520 1.521 1.442 121.52 115.59 121.32 110.86 110.71 110.84 123.08 * * 92 MET 92 1.304 1.230 1.523 1.535 1.447 122.26 119.02 119.66 109.30 108.57 109.75 121.31 +* * * +* 93 PRO 93 1.332 1.237 1.524 1.527 1.453 124.02 116.40 121.15 109.91 111.66 102.68 122.39 94 THR 94 1.286 1.225 1.512 1.531 1.419 120.58 116.60 120.53 109.98 108.99 111.57 122.86 *** ** *** 95 PHE 95 1.296 1.226 1.492 1.523 1.406 121.80 116.77 120.29 108.74 107.46 110.38 122.92 ** +* +** * +** 96 MET 96 1.282 1.235 1.496 1.524 1.428 120.54 115.33 120.90 110.28 108.86 111.10 123.76 *** * +* *** 97 PHE 97 1.286 1.241 1.500 1.516 1.399 123.38 116.20 121.41 109.14 109.42 109.55 122.39 *** * *** *** 98 LEU 98 1.276 1.216 1.515 1.567 1.409 120.23 116.97 120.63 112.69 109.70 112.79 122.39 +*** +* +** * * +*** 99 LYS 99 1.287 1.224 1.475 1.530 1.433 121.63 114.53 120.89 110.15 110.12 111.23 124.50 *** ** * *** 100 GLU 100 1.322 1.225 1.549 1.517 1.452 124.47 116.58 120.85 107.66 110.08 110.81 122.57 * +* * +* 101 GLY 101 1.317 1.236 1.542 - 1.450 121.04 117.69 119.96 - 113.71 - 122.35 * * Residue-by-residue listing for refined_3 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 ----------------------------------------------------------------------------------------------------------------------------------- 102 LYS 102 1.332 1.227 1.517 1.557 1.474 121.78 116.68 120.20 109.21 109.29 113.40 123.11 * +* +* 103 ILE 103 1.314 1.231 1.522 1.554 1.459 122.71 116.17 120.98 110.29 111.50 111.21 122.84 * * 104 LEU 104 1.311 1.244 1.508 1.518 1.428 121.42 115.40 121.13 108.88 110.38 110.47 123.47 * +* +* 105 ASP 105 1.314 1.219 1.494 1.523 1.433 122.65 115.62 121.25 109.50 110.92 112.44 123.09 * * * * * 106 LYS 106 1.284 1.231 1.519 1.535 1.442 121.62 116.57 120.66 110.18 109.87 110.59 122.76 *** *** 107 VAL 107 1.300 1.231 1.513 1.564 1.446 121.98 116.54 120.45 108.85 108.58 112.15 122.99 ** ** 108 VAL 108 1.302 1.242 1.532 1.568 1.437 121.31 116.40 120.74 111.84 109.08 111.93 122.78 +* * * * +* 109 GLY 109 1.310 1.239 1.506 - 1.441 120.92 117.95 120.17 - 110.01 - 121.88 * * 110 ALA 110 1.308 1.235 1.499 1.520 1.428 118.17 115.18 121.58 110.30 110.74 110.80 123.24 * * +* +* +* 111 LYS 111 1.296 1.232 1.485 1.512 1.403 122.83 116.53 120.17 111.38 107.37 110.64 123.29 ** +* +** * +** 112 LYS 112 1.303 1.227 1.526 1.522 1.429 121.87 115.92 120.65 112.48 110.77 109.25 123.34 +* +* * +* 113 ASP 113 1.322 1.237 1.527 1.525 1.464 122.35 116.90 120.69 110.48 111.76 110.55 122.40 114 GLU 114 1.324 1.237 1.510 1.523 1.458 120.51 116.25 120.68 110.77 111.74 113.58 123.07 +* +* 115 LEU 115 1.321 1.220 1.505 1.503 1.448 121.75 115.35 120.91 108.82 109.64 110.36 123.73 * * 116 GLN 116 1.322 1.240 1.521 1.539 1.482 122.28 115.42 121.13 107.50 110.08 112.09 123.44 * * * 117 SER 117 1.313 1.227 1.520 1.520 1.447 122.30 115.53 121.23 111.12 110.00 109.28 123.19 * * 118 THR 118 1.312 1.236 1.545 1.540 1.431 122.05 116.41 121.15 110.91 108.94 110.25 122.40 * * * 119 ILE 119 1.339 1.218 1.529 1.554 1.451 121.13 116.04 120.85 109.39 109.15 112.16 123.06 120 ALA 120 1.327 1.233 1.531 1.518 1.470 122.72 115.52 121.20 110.65 111.31 110.35 123.28 121 LYS 121 1.317 1.228 1.523 1.500 1.452 123.45 114.95 121.74 109.19 109.51 107.98 123.31 * * * 122 HIS 122 1.309 1.229 1.525 1.520 1.442 122.93 116.30 120.17 110.00 112.58 110.53 123.53 * * 123 LEU 123 1.325 1.238 1.531 1.539 1.441 124.11 115.90 121.14 112.28 110.66 107.64 122.93 * * +* +* 124 ALA 124 1.306 - 1.513 1.525 1.435 122.23 - - 110.86 109.41 110.50 - +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** ** *** ** ** * ** ** *** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 1.266 1.350 1.311 .015 **** +* * C-N (Pro) 1.341 .016 4 1.332 1.382 1.354 .019 +** C-O C-O 1.231 .020 123 1.207 1.253 1.232 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 119 1.475 1.559 1.520 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.492 1.542 1.514 .018 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.512 1.533 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.522 1.570 1.551 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.484 1.567 1.530 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.396 1.492 1.444 .018 *** +* NH1-CH2G* (Gly) 1.451 .016 5 1.415 1.458 1.439 .015 ** N-CH1E (Pro) 1.466 .015 4 1.453 1.478 1.469 .010 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_3 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 2.0 114 112.54 120.27 116.19 .98 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.91 118.56 117.36 .94 * CH1E-C-N (Pro) 116.9 1.5 4 115.47 116.68 116.04 .51 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.71 125.04 122.99 .59 * * O-C-N (Pro) 122.0 1.4 4 122.39 123.03 122.74 .29 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 117.94 124.47 121.98 1.15 ** +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.98 121.93 121.05 .64 C-N-CH1E (Pro) 122.6 5.0 4 122.06 124.02 123.12 .70 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.82 122.39 120.79 .55 * CH2G*-C-O (Gly) 120.8 2.1 5 119.69 120.67 120.20 .36 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.30 111.40 110.70 .27 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.09 111.95 110.07 1.01 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.50 114.60 110.38 1.36 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.26 114.71 110.14 1.81 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.01 113.71 112.16 1.40 N-CH1E-C (Pro) 111.8 2.5 4 111.35 112.88 112.02 .58 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.20 111.18 110.58 .30 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.58 112.73 111.31 .88 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.53 103.91 103.25 .64 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.42 116.31 110.44 1.57 +* *** ------------------------------------------------------------------------------------------------------------- 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_3 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] 104 92.0% Residues in additional allowed regions [a,b,l,p] 9 8.0% 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 92.0 83.8 10.0 .8 Inside b. Omega angle st dev 122 3.3 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 82 .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 5.7 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 44 5.4 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 44 7.9 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.4 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 31 8.5 20.4 5.0 -2.4 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% 92.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .82 2 Residue-by-residue listing for refined_3 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.10 Chi1-chi2 distribution -.11 Chi1 only .17 Chi3 & chi4 .47 Omega .09 ------ .04 ===== Main-chain covalent forces:- Main-chain bond lengths -.05 Main-chain bond angles .45 ------ .24 ===== OVERALL AVERAGE .10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.