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 - 61.1 - - 179.2 - - - - - - 179.5 - 33.9 - 2 GLY 2 - - - - - - - - - - - 176.8 - - - 3 HIS 3 B 66.7 - - - - - - - - - 180.1 - 32.7 - 4 HIS 4 B 61.4 - - - - - - - - - 174.8 - 32.6 - 5 HIS 5 S XX - 190.0 - - - - - - - - 183.3 - 30.9 - **** **** 6 HIS 6 B - 186.5 - - - - - - - - 181.5 -2.1 32.7 - 7 HIS 7 B - 182.6 - - - - - - - - 177.1 - 36.3 - 8 HIS 8 b - - -62.5 - - - - - - - 182.9 - 32.6 - 9 LEU 9 B 66.1 - - 174.3 - - - - - - 179.2 -1.6 32.8 - 10 GLU 10 B - - -55.6 173.3 - - - - - - 183.8 - 35.2 - 11 MET 11 B - - -58.8 - - - - - - - 178.6 - 34.3 - 12 ALA 12 B - - - - - - - - - - 183.9 - 33.8 - 13 SER 13 b - - -55.9 - - - - - - - 176.4 -1.1 33.6 - * * 14 GLU 14 t A - 185.9 - - - - - - - - 180.2 -1.2 35.7 - * * 15 GLU 15 T B 59.3 - - 187.8 - - - - - - 176.1 - 36.2 - 16 GLY 16 T - - - - - - - - - - - 178.3 -3.0 - - * * 17 GLN 17 t B 57.3 - - 174.9 - - - - - - 179.0 -.5 31.5 - ** ** 18 VAL 18 B - 182.9 - - - - - - - - 179.2 - 35.5 - 19 ILE 19 E B - - -61.8 - - - - - - - 180.1 -3.1 33.2 - * * 20 ALA 20 E B - - - - - - - - - - 180.9 -.8 33.7 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B - - -50.6 - - - - - - - 176.7 -2.6 36.0 - * * 22 HIS 22 A - - -62.9 - - - - - - - 185.5 -.6 34.7 - +* +* 23 THR 23 h B 52.9 - - - - - - - - - 182.6 - 34.6 - 24 VAL 24 H A 62.6 - - - - -75.3 -26.3 - - - 179.2 - 32.3 - * * 25 GLU 25 H A - 178.1 - - - -63.8 -51.8 - - - 178.2 - 34.8 - * * 26 THR 26 H A - - -53.1 - - -62.2 -41.1 - - - 176.3 - 35.1 - 27 TRP 27 H A - 172.3 - - - -54.3 -53.4 - - - 180.7 -1.6 34.5 - * * 28 ASN 28 H A - 185.9 - - - -64.8 -44.1 - - - 181.6 -2.9 34.8 - * * 29 GLU 29 H A - 179.9 - 179.6 - -56.9 -48.4 - - - 181.3 -2.8 34.4 - * * 30 GLN 30 H A - - -71.2 - - -65.2 -39.0 - - - 179.6 -2.8 33.1 - 31 LEU 31 H A - - -67.5 180.7 - -69.0 -46.8 - - - 179.3 -1.7 34.0 - 32 GLN 32 H A - 183.8 - 177.5 - -60.1 -41.1 - - - 178.1 -3.0 33.7 - * * 33 LYS 33 H A - 181.1 - 181.6 - -65.9 -48.3 - - - 183.2 -2.5 34.2 - 34 ALA 34 H A - - - - - -69.1 -31.8 - - - 179.9 -3.1 33.5 - * * 35 ASN 35 H A - 192.1 - - - -67.5 -53.4 - - - 179.0 -2.9 36.4 - * * * 36 GLU 36 H A - 179.0 - 180.7 - -60.0 -40.5 - - - 181.8 -2.3 34.0 - 37 SER 37 H A - - -56.9 - - -79.7 -11.0 - - - 182.1 -2.6 35.0 - * +** +** 38 LYS 38 h L - - -63.2 181.1 - - - - - - 178.8 -.8 32.6 - +* +* 39 THR 39 t B - - -48.3 - - - - - - - 178.6 -2.0 36.3 - * * 40 LEU 40 E B - 188.0 - 172.9 - - - - - - 186.5 -1.9 34.6 - * * 41 VAL 41 E B 59.4 - - - - - - - - - 176.9 -.7 32.8 - +* +* 42 VAL 42 E B 63.7 - - - - - - - - - 181.7 -3.3 33.1 - +* +* 43 VAL 43 E B - 178.9 - - - - - - - - 176.2 -3.3 35.3 - +* +* 44 ASP 44 E B - 175.6 - - - - - - - - 178.7 -2.8 32.9 - 45 PHE 45 E B - - -61.5 - - - - - - - 184.8 -3.0 35.7 - * * 46 THR 46 E B - 188.9 - - - - - - - - 176.4 -2.8 35.5 - 47 ALA 47 t B - - - - - - - - - - 183.1 - 34.2 - 48 SER 48 T A - 185.5 - - - - - - - - 179.8 - 33.1 - 49 TRP 49 T A 56.6 - - - - - - - - - 180.6 - 31.9 - 50 CYS 50 h B - 176.2 - 219.7 - - - 58.9 - 2.0 182.2 -1.9 34.2 - ** +** +** 51 GLY 51 H - - - - - - -65.7 -63.1 - - - 179.4 -.6 - - ** +* ** 52 PRO 52 H - - - - - -56.8 -56.8 -30.2 - - - 178.5 - 38.3 - * * 53 CYS 53 H A - - -56.3 - - -67.8 -38.5 58.9 - 2.0 177.4 - 35.1 - +** +** 54 ARG 54 H A - 188.6 - - - -70.8 -37.3 - - - 180.1 -1.4 34.7 - 55 PHE 55 H A - 178.1 - - - -62.7 -32.0 - - - 181.7 -2.3 33.8 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 ILE 56 H A - 193.4 - - - -87.9 -10.5 - - - 182.6 -1.5 33.8 - +* +** +** 57 ALA 57 H A - - - - - -60.6 -50.7 - - - 179.1 -.7 31.1 - * +* +* 58 PRO 58 H - - - - - -55.3 -55.3 -31.5 - - - 179.5 - 38.5 - * * 59 PHE 59 H A - 182.0 - - - -75.0 -44.6 - - - 177.4 - 33.0 - 60 PHE 60 H A - 184.4 - - - -63.7 -33.5 - - - 176.4 -2.1 34.5 - 61 ALA 61 H A - - - - - -66.1 -31.5 - - - 177.2 -2.7 33.9 - 62 ASP 62 H A - 182.2 - - - -64.8 -46.4 - - - 173.7 -1.0 35.3 - * * * 63 LEU 63 H A - - -85.5 - - -54.0 -45.3 - - - 179.1 -1.8 34.6 - * * 64 ALA 64 H A - - - - - -62.0 -32.2 - - - 179.6 -2.0 33.0 - 65 LYS 65 H A - 182.1 - 185.5 - -79.2 -26.0 - - - 187.6 -1.5 35.9 - * * * * 66 LYS 66 H A - 180.0 - 181.6 - -96.6 -41.0 - - - 190.7 -1.5 34.9 - +** +* +** 67 LEU 67 h B - - -63.2 172.8 - - - - - - 181.1 -3.3 31.4 - +* +* 68 PRO 68 S - - - - - -79.7 - - - - - 185.2 - 39.5 - * +* +* 69 ASN 69 e A - 193.6 - - - - - - - - 185.0 - 35.7 - 70 VAL 70 E B - 183.9 - - - - - - - - 173.9 - 33.6 - * * 71 LEU 71 E B - 185.1 - - - - - - - - 188.4 -3.1 35.1 - * * * 72 PHE 72 E B - - -41.5 - - - - - - - 179.5 - 37.2 - +* +* 73 LEU 73 E B - - -71.7 - - - - - - - 173.9 -2.6 33.7 - * * 74 LYS 74 E B - - -66.5 - - - - - - - 181.8 -2.4 36.8 - 75 VAL 75 E B - 178.9 - - - - - - - - 181.1 -3.3 34.1 - +* +* 76 ASP 76 E B - 187.2 - - - - - - - - 184.6 -2.4 31.7 - 77 THR 77 e A - - -55.6 - - - - - - - 179.2 -3.2 35.1 - +* +* 78 ASP 78 T A - 187.8 - - - - - - - - 174.7 - 33.8 - 79 GLU 79 T A - - -89.3 - - - - - - - 184.2 - 33.9 - +* +* 80 LEU 80 h a - 188.1 - - - - - - - - 187.4 -3.0 35.0 - * * * 81 LYS 81 H A - 204.4 - - - -53.3 -49.4 - - - 184.4 -.7 35.6 - * * +* +* 82 SER 82 H A - - -59.4 - - -69.5 -44.0 - - - 179.8 - 32.3 - 83 VAL 83 H A - 177.2 - - - -70.0 -38.6 - - - 177.8 - 32.0 - 84 ALA 84 H A - - - - - -63.9 -31.6 - - - 176.4 -3.0 33.2 - * * 85 SER 85 H A - 181.7 - - - -66.0 -30.7 - - - 178.5 -1.6 34.2 - 86 ASP 86 H A - 180.4 - - - -72.9 -35.9 - - - 176.1 -1.0 32.8 - * * 87 TRP 87 h A - - -67.6 - - - - - - - 177.1 -1.7 33.0 - 88 ALA 88 T l - - - - - - - - - - 181.3 -.8 33.1 - +* +* 89 ILE 89 t B - - -56.4 - - - - - - - 179.7 -2.7 33.9 - 90 GLN 90 a - 187.1 - 184.1 - - - - - - 179.1 -.6 34.4 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 91 ALA 91 S B - - - - - - - - - - 183.1 - 34.2 - 92 MET 92 S B - - -62.0 178.1 - - - - - - -1.3 -.7 34.7 - +* +* 93 PRO 93 e cis - - - - - -92.7 - - - - - 175.8 - 39.5 - ** +* ** 94 THR 94 E B - - -55.8 - - - - - - - 181.5 -2.3 35.1 - 95 PHE 95 E B - - -63.2 - - - - - - - 179.6 -3.0 36.5 - * * 96 MET 96 E B - 177.0 - 181.3 - - - - - - 182.7 -3.4 35.2 - +* +* 97 PHE 97 E B - - -67.8 - - - - - - - 176.8 -3.3 36.3 - +* +* 98 LEU 98 E B - - -54.3 - - - - - - - 176.6 -3.0 35.3 - * * 99 LYS 99 E B - 177.4 - 175.2 - - - - - - 177.5 -3.5 33.7 - ** ** 100 GLU 100 T l - - -57.9 175.2 - - - - - - 180.7 - 33.5 - 101 GLY 101 T - - - - - - - - - - - 177.9 - - - 102 LYS 102 E B - 178.7 - 181.5 - - - - - - 181.1 -2.0 34.6 - 103 ILE 103 E B - - -59.9 172.8 - - - - - - 176.6 - 34.9 - 104 LEU 104 E a - - -67.6 186.1 - - - - - - 187.6 -2.3 33.4 - * * 105 ASP 105 E B 56.3 - - - - - - - - - 181.4 -1.9 32.7 - 106 LYS 106 E B 60.3 - - 176.9 - - - - - - 176.2 - 34.6 - 107 VAL 107 E B - 179.1 - - - - - - - - 181.4 -3.3 34.7 - +* +* 108 VAL 108 E B 60.3 - - - - - - - - - 180.0 - 32.2 - 109 GLY 109 e - - - - - - - - - - - 180.5 -2.3 - - 110 ALA 110 B - - - - - - - - - - 176.1 - 34.6 - 111 LYS 111 h B - - -71.0 175.7 - - - - - - 187.2 -1.0 33.7 - * * * 112 LYS 112 H A - - -66.8 - - -67.0 -50.1 - - - 182.6 - 33.2 - 113 ASP 113 H A 64.3 - - - - -71.3 -39.8 - - - 181.4 - 32.5 - 114 GLU 114 H A - 185.8 - 183.7 - -68.9 -35.9 - - - 178.3 - 33.7 - 115 LEU 115 H A - 184.6 - - - -60.1 -50.5 - - - 178.3 -2.0 35.4 - 116 GLN 116 H A - - -63.0 175.2 - -55.2 -41.3 - - - 179.9 -1.8 34.2 - 117 SER 117 H A - - -55.5 - - -68.0 -38.4 - - - 178.1 -1.9 34.1 - 118 THR 118 H A - - -57.9 - - -67.3 -33.7 - - - 176.2 -2.5 33.9 - 119 ILE 119 H A - - -59.0 176.5 - -64.5 -51.8 - - - 180.6 -2.3 34.3 - * * 120 ALA 120 H A - - - - - -63.4 -31.6 - - - 176.2 -2.6 33.1 - 121 LYS 121 H A - 190.6 - 182.0 - -60.2 -44.3 - - - 177.7 -2.1 36.5 - 122 HIS 122 H A - - -79.5 - - -73.0 -37.2 - - - 180.5 -1.8 33.0 - 123 LEU 123 h A - - -84.2 - - - - - - - 175.6 -2.6 32.8 - * * 124 ALA 124 t - - - - - - - - - - - - -.7 34.4 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** ** +** +** +** +* ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.6 183.8 -62.6 180.3 -71.1 -66.3 -39.5 58.9 - 2.0 180.0 -2.1 34.3 +** +** Standard deviations: 3.8 5.9 9.7 8.6 18.2 8.4 10.2 .0 - .0 3.3 .9 1.6 Numbers of values: 15 46 41 30 4 47 47 2 0 2 122 82 119 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 - 1.231 1.510 1.548 1.465 - 116.73 119.92 110.33 109.57 111.35 123.34 2 GLY 2 1.328 1.230 1.513 - 1.455 121.47 116.84 120.23 - 111.63 - 122.94 3 HIS 3 1.313 1.235 1.520 1.572 1.451 121.61 117.20 120.02 111.77 109.12 112.06 122.73 * ** ** 4 HIS 4 1.317 1.239 1.529 1.556 1.457 120.77 114.73 121.12 110.44 112.56 112.07 124.14 * * 5 HIS 5 1.324 1.225 1.533 1.546 1.471 126.37 117.95 119.80 111.89 113.67 112.13 122.25 +** +** 6 HIS 6 1.326 1.221 1.504 1.539 1.453 119.85 115.48 121.00 110.36 110.12 112.90 123.52 * * * 7 HIS 7 1.283 1.234 1.517 1.546 1.434 123.25 118.99 118.68 111.48 105.76 107.75 122.28 *** * * * +* +* *** 8 HIS 8 1.330 1.230 1.511 1.539 1.466 119.39 115.41 120.86 109.99 109.13 113.55 123.64 * +* +* 9 LEU 9 1.305 1.245 1.511 1.556 1.441 122.80 115.07 121.49 110.28 111.85 112.30 123.43 +* * * +* 10 GLU 10 1.294 1.242 1.516 1.514 1.431 122.61 116.69 120.28 111.46 108.48 108.45 123.03 ** * * ** 11 MET 11 1.299 1.234 1.515 1.550 1.444 122.06 116.63 120.43 109.93 110.05 111.21 122.92 ** ** 12 ALA 12 1.311 1.245 1.517 1.525 1.447 121.59 115.98 120.91 110.90 109.41 110.83 123.09 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 SER 13 1.305 1.231 1.529 1.528 1.432 122.01 115.58 121.21 111.21 111.94 110.04 123.17 +* * +* 14 GLU 14 1.317 1.242 1.532 1.543 1.455 122.24 113.57 122.54 110.17 107.36 109.28 123.88 * * * * 15 GLU 15 1.307 1.243 1.532 1.536 1.437 124.53 116.63 120.72 110.26 110.13 107.87 122.64 +* * +* +* +* 16 GLY 16 1.310 1.233 1.511 - 1.442 120.41 117.67 120.03 - 113.80 - 122.30 * * 17 GLN 17 1.315 1.232 1.492 1.520 1.448 120.04 113.71 121.93 109.94 112.87 113.77 124.36 +* * +* +* 18 VAL 18 1.288 1.238 1.531 1.548 1.440 123.74 118.03 119.62 109.07 108.43 110.61 122.35 +** * +** 19 ILE 19 1.324 1.237 1.523 1.571 1.439 120.52 116.39 121.04 109.79 109.38 113.33 122.56 * * * 20 ALA 20 1.301 1.232 1.513 1.524 1.438 121.52 116.17 120.94 110.93 109.79 110.85 122.89 ** * ** 21 CYS 21 1.304 1.231 1.509 1.505 1.407 121.84 116.11 121.04 108.92 108.92 109.72 122.82 +* * +** +** 22 HIS 22 1.285 1.235 1.509 1.547 1.442 121.70 115.10 121.52 110.13 108.01 111.05 123.36 *** * *** 23 THR 23 1.327 1.244 1.528 1.549 1.439 122.01 116.50 120.43 109.90 110.51 110.56 123.07 24 VAL 24 1.327 1.232 1.545 1.570 1.462 121.83 116.64 120.77 111.19 111.71 111.99 122.58 * * 25 GLU 25 1.327 1.232 1.522 1.530 1.465 122.13 115.62 120.85 110.49 110.35 109.33 123.50 26 THR 26 1.316 1.234 1.536 1.535 1.448 122.46 115.15 121.05 110.34 109.67 109.36 123.79 * * 27 TRP 27 1.327 1.236 1.540 1.539 1.456 123.43 116.32 120.71 111.39 111.50 108.59 122.95 * * 28 ASN 28 1.325 1.238 1.529 1.534 1.466 121.75 115.69 120.80 108.97 110.47 110.83 123.50 29 GLU 29 1.334 1.234 1.526 1.536 1.463 123.05 116.58 120.47 110.04 111.63 110.14 122.92 30 GLN 30 1.322 1.223 1.510 1.489 1.419 121.91 117.14 120.31 111.16 112.86 110.12 122.54 ** ** ** 31 LEU 31 1.314 1.222 1.501 1.487 1.408 121.39 116.72 120.03 110.30 111.89 110.20 123.26 * * ** +** +** 32 GLN 32 1.315 1.237 1.527 1.526 1.445 121.49 115.45 121.01 111.31 109.59 110.47 123.49 33 LYS 33 1.322 1.236 1.534 1.532 1.442 122.44 117.23 120.16 110.24 110.88 110.38 122.58 34 ALA 34 1.344 1.228 1.513 1.522 1.463 121.35 115.87 120.84 110.34 111.38 111.01 123.29 * * 35 ASN 35 1.316 1.230 1.506 1.523 1.454 122.44 114.80 121.36 108.16 108.71 109.80 123.84 * * 36 GLU 36 1.321 1.236 1.536 1.533 1.465 122.95 116.50 120.79 109.95 111.63 110.57 122.71 37 SER 37 1.315 1.233 1.529 1.518 1.443 121.44 116.10 120.47 109.98 111.60 109.15 123.39 38 LYS 38 1.344 1.231 1.523 1.512 1.464 123.18 114.91 121.70 111.51 110.80 111.14 123.35 * * 39 THR 39 1.298 1.243 1.522 1.527 1.432 123.37 116.42 120.74 108.35 108.13 110.06 122.81 ** * * ** 40 LEU 40 1.286 1.212 1.532 1.559 1.439 121.49 118.17 119.93 112.80 105.39 109.25 121.89 *** * * * ** *** 41 VAL 41 1.299 1.240 1.531 1.565 1.441 120.04 115.63 121.09 111.87 112.57 110.53 123.25 ** * ** 42 VAL 42 1.318 1.233 1.526 1.571 1.434 122.46 116.27 121.09 110.85 109.06 112.49 122.61 * * * 43 VAL 43 1.290 1.219 1.509 1.546 1.436 121.77 116.87 120.28 108.48 110.16 111.15 122.84 +** * +** 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.296 1.239 1.510 1.522 1.444 120.72 115.74 120.86 110.58 110.71 111.94 123.38 ** ** 45 PHE 45 1.304 1.242 1.515 1.520 1.426 123.09 116.54 120.56 109.37 108.47 109.85 122.90 +* +* +* 46 THR 46 1.302 1.208 1.532 1.548 1.425 121.22 117.24 120.24 109.95 109.52 109.62 122.53 +* * +* * +* 47 ALA 47 1.304 1.239 1.509 1.518 1.444 122.54 116.77 119.98 110.55 108.19 110.96 123.26 +* * +* 48 SER 48 1.310 1.233 1.555 1.546 1.456 122.27 117.15 120.69 112.05 111.83 109.86 122.12 * * * * 49 TRP 49 1.335 1.235 1.537 1.556 1.464 121.59 116.71 120.85 111.43 112.61 111.86 122.43 * * 50 CYS 50 1.308 1.236 1.537 1.528 1.446 121.80 115.71 120.93 111.17 110.80 109.43 123.36 * * 51 GLY 51 1.331 1.237 1.529 - 1.466 122.65 118.89 119.67 - 113.91 - 121.45 * * * 52 PRO 52 1.369 1.231 1.527 1.542 1.477 122.88 115.32 121.57 110.53 111.43 104.06 123.11 +* * +* 53 CYS 53 1.311 1.224 1.529 1.500 1.442 122.73 116.91 120.79 109.93 110.71 109.09 122.30 * +* +* 54 ARG 54 1.318 1.222 1.531 1.557 1.450 121.19 115.31 121.38 111.82 107.37 109.37 123.28 * * * 55 PHE 55 1.313 1.233 1.544 1.540 1.454 123.11 117.23 120.59 111.31 112.30 109.44 122.16 * * 56 ILE 56 1.322 1.240 1.558 1.579 1.462 120.80 115.75 121.44 110.73 110.12 110.99 122.77 +* * +* 57 ALA 57 1.335 1.223 1.549 1.528 1.469 122.72 120.26 118.84 111.48 113.99 111.92 120.90 * ** * * * ** 58 PRO 58 1.383 1.239 1.527 1.539 1.478 122.38 115.88 120.98 109.84 112.55 104.19 123.13 +** * +** 59 PHE 59 1.318 1.212 1.531 1.534 1.439 121.51 116.51 120.85 111.79 109.97 110.91 122.61 60 PHE 60 1.318 1.233 1.541 1.541 1.474 122.42 115.82 121.35 111.34 109.51 109.11 122.83 61 ALA 61 1.324 1.231 1.531 1.520 1.452 122.23 116.21 120.81 110.60 110.36 110.46 122.98 62 ASP 62 1.327 1.232 1.495 1.516 1.473 122.41 114.37 121.34 108.85 108.84 110.62 124.29 * * 63 LEU 63 1.313 1.227 1.519 1.531 1.434 123.68 116.22 120.43 110.58 111.09 109.55 123.33 * * * * 64 ALA 64 1.322 1.233 1.522 1.515 1.457 122.78 116.00 121.07 110.80 112.07 110.90 122.92 65 LYS 65 1.306 1.238 1.541 1.535 1.441 121.92 116.03 120.85 109.63 110.44 108.81 123.11 +* +* 66 LYS 66 1.320 1.235 1.537 1.539 1.450 121.93 118.06 119.85 109.57 114.62 108.97 122.08 * * 67 LEU 67 1.317 1.219 1.532 1.518 1.453 120.45 116.20 121.43 112.76 114.82 110.06 122.37 * * * 68 PRO 68 1.345 1.230 1.551 1.531 1.474 123.51 117.59 120.30 109.51 114.89 102.37 122.10 * * * 69 ASN 69 1.329 1.219 1.528 1.556 1.481 121.35 116.12 121.91 110.13 109.30 108.98 121.96 * * * 70 VAL 70 1.299 1.225 1.523 1.552 1.433 120.42 115.71 121.02 110.17 111.37 111.46 123.22 ** * ** 71 LEU 71 1.306 1.228 1.526 1.535 1.440 123.17 117.59 119.92 110.83 106.27 109.89 122.49 +* +* +* 72 PHE 72 1.308 1.236 1.515 1.519 1.459 120.82 116.65 120.40 107.24 109.57 109.20 122.95 * +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 LEU 73 1.298 1.233 1.515 1.541 1.446 122.55 114.98 121.33 108.16 112.27 112.87 123.69 ** * * ** 74 LYS 74 1.308 1.222 1.509 1.514 1.412 124.60 117.21 120.22 109.33 106.85 108.71 122.55 * ** +* +* * ** 75 VAL 75 1.283 1.235 1.502 1.548 1.439 121.21 116.53 120.24 110.11 109.49 111.49 123.23 *** * * *** 76 ASP 76 1.320 1.236 1.507 1.508 1.443 120.19 113.77 121.96 111.20 109.96 113.16 124.25 * * +* +* 77 THR 77 1.281 1.247 1.538 1.515 1.420 125.81 116.73 120.74 112.11 112.68 106.69 122.52 *** +* ** * +** *** 78 ASP 78 1.321 1.238 1.509 1.522 1.442 120.38 115.27 120.90 110.37 108.29 111.76 123.83 * * 79 GLU 79 1.333 1.224 1.523 1.529 1.434 122.97 117.48 120.49 108.19 112.41 112.44 122.04 * * * * 80 LEU 80 1.318 1.235 1.545 1.535 1.447 121.33 113.84 122.17 111.86 108.69 108.27 123.84 * * * 81 LYS 81 1.320 1.235 1.554 1.553 1.457 125.60 117.44 120.28 110.71 112.12 107.70 122.27 * * ** +* ** 82 SER 82 1.326 1.239 1.539 1.522 1.463 120.86 117.23 120.60 111.16 112.81 111.20 122.16 83 VAL 83 1.318 1.230 1.529 1.556 1.454 120.71 116.70 120.79 111.51 110.48 112.57 122.44 * * 84 ALA 84 1.327 1.236 1.528 1.511 1.457 121.26 115.93 120.93 110.85 110.53 110.99 123.13 85 SER 85 1.330 1.236 1.535 1.541 1.445 122.24 116.59 120.69 110.45 110.22 110.58 122.72 86 ASP 86 1.331 1.226 1.514 1.533 1.463 121.70 115.67 121.19 111.19 109.99 111.67 123.08 87 TRP 87 1.322 1.235 1.535 1.528 1.454 122.29 115.85 120.45 110.66 111.71 111.34 123.70 88 ALA 88 1.348 1.236 1.525 1.534 1.474 124.39 116.14 120.82 111.14 111.82 110.63 122.97 * * * 89 ILE 89 1.315 1.239 1.523 1.553 1.443 121.44 115.75 121.12 109.58 110.04 112.05 123.12 90 GLN 90 1.307 1.236 1.525 1.529 1.446 121.53 116.16 121.31 110.06 109.69 110.67 122.53 +* +* 91 ALA 91 1.312 1.222 1.505 1.523 1.433 121.18 116.58 120.83 110.86 108.75 110.62 122.59 * * * 92 MET 92 1.289 1.233 1.507 1.523 1.434 121.05 118.19 120.14 110.14 110.00 110.24 121.66 +** * +** 93 PRO 93 1.328 1.236 1.536 1.525 1.457 124.03 116.69 121.09 110.57 112.08 101.87 122.13 * * 94 THR 94 1.293 1.227 1.513 1.526 1.427 120.72 116.76 120.12 109.02 108.87 111.12 123.06 +** +* +** 95 PHE 95 1.308 1.218 1.498 1.529 1.413 121.68 115.80 121.17 108.47 108.08 109.91 123.02 +* * ** * ** 96 MET 96 1.271 1.228 1.505 1.518 1.422 122.55 115.27 121.22 111.64 108.70 108.34 123.50 **** +* * **** 97 PHE 97 1.282 1.245 1.504 1.514 1.407 123.70 116.26 121.18 109.03 110.35 108.96 122.56 *** * +** * *** 98 LEU 98 1.286 1.218 1.520 1.558 1.423 120.55 117.22 120.26 107.48 107.21 113.10 122.50 *** * +* * * +* *** 99 LYS 99 1.289 1.239 1.489 1.526 1.430 121.39 114.59 120.92 110.98 109.31 111.22 124.44 +** +* * +** 100 GLU 100 1.321 1.231 1.533 1.514 1.445 124.22 115.64 121.08 111.63 111.28 109.72 123.22 * * 101 GLY 101 1.322 1.230 1.523 - 1.447 121.65 117.23 120.01 - 113.51 - 122.75 102 LYS 102 1.321 1.224 1.525 1.537 1.459 121.67 116.83 120.09 110.08 109.44 110.43 123.08 103 ILE 103 1.317 1.234 1.529 1.559 1.471 122.62 116.74 120.45 108.81 110.95 110.94 122.80 104 LEU 104 1.321 1.231 1.508 1.524 1.429 120.64 116.22 120.53 109.26 111.42 112.52 123.24 +* * +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 105 ASP 105 1.311 1.222 1.500 1.524 1.450 121.30 115.80 120.97 110.32 112.68 111.83 123.19 * * * 106 LYS 106 1.308 1.240 1.533 1.536 1.449 121.80 115.64 121.19 109.46 111.38 110.56 123.17 * * 107 VAL 107 1.309 1.231 1.521 1.562 1.448 123.07 117.07 120.28 109.34 108.15 111.85 122.63 * * * 108 VAL 108 1.308 1.247 1.540 1.566 1.447 121.10 115.74 121.46 111.77 111.47 111.81 122.78 * * * 109 GLY 109 1.315 1.240 1.503 - 1.435 121.30 117.46 120.11 - 110.40 - 122.43 110 ALA 110 1.318 1.225 1.495 1.527 1.433 119.59 115.13 121.46 110.02 109.09 110.80 123.39 * * * * 111 LYS 111 1.284 1.222 1.485 1.515 1.408 123.16 116.07 120.36 112.67 108.09 109.86 123.58 *** +* +** * * *** 112 LYS 112 1.300 1.223 1.518 1.532 1.402 122.72 116.55 120.47 111.63 112.06 110.32 122.93 ** +** +** 113 ASP 113 1.314 1.228 1.534 1.546 1.464 121.41 117.31 120.30 110.84 112.06 111.80 122.36 * * 114 GLU 114 1.332 1.241 1.514 1.528 1.465 121.13 116.13 120.64 109.82 110.52 111.60 123.23 115 LEU 115 1.326 1.216 1.499 1.511 1.445 121.50 114.87 120.94 109.03 108.77 110.47 124.17 * * 116 GLN 116 1.316 1.242 1.517 1.515 1.469 123.15 116.49 120.31 109.43 111.81 110.63 123.19 117 SER 117 1.322 1.221 1.527 1.524 1.447 120.82 115.75 121.21 111.21 109.64 109.95 122.97 118 THR 118 1.316 1.237 1.550 1.546 1.437 122.35 116.57 120.81 111.37 110.07 110.05 122.60 * * * * 119 ILE 119 1.333 1.223 1.519 1.550 1.453 121.67 116.19 120.63 108.96 109.41 112.14 123.13 120 ALA 120 1.326 1.226 1.525 1.518 1.461 122.08 115.67 120.76 111.33 110.87 110.66 123.58 121 LYS 121 1.322 1.223 1.528 1.504 1.451 123.42 115.61 121.34 109.12 109.17 108.30 123.05 * * * 122 HIS 122 1.326 1.236 1.523 1.529 1.451 122.40 116.98 120.69 110.35 112.15 111.59 122.32 123 LEU 123 1.320 1.224 1.523 1.512 1.427 122.56 115.50 121.30 112.08 112.62 109.88 123.17 +* * +* 124 ALA 124 1.289 - 1.510 1.524 1.429 122.36 - - 110.78 107.56 110.75 - +** +* * +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** +** +** ** * +* ** +** * **** ----------------------------------------------------------------------------------------------------------------------------------- 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 1.271 1.348 1.314 .015 **** * * C-N (Pro) 1.341 .016 4 1.328 1.383 1.356 .021 +** C-O C-O 1.231 .020 123 1.208 1.247 1.232 .008 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.485 1.558 1.523 .014 +* +* CH2G*-C (Gly) 1.516 .018 5 1.503 1.529 1.516 .009 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.511 1.534 1.522 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.515 1.579 1.552 .016 * CH1E-CH2E (the rest) 1.530 .020 84 1.487 1.572 1.531 .016 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.402 1.481 1.445 .016 +** * NH1-CH2G* (Gly) 1.451 .016 5 1.435 1.466 1.449 .011 N-CH1E (Pro) 1.466 .015 4 1.457 1.478 1.471 .009 ------------------------------------------------------------------------------------------------------------- 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 2.0 114 113.57 120.26 116.23 1.02 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.84 118.89 117.62 .69 * CH1E-C-N (Pro) 116.9 1.5 4 115.32 117.59 116.37 .86 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.90 124.44 122.96 .60 * O-C-N (Pro) 122.0 1.4 4 122.10 123.13 122.62 .50 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.39 126.37 122.04 1.22 * +** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.41 122.65 121.50 .72 * C-N-CH1E (Pro) 122.6 5.0 4 122.38 124.03 123.20 .62 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.68 122.54 120.78 .58 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.67 120.23 120.01 .19 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.02 111.48 110.81 .37 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.35 112.11 110.15 1.12 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.24 112.80 110.40 1.14 +* * N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.39 114.82 110.29 1.78 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.40 113.91 112.65 1.40 N-CH1E-C (Pro) 111.8 2.5 4 111.43 114.89 112.74 1.31 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.46 111.92 110.87 .34 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 106.69 113.33 111.04 1.36 +** * N-CH1E-CH2E (Pro) 103.0 1.1 4 101.87 104.19 103.12 1.02 * * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.70 113.77 110.42 1.41 +* +* ------------------------------------------------------------------------------------------------------------- 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] 105 92.9% Residues in additional allowed regions [a,b,l,p] 7 6.2% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 1 .9% ---- ------ 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 92.9 83.8 10.0 .9 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 1.6 3.1 1.6 -1.0 Inside e. H-bond energy st dev 82 .9 .8 .2 .3 Inside f. Overall G-factor 124 .1 -.4 .3 1.5 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 15 3.8 18.1 6.5 -2.2 BETTER b. Chi-1 trans st dev 46 5.9 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 41 9.7 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 102 7.7 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 30 8.6 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% 92.9 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 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 -.15 Chi1-chi2 distribution -.16 Chi1 only -.10 Chi3 & chi4 .28 Omega .03 ------ -.04 ===== Main-chain covalent forces:- Main-chain bond lengths .05 Main-chain bond angles .45 ------ .28 ===== OVERALL AVERAGE .07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.