Residue-by-residue listing for refined_4 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 - - - -60.4 - - - - - - - 177.9 - 34.9 - 2 GLY 2 - - - - - - - - - - - 181.2 - - - 3 HIS 3 l - - -63.4 - - - - - - - 182.1 - 31.8 - 4 HIS 4 b 56.7 - - - - - - - - - 177.6 - 30.4 - 5 HIS 5 b 60.8 - - - - - - - - - 182.4 -.9 33.0 - * * 6 HIS 6 B - - -59.8 - - - - - - - 173.7 - 34.8 - * * 7 HIS 7 B - 185.2 - - - - - - - - 190.3 - 34.8 - +* +* 8 HIS 8 B 61.0 - - - - - - - - - 172.4 -1.1 34.4 - * * * 9 LEU 9 b - - -63.3 - - - - - - - 186.9 - 34.0 - * * 10 GLU 10 B - 186.8 - 172.5 - - - - - - 177.3 -1.2 33.9 - * * 11 MET 11 b - 181.3 - - - - - - - - 177.3 -.8 32.6 - +* +* 12 ALA 12 b - - - - - - - - - - 180.1 -2.0 33.3 - 13 SER 13 B 48.1 - - - - - - - - - 181.8 - 34.0 - * * 14 GLU 14 S b - 185.3 - 170.9 - - - - - - 176.6 - 30.0 - * * 15 GLU 15 S b 51.7 - - - - - - - - - 181.3 -2.0 32.1 - 16 GLY 16 S - - - - - - - - - - - 181.9 -2.1 - - 17 GLN 17 S B 56.8 - - 178.9 - - - - - - 180.1 - 35.5 - 18 VAL 18 B - 182.0 - - - - - - - - 181.9 - 34.7 - 19 ILE 19 E B - - -58.8 - - - - - - - 178.7 -2.6 34.2 - Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 ALA 20 E B - - - - - - - - - - 178.9 -.8 34.1 - +* +* 21 CYS 21 E B - - -56.6 - - - - - - - 179.9 -1.6 35.2 - 22 HIS 22 S A - - -63.6 - - - - - - - 181.9 - 33.5 - 23 THR 23 h B 60.3 - - - - - - - - - 174.9 - 35.8 - 24 VAL 24 H A 60.0 - - - - -72.3 -24.1 - - - 178.8 - 33.7 - * * 25 GLU 25 H A - 180.9 - 175.0 - -64.2 -50.5 - - - 176.9 - 35.0 - 26 THR 26 H A - - -58.9 - - -64.7 -33.9 - - - 176.4 - 33.1 - 27 TRP 27 H A - 170.5 - - - -54.9 -52.9 - - - 177.5 -1.5 33.5 - * * 28 ASN 28 H A - 179.3 - - - -60.8 -43.0 - - - 180.5 -2.3 35.1 - 29 GLU 29 H A - 179.9 - 172.1 - -58.7 -42.2 - - - 179.4 -2.2 33.5 - 30 GLN 30 H A - - -65.7 - - -70.0 -39.8 - - - 178.0 -2.9 34.5 - * * 31 LEU 31 H A - - -66.3 180.7 - -65.9 -45.5 - - - 176.7 -2.2 34.3 - 32 GLN 32 H A - 180.9 - 179.1 - -61.1 -38.7 - - - 176.6 -3.1 33.1 - * * 33 LYS 33 H A - 180.2 - 182.1 - -61.1 -50.8 - - - 182.2 -2.1 34.5 - * * 34 ALA 34 H A - - - - - -67.7 -34.9 - - - 180.0 -3.0 33.6 - * * 35 ASN 35 H A - 186.3 - - - -66.9 -54.3 - - - 182.0 -2.9 36.6 - * * * 36 GLU 36 H A - 187.0 - - - -61.0 -43.7 - - - 181.9 -3.1 34.5 - * * 37 SER 37 H A - - -62.0 - - -81.7 -9.2 - - - 182.2 -2.7 33.9 - * +** +** 38 LYS 38 h L - - -82.2 164.0 - - - - - - 176.2 -.8 31.0 - * +* +* 39 THR 39 t B - - -45.6 - - - - - - - 179.1 -1.5 36.5 - * * 40 LEU 40 E B - - -81.0 - - - - - - - 183.6 -.8 34.6 - +* +* 41 VAL 41 E B 60.2 - - - - - - - - - 176.5 -.6 32.8 - +* +* 42 VAL 42 E B - 180.7 - - - - - - - - 184.6 -2.8 33.9 - * * 43 VAL 43 E B - 183.7 - - - - - - - - 175.2 -2.9 34.3 - * * 44 ASP 44 E B - 172.1 - - - - - - - - 175.1 -3.0 36.2 - * * 45 PHE 45 E B - - -62.4 - - - - - - - 182.1 -2.8 36.1 - * * 46 THR 46 e B - - -58.5 - - - - - - - 169.7 -2.4 37.0 - +* +* 47 ALA 47 t B - - - - - - - - - - 185.6 - 34.6 - 48 SER 48 T A - - -56.1 - - - - - - - 181.5 - 33.3 - 49 TRP 49 T A 51.9 - - - - - - - - - 181.2 - 31.9 - 50 CYS 50 h B - 177.5 - 219.2 - - - 54.8 - 2.0 182.5 -2.1 34.0 - ** +** +** 51 GLY 51 H - - - - - - -63.8 -65.4 - - - 180.7 -.6 - - ** +* ** 52 PRO 52 H - - - - - -58.4 -58.4 -30.6 - - - 179.1 - 38.3 - * * 53 CYS 53 H A - - -52.7 - - -69.4 -34.3 54.8 - 2.0 178.0 - 36.0 - +** +** Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 54 ARG 54 H A - 182.8 - 176.9 - -73.0 -29.2 - - - 178.3 -1.3 33.1 - 55 PHE 55 H A - 179.3 - - - -67.0 -35.4 - - - 183.5 -1.5 34.4 - 56 ILE 56 H A - 192.4 - - - -87.4 -17.0 - - - 182.4 -1.4 34.2 - +* +* +* 57 ALA 57 H A - - - - - -59.0 -47.3 - - - 180.6 -1.0 31.8 - * * 58 PRO 58 H - - - - - -57.8 -57.8 -31.4 - - - 179.2 - 38.5 - * * 59 PHE 59 H A - 180.6 - - - -71.2 -37.6 - - - 178.9 - 33.5 - 60 PHE 60 H A - 186.6 - - - -69.7 -33.7 - - - 175.5 -1.3 34.2 - 61 ALA 61 H A - - - - - -70.6 -32.0 - - - 177.9 -2.2 34.3 - 62 ASP 62 H A - 184.9 - - - -67.6 -44.6 - - - 174.8 -1.6 35.6 - 63 LEU 63 H A - - -65.8 181.1 - -54.9 -42.7 - - - 180.0 -2.4 36.3 - 64 ALA 64 H A - - - - - -61.9 -35.4 - - - 176.7 -1.7 33.2 - 65 LYS 65 H A 70.2 - - 175.4 - -81.0 -21.8 - - - 179.3 -1.2 28.6 - * +* * +* +* 66 LYS 66 H A - 178.6 - 184.3 - -77.7 -40.8 - - - 183.4 -1.6 34.0 - * * 67 LEU 67 h b - - -68.0 171.2 - - - - - - 174.0 -2.8 32.7 - * * * 68 PRO 68 S - - - - - -79.8 - - - - - 179.9 - 39.4 - * +* +* 69 ASN 69 e A - 181.2 - - - - - - - - 182.4 - 35.8 - 70 VAL 70 E B - 180.7 - - - - - - - - 178.4 - 34.2 - 71 LEU 71 E B - 181.8 - - - - - - - - 181.6 -3.5 34.4 - +* +* 72 PHE 72 E B - - -57.4 - - - - - - - 180.9 -.6 34.8 - +* +* 73 LEU 73 E B - - -73.6 - - - - - - - 176.2 -2.7 33.3 - 74 LYS 74 E B - 194.7 - 185.9 - - - - - - 175.9 -2.5 36.0 - 75 VAL 75 E B - 179.4 - - - - - - - - 178.2 -3.2 34.5 - +* +* 76 ASP 76 e B - 184.9 - - - - - - - - 184.7 -.6 33.8 - +* +* 77 THR 77 T A 51.9 - - - - - - - - - 178.7 -.8 32.8 - +* +* 78 ASP 78 T A - 189.6 - - - - - - - - 174.6 - 34.8 - 79 GLU 79 T a - - -67.5 - - - - - - - 181.9 - 36.4 - 80 LEU 80 h b - - -67.8 - - - - - - - 181.0 -3.3 33.7 - +* +* 81 LYS 81 H A - - -61.1 176.6 - -68.9 -36.6 - - - 178.4 -1.3 34.0 - 82 SER 82 H A - - -54.5 - - -64.4 -34.2 - - - 177.4 - 33.9 - 83 VAL 83 H A - 178.9 - - - -71.9 -43.6 - - - 178.0 - 34.0 - 84 ALA 84 H A - - - - - -56.9 -47.2 - - - 180.0 -2.3 34.1 - 85 SER 85 H A - 181.1 - - - -66.9 -39.7 - - - 181.2 -3.0 34.1 - * * 86 ASP 86 H A - 177.3 - - - -66.6 -36.3 - - - 178.1 -2.0 33.6 - 87 TRP 87 h A - - -68.3 - - - - - - - 178.5 -2.5 32.0 - 88 ALA 88 T L - - - - - - - - - - 179.9 -.6 33.5 - +* +* 89 ILE 89 t B - - -57.1 - - - - - - - 184.6 -2.5 33.6 - 90 GLN 90 A - 185.6 - 184.3 - - - - - - 183.1 -.8 35.4 - +* +* 91 ALA 91 S B - - - - - - - - - - 179.7 - 33.7 - 92 MET 92 S B - - -58.1 178.1 - - - - - - -1.0 - 35.7 - 93 PRO 93 e cis - - - - - -94.6 - - - - - 172.9 - 40.2 - +** * +* +** Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 THR 94 E B - - -57.0 - - - - - - - 179.1 -1.8 34.6 - 95 PHE 95 E B - - -60.7 - - - - - - - 179.1 -3.0 36.0 - * * 96 MET 96 E B - 181.3 - 177.3 - - - - - - 181.7 -3.3 32.9 - +* +* 97 PHE 97 E B - - -68.8 - - - - - - - 180.0 -3.5 36.5 - +* +* 98 LEU 98 E B - - -54.1 - - - - - - - 176.7 -3.0 35.0 - * * 99 LYS 99 E B - 175.5 - 173.2 - - - - - - 179.1 -3.2 33.5 - +* +* 100 GLU 100 T l - - -55.2 173.6 - - - - - - 181.0 - 34.3 - 101 GLY 101 T - - - - - - - - - - - 178.2 - - - 102 LYS 102 E B - 184.7 - 185.5 - - - - - - 182.0 -2.0 36.5 - 103 ILE 103 E B - - -60.4 175.0 - - - - - - 176.5 - 34.2 - 104 LEU 104 E a - - -68.8 186.1 - - - - - - 184.4 -1.8 32.8 - 105 ASP 105 E B 58.6 - - - - - - - - - 183.0 -2.3 32.0 - 106 LYS 106 E B 46.8 - - - - - - - - - 180.0 - 30.7 - * * 107 VAL 107 E B - 181.9 - - - - - - - - 178.6 -3.3 35.8 - +* +* 108 VAL 108 E B 62.8 - - - - - - - - - 178.9 - 32.9 - 109 GLY 109 e - - - - - - - - - - - 179.6 -2.6 - - 110 ALA 110 B - - - - - - - - - - 179.2 - 33.9 - 111 LYS 111 h B - - -65.3 182.8 - - - - - - 187.3 -1.0 34.3 - * * * 112 LYS 112 H A - 182.2 - - - -60.6 -52.2 - - - 181.3 -.5 35.1 - * ** ** 113 ASP 113 H A 66.5 - - - - -73.9 -29.0 - - - 180.1 - 31.1 - 114 GLU 114 H A - - -77.8 - - -77.1 -35.6 - - - 179.3 - 31.9 - 115 LEU 115 H A - 185.2 - - - -63.3 -53.7 - - - 178.7 -2.6 34.7 - * * 116 GLN 116 H A 55.9 - - 178.3 - -61.8 -29.9 - - - 176.3 -1.5 32.0 - 117 SER 117 H A - 180.9 - - - -65.7 -45.6 - - - 180.0 -1.1 34.7 - * * 118 THR 118 H A - - -52.4 - - -67.7 -29.4 - - - 176.0 -2.6 33.8 - 119 ILE 119 H A - - -58.4 175.1 - -70.8 -44.4 - - - 178.3 -1.9 33.5 - 120 ALA 120 H A - - - - - -65.1 -32.3 - - - 175.7 -2.7 33.9 - 121 LYS 121 H A - 184.6 - 180.2 - -57.9 -44.7 - - - 179.9 -2.3 37.8 - * * 122 HIS 122 H A - - -73.3 - - -89.3 -8.8 - - - 179.7 -1.5 33.8 - ** +** +** 123 LEU 123 h B - 197.3 - 172.1 - - - - - - 180.5 -.9 35.0 - * * 124 ALA 124 - - - - - - - - - - - - -.8 34.1 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * ** +** ** +** +** +* ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.7 182.6 -62.7 178.9 -72.6 -67.0 -38.0 54.8 - 2.0 179.5 -2.0 34.2 +** +** Standard deviations: 6.2 5.0 7.7 9.2 17.9 7.8 11.1 .0 - .0 3.1 .9 1.7 Numbers of values: 17 44 41 30 4 47 47 2 0 2 122 83 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_4 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_4 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 - 1.236 1.508 1.547 1.466 - 116.73 120.29 108.21 108.93 112.20 122.98 2 GLY 2 1.311 1.229 1.498 - 1.432 120.58 115.74 120.39 - 112.02 - 123.86 * * * 3 HIS 3 1.326 1.234 1.511 1.548 1.469 123.66 116.18 121.18 110.61 110.76 113.51 122.59 * +* +* 4 HIS 4 1.297 1.230 1.520 1.551 1.443 121.04 114.66 122.03 112.91 112.18 112.61 123.26 ** * * * ** 5 HIS 5 1.299 1.224 1.516 1.572 1.440 123.41 116.62 121.21 112.03 107.61 112.07 122.03 ** ** * * ** 6 HIS 6 1.292 1.240 1.496 1.550 1.446 120.55 116.48 119.96 108.38 110.22 111.98 123.54 +** * +** 7 HIS 7 1.318 1.230 1.517 1.537 1.447 121.52 116.19 120.92 110.58 105.72 110.87 122.85 +* +* 8 HIS 8 1.291 1.234 1.501 1.554 1.433 121.03 115.43 120.91 110.37 112.86 109.88 123.66 +** * * * +** 9 LEU 9 1.316 1.236 1.500 1.556 1.437 121.83 115.75 121.04 109.94 105.65 113.11 123.10 * * * +* +* +* 10 GLU 10 1.294 1.235 1.491 1.522 1.420 120.94 115.89 120.76 111.67 110.51 109.79 123.31 ** +* ** ** 11 MET 11 1.312 1.231 1.513 1.538 1.433 121.04 114.28 121.57 111.48 108.90 112.34 123.80 * * * * Residue-by-residue listing for refined_4 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 1.296 1.233 1.497 1.533 1.426 124.42 114.97 121.27 110.98 107.70 112.30 123.47 ** * +* +* * * ** 13 SER 13 1.296 1.247 1.507 1.532 1.424 122.49 116.78 120.54 112.27 109.65 109.42 122.66 ** +* * ** 14 GLU 14 1.308 1.238 1.521 1.514 1.422 120.14 112.14 122.70 114.24 111.42 111.95 124.83 +* +* ** * ** * ** 15 GLU 15 1.298 1.236 1.502 1.566 1.430 127.85 118.47 118.70 113.39 105.66 112.70 122.73 ** * +* * *** * * +* +* * *** 16 GLY 16 1.309 1.233 1.510 - 1.453 119.32 115.13 121.19 - 112.02 - 123.68 * * 17 GLN 17 1.306 1.233 1.490 1.529 1.429 123.59 115.63 120.61 108.85 108.59 110.86 123.74 +* +* +* * +* 18 VAL 18 1.280 1.237 1.515 1.556 1.437 121.96 117.69 119.79 110.00 107.89 111.21 122.50 *** * * *** 19 ILE 19 1.316 1.225 1.515 1.544 1.428 119.89 116.36 121.15 110.07 110.18 111.18 122.49 +* * +* 20 ALA 20 1.292 1.233 1.505 1.518 1.425 121.09 116.74 120.45 110.74 109.11 110.72 122.79 +** +* +** 21 CYS 21 1.304 1.232 1.508 1.513 1.422 121.16 116.54 120.55 110.03 108.83 109.82 122.89 +* +* +* 22 HIS 22 1.308 1.233 1.508 1.540 1.448 121.06 115.88 120.90 110.04 110.32 111.93 123.22 * * 23 THR 23 1.321 1.247 1.518 1.557 1.445 122.10 116.39 120.44 107.34 109.34 111.81 123.16 24 VAL 24 1.322 1.234 1.542 1.561 1.459 121.46 114.91 121.86 110.63 109.02 111.57 123.20 25 GLU 25 1.321 1.242 1.521 1.513 1.441 123.23 115.83 120.82 110.83 109.97 108.88 123.35 26 THR 26 1.325 1.212 1.531 1.542 1.443 121.70 116.54 120.38 111.31 110.46 111.23 123.04 * * 27 TRP 27 1.330 1.237 1.537 1.539 1.459 122.05 116.29 120.62 111.69 110.87 109.90 123.07 28 ASN 28 1.328 1.232 1.527 1.531 1.467 121.78 115.29 121.42 108.98 110.14 110.50 123.28 29 GLU 29 1.318 1.229 1.538 1.534 1.456 123.14 116.62 120.38 111.89 111.66 109.45 122.98 30 GLN 30 1.319 1.227 1.511 1.492 1.422 122.85 116.79 120.53 110.59 111.92 109.17 122.68 +* +* +* 31 LEU 31 1.318 1.219 1.501 1.486 1.409 121.63 116.47 120.21 110.30 110.95 110.04 123.31 * ** +** +** 32 GLN 32 1.315 1.218 1.519 1.529 1.441 121.64 116.29 120.34 111.32 109.74 111.28 123.35 33 LYS 33 1.324 1.232 1.535 1.533 1.449 122.04 116.82 120.43 110.03 110.53 110.24 122.72 34 ALA 34 1.337 1.229 1.520 1.520 1.456 121.15 115.71 120.94 110.70 110.94 110.67 123.34 35 ASN 35 1.316 1.237 1.494 1.522 1.454 122.91 114.25 121.43 108.06 109.83 109.47 124.30 * * * 36 GLU 36 1.309 1.237 1.539 1.532 1.453 122.81 116.73 120.90 110.02 111.58 109.95 122.34 * * 37 SER 37 1.312 1.237 1.532 1.521 1.438 121.27 117.26 119.80 110.59 113.00 109.77 122.95 * * * 38 LYS 38 1.349 1.242 1.505 1.513 1.467 121.83 114.41 121.96 113.17 112.06 111.29 123.56 * +* +* 39 THR 39 1.297 1.240 1.519 1.528 1.408 122.21 116.86 120.83 108.10 106.26 110.57 122.29 ** +** +* +** 40 LEU 40 1.268 1.227 1.520 1.520 1.394 121.68 116.96 120.29 110.90 108.60 110.14 122.74 **** *** **** 41 VAL 41 1.303 1.228 1.534 1.567 1.437 121.01 116.16 120.84 111.86 111.58 110.86 122.95 +* * * * +* 42 VAL 42 1.309 1.237 1.513 1.542 1.445 122.68 116.73 120.61 109.72 108.05 112.48 122.65 * * * 43 VAL 43 1.302 1.231 1.521 1.549 1.440 120.88 115.19 120.90 109.13 111.71 111.39 123.90 +* +* Residue-by-residue listing for refined_4 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 1.302 1.235 1.519 1.537 1.449 124.14 117.52 120.22 108.91 109.10 109.50 122.22 +* * +* 45 PHE 45 1.304 1.244 1.517 1.522 1.424 120.42 116.22 120.15 109.24 108.16 109.51 123.63 +* +* * +* 46 THR 46 1.322 1.211 1.530 1.535 1.448 122.57 117.21 120.25 106.63 110.60 110.01 122.54 * * * 47 ALA 47 1.300 1.238 1.522 1.518 1.440 121.96 116.76 119.94 110.35 106.75 110.85 123.30 ** +* ** 48 SER 48 1.315 1.229 1.552 1.530 1.474 123.79 117.79 120.01 110.57 114.80 109.63 122.18 * * * * * 49 TRP 49 1.324 1.237 1.540 1.546 1.458 121.58 117.50 120.35 111.41 113.65 111.45 122.10 50 CYS 50 1.316 1.233 1.530 1.536 1.459 120.62 115.49 120.86 110.45 110.83 110.45 123.65 51 GLY 51 1.332 1.236 1.526 - 1.461 122.97 119.25 119.49 - 114.41 - 121.25 * * * * 52 PRO 52 1.362 1.232 1.528 1.543 1.481 122.53 115.23 121.72 110.57 111.37 103.88 123.03 * * * 53 CYS 53 1.307 1.223 1.528 1.503 1.442 122.71 116.19 121.31 109.24 110.00 108.77 122.50 +* * * +* 54 ARG 54 1.312 1.209 1.524 1.533 1.447 121.59 116.30 120.70 111.37 109.90 111.15 122.99 * * * 55 PHE 55 1.325 1.235 1.535 1.545 1.464 122.07 116.24 121.07 109.95 110.81 110.43 122.67 56 ILE 56 1.319 1.240 1.555 1.576 1.455 121.26 115.48 121.41 110.79 110.17 110.48 123.06 * * * 57 ALA 57 1.328 1.231 1.557 1.522 1.467 123.40 120.44 119.00 111.08 114.74 111.11 120.55 +* ** * * +* ** 58 PRO 58 1.381 1.229 1.521 1.529 1.473 122.04 116.51 120.63 110.21 112.34 103.75 122.85 +** +** 59 PHE 59 1.322 1.214 1.526 1.534 1.446 121.17 116.11 121.00 111.16 109.84 110.97 122.86 60 PHE 60 1.315 1.228 1.537 1.542 1.460 122.49 115.87 121.32 112.10 109.27 109.13 122.80 * * 61 ALA 61 1.322 1.234 1.536 1.519 1.458 121.94 115.49 121.48 110.48 109.78 110.12 123.03 62 ASP 62 1.322 1.234 1.499 1.512 1.462 122.79 114.24 121.56 108.99 108.88 110.02 124.20 * * 63 LEU 63 1.317 1.235 1.515 1.524 1.435 123.96 115.30 121.05 109.21 110.00 108.70 123.63 * * * * 64 ALA 64 1.316 1.235 1.527 1.514 1.436 122.70 117.95 120.21 111.01 112.21 110.56 121.81 * * 65 LYS 65 1.335 1.240 1.515 1.540 1.448 118.45 116.73 120.55 111.97 112.19 115.69 122.72 +* *** *** 66 LYS 66 1.327 1.226 1.515 1.534 1.444 120.44 116.90 120.51 109.04 110.80 112.01 122.59 67 LEU 67 1.308 1.217 1.512 1.510 1.418 120.90 116.67 121.21 111.31 113.79 110.42 122.11 +* ** ** 68 PRO 68 1.336 1.229 1.535 1.530 1.464 122.69 114.69 121.71 110.20 109.85 102.78 123.60 * * * 69 ASN 69 1.327 1.225 1.513 1.533 1.456 123.70 115.57 121.36 109.30 110.12 109.26 123.07 * * 70 VAL 70 1.306 1.228 1.516 1.558 1.434 122.16 116.34 120.81 110.24 109.34 111.42 122.77 +* * +* 71 LEU 71 1.291 1.228 1.527 1.534 1.430 121.78 116.78 120.56 111.43 108.84 109.71 122.64 +** * +** 72 PHE 72 1.313 1.242 1.505 1.518 1.452 121.41 115.49 121.09 108.46 110.11 111.53 123.42 * * 73 LEU 73 1.291 1.227 1.493 1.538 1.437 122.60 114.80 121.20 108.20 112.01 113.56 124.01 +** +* * +* +** Residue-by-residue listing for refined_4 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 LYS 74 1.301 1.235 1.498 1.498 1.413 123.16 116.52 120.69 107.88 108.01 110.97 122.75 +* * +* ** * * ** 75 VAL 75 1.281 1.232 1.493 1.553 1.426 121.27 116.33 120.16 109.46 107.71 112.36 123.48 *** +* +* * *** 76 ASP 76 1.307 1.233 1.506 1.516 1.435 120.65 115.91 120.76 110.92 107.83 111.36 123.29 +* * * +* 77 THR 77 1.299 1.232 1.531 1.539 1.437 122.68 116.86 120.50 111.50 113.24 110.38 122.64 ** * * ** 78 ASP 78 1.319 1.233 1.517 1.524 1.456 121.52 114.42 121.92 110.29 107.94 110.23 123.66 * * 79 GLU 79 1.311 1.241 1.526 1.513 1.422 123.71 115.97 121.17 109.28 110.16 108.41 122.85 * +* * * +* 80 LEU 80 1.320 1.237 1.519 1.531 1.406 122.64 115.25 121.40 110.53 110.91 111.08 123.32 +** +** 81 LYS 81 1.303 1.231 1.513 1.516 1.450 122.95 116.15 120.79 110.77 111.14 110.03 123.05 +* +* 82 SER 82 1.321 1.224 1.532 1.517 1.440 121.54 115.95 121.11 111.38 110.16 109.81 122.90 83 VAL 83 1.326 1.227 1.527 1.557 1.450 121.63 115.82 120.98 110.62 108.82 111.33 123.16 84 ALA 84 1.327 1.232 1.527 1.521 1.459 122.49 116.29 120.59 110.17 110.96 110.45 123.09 85 SER 85 1.326 1.236 1.538 1.541 1.448 122.13 116.38 120.85 110.94 110.95 109.93 122.76 86 ASP 86 1.324 1.236 1.526 1.526 1.465 122.13 116.58 121.05 110.98 112.04 109.95 122.36 87 TRP 87 1.313 1.241 1.521 1.521 1.447 121.55 115.92 120.43 111.34 112.50 111.74 123.65 * * 88 ALA 88 1.341 1.237 1.523 1.531 1.472 123.82 116.12 120.80 110.81 111.29 110.65 123.02 * * 89 ILE 89 1.325 1.237 1.521 1.555 1.449 121.61 115.35 121.31 110.24 108.85 112.18 123.30 90 GLN 90 1.303 1.228 1.522 1.532 1.437 121.90 116.54 120.95 110.02 110.56 109.10 122.50 +* * +* 91 ALA 91 1.313 1.230 1.517 1.520 1.441 120.74 116.12 120.87 111.13 111.15 110.09 123.00 * * 92 MET 92 1.307 1.231 1.522 1.528 1.449 122.09 118.99 120.01 108.78 109.07 110.22 121.01 +* * * +* 93 PRO 93 1.325 1.240 1.527 1.535 1.446 123.88 116.77 121.01 109.50 111.65 102.40 122.18 * * 94 THR 94 1.290 1.233 1.517 1.532 1.424 120.13 116.94 120.07 109.63 108.17 111.42 122.99 +** +* * +** 95 PHE 95 1.312 1.224 1.498 1.531 1.414 121.80 116.93 120.44 108.88 107.91 110.40 122.63 * * ** * ** 96 MET 96 1.283 1.230 1.500 1.532 1.428 120.75 115.10 121.09 111.95 109.51 111.33 123.79 *** * +* *** 97 PHE 97 1.289 1.245 1.507 1.523 1.404 124.27 116.07 121.29 109.95 109.43 108.16 122.63 +** +** * * +** 98 LEU 98 1.289 1.234 1.522 1.561 1.420 121.10 116.31 121.01 107.78 108.37 112.96 122.67 +** +* +* * * * +** 99 LYS 99 1.288 1.226 1.484 1.520 1.428 122.13 115.12 120.61 111.13 109.26 111.32 124.21 +** +* +* +** 100 GLU 100 1.319 1.227 1.535 1.522 1.462 124.30 116.47 120.88 109.29 110.67 111.09 122.66 * * 101 GLY 101 1.320 1.225 1.520 - 1.451 120.77 116.34 120.65 - 112.30 - 123.01 102 LYS 102 1.317 1.232 1.525 1.529 1.449 122.59 117.19 119.91 109.52 107.95 108.54 122.90 * * * 103 ILE 103 1.318 1.237 1.516 1.561 1.462 122.15 116.23 120.72 109.09 110.93 111.81 123.04 104 LEU 104 1.312 1.241 1.504 1.531 1.421 121.18 116.70 120.48 110.82 110.75 112.08 122.79 * * +* +* Residue-by-residue listing for refined_4 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 1.310 1.213 1.500 1.521 1.443 120.85 115.65 121.07 110.96 112.92 112.03 123.27 * * * 106 LYS 106 1.309 1.239 1.540 1.564 1.448 122.61 115.26 121.28 113.44 113.41 111.18 123.44 * +* +* +* 107 VAL 107 1.314 1.237 1.523 1.561 1.455 123.78 117.12 120.09 108.14 108.85 111.15 122.78 * * * 108 VAL 108 1.311 1.247 1.533 1.561 1.445 120.99 116.03 121.01 110.63 110.52 112.23 122.92 * * 109 GLY 109 1.317 1.240 1.500 - 1.434 121.22 117.18 120.60 - 110.88 - 122.23 * * 110 ALA 110 1.306 1.230 1.510 1.524 1.427 119.18 115.40 121.33 111.01 109.00 110.80 123.27 +* +* * +* 111 LYS 111 1.301 1.234 1.505 1.518 1.420 123.18 116.02 120.40 111.60 108.66 109.80 123.57 +* ** ** 112 LYS 112 1.313 1.230 1.541 1.519 1.434 123.00 117.44 120.17 110.87 113.14 107.77 122.37 * * +* +* 113 ASP 113 1.326 1.231 1.528 1.542 1.477 120.97 116.43 120.92 111.34 112.22 112.96 122.65 * * * 114 GLU 114 1.317 1.237 1.511 1.513 1.461 121.92 117.48 119.91 110.92 113.58 111.75 122.61 115 LEU 115 1.323 1.225 1.500 1.521 1.453 120.36 115.11 121.10 109.31 108.96 111.23 123.72 * * 116 GLN 116 1.315 1.237 1.533 1.527 1.461 122.05 116.57 120.38 111.51 112.02 111.57 123.04 * * 117 SER 117 1.335 1.224 1.524 1.542 1.452 121.92 115.90 121.10 110.27 109.22 110.36 122.94 118 THR 118 1.318 1.234 1.543 1.538 1.443 122.26 116.26 121.38 111.23 110.15 110.27 122.36 119 ILE 119 1.315 1.212 1.527 1.537 1.444 121.00 116.87 120.20 110.27 109.83 111.87 122.89 * * 120 ALA 120 1.337 1.232 1.522 1.518 1.475 121.87 114.47 121.44 110.63 109.97 110.41 124.08 121 LYS 121 1.309 1.223 1.526 1.502 1.449 124.77 115.52 121.41 109.31 109.65 106.05 123.05 * * +* +** +** 122 HIS 122 1.317 1.232 1.528 1.524 1.447 122.65 117.25 119.97 109.63 112.90 110.90 122.76 123 LEU 123 1.323 1.237 1.519 1.527 1.427 121.90 115.93 120.93 111.76 108.39 108.70 123.09 +* * * +* 124 ALA 124 1.299 - 1.506 1.524 1.430 122.14 - - 111.05 109.23 110.44 - ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** *** *** ** * ** +* *** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 1.268 1.349 1.312 .014 **** * * C-N (Pro) 1.341 .016 4 1.325 1.381 1.351 .022 +** C-O C-O 1.231 .020 123 1.209 1.247 1.232 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.484 1.557 1.519 .014 +* +* CH2G*-C (Gly) 1.516 .018 5 1.498 1.526 1.511 .011 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.514 1.533 1.522 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.528 1.576 1.550 .012 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.572 1.529 .015 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.394 1.477 1.442 .017 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.432 1.461 1.446 .011 * N-CH1E (Pro) 1.466 .015 4 1.446 1.481 1.466 .013 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_4 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 2.0 114 112.14 120.44 116.20 1.02 ** ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.13 119.25 116.73 1.43 * CH1E-C-N (Pro) 116.9 1.5 4 114.69 116.77 115.80 .87 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.55 124.83 122.99 .61 +* * O-C-N (Pro) 122.0 1.4 4 122.18 123.60 122.92 .51 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.45 127.85 122.03 1.25 +* *** C-NH1-CH2G* (Gly) 120.6 1.7 5 119.32 122.97 120.97 1.18 * C-N-CH1E (Pro) 122.6 5.0 4 122.04 123.88 122.78 .68 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.70 122.70 120.79 .59 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.49 121.19 120.46 .55 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.17 111.13 110.78 .29 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 106.63 111.86 109.85 1.31 * * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.78 114.24 110.47 1.33 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.65 114.80 110.14 1.84 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.88 114.41 112.32 1.15 N-CH1E-C (Pro) 111.8 2.5 4 109.85 112.34 111.30 .91 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.09 112.30 110.70 .53 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 110.01 112.48 111.33 .68 N-CH1E-CH2E (Pro) 103.0 1.1 4 102.40 103.88 103.20 .63 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.05 115.69 110.63 1.50 +** *** ------------------------------------------------------------------------------------------------------------- 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_4 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 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 83 .9 .8 .2 .3 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 17 6.2 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 44 5.0 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 41 7.7 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 7.2 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 30 9.2 20.4 5.0 -2.2 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 88.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.7 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 2 Residue-by-residue listing for refined_4 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.21 Chi1-chi2 distribution -.05 Chi1 only .13 Chi3 & chi4 .45 Omega .11 ------ .02 ===== Main-chain covalent forces:- Main-chain bond lengths .01 Main-chain bond angles .44 ------ .26 ===== OVERALL AVERAGE .10 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.