Residue-by-residue listing for analyzed_12 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 - - - -91.1 209.3 - - - - - - 180.0 - 35.3 - +* +* +* 2 GLY 2 - - - - - - - - - - - 180.0 - - - 3 HIS 3 b 93.7 - - - - - - - - - 180.0 - 32.4 - +* +* 4 HIS 4 b - - -95.5 - - - - - - - 180.0 - 32.4 - +* +* 5 HIS 5 B 56.2 - - - - - - - - - 180.0 - 32.4 - 6 HIS 6 b - 226.9 - - - - - - - - 179.9 - 32.4 1 +** * +** 7 HIS 7 a - - -89.4 - - - - - - - 180.0 - 32.4 - +* +* 8 HIS 8 ~l - - -105.5 - - - - - - - 180.0 - 32.4 - ** +** +** 9 LEU 9 B - - -99.4 - - - - - - - 180.0 - 32.0 - ** ** 10 GLU 10 b - 202.2 - 160.4 - - - - - - 180.0 - 33.3 - * * 11 MET 11 b - 234.8 - 123.8 - - - - - - 180.0 - 35.3 - *** +** *** 12 ALA 12 b - - - - - - - - - - 179.9 - 33.6 - 13 SER 13 b - - -96.7 - - - - - - - 180.0 - 33.8 - +* +* 14 GLU 14 a - 192.5 - 156.2 - - - - - - 179.9 - 33.3 1 * * * 15 GLU 15 ~p - - -113.0 - - - - - - - 180.0 - 33.3 - ** *** *** 16 GLY 16 S - - - - - - - - - - - 180.0 - - - Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 17 GLN 17 S B 26.3 - - 148.5 - - - - - - 180.0 - 33.3 - ** +* ** 18 VAL 18 B 71.7 - - - - - - - - - 179.9 - 32.9 - 19 ILE 19 E B - - -55.1 - - - - - - - 179.9 -1.6 32.1 - 20 ALA 20 E B - - - - - - - - - - 180.0 -.7 33.7 - +* +* 21 CYS 21 e B - - -86.1 - - - - - - - 180.0 -.8 32.7 - * +* +* 22 HIS 22 S a - - -70.4 - - - - - - - 180.0 - 32.4 - 23 THR 23 h B 71.3 - - - - - - - - - 180.0 - 33.8 - 24 VAL 24 H A 69.6 - - - - -74.7 -37.6 - - - 180.0 - 32.9 - 25 GLU 25 H A - 227.9 - - - -55.9 -46.5 - - - 180.0 - 33.3 - +** +** 26 THR 26 H A - - -60.7 - - -70.1 -39.5 - - - 180.0 - 33.7 - 27 TRP 27 H A - 164.1 - - - -54.5 -47.8 - - - 180.0 -1.7 32.5 - * * 28 ASN 28 H A - 229.6 - - - -73.7 -35.8 - - - 180.0 -2.9 35.5 - +** * +** 29 GLU 29 H A - 192.6 - 174.5 - -57.4 -46.0 - - - 180.0 -2.4 33.4 - 30 GLN 30 H A - - -111.4 - - -72.3 -33.5 - - - 180.0 -3.6 33.3 - +** ** +** 31 LEU 31 H A - - -110.9 178.1 - -60.8 -49.8 - - - 180.0 -1.5 32.0 - +** +** 32 GLN 32 H A - 208.4 - 181.1 - -55.4 -33.5 - - - 180.0 -3.1 33.3 - * * * 33 LYS 33 H A - 185.7 - 167.1 - -72.4 -40.0 - - - 180.0 -.9 32.0 - * * 34 ALA 34 H A - - - - - -70.6 -28.4 - - - 180.0 -2.3 33.7 - 35 ASN 35 H A - 221.9 - - - -75.3 -51.1 - - - 180.0 -2.6 35.5 - ** * ** 36 GLU 36 H A - 234.6 - 179.5 - -60.1 -39.6 - - - 180.0 -2.9 33.3 - *** * *** 37 SER 37 h A - - -88.9 - - - - - - - 180.1 -2.4 33.8 - * * 38 LYS 38 T l - - -116.8 180.9 - - - - - - 180.0 -.6 32.1 - *** +* *** 39 THR 39 t B - - -23.6 - - - - - - - 180.0 -2.6 33.8 - +** +** 40 LEU 40 e B - 129.4 - - - - - - - - 180.1 - 32.1 1 *** * *** 41 VAL 41 E B 91.5 - - - - - - - - - 180.0 - 32.9 - +* +* 42 VAL 42 E B - 167.0 - - - - - - - - 180.0 -1.9 32.9 - 43 VAL 43 E B - 181.0 - - - - - - - - 180.0 -1.0 32.8 - * * 44 ASP 44 E B - 171.4 - - - - - - - - 180.0 -1.4 35.5 - 45 PHE 45 E B - - -84.1 - - - - - - - 180.0 -2.1 37.4 - * * 46 THR 46 E B - 168.5 - - - - - - - - 180.0 -.8 33.7 - +* +* 47 ALA 47 t B - - - - - - - - - - 180.1 - 33.6 - 48 SER 48 T A - - -104.2 - - - - - - - 180.0 - 33.8 - ** ** 49 TRP 49 T A 46.6 - - - - - - - - - 180.0 - 32.5 - * * 50 CYS 50 t B 90.7 - - 165.1 - - - - -59.6 2.0 180.0 -1.7 32.7 - +* ** ** Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 51 GLY 51 S - - - - - - - - - - - 180.0 - - - 52 PRO 52 g - - - - - -75.0 - - - - - 180.0 - 35.9 - 53 CYS 53 G A 101.9 - - - - - - - -59.6 2.0 180.0 - 32.7 - ** ** ** 54 ARG 54 G A - 187.5 - 195.1 - - - - - - 180.0 - 34.5 - 55 PHE 55 h A - 209.2 - - - - - - - - 180.0 -1.3 37.4 - +* +* 56 ILE 56 H A - 214.4 - - - -96.2 -5.9 - - - 180.0 -2.8 32.1 - +* +** +** * +** 57 ALA 57 H A - - - - - -57.4 -45.8 - - - 179.9 -1.5 33.7 1 * * 58 PRO 58 H - - - - - -75.0 -75.0 -41.5 - - - 180.0 - 35.8 - 59 PHE 59 H A - 208.2 - - - -63.9 -36.3 - - - 180.0 -.6 37.4 - * +* +* 60 PHE 60 H A - 185.2 - - - -72.1 -35.2 - - - 179.9 -3.5 37.4 - ** * ** 61 ALA 61 H A - - - - - -69.7 -35.4 - - - 180.0 -1.3 33.6 - 62 ASP 62 H A - 209.2 - - - -70.0 -42.8 - - - 180.0 -2.1 35.5 - +* +* 63 LEU 63 H A - - -113.6 - - -52.6 -37.5 - - - 180.0 -2.1 32.0 - *** * *** 64 ALA 64 H A - - - - - -71.1 -39.7 - - - 180.0 -1.2 33.6 - * * 65 LYS 65 H A - 223.7 - - - -68.5 -21.1 - - - 180.0 -1.5 32.0 - ** +* ** 66 LYS 66 H A - 208.8 - - - -73.4 -39.2 - - - 180.0 -1.9 32.0 - * * 67 LEU 67 h B - - -105.2 167.2 - - - - - - 180.0 -1.2 32.1 - +** * +** 68 PRO 68 T - - - - - -75.1 - - - - - 180.0 - 35.9 - 69 ASN 69 T A - 235.3 - - - - - - - - 180.0 - 35.5 - *** *** 70 VAL 70 t B - 175.0 - - - - - - - - 180.0 -.5 32.8 - +* +* 71 LEU 71 E B - 223.2 - 131.1 - - - - - - 180.0 -1.5 32.0 - ** +** +** 72 PHE 72 E B - - -37.1 - - - - - - - 179.9 -.5 37.4 - +* ** * ** 73 LEU 73 E B - - -95.0 - - - - - - - 180.1 -2.0 32.1 - +* +* 74 LYS 74 E B - 218.2 - - - - - - - - 180.0 -1.6 32.0 - ** ** 75 VAL 75 E B - 183.3 - - - - - - - - 180.0 -.7 32.9 - +* +* 76 ASP 76 E B - - -119.5 - - - - - - - 180.0 -.5 35.5 - +*** ** +*** 77 THR 77 e A 70.1 - - - - - - - - - 180.0 -.9 33.7 - +* +* 78 ASP 78 T A - 239.8 - - - - - - - - 180.0 - 35.5 - *** *** 79 GLU 79 T a - - -114.8 - - - - - - - 180.0 -1.4 33.3 - *** *** 80 LEU 80 h b - - -111.5 160.7 - - - - - - 180.0 -2.5 32.0 - +** +** 81 LYS 81 H A 60.2 - - 144.4 - -68.1 -29.1 - - - 180.0 -.8 32.0 - +* +* +* Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 82 SER 82 H A - 239.9 - - - -60.3 -40.9 - - - 180.0 - 33.8 - *** *** 83 VAL 83 H A - 174.5 - - - -62.7 -51.5 - - - 180.0 - 32.9 - * * 84 ALA 84 H A - - - - - -54.7 -43.1 - - - 180.0 -1.5 33.7 - 85 SER 85 H A - 221.3 - - - -72.7 -30.8 - - - 180.0 -2.7 33.8 - ** ** 86 ASP 86 H A - 192.7 - - - -67.6 -34.9 - - - 180.0 -2.4 35.5 - 87 TRP 87 h A - - -87.0 - - - - - - - 180.0 -2.6 32.5 - * * 88 ALA 88 T L - - - - - - - - - - 180.0 -1.1 33.7 - * * 89 ILE 89 t b - - -48.8 - - - - - - - 180.0 -3.8 32.0 - * ** ** 90 GLN 90 A - 219.5 - 128.6 - - - - - - 180.0 -1.0 33.3 - ** +** * +** 91 ALA 91 S B - - - - - - - - - - 180.0 - 33.6 - 92 MET 92 S B - - -95.2 175.9 - - - - - - .0 - 35.3 - +* +* 93 PRO 93 e cis - - - - - -75.0 - - - - - 180.0 - 35.9 - 94 THR 94 E B - 226.4 - - - - - - - - 180.0 -.7 33.8 - +** +* +** 95 PHE 95 E B - - -70.9 - - - - - - - 180.0 -3.1 37.4 - * * 96 MET 96 E B - 176.5 - 185.6 - - - - - - 180.0 -2.0 35.3 - 97 PHE 97 E B - - -101.5 - - - - - - - 180.0 -3.4 37.4 - ** +* ** 98 LEU 98 E B 53.6 - - 135.6 - - - - - - 180.0 -1.3 32.0 - ** * ** 99 LYS 99 E B - 171.6 - 173.5 - - - - - - 180.0 -4.0 32.0 - +** +** 100 GLU 100 T l - - -88.4 213.2 - - - - - - 180.0 - 33.4 - * +* +* 101 GLY 101 T - - - - - - - - - - - 180.0 - - - 102 LYS 102 E B - 229.6 - - - - - - - - 180.0 -1.9 32.0 - +** +** 103 ILE 103 E B - - -65.0 174.5 - - - - - - 180.0 - 32.0 - 104 LEU 104 E a - - -95.1 188.6 - - - - - - 180.0 -1.8 32.1 - +* +* 105 ASP 105 E B 26.1 - - - - - - - - - 180.0 -2.9 35.5 - ** * ** 106 LYS 106 E B - 206.9 - - - - - - - - 180.0 - 32.0 - * * 107 VAL 107 E B - 167.5 - - - - - - - - 180.0 -3.3 32.9 - +* +* 108 VAL 108 E B 60.2 - - - - - - - - - 180.0 - 32.9 - 109 GLY 109 e - - - - - - - - - - - 180.0 -4.0 - - +** +** 110 ALA 110 B - - - - - - - - - - 180.0 - 33.7 - 111 LYS 111 h B - - -88.2 220.5 - - - - - - 180.0 -.8 32.1 - * ** +* ** 112 LYS 112 H A - 238.9 - 182.3 - -56.7 -48.8 - - - 180.1 -.5 32.1 - *** ** *** 113 ASP 113 H A - 212.4 - - - -63.4 -47.3 - - - 180.0 - 35.5 - +* +* 114 GLU 114 H A - 204.2 - 202.1 - -62.8 -31.0 - - - 180.0 - 33.3 - * * * Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 115 LEU 115 H A - 217.0 - - - -53.5 -53.6 - - - 180.0 -3.0 32.1 - +* * * +* 116 GLN 116 H A - - -72.2 145.6 - -53.6 -26.4 - - - 180.0 -1.4 33.3 - +* * +* 117 SER 117 H A - - -35.8 - - -65.9 -46.1 - - - 180.0 -.7 33.8 - ** +* ** 118 THR 118 H A - - -46.7 - - -63.1 -35.5 - - - 180.1 -1.5 33.7 - * * 119 ILE 119 H A - - -52.5 - - -67.0 -43.6 - - - 180.0 -1.8 32.1 - 120 ALA 120 H A - - - - - -66.3 -31.9 - - - 180.1 -2.3 33.6 - 121 LYS 121 H A - 229.0 - 157.9 - -59.5 -39.3 - - - 180.0 -2.0 32.1 - +** * +** 122 HIS 122 H A - - -88.1 - - -77.8 -35.8 - - - 180.0 -1.3 32.4 - * * * * 123 LEU 123 h B - - -114.9 - - - - - - - 180.0 -2.1 32.1 - *** *** 124 ALA 124 - - - - - - - - - - - - - 33.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** ** *** +*** +** +** +** ** +** * * +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 66.0 204.0 -86.2 170.2 -75.0 -65.8 -38.5 - -59.6 2.0 180.0 -1.8 33.5 * * ** ** Standard deviations: 22.8 25.7 25.2 24.7 .0 8.7 9.0 - .0 .0 .0 .9 1.5 Numbers of values: 15 47 40 30 4 41 41 0 2 2 122 74 119 4 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 analyzed_12 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 - 1.230 1.531 1.530 1.452 - 114.97 120.49 109.47 111.02 109.53 124.54 2 GLY 2 1.325 1.230 1.531 - 1.453 120.99 114.99 120.51 - 111.00 - 124.50 3 HIS 3 1.325 1.230 1.530 1.530 1.453 120.96 115.00 120.52 112.80 109.57 110.80 124.47 * * 4 HIS 4 1.325 1.230 1.531 1.530 1.453 121.05 114.98 120.51 112.81 109.56 110.83 124.51 * * 5 HIS 5 1.325 1.230 1.530 1.529 1.454 121.00 114.99 120.55 112.82 109.56 110.82 124.46 * * 6 HIS 6 1.326 1.230 1.531 1.531 1.453 121.00 115.00 120.48 112.80 109.58 110.82 124.52 * * 7 HIS 7 1.325 1.230 1.530 1.530 1.453 121.00 115.04 120.46 112.78 109.58 110.76 124.50 * * 8 HIS 8 1.324 1.230 1.530 1.530 1.453 121.04 114.96 120.53 112.77 109.60 110.79 124.51 * * 9 LEU 9 1.325 1.230 1.530 1.530 1.454 120.97 114.96 120.50 113.73 109.27 110.46 124.54 +* +* 10 GLU 10 1.325 1.230 1.529 1.530 1.453 120.99 114.99 120.51 111.04 110.28 110.97 124.50 11 MET 11 1.325 1.230 1.530 1.530 1.453 121.02 114.97 120.54 109.48 111.01 109.53 124.49 12 ALA 12 1.326 1.230 1.530 1.529 1.454 120.98 114.99 120.46 112.42 109.25 109.53 124.54 * * 13 SER 13 1.325 1.230 1.530 1.530 1.453 120.95 115.00 120.50 110.30 109.97 111.11 124.50 14 GLU 14 1.325 1.230 1.530 1.530 1.453 121.01 114.94 120.56 110.98 110.34 111.03 124.50 Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 15 GLU 15 1.326 1.230 1.530 1.530 1.454 120.97 114.99 120.54 111.02 110.26 111.02 124.47 16 GLY 16 1.325 1.230 1.530 - 1.453 121.03 115.02 120.52 - 110.98 - 124.46 17 GLN 17 1.326 1.230 1.530 1.529 1.453 120.99 115.00 120.46 111.03 110.26 111.02 124.53 18 VAL 18 1.324 1.230 1.530 1.530 1.453 121.00 115.01 120.52 113.03 109.29 110.01 124.47 +* +* 19 ILE 19 1.325 1.230 1.530 1.530 1.454 121.00 114.96 120.49 113.73 109.30 110.46 124.56 ** ** 20 ALA 20 1.325 1.230 1.530 1.531 1.453 120.97 114.98 120.52 112.36 109.33 109.50 124.50 * * 21 CYS 21 1.326 1.231 1.530 1.530 1.454 120.95 115.01 120.49 111.89 108.31 111.67 124.50 * * 22 HIS 22 1.325 1.230 1.530 1.530 1.453 120.98 115.01 120.49 112.79 109.58 110.83 124.50 * * 23 THR 23 1.325 1.229 1.530 1.530 1.453 121.01 114.96 120.52 113.41 110.39 107.98 124.52 +* ** ** 24 VAL 24 1.325 1.231 1.529 1.530 1.453 120.97 115.01 120.49 113.02 109.30 109.98 124.50 +* +* 25 GLU 25 1.325 1.230 1.530 1.530 1.453 120.98 115.00 120.55 111.00 110.34 111.00 124.45 26 THR 26 1.325 1.230 1.531 1.529 1.453 121.03 114.98 120.46 113.42 110.36 108.02 124.55 +* ** ** 27 TRP 27 1.325 1.230 1.530 1.530 1.453 120.97 115.00 120.55 113.04 108.00 110.97 124.45 +* * +* 28 ASN 28 1.325 1.230 1.530 1.530 1.453 121.03 115.03 120.47 108.00 109.31 111.12 124.51 * * 29 GLU 29 1.325 1.230 1.530 1.530 1.453 121.00 115.01 120.51 110.97 110.31 110.96 124.48 30 GLN 30 1.326 1.230 1.529 1.530 1.453 121.02 114.99 120.52 111.02 110.31 111.02 124.49 31 LEU 31 1.325 1.230 1.530 1.530 1.453 121.00 114.98 120.49 113.71 109.29 110.50 124.53 +* +* 32 GLN 32 1.325 1.230 1.530 1.530 1.453 120.99 114.98 120.49 111.03 110.28 110.99 124.54 33 LYS 33 1.325 1.230 1.530 1.530 1.453 120.96 114.99 120.52 113.70 109.33 110.49 124.48 +* +* 34 ALA 34 1.325 1.230 1.530 1.530 1.453 120.98 115.03 120.49 112.37 109.31 109.49 124.48 * * 35 ASN 35 1.324 1.230 1.530 1.530 1.453 121.02 115.02 120.46 107.97 109.27 111.09 124.52 * * 36 GLU 36 1.325 1.230 1.531 1.530 1.452 120.99 114.95 120.51 110.97 110.33 111.02 124.54 37 SER 37 1.325 1.230 1.530 1.530 1.453 120.97 115.03 120.52 110.32 109.99 111.10 124.45 38 LYS 38 1.325 1.230 1.530 1.531 1.453 121.03 114.97 120.51 113.69 109.31 110.50 124.53 +* +* 39 THR 39 1.325 1.230 1.530 1.530 1.454 120.95 114.99 120.49 113.38 110.39 108.00 124.52 +* ** ** 40 LEU 40 1.325 1.229 1.530 1.530 1.453 120.99 114.97 120.54 113.66 109.28 110.49 124.49 +* +* 41 VAL 41 1.325 1.231 1.530 1.530 1.453 121.00 115.01 120.47 112.99 109.29 110.04 124.52 +* +* 42 VAL 42 1.325 1.230 1.530 1.530 1.454 121.00 114.96 120.50 113.03 109.27 109.97 124.54 +* +* 43 VAL 43 1.324 1.230 1.529 1.530 1.454 121.00 115.02 120.47 113.03 109.31 110.02 124.50 +* +* 44 ASP 44 1.325 1.230 1.530 1.529 1.453 120.98 115.00 120.56 108.00 109.26 111.11 124.45 * * 45 PHE 45 1.326 1.230 1.531 1.530 1.452 120.99 114.96 120.49 108.97 111.01 107.01 124.54 ** ** 46 THR 46 1.326 1.230 1.530 1.530 1.453 120.94 114.97 120.52 113.39 110.36 108.03 124.51 +* ** ** Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 47 ALA 47 1.325 1.230 1.530 1.530 1.453 120.97 115.01 120.48 112.40 109.30 109.51 124.52 * * 48 SER 48 1.324 1.231 1.530 1.530 1.453 120.99 115.04 120.45 110.27 109.95 111.12 124.51 49 TRP 49 1.325 1.230 1.530 1.530 1.453 121.00 114.98 120.55 113.00 108.01 110.97 124.47 +* * +* 50 CYS 50 1.325 1.230 1.530 1.530 1.454 120.99 114.97 120.56 111.88 108.23 111.70 124.47 * * 51 GLY 51 1.326 1.229 1.531 - 1.453 121.01 114.96 120.52 - 111.02 - 124.52 52 PRO 52 1.360 1.230 1.530 1.520 1.452 120.98 115.03 120.48 113.00 111.00 105.00 124.49 * * +* +* +* +* 53 CYS 53 1.325 1.230 1.530 1.530 1.453 121.03 115.04 120.50 111.91 108.30 111.68 124.46 * * 54 ARG 54 1.325 1.231 1.530 1.530 1.452 121.01 115.00 120.54 109.19 110.31 111.07 124.46 55 PHE 55 1.325 1.230 1.529 1.531 1.454 120.99 115.02 120.50 109.02 111.00 106.97 124.49 ** ** 56 ILE 56 1.326 1.230 1.530 1.530 1.453 121.00 115.00 120.54 113.68 109.33 110.50 124.47 ** ** 57 ALA 57 1.326 1.230 1.530 1.530 1.452 121.01 115.03 120.51 112.36 109.32 109.49 124.46 * * 58 PRO 58 1.360 1.230 1.530 1.520 1.452 121.06 114.98 120.56 112.98 111.05 105.06 124.47 * * +* +* +* +* 59 PHE 59 1.325 1.230 1.530 1.530 1.452 121.02 114.98 120.51 108.98 111.03 107.01 124.51 ** ** 60 PHE 60 1.324 1.230 1.531 1.530 1.453 120.98 115.00 120.50 108.96 111.00 106.98 124.50 ** ** 61 ALA 61 1.324 1.230 1.530 1.530 1.453 121.01 114.99 120.48 112.43 109.32 109.51 124.53 * * 62 ASP 62 1.324 1.230 1.531 1.530 1.453 121.00 115.00 120.50 108.00 109.30 111.13 124.50 * * 63 LEU 63 1.324 1.230 1.530 1.530 1.453 121.02 114.93 120.52 113.68 109.34 110.53 124.55 +* +* 64 ALA 64 1.325 1.229 1.530 1.531 1.453 120.94 114.95 120.53 112.40 109.35 109.51 124.52 * * 65 LYS 65 1.326 1.229 1.531 1.529 1.453 120.99 115.02 120.49 113.70 109.28 110.51 124.49 +* +* 66 LYS 66 1.325 1.230 1.530 1.530 1.452 121.02 115.00 120.55 113.71 109.30 110.54 124.45 +* +* 67 LEU 67 1.325 1.230 1.530 1.530 1.453 121.02 114.99 120.55 113.70 109.30 110.48 124.46 +* +* 68 PRO 68 1.360 1.230 1.530 1.520 1.453 121.00 115.02 120.50 112.94 111.00 104.98 124.47 * * * +* +* +* 69 ASN 69 1.325 1.230 1.530 1.530 1.452 121.00 115.03 120.48 108.00 109.29 111.11 124.48 * * 70 VAL 70 1.324 1.231 1.530 1.530 1.453 121.06 115.02 120.48 113.03 109.26 110.04 124.51 +* +* 71 LEU 71 1.325 1.230 1.530 1.529 1.453 121.02 115.02 120.50 113.71 109.30 110.52 124.49 +* +* 72 PHE 72 1.325 1.229 1.530 1.530 1.453 121.01 114.96 120.53 108.99 110.97 106.99 124.51 ** ** 73 LEU 73 1.325 1.230 1.530 1.531 1.453 121.01 114.98 120.46 113.70 109.36 110.46 124.56 +* +* 74 LYS 74 1.325 1.230 1.530 1.530 1.453 120.96 115.06 120.53 113.67 109.30 110.55 124.41 +* +* 75 VAL 75 1.325 1.230 1.530 1.530 1.452 121.03 115.01 120.49 112.99 109.30 109.99 124.49 +* +* Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 76 ASP 76 1.324 1.230 1.530 1.530 1.453 121.03 115.01 120.48 108.01 109.32 111.10 124.50 * * 77 THR 77 1.324 1.230 1.530 1.529 1.453 121.05 115.01 120.51 113.43 110.37 108.05 124.48 +* ** ** 78 ASP 78 1.325 1.230 1.529 1.530 1.453 121.03 115.05 120.54 108.01 109.28 111.10 124.40 * * 79 GLU 79 1.326 1.230 1.530 1.530 1.453 121.04 115.02 120.47 111.01 110.28 111.00 124.51 80 LEU 80 1.324 1.230 1.530 1.531 1.453 121.05 114.98 120.55 113.69 109.33 110.53 124.47 +* +* 81 LYS 81 1.325 1.230 1.530 1.530 1.453 121.03 115.02 120.49 113.72 109.28 110.55 124.49 +* +* 82 SER 82 1.325 1.231 1.530 1.530 1.453 121.02 115.05 120.46 110.27 109.98 111.10 124.49 83 VAL 83 1.325 1.230 1.529 1.530 1.454 121.01 115.04 120.49 113.02 109.29 109.98 124.47 +* +* 84 ALA 84 1.325 1.230 1.530 1.531 1.453 121.01 114.96 120.48 112.38 109.32 109.51 124.57 * * 85 SER 85 1.325 1.230 1.530 1.531 1.453 120.95 115.01 120.47 110.30 110.01 111.09 124.52 86 ASP 86 1.325 1.231 1.529 1.530 1.454 120.99 115.03 120.51 108.01 109.31 111.07 124.46 * * 87 TRP 87 1.325 1.230 1.530 1.531 1.453 121.02 115.02 120.48 113.00 108.01 111.01 124.51 +* * +* 88 ALA 88 1.325 1.230 1.530 1.530 1.452 121.01 114.98 120.51 112.39 109.34 109.51 124.51 * * 89 ILE 89 1.325 1.230 1.530 1.530 1.453 121.00 114.95 120.50 113.70 109.30 110.49 124.55 ** ** 90 GLN 90 1.326 1.230 1.530 1.530 1.454 120.96 115.02 120.48 111.06 110.30 110.97 124.50 91 ALA 91 1.325 1.230 1.530 1.529 1.453 121.03 114.98 120.50 112.41 109.29 109.50 124.52 * * 92 MET 92 1.325 1.230 1.530 1.530 1.453 121.02 115.00 120.51 109.49 111.03 109.53 124.49 93 PRO 93 1.360 1.230 1.531 1.521 1.452 121.00 115.01 120.46 112.98 111.04 105.01 124.53 * * +* +* +* +* 94 THR 94 1.325 1.230 1.530 1.530 1.453 120.97 114.99 120.54 113.39 110.36 107.99 124.47 +* ** ** 95 PHE 95 1.325 1.231 1.531 1.530 1.453 121.02 115.00 120.48 109.01 111.02 107.01 124.51 ** ** 96 MET 96 1.324 1.230 1.531 1.530 1.452 121.00 114.97 120.44 109.47 111.04 109.52 124.59 97 PHE 97 1.325 1.230 1.530 1.530 1.453 120.96 115.00 120.50 108.99 111.03 107.02 124.50 ** ** 98 LEU 98 1.325 1.229 1.530 1.530 1.453 121.01 114.99 120.53 113.76 109.28 110.49 124.48 +* +* 99 LYS 99 1.326 1.230 1.530 1.530 1.452 121.00 114.97 120.46 113.70 109.30 110.50 124.56 +* +* 100 GLU 100 1.325 1.230 1.530 1.530 1.454 120.99 115.04 120.48 111.01 110.27 110.97 124.48 101 GLY 101 1.325 1.230 1.530 - 1.452 121.04 114.99 120.51 - 111.02 - 124.51 102 LYS 102 1.325 1.230 1.530 1.530 1.453 121.02 115.02 120.49 113.71 109.30 110.52 124.50 +* +* 103 ILE 103 1.325 1.230 1.530 1.530 1.453 121.01 115.00 120.47 113.70 109.29 110.52 124.52 ** ** 104 LEU 104 1.325 1.231 1.530 1.530 1.452 120.97 115.00 120.49 113.67 109.30 110.51 124.51 +* +* 105 ASP 105 1.325 1.230 1.530 1.530 1.453 121.00 115.00 120.50 108.05 109.30 111.08 124.50 * * 106 LYS 106 1.326 1.230 1.530 1.529 1.453 120.98 115.01 120.50 113.75 109.27 110.48 124.49 +* +* Residue-by-residue listing for analyzed_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 107 VAL 107 1.325 1.231 1.529 1.530 1.453 121.04 115.05 120.46 113.01 109.37 110.00 124.49 +* +* 108 VAL 108 1.325 1.230 1.531 1.530 1.453 120.97 114.99 120.47 112.96 109.29 109.99 124.54 +* +* 109 GLY 109 1.325 1.230 1.530 - 1.453 121.00 114.98 120.52 - 110.98 - 124.50 110 ALA 110 1.325 1.230 1.530 1.530 1.452 121.01 114.99 120.51 112.40 109.33 109.48 124.50 * * 111 LYS 111 1.325 1.230 1.530 1.530 1.453 120.99 114.96 120.53 113.69 109.27 110.48 124.51 +* +* 112 LYS 112 1.325 1.230 1.530 1.530 1.453 120.95 115.00 120.48 113.70 109.30 110.46 124.51 +* +* 113 ASP 113 1.325 1.230 1.530 1.530 1.453 121.02 114.96 120.50 108.01 109.26 111.12 124.55 * * 114 GLU 114 1.325 1.231 1.530 1.530 1.453 120.97 115.04 120.49 111.02 110.30 110.97 124.48 115 LEU 115 1.324 1.230 1.530 1.530 1.453 121.02 115.01 120.52 113.66 109.32 110.51 124.47 +* +* 116 GLN 116 1.326 1.230 1.530 1.531 1.453 120.99 115.00 120.51 111.03 110.30 110.97 124.49 117 SER 117 1.325 1.230 1.530 1.530 1.452 121.01 114.93 120.55 110.30 110.05 111.13 124.52 118 THR 118 1.325 1.230 1.529 1.530 1.454 120.95 115.02 120.47 113.41 110.39 107.99 124.51 +* ** ** 119 ILE 119 1.325 1.231 1.531 1.531 1.453 120.98 115.03 120.43 113.69 109.24 110.47 124.54 ** ** 120 ALA 120 1.324 1.230 1.530 1.530 1.453 121.03 114.94 120.57 112.43 109.32 109.55 124.49 * * 121 LYS 121 1.326 1.230 1.530 1.529 1.453 120.97 115.06 120.48 113.69 109.25 110.50 124.46 +* +* 122 HIS 122 1.325 1.230 1.530 1.530 1.452 121.05 114.98 120.52 112.80 109.61 110.83 124.50 * * 123 LEU 123 1.325 1.230 1.531 1.530 1.453 121.00 115.03 120.49 113.67 109.31 110.52 124.48 +* +* 124 ALA 124 1.325 - 1.530 1.530 1.453 121.02 - - 112.39 109.28 109.50 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * ** * ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for analyzed_12 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 1.324 1.326 1.325 .000 C-N (Pro) 1.341 .016 4 1.360 1.360 1.360 .000 * * * C-O C-O 1.231 .020 123 1.229 1.231 1.230 .000 CA-C CH1E-C (except Gly) 1.525 .021 119 1.529 1.531 1.530 .000 CH2G*-C (Gly) 1.516 .018 5 1.530 1.531 1.530 .000 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.529 1.531 1.530 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.529 1.531 1.530 .000 CH1E-CH2E (the rest) 1.530 .020 84 1.520 1.531 1.529 .002 N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.452 1.454 1.453 .000 NH1-CH2G* (Gly) 1.451 .016 5 1.452 1.453 1.453 .000 N-CH1E (Pro) 1.466 .015 4 1.452 1.453 1.453 .000 ------------------------------------------------------------------------------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 114 114.93 115.06 115.00 .03 CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.96 115.02 114.99 .02 CH1E-C-N (Pro) 116.9 1.5 4 114.98 115.03 115.01 .02 * * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 124.40 124.59 124.50 .03 O-C-N (Pro) 122.0 1.4 4 124.47 124.53 124.49 .03 +* +* +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 120.94 121.06 121.00 .03 C-NH1-CH2G* (Gly) 120.6 1.7 5 120.99 121.04 121.01 .02 C-N-CH1E (Pro) 122.6 5.0 4 120.98 121.06 121.01 .03 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 120.43 120.57 120.50 .03 CH2G*-C-O (Gly) 120.8 2.1 5 120.51 120.52 120.51 .01 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 112.36 112.43 112.40 .02 * * * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 112.96 113.73 113.29 .28 +* ** +* CH2E-CH1E-C (the rest) 110.1 1.9 84 107.97 113.76 111.47 2.03 * +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 108.00 111.04 109.65 .68 * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.98 111.02 111.00 .02 N-CH1E-C (Pro) 111.8 2.5 4 111.00 111.05 111.02 .02 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.48 109.55 109.51 .02 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 107.98 110.52 109.48 1.02 ** * N-CH1E-CH2E (Pro) 103.0 1.1 4 104.98 105.06 105.01 .03 +* +* +* Residue-by-residue listing for analyzed_12 Page 12 ---------------------------------------- ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.97 111.70 110.45 1.14 ** ------------------------------------------------------------------------------------------------------------- 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 analyzed_12 Page 13 ---------------------------------------- B A D C O N T A C T S L I S T I N G ....................................................................... Residue Residue ----------- ----------- No. Type No. Type Contact Distance Chain Atom Chain Atom type (Angstroms) ----------------------------------------------------------------------- 1. 6 HIS O --> 7 HIS CG Main-Side 2.6 2. 14 GLU O --> 15 GLU O Main-Main 2.4 3. 40 LEU CD1 --> 98 LEU O Side-Main 2.6 4. 57 ALA N --> 58 PRO CD Main-Side 2.6 Residue-by-residue listing for analyzed_12 Page 14 ---------------------------------------- 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] 95 84.1% Residues in additional allowed regions [a,b,l,p] 16 14.2% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.8% 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 84.1 83.8 10.0 .0 Inside b. Omega angle st dev 122 .0 6.0 3.0 -2.0 BETTER c. Bad contacts / 100 residues 4 3.2 4.2 10.0 -.1 Inside d. Zeta angle st dev 119 1.5 3.1 1.6 -1.0 BETTER e. H-bond energy st dev 74 .9 .8 .2 .6 Inside f. Overall G-factor 124 .0 -.4 .3 1.4 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 22.8 18.1 6.5 .7 Inside b. Chi-1 trans st dev 47 25.7 19.0 5.3 1.3 WORSE c. Chi-1 gauche plus st dev 40 25.2 17.5 4.9 1.6 WORSE d. Chi-1 pooled st dev 102 31.1 18.2 4.8 2.7 WORSE e. Chi-2 trans st dev 30 24.7 20.4 5.0 .9 Inside 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% 84.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 32.0 4 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for analyzed_12 Page 15 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.38 Chi1-chi2 distribution -1.60 Chi1 only -.28 Chi3 & chi4 .01 Omega .70 ------ -.23 ===== Main-chain covalent forces:- Main-chain bond lengths .66 Main-chain bond angles .24 ------ .41 ===== OVERALL AVERAGE .03 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.