Residue-by-residue listing for refined_20 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 - - - -58.3 182.3 - - - - - - 180.1 - 34.5 - 2 GLY 2 - - - - - - - - - - - 175.6 - - - 3 HIS 3 L - 183.8 - - - - - - - - 178.2 -.9 33.8 - +* +* 4 HIS 4 A - - -68.3 - - - - - - - 170.0 - 31.1 - +* +* 5 HIS 5 l - 187.8 - - - - - - - - 178.0 - 33.2 - 6 HIS 6 b - - -70.5 - - - - - - - 175.9 - 28.8 - * * 7 HIS 7 B - - -59.5 - - - - - - - 183.3 -2.5 35.0 - 8 HIS 8 a - - -58.2 - - - - - - - 178.4 - 33.2 - 9 LEU 9 b - 192.0 - 173.9 - - - - - - 183.9 - 34.1 - 10 GLU 10 B - 188.3 - - - - - - - - 178.3 - 35.9 - 11 MET 11 b - 197.4 - - - - - - - - 172.6 - 33.6 - * * 12 ALA 12 b - - - - - - - - - - 181.8 - 32.1 - 13 SER 13 a 49.6 - - - - - - - - - 184.0 - 35.5 - 14 GLU 14 A - 185.2 - 181.2 - - - - - - 180.8 - 34.8 - 15 GLU 15 B - - -51.0 - - - - - - - 181.1 - 33.9 - * * 16 GLY 16 S - - - - - - - - - - - 177.1 -1.8 - - 17 GLN 17 B 58.3 - - 176.2 - - - - - - 177.3 - 33.0 - 18 VAL 18 B 66.6 - - - - - - - - - 181.4 - 35.2 - 19 ILE 19 E B - - -57.0 177.6 - - - - - - 180.4 -2.5 34.4 - 20 ALA 20 E B - - - - - - - - - - 180.0 -.8 34.1 - +* +* 21 CYS 21 E B - - -53.2 - - - - - - - 179.8 -1.5 35.2 - 22 HIS 22 S A - - -51.7 - - - - - - - 183.1 - 35.1 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 23 THR 23 h B 57.0 - - - - - - - - - 177.4 - 35.7 - 24 VAL 24 H A - 178.3 - - - -75.0 -28.4 - - - 180.3 - 33.7 - 25 GLU 25 H A - 185.4 - 180.9 - -60.7 -50.9 - - - 177.0 - 34.4 - * * 26 THR 26 H A - - -58.6 - - -63.5 -43.9 - - - 178.4 - 34.4 - 27 TRP 27 H A - 173.6 - - - -54.1 -52.2 - - - 179.2 -1.7 35.3 - * * 28 ASN 28 H A - 179.0 - - - -58.3 -48.8 - - - 181.1 -3.6 35.6 - ** ** 29 GLU 29 H A - 177.1 - 181.0 - -57.6 -47.9 - - - 183.6 -2.5 35.6 - 30 GLN 30 H A - - -62.3 - - -69.0 -40.6 - - - 177.8 -2.8 33.2 - * * 31 LEU 31 H A - - -67.4 183.4 - -67.7 -45.1 - - - 178.4 -2.4 34.5 - 32 GLN 32 H A - 183.1 - 177.4 - -60.9 -37.3 - - - 176.3 -2.8 33.3 - * * 33 LYS 33 H A - 178.5 - 183.2 - -61.6 -46.7 - - - 181.2 -2.3 34.3 - 34 ALA 34 H A - - - - - -64.7 -44.3 - - - 181.2 -2.3 33.8 - 35 ASN 35 H A - 189.8 - - - -63.5 -54.1 - - - 181.8 -3.2 36.5 - * +* +* 36 GLU 36 H A - 189.2 - - - -59.6 -41.0 - - - 181.7 -3.1 34.6 - * * 37 SER 37 h A - - -52.1 - - - - - - - 178.1 -2.4 34.8 - 38 LYS 38 T l - 187.6 - 178.8 - - - - - - 180.4 -1.2 32.2 - * * 39 THR 39 t B - - -51.0 - - - - - - - 183.8 -2.1 35.0 - * * 40 LEU 40 E B - 185.6 - 168.9 - - - - - - 185.3 -1.4 33.9 - 41 VAL 41 E B 60.2 - - - - - - - - - 177.6 -1.0 33.1 - * * 42 VAL 42 E B - 179.8 - - - - - - - - 182.3 -2.9 33.8 - * * 43 VAL 43 E B - 182.0 - - - - - - - - 177.1 -3.1 34.8 - * * 44 ASP 44 E B - 173.2 - - - - - - - - 174.6 -3.1 35.2 - * * 45 PHE 45 E B - - -65.9 - - - - - - - 182.1 -2.7 35.4 - 46 THR 46 E B - 181.5 - - - - - - - - 184.0 -2.0 33.6 - 47 ALA 47 t B - - - - - - - - - - 181.1 - 34.3 - 48 SER 48 T A - - -54.8 - - - - - - - 178.3 - 33.8 - 49 TRP 49 T A 55.6 - - - - - - - - - 184.3 - 34.5 - 50 CYS 50 t B - 163.3 - - - - - - -149.8 2.0 179.9 -1.0 34.1 - * *6.0* * *6.0* 51 GLY 51 h - - - - - - - - - - - 181.1 - - - 52 PRO 52 H - - - - - -44.3 -44.3 -31.8 - - - 179.6 - 38.5 - +* +* * +* 53 CYS 53 H A 47.8 - - - - -63.2 -38.0 - -149.8 2.0 178.0 - 34.1 - * *6.0* *6.0* 54 ARG 54 H A - 178.2 - - - -61.0 -34.7 - - - 182.2 -2.0 34.0 - 55 PHE 55 H A - 180.5 - - - -81.7 -32.0 - - - 183.7 -.8 34.3 - * +* +* 56 ILE 56 H A - 190.2 - - - -87.3 -19.8 - - - 180.4 -1.9 34.2 - +* +* +* 57 ALA 57 H A - - - - - -51.1 -47.9 - - - 177.8 -2.0 31.5 - * * 58 PRO 58 H - - - - - -58.4 -58.4 -29.3 - - - 180.0 - 38.7 - * * Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 PHE 59 H A - 182.9 - - - -78.9 -34.9 - - - 177.2 -.9 33.2 - * * * 60 PHE 60 H A - 186.3 - - - -69.6 -33.8 - - - 175.8 -1.8 34.1 - 61 ALA 61 H A - - - - - -68.2 -32.6 - - - 176.9 -2.4 34.0 - 62 ASP 62 H A - 182.5 - - - -65.4 -46.3 - - - 175.0 -1.1 36.0 - * * 63 LEU 63 H A - - -67.9 179.2 - -56.1 -44.4 - - - 177.7 -2.3 35.3 - 64 ALA 64 H A - - - - - -60.2 -31.0 - - - 178.8 -2.1 33.0 - 65 LYS 65 H A - - -60.6 179.6 - -75.6 -32.7 - - - 187.8 -1.1 35.2 - * * * 66 LYS 66 H A - - -61.6 179.5 - -88.3 -29.2 - - - 184.6 -1.6 33.3 - +* +* 67 LEU 67 h B - - -67.9 171.4 - - - - - - 175.5 -2.2 32.2 - 68 PRO 68 S - - - - - -81.8 - - - - - 181.9 - 39.7 - * +* +* 69 ASN 69 e A - 184.3 - - - - - - - - 180.0 - 34.2 - 70 VAL 70 E B - 179.3 - - - - - - - - 179.3 - 34.5 - 71 LEU 71 E B - 187.3 - - - - - - - - 181.7 -3.1 34.8 - * * 72 PHE 72 E B - - -57.5 - - - - - - - 180.0 -.6 34.3 - +* +* 73 LEU 73 E B - - -71.3 - - - - - - - 181.4 -2.6 32.3 - 74 LYS 74 E B - 174.1 - - - - - - - - 176.5 -3.2 36.5 - +* +* 75 VAL 75 E B - 178.1 - - - - - - - - 175.3 -3.2 33.8 - +* +* 76 ASP 76 E B - 179.3 - - - - - - - - 185.5 -.6 34.2 - +* +* 77 THR 77 e A 55.8 - - - - - - - - - 176.0 -1.6 32.1 - 78 ASP 78 T A - 178.9 - - - - - - - - 177.4 - 35.2 - 79 GLU 79 T a - - -63.0 185.0 - - - - - - 189.9 - 36.2 - +* +* 80 LEU 80 h a - 187.5 - - - - - - - - 180.0 -2.8 35.1 - * * 81 LYS 81 H A 56.1 - - - - -57.8 -27.6 - - - 180.4 -.8 30.6 - * +* +* 82 SER 82 H A 50.1 - - - - -62.2 -43.8 - - - 178.9 - 33.6 - 83 VAL 83 H A - 173.0 - - - -66.8 -37.1 - - - 178.2 -.9 32.9 - +* +* 84 ALA 84 H A - - - - - -62.2 -40.6 - - - 179.3 -1.3 34.1 - 85 SER 85 H A - 184.4 - - - -72.8 -30.6 - - - 180.9 -2.2 33.9 - 86 ASP 86 H A - 186.4 - - - -71.5 -36.2 - - - 176.8 -1.9 33.4 - 87 TRP 87 h A - - -71.6 - - - - - - - 176.1 -2.4 32.4 - 88 ALA 88 T l - - - - - - - - - - 181.1 -.8 33.5 - +* +* 89 ILE 89 t b - - -57.0 - - - - - - - 182.2 -2.3 34.2 - 90 GLN 90 A - 181.9 - - - - - - - - 182.2 -.8 34.6 - +* +* 91 ALA 91 S B - - - - - - - - - - 179.4 - 34.0 - 92 MET 92 S B - - -72.3 176.1 - - - - - - 1.4 - 33.4 - 93 PRO 93 e cis - - - - - -77.6 - - - - - 177.0 - 39.1 - * * * 94 THR 94 E B - - -64.5 - - - - - - - 179.4 -2.0 33.2 - 95 PHE 95 E B - - -59.7 - - - - - - - 181.9 -2.8 36.5 - 96 MET 96 E B - 188.2 - - - - - - - - 183.2 -3.3 34.5 - +* +* 97 PHE 97 E B - - -69.5 - - - - - - - 177.6 -2.8 35.8 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 LEU 98 E B - - -54.6 - - - - - - - 176.0 -3.0 35.2 - * * 99 LYS 99 E B - 174.4 - 170.4 - - - - - - 180.4 -3.0 32.5 - * * 100 GLU 100 T l - - -57.5 172.7 - - - - - - 183.9 - 34.3 - 101 GLY 101 T - - - - - - - - - - - 178.8 - - - 102 LYS 102 E B - - -56.1 176.1 - - - - - - 181.4 -1.9 36.4 - 103 ILE 103 E B - - -68.0 176.2 - - - - - - 177.3 - 33.3 - 104 LEU 104 E a - - -69.4 186.4 - - - - - - 186.2 -1.8 33.5 - * * 105 ASP 105 E B 52.3 - - - - - - - - - 180.9 -2.2 32.2 - 106 LYS 106 E B 50.4 - - - - - - - - - 173.4 - 33.1 - * * 107 VAL 107 E B - 182.4 - - - - - - - - 178.0 -2.9 35.5 - * * 108 VAL 108 E B 60.6 - - - - - - - - - 181.9 - 32.2 - 109 GLY 109 e - - - - - - - - - - - 177.2 -3.2 - - +* +* 110 ALA 110 B - - - - - - - - - - 180.5 - 34.8 - 111 LYS 111 h B - - -62.2 180.5 - - - - - - 185.2 -1.1 35.3 - * * 112 LYS 112 H A - 183.4 - 179.9 - -59.1 -50.5 - - - 182.4 -.5 34.5 - ** ** 113 ASP 113 H A - 183.6 - - - -67.6 -45.3 - - - 182.1 - 35.0 - 114 GLU 114 H A - 186.0 - - - -65.8 -33.6 - - - 179.1 - 34.0 - 115 LEU 115 H A - 186.8 - - - -64.0 -48.4 - - - 178.6 -2.3 34.9 - 116 GLN 116 H A - - -51.8 - - -58.1 -40.0 - - - 180.6 -1.9 34.6 - 117 SER 117 H A - 183.6 - - - -66.7 -34.4 - - - 178.1 -2.2 33.8 - 118 THR 118 H A - - -55.7 - - -73.4 -36.1 - - - 176.4 -2.1 34.2 - 119 ILE 119 H A - - -61.0 177.2 - -63.2 -46.7 - - - 178.9 -2.6 33.6 - 120 ALA 120 H A - - - - - -65.3 -31.5 - - - 177.0 -2.9 33.1 - * * 121 LYS 121 H A - 184.9 - 177.3 - -63.0 -44.3 - - - 178.5 -1.6 36.0 - 122 HIS 122 H A - - -72.1 - - -79.9 -17.3 - - - 179.2 -2.1 33.2 - * +* +* 123 LEU 123 h b - 195.2 - 171.8 - - - - - - 180.3 -1.3 34.4 - 124 ALA 124 - - - - - - - - - - - - -1.0 34.3 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * +* +* +* *6.0* +* ** +* *6.0* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 55.4 182.9 -61.3 178.0 -65.6 -65.5 -38.8 - -149.8 2.0 179.7 -2.0 34.3 *6.0* *6.0* Standard deviations: 5.3 6.1 6.7 4.4 17.4 8.8 8.5 - .0 .0 3.1 .8 1.5 Numbers of values: 13 50 39 28 4 45 45 0 2 2 122 80 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_20 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_20 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 - 1.242 1.515 1.538 1.473 - 116.64 120.28 108.99 109.41 111.62 123.08 2 GLY 2 1.322 1.235 1.503 - 1.445 121.48 116.28 120.16 - 110.81 - 123.56 3 HIS 3 1.334 1.227 1.554 1.564 1.472 122.89 116.49 121.50 112.32 110.83 109.05 121.96 * +* * +* 4 HIS 4 1.328 1.234 1.525 1.529 1.464 121.09 115.65 120.57 112.40 111.14 112.35 123.77 * * * 5 HIS 5 1.341 1.227 1.548 1.573 1.471 123.59 117.85 120.93 112.75 112.40 109.03 121.11 * ** * * * ** 6 HIS 6 1.326 1.228 1.517 1.536 1.470 119.76 114.17 121.88 112.18 112.87 114.85 123.80 * * * +** +** 7 HIS 7 1.309 1.238 1.502 1.554 1.444 126.07 118.14 119.45 108.61 104.67 112.95 122.41 * * * ** ** * ** 8 HIS 8 1.290 1.235 1.521 1.540 1.448 119.94 115.62 120.93 110.69 110.65 111.63 123.42 +** +** 9 LEU 9 1.311 1.240 1.505 1.563 1.443 123.58 115.95 120.73 111.61 105.79 111.29 123.27 * +* * +* +* 10 GLU 10 1.291 1.239 1.507 1.557 1.432 121.96 116.65 120.51 111.44 107.27 108.32 122.79 +** * * * * +** 11 MET 11 1.301 1.237 1.510 1.538 1.426 120.04 114.81 121.38 111.02 109.48 111.33 123.62 +* +* +* 12 ALA 12 1.289 1.243 1.498 1.515 1.423 123.22 113.18 122.47 112.30 107.40 112.71 123.97 +** * +* +* * * +* +** Residue-by-residue listing for refined_20 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 1.293 1.241 1.515 1.532 1.430 124.09 114.49 122.09 111.55 108.48 108.13 123.36 +** * * * +** 14 GLU 14 1.313 1.233 1.522 1.536 1.445 122.32 115.51 121.28 110.40 109.32 109.94 123.20 * * 15 GLU 15 1.315 1.251 1.525 1.540 1.444 122.72 115.52 121.15 108.90 110.85 112.29 123.32 * * * 16 GLY 16 1.305 1.230 1.501 - 1.436 121.11 116.60 120.48 - 112.73 - 122.92 +* +* 17 GLN 17 1.316 1.233 1.481 1.519 1.440 120.99 113.66 121.68 108.87 111.31 113.43 124.65 ** * +* * ** 18 VAL 18 1.273 1.239 1.537 1.549 1.412 123.78 118.42 119.70 111.54 107.53 109.01 121.82 +*** ** * * * * * +*** 19 ILE 19 1.314 1.225 1.516 1.537 1.450 119.57 116.48 120.67 109.30 110.24 111.32 122.85 * * * 20 ALA 20 1.304 1.229 1.509 1.524 1.441 121.44 116.76 120.65 110.60 109.99 110.54 122.58 +* +* 21 CYS 21 1.299 1.228 1.508 1.508 1.417 120.98 116.29 120.72 110.19 108.71 109.68 122.96 ** * ** ** 22 HIS 22 1.296 1.237 1.518 1.545 1.444 121.07 115.25 121.26 109.29 108.19 111.06 123.49 ** * ** 23 THR 23 1.327 1.249 1.516 1.555 1.449 123.07 116.50 120.21 107.89 109.38 111.31 123.28 24 VAL 24 1.319 1.214 1.526 1.554 1.444 121.76 116.49 120.71 110.16 109.89 111.87 122.77 25 GLU 25 1.324 1.240 1.531 1.522 1.460 122.25 116.14 120.74 110.17 110.48 110.15 123.12 26 THR 26 1.328 1.226 1.533 1.544 1.454 121.64 115.58 120.74 110.10 109.76 110.74 123.65 27 TRP 27 1.326 1.239 1.537 1.537 1.460 123.64 115.13 121.18 111.33 110.77 107.70 123.66 * +* +* 28 ASN 28 1.313 1.231 1.518 1.539 1.460 124.18 115.49 120.69 110.08 110.63 108.71 123.80 * * * * 29 GLU 29 1.318 1.236 1.524 1.521 1.450 123.35 115.96 120.75 109.61 111.64 108.79 123.28 * * 30 GLN 30 1.312 1.237 1.519 1.494 1.407 122.56 117.48 120.13 112.01 113.04 109.19 122.39 * +* +** * +** 31 LEU 31 1.328 1.233 1.499 1.483 1.419 120.95 115.95 120.48 109.54 111.02 110.37 123.57 * ** ** ** 32 GLN 32 1.314 1.219 1.514 1.519 1.436 121.72 116.42 120.30 111.58 109.88 110.74 123.25 * * * 33 LYS 33 1.333 1.230 1.517 1.533 1.450 121.70 116.57 120.32 109.27 110.12 111.55 123.10 34 ALA 34 1.332 1.226 1.520 1.522 1.452 121.36 115.76 120.71 110.55 110.85 110.61 123.50 35 ASN 35 1.317 1.229 1.513 1.529 1.463 123.13 114.94 121.37 108.77 109.82 108.74 123.67 * * 36 GLU 36 1.314 1.237 1.543 1.533 1.471 122.97 116.81 120.68 109.44 111.69 110.19 122.51 * * 37 SER 37 1.322 1.236 1.533 1.512 1.450 121.62 115.76 120.68 110.19 111.12 109.24 123.56 38 LYS 38 1.345 1.238 1.559 1.511 1.426 124.82 114.32 123.08 114.26 111.13 108.91 122.44 * +* +* +* * ** ** 39 THR 39 1.301 1.240 1.534 1.521 1.428 123.33 115.77 121.29 110.38 109.04 109.67 122.91 +* +* * +* 40 LEU 40 1.288 1.225 1.547 1.570 1.449 122.36 117.58 120.13 113.71 107.96 108.68 122.28 +** * ** +* * * +** 41 VAL 41 1.320 1.234 1.545 1.567 1.453 121.13 116.11 121.03 111.44 112.33 110.56 122.85 * * 42 VAL 42 1.319 1.235 1.520 1.542 1.451 122.72 116.44 120.83 109.41 109.29 112.38 122.73 43 VAL 43 1.303 1.234 1.525 1.548 1.442 121.77 115.77 120.59 108.67 110.80 111.36 123.64 +* +* Residue-by-residue listing for refined_20 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 1.308 1.245 1.517 1.535 1.454 123.47 116.49 120.68 109.35 110.20 110.14 122.78 +* +* 45 PHE 45 1.313 1.246 1.515 1.532 1.424 121.66 116.34 120.49 109.28 108.29 110.62 123.15 * +* * +* 46 THR 46 1.300 1.238 1.528 1.560 1.431 121.57 117.01 120.21 111.43 109.66 110.90 122.78 ** * * ** 47 ALA 47 1.320 1.232 1.512 1.513 1.447 121.90 116.03 120.78 110.13 111.08 110.18 123.19 48 SER 48 1.307 1.230 1.548 1.514 1.450 122.85 116.49 120.93 111.58 112.25 108.85 122.58 +* * +* 49 TRP 49 1.324 1.242 1.529 1.547 1.475 122.30 114.86 121.69 110.29 110.29 110.11 123.45 50 CYS 50 1.293 1.237 1.526 1.524 1.433 123.50 115.53 121.03 111.89 112.22 108.47 123.43 +** * * +** 51 GLY 51 1.318 1.225 1.533 - 1.447 122.04 118.41 119.60 - 112.58 - 121.99 52 PRO 52 1.374 1.232 1.545 1.547 1.490 124.76 116.93 120.55 109.91 115.03 103.55 122.52 ** +* * ** 53 CYS 53 1.317 1.225 1.520 1.492 1.462 122.51 115.38 121.20 111.07 111.65 109.01 123.38 +* +* 54 ARG 54 1.305 1.230 1.540 1.568 1.461 123.42 115.85 120.98 113.07 109.94 108.37 123.12 +* +* +* * +* 55 PHE 55 1.318 1.230 1.543 1.545 1.456 122.81 117.01 120.66 110.94 111.84 109.25 122.32 56 ILE 56 1.321 1.239 1.550 1.572 1.468 121.00 115.81 121.08 110.36 110.25 110.76 123.08 * * * 57 ALA 57 1.336 1.235 1.557 1.531 1.471 123.42 120.12 119.05 111.49 113.98 111.42 120.83 +* +* * * +* 58 PRO 58 1.381 1.232 1.536 1.533 1.477 122.08 116.73 120.78 109.88 112.60 103.73 122.48 +** +** 59 PHE 59 1.326 1.224 1.527 1.538 1.453 121.00 116.20 121.16 111.13 109.96 111.30 122.63 60 PHE 60 1.315 1.228 1.533 1.538 1.459 121.75 115.87 121.19 111.71 108.66 109.72 122.93 * * 61 ALA 61 1.326 1.225 1.531 1.521 1.457 121.97 115.57 121.08 110.66 109.83 110.45 123.35 62 ASP 62 1.327 1.227 1.503 1.517 1.473 123.33 114.53 121.56 109.29 108.77 109.19 123.91 * * 63 LEU 63 1.313 1.238 1.531 1.529 1.437 123.72 115.48 121.00 110.94 110.49 108.37 123.49 * * * * * 64 ALA 64 1.324 1.224 1.529 1.522 1.456 123.17 116.77 120.66 110.86 111.69 110.97 122.52 65 LYS 65 1.325 1.234 1.521 1.529 1.460 121.68 116.30 120.90 107.87 111.31 111.13 122.80 * * 66 LYS 66 1.309 1.228 1.515 1.517 1.447 120.79 118.15 119.84 110.08 114.24 110.59 122.01 * * * 67 LEU 67 1.308 1.213 1.520 1.510 1.431 119.93 116.72 121.00 112.03 114.38 109.98 122.27 * * * * * 68 PRO 68 1.346 1.230 1.534 1.531 1.471 123.10 115.44 121.48 109.73 110.96 102.62 123.08 69 ASN 69 1.326 1.231 1.523 1.548 1.462 122.87 115.16 121.97 111.73 109.60 109.41 122.86 70 VAL 70 1.314 1.223 1.518 1.551 1.429 122.33 116.41 120.70 109.62 109.25 111.49 122.88 * +* +* 71 LEU 71 1.303 1.233 1.525 1.535 1.434 121.49 117.05 120.33 110.86 108.43 109.88 122.60 +* * +* 72 PHE 72 1.314 1.243 1.513 1.519 1.452 121.10 115.39 121.32 108.89 110.79 111.53 123.29 * * 73 LEU 73 1.294 1.226 1.513 1.543 1.440 122.81 115.03 121.20 110.05 111.41 113.23 123.77 ** +* ** 74 LYS 74 1.298 1.238 1.512 1.543 1.439 124.19 116.72 120.42 109.26 108.75 109.03 122.85 ** * * ** 75 VAL 75 1.299 1.237 1.507 1.556 1.433 120.80 115.45 121.00 109.60 109.72 112.52 123.54 ** * ** Residue-by-residue listing for refined_20 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 1.306 1.235 1.494 1.516 1.437 121.90 115.91 120.72 110.47 107.30 111.27 123.32 +* * * * +* 77 THR 77 1.300 1.219 1.519 1.522 1.445 122.08 116.52 120.72 111.49 113.44 111.11 122.76 ** * ** 78 ASP 78 1.303 1.235 1.511 1.518 1.444 121.32 114.94 121.74 110.32 108.36 109.62 123.32 +* * +* 79 GLU 79 1.309 1.236 1.529 1.509 1.418 122.92 115.78 121.33 108.21 112.28 109.16 122.87 * * ** ** 80 LEU 80 1.311 1.242 1.550 1.536 1.436 123.08 114.91 122.11 112.33 110.69 107.13 122.90 * * * * +* +* 81 LYS 81 1.320 1.234 1.544 1.561 1.467 123.67 116.52 120.69 113.38 113.53 111.20 122.78 +* * +* +* 82 SER 82 1.322 1.229 1.535 1.524 1.448 122.42 116.56 120.54 111.96 111.65 109.14 122.87 83 VAL 83 1.325 1.230 1.523 1.554 1.458 121.77 116.10 120.98 111.13 110.61 111.71 122.86 84 ALA 84 1.319 1.233 1.520 1.513 1.454 121.48 115.67 121.23 110.40 110.01 110.45 123.06 85 SER 85 1.319 1.240 1.539 1.539 1.436 121.65 116.50 120.96 111.43 110.32 110.00 122.53 * * 86 ASP 86 1.325 1.235 1.526 1.537 1.460 121.89 116.15 120.91 111.08 110.49 110.80 122.92 87 TRP 87 1.326 1.230 1.518 1.527 1.460 122.42 116.14 120.30 110.72 112.26 111.83 123.56 88 ALA 88 1.342 1.235 1.533 1.534 1.473 123.57 116.15 120.73 110.91 112.10 110.12 123.05 * * 89 ILE 89 1.327 1.236 1.527 1.562 1.457 122.42 115.79 121.05 109.99 109.61 111.29 123.12 90 GLN 90 1.312 1.232 1.521 1.541 1.444 122.16 116.24 121.04 110.30 110.59 110.08 122.70 * * 91 ALA 91 1.306 1.225 1.505 1.520 1.443 121.24 116.42 120.71 110.70 110.00 110.62 122.84 +* +* 92 MET 92 1.304 1.238 1.512 1.527 1.434 122.52 118.29 119.89 111.73 110.09 110.40 121.82 +* * * +* 93 PRO 93 1.346 1.223 1.531 1.525 1.485 124.18 116.00 120.94 109.69 113.34 102.99 123.04 * * 94 THR 94 1.303 1.232 1.521 1.541 1.438 122.43 116.22 120.63 110.65 109.95 111.95 123.14 +* * +* 95 PHE 95 1.306 1.235 1.503 1.522 1.415 122.41 116.78 120.38 108.86 107.31 109.68 122.83 +* * ** * ** 96 MET 96 1.291 1.230 1.503 1.516 1.434 120.79 115.58 120.86 110.23 109.19 110.49 123.56 +** * * +** 97 PHE 97 1.291 1.250 1.512 1.510 1.411 123.33 115.91 121.46 109.20 110.92 109.19 122.63 +** ** +** 98 LEU 98 1.293 1.217 1.516 1.559 1.423 121.00 117.08 120.51 107.79 107.64 112.90 122.40 +** * +* * * * +** 99 LYS 99 1.283 1.219 1.468 1.526 1.431 121.45 114.94 120.42 111.74 108.87 112.33 124.53 *** +** * * *** 100 GLU 100 1.324 1.221 1.531 1.518 1.457 124.43 115.98 120.96 109.19 110.66 111.15 123.05 +* +* 101 GLY 101 1.315 1.229 1.525 - 1.448 120.98 115.75 120.96 - 111.32 - 123.29 * * 102 LYS 102 1.326 1.237 1.524 1.534 1.452 123.30 117.18 119.87 108.81 108.43 109.32 122.96 103 ILE 103 1.314 1.235 1.531 1.560 1.463 122.20 116.14 120.89 110.20 111.94 111.50 122.96 * * 104 LEU 104 1.324 1.242 1.509 1.520 1.431 121.27 116.49 120.30 108.91 112.31 112.25 123.20 * * * 105 ASP 105 1.320 1.218 1.505 1.520 1.444 121.59 115.55 121.19 110.59 113.06 112.00 123.21 106 LYS 106 1.308 1.237 1.532 1.562 1.445 122.63 116.12 120.79 111.84 111.83 110.37 123.05 +* +* +* Residue-by-residue listing for refined_20 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 1.307 1.231 1.510 1.561 1.452 122.53 117.19 119.93 107.67 107.26 112.47 122.87 +* * +* 108 VAL 108 1.300 1.248 1.527 1.569 1.435 120.84 115.68 120.80 112.03 109.40 112.43 123.45 ** * * * ** 109 GLY 109 1.316 1.243 1.512 - 1.432 121.59 117.33 120.57 - 110.95 - 122.09 * * 110 ALA 110 1.318 1.240 1.498 1.522 1.431 119.23 115.01 121.39 110.51 107.40 110.52 123.59 * * * * * 111 LYS 111 1.287 1.228 1.492 1.513 1.404 123.11 116.62 119.85 111.12 108.16 108.96 123.53 +** +* +** * +** 112 LYS 112 1.310 1.225 1.527 1.525 1.440 122.59 115.98 120.56 110.79 111.40 109.22 123.40 * * 113 ASP 113 1.319 1.234 1.521 1.526 1.468 122.86 115.97 121.18 109.43 111.34 109.84 122.84 114 GLU 114 1.324 1.235 1.519 1.528 1.455 121.55 116.28 120.88 110.07 110.46 111.02 122.84 115 LEU 115 1.315 1.219 1.498 1.507 1.438 121.21 115.34 120.73 109.35 109.03 110.80 123.91 * * * * 116 GLN 116 1.319 1.232 1.520 1.536 1.476 122.08 115.81 120.99 108.42 109.88 111.83 123.16 117 SER 117 1.324 1.236 1.535 1.539 1.445 121.69 115.90 121.14 111.76 109.88 109.84 122.92 118 THR 118 1.316 1.239 1.545 1.544 1.438 122.29 116.24 121.15 111.12 109.65 110.08 122.58 * * 119 ILE 119 1.332 1.222 1.522 1.559 1.451 121.84 116.46 120.49 110.05 109.38 112.20 123.00 120 ALA 120 1.329 1.231 1.526 1.515 1.460 121.97 115.91 120.82 111.10 110.99 110.78 123.27 121 LYS 121 1.321 1.225 1.514 1.501 1.455 122.75 115.42 121.37 109.15 109.52 108.95 123.21 * * 122 HIS 122 1.311 1.233 1.519 1.519 1.444 122.30 117.33 119.86 109.80 113.03 111.43 122.80 * * 123 LEU 123 1.325 1.242 1.526 1.529 1.429 121.98 114.96 121.07 112.05 109.04 108.96 123.90 +* * +* 124 ALA 124 1.305 - 1.506 1.532 1.434 124.22 - - 110.53 107.50 111.22 - +* * * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +** ** +** ** +* * ** ** +** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 1.273 1.345 1.314 .013 +*** * * C-N (Pro) 1.341 .016 4 1.346 1.381 1.362 .016 +** * C-O C-O 1.231 .020 123 1.213 1.251 1.233 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.468 1.559 1.522 .015 +** +* CH2G*-C (Gly) 1.516 .018 5 1.501 1.533 1.515 .012 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.513 1.534 1.522 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.521 1.572 1.551 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.483 1.573 1.531 .017 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.404 1.476 1.446 .016 +** NH1-CH2G* (Gly) 1.451 .016 5 1.432 1.448 1.442 .007 * N-CH1E (Pro) 1.466 .015 4 1.471 1.490 1.481 .007 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 2.0 114 113.18 120.12 116.08 .96 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.75 118.41 116.88 .92 CH1E-C-N (Pro) 116.9 1.5 4 115.44 116.93 116.28 .59 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.83 124.65 123.03 .57 * * O-C-N (Pro) 122.0 1.4 4 122.48 123.08 122.78 .28 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.23 126.07 122.24 1.15 * ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.98 122.04 121.44 .38 C-N-CH1E (Pro) 122.6 5.0 4 122.08 124.76 123.53 1.03 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.05 123.08 120.85 .57 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.60 120.96 120.35 .46 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.13 112.30 110.83 .53 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.67 112.03 110.19 1.13 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.79 114.26 110.51 1.38 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.67 114.38 110.22 1.73 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.81 112.73 111.68 .82 N-CH1E-C (Pro) 111.8 2.5 4 110.96 115.03 112.98 1.46 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.12 112.71 110.81 .65 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.01 112.52 111.30 .90 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.62 103.73 103.22 .44 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.13 114.85 110.24 1.45 +* +** ------------------------------------------------------------------------------------------------------------- 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_20 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] 98 86.7% Residues in additional allowed regions [a,b,l,p] 15 13.3% 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 86.7 83.8 10.0 .3 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 1.5 3.1 1.6 -1.0 BETTER e. H-bond energy st dev 80 .8 .8 .2 .0 Inside f. Overall G-factor 124 .1 -.4 .3 1.7 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 13 5.3 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 50 6.1 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 39 6.7 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 7.6 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 28 4.4 20.4 5.0 -3.2 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% 86.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .80 2 Residue-by-residue listing for refined_20 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.21 Chi1-chi2 distribution -.02 Chi1 only .11 Chi3 & chi4 .54 Omega .07 ------ .02 ===== Main-chain covalent forces:- Main-chain bond lengths .07 Main-chain bond angles .45 ------ .29 ===== OVERALL AVERAGE .12 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.