Residue-by-residue listing for refined_8 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 - - 183.8 - 182.4 - - - - - - 179.7 - 35.2 - 2 GLY 2 - - - - - - - - - - - 181.0 - - - 3 HIS 3 B - - -68.9 - - - - - - - 173.4 - 33.4 - * * 4 HIS 4 b - 179.1 - - - - - - - - 180.2 - 33.4 - 5 HIS 5 b - - -69.8 - - - - - - - 177.2 - 34.0 - 6 HIS 6 b - - -75.2 - - - - - - - 174.5 - 31.0 - 7 HIS 7 B - - -64.1 - - - - - - - 182.4 - 34.2 - 8 HIS 8 b 63.4 - - - - - - - - - 175.9 -1.1 27.6 - * +* +* 9 LEU 9 S b 68.0 - - 174.0 - - - - - - 181.3 -1.7 33.7 - 10 GLU 10 B - 197.9 - - - - - - - - 180.9 - 32.6 - 11 MET 11 S B - - -57.4 - - - - - - - 183.4 - 34.4 - 12 ALA 12 S l - - - - - - - - - - 182.6 -.6 31.0 - +* +* 13 SER 13 b 49.4 - - - - - - - - - 179.9 - 34.5 - 14 GLU 14 S b 26.8 - - - - - - - - - 178.5 - 30.2 - ** * ** 15 GLU 15 B 59.8 - - 166.6 - - - - - - 173.8 -1.1 35.6 - * * * 16 GLY 16 S - - - - - - - - - - - 178.8 -1.5 - - 17 GLN 17 B - - -56.5 181.2 - - - - - - 181.8 - 33.8 - 18 VAL 18 B - 188.9 - - - - - - - - 184.3 - 35.3 - 19 ILE 19 E B - - -58.9 177.4 - - - - - - 180.4 -3.1 34.8 - * * 20 ALA 20 E B - - - - - - - - - - 180.5 -.8 33.8 - +* +* 21 CYS 21 E B - - -55.4 - - - - - - - 176.9 -1.9 35.5 - Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 HIS 22 S A - - -62.8 - - - - - - - 180.4 - 33.5 - 23 THR 23 h B 55.9 - - - - - - - - - 176.4 - 35.7 - 24 VAL 24 H A 62.8 - - - - -72.7 -22.5 - - - 179.4 - 33.0 - * * 25 GLU 25 H A - 181.5 - 179.6 - -63.4 -52.0 - - - 178.5 - 35.0 - * * 26 THR 26 H A - - -55.5 - - -61.7 -39.0 - - - 177.8 - 34.5 - 27 TRP 27 H A - 169.9 - - - -55.6 -53.2 - - - 180.9 -1.4 34.4 - * * 28 ASN 28 H A - 185.2 - - - -69.9 -43.4 - - - 182.9 -2.8 34.2 - 29 GLU 29 H A - 189.3 - - - -55.4 -48.1 - - - 183.2 -3.0 36.1 - * * 30 GLN 30 H A - - -65.4 - - -72.7 -41.3 - - - 178.0 -2.6 32.7 - 31 LEU 31 H A - - -70.2 183.8 - -65.9 -36.4 - - - 174.2 -1.7 34.4 - 32 GLN 32 H A - 178.6 - 183.2 - -58.5 -49.5 - - - 181.0 -2.8 33.3 - * * 33 LYS 33 H A - 188.5 - 181.4 - -61.6 -37.0 - - - 178.4 -2.1 32.6 - 34 ALA 34 H A - - - - - -64.6 -44.1 - - - 179.8 -2.2 33.7 - 35 ASN 35 H A - 189.2 - - - -67.8 -50.7 - - - 182.4 -2.8 36.8 - * * 36 GLU 36 H A - 186.0 - 179.4 - -58.7 -35.0 - - - 179.3 -3.8 35.5 - ** ** 37 SER 37 h A - - -57.8 - - - - - - - 180.0 -2.2 35.0 - 38 LYS 38 T L - 191.2 - 190.4 - - - - - - 183.7 -1.7 34.5 - 39 THR 39 t B - - -46.6 - - - - - - - 178.1 -3.4 34.5 - * +* +* 40 LEU 40 e B - 173.8 - - - - - - - - 180.1 - 36.0 - 41 VAL 41 E B 57.9 - - - - - - - - - 178.6 -1.2 32.8 - * * 42 VAL 42 E B - 183.6 - - - - - - - - 184.2 -3.1 33.7 - * * 43 VAL 43 E B - 180.2 - - - - - - - - 175.3 -2.8 34.8 - * * 44 ASP 44 E B - 168.9 - - - - - - - - 176.9 -3.2 34.4 - +* +* 45 PHE 45 E B - - -62.0 - - - - - - - 185.1 -2.7 35.6 - 46 THR 46 E B - - -71.1 - - - - - - - 172.5 -2.8 35.6 - * * * 47 ALA 47 t B - - - - - - - - - - 183.0 - 34.4 - 48 SER 48 T A - 184.6 - - - - - - - - 178.0 - 33.0 - 49 TRP 49 T A 53.6 - - - - - - - - - 180.8 - 31.9 - 50 CYS 50 h B - 176.1 - 218.1 - - - 56.6 - 2.0 182.9 -2.4 33.7 - ** +** +** 51 GLY 51 H - - - - - - -63.3 -64.9 - - - 180.7 -.6 - - ** +* ** 52 PRO 52 H - - - - - -59.6 -59.6 -30.8 - - - 179.3 - 38.5 - * * 53 CYS 53 H A - - -51.8 - - -68.2 -43.2 56.6 - 2.0 179.2 - 35.4 - +** +** 54 ARG 54 H A - 184.9 - 184.7 - -66.4 -29.7 - - - 179.8 -2.1 35.6 - 55 PHE 55 H A - 179.6 - - - -74.0 -35.6 - - - 183.8 -1.7 34.5 - 56 ILE 56 H A - 195.1 - - - -87.8 -23.2 - - - 181.2 -1.8 34.0 - +* * +* 57 ALA 57 H A - - - - - -49.2 -46.2 - - - 177.6 -2.0 32.2 - * * 58 PRO 58 H - - - - - -48.4 -48.4 -38.6 - - - 183.6 - 39.8 - +* * +* +* Residue-by-residue listing for refined_8 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 - 185.8 - - - -72.5 -36.3 - - - 179.8 -1.2 33.5 - * * 60 PHE 60 H A - 187.4 - - - -70.4 -33.4 - - - 176.2 -1.1 33.8 - * * 61 ALA 61 H A - - - - - -69.4 -28.5 - - - 178.8 -2.1 33.7 - 62 ASP 62 H A - 190.0 - - - -71.9 -40.8 - - - 175.7 -1.2 35.7 - * * 63 LEU 63 H A - - -69.9 180.1 - -56.2 -43.3 - - - 177.2 -2.0 34.9 - 64 ALA 64 H A - - - - - -62.8 -31.1 - - - 179.9 -1.7 33.7 - 65 LYS 65 H A - 185.4 - 175.4 - -77.2 -33.2 - - - 179.5 -.9 33.9 - * * * 66 LYS 66 H A - - -66.1 - - -74.9 -40.9 - - - 179.7 -1.9 34.2 - 67 LEU 67 h b - - -65.1 - - - - - - - 186.4 -2.6 33.7 - * * 68 PRO 68 S - - - - - -82.3 - - - - - 182.0 - 38.7 - +* * +* 69 ASN 69 S A - 191.3 - - - - - - - - 180.5 - 34.4 - 70 VAL 70 S B - 176.9 - - - - - - - - 182.2 - 33.9 - 71 LEU 71 E B - - -64.0 - - - - - - - 174.5 -1.5 35.0 - 72 PHE 72 E B - - -61.2 - - - - - - - 183.2 -.6 34.4 - +* +* 73 LEU 73 E B - - -68.3 - - - - - - - 175.4 -2.2 33.0 - 74 LYS 74 E B - - -65.5 - - - - - - - 175.4 -2.5 37.2 - 75 VAL 75 E B - 178.6 - - - - - - - - 177.8 -3.2 34.9 - +* +* 76 ASP 76 E B - 183.4 - - - - - - - - 184.9 -.8 32.8 - +* +* 77 THR 77 e A 57.9 - - - - - - - - - 178.6 -1.1 34.2 - * * 78 ASP 78 T A - 186.8 - - - - - - - - 173.5 - 34.2 - * * 79 GLU 79 T a - - -67.0 184.1 - - - - - - 183.6 - 35.3 - 80 LEU 80 h b - - -71.2 - - - - - - - 182.2 -3.3 33.4 - +* +* 81 LYS 81 H A 49.1 - - - - -68.0 -30.9 - - - 179.3 -1.7 30.2 - * * 82 SER 82 H A - - -56.5 - - -75.5 -34.1 - - - 178.4 - 34.0 - 83 VAL 83 H A - 181.4 - - - -71.9 -42.2 - - - 178.3 - 34.3 - 84 ALA 84 H A - - - - - -58.4 -45.0 - - - 180.2 -2.5 34.3 - 85 SER 85 H A - - -57.7 - - -66.4 -36.6 - - - 182.5 -2.0 34.4 - 86 ASP 86 H A - 186.0 - - - -71.0 -34.1 - - - 177.2 -1.7 33.6 - 87 TRP 87 h A - - -73.4 - - - - - - - 178.4 -2.2 32.3 - 88 ALA 88 T l - - - - - - - - - - 180.8 -1.1 33.1 - * * 89 ILE 89 t b - - -56.8 - - - - - - - 180.4 -2.8 33.7 - 90 GLN 90 A - - -65.8 178.3 - - - - - - 178.1 -1.2 34.2 - * * 91 ALA 91 S B - - - - - - - - - - 182.2 - 33.8 - 92 MET 92 S B - - -62.9 177.4 - - - - - - -3.2 - 35.6 - 93 PRO 93 e cis - - - - - -89.9 - - - - - 175.2 - 39.6 - ** +* ** 94 THR 94 E B - - -60.7 - - - - - - - 179.7 -1.7 34.2 - 95 PHE 95 E B - - -63.9 - - - - - - - 179.8 -2.4 36.0 - 96 MET 96 E B - 179.6 - 177.3 - - - - - - 180.6 -3.5 33.1 - +* +* 97 PHE 97 E B - - -68.1 - - - - - - - 178.2 -3.4 36.4 - +* +* Residue-by-residue listing for refined_8 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 57.9 - - 168.1 - - - - - - 186.6 -1.8 31.6 - * * 99 LYS 99 E B - 175.6 - 179.3 - - - - - - 174.6 -3.4 34.2 - +* +* 100 GLU 100 T l - - -59.3 175.1 - - - - - - 180.0 - 33.7 - 101 GLY 101 T - - - - - - - - - - - 175.9 - - - 102 LYS 102 E B - 180.1 - - - - - - - - 181.9 -2.0 34.8 - 103 ILE 103 E B - - -60.6 177.9 - - - - - - 179.5 - 32.5 - 104 LEU 104 E a - - -67.2 180.4 - - - - - - 185.3 -1.9 34.2 - 105 ASP 105 E B 60.2 - - - - - - - - - 180.6 -2.2 33.0 - 106 LYS 106 E B 58.7 - - 181.9 - - - - - - 175.4 - 34.4 - 107 VAL 107 E B 60.1 - - - - - - - - - 183.2 -2.7 32.6 - 108 VAL 108 E B 57.4 - - - - - - - - - 180.1 - 32.8 - 109 GLY 109 e - - - - - - - - - - - 179.3 -2.5 - - 110 ALA 110 B - - - - - - - - - - 177.9 -.6 34.6 - +* +* 111 LYS 111 h B - - -62.9 179.5 - - - - - - 182.6 -1.1 34.8 - * * 112 LYS 112 H A - 181.3 - 181.0 - -57.0 -50.5 - - - 180.5 - 35.0 - 113 ASP 113 H A - 170.9 - - - -64.1 -45.5 - - - 185.4 - 34.8 - 114 GLU 114 H A - 194.7 - - - -69.7 -34.6 - - - 177.6 - 33.2 - 115 LEU 115 H A - 184.5 - - - -61.2 -47.5 - - - 178.0 -2.7 35.7 - 116 GLN 116 H A - - -61.2 - - -57.9 -39.4 - - - 178.0 -1.9 33.9 - 117 SER 117 H A - 184.2 - - - -67.0 -41.1 - - - 177.9 -2.0 33.5 - 118 THR 118 H A - - -55.0 - - -64.8 -33.8 - - - 176.4 -2.7 33.7 - 119 ILE 119 H A - - -60.2 176.4 - -68.4 -46.7 - - - 179.2 -2.4 33.8 - 120 ALA 120 H A - - - - - -59.7 -34.1 - - - 177.4 -2.8 33.7 - 121 LYS 121 H A - 187.8 - 187.0 - -57.7 -41.7 - - - 180.4 -2.2 37.4 - 122 HIS 122 H A - - -70.7 - - -93.6 -6.1 - - - 184.5 -1.1 35.1 - ** +** * +** 123 LEU 123 h B - 201.2 - 173.4 - - - - - - 179.0 -.9 34.1 - * +* +* 124 ALA 124 - - - - - - - - - - - - - 34.5 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * ** ** ** +** +** * ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.2 183.9 -63.0 180.5 -70.0 -65.9 -39.0 56.6 - 2.0 179.7 -2.0 34.2 +** +** Standard deviations: 9.2 7.0 6.2 8.6 19.3 8.7 9.6 .0 - .0 3.0 .8 1.7 Numbers of values: 16 43 43 30 4 46 46 2 0 2 122 80 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_8 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_8 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 - 1.232 1.516 1.530 1.459 - 117.38 120.05 110.20 108.68 109.67 122.55 2 GLY 2 1.317 1.245 1.508 - 1.440 120.11 116.35 120.57 - 111.32 - 123.08 3 HIS 3 1.306 1.233 1.504 1.540 1.448 122.34 115.22 121.16 109.33 111.57 112.40 123.59 +* * +* 4 HIS 4 1.299 1.228 1.517 1.545 1.436 123.24 115.88 120.82 111.11 108.23 111.91 123.10 ** * * ** 5 HIS 5 1.305 1.227 1.506 1.561 1.453 123.02 116.93 120.14 108.81 109.94 112.80 122.86 +* +* * +* 6 HIS 6 1.313 1.239 1.505 1.551 1.456 121.62 115.91 121.24 110.37 112.54 114.18 122.82 * * ** ** 7 HIS 7 1.303 1.231 1.510 1.551 1.438 121.06 117.56 119.96 109.27 107.41 112.81 122.43 +* * * * * +* 8 HIS 8 1.319 1.233 1.518 1.561 1.453 119.35 113.08 122.30 113.66 112.70 115.19 124.42 +* * +* +* +** +** 9 LEU 9 1.300 1.252 1.498 1.568 1.441 126.59 119.17 118.92 110.26 104.19 113.87 121.90 ** * * +* +** * * +** +* +** 10 GLU 10 1.292 1.231 1.515 1.523 1.425 118.01 116.10 120.96 111.63 110.94 111.41 122.93 +** +* ** +** 11 MET 11 1.305 1.232 1.506 1.534 1.445 121.81 115.95 119.99 110.45 108.82 110.71 124.06 +* +* 12 ALA 12 1.327 1.239 1.518 1.535 1.459 123.96 114.91 121.80 112.21 110.63 113.00 123.19 * * +* +* Residue-by-residue listing for refined_8 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 1.298 1.238 1.531 1.527 1.430 122.76 116.47 120.35 112.26 111.06 107.93 123.17 ** * * +* ** 14 GLU 14 1.315 1.232 1.531 1.548 1.437 122.91 114.81 121.81 113.30 113.44 111.91 123.32 * +* +* 15 GLU 15 1.316 1.244 1.508 1.538 1.445 123.94 116.53 120.09 107.70 108.34 111.87 123.38 * * * * 16 GLY 16 1.318 1.227 1.503 - 1.451 121.07 116.89 120.50 - 114.18 - 122.60 17 GLN 17 1.302 1.237 1.485 1.509 1.429 121.18 115.54 120.89 109.79 109.12 112.07 123.57 +* +* * +* +* 18 VAL 18 1.276 1.238 1.522 1.548 1.429 122.08 117.64 119.93 109.68 107.59 110.73 122.43 +*** +* * +*** 19 ILE 19 1.314 1.220 1.516 1.544 1.432 120.73 116.35 121.04 110.55 109.71 109.91 122.60 * * * 20 ALA 20 1.296 1.238 1.502 1.517 1.433 121.47 115.99 120.84 110.98 109.53 110.80 123.16 ** * * ** 21 CYS 21 1.298 1.235 1.505 1.512 1.412 121.40 116.31 120.60 109.81 109.00 109.59 123.04 ** ** ** 22 HIS 22 1.298 1.223 1.507 1.536 1.444 121.41 115.36 121.40 110.71 109.44 111.63 123.23 ** ** 23 THR 23 1.315 1.248 1.515 1.556 1.439 122.84 116.80 119.93 108.01 108.53 111.56 123.27 * * 24 VAL 24 1.321 1.232 1.541 1.570 1.453 121.42 115.54 121.43 111.09 109.30 112.06 123.01 * * 25 GLU 25 1.336 1.225 1.521 1.515 1.449 122.37 116.44 120.40 109.41 110.85 109.90 123.14 26 THR 26 1.335 1.233 1.533 1.543 1.464 121.35 114.95 121.32 110.00 109.68 110.57 123.69 27 TRP 27 1.323 1.235 1.540 1.537 1.447 123.60 116.54 120.72 112.14 111.49 108.05 122.72 * * * * 28 ASN 28 1.317 1.229 1.527 1.551 1.463 121.61 115.82 120.52 111.12 110.21 109.92 123.61 * * 29 GLU 29 1.326 1.249 1.540 1.537 1.469 123.61 116.27 121.12 108.49 111.40 109.19 122.61 * * 30 GLN 30 1.322 1.239 1.507 1.485 1.409 121.80 116.99 120.16 111.61 113.20 110.12 122.85 ** +** +** 31 LEU 31 1.321 1.233 1.494 1.480 1.413 121.66 115.54 120.70 110.10 111.02 110.01 123.75 * +** ** +** 32 GLN 32 1.310 1.195 1.492 1.525 1.429 121.75 117.78 119.07 109.93 109.68 112.63 123.10 * +* +* * * * +* 33 LYS 33 1.337 1.228 1.525 1.535 1.454 120.03 116.71 120.25 110.00 110.43 113.11 123.02 +* +* 34 ALA 34 1.331 1.220 1.528 1.521 1.452 121.39 116.26 120.84 110.69 110.39 110.65 122.87 35 ASN 35 1.317 1.234 1.511 1.528 1.472 122.60 113.49 122.06 107.65 109.18 109.56 124.43 * * * 36 GLU 36 1.303 1.226 1.538 1.539 1.463 125.31 117.31 120.32 111.01 111.43 107.63 122.37 +* ** +* ** 37 SER 37 1.319 1.239 1.544 1.515 1.446 121.77 116.65 120.21 109.87 111.97 109.12 123.13 38 LYS 38 1.351 1.230 1.558 1.513 1.444 124.11 115.50 122.22 111.33 109.86 108.81 122.26 +* +* * +* 39 THR 39 1.302 1.241 1.532 1.525 1.436 122.19 114.79 121.36 109.25 110.87 110.97 123.79 +* * +* 40 LEU 40 1.294 1.238 1.549 1.550 1.449 124.42 116.95 120.33 110.46 109.15 108.18 122.67 ** * * +* * ** 41 VAL 41 1.319 1.225 1.541 1.563 1.442 121.84 117.29 120.45 112.32 110.72 110.75 122.24 * * 42 VAL 42 1.310 1.234 1.523 1.545 1.451 121.56 116.70 120.78 109.86 109.06 112.23 122.51 * * Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.308 1.227 1.527 1.556 1.452 121.26 115.91 120.57 108.79 111.59 111.05 123.51 +* +* 44 ASP 44 1.311 1.242 1.516 1.524 1.452 123.61 116.34 120.72 109.29 110.50 111.11 122.91 * * * 45 PHE 45 1.306 1.234 1.525 1.521 1.420 122.13 116.13 120.35 109.80 108.69 109.48 123.48 +* +* +* 46 THR 46 1.311 1.209 1.521 1.560 1.447 123.21 116.13 121.06 109.52 110.91 109.49 122.80 * * * * 47 ALA 47 1.288 1.237 1.510 1.519 1.439 122.42 117.29 119.64 110.40 106.75 111.15 123.07 +** * +* +** 48 SER 48 1.307 1.238 1.553 1.548 1.457 122.57 116.95 120.78 112.07 111.74 110.04 122.24 +* * * +* 49 TRP 49 1.330 1.235 1.538 1.551 1.458 121.76 117.14 120.79 111.27 112.80 111.91 122.06 * * 50 CYS 50 1.315 1.234 1.523 1.532 1.448 120.99 115.40 120.93 110.69 110.56 110.78 123.66 51 GLY 51 1.325 1.240 1.527 - 1.454 122.89 118.89 119.53 - 114.26 - 121.58 * * * 52 PRO 52 1.361 1.230 1.520 1.541 1.477 122.74 115.45 121.44 110.36 111.58 103.83 123.09 * * 53 CYS 53 1.309 1.221 1.536 1.510 1.440 122.36 116.12 121.20 109.76 109.76 109.24 122.65 * * 54 ARG 54 1.327 1.230 1.535 1.526 1.462 122.64 115.08 121.55 109.97 109.52 108.88 123.37 55 PHE 55 1.318 1.232 1.535 1.545 1.452 123.14 117.02 120.63 110.52 111.44 109.61 122.35 56 ILE 56 1.321 1.242 1.553 1.568 1.459 120.67 115.36 121.16 110.31 110.39 111.03 123.45 * * * 57 ALA 57 1.336 1.242 1.562 1.531 1.472 124.22 119.81 119.12 111.14 114.52 110.62 121.07 +* * +* * * +* 58 PRO 58 1.383 1.241 1.526 1.525 1.478 122.99 116.16 120.81 109.14 113.38 102.64 123.00 +** +** 59 PHE 59 1.318 1.224 1.533 1.533 1.440 121.53 116.45 120.93 111.23 110.85 110.43 122.60 60 PHE 60 1.314 1.233 1.529 1.534 1.462 121.77 115.88 121.29 111.85 109.48 109.75 122.82 * * 61 ALA 61 1.319 1.231 1.535 1.522 1.452 121.34 115.70 121.26 111.12 109.85 110.46 123.01 62 ASP 62 1.334 1.229 1.502 1.517 1.468 122.28 114.52 121.53 108.52 108.45 110.44 123.95 * * 63 LEU 63 1.320 1.235 1.533 1.530 1.438 123.96 115.75 120.94 110.96 110.76 108.74 123.29 * * * * 64 ALA 64 1.324 1.231 1.527 1.516 1.466 123.05 115.62 121.42 110.46 111.21 110.47 122.93 65 LYS 65 1.309 1.238 1.537 1.535 1.439 122.13 116.05 120.96 111.76 110.40 109.48 122.97 * * 66 LYS 66 1.323 1.235 1.525 1.534 1.462 122.02 116.65 120.49 109.41 111.48 111.02 122.85 67 LEU 67 1.316 1.225 1.535 1.550 1.432 122.07 117.54 120.76 110.92 109.07 111.34 121.68 * * * 68 PRO 68 1.343 1.227 1.539 1.524 1.464 122.69 118.08 120.38 110.28 115.09 102.69 121.53 * * 69 ASN 69 1.317 1.229 1.520 1.528 1.472 119.78 114.98 121.86 109.98 109.36 110.64 123.16 * * 70 VAL 70 1.306 1.239 1.510 1.553 1.437 122.51 115.94 120.73 111.11 109.46 110.83 123.31 +* * +* 71 LEU 71 1.306 1.224 1.506 1.542 1.410 121.85 116.12 120.83 109.22 110.23 110.96 123.04 +* +** +** 72 PHE 72 1.294 1.242 1.496 1.519 1.438 121.75 116.54 120.21 109.52 107.34 112.04 123.24 ** * * * ** 73 LEU 73 1.293 1.226 1.515 1.545 1.440 121.66 115.27 121.00 109.24 112.83 112.56 123.73 +** * +** Residue-by-residue listing for refined_8 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 1.321 1.241 1.503 1.523 1.418 124.33 116.68 120.34 107.50 108.31 109.67 122.96 * ** * * * ** 75 VAL 75 1.286 1.231 1.499 1.551 1.432 120.94 116.55 120.18 109.18 108.17 111.81 123.26 *** * * * *** 76 ASP 76 1.311 1.224 1.496 1.519 1.437 120.70 115.91 120.80 111.30 108.51 112.18 123.25 * * * * 77 THR 77 1.300 1.237 1.528 1.531 1.451 122.74 116.50 120.80 109.76 112.51 110.33 122.69 ** ** 78 ASP 78 1.309 1.238 1.506 1.518 1.438 120.97 114.88 121.38 110.89 108.01 110.73 123.73 * * * * 79 GLU 79 1.316 1.234 1.527 1.509 1.421 123.07 116.47 120.79 108.74 110.92 110.25 122.72 * +* +* 80 LEU 80 1.328 1.238 1.517 1.537 1.421 122.89 114.85 121.71 111.15 110.60 111.02 123.44 +* +* 81 LYS 81 1.306 1.238 1.536 1.562 1.444 123.24 116.72 120.93 114.44 113.31 110.90 122.28 +* +* ** ** 82 SER 82 1.312 1.235 1.526 1.516 1.442 121.19 115.84 121.00 111.18 110.05 109.91 123.12 * * 83 VAL 83 1.324 1.229 1.526 1.557 1.450 121.87 115.58 121.05 109.94 108.99 111.39 123.33 84 ALA 84 1.331 1.231 1.522 1.518 1.456 122.44 116.10 120.77 110.13 110.85 110.23 123.11 85 SER 85 1.323 1.231 1.534 1.526 1.448 121.78 116.30 120.98 110.61 111.14 109.59 122.68 86 ASP 86 1.324 1.224 1.534 1.527 1.463 121.80 116.56 120.89 111.06 111.18 110.16 122.54 87 TRP 87 1.326 1.242 1.523 1.523 1.457 121.91 116.15 120.17 110.60 112.78 111.92 123.68 88 ALA 88 1.342 1.239 1.527 1.537 1.477 123.90 116.13 120.89 110.99 111.63 110.90 122.90 * * * 89 ILE 89 1.321 1.234 1.523 1.558 1.442 121.70 115.60 121.29 109.97 109.57 112.20 123.03 90 GLN 90 1.309 1.238 1.521 1.521 1.437 122.61 115.96 121.29 110.73 110.83 109.93 122.75 * * * 91 ALA 91 1.304 1.229 1.504 1.515 1.433 122.00 116.38 120.83 110.93 108.97 110.98 122.77 +* * +* 92 MET 92 1.288 1.237 1.505 1.514 1.425 121.92 117.68 120.24 109.26 110.02 109.68 122.08 +** +* +** 93 PRO 93 1.326 1.233 1.526 1.520 1.457 123.46 116.61 120.98 109.87 111.54 102.51 122.36 94 THR 94 1.285 1.234 1.510 1.534 1.424 120.37 116.67 120.27 110.13 108.61 111.52 123.06 *** +* *** 95 PHE 95 1.313 1.227 1.496 1.521 1.411 121.53 116.78 120.26 109.11 107.93 110.11 122.95 * * ** * ** 96 MET 96 1.287 1.237 1.500 1.528 1.427 120.91 114.60 121.39 111.27 110.19 111.42 124.01 +** * +* +** 97 PHE 97 1.287 1.242 1.503 1.521 1.399 124.24 116.22 121.19 109.60 109.06 108.74 122.58 +** * *** * * *** 98 LEU 98 1.282 1.214 1.503 1.562 1.406 120.76 117.72 120.14 112.70 108.24 113.24 122.13 *** * +* +** * * +* *** 99 LYS 99 1.283 1.232 1.481 1.530 1.423 120.50 113.94 121.24 110.27 111.51 110.55 124.74 *** ** +* * * *** 100 GLU 100 1.323 1.230 1.541 1.526 1.445 124.21 115.94 121.13 111.48 111.52 109.54 122.87 * * 101 GLY 101 1.324 1.230 1.527 - 1.451 121.34 117.36 120.29 - 113.71 - 122.35 102 LYS 102 1.318 1.222 1.521 1.541 1.455 121.71 117.45 119.87 110.50 108.73 109.99 122.68 103 ILE 103 1.319 1.227 1.510 1.559 1.457 121.25 116.02 120.62 110.86 110.98 112.42 123.34 104 LEU 104 1.315 1.241 1.500 1.526 1.426 121.92 116.19 120.76 110.00 111.03 110.90 123.03 * * +* +* 105 ASP 105 1.308 1.218 1.488 1.509 1.432 121.20 115.11 121.44 109.85 112.56 111.94 123.42 +* +* * * +* Residue-by-residue listing for refined_8 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 ----------------------------------------------------------------------------------------------------------------------------------- 106 LYS 106 1.289 1.231 1.522 1.542 1.434 122.37 116.22 120.75 110.65 110.33 110.11 122.98 +** * +** 107 VAL 107 1.299 1.235 1.522 1.563 1.435 122.36 116.12 120.77 111.74 109.14 112.24 123.07 ** * * ** 108 VAL 108 1.302 1.245 1.543 1.559 1.436 121.93 115.59 121.41 111.97 111.85 110.53 122.99 +* * * +* 109 GLY 109 1.316 1.240 1.503 - 1.441 121.59 117.89 119.90 - 110.18 - 122.21 110 ALA 110 1.322 1.231 1.486 1.527 1.432 118.85 114.96 121.36 110.22 107.94 111.05 123.66 +* * +* * +* 111 LYS 111 1.289 1.235 1.501 1.522 1.399 122.93 116.59 119.93 111.87 108.35 109.14 123.46 +** * *** * *** 112 LYS 112 1.318 1.236 1.529 1.526 1.442 122.84 115.51 120.84 110.35 110.77 109.12 123.58 113 ASP 113 1.322 1.234 1.512 1.531 1.462 122.88 115.81 121.20 109.15 111.87 110.35 122.97 114 GLU 114 1.314 1.220 1.518 1.518 1.439 120.79 116.58 120.21 111.32 110.74 110.72 123.19 * * 115 LEU 115 1.330 1.218 1.500 1.513 1.454 121.59 115.07 121.06 108.25 109.04 110.59 123.87 * * 116 GLN 116 1.315 1.230 1.523 1.530 1.469 122.49 116.07 120.78 110.11 110.36 111.05 123.13 * * 117 SER 117 1.317 1.235 1.540 1.541 1.442 121.69 116.58 120.73 111.36 109.89 110.69 122.65 118 THR 118 1.333 1.240 1.546 1.556 1.448 121.96 116.39 121.17 110.60 109.88 111.22 122.42 * * 119 ILE 119 1.331 1.218 1.518 1.548 1.446 121.16 116.30 120.28 109.69 109.55 112.26 123.40 120 ALA 120 1.334 1.223 1.516 1.518 1.467 122.76 115.49 120.90 110.46 111.12 110.58 123.60 121 LYS 121 1.314 1.224 1.524 1.494 1.449 123.91 115.23 121.57 108.26 110.04 107.52 123.19 * +* * +* +* 122 HIS 122 1.307 1.230 1.522 1.522 1.441 122.70 117.29 120.03 108.61 112.50 110.29 122.68 +* +* 123 LEU 123 1.316 1.242 1.521 1.526 1.421 121.63 114.80 121.50 112.00 110.11 109.19 123.69 +* +* 124 ALA 124 1.296 - 1.504 1.529 1.428 123.69 - - 110.81 107.33 110.65 - ** +* * * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** +* ** +** *** +** +* * ** +** +** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 1.276 1.351 1.313 .014 +*** +* * C-N (Pro) 1.341 .016 4 1.326 1.383 1.353 .021 +** C-O C-O 1.231 .020 123 1.195 1.252 1.232 .008 +* * CA-C CH1E-C (except Gly) 1.525 .021 119 1.481 1.562 1.520 .016 ** +* CH2G*-C (Gly) 1.516 .018 5 1.503 1.527 1.513 .011 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.515 1.537 1.523 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.570 1.552 .011 * CH1E-CH2E (the rest) 1.530 .020 84 1.480 1.568 1.530 .016 +** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.399 1.477 1.443 .016 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.440 1.454 1.448 .006 N-CH1E (Pro) 1.466 .015 4 1.457 1.478 1.469 .009 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_8 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 2.0 114 113.08 119.81 116.13 .97 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.35 118.89 117.48 .87 * CH1E-C-N (Pro) 116.9 1.5 4 115.45 118.08 116.57 .96 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 121.07 124.74 123.02 .57 * * O-C-N (Pro) 122.0 1.4 4 121.53 123.09 122.50 .62 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.01 126.59 122.14 1.25 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.11 122.89 121.40 .90 * C-N-CH1E (Pro) 122.6 5.0 4 122.69 123.46 122.97 .31 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.92 122.30 120.80 .60 * CH2G*-C-O (Gly) 120.8 2.1 5 119.53 120.57 120.16 .39 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.13 112.21 110.81 .52 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.01 112.32 110.20 1.01 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.50 114.44 110.38 1.29 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.19 114.52 110.16 1.60 +** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.18 114.26 112.73 1.67 N-CH1E-C (Pro) 111.8 2.5 4 111.54 115.09 112.90 1.47 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.23 113.00 110.89 .66 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.49 112.42 111.23 .80 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.51 103.83 102.92 .53 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.52 115.19 110.57 1.49 +* +** ------------------------------------------------------------------------------------------------------------- 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_8 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 3.0 6.0 3.0 -1.0 BETTER 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 80 .8 .8 .2 .0 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 16 9.2 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 43 7.0 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 43 6.2 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 102 7.9 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 30 8.6 20.4 5.0 -2.4 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 86.7 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .80 2 Residue-by-residue listing for refined_8 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.22 Chi1-chi2 distribution -.03 Chi1 only -.06 Chi3 & chi4 .35 Omega .07 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths .00 Main-chain bond angles .45 ------ .26 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.