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 - - 184.1 - - - - - - - - 178.4 - 35.2 - 2 GLY 2 - - - - - - - - - - - 180.8 - - - 3 HIS 3 B - 184.6 - - - - - - - - 181.6 - 33.5 - 4 HIS 4 B 61.5 - - - - - - - - - 178.5 -1.0 31.4 - * * 5 HIS 5 B - 182.9 - - - - - - - - 182.6 - 34.7 - 6 HIS 6 b - 187.4 - - - - - - - - 177.5 - 33.1 - 7 HIS 7 ~b - 187.5 - - - - - - - - 177.9 -1.1 33.0 - ** * ** 8 HIS 8 S b 61.4 - - - - - - - - - 179.7 - 32.8 - 9 LEU 9 B - 183.7 - - - - - - - - 182.6 - 32.8 - 10 GLU 10 B - 189.2 - 169.0 - - - - - - 185.5 -1.0 34.3 - * * 11 MET 11 b - - -52.7 178.4 - - - - - - 174.4 -.5 36.4 - ** ** 12 ALA 12 B - - - - - - - - - - 179.4 - 34.1 - 13 SER 13 B - 185.1 - - - - - - - - 178.2 - 33.1 - 14 GLU 14 a - 186.5 - - - - - - - - 180.0 - 34.9 - 15 GLU 15 S B 66.0 - - - - - - - - - 178.4 - 34.1 - 16 GLY 16 S - - - - - - - - - - - 180.9 -2.6 - - 17 GLN 17 B 44.9 - - 177.7 - - - - - - 178.4 - 30.9 - * * 18 VAL 18 B - 185.7 - - - - - - - - 180.1 -.5 35.5 - ** ** 19 ILE 19 E B - - -59.2 - - - - - - - 178.7 -3.2 33.9 - +* +* 20 ALA 20 E B - - - - - - - - - - 180.5 -.8 34.2 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B 47.2 - - - - - - - - - 176.5 -1.3 33.2 - * * * 22 HIS 22 S A - - -60.2 - - - - - - - 181.0 - 34.4 - 23 THR 23 h B 54.6 - - - - - - - - - 182.9 - 33.6 - 24 VAL 24 H A 62.5 - - - - -72.5 -27.9 - - - 180.7 - 32.5 - * * 25 GLU 25 H A - 193.7 - - - -66.9 -47.1 - - - 177.0 - 34.2 - 26 THR 26 H A - - -58.7 - - -63.5 -41.5 - - - 175.5 - 34.3 - 27 TRP 27 H A - 164.8 - - - -53.2 -55.1 - - - 181.2 -2.0 35.0 - * * * * 28 ASN 28 H A - 182.9 - - - -65.3 -39.9 - - - 180.7 -3.0 34.8 - * * 29 GLU 29 H A - 180.2 - 173.8 - -61.8 -40.1 - - - 178.9 -2.7 33.5 - 30 GLN 30 H A - - -69.9 - - -70.9 -35.3 - - - 174.5 -2.4 32.7 - 31 LEU 31 H A - - -66.3 180.2 - -65.8 -40.2 - - - 174.8 -1.7 35.5 - 32 GLN 32 H A - 179.3 - 183.7 - -55.5 -46.0 - - - 176.8 -2.6 34.8 - 33 LYS 33 H A - - -73.7 - - -64.8 -39.5 - - - 177.0 -2.1 30.7 - 34 ALA 34 H A - - - - - -63.1 -39.4 - - - 179.3 -2.3 33.8 - 35 ASN 35 H A - 181.0 - - - -68.1 -54.8 - - - 183.4 -2.8 37.8 - * * * 36 GLU 36 H A - 174.3 - - - -59.8 -44.2 - - - 181.7 -3.5 32.5 - +* +* 37 SER 37 h A - - -59.9 - - - - - - - 177.8 -2.7 33.3 - 38 LYS 38 T l - - -61.7 179.6 - - - - - - 182.5 -.9 33.5 - * * 39 THR 39 t B - - -50.6 - - - - - - - 180.7 -1.2 35.0 - * * * 40 LEU 40 E B - 186.9 - 171.5 - - - - - - 183.7 -.6 34.6 - +* +* 41 VAL 41 E B 59.6 - - - - - - - - - 176.5 - 33.5 - 42 VAL 42 E B - 180.3 - - - - - - - - 183.7 -2.2 33.5 - 43 VAL 43 E B - 183.6 - - - - - - - - 176.5 -2.7 34.0 - 44 ASP 44 E B - 175.0 - - - - - - - - 176.3 -3.2 36.1 - +* +* 45 PHE 45 E B - - -61.1 - - - - - - - 186.1 -3.4 35.6 - * +* +* 46 THR 46 E B - 183.9 - - - - - - - - 177.0 -3.2 35.4 - +* +* 47 ALA 47 t B - - - - - - - - - - 183.0 - 34.1 - 48 SER 48 T A - - -53.0 - - - - - - - 179.4 - 33.7 - 49 TRP 49 T A 50.5 - - - - - - - - - 182.7 - 33.1 - 50 CYS 50 h B - 174.1 - 219.4 - - - 63.0 - 2.0 181.8 -1.8 34.0 - ** ** ** 51 GLY 51 H - - - - - - -66.1 -62.3 - - - 178.7 -.6 - - ** +* ** 52 PRO 52 H - - - - - -56.4 -56.4 -30.9 - - - 178.8 - 38.3 - * * 53 CYS 53 H A - - -54.9 - - -67.7 -40.8 63.0 - 2.0 177.7 - 35.1 - ** ** 54 ARG 54 H A - 183.4 - - - -64.9 -41.8 - - - 180.5 -1.6 34.8 - 55 PHE 55 H A - 175.7 - - - -64.9 -36.1 - - - 184.9 -2.4 34.1 - 56 ILE 56 H A - 193.8 - - - -87.5 -22.5 - - - 183.0 -1.9 34.2 - +* * +* 57 ALA 57 H A - - - - - -51.1 -46.3 - - - 181.0 -1.7 32.0 - * * 58 PRO 58 H - - - - - -53.5 -53.5 -32.3 - - - 180.2 - 38.6 - * * * 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 - 177.0 - - - -70.7 -35.5 - - - 182.1 -1.2 33.1 - * * 60 PHE 60 H A - 188.7 - - - -69.6 -35.3 - - - 177.4 -.9 33.9 - +* +* 61 ALA 61 H A - - - - - -73.9 -27.6 - - - 179.5 -1.7 34.3 - * * 62 ASP 62 H A - 185.0 - - - -73.5 -48.1 - - - 175.2 -1.4 35.9 - 63 LEU 63 H A - 205.5 - 178.0 - -54.4 -38.8 - - - 178.2 -3.1 37.5 - * * * * 64 ALA 64 H A - - - - - -58.7 -30.8 - - - 178.1 -1.5 32.4 - 65 LYS 65 H A - - -59.6 180.8 - -79.4 -29.2 - - - 186.5 -1.5 34.8 - * * * 66 LYS 66 H A - - -63.2 170.1 - -91.2 -3.9 - - - 181.6 -1.2 34.1 - ** *** * *** 67 LEU 67 h B 79.5 - - 183.1 - - - - - - 168.6 -.7 35.9 - +* +* +* 68 PRO 68 S - - - - - -71.7 - - - - - 173.0 - 38.2 - * * * 69 ASN 69 e b - 183.0 - - - - - - - - 185.1 - 32.8 - 70 VAL 70 E B - 179.5 - - - - - - - - 178.2 - 34.5 - 71 LEU 71 E B - 203.2 - 179.7 - - - - - - 182.3 -2.7 34.9 - * * 72 PHE 72 E B - - -58.2 - - - - - - - 178.0 -.6 35.2 - +* +* 73 LEU 73 E B - - -63.3 - - - - - - - 173.4 -1.6 33.8 - * * 74 LYS 74 E B - - -67.7 - - - - - - - 181.6 -2.2 36.4 - 75 VAL 75 E B - 179.7 - - - - - - - - 175.4 -3.4 34.6 - +* +* 76 ASP 76 E B - 180.6 - - - - - - - - 184.9 -.8 33.7 - +* +* 77 THR 77 e A 55.5 - - - - - - - - - 177.6 -3.2 33.8 - +* +* 78 ASP 78 T A - 183.5 - - - - - - - - 175.3 - 34.4 - 79 GLU 79 T A - - -73.4 186.1 - - - - - - 179.9 - 34.2 - 80 LEU 80 h b - - -70.3 - - - - - - - 185.4 -3.2 34.8 - +* +* 81 LYS 81 H A - 195.1 - 180.0 - -65.8 -39.3 - - - 177.3 -1.7 35.3 - 82 SER 82 H A - - -58.8 - - -64.5 -33.4 - - - 179.1 - 34.3 - 83 VAL 83 H A - 178.1 - - - -70.2 -41.8 - - - 177.6 - 34.2 - 84 ALA 84 H A - - - - - -59.2 -40.5 - - - 178.5 -2.2 34.1 - 85 SER 85 H A - - -56.2 - - -73.1 -30.7 - - - 181.5 -2.0 34.0 - 86 ASP 86 H A - 178.6 - - - -71.9 -37.0 - - - 178.5 -1.7 33.9 - 87 TRP 87 h A - - -66.2 - - - - - - - 180.3 -2.5 33.0 - 88 ALA 88 T l - - - - - - - - - - 181.0 - 31.2 - 89 ILE 89 t B - - -58.7 179.6 - - - - - - 179.3 -1.2 35.0 - * * 90 GLN 90 S A - 195.0 - - - - - - - - 184.5 - 35.1 - 91 ALA 91 S B - - - - - - - - - - 177.0 - 34.1 - 92 MET 92 S B - - -70.3 - - - - - - - -.8 - 33.9 - 93 PRO 93 e cis - - - - - -90.0 - - - - - 176.2 - 39.3 - ** +* ** 94 THR 94 E B - - -57.0 - - - - - - - 177.7 -2.9 34.6 - * * 95 PHE 95 E B - - -62.4 - - - - - - - 181.4 -2.4 36.3 - 96 MET 96 E B - 188.6 - 162.0 - - - - - - 185.7 -3.0 31.4 - * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 97 PHE 97 E B - - -67.7 - - - - - - - 179.6 -2.7 36.1 - 98 LEU 98 E B - - -56.7 - - - - - - - 173.4 -2.2 35.7 - * * 99 LYS 99 E B - 182.7 - 181.4 - - - - - - 183.3 -2.8 32.8 - * * 100 GLU 100 T l - - -56.8 180.5 - - - - - - 184.0 - 33.0 - 101 GLY 101 T - - - - - - - - - - - 179.6 - - - 102 LYS 102 E B - - -55.6 168.9 - - - - - - 183.4 -2.0 36.5 - 103 ILE 103 E B - - -65.1 170.8 - - - - - - 175.1 - 33.3 - 104 LEU 104 E a - - -62.6 182.8 - - - - - - 180.0 -1.8 33.6 - 105 ASP 105 E B 56.0 - - - - - - - - - 180.3 -2.5 31.8 - 106 LYS 106 E B 57.1 - - 180.6 - - - - - - 179.0 - 33.9 - 107 VAL 107 E B - 178.6 - - - - - - - - 180.1 -3.5 36.2 - ** ** 108 VAL 108 E B 59.7 - - - - - - - - - 182.0 -.5 32.2 - +* +* 109 GLY 109 e - - - - - - - - - - - 182.4 -3.1 - - * * 110 ALA 110 B - - - - - - - - - - 175.5 - 33.9 - 111 LYS 111 h B - - -59.8 184.8 - - - - - - 179.3 -1.0 36.0 - * * 112 LYS 112 H A - 180.6 - 177.1 - -69.2 -48.5 - - - 183.2 - 33.8 - 113 ASP 113 H A - 176.6 - - - -70.8 -43.2 - - - 179.4 - 32.2 - 114 GLU 114 H A - 182.8 - 180.2 - -65.3 -33.2 - - - 176.6 - 32.8 - 115 LEU 115 H A - 183.9 - - - -63.7 -53.5 - - - 178.0 -1.2 35.5 - * * * 116 GLN 116 H A - - -65.9 - - -56.5 -37.0 - - - 178.5 -2.4 33.0 - 117 SER 117 H A - - -55.9 - - -66.3 -40.2 - - - 178.3 -2.6 34.2 - 118 THR 118 H A - - -58.6 - - -69.1 -36.0 - - - 176.9 -2.2 34.2 - 119 ILE 119 H A - - -57.4 - - -62.6 -46.8 - - - 179.9 -2.6 33.6 - 120 ALA 120 H A - - - - - -66.5 -31.8 - - - 177.3 -2.6 32.9 - 121 LYS 121 H A - 181.8 - 188.1 - -59.9 -45.4 - - - 181.9 -1.9 37.6 - * * 122 HIS 122 H A - - -71.1 - - -83.4 -19.5 - - - 182.2 -2.0 33.8 - +* +* +* 123 LEU 123 h B - 202.5 - - - - - - - - 177.1 -1.6 35.8 - * * 124 ALA 124 - - - - - - - - - - - - -.5 34.5 - ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * ** ** ** *** ** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.3 184.1 -61.6 179.6 -67.9 -66.4 -38.5 63.0 - 2.0 179.6 -2.0 34.3 ** ** Standard deviations: 8.5 7.6 5.9 9.8 16.8 8.4 9.9 .0 - .0 3.1 .9 1.6 Numbers of values: 14 49 39 28 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 - 1.230 1.510 1.530 1.461 - 116.89 120.13 109.31 109.18 110.41 122.98 2 GLY 2 1.307 1.241 1.503 - 1.437 120.67 117.26 120.14 - 110.28 - 122.59 +* +* 3 HIS 3 1.303 1.237 1.515 1.534 1.438 120.32 116.01 121.06 111.14 109.07 111.29 122.91 +* * +* 4 HIS 4 1.306 1.233 1.510 1.556 1.440 120.78 115.46 121.16 111.48 111.03 113.37 123.36 +* * +* +* 5 HIS 5 1.293 1.238 1.503 1.546 1.432 122.58 116.24 120.37 111.15 107.30 110.33 123.34 +** * * * +** 6 HIS 6 1.313 1.230 1.519 1.538 1.445 121.14 115.18 120.61 110.60 110.68 111.79 124.15 * * 7 HIS 7 1.315 1.234 1.515 1.554 1.457 124.69 114.59 121.06 110.64 107.84 112.92 124.04 * * +* * * +* 8 HIS 8 1.307 1.237 1.508 1.579 1.460 124.95 117.59 119.82 110.58 107.98 113.51 122.57 +* ** +* * +* ** 9 LEU 9 1.307 1.233 1.514 1.526 1.440 120.06 115.32 121.37 111.18 109.33 112.02 123.24 +* +* 10 GLU 10 1.298 1.237 1.511 1.523 1.428 122.01 116.35 120.54 112.52 108.67 108.75 123.10 ** +* * * ** 11 MET 11 1.305 1.245 1.514 1.540 1.444 121.58 115.58 121.17 108.46 109.85 109.58 123.24 +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.305 1.243 1.513 1.520 1.431 121.95 117.45 119.97 111.03 108.04 110.74 122.58 +* * * +* 13 SER 13 1.299 1.236 1.530 1.535 1.426 120.16 115.45 121.15 111.28 110.08 111.42 123.37 ** +* ** 14 GLU 14 1.311 1.235 1.535 1.546 1.454 123.06 114.66 122.67 111.40 107.21 109.45 122.67 * * * * 15 GLU 15 1.314 1.240 1.517 1.554 1.431 122.86 116.68 120.51 110.23 108.77 111.61 122.77 * * * * 16 GLY 16 1.305 1.227 1.503 - 1.453 121.05 115.78 120.68 - 112.33 - 123.54 +* +* 17 GLN 17 1.314 1.243 1.473 1.510 1.421 121.80 112.85 122.34 111.68 113.05 112.87 124.79 * ** +* +* * * ** 18 VAL 18 1.268 1.232 1.523 1.548 1.422 124.21 118.28 119.45 109.66 107.05 110.55 122.27 **** +* * * * **** 19 ILE 19 1.308 1.223 1.519 1.543 1.441 120.24 116.82 120.68 109.84 110.13 111.73 122.48 * * 20 ALA 20 1.299 1.229 1.507 1.524 1.434 120.77 116.46 120.72 110.73 109.31 110.56 122.81 ** * ** 21 CYS 21 1.299 1.233 1.495 1.516 1.414 121.32 114.97 121.46 110.91 111.87 111.03 123.56 ** * ** ** 22 HIS 22 1.297 1.231 1.514 1.539 1.430 122.70 116.10 121.06 110.18 108.44 111.20 122.84 ** * ** 23 THR 23 1.330 1.244 1.517 1.548 1.441 121.39 116.37 120.48 110.27 110.37 111.66 123.15 24 VAL 24 1.324 1.229 1.533 1.569 1.456 121.71 116.50 120.80 110.97 111.34 112.15 122.67 * * 25 GLU 25 1.325 1.229 1.528 1.523 1.446 121.24 116.10 120.79 110.42 109.43 110.58 123.10 26 THR 26 1.334 1.234 1.534 1.542 1.455 122.01 115.55 120.85 110.42 109.79 110.48 123.59 27 TRP 27 1.329 1.235 1.536 1.543 1.458 123.17 115.93 120.89 111.13 111.14 108.35 123.14 * * 28 ASN 28 1.314 1.221 1.524 1.525 1.454 122.18 115.87 120.92 109.97 110.87 109.80 123.20 * * 29 GLU 29 1.314 1.234 1.536 1.523 1.461 122.74 117.18 120.60 110.97 112.47 109.98 122.23 * * 30 GLN 30 1.318 1.230 1.513 1.490 1.418 121.05 116.27 120.73 112.28 111.74 109.95 122.99 ** ** * ** 31 LEU 31 1.320 1.230 1.514 1.489 1.416 122.40 115.20 121.01 110.02 109.67 108.92 123.79 ** ** ** 32 GLN 32 1.323 1.218 1.521 1.527 1.450 123.30 116.38 120.65 110.00 109.55 110.10 122.96 33 LYS 33 1.321 1.237 1.518 1.530 1.455 121.72 117.06 120.03 112.51 112.77 112.13 122.90 * * 34 ALA 34 1.324 1.223 1.528 1.520 1.453 120.93 115.40 121.15 110.70 109.76 110.64 123.43 35 ASN 35 1.317 1.235 1.512 1.525 1.462 123.51 114.30 121.39 107.25 110.63 108.20 124.29 * * * * 36 GLU 36 1.310 1.228 1.515 1.570 1.463 123.80 117.36 120.47 113.45 112.53 109.28 122.10 * ** * +* ** 37 SER 37 1.301 1.244 1.531 1.506 1.427 120.32 116.07 120.65 112.32 112.07 109.03 123.28 ** * +* * ** 38 LYS 38 1.347 1.233 1.527 1.519 1.477 123.86 115.19 121.53 111.00 111.66 110.10 123.20 * * * 39 THR 39 1.305 1.238 1.525 1.527 1.427 122.71 114.94 121.59 109.67 109.67 110.29 123.45 +* +* +* 40 LEU 40 1.279 1.240 1.540 1.565 1.438 123.50 116.60 120.50 112.98 107.70 108.44 122.89 +*** +* * +* * * +*** 41 VAL 41 1.311 1.238 1.533 1.567 1.436 121.49 116.10 121.05 111.15 111.36 110.82 122.83 * * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.305 1.240 1.507 1.543 1.439 121.90 116.38 120.76 109.86 108.20 112.88 122.85 +* * +* 43 VAL 43 1.300 1.240 1.518 1.547 1.431 120.67 114.95 120.98 109.52 111.11 111.74 124.06 ** * ** 44 ASP 44 1.303 1.236 1.510 1.530 1.442 124.12 116.48 120.70 109.27 108.53 109.41 122.71 +* * +* 45 PHE 45 1.293 1.232 1.509 1.512 1.415 121.50 116.63 120.55 109.55 107.38 110.09 122.79 +** ** * +** 46 THR 46 1.283 1.224 1.524 1.564 1.420 121.04 115.84 121.11 110.23 110.26 109.50 123.06 *** ** * *** 47 ALA 47 1.293 1.242 1.506 1.521 1.422 122.86 116.45 120.33 111.19 107.23 110.89 123.21 +** +* * +** 48 SER 48 1.304 1.233 1.549 1.525 1.455 122.30 116.61 120.77 111.43 111.98 109.33 122.58 +* * +* 49 TRP 49 1.324 1.229 1.539 1.551 1.467 122.35 116.48 121.07 111.20 112.36 110.49 122.45 * * 50 CYS 50 1.307 1.238 1.530 1.523 1.448 121.93 115.45 120.87 111.28 111.62 109.26 123.67 +* +* 51 GLY 51 1.327 1.230 1.529 - 1.463 122.77 119.02 119.67 - 114.06 - 121.31 * * * * 52 PRO 52 1.360 1.228 1.533 1.542 1.477 122.73 115.80 121.18 110.46 111.84 103.97 123.00 * * 53 CYS 53 1.315 1.226 1.534 1.518 1.450 122.71 115.65 121.14 110.25 109.87 109.18 123.18 54 ARG 54 1.323 1.224 1.523 1.570 1.456 123.21 115.37 121.21 113.67 107.96 107.45 123.35 ** +* * +* ** 55 PHE 55 1.316 1.241 1.544 1.539 1.461 123.20 117.05 120.61 110.43 113.12 109.53 122.34 56 ILE 56 1.314 1.240 1.553 1.570 1.457 120.87 115.50 121.13 110.34 110.70 110.69 123.31 * * * * 57 ALA 57 1.330 1.237 1.558 1.518 1.472 124.12 120.27 118.70 110.78 115.49 110.70 121.02 +* * ** * +* * ** 58 PRO 58 1.383 1.232 1.527 1.525 1.478 122.47 116.66 120.47 109.98 113.03 103.59 122.85 +** +** 59 PHE 59 1.331 1.221 1.518 1.540 1.451 121.29 116.69 120.58 110.24 111.15 111.94 122.71 60 PHE 60 1.314 1.231 1.533 1.536 1.451 121.10 115.59 121.34 111.49 109.42 110.04 123.04 * * 61 ALA 61 1.323 1.230 1.534 1.520 1.460 122.08 115.21 121.64 110.56 110.22 109.94 123.15 62 ASP 62 1.313 1.236 1.507 1.515 1.463 123.26 114.34 121.49 109.84 109.11 108.69 124.17 * * * 63 LEU 63 1.317 1.231 1.537 1.535 1.441 125.10 115.24 121.40 110.50 108.25 105.94 123.34 +* * +** +** 64 ALA 64 1.320 1.210 1.528 1.518 1.444 123.42 118.08 119.92 111.20 112.34 111.36 121.92 * * 65 LYS 65 1.329 1.238 1.531 1.528 1.473 120.92 115.33 121.28 108.28 111.14 111.14 123.39 66 LYS 66 1.315 1.244 1.521 1.517 1.464 123.74 115.64 120.54 111.37 112.83 108.65 123.79 * * * * 67 LEU 67 1.315 1.233 1.543 1.560 1.461 123.75 118.24 120.84 108.06 112.00 110.09 120.86 * +* * * * * +* 68 PRO 68 1.329 1.239 1.533 1.541 1.447 121.02 115.13 121.14 111.32 107.40 104.18 123.70 * * +* * * +* 69 ASN 69 1.333 1.225 1.528 1.536 1.454 124.22 116.13 121.25 111.40 108.86 112.01 122.50 * * 70 VAL 70 1.321 1.230 1.523 1.564 1.465 122.49 116.89 120.45 108.93 110.77 111.65 122.65 71 LEU 71 1.309 1.236 1.553 1.556 1.443 121.10 116.98 120.50 111.75 106.63 109.24 122.48 * * * +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 PHE 72 1.321 1.240 1.517 1.524 1.470 122.05 116.65 120.27 107.41 110.64 111.74 123.09 * * 73 LEU 73 1.320 1.228 1.531 1.543 1.453 122.20 116.17 120.36 108.02 111.62 113.00 123.46 * * * 74 LYS 74 1.332 1.237 1.515 1.529 1.431 124.23 117.04 120.30 108.24 107.46 110.18 122.65 * * * * 75 VAL 75 1.293 1.226 1.514 1.554 1.440 121.29 116.47 120.40 109.33 110.58 111.18 123.12 +** +** 76 ASP 76 1.321 1.230 1.510 1.527 1.457 121.25 115.98 120.68 110.61 108.33 111.61 123.32 * * 77 THR 77 1.306 1.232 1.519 1.533 1.452 123.55 116.78 120.68 109.85 112.96 110.76 122.49 +* * +* 78 ASP 78 1.301 1.228 1.515 1.514 1.439 120.69 115.37 121.31 110.94 108.00 110.16 123.32 +* * * +* 79 GLU 79 1.319 1.226 1.513 1.517 1.430 122.72 116.35 120.81 109.74 110.70 111.06 122.82 * * 80 LEU 80 1.322 1.237 1.519 1.530 1.432 123.41 113.99 122.13 110.66 108.86 109.88 123.83 * * * 81 LYS 81 1.298 1.235 1.534 1.518 1.430 124.34 115.92 121.08 111.57 110.37 107.54 122.97 ** * * +* ** 82 SER 82 1.324 1.236 1.534 1.521 1.450 122.25 115.88 120.94 110.62 110.62 109.85 123.15 83 VAL 83 1.326 1.225 1.522 1.552 1.452 122.53 115.88 120.95 110.14 109.45 111.22 123.13 84 ALA 84 1.324 1.218 1.522 1.519 1.460 122.26 116.26 121.11 110.49 110.27 110.29 122.61 85 SER 85 1.311 1.228 1.541 1.519 1.441 121.22 116.41 120.71 111.43 111.23 109.28 122.85 * * 86 ASP 86 1.325 1.234 1.530 1.540 1.471 122.58 116.21 120.91 110.79 111.45 110.05 122.84 87 TRP 87 1.321 1.244 1.524 1.527 1.456 122.31 114.80 120.90 111.16 111.37 110.99 124.28 88 ALA 88 1.333 1.233 1.521 1.522 1.458 124.80 115.34 121.49 111.95 112.10 112.30 123.09 +* * +* 89 ILE 89 1.305 1.242 1.505 1.552 1.442 123.08 115.76 120.86 109.49 109.26 110.87 123.35 +* +* 90 GLN 90 1.310 1.234 1.519 1.558 1.441 121.27 115.80 121.19 111.14 108.07 109.48 122.99 * * * * 91 ALA 91 1.318 1.228 1.508 1.523 1.439 121.36 115.57 121.17 110.34 111.61 110.34 123.26 * * 92 MET 92 1.295 1.238 1.513 1.505 1.425 122.28 119.04 119.76 110.55 110.17 110.68 121.19 ** * +* * * ** 93 PRO 93 1.333 1.236 1.521 1.524 1.451 124.14 116.33 121.17 110.35 111.68 102.71 122.43 * * 94 THR 94 1.282 1.224 1.517 1.526 1.410 120.90 116.41 120.68 110.26 109.04 110.64 122.91 *** +** *** 95 PHE 95 1.298 1.226 1.480 1.522 1.410 122.23 117.50 120.13 108.80 106.47 110.29 122.35 ** ** +** +* +** 96 MET 96 1.274 1.239 1.495 1.531 1.416 118.90 114.12 121.61 115.11 109.71 110.24 124.24 +*** * ** +* * +** +*** 97 PHE 97 1.295 1.247 1.499 1.516 1.397 124.35 115.45 121.39 110.30 110.20 108.22 123.14 ** * *** * * *** 98 LEU 98 1.289 1.222 1.524 1.560 1.416 121.64 117.11 120.52 107.52 107.86 112.34 122.37 +** +* ** * * * +** 99 LYS 99 1.295 1.215 1.502 1.532 1.440 121.25 116.07 120.03 110.95 107.81 112.89 123.82 ** * * * ** 100 GLU 100 1.326 1.226 1.542 1.536 1.476 124.52 116.00 121.23 109.28 110.75 112.82 122.76 +* * +* 101 GLY 101 1.318 1.230 1.524 - 1.453 121.38 115.75 121.10 - 111.40 - 123.15 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 ----------------------------------------------------------------------------------------------------------------------------------- 102 LYS 102 1.318 1.235 1.517 1.519 1.449 123.12 116.51 120.15 109.38 108.27 108.50 123.34 * * * 103 ILE 103 1.308 1.247 1.527 1.554 1.457 122.67 115.32 121.35 110.53 112.79 110.89 123.31 * * 104 LEU 104 1.317 1.234 1.515 1.525 1.420 122.02 116.37 120.59 111.03 109.67 111.07 123.03 +* +* 105 ASP 105 1.331 1.230 1.511 1.520 1.450 121.53 115.51 121.20 110.21 112.95 112.98 123.26 * * 106 LYS 106 1.319 1.231 1.539 1.546 1.459 122.62 116.53 120.94 110.48 111.31 110.50 122.53 107 VAL 107 1.308 1.222 1.514 1.565 1.458 122.65 116.82 120.20 107.99 108.38 110.78 122.97 +* * +* 108 VAL 108 1.311 1.248 1.541 1.567 1.439 121.65 115.57 121.67 112.31 111.06 111.46 122.73 * * * * * 109 GLY 109 1.305 1.233 1.502 - 1.434 121.49 117.68 120.02 - 109.99 - 122.30 +* * +* 110 ALA 110 1.310 1.244 1.509 1.522 1.433 119.16 114.72 121.74 110.76 110.51 110.50 123.54 * * * * 111 LYS 111 1.298 1.224 1.496 1.513 1.416 123.15 117.39 119.62 108.01 107.52 111.02 123.00 ** * ** * * ** 112 LYS 112 1.296 1.231 1.538 1.526 1.424 121.09 116.41 120.86 111.45 110.62 109.88 122.67 ** +* ** 113 ASP 113 1.325 1.231 1.527 1.528 1.466 121.63 117.66 120.21 110.77 113.18 111.73 122.13 114 GLU 114 1.326 1.242 1.523 1.530 1.473 120.59 116.11 120.84 111.13 110.21 111.63 123.04 115 LEU 115 1.326 1.219 1.505 1.516 1.442 121.48 115.30 120.84 109.17 108.37 110.34 123.81 * * 116 GLN 116 1.323 1.236 1.525 1.528 1.469 122.55 116.61 120.34 110.16 112.14 111.54 123.04 117 SER 117 1.326 1.230 1.528 1.538 1.457 121.64 115.71 121.22 110.57 109.53 110.61 123.05 118 THR 118 1.315 1.236 1.537 1.538 1.436 122.27 116.29 120.96 110.84 110.14 110.18 122.74 * * 119 ILE 119 1.324 1.220 1.521 1.558 1.446 121.22 116.46 120.34 109.46 109.33 112.91 123.13 120 ALA 120 1.332 1.220 1.521 1.519 1.461 121.75 116.16 120.63 111.18 111.02 111.05 123.21 121 LYS 121 1.321 1.230 1.517 1.502 1.462 122.62 114.73 121.79 107.01 109.97 108.49 123.47 * +* * +* 122 HIS 122 1.311 1.230 1.512 1.527 1.434 122.38 117.27 120.03 109.97 112.71 110.77 122.69 * * * 123 LEU 123 1.320 1.242 1.527 1.510 1.409 121.52 115.38 121.12 111.09 109.57 107.59 123.46 * +** +* +** 124 ALA 124 1.299 - 1.504 1.526 1.430 123.16 - - 110.76 107.53 110.71 - ** * * ** ----------------------------------------------------------------------------------------------------------------------------------- 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 1.268 1.347 1.312 .013 **** * * C-N (Pro) 1.341 .016 4 1.329 1.383 1.351 .022 +** C-O C-O 1.231 .020 123 1.210 1.248 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.473 1.558 1.521 .014 ** +* CH2G*-C (Gly) 1.516 .018 5 1.502 1.529 1.512 .012 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.518 1.526 1.521 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.526 1.570 1.551 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.489 1.579 1.531 .017 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.397 1.477 1.444 .017 *** NH1-CH2G* (Gly) 1.451 .016 5 1.434 1.463 1.448 .011 * N-CH1E (Pro) 1.466 .015 4 1.447 1.478 1.463 .014 * ------------------------------------------------------------------------------------------------------------- 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 2.0 114 112.85 120.27 116.10 1.02 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.75 119.02 117.10 1.23 * CH1E-C-N (Pro) 116.9 1.5 4 115.13 116.66 115.98 .58 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.86 124.79 123.02 .62 * * O-C-N (Pro) 122.0 1.4 4 122.43 123.70 123.00 .46 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.90 125.10 122.22 1.24 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.67 122.77 121.47 .71 * C-N-CH1E (Pro) 122.6 5.0 4 121.02 124.14 122.59 1.11 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.70 122.67 120.84 .57 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.67 121.10 120.32 .51 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.34 111.95 110.90 .40 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.99 112.31 110.05 .85 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.01 115.11 110.53 1.41 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 106.47 115.49 110.10 1.74 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 5 109.99 114.06 111.61 1.48 N-CH1E-C (Pro) 111.8 2.5 4 107.40 113.03 110.99 2.13 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.94 112.30 110.77 .56 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.50 112.91 111.14 .81 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.71 104.18 103.61 .56 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 105.94 113.51 110.35 1.52 +** +* ------------------------------------------------------------------------------------------------------------- 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] 102 90.3% Residues in additional allowed regions [a,b,l,p] 10 8.8% Residues in generously allowed regions [~a,~b,~l,~p] 1 .9% 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 90.3 83.8 10.0 .6 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 1.6 3.1 1.6 -1.0 Inside e. H-bond energy st dev 80 .9 .8 .2 .3 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 14 8.5 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 49 7.6 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 39 5.9 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 102 8.1 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 28 9.8 20.4 5.0 -2.1 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% 90.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 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 -.24 Chi1 only .14 Chi3 & chi4 .62 Omega .11 ------ .00 ===== Main-chain covalent forces:- Main-chain bond lengths .02 Main-chain bond angles .43 ------ .26 ===== OVERALL AVERAGE .09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.