Residue-by-residue listing for refined_17 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 - - - -64.1 - - - - - - - 178.7 - 34.2 - 2 GLY 2 - - - - - - - - - - - 178.2 - - - 3 HIS 3 l - - -58.3 - - - - - - - 180.0 - 32.7 - 4 HIS 4 b 64.0 - - - - - - - - - 182.5 - 30.0 - * * 5 HIS 5 A 53.8 - - - - - - - - - 178.8 -1.2 31.9 - * * 6 HIS 6 l - 184.0 - - - - - - - - 175.6 - 32.2 - 7 HIS 7 b - 183.1 - - - - - - - - 176.1 - 32.7 - 8 HIS 8 b 51.9 - - - - - - - - - 177.8 - 28.1 - +* +* 9 LEU 9 S a - 181.8 - - - - - - - - 178.9 - 35.2 - 10 GLU 10 S b - - -58.9 176.6 - - - - - - 179.9 - 33.5 - 11 MET 11 S B 58.7 - - 178.0 - - - - - - 183.3 -1.2 34.9 - * * 12 ALA 12 S l - - - - - - - - - - 187.0 - 31.9 - * * 13 SER 13 b - - -54.9 - - - - - - - 176.8 - 34.2 - 14 GLU 14 b - 190.6 - - - - - - - - 182.3 - 33.8 - 15 GLU 15 B 60.5 - - 181.1 - - - - - - 178.6 -1.6 35.1 - 16 GLY 16 S - - - - - - - - - - - 183.7 -1.9 - - 17 GLN 17 e B 52.7 - - - - - - - - - 178.4 -.5 27.4 - ** +* ** 18 VAL 18 E B 69.6 - - - - - - - - - 182.8 - 33.7 - 19 ILE 19 E B - - -60.4 176.8 - - - - - - 177.7 -3.5 34.8 - +* +* 20 ALA 20 E B - - - - - - - - - - 178.5 -.8 34.3 - +* +* Residue-by-residue listing for refined_17 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 - - -56.6 - - - - - - - 180.7 -.8 34.6 - +* +* 22 HIS 22 S A - - -60.2 - - - - - - - 182.3 -.5 34.3 - ** ** 23 THR 23 h B 50.9 - - - - - - - - - 179.6 - 34.5 - 24 VAL 24 H A 64.5 - - - - -70.3 -22.9 - - - 175.9 - 32.3 - * * 25 GLU 25 H A - - -69.8 - - -55.9 -49.9 - - - 178.4 - 36.3 - 26 THR 26 H A - - -53.8 - - -70.0 -42.8 - - - 180.7 - 35.5 - 27 TRP 27 H A - 171.6 - - - -52.8 -53.9 - - - 181.8 -2.1 35.3 - * * * 28 ASN 28 H A - 181.7 - - - -61.8 -41.6 - - - 181.4 -3.2 35.0 - +* +* 29 GLU 29 H A - 182.0 - 176.1 - -65.0 -41.3 - - - 179.3 -1.4 33.4 - 30 GLN 30 H A - - -63.2 - - -63.9 -40.6 - - - 177.2 -2.7 34.1 - 31 LEU 31 H A - - -66.5 180.1 - -67.3 -41.8 - - - 175.6 -2.0 35.1 - 32 GLN 32 H A - 178.2 - - - -56.9 -44.3 - - - 177.4 -2.5 34.1 - 33 LYS 33 H A - 177.6 - 179.3 - -63.4 -45.2 - - - 180.4 -2.6 34.0 - 34 ALA 34 H A - - - - - -63.6 -42.2 - - - 178.9 -2.6 33.8 - 35 ASN 35 H A - 185.1 - - - -60.5 -53.1 - - - 181.7 -3.1 37.4 - * * * 36 GLU 36 H A - 179.2 - 182.8 - -59.5 -42.3 - - - 183.9 -2.8 35.5 - 37 SER 37 H A - - -52.1 - - -87.2 -8.0 - - - 183.6 -2.5 35.7 - +* +** +** 38 LYS 38 h L - - -60.7 182.1 - - - - - - 181.4 -.9 33.1 - * * 39 THR 39 e B - - -50.8 - - - - - - - 179.4 -2.3 35.3 - * * 40 LEU 40 E B - 180.9 - 166.7 - - - - - - 183.1 - 34.0 - 41 VAL 41 E B 59.3 - - - - - - - - - 179.1 -1.1 33.1 - * * 42 VAL 42 E B - 181.8 - - - - - - - - 182.8 -2.7 34.4 - 43 VAL 43 E B - 183.0 - - - - - - - - 176.8 -3.0 34.9 - * * 44 ASP 44 E B - 169.5 - - - - - - - - 176.7 -3.1 34.8 - * * 45 PHE 45 E B - - -64.1 - - - - - - - 188.6 -3.2 34.8 - * * * 46 THR 46 E B - 187.6 - - - - - - - - 175.9 -3.3 37.0 - +* +* 47 ALA 47 t B - - - - - - - - - - 181.9 - 34.3 - 48 SER 48 T A - - -56.3 - - - - - - - 179.1 - 32.7 - 49 TRP 49 T A 52.7 - - - - - - - - - 177.2 - 31.5 - 50 CYS 50 h B 51.5 - - - - - - - -110.7 2.0 184.6 -1.6 28.9 - ** * ** 51 GLY 51 H - - - - - - -52.0 -62.2 - - - 181.5 -.6 - - * ** +* ** 52 PRO 52 H - - - - - -57.0 -57.0 -30.3 - - - 181.0 - 38.4 - * * 53 CYS 53 H A - - -45.2 152.8 - -70.3 -42.7 - -110.7 2.0 182.6 - 37.1 - * * ** ** 54 ARG 54 H A - 193.9 - - - -73.9 -29.6 - - - 178.1 -2.1 35.0 - 55 PHE 55 H A - 179.4 - - - -70.8 -31.8 - - - 183.2 -2.3 34.8 - 56 ILE 56 H A - 192.4 - - - -87.2 -18.5 - - - 180.5 -1.5 33.7 - +* +* +* 57 ALA 57 H A - - - - - -53.2 -48.5 - - - 179.0 -1.1 31.5 - * * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 PRO 58 H - - - - - -58.0 -58.0 -32.6 - - - 180.5 - 38.9 - * * 59 PHE 59 H A - 183.6 - - - -73.7 -41.8 - - - 177.6 -.6 34.0 - +* +* 60 PHE 60 H A - 183.8 - - - -66.6 -33.7 - - - 176.6 -2.1 34.2 - 61 ALA 61 H A - - - - - -65.9 -29.1 - - - 178.6 -2.6 34.0 - 62 ASP 62 H A - 185.9 - - - -74.0 -44.5 - - - 176.8 -1.0 35.4 - * * 63 LEU 63 H A - - -62.9 181.9 - -55.9 -47.2 - - - 177.4 -2.2 35.2 - 64 ALA 64 H A - - - - - -61.0 -31.6 - - - 182.1 -2.7 34.2 - 65 LYS 65 H A - 186.9 - 183.2 - -77.5 -35.1 - - - 182.5 -1.0 33.3 - * * * 66 LYS 66 H A - 186.7 - 180.2 - -75.4 -29.5 - - - 178.3 -2.2 32.7 - 67 LEU 67 h b - - -67.4 170.8 - - - - - - 183.3 -1.8 32.8 - 68 PRO 68 S - - - - - -73.4 - - - - - 182.9 - 39.5 - +* +* 69 ASN 69 S A 63.5 - - - - - - - - - 180.7 - 34.9 - 70 VAL 70 S B - 178.4 - - - - - - - - 180.7 - 33.8 - 71 LEU 71 E B - - -72.1 - - - - - - - 174.8 -1.4 34.0 - 72 PHE 72 E B - - -60.6 - - - - - - - 182.3 -.7 34.7 - +* +* 73 LEU 73 E B - - -74.9 - - - - - - - 178.2 -3.0 32.6 - * * 74 LYS 74 E B - 196.1 - - - - - - - - 179.7 -1.8 37.0 - 75 VAL 75 E B - 177.6 - - - - - - - - 177.4 -3.2 33.9 - +* +* 76 ASP 76 E B - 191.1 - - - - - - - - 186.4 -.6 34.3 - * +* +* 77 THR 77 e A 54.4 - - - - - - - - - 174.2 -2.5 31.8 - 78 ASP 78 T A - 183.1 - - - - - - - - 180.2 - 33.1 - 79 GLU 79 T A - - -66.7 - - - - - - - 181.3 - 35.5 - 80 LEU 80 h b - 184.8 - - - - - - - - 188.3 -3.5 33.3 - * +* +* 81 LYS 81 H A - 193.8 - 179.7 - -69.1 -41.9 - - - 182.9 -.8 34.6 - +* +* 82 SER 82 H A - - -53.6 - - -63.9 -44.3 - - - 180.2 - 33.7 - 83 VAL 83 H A - 177.3 - - - -69.3 -37.7 - - - 177.2 - 32.6 - 84 ALA 84 H A - - - - - -62.7 -35.1 - - - 177.7 -1.6 34.2 - 85 SER 85 H A - 183.1 - - - -75.7 -37.5 - - - 181.1 -1.9 34.0 - 86 ASP 86 H A - 178.5 - - - -65.9 -37.1 - - - 179.4 -2.5 34.1 - 87 TRP 87 h A - - -67.7 - - - - - - - 180.4 -2.5 33.0 - 88 ALA 88 T l - - - - - - - - - - 178.2 -.6 31.1 - +* +* 89 ILE 89 t B - - -56.7 - - - - - - - 182.5 -2.2 34.5 - 90 GLN 90 A 70.1 - - - - - - - - - 182.4 -1.0 32.2 - * * 91 ALA 91 S B - - - - - - - - - - 180.6 - 32.9 - 92 MET 92 S B - - -59.6 175.9 - - - - - - -.2 - 36.0 - 93 PRO 93 e cis - - - - - -86.1 - - - - - 177.7 - 39.6 - +* +* +* 94 THR 94 E B - 187.8 - - - - - - - - 183.7 -2.3 32.4 - 95 PHE 95 E B - - -59.9 - - - - - - - 179.2 -2.7 36.8 - 96 MET 96 E B - 177.7 - 183.7 - - - - - - 181.9 -3.7 34.3 - ** ** 97 PHE 97 E B - - -65.7 - - - - - - - 179.9 -3.0 36.3 - * * Residue-by-residue listing for refined_17 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 - - -50.9 177.1 - - - - - - 176.3 -2.8 37.1 - * * * 99 LYS 99 E B - 177.4 - 174.6 - - - - - - 179.8 -3.2 32.5 - +* +* 100 GLU 100 e l - - -58.0 172.8 - - - - - - 182.4 -.6 33.6 - +* +* 101 GLY 101 T - - - - - - - - - - - 177.2 - - - 102 LYS 102 E B - - -75.7 - - - - - - - 180.4 -2.3 34.5 - 103 ILE 103 E B - - -61.4 175.5 - - - - - - 176.1 - 34.2 - 104 LEU 104 E a - - -67.5 187.6 - - - - - - 187.9 -1.9 33.6 - * * 105 ASP 105 E B 46.2 - - - - - - - - - 184.3 -2.1 31.8 - * * 106 LYS 106 E B - 188.8 - 181.4 - - - - - - 179.1 - 35.6 - 107 VAL 107 E B - 180.4 - - - - - - - - 179.5 -3.5 35.2 - +* +* 108 VAL 108 E B - 181.5 - - - - - - - - 180.5 -.5 34.4 - ** ** 109 GLY 109 e - - - - - - - - - - - 178.1 -2.6 - - 110 ALA 110 B - - - - - - - - - - 178.5 - 34.1 - 111 LYS 111 h B - - -60.6 183.0 - - - - - - 187.1 -1.0 35.8 - * * * 112 LYS 112 H A - 185.3 - 175.8 - -67.9 -45.1 - - - 181.7 -.5 32.5 - ** ** 113 ASP 113 H A - 185.8 - - - -72.6 -48.2 - - - 181.5 - 33.1 - 114 GLU 114 H A - 185.7 - 178.9 - -65.3 -29.9 - - - 176.9 - 31.8 - 115 LEU 115 H A - 186.4 - - - -63.8 -51.3 - - - 178.0 -1.8 35.0 - * * 116 GLN 116 H A - - -62.5 180.2 - -59.0 -36.0 - - - 177.1 -1.7 32.6 - 117 SER 117 H A - - -57.1 - - -65.2 -37.3 - - - 178.1 -2.3 34.2 - 118 THR 118 H A - - -55.1 - - -71.7 -31.9 - - - 174.9 -2.1 33.9 - 119 ILE 119 H A - - -60.2 178.0 - -65.3 -48.3 - - - 177.9 -2.1 33.8 - 120 ALA 120 H A - - - - - -60.2 -33.8 - - - 175.8 -2.8 33.8 - * * 121 LYS 121 H A - 183.2 - 181.1 - -58.6 -44.5 - - - 178.6 -1.8 36.6 - 122 HIS 122 H A - - -75.5 - - -76.0 -24.5 - - - 181.2 -1.7 33.2 - * * 123 LEU 123 h A - - -68.2 180.3 - - - - - - 178.4 -1.6 34.3 - 124 ALA 124 t - - - - - - - - - - - - -.7 33.7 - +* +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * +* +* +** ** * ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.8 183.4 -61.4 177.9 -68.6 -66.0 -38.8 - -110.7 2.0 180.0 -2.0 34.1 ** ** Standard deviations: 7.1 5.5 6.9 6.2 13.9 8.0 9.8 - .0 .0 2.9 .9 1.9 Numbers of values: 16 45 41 31 4 47 47 0 2 2 122 84 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_17 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_17 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 - 1.238 1.511 1.545 1.462 - 116.41 120.33 109.53 109.72 111.61 123.26 2 GLY 2 1.317 1.232 1.509 - 1.439 121.41 115.91 120.53 - 112.46 - 123.55 3 HIS 3 1.327 1.239 1.526 1.544 1.481 124.51 117.34 120.31 109.95 112.69 112.14 122.32 * +* +* 4 HIS 4 1.324 1.231 1.518 1.569 1.447 120.03 114.83 121.98 113.09 109.70 114.20 123.08 +* +* ** ** 5 HIS 5 1.298 1.222 1.516 1.551 1.447 122.45 115.96 120.22 112.47 112.05 111.19 123.80 ** * * ** 6 HIS 6 1.332 1.232 1.528 1.561 1.473 123.68 116.06 121.11 111.37 111.79 111.93 122.77 +* * +* 7 HIS 7 1.309 1.234 1.506 1.544 1.449 121.80 115.66 120.94 110.45 110.09 112.77 123.25 * * * 8 HIS 8 1.296 1.225 1.505 1.565 1.441 122.00 114.27 122.29 114.03 111.85 114.73 123.25 ** +* ** ** ** 9 LEU 9 1.300 1.227 1.506 1.541 1.438 122.67 115.21 121.60 110.34 107.58 110.07 123.16 ** * * ** 10 GLU 10 1.303 1.232 1.521 1.521 1.429 122.08 114.66 121.56 112.08 109.62 110.08 123.61 +* +* * +* 11 MET 11 1.305 1.237 1.512 1.551 1.447 124.45 117.10 119.07 110.28 106.87 110.83 123.80 +* * +* * +* +* 12 ALA 12 1.341 1.238 1.519 1.531 1.473 122.61 114.27 121.32 111.90 109.41 112.38 124.24 * * Residue-by-residue listing for refined_17 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 1.312 1.242 1.523 1.515 1.437 124.45 115.55 121.51 111.05 113.55 108.59 122.93 * * +* * +* 14 GLU 14 1.316 1.236 1.517 1.536 1.422 121.02 114.69 121.70 111.30 107.23 111.40 123.36 +* * +* 15 GLU 15 1.301 1.240 1.502 1.546 1.432 123.14 116.75 119.84 110.39 108.09 110.16 123.39 +* * * * +* 16 GLY 16 1.316 1.237 1.489 - 1.449 120.68 115.80 120.91 - 111.92 - 123.28 +* +* 17 GLN 17 1.310 1.229 1.472 1.537 1.411 120.31 113.35 122.40 114.71 113.89 113.88 124.13 * +** ** * ** +* +** 18 VAL 18 1.266 1.233 1.523 1.547 1.396 122.15 116.91 120.71 112.63 107.95 110.31 122.33 *4.5* *** +* * *4.5* 19 ILE 19 1.286 1.226 1.512 1.536 1.419 120.62 116.13 120.96 110.10 110.17 110.24 122.90 *** ** *** 20 ALA 20 1.293 1.235 1.511 1.525 1.425 121.14 116.95 120.45 110.76 108.82 110.58 122.55 +** +* +** 21 CYS 21 1.309 1.224 1.503 1.510 1.418 121.04 115.89 121.02 110.11 108.92 110.63 123.07 * * * ** ** 22 HIS 22 1.292 1.220 1.507 1.540 1.447 121.69 115.70 120.94 110.35 109.77 110.68 123.34 +** +** 23 THR 23 1.325 1.254 1.520 1.561 1.453 122.74 116.95 119.82 109.35 109.41 111.73 123.23 * * 24 VAL 24 1.329 1.233 1.534 1.567 1.453 121.53 115.50 121.09 111.21 109.79 112.82 123.38 * * 25 GLU 25 1.340 1.230 1.534 1.528 1.419 124.01 115.50 121.31 109.69 109.58 108.45 123.18 ** * * ** 26 THR 26 1.326 1.225 1.539 1.536 1.446 122.21 115.48 120.86 109.46 109.81 109.62 123.62 * * 27 TRP 27 1.329 1.238 1.533 1.538 1.469 123.90 115.92 120.75 110.49 111.73 108.22 123.32 * * * 28 ASN 28 1.316 1.237 1.522 1.527 1.457 122.59 115.49 120.98 109.91 110.77 109.64 123.51 29 GLU 29 1.316 1.235 1.537 1.525 1.451 122.60 116.90 120.51 111.45 111.69 109.98 122.57 30 GLN 30 1.328 1.233 1.521 1.499 1.426 122.19 116.16 120.95 110.95 111.18 109.55 122.88 +* +* +* 31 LEU 31 1.321 1.228 1.515 1.491 1.413 122.58 115.91 120.78 110.39 110.73 108.86 123.30 +* ** ** 32 GLN 32 1.321 1.235 1.532 1.540 1.452 122.40 115.93 120.72 111.06 109.83 110.12 123.34 33 LYS 33 1.325 1.238 1.530 1.533 1.453 122.65 116.82 120.28 110.16 111.29 110.69 122.90 34 ALA 34 1.337 1.222 1.523 1.523 1.459 121.65 115.47 120.89 110.60 110.46 110.70 123.63 35 ASN 35 1.317 1.230 1.513 1.520 1.468 123.75 113.83 121.85 107.44 110.02 108.59 124.32 * * * * * 36 GLU 36 1.307 1.237 1.537 1.536 1.463 124.20 116.37 121.00 109.79 111.82 108.71 122.62 +* * * +* 37 SER 37 1.308 1.240 1.532 1.510 1.442 121.78 116.13 120.33 109.94 111.81 108.16 123.54 * * * 38 LYS 38 1.348 1.237 1.519 1.514 1.470 123.46 114.49 122.12 111.06 109.59 111.34 123.35 * * 39 THR 39 1.297 1.240 1.515 1.524 1.420 123.00 115.08 121.61 108.63 109.62 110.96 123.30 ** +* ** 40 LEU 40 1.273 1.237 1.544 1.560 1.427 122.61 116.98 120.31 113.55 107.84 108.82 122.69 **** +* +* +* * **** 41 VAL 41 1.314 1.232 1.545 1.565 1.442 121.57 116.59 120.81 111.92 111.31 110.50 122.58 * * * 42 VAL 42 1.317 1.227 1.515 1.541 1.453 122.14 116.69 120.62 108.95 109.24 112.10 122.68 Residue-by-residue listing for refined_17 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 1.299 1.219 1.524 1.546 1.444 121.34 116.23 120.40 108.65 110.86 111.23 123.37 ** ** 44 ASP 44 1.303 1.239 1.520 1.544 1.458 123.17 117.27 120.32 110.53 110.21 109.67 122.36 +* +* 45 PHE 45 1.331 1.239 1.498 1.521 1.425 120.75 116.48 120.62 109.90 106.56 111.31 122.89 * +* +* +* 46 THR 46 1.286 1.233 1.529 1.555 1.415 120.47 116.18 120.87 109.98 109.95 107.47 122.94 *** ** ** *** 47 ALA 47 1.296 1.235 1.500 1.510 1.429 122.39 116.72 120.59 110.48 107.87 110.94 122.69 ** * +* * ** 48 SER 48 1.290 1.238 1.544 1.525 1.444 121.73 116.23 120.75 112.64 111.62 109.71 123.01 +** * +** 49 TRP 49 1.327 1.224 1.543 1.549 1.452 122.19 118.65 119.81 111.44 114.03 111.81 121.54 * * * 50 CYS 50 1.323 1.239 1.532 1.557 1.462 119.56 115.02 121.01 113.88 112.23 113.55 123.95 * * +* +* +* 51 GLY 51 1.341 1.229 1.527 - 1.469 123.73 119.38 119.35 - 115.33 - 121.27 * +* * * +* 52 PRO 52 1.362 1.230 1.524 1.535 1.476 122.77 115.47 121.30 110.29 112.19 103.91 123.22 * * 53 CYS 53 1.309 1.218 1.525 1.512 1.443 122.89 115.38 121.87 107.93 108.95 108.81 122.74 * * * 54 ARG 54 1.305 1.230 1.530 1.525 1.435 121.97 114.90 121.46 111.21 109.03 108.89 123.63 +* * +* 55 PHE 55 1.322 1.225 1.537 1.543 1.452 123.67 117.08 120.47 110.41 111.35 109.27 122.43 * * 56 ILE 56 1.327 1.243 1.551 1.579 1.462 120.71 115.52 121.29 110.63 110.15 111.32 123.17 * * * 57 ALA 57 1.334 1.226 1.559 1.530 1.469 123.29 120.40 119.06 111.48 113.97 111.35 120.54 +* ** * +* ** 58 PRO 58 1.384 1.237 1.533 1.533 1.481 122.11 115.98 120.88 109.91 112.38 103.43 123.11 +** +** 59 PHE 59 1.325 1.226 1.529 1.543 1.452 122.01 115.99 121.14 111.35 109.36 110.11 122.84 60 PHE 60 1.319 1.227 1.535 1.539 1.461 122.31 115.90 121.11 111.84 109.36 109.34 122.97 61 ALA 61 1.324 1.237 1.530 1.522 1.458 122.40 116.14 120.85 110.30 110.72 110.54 123.01 62 ASP 62 1.330 1.233 1.490 1.516 1.465 121.93 114.17 121.52 108.44 108.63 110.97 124.32 +* * +* 63 LEU 63 1.312 1.241 1.524 1.528 1.432 124.00 115.21 120.96 110.66 110.26 108.80 123.81 * * * * * 64 ALA 64 1.322 1.229 1.521 1.526 1.451 123.21 116.16 121.31 110.28 111.02 110.36 122.53 65 LYS 65 1.310 1.234 1.516 1.523 1.434 121.21 116.93 120.61 110.54 111.66 111.17 122.45 * * * 66 LYS 66 1.315 1.231 1.528 1.526 1.449 119.61 116.55 120.68 111.15 110.80 111.61 122.76 * * 67 LEU 67 1.320 1.223 1.528 1.509 1.432 121.75 116.56 121.19 112.15 111.50 110.13 122.23 * * * * 68 PRO 68 1.338 1.240 1.531 1.529 1.477 123.60 116.19 121.04 109.63 113.52 102.52 122.77 69 ASN 69 1.318 1.214 1.512 1.530 1.438 122.18 116.30 120.63 110.07 111.11 109.69 123.07 * * 70 VAL 70 1.310 1.238 1.516 1.559 1.439 121.76 116.11 120.72 110.76 109.10 111.50 123.15 * * * 71 LEU 71 1.309 1.235 1.508 1.544 1.414 121.78 115.53 121.23 109.99 110.48 111.54 123.21 * ** ** 72 PHE 72 1.294 1.225 1.496 1.522 1.428 121.91 116.58 120.40 109.68 107.14 111.56 123.00 ** * +* * ** Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 LEU 73 1.281 1.224 1.500 1.547 1.439 122.06 115.30 120.93 110.01 111.91 112.89 123.77 *** * * *** 74 LYS 74 1.306 1.234 1.496 1.551 1.426 122.59 116.87 120.64 109.99 104.93 108.61 122.48 +* * * +* ** * ** 75 VAL 75 1.278 1.228 1.480 1.554 1.415 120.19 115.64 121.15 110.15 108.87 112.36 123.19 +*** ** ** +*** 76 ASP 76 1.288 1.230 1.491 1.499 1.412 120.35 116.72 119.97 110.61 106.78 111.24 123.29 +** +* +* ** +* +** 77 THR 77 1.288 1.232 1.526 1.533 1.433 121.59 117.95 120.20 111.70 113.75 111.26 121.84 +** * * +** 78 ASP 78 1.316 1.230 1.494 1.507 1.438 118.51 113.93 121.71 109.82 108.80 113.02 124.34 * * * +* * * +* 79 GLU 79 1.300 1.230 1.515 1.505 1.420 124.22 116.56 120.90 109.78 111.86 108.72 122.54 ** * +* * * ** 80 LEU 80 1.303 1.240 1.518 1.523 1.414 121.26 113.11 122.89 112.97 107.72 110.19 123.94 +* ** +* * +* * ** 81 LYS 81 1.299 1.237 1.528 1.531 1.432 124.15 116.14 120.79 111.46 111.96 108.37 123.05 ** * * * ** 82 SER 82 1.316 1.227 1.535 1.510 1.451 122.36 117.29 120.27 110.85 112.53 109.65 122.41 83 VAL 83 1.326 1.231 1.528 1.555 1.465 121.02 116.17 120.91 111.31 110.29 111.98 122.86 * * 84 ALA 84 1.325 1.233 1.530 1.515 1.457 121.59 115.68 121.25 110.32 110.08 110.28 123.07 85 SER 85 1.318 1.234 1.548 1.539 1.434 121.82 116.64 120.68 111.41 110.30 109.73 122.66 * * * 86 ASP 86 1.338 1.241 1.520 1.538 1.477 122.53 116.31 120.65 109.51 111.92 110.84 123.03 87 TRP 87 1.315 1.235 1.512 1.525 1.451 122.12 115.56 120.45 110.84 111.70 111.29 123.99 88 ALA 88 1.328 1.233 1.523 1.529 1.457 124.24 115.52 121.47 111.93 112.47 112.31 122.88 * * * 89 ILE 89 1.302 1.246 1.522 1.559 1.438 121.77 116.42 120.78 110.19 108.39 111.16 122.72 +* * * +* 90 GLN 90 1.316 1.238 1.523 1.552 1.430 120.99 117.17 120.45 110.98 111.79 112.44 122.36 * * * * 91 ALA 91 1.320 1.235 1.507 1.515 1.440 120.14 115.26 121.10 111.33 111.28 111.03 123.63 92 MET 92 1.306 1.233 1.518 1.521 1.441 122.93 118.50 119.84 109.34 109.03 109.26 121.66 +* * +* 93 PRO 93 1.335 1.237 1.521 1.518 1.459 123.76 116.66 120.97 110.04 111.42 102.38 122.33 94 THR 94 1.277 1.236 1.518 1.560 1.412 120.16 115.71 121.23 113.08 108.80 111.48 123.05 +*** ** +* +*** 95 PHE 95 1.298 1.224 1.494 1.526 1.403 122.19 116.21 120.81 108.87 108.33 109.10 122.98 ** * +** * +** 96 MET 96 1.277 1.233 1.498 1.532 1.422 121.72 114.99 121.33 111.47 108.57 110.10 123.68 +*** * +* +*** 97 PHE 97 1.283 1.249 1.498 1.512 1.396 123.40 115.76 121.47 109.44 109.03 109.02 122.77 *** * *** *** 98 LEU 98 1.276 1.220 1.515 1.541 1.412 120.73 117.65 120.13 107.73 106.63 110.19 122.21 +*** ** * +* +*** 99 LYS 99 1.282 1.230 1.477 1.522 1.431 120.60 114.67 120.81 110.79 109.60 113.01 124.41 *** ** * * *** 100 GLU 100 1.324 1.230 1.541 1.526 1.448 124.31 115.64 121.46 110.80 110.09 110.77 122.88 * * 101 GLY 101 1.325 1.224 1.528 - 1.447 121.78 117.05 120.56 - 112.66 - 122.38 102 LYS 102 1.324 1.232 1.525 1.553 1.462 121.85 117.07 120.01 108.66 108.92 112.29 122.92 * * * 103 ILE 103 1.319 1.231 1.516 1.572 1.461 122.03 116.47 120.66 109.22 110.76 111.95 122.86 * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 104 LEU 104 1.315 1.231 1.490 1.524 1.423 120.81 116.11 120.60 109.10 110.77 112.68 123.24 * +* +* * +* 105 ASP 105 1.316 1.221 1.485 1.537 1.434 121.63 116.25 120.77 112.02 111.20 112.27 122.93 +* * * * +* 106 LYS 106 1.295 1.238 1.527 1.526 1.421 120.98 116.22 120.53 110.46 109.88 108.59 123.25 ** +* * ** 107 VAL 107 1.313 1.223 1.523 1.562 1.449 122.90 116.44 120.75 109.02 108.89 111.15 122.80 * * 108 VAL 108 1.305 1.249 1.521 1.537 1.440 122.38 115.71 120.64 109.67 109.94 111.14 123.63 +* +* 109 GLY 109 1.317 1.244 1.499 - 1.431 121.75 117.46 120.04 - 110.51 - 122.49 * * 110 ALA 110 1.320 1.243 1.502 1.525 1.430 119.43 114.75 121.57 110.45 108.80 111.23 123.68 * * * * 111 LYS 111 1.292 1.220 1.487 1.513 1.405 123.29 117.53 119.57 110.67 107.18 108.94 122.90 +** +* +** * +** 112 LYS 112 1.306 1.234 1.528 1.530 1.425 120.92 116.85 120.34 112.14 111.97 110.68 122.77 +* +* * +* 113 ASP 113 1.322 1.235 1.522 1.528 1.462 120.86 116.62 120.59 109.89 111.73 111.92 122.77 114 GLU 114 1.334 1.233 1.531 1.543 1.456 121.31 117.18 120.47 111.65 111.22 112.25 122.34 * * 115 LEU 115 1.334 1.219 1.502 1.515 1.455 120.75 115.37 120.89 108.69 108.70 111.34 123.72 * * 116 GLN 116 1.320 1.226 1.527 1.529 1.467 122.39 116.53 120.76 111.14 111.34 111.42 122.67 117 SER 117 1.322 1.228 1.534 1.531 1.455 121.42 115.56 121.36 110.78 109.76 110.11 123.04 118 THR 118 1.317 1.232 1.543 1.543 1.440 122.40 116.24 121.26 111.34 109.83 110.14 122.48 * * 119 ILE 119 1.320 1.223 1.528 1.552 1.446 121.35 116.13 120.66 110.21 108.71 111.97 123.16 120 ALA 120 1.333 1.231 1.531 1.521 1.465 122.84 115.67 121.05 110.68 110.97 110.23 123.28 121 LYS 121 1.322 1.232 1.520 1.504 1.462 123.59 114.93 121.62 109.17 109.72 107.84 123.44 * * +* +* 122 HIS 122 1.309 1.224 1.526 1.525 1.440 122.78 117.42 120.39 110.23 112.76 111.14 122.19 * * 123 LEU 123 1.326 1.239 1.522 1.486 1.422 122.76 115.54 121.45 111.02 112.87 108.59 122.94 ** +* * ** 124 ALA 124 1.282 - 1.511 1.523 1.431 122.62 - - 111.61 108.39 110.68 - *** * * *** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.5* * +** ** *** +* ** * ** ** ** +* *4.5* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 1.266 1.348 1.312 .017 *4.5* * * C-N (Pro) 1.341 .016 4 1.335 1.384 1.354 .020 +** C-O C-O 1.231 .020 123 1.214 1.254 1.232 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.472 1.559 1.519 .016 +** +* CH2G*-C (Gly) 1.516 .018 5 1.489 1.528 1.510 .015 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.531 1.523 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.524 1.579 1.552 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.569 1.530 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.396 1.481 1.441 .019 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.431 1.469 1.447 .013 * * N-CH1E (Pro) 1.466 .015 4 1.459 1.481 1.473 .009 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 2.0 114 113.11 120.40 116.05 1.05 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.80 119.38 117.12 1.30 * CH1E-C-N (Pro) 116.9 1.5 4 115.47 116.66 116.07 .43 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.54 124.41 123.03 .61 +* O-C-N (Pro) 122.0 1.4 4 122.33 123.22 122.86 .35 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.51 124.51 122.07 1.20 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.68 123.73 121.87 1.01 +* C-N-CH1E (Pro) 122.6 5.0 4 122.11 123.76 123.06 .67 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.06 122.89 120.87 .60 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.35 120.91 120.28 .54 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.28 111.93 110.93 .60 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.63 113.08 110.37 1.23 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 107.44 114.71 110.64 1.32 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.93 114.03 110.15 1.74 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.51 115.33 112.58 1.57 N-CH1E-C (Pro) 111.8 2.5 4 111.42 113.52 112.38 .75 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.23 112.38 110.97 .67 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 107.47 112.82 111.11 1.10 ** N-CH1E-CH2E (Pro) 103.0 1.1 4 102.38 103.91 103.06 .63 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.84 114.73 110.53 1.57 +* ** ------------------------------------------------------------------------------------------------------------- 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_17 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 2.9 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 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 84 .9 .8 .2 .4 Inside f. Overall G-factor 124 .0 -.4 .3 1.5 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 7.1 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 45 5.5 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 41 6.9 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 7.5 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 31 6.2 20.4 5.0 -2.8 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 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_17 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.19 Chi1-chi2 distribution -.04 Chi1 only -.12 Chi3 & chi4 .23 Omega .11 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .42 ------ .19 ===== OVERALL AVERAGE .05 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.