Residue-by-residue listing for refined_16 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 - 61.7 - - 177.8 - - - - - - 179.4 - 34.0 - 2 GLY 2 - - - - - - - - - - - 178.7 - - - 3 HIS 3 B - 182.2 - - - - - - - - 183.2 - 34.7 - 4 HIS 4 B - - -56.8 - - - - - - - 177.4 - 35.3 - 5 HIS 5 ~p - - -70.2 - - - - - - - 183.7 - 29.6 - ** * ** 6 HIS 6 l - - -65.3 - - - - - - - 173.9 - 30.7 - * * 7 HIS 7 B - - -66.3 - - - - - - - 181.6 - 34.2 - 8 HIS 8 B 62.4 - - - - - - - - - 176.5 - 30.4 - * * 9 LEU 9 B - - -59.0 180.2 - - - - - - 181.4 -1.2 34.0 - * * 10 GLU 10 B - - -75.1 - - - - - - - 182.1 -.8 33.0 - +* +* 11 MET 11 B - - -63.7 180.5 - - - - - - 184.5 - 32.9 - 12 ALA 12 B - - - - - - - - - - 174.6 - 34.4 - 13 SER 13 b - - -62.9 - - - - - - - 174.5 -.7 35.8 - +* +* 14 GLU 14 S b - - -71.3 - - - - - - - 186.4 - 32.1 - * * 15 GLU 15 B - 172.0 - - - - - - - - 182.9 -2.2 34.3 - 16 GLY 16 S - - - - - - - - - - - 181.2 -.9 - - +* +* 17 GLN 17 S B 52.8 - - 176.2 - - - - - - 176.8 - 35.1 - 18 VAL 18 B 66.5 - - - - - - - - - 180.6 - 34.8 - 19 ILE 19 E B - - -60.9 180.7 - - - - - - 180.6 -2.8 32.7 - * * Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 ALA 20 E B - - - - - - - - - - 178.8 -.8 34.0 - +* +* 21 CYS 21 E B - - -55.2 - - - - - - - 179.0 -1.3 35.7 - 22 HIS 22 a - - -62.9 - - - - - - - 183.0 - 34.1 - 23 THR 23 h B 48.2 - - - - - - - - - 178.2 - 34.5 - * * 24 VAL 24 H A - 179.6 - - - -64.4 -35.0 - - - 176.7 - 33.6 - 25 GLU 25 H A - 179.2 - - - -53.0 -51.3 - - - 180.2 - 35.8 - * * * 26 THR 26 H A - - -52.1 - - -70.9 -44.2 - - - 179.5 - 34.6 - 27 TRP 27 H A - 168.3 - - - -53.5 -54.9 - - - 182.6 -2.9 34.9 - * * * 28 ASN 28 H A - 186.4 - - - -65.2 -35.4 - - - 180.5 -3.5 35.1 - +* +* 29 GLU 29 H A - 186.3 - - - -63.9 -48.2 - - - 182.4 -1.5 36.0 - 30 GLN 30 H A - - -62.5 - - -66.0 -40.7 - - - 178.5 -2.7 34.2 - 31 LEU 31 H A - - -66.8 180.9 - -63.2 -45.0 - - - 177.7 -2.1 34.6 - 32 GLN 32 H A - 180.4 - 182.1 - -58.0 -44.6 - - - 178.5 -2.2 34.4 - 33 LYS 33 H A - 180.9 - 173.8 - -63.3 -41.3 - - - 180.2 -2.2 33.5 - 34 ALA 34 H A - - - - - -70.3 -42.5 - - - 181.9 -2.6 34.0 - 35 ASN 35 H A - 192.6 - - - -64.4 -54.0 - - - 178.9 -3.5 36.6 - * +* +* 36 GLU 36 H A - - -86.9 - - -62.8 -26.4 - - - 177.9 -3.1 29.6 - * * * * * 37 SER 37 h A - - -58.0 - - - - - - - 179.7 -1.3 33.6 - 38 LYS 38 T L - 182.5 - 178.8 - - - - - - 180.3 -1.7 32.4 - 39 THR 39 t B - - -48.3 - - - - - - - 180.9 -2.4 35.2 - * * 40 LEU 40 E B - 191.4 - 171.1 - - - - - - 187.0 -1.1 34.2 - * * * 41 VAL 41 E B 59.3 - - - - - - - - - 178.0 - 33.2 - 42 VAL 42 E B - 181.4 - - - - - - - - 182.5 -2.5 34.2 - 43 VAL 43 E B - 184.3 - - - - - - - - 177.1 -2.6 33.8 - 44 ASP 44 E B - 165.1 - - - - - - - - 178.9 -3.0 34.5 - * * * 45 PHE 45 E B - - -61.7 - - - - - - - 186.0 -3.2 35.9 - * +* +* 46 THR 46 E B - - -49.1 - - - - - - - 170.6 -3.0 37.7 - * +* * * +* 47 ALA 47 t B - - - - - - - - - - 185.9 - 34.5 - * * 48 SER 48 T A - 186.0 - - - - - - - - 186.9 - 32.7 - * * 49 TRP 49 T A 56.4 - - - - - - - - - 182.6 - 34.1 - 50 CYS 50 h B 41.8 - - - - - - - -112.9 2.8 182.9 -1.0 31.2 - * +** *7.6* * *7.6* 51 GLY 51 H - - - - - - -57.4 -59.6 - - - 180.9 -.6 - - +* +* +* 52 PRO 52 H - - - - - -55.3 -55.3 -30.6 - - - 180.6 - 38.4 - * * 53 CYS 53 H A - - -50.1 150.6 - -72.0 -39.5 - -112.9 2.8 177.3 - 35.4 - * * +** *7.6* *7.6* 54 ARG 54 H A - 181.9 - 181.6 - -72.2 -29.4 - - - 179.8 -1.7 34.2 - 55 PHE 55 H A - 181.5 - - - -72.4 -31.5 - - - 184.4 -2.1 34.3 - 56 ILE 56 H A - 189.8 - - - -87.0 -23.2 - - - 181.7 -1.5 34.0 - +* * +* Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 H A - - - - - -56.2 -46.8 - - - 180.8 -1.2 31.7 - * * 58 PRO 58 H - - - - - -63.4 -63.4 -30.1 - - - 178.7 - 38.1 - * * 59 PHE 59 H A - 182.1 - - - -65.9 -39.7 - - - 177.4 - 33.5 - 60 PHE 60 H A - 182.4 - - - -61.5 -33.3 - - - 178.2 -1.4 34.7 - 61 ALA 61 H A - - - - - -67.8 -27.8 - - - 176.8 -1.2 33.3 - * * * 62 ASP 62 H A - 179.9 - - - -70.8 -46.6 - - - 174.4 -.9 34.6 - +* +* 63 LEU 63 H A - - -86.0 - - -52.6 -37.3 - - - 178.3 -1.9 34.6 - * * * 64 ALA 64 H A - - - - - -61.3 -40.2 - - - 178.3 -1.5 32.9 - 65 LYS 65 H A 66.5 - - 178.8 - -80.9 -18.8 - - - 180.2 -1.0 29.0 - * +* * * +* 66 LYS 66 H A - - -66.1 179.6 - -81.2 -36.2 - - - 180.8 -1.5 32.5 - * * 67 LEU 67 h b - - -68.2 172.8 - - - - - - 180.7 -2.3 32.4 - 68 PRO 68 T - - - - - -68.3 - - - - - 181.5 - 38.3 - * * 69 ASN 69 e A - 185.5 - - - - - - - - 180.2 - 33.5 - 70 VAL 70 E B - 182.2 - - - - - - - - 180.4 -.7 33.5 - +* +* 71 LEU 71 E B - 199.0 - 178.9 - - - - - - 183.4 -3.2 36.0 - +* +* 72 PHE 72 E B - - -59.3 - - - - - - - 178.1 -.5 34.8 - ** ** 73 LEU 73 E B - - -68.7 - - - - - - - 179.4 -2.1 32.8 - 74 LYS 74 E B - 194.9 - - - - - - - - 182.7 -2.3 36.9 - 75 VAL 75 E B - 177.9 - - - - - - - - 174.8 -3.5 34.6 - +* +* 76 ASP 76 E B - 179.6 - - - - - - - - 184.9 -.6 34.2 - +* +* 77 THR 77 e A 48.0 - - - - - - - - - 179.0 -2.5 32.9 - * * 78 ASP 78 T A - 186.0 - - - - - - - - 175.2 - 34.1 - 79 GLU 79 T A - 191.0 - - - - - - - - 177.7 - 37.7 - * * 80 LEU 80 h b - - -66.2 - - - - - - - 186.4 -2.8 33.4 - * * * 81 LYS 81 H A - 202.0 - - - -68.3 -39.6 - - - 179.2 -1.3 34.4 - * * * 82 SER 82 H A 52.3 - - - - -63.3 -39.7 - - - 178.4 - 33.9 - 83 VAL 83 H A - 176.8 - - - -66.3 -38.5 - - - 177.0 - 33.7 - 84 ALA 84 H A - - - - - -60.4 -39.8 - - - 177.2 -1.9 33.6 - 85 SER 85 H A - - -56.1 - - -69.8 -44.9 - - - 184.7 -1.9 35.5 - 86 ASP 86 H A - 181.4 - - - -63.7 -36.4 - - - 178.0 -2.8 33.0 - * * 87 TRP 87 h A - - -67.4 - - - - - - - 181.0 -2.6 32.8 - 88 ALA 88 T l - - - - - - - - - - 181.1 -1.2 31.5 - * * 89 ILE 89 t b - - -54.7 176.9 - - - - - - 177.3 -2.6 33.9 - 90 GLN 90 A - - -68.7 - - - - - - - 180.1 -.6 34.0 - +* +* 91 ALA 91 S B - - - - - - - - - - 181.7 - 32.9 - 92 MET 92 S B - - -63.6 161.4 - - - - - - .7 -.6 35.8 - +* +* Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 PRO 93 e cis - - - - - -87.9 - - - - - 178.2 - 39.4 - ** +* ** 94 THR 94 E B - - -59.9 - - - - - - - 174.3 -2.2 34.6 - 95 PHE 95 E B - - -64.4 - - - - - - - 183.6 -2.7 35.6 - 96 MET 96 E B - 191.8 - 162.6 - - - - - - 187.9 -2.7 32.2 - * * 97 PHE 97 E B - - -64.9 - - - - - - - 176.7 -2.3 36.6 - 98 LEU 98 E B - - -58.0 - - - - - - - 174.3 -2.5 36.0 - 99 LYS 99 E B - 175.8 - 171.2 - - - - - - 177.8 -3.5 33.0 - ** ** 100 GLU 100 T l - - -55.7 171.6 - - - - - - 181.9 - 33.7 - 101 GLY 101 T - - - - - - - - - - - 179.7 - - - 102 LYS 102 E B - 182.1 - 182.2 - - - - - - 181.3 -2.2 35.4 - 103 ILE 103 E B - - -76.4 - - - - - - - 173.6 - 32.2 - * * 104 LEU 104 E a - - -68.7 183.2 - - - - - - 184.5 -2.2 34.1 - 105 ASP 105 E B 50.8 - - - - - - - - - 184.2 -2.2 30.3 - * * 106 LYS 106 E B - 189.4 - 188.9 - - - - - - 180.7 - 37.5 - * * 107 VAL 107 E B - 181.4 - - - - - - - - 178.5 -3.2 34.9 - +* +* 108 VAL 108 E B 60.7 - - - - - - - - - 181.1 -.6 32.9 - +* +* 109 GLY 109 e - - - - - - - - - - - 182.9 -2.9 - - * * 110 ALA 110 B - - - - - - - - - - 173.3 - 34.4 - * * 111 LYS 111 h B - - -69.4 180.0 - - - - - - 187.7 -.7 33.4 - * +* +* 112 LYS 112 H A - 186.2 - 175.5 - -58.1 -50.3 - - - 183.0 - 34.3 - 113 ASP 113 H A - - -58.1 - - -72.6 -36.8 - - - 184.0 - 34.4 - 114 GLU 114 H A - 195.0 - - - -75.1 -35.4 - - - 177.5 - 34.2 - 115 LEU 115 H A - 187.1 - - - -58.7 -37.9 - - - 179.0 -2.8 36.4 - * * 116 GLN 116 H A - - -57.5 - - -57.0 -36.1 - - - 179.7 -1.1 33.1 - * * 117 SER 117 H A - 183.1 - - - -69.6 -35.8 - - - 177.9 -.8 33.2 - +* +* 118 THR 118 H A - - -50.5 - - -66.6 -36.4 - - - 177.8 -1.3 35.0 - * * 119 ILE 119 H A - - -59.9 177.7 - -64.2 -45.9 - - - 179.2 -2.2 33.6 - 120 ALA 120 H A - - - - - -63.0 -32.0 - - - 176.1 -2.3 32.9 - 121 LYS 121 H A - 180.4 - 190.5 - -60.7 -44.5 - - - 182.6 -1.8 37.3 - 122 HIS 122 H A - - -73.4 - - -82.8 -20.9 - - - 181.4 -1.7 33.6 - * +* +* 123 LEU 123 h B - 193.9 - - - - - - - - 180.6 -1.8 35.0 - 124 ALA 124 - - - - - - - - - - - - - 34.4 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * * ** +* +* +** *7.6* +* ** +* *7.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 Page 5 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.0 184.1 -63.3 176.7 -68.7 -65.6 -38.8 - -112.9 2.8 180.0 -1.9 34.2 +** *7.6* *7.6* Standard deviations: 7.7 7.3 8.5 8.1 13.9 7.8 8.6 - .0 .0 3.3 .9 1.8 Numbers of values: 13 44 45 28 4 46 46 0 2 2 122 81 119 0 Number of cis-peptides (labelled cis): 1 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_16 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 - 1.245 1.516 1.544 1.463 - 116.24 120.27 110.20 109.54 111.35 123.47 2 GLY 2 1.321 1.251 1.514 - 1.442 121.76 115.65 121.00 - 112.31 - 123.34 * * 3 HIS 3 1.301 1.225 1.518 1.540 1.439 122.79 116.73 120.63 111.24 108.01 109.78 122.57 ** * * ** 4 HIS 4 1.313 1.235 1.507 1.534 1.457 120.91 115.39 120.46 108.19 110.90 110.95 124.15 * * * 5 HIS 5 1.327 1.237 1.521 1.544 1.465 124.36 114.93 121.05 112.12 113.97 113.46 124.03 * * +* +* 6 HIS 6 1.331 1.237 1.503 1.548 1.463 124.95 115.60 121.39 110.47 111.49 114.89 122.92 * +* +** +** 7 HIS 7 1.302 1.237 1.501 1.541 1.437 120.99 117.16 120.12 109.75 107.39 112.21 122.71 +* * * * * +* 8 HIS 8 1.300 1.239 1.515 1.561 1.436 119.96 114.81 121.91 112.73 110.61 113.69 123.13 ** +* * * +* ** 9 LEU 9 1.292 1.239 1.502 1.536 1.419 122.17 115.10 121.12 110.99 107.64 111.34 123.64 +** * ** * +** 10 GLU 10 1.304 1.241 1.515 1.538 1.440 122.70 115.86 120.06 111.40 110.94 111.10 124.08 +* +* 11 MET 11 1.341 1.245 1.510 1.532 1.465 122.80 115.12 121.03 110.70 111.21 111.72 123.84 12 ALA 12 1.299 1.220 1.515 1.517 1.433 123.04 115.82 120.91 110.28 112.06 109.76 123.27 ** * ** Residue-by-residue listing for refined_16 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 1.303 1.244 1.523 1.533 1.439 122.98 117.53 119.94 109.58 108.03 109.60 122.53 +* * +* 14 GLU 14 1.319 1.229 1.521 1.532 1.414 121.06 113.53 122.28 112.74 108.58 111.94 124.03 ** * * ** 15 GLU 15 1.295 1.233 1.514 1.558 1.430 124.94 116.56 120.40 114.55 109.83 106.78 123.02 ** * * +* ** ** ** 16 GLY 16 1.316 1.228 1.498 - 1.441 120.18 115.36 121.40 - 110.79 - 123.23 * * 17 GLN 17 1.303 1.234 1.492 1.523 1.435 122.53 114.72 121.18 108.91 110.62 110.79 124.09 +* +* * +* 18 VAL 18 1.283 1.237 1.536 1.550 1.419 123.62 117.88 120.03 111.48 107.82 109.60 121.99 *** ** * * * * *** 19 ILE 19 1.313 1.228 1.522 1.549 1.444 119.89 115.88 121.33 111.13 110.86 111.87 122.78 * * * 20 ALA 20 1.300 1.237 1.516 1.523 1.438 122.16 116.16 120.99 110.61 110.42 110.58 122.84 ** * ** 21 CYS 21 1.305 1.231 1.515 1.509 1.416 121.97 116.55 120.52 109.69 108.87 109.44 122.90 +* * ** ** 22 HIS 22 1.307 1.218 1.504 1.538 1.451 121.78 116.17 120.87 109.57 110.24 111.57 122.95 +* * +* 23 THR 23 1.317 1.242 1.523 1.555 1.451 121.97 116.82 119.73 109.51 110.86 110.95 123.44 24 VAL 24 1.339 1.228 1.516 1.550 1.462 122.32 115.50 120.85 109.62 109.82 112.42 123.63 25 GLU 25 1.328 1.231 1.533 1.533 1.456 122.93 115.81 121.15 109.47 109.70 109.13 123.01 26 THR 26 1.312 1.218 1.541 1.538 1.442 121.54 115.84 120.89 110.29 110.15 110.14 123.23 * * 27 TRP 27 1.320 1.237 1.539 1.534 1.468 124.04 115.99 120.82 111.16 112.42 107.94 123.17 * +* +* 28 ASN 28 1.316 1.233 1.524 1.535 1.462 122.77 114.98 121.36 110.27 110.00 109.31 123.62 29 GLU 29 1.322 1.237 1.539 1.538 1.458 123.23 115.99 120.99 109.57 110.04 108.70 122.98 * * 30 GLN 30 1.331 1.229 1.517 1.495 1.420 122.96 116.67 120.50 110.33 112.32 109.68 122.83 +* +* +* 31 LEU 31 1.322 1.221 1.503 1.486 1.416 122.08 116.28 120.15 109.88 111.53 109.84 123.57 * ** ** ** 32 GLN 32 1.313 1.232 1.512 1.525 1.449 122.42 115.61 120.87 110.76 109.82 109.93 123.49 * * 33 LYS 33 1.311 1.230 1.530 1.528 1.437 122.07 117.26 120.21 111.44 111.14 110.18 122.51 * * * 34 ALA 34 1.329 1.240 1.525 1.521 1.454 121.34 115.46 120.97 110.32 110.99 110.43 123.56 35 ASN 35 1.323 1.229 1.502 1.527 1.462 123.52 115.17 121.28 108.41 109.16 109.26 123.54 * * * 36 GLU 36 1.317 1.225 1.525 1.533 1.469 122.03 117.90 120.04 111.93 114.70 113.13 122.05 * +* +* 37 SER 37 1.308 1.237 1.539 1.514 1.435 120.25 116.43 120.30 111.19 111.32 110.01 123.27 * * * 38 LYS 38 1.359 1.239 1.557 1.523 1.433 124.08 114.75 123.21 114.39 110.42 108.77 121.99 ** +* * * * ** * ** 39 THR 39 1.300 1.241 1.526 1.524 1.427 122.06 115.75 121.13 109.74 108.87 110.13 123.09 ** +* ** 40 LEU 40 1.288 1.223 1.533 1.560 1.440 122.22 117.41 120.07 113.41 106.56 108.86 122.50 +** +* +* +* +** 41 VAL 41 1.312 1.230 1.538 1.565 1.446 121.08 115.98 121.17 111.34 112.64 110.39 122.85 * * * 42 VAL 42 1.313 1.239 1.520 1.539 1.448 122.40 116.93 120.53 109.30 108.82 112.08 122.53 * * Residue-by-residue listing for refined_16 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 1.311 1.241 1.533 1.553 1.447 120.60 115.09 120.82 109.63 111.35 111.59 124.08 * * 44 ASP 44 1.319 1.241 1.524 1.541 1.463 124.71 115.89 120.84 110.87 110.57 109.43 123.22 +* +* 45 PHE 45 1.318 1.229 1.526 1.520 1.434 123.02 117.13 120.43 109.08 108.98 109.53 122.42 * * 46 THR 46 1.306 1.225 1.534 1.531 1.448 121.44 115.96 120.59 107.45 111.45 108.02 123.43 +* ** ** 47 ALA 47 1.319 1.229 1.523 1.510 1.431 122.85 117.08 120.31 110.69 106.55 110.62 122.59 * +* +* 48 SER 48 1.291 1.234 1.550 1.539 1.448 121.78 118.14 120.11 111.57 113.86 110.11 121.73 +** * +** 49 TRP 49 1.332 1.230 1.536 1.537 1.441 120.78 116.73 120.90 111.19 112.20 109.28 122.37 50 CYS 50 1.307 1.238 1.526 1.533 1.442 121.14 114.64 121.55 113.39 113.02 110.59 123.81 +* +* +* 51 GLY 51 1.329 1.227 1.526 - 1.456 123.59 119.53 119.18 - 115.05 - 121.28 +* * * +* 52 PRO 52 1.367 1.229 1.528 1.542 1.478 122.72 115.36 121.44 110.42 112.11 103.83 123.18 +* * +* 53 CYS 53 1.307 1.222 1.536 1.510 1.440 123.12 116.19 121.33 110.71 110.05 108.16 122.47 +* * +* 54 ARG 54 1.316 1.238 1.539 1.536 1.453 121.98 115.46 121.36 110.78 109.52 110.29 123.18 55 PHE 55 1.326 1.228 1.539 1.544 1.462 123.37 117.12 120.59 110.25 111.90 109.88 122.27 56 ILE 56 1.319 1.238 1.549 1.574 1.465 120.90 115.56 121.17 110.51 110.39 110.80 123.22 * * * 57 ALA 57 1.327 1.237 1.571 1.526 1.465 123.26 120.60 119.01 111.51 114.77 110.70 120.39 ** ** * * +* ** 58 PRO 58 1.382 1.230 1.526 1.531 1.475 122.00 116.59 120.76 110.31 112.71 104.10 122.65 +** +** 59 PHE 59 1.318 1.222 1.529 1.538 1.449 121.66 115.86 121.06 111.70 109.72 110.42 123.01 60 PHE 60 1.322 1.230 1.539 1.537 1.466 123.09 115.94 121.23 111.27 109.79 108.89 122.82 61 ALA 61 1.324 1.236 1.537 1.517 1.455 122.01 116.63 120.89 110.90 111.19 110.65 122.48 62 ASP 62 1.325 1.224 1.487 1.516 1.472 121.85 114.62 121.06 109.47 108.92 111.14 124.31 +* +* 63 LEU 63 1.305 1.234 1.528 1.531 1.439 123.65 116.08 120.58 110.69 111.46 109.36 123.31 +* * +* 64 ALA 64 1.324 1.235 1.526 1.523 1.452 122.32 117.01 120.47 111.08 111.97 110.94 122.52 65 LYS 65 1.330 1.233 1.531 1.539 1.448 120.04 116.33 121.15 113.12 112.34 113.92 122.51 +* ** ** 66 LYS 66 1.312 1.233 1.520 1.524 1.451 121.43 117.53 120.18 110.68 112.92 111.51 122.29 * * 67 LEU 67 1.316 1.226 1.522 1.511 1.436 120.72 116.87 120.92 112.01 112.49 110.46 122.20 * * * 68 PRO 68 1.346 1.235 1.533 1.536 1.466 123.31 117.59 120.10 110.34 114.08 103.58 122.31 69 ASN 69 1.333 1.225 1.521 1.552 1.473 120.75 115.93 121.60 110.98 110.00 111.11 122.47 * * 70 VAL 70 1.305 1.233 1.517 1.547 1.426 121.11 115.70 120.99 110.42 109.52 111.98 123.30 +* +* +* 71 LEU 71 1.293 1.235 1.533 1.547 1.430 122.63 117.24 120.30 111.65 106.21 107.85 122.44 +** * +* +* +** 72 PHE 72 1.311 1.241 1.519 1.525 1.453 121.16 115.68 121.14 108.58 111.22 111.05 123.18 * * 73 LEU 73 1.309 1.227 1.513 1.543 1.446 122.47 115.37 120.93 108.98 111.20 113.70 123.70 * +* +* Residue-by-residue listing for refined_16 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 1.306 1.231 1.527 1.558 1.446 123.40 117.13 120.49 110.79 104.99 107.61 122.36 +* * ** +* ** 75 VAL 75 1.302 1.225 1.517 1.564 1.447 121.34 116.19 120.91 109.60 110.81 111.00 122.88 +* +* 76 ASP 76 1.306 1.240 1.515 1.516 1.444 121.41 116.30 120.54 110.59 107.77 110.93 123.14 +* * +* 77 THR 77 1.294 1.225 1.521 1.521 1.442 122.81 117.52 120.33 110.97 114.20 110.22 122.14 +** * +** 78 ASP 78 1.299 1.233 1.506 1.514 1.448 120.05 113.76 121.82 110.49 108.24 110.99 124.41 ** * * ** 79 GLU 79 1.324 1.230 1.510 1.519 1.457 124.50 115.25 121.49 107.85 107.59 108.33 123.25 +* * * * +* 80 LEU 80 1.321 1.239 1.514 1.532 1.404 121.75 114.94 121.46 110.98 108.67 111.85 123.56 +** +** 81 LYS 81 1.314 1.241 1.537 1.555 1.446 122.95 116.02 121.14 112.16 109.73 108.84 122.81 * * * * 82 SER 82 1.318 1.229 1.532 1.527 1.449 122.09 115.73 121.10 111.70 110.72 109.40 123.13 83 VAL 83 1.322 1.238 1.526 1.549 1.455 123.04 116.22 120.71 110.86 110.53 110.78 123.05 84 ALA 84 1.328 1.223 1.525 1.516 1.455 121.61 116.18 120.90 110.72 110.16 110.84 122.90 85 SER 85 1.318 1.235 1.541 1.529 1.446 121.42 115.52 121.20 109.30 110.08 109.67 123.24 86 ASP 86 1.327 1.227 1.539 1.539 1.468 123.35 117.61 120.42 111.45 113.26 110.00 121.96 87 TRP 87 1.321 1.242 1.516 1.520 1.465 121.14 115.60 120.27 109.84 112.33 112.05 124.13 88 ALA 88 1.334 1.239 1.521 1.529 1.463 123.89 115.35 121.76 111.83 111.58 112.30 122.78 * * * 89 ILE 89 1.302 1.241 1.509 1.545 1.426 121.81 115.37 121.45 110.19 109.87 111.59 123.01 +* +* +* 90 GLN 90 1.293 1.229 1.511 1.548 1.427 121.81 115.70 120.98 110.20 108.56 111.84 123.30 +** +* +** 91 ALA 91 1.316 1.234 1.519 1.517 1.434 121.43 115.25 121.60 111.55 110.38 111.08 123.14 * * 92 MET 92 1.294 1.225 1.527 1.535 1.448 123.09 119.48 119.65 111.15 108.75 107.89 120.86 +** +* +* * +** 93 PRO 93 1.342 1.237 1.534 1.528 1.457 124.50 116.41 121.00 110.41 111.99 102.29 122.56 94 THR 94 1.293 1.227 1.520 1.528 1.424 121.28 116.15 120.66 109.20 110.36 111.18 123.19 +** +* +** 95 PHE 95 1.301 1.230 1.492 1.521 1.410 122.52 117.62 120.27 109.80 106.26 110.35 122.08 ** +* +** +* +** 96 MET 96 1.279 1.239 1.498 1.525 1.423 118.69 114.24 121.50 115.01 109.59 109.14 124.24 +*** * +* +* +** +*** 97 PHE 97 1.299 1.250 1.513 1.519 1.406 124.04 115.83 121.39 109.28 111.40 108.10 122.78 ** +** * * +** 98 LEU 98 1.295 1.219 1.527 1.564 1.426 121.36 116.89 120.70 106.28 107.04 113.14 122.40 ** +* +* ** * +* ** 99 LYS 99 1.285 1.222 1.485 1.519 1.430 122.19 115.02 120.54 111.79 109.28 111.39 124.31 *** +* * *** 100 GLU 100 1.333 1.228 1.540 1.520 1.455 124.03 115.00 121.41 111.94 110.45 109.40 123.51 * * 101 GLY 101 1.334 1.225 1.524 - 1.449 122.37 116.76 120.52 - 112.90 - 122.72 * * 102 LYS 102 1.315 1.223 1.534 1.525 1.452 122.32 116.97 120.42 110.20 109.65 108.96 122.61 103 ILE 103 1.315 1.234 1.519 1.571 1.468 122.70 115.47 121.21 110.97 113.61 111.80 123.31 * * * 104 LEU 104 1.320 1.237 1.493 1.514 1.430 121.81 116.40 120.32 108.57 110.39 112.44 123.28 * * * * Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 105 ASP 105 1.333 1.238 1.478 1.538 1.426 120.94 114.79 121.54 111.81 112.13 114.03 123.66 ** +* ** ** 106 LYS 106 1.283 1.239 1.526 1.524 1.407 122.09 116.96 120.30 110.00 107.88 106.77 122.73 *** +** * ** *** 107 VAL 107 1.309 1.231 1.517 1.559 1.444 121.38 116.09 121.09 109.16 109.84 111.27 122.83 * * 108 VAL 108 1.296 1.234 1.538 1.563 1.430 121.64 116.42 121.08 112.05 109.95 111.21 122.43 ** * * ** 109 GLY 109 1.309 1.241 1.513 - 1.440 120.66 117.03 120.43 - 110.96 - 122.54 * * 110 ALA 110 1.310 1.239 1.516 1.522 1.444 120.75 115.70 120.94 110.07 111.71 109.99 123.36 * * 111 LYS 111 1.313 1.218 1.499 1.512 1.430 123.07 115.48 120.70 111.22 108.48 111.38 123.82 * * * * 112 LYS 112 1.297 1.232 1.548 1.524 1.439 124.06 117.08 120.23 112.21 113.13 107.48 122.64 ** * * * +* ** 113 ASP 113 1.328 1.233 1.519 1.542 1.482 121.97 115.73 121.30 108.47 111.45 111.70 122.97 * * 114 GLU 114 1.311 1.230 1.533 1.554 1.457 122.48 115.96 120.90 113.36 108.93 108.00 123.06 * * +* * +* 115 LEU 115 1.330 1.226 1.500 1.510 1.461 122.78 114.84 121.38 107.66 109.40 109.98 123.78 * * * * 116 GLN 116 1.318 1.235 1.523 1.535 1.466 121.95 116.65 120.46 109.42 111.00 112.74 122.86 * * 117 SER 117 1.327 1.244 1.541 1.540 1.442 120.80 116.21 120.87 112.03 109.70 110.54 122.86 * * 118 THR 118 1.338 1.237 1.536 1.548 1.454 122.07 115.69 121.27 109.25 108.94 110.84 123.02 119 ILE 119 1.327 1.214 1.528 1.550 1.444 121.75 116.63 120.32 110.26 109.86 111.79 122.99 120 ALA 120 1.331 1.234 1.532 1.520 1.469 121.98 116.14 120.70 111.17 111.50 110.88 123.15 121 LYS 121 1.332 1.228 1.512 1.509 1.460 122.38 114.34 121.96 106.86 109.34 109.36 123.71 * +* +* 122 HIS 122 1.308 1.227 1.521 1.522 1.436 122.82 117.72 119.58 109.85 113.76 110.65 122.69 +* * +* 123 LEU 123 1.326 1.239 1.528 1.515 1.422 122.03 115.66 121.12 112.21 109.67 107.65 123.19 +* * +* +* 124 ALA 124 1.305 - 1.497 1.517 1.433 122.68 - - 110.33 108.76 110.81 - +* * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** ** +** +* ** * +** ** +** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 1.279 1.359 1.314 .014 +*** ** * C-N (Pro) 1.341 .016 4 1.342 1.382 1.359 .016 +** * C-O C-O 1.231 .020 123 1.214 1.251 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.478 1.571 1.522 .015 ** ** CH2G*-C (Gly) 1.516 .018 5 1.498 1.526 1.515 .010 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.529 1.520 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.521 1.574 1.549 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.564 1.531 .014 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.404 1.482 1.444 .016 +** * NH1-CH2G* (Gly) 1.451 .016 5 1.440 1.456 1.446 .006 N-CH1E (Pro) 1.466 .015 4 1.457 1.478 1.469 .008 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 2.0 114 113.53 120.60 116.10 1.05 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.36 119.53 116.87 1.48 * CH1E-C-N (Pro) 116.9 1.5 4 115.36 117.59 116.49 .79 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.39 124.41 123.01 .67 +* O-C-N (Pro) 122.0 1.4 4 122.31 123.18 122.68 .32 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.69 124.95 122.19 1.14 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 120.18 123.59 121.71 1.22 +* C-N-CH1E (Pro) 122.6 5.0 4 122.00 124.50 123.13 .92 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.01 123.21 120.85 .58 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.18 121.40 120.51 .75 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.07 111.83 110.85 .53 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.45 112.05 110.13 1.00 * CH2E-CH1E-C (the rest) 110.1 1.9 84 106.28 115.01 110.69 1.59 ** +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.99 114.77 110.31 1.86 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.79 115.05 112.40 1.55 N-CH1E-C (Pro) 111.8 2.5 4 111.99 114.08 112.72 .83 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 109.76 112.30 110.74 .57 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.02 112.42 110.98 .96 ** N-CH1E-CH2E (Pro) 103.0 1.1 4 102.29 104.10 103.45 .69 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.77 114.89 110.31 1.76 ** +** ------------------------------------------------------------------------------------------------------------- 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_16 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 3.3 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 81 .9 .8 .2 .3 Inside f. Overall G-factor 124 .1 -.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 13 7.7 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 44 7.3 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 45 8.5 17.5 4.9 -1.8 BETTER d. Chi-1 pooled st dev 102 8.7 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 28 8.1 20.4 5.0 -2.5 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 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .87 2 Residue-by-residue listing for refined_16 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.12 Chi1-chi2 distribution -.23 Chi1 only .08 Chi3 & chi4 .25 Omega .05 ------ -.03 ===== Main-chain covalent forces:- Main-chain bond lengths .08 Main-chain bond angles .40 ------ .26 ===== OVERALL AVERAGE .07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.