Residue-by-residue listing for refined_11 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 - - - -61.5 176.8 - - - - - - 180.6 - 34.7 - 2 GLY 2 - - - - - - - - - - - 182.5 - - - 3 HIS 3 B - - -64.0 - - - - - - - 178.7 - 33.4 - 4 HIS 4 B - - -56.8 - - - - - - - 179.2 - 35.5 - 5 HIS 5 b 55.4 - - - - - - - - - 177.5 - 29.3 - * * 6 HIS 6 a - - -73.3 - - - - - - - 175.1 -.6 32.7 - +* +* 7 HIS 7 b - - -63.9 - - - - - - - 179.8 - 31.2 - 8 HIS 8 B - 178.1 - - - - - - - - 184.0 -2.2 35.7 - 9 LEU 9 B 53.0 - - - - - - - - - 172.3 - 32.5 - * * 10 GLU 10 B - - -55.4 177.6 - - - - - - 179.1 - 37.0 - 11 MET 11 B - 180.7 - 179.1 - - - - - - 179.4 - 32.3 - 12 ALA 12 S b - - - - - - - - - - 180.2 -.5 32.8 - ** ** 13 SER 13 S b - 181.6 - - - - - - - - 178.6 -1.6 35.6 - 14 GLU 14 A 54.3 - - 176.1 - - - - - - 181.7 - 33.8 - 15 GLU 15 ~p - - -64.8 - - - - - - - 184.8 - 30.2 - ** * ** 16 GLY 16 - - - - - - - - - - - 182.6 -1.2 - - * * 17 GLN 17 B 50.0 - - - - - - - - - 178.8 - 28.6 - +* +* 18 VAL 18 B - 181.0 - - - - - - - - 179.6 - 35.3 - 19 ILE 19 E B - - -59.8 - - - - - - - 179.8 -3.0 33.9 - * * Residue-by-residue listing for refined_11 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 - - - - - - - - - - 181.2 -.9 34.2 - +* +* 21 CYS 21 E B - - -51.9 - - - - - - - 177.9 -2.3 35.5 - 22 HIS 22 S A - - -63.0 - - - - - - - 183.5 -.8 35.0 - +* +* 23 THR 23 h B - - -41.5 - - - - - - - 179.4 - 37.0 - +* +* 24 VAL 24 H A 62.6 - - - - -72.4 -22.8 - - - 180.2 - 34.1 - * * 25 GLU 25 H A - 186.3 - - - -62.2 -52.8 - - - 179.9 - 35.6 - * * 26 THR 26 H A - - -51.0 - - -65.1 -37.5 - - - 179.8 - 36.1 - * * 27 TRP 27 H A - 169.3 - - - -61.3 -55.5 - - - 186.1 -1.5 34.9 - * * * 28 ASN 28 H A - 188.5 - - - -72.3 -41.1 - - - 183.0 -3.2 34.3 - +* +* 29 GLU 29 H A - 183.8 - - - -58.1 -47.9 - - - 179.2 -2.3 34.8 - 30 GLN 30 H A - - -85.8 - - -67.2 -32.7 - - - 177.2 -1.6 31.7 - * * 31 LEU 31 H A - - -67.4 179.5 - -67.2 -47.3 - - - 177.4 -1.3 34.5 - 32 GLN 32 H A - - -63.4 179.9 - -59.0 -41.2 - - - 178.4 -2.6 34.0 - 33 LYS 33 H A - 186.0 - - - -63.2 -44.9 - - - 181.4 -2.2 33.0 - 34 ALA 34 H A - - - - - -67.7 -35.4 - - - 181.0 -2.7 33.7 - 35 ASN 35 H A - 192.5 - - - -70.6 -54.0 - - - 182.7 -2.7 37.1 - * * 36 GLU 36 H A - 183.0 - 181.9 - -64.0 -43.3 - - - 181.5 -3.0 34.6 - * * 37 SER 37 h A - - -56.6 - - - - - - - 176.1 -2.7 33.8 - 38 LYS 38 T l - - -61.5 180.1 - - - - - - 178.8 -1.2 31.6 - * * 39 THR 39 e B - - -46.9 - - - - - - - 179.2 -3.2 36.0 - * +* +* 40 LEU 40 E B - 190.8 - 174.1 - - - - - - 186.9 -.7 34.4 - * +* +* 41 VAL 41 E B 58.3 - - - - - - - - - 176.9 -1.1 33.0 - * * 42 VAL 42 E B - 179.0 - - - - - - - - 182.1 -3.0 34.0 - * * 43 VAL 43 E B - 181.7 - - - - - - - - 175.6 -2.7 34.4 - 44 ASP 44 E B - 169.4 - - - - - - - - 174.7 -3.1 34.5 - * * 45 PHE 45 E B - - -61.6 - - - - - - - 188.5 -3.2 35.9 - * +* +* 46 THR 46 E B - 185.5 - - - - - - - - 175.7 -2.9 35.8 - * * 47 ALA 47 t B - - - - - - - - - - 183.3 - 33.8 - 48 SER 48 T A - - -52.5 - - - - - - - 183.2 - 35.0 - 49 TRP 49 T A 49.0 - - - - - - - - - 181.0 - 31.9 - 50 CYS 50 h B 50.5 - - - - - - - -106.9 2.0 184.1 -1.8 28.4 - +* +* +* 51 GLY 51 H - - - - - - -56.2 -61.4 - - - 179.0 -.5 - - +* ** ** 52 PRO 52 H - - - - - -53.7 -53.7 -30.7 - - - 181.1 - 38.4 - * * * 53 CYS 53 H A - - -47.0 152.3 - -71.9 -39.0 - -106.9 2.0 180.6 - 36.9 - * * +* +* Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 54 ARG 54 H A - 182.0 - 176.7 - -73.2 -37.1 - - - 179.9 -1.8 35.5 - 55 PHE 55 H A - 182.1 - - - -70.0 -31.9 - - - 183.1 -2.6 34.6 - 56 ILE 56 H A - 195.0 - - - -87.6 -11.3 - - - 181.6 -1.6 34.2 - +* ** ** 57 ALA 57 H A - - - - - -57.8 -50.7 - - - 178.7 -.7 31.3 - +* +* 58 PRO 58 H - - - - - -64.6 -64.6 -20.7 - - - 180.1 - 39.3 - +* +* +* 59 PHE 59 H A - 193.4 - - - -79.8 -45.4 - - - 178.6 - 34.5 - * * 60 PHE 60 H A - 185.5 - - - -64.1 -34.0 - - - 176.2 -2.6 34.1 - 61 ALA 61 H A - - - - - -66.9 -31.6 - - - 178.4 -2.2 33.9 - 62 ASP 62 H A - 184.0 - - - -66.6 -47.0 - - - 173.3 -.8 35.5 - * +* +* 63 LEU 63 H A - - -85.8 - - -54.1 -46.3 - - - 179.7 -2.0 34.7 - * * 64 ALA 64 H A - - - - - -63.5 -32.9 - - - 179.9 -2.2 33.5 - 65 LYS 65 H A - 184.8 - 178.0 - -79.9 -33.7 - - - 184.6 -1.5 33.2 - * * 66 LYS 66 H A - 212.6 - - - -82.7 -37.3 - - - 180.4 -2.5 35.3 - +* * +* 67 LEU 67 h b - - -69.5 - - - - - - - 179.7 -3.1 33.5 - * * 68 PRO 68 S - - - - - -88.1 - - - - - 181.2 - 39.1 - ** * ** 69 ASN 69 e A - 185.3 - - - - - - - - 180.9 - 35.5 - 70 VAL 70 E B - 180.2 - - - - - - - - 180.1 - 34.0 - 71 LEU 71 E B - 197.6 - 178.8 - - - - - - 181.9 -3.1 36.0 - * * 72 PHE 72 E B - - -58.8 - - - - - - - 176.7 - 34.5 - 73 LEU 73 E B - - -69.6 - - - - - - - 179.7 -2.2 33.2 - 74 LYS 74 E B - 196.2 - 177.9 - - - - - - 182.9 -2.9 35.9 - * * 75 VAL 75 E B - 181.5 - - - - - - - - 174.2 -3.2 34.9 - * * * 76 ASP 76 E B - 180.2 - - - - - - - - 183.8 -.6 33.9 - +* +* 77 THR 77 e A 52.6 - - - - - - - - - 176.5 -3.1 33.8 - * * 78 ASP 78 T A - 179.4 - - - - - - - - 174.9 -.5 35.7 - ** ** 79 GLU 79 T a - 191.7 - - - - - - - - 180.3 -.7 36.9 - +* +* 80 LEU 80 h b - - -68.1 - - - - - - - 180.6 -2.9 34.0 - * * 81 LYS 81 H A - - -64.8 179.5 - -69.7 -34.3 - - - 180.1 -2.0 32.2 - 82 SER 82 H A - 188.6 - - - -66.4 -42.8 - - - 177.4 - 33.7 - 83 VAL 83 H A - 176.6 - - - -63.0 -38.9 - - - 178.7 - 34.0 - 84 ALA 84 H A - - - - - -59.1 -44.0 - - - 179.1 -1.8 33.7 - 85 SER 85 H A - 184.5 - - - -75.6 -36.9 - - - 183.0 -2.0 33.7 - 86 ASP 86 H A - 184.3 - - - -63.2 -36.3 - - - 178.6 -2.8 34.1 - * * 87 TRP 87 h A - - -70.5 - - - - - - - 181.1 -2.4 32.4 - 88 ALA 88 T l - - - - - - - - - - 178.2 - 30.5 - 89 ILE 89 t B - - -54.5 - - - - - - - 179.0 -3.0 34.8 - * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 90 GLN 90 A - - -69.4 - - - - - - - 183.5 -.5 34.0 - ** ** 91 ALA 91 S B - - - - - - - - - - 178.4 - 33.5 - 92 MET 92 S B - - -71.8 - - - - - - - -.9 -.6 33.3 - +* +* 93 PRO 93 e cis - - - - - -92.5 - - - - - 176.8 - 39.5 - ** +* ** 94 THR 94 E B - - -52.7 - - - - - - - 179.7 -2.9 34.8 - * * 95 PHE 95 E B - - -63.4 - - - - - - - 180.1 -3.0 36.5 - * * 96 MET 96 E B - 181.5 - 177.0 - - - - - - 180.8 -3.1 33.3 - * * 97 PHE 97 E B - - -65.7 - - - - - - - 177.4 -3.2 36.7 - +* +* 98 LEU 98 E B 58.0 - - 167.3 - - - - - - 185.4 -2.4 30.9 - 99 LYS 99 E B - 178.6 - 174.8 - - - - - - 175.4 -3.8 34.9 - ** ** 100 GLU 100 e L - - -58.0 173.0 - - - - - - 179.4 -.7 33.5 - +* +* 101 GLY 101 T - - - - - - - - - - - 178.3 - - - 102 LYS 102 E B - 183.3 - - - - - - - - 182.4 -2.1 35.4 - 103 ILE 103 E B - - -58.8 178.1 - - - - - - 178.2 - 32.4 - 104 LEU 104 E a - - -63.6 182.8 - - - - - - 184.0 -2.3 34.7 - 105 ASP 105 E B 61.4 - - - - - - - - - 177.9 -2.2 33.8 - 106 LYS 106 E B 46.0 - - - - - - - - - 181.4 - 29.4 - * * * 107 VAL 107 E B - 181.9 - - - - - - - - 176.7 -3.2 35.2 - +* +* 108 VAL 108 E B 58.8 - - - - - - - - - 182.9 -.5 32.2 - ** ** 109 GLY 109 e - - - - - - - - - - - 180.2 -3.5 - - +* +* 110 ALA 110 B - - - - - - - - - - 178.7 - 34.4 - 111 LYS 111 h B - - -63.2 177.6 - - - - - - 186.0 -1.0 34.9 - * * * 112 LYS 112 H A - 181.8 - 178.1 - -65.2 -50.1 - - - 181.5 -.5 33.7 - ** ** 113 ASP 113 H A - 176.6 - - - -65.7 -43.3 - - - 179.8 - 33.4 - 114 GLU 114 H A - 187.8 - - - -68.4 -32.5 - - - 177.1 - 34.2 - 115 LEU 115 H A - 186.1 - - - -65.3 -49.7 - - - 176.0 -2.0 35.1 - 116 GLN 116 H A - - -69.4 - - -54.4 -39.0 - - - 178.0 -2.7 33.8 - 117 SER 117 H A - 179.1 - - - -64.6 -44.9 - - - 179.1 -2.0 33.8 - 118 THR 118 H A - - -57.0 - - -64.0 -37.6 - - - 177.9 -2.4 34.5 - 119 ILE 119 H A - - -57.1 177.6 - -64.2 -42.3 - - - 179.4 -2.7 33.5 - 120 ALA 120 H A - - - - - -67.7 -32.4 - - - 176.5 -2.4 32.9 - 121 LYS 121 H A - - -77.4 181.1 - -66.8 -31.9 - - - 176.1 -2.1 34.6 - 122 HIS 122 H A - - -76.7 - - -84.5 -33.1 - - - 183.0 -1.5 33.9 - +* +* 123 LEU 123 h B - 189.5 - - - - - - - - 178.3 -2.5 35.5 - 124 ALA 124 - - - - - - - - - - - - - 34.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * +* +* * ** +* ** +* * ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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: 54.6 184.5 -62.7 176.6 -74.7 -66.8 -39.5 - -106.9 2.0 179.8 -2.1 34.2 +* +* Standard deviations: 5.0 7.3 9.4 5.9 18.6 7.6 9.3 - .0 .0 2.9 .9 1.9 Numbers of values: 13 46 43 25 4 46 46 0 2 2 122 84 119 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_11 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 - 1.228 1.506 1.536 1.471 - 116.50 120.40 109.21 109.26 111.21 123.09 2 GLY 2 1.308 1.234 1.499 - 1.432 121.37 116.28 120.77 - 110.58 - 122.94 * * * 3 HIS 3 1.303 1.234 1.506 1.530 1.452 121.55 116.02 120.81 110.32 111.12 111.41 123.16 +* +* 4 HIS 4 1.310 1.234 1.512 1.543 1.450 122.71 117.26 120.17 108.49 107.97 111.30 122.56 * * * 5 HIS 5 1.298 1.225 1.519 1.562 1.442 120.60 115.46 121.79 113.51 112.27 113.47 122.64 ** +* +* +* ** 6 HIS 6 1.315 1.237 1.500 1.535 1.457 122.15 116.26 120.99 110.19 111.20 112.64 122.73 * * * * 7 HIS 7 1.318 1.232 1.516 1.542 1.447 120.47 113.29 122.24 111.79 108.99 113.89 124.21 * +* +* 8 HIS 8 1.298 1.237 1.503 1.544 1.429 125.77 117.63 119.70 110.00 105.26 110.38 122.66 ** * +* ** ** ** 9 LEU 9 1.288 1.242 1.508 1.561 1.429 120.04 114.36 121.63 112.02 113.45 110.60 123.99 +** +* +* * +** 10 GLU 10 1.298 1.237 1.508 1.530 1.431 123.33 119.03 119.02 108.71 104.61 109.53 121.93 ** * * * ** ** 11 MET 11 1.296 1.236 1.517 1.530 1.445 118.61 116.23 120.74 110.90 110.01 112.76 123.02 ** +* * ** Residue-by-residue listing for refined_11 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 1.320 1.239 1.517 1.515 1.436 121.11 114.50 121.35 111.53 110.21 111.28 124.01 * * 13 SER 13 1.304 1.244 1.517 1.548 1.426 124.71 117.29 119.72 110.35 106.46 109.90 122.97 +* +* +* +* +* 14 GLU 14 1.316 1.239 1.530 1.527 1.422 121.42 115.41 120.66 111.31 110.87 110.09 123.91 +* +* 15 GLU 15 1.333 1.240 1.525 1.535 1.457 124.06 115.88 121.25 113.05 112.62 112.39 122.83 * +* * +* 16 GLY 16 1.296 1.235 1.497 - 1.443 121.41 114.75 121.62 - 109.48 - 123.62 ** * * ** 17 GLN 17 1.317 1.232 1.482 1.538 1.413 121.98 112.89 122.54 114.02 113.52 113.33 124.47 ** ** +* * ** +* ** 18 VAL 18 1.266 1.239 1.513 1.553 1.427 123.97 118.08 119.53 109.94 107.08 110.68 122.38 **** +* * * **** 19 ILE 19 1.309 1.239 1.520 1.542 1.431 119.44 115.81 121.27 110.27 109.70 111.51 122.92 * * * * 20 ALA 20 1.302 1.236 1.505 1.522 1.435 122.04 116.26 120.97 110.64 109.34 110.69 122.75 +* * +* 21 CYS 21 1.295 1.223 1.505 1.500 1.408 121.14 115.96 120.87 109.80 109.30 109.45 123.14 ** * +** +** 22 HIS 22 1.297 1.237 1.511 1.539 1.452 121.89 115.02 121.67 109.33 108.67 110.90 123.31 ** ** 23 THR 23 1.322 1.243 1.526 1.547 1.424 121.93 116.33 120.31 107.75 107.42 110.09 123.34 +* * +* 24 VAL 24 1.306 1.229 1.537 1.569 1.457 123.04 115.04 121.67 110.30 109.48 111.29 123.27 +* * +* 25 GLU 25 1.327 1.234 1.532 1.556 1.451 123.31 115.75 120.64 112.09 109.16 107.35 123.48 * * +* +* 26 THR 26 1.321 1.229 1.531 1.537 1.450 122.85 114.57 121.66 109.49 109.92 108.76 123.76 +* +* 27 TRP 27 1.305 1.226 1.534 1.538 1.439 123.65 116.67 120.64 111.93 112.43 107.34 122.61 +* * * +* +* 28 ASN 28 1.308 1.236 1.525 1.521 1.458 121.15 115.89 120.66 109.73 112.04 110.29 123.43 +* +* 29 GLU 29 1.327 1.240 1.541 1.534 1.473 122.75 116.11 121.21 110.16 110.98 109.46 122.67 30 GLN 30 1.321 1.228 1.517 1.500 1.417 122.58 117.54 119.76 113.09 113.68 109.91 122.70 * ** +* ** 31 LEU 31 1.324 1.230 1.505 1.488 1.421 121.72 116.30 120.36 109.96 111.00 110.06 123.34 ** +* ** 32 GLN 32 1.328 1.227 1.508 1.519 1.449 121.39 115.48 120.85 109.83 109.79 111.40 123.64 33 LYS 33 1.323 1.219 1.542 1.567 1.441 122.33 117.45 120.26 113.05 110.14 109.87 122.26 +* +* +* 34 ALA 34 1.332 1.230 1.529 1.520 1.464 121.23 115.97 120.87 110.44 111.29 110.55 123.16 35 ASN 35 1.312 1.237 1.516 1.531 1.462 122.82 114.50 121.71 108.17 109.29 108.68 123.76 * * * * 36 GLU 36 1.313 1.233 1.529 1.529 1.464 123.51 116.59 120.84 109.96 111.93 109.64 122.56 * * * 37 SER 37 1.311 1.232 1.527 1.515 1.435 121.38 116.05 120.30 111.54 111.52 109.34 123.65 * * * 38 LYS 38 1.343 1.237 1.515 1.508 1.458 123.62 115.22 121.91 112.14 112.82 111.13 122.81 * * * * 39 THR 39 1.289 1.237 1.519 1.520 1.419 121.84 116.30 120.83 108.94 107.97 110.01 122.86 +** ** * +** 40 LEU 40 1.283 1.230 1.526 1.561 1.442 121.48 117.26 120.04 112.54 105.47 109.79 122.67 *** +* * ** *** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 VAL 41 1.303 1.228 1.544 1.563 1.436 121.05 116.09 121.10 112.22 112.71 109.87 122.77 +* * * +* 42 VAL 42 1.311 1.236 1.521 1.544 1.447 122.96 116.63 120.72 109.72 109.00 112.03 122.64 * * 43 VAL 43 1.303 1.236 1.522 1.553 1.444 121.35 115.53 120.54 108.84 111.10 111.71 123.93 +* +* 44 ASP 44 1.309 1.243 1.518 1.539 1.452 123.69 116.09 120.97 110.08 110.33 110.42 122.85 * * * 45 PHE 45 1.308 1.228 1.506 1.523 1.422 121.78 117.16 120.24 109.38 106.39 110.23 122.57 * +* +* +* 46 THR 46 1.286 1.227 1.522 1.565 1.426 120.37 115.93 120.84 110.11 110.44 108.98 123.22 *** +* * *** 47 ALA 47 1.301 1.233 1.505 1.520 1.424 123.03 116.18 120.61 111.22 107.48 111.19 123.20 ** +* * ** 48 SER 48 1.300 1.227 1.546 1.523 1.462 123.42 116.66 120.71 109.73 112.60 108.96 122.62 ** * ** 49 TRP 49 1.321 1.227 1.542 1.545 1.449 122.06 118.93 119.53 111.46 114.74 110.94 121.54 * * * 50 CYS 50 1.321 1.238 1.535 1.551 1.465 119.06 114.92 121.31 114.01 113.52 113.33 123.77 * * ** +* ** 51 GLY 51 1.335 1.232 1.525 - 1.467 123.66 119.16 119.44 - 114.65 - 121.40 +* * * +* 52 PRO 52 1.363 1.222 1.530 1.542 1.474 122.84 115.77 121.06 110.32 112.11 103.90 123.14 * * 53 CYS 53 1.315 1.229 1.527 1.510 1.453 122.92 115.20 121.80 108.16 109.50 108.63 123.01 * * * * 54 ARG 54 1.300 1.227 1.525 1.520 1.439 123.05 115.45 121.15 111.12 109.77 107.94 123.38 ** * +* ** 55 PHE 55 1.316 1.237 1.539 1.544 1.454 122.80 116.41 121.03 110.72 111.07 109.34 122.55 56 ILE 56 1.324 1.230 1.551 1.573 1.458 121.14 116.32 121.11 110.29 110.46 110.83 122.55 * * * 57 ALA 57 1.331 1.232 1.551 1.526 1.469 122.26 119.87 119.50 111.70 113.54 111.62 120.62 * +* * +* 58 PRO 58 1.375 1.235 1.527 1.532 1.477 121.92 115.44 121.62 109.58 111.54 103.36 122.94 ** ** 59 PHE 59 1.307 1.213 1.529 1.533 1.439 121.88 116.31 120.92 110.82 108.91 110.03 122.74 +* +* 60 PHE 60 1.324 1.234 1.537 1.540 1.467 122.45 116.04 121.08 111.59 109.93 109.45 122.86 61 ALA 61 1.325 1.232 1.537 1.522 1.462 121.92 115.63 121.16 110.55 110.20 110.47 123.19 62 ASP 62 1.329 1.223 1.504 1.524 1.471 123.10 114.60 121.55 109.56 108.69 109.75 123.85 * * 63 LEU 63 1.310 1.221 1.517 1.526 1.434 123.81 116.51 120.23 110.49 111.47 109.32 123.25 * * * * 64 ALA 64 1.313 1.227 1.523 1.518 1.450 121.92 116.68 120.80 110.67 111.82 110.60 122.51 * * 65 LYS 65 1.314 1.230 1.524 1.530 1.441 121.03 116.41 120.74 111.11 111.54 110.74 122.83 * * 66 LYS 66 1.314 1.227 1.543 1.545 1.449 121.07 116.80 120.93 111.14 108.98 108.61 122.27 * * * 67 LEU 67 1.321 1.231 1.531 1.552 1.442 121.83 117.78 120.75 110.30 110.86 111.57 121.45 * * 68 PRO 68 1.344 1.232 1.531 1.527 1.452 122.29 115.61 121.31 110.78 111.35 102.55 123.07 69 ASN 69 1.324 1.235 1.523 1.530 1.453 122.98 115.10 121.64 109.89 109.50 109.24 123.25 70 VAL 70 1.310 1.223 1.520 1.549 1.438 122.65 116.09 120.65 110.38 109.88 111.26 123.20 * * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 LEU 71 1.301 1.225 1.540 1.550 1.445 122.75 118.07 119.89 111.59 106.69 107.64 122.02 ** +* +* ** 72 PHE 72 1.312 1.235 1.523 1.527 1.458 120.92 115.78 120.94 108.80 111.62 111.16 123.28 * * 73 LEU 73 1.315 1.224 1.510 1.548 1.456 123.36 115.79 120.59 108.38 110.34 114.11 123.62 * ** ** 74 LYS 74 1.306 1.243 1.509 1.498 1.430 123.12 116.73 120.38 109.45 108.37 109.16 122.86 +* +* * * +* 75 VAL 75 1.312 1.238 1.525 1.565 1.451 121.57 116.16 120.67 108.59 111.00 111.42 123.16 * * 76 ASP 76 1.319 1.230 1.519 1.535 1.454 121.88 116.15 120.93 110.99 108.32 110.99 122.88 * * 77 THR 77 1.311 1.228 1.521 1.530 1.454 123.04 115.63 121.21 110.40 111.95 110.43 123.15 * * 78 ASP 78 1.306 1.233 1.518 1.515 1.453 122.80 114.22 122.23 110.61 108.29 108.41 123.56 +* * * +* 79 GLU 79 1.302 1.233 1.513 1.522 1.442 123.37 114.91 121.51 108.12 107.86 109.35 123.55 +* * * +* 80 LEU 80 1.315 1.241 1.534 1.540 1.416 123.21 116.03 121.17 110.13 111.12 110.93 122.72 ** ** 81 LYS 81 1.316 1.242 1.514 1.520 1.454 122.24 116.43 120.48 111.06 112.41 111.68 123.09 82 SER 82 1.324 1.231 1.522 1.530 1.439 121.11 116.14 120.36 111.43 108.97 110.69 123.46 83 VAL 83 1.342 1.237 1.527 1.559 1.466 122.37 115.67 121.14 109.81 109.97 111.68 123.16 84 ALA 84 1.325 1.215 1.524 1.514 1.448 121.99 117.19 120.60 110.44 111.29 110.55 122.21 85 SER 85 1.311 1.234 1.543 1.535 1.448 120.68 115.86 121.06 111.16 110.45 110.31 123.03 * * 86 ASP 86 1.323 1.234 1.536 1.543 1.472 123.44 116.71 120.83 111.18 111.74 109.36 122.46 87 TRP 87 1.320 1.238 1.525 1.521 1.456 122.03 115.68 120.40 111.05 112.95 111.23 123.90 88 ALA 88 1.329 1.237 1.528 1.532 1.469 124.48 115.30 121.57 111.92 112.53 112.99 123.03 +* +* +* 89 ILE 89 1.311 1.246 1.524 1.564 1.439 122.70 116.16 121.06 108.86 108.67 111.96 122.66 * * 90 GLN 90 1.305 1.239 1.522 1.543 1.440 121.88 116.46 120.71 109.24 110.77 111.92 122.82 +* +* 91 ALA 91 1.322 1.229 1.516 1.521 1.444 120.81 115.90 121.19 110.78 111.54 110.57 122.91 92 MET 92 1.305 1.243 1.507 1.503 1.433 121.86 118.39 119.95 110.23 111.42 111.44 121.66 +* * * * +* 93 PRO 93 1.341 1.229 1.533 1.524 1.460 124.15 116.77 121.02 110.24 112.00 102.32 122.16 94 THR 94 1.290 1.227 1.515 1.518 1.421 120.83 116.35 120.51 109.25 109.09 111.15 123.14 +** +* +** 95 PHE 95 1.299 1.228 1.492 1.520 1.413 122.07 116.84 120.44 109.04 108.05 109.42 122.71 ** +* ** * ** 96 MET 96 1.286 1.235 1.492 1.522 1.429 120.37 114.98 121.13 111.23 110.06 111.21 123.89 *** +* +* *** 97 PHE 97 1.287 1.247 1.505 1.516 1.394 123.73 116.21 121.33 109.14 109.40 108.68 122.46 +** *** * * *** 98 LEU 98 1.278 1.219 1.512 1.564 1.409 120.69 117.16 120.75 112.85 109.34 113.63 122.09 +*** +* +** * +* +*** 99 LYS 99 1.278 1.238 1.481 1.531 1.418 120.52 113.87 121.32 111.02 110.31 109.28 124.76 +*** ** ** * * +*** 100 GLU 100 1.322 1.225 1.535 1.515 1.437 124.27 115.49 121.25 112.74 111.12 108.70 123.22 * * * * * 101 GLY 101 1.327 1.233 1.527 - 1.452 121.97 117.69 119.99 - 114.21 - 122.31 102 LYS 102 1.321 1.218 1.522 1.535 1.461 120.97 117.47 119.98 109.53 108.93 109.97 122.54 103 ILE 103 1.316 1.239 1.524 1.560 1.459 121.21 115.72 121.09 110.80 111.71 112.36 123.16 Residue-by-residue listing for refined_11 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 1.319 1.232 1.503 1.525 1.431 121.99 116.15 120.68 109.17 110.27 111.20 123.17 * * * 105 ASP 105 1.316 1.217 1.498 1.516 1.439 121.97 115.43 121.29 109.01 111.78 111.91 123.22 * * 106 LYS 106 1.292 1.241 1.534 1.561 1.447 122.22 115.86 121.19 114.13 112.79 112.42 122.92 +** +* ** * +** 107 VAL 107 1.308 1.232 1.521 1.564 1.453 122.71 116.58 120.45 108.43 109.64 111.59 122.95 +* +* 108 VAL 108 1.309 1.241 1.537 1.567 1.440 121.51 115.65 121.37 112.07 109.79 112.21 122.95 * * * * 109 GLY 109 1.306 1.239 1.505 - 1.428 121.45 117.52 120.23 - 109.77 - 122.25 +* * +* 110 ALA 110 1.313 1.234 1.493 1.519 1.432 119.07 115.52 121.30 110.22 108.86 110.96 123.18 * +* * * +* 111 LYS 111 1.289 1.216 1.500 1.515 1.413 122.56 116.53 120.07 112.15 108.33 108.44 123.40 +** * ** * * * +** 112 LYS 112 1.308 1.236 1.528 1.524 1.439 122.98 116.65 120.36 111.12 112.49 109.65 122.97 +* * +* 113 ASP 113 1.317 1.233 1.526 1.536 1.472 121.68 115.91 121.18 110.86 111.21 110.77 122.88 114 GLU 114 1.315 1.240 1.538 1.533 1.454 122.08 116.20 121.08 111.23 110.08 109.59 122.71 * * 115 LEU 115 1.325 1.214 1.503 1.515 1.448 121.95 115.38 120.69 109.33 108.66 110.60 123.92 * * 116 GLN 116 1.324 1.231 1.521 1.534 1.478 122.66 116.09 120.74 110.19 110.87 110.99 123.14 * * 117 SER 117 1.319 1.223 1.522 1.533 1.443 121.33 115.83 120.84 111.17 109.76 110.52 123.28 118 THR 118 1.309 1.230 1.542 1.545 1.438 122.68 116.92 120.60 111.10 110.13 109.49 122.43 * * * * 119 ILE 119 1.327 1.220 1.530 1.554 1.449 121.16 116.60 120.49 109.67 109.53 112.56 122.85 120 ALA 120 1.329 1.236 1.527 1.520 1.461 121.81 116.17 120.76 111.25 111.08 111.03 123.06 121 LYS 121 1.323 1.232 1.524 1.492 1.402 123.52 116.09 120.79 112.19 111.58 107.54 123.11 +* +** * * +* +** 122 HIS 122 1.311 1.226 1.528 1.528 1.438 122.25 116.31 120.24 109.83 111.65 111.06 123.44 * * * 123 LEU 123 1.333 1.250 1.529 1.524 1.444 124.37 115.42 120.70 111.85 111.89 106.57 123.87 * ** ** 124 ALA 124 1.331 - 1.528 1.528 1.449 123.49 - - 110.54 109.38 110.80 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** ** ** *** ** +* * ** ** ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 1.343 1.312 .014 **** * C-N (Pro) 1.341 .016 4 1.341 1.375 1.356 .014 ** C-O C-O 1.231 .020 123 1.213 1.250 1.232 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.481 1.551 1.521 .014 ** * CH2G*-C (Gly) 1.516 .018 5 1.497 1.527 1.510 .013 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.514 1.532 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.518 1.573 1.552 .015 * CH1E-CH2E (the rest) 1.530 .020 84 1.488 1.567 1.531 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.394 1.478 1.443 .017 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.428 1.467 1.444 .014 * N-CH1E (Pro) 1.466 .015 4 1.452 1.477 1.466 .010 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 2.0 114 112.89 119.87 116.12 1.04 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.75 119.16 117.08 1.48 * CH1E-C-N (Pro) 116.9 1.5 4 115.44 116.77 115.90 .52 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.62 124.76 123.00 .62 * * O-C-N (Pro) 122.0 1.4 4 122.16 123.14 122.83 .39 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.61 125.77 122.15 1.21 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 5 121.37 123.66 121.97 .87 +* C-N-CH1E (Pro) 122.6 5.0 4 121.92 124.15 122.80 .84 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.02 122.54 120.85 .59 * * CH2G*-C-O (Gly) 120.8 2.1 5 119.44 121.62 120.41 .74 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.22 111.92 110.92 .52 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.75 112.22 109.87 1.08 * CH2E-CH1E-C (the rest) 110.1 1.9 84 108.12 114.13 110.70 1.39 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.61 114.74 110.25 1.86 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.48 114.65 111.74 2.23 * N-CH1E-C (Pro) 111.8 2.5 4 111.35 112.11 111.75 .32 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.47 112.99 111.02 .66 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.76 112.56 110.99 1.06 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.32 103.90 103.03 .63 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.57 114.11 110.33 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_11 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] 101 89.4% Residues in additional allowed regions [a,b,l,p] 11 9.7% 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 89.4 83.8 10.0 .6 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 .5 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 13 5.0 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 46 7.3 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 43 9.4 17.5 4.9 -1.7 BETTER d. Chi-1 pooled st dev 102 9.1 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 25 5.9 20.4 5.0 -2.9 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% 89.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.3 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .92 3 Residue-by-residue listing for refined_11 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.16 Chi1-chi2 distribution -.30 Chi1 only .05 Chi3 & chi4 .49 Omega .14 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths .02 Main-chain bond angles .42 ------ .25 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.