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 - - 176.2 - - - - - - - - 177.4 - 33.0 - 2 GLY 2 - - - - - - - - - - - 175.6 - - - 3 HIS 3 ~a - - -68.4 - - - - - - - 176.1 - 33.7 - ** ** 4 HIS 4 b - 190.9 - - - - - - - - 182.1 - 34.2 - 5 HIS 5 b 57.8 - - - - - - - - - 175.2 - 30.8 - 6 HIS 6 b - - -67.8 - - - - - - - 175.7 - 34.7 - 7 HIS 7 b 61.8 - - - - - - - - - 184.9 - 30.2 - * * 8 HIS 8 B - 177.4 - - - - - - - - 174.4 -1.4 35.7 - 9 LEU 9 B 52.5 - - - - - - - - - 183.4 - 31.4 - 10 GLU 10 b 53.9 - - 181.5 - - - - - - 177.8 - 30.6 - 11 MET 11 B - - -66.8 179.1 - - - - - - 178.4 - 34.4 - 12 ALA 12 B - - - - - - - - - - 176.8 - 33.6 - 13 SER 13 B 49.7 - - - - - - - - - 181.6 - 34.3 - 14 GLU 14 a - 180.8 - 183.2 - - - - - - 176.6 - 34.2 - 15 GLU 15 ~p - - -63.5 - - - - - - - 180.1 - 32.5 - ** ** 16 GLY 16 - - - - - - - - - - - 181.6 -.9 - - +* +* 17 GLN 17 B 48.7 - - 176.4 - - - - - - 177.0 - 30.7 - 18 VAL 18 B - 185.9 - - - - - - - - 180.5 -.5 35.7 - +* +* 19 ILE 19 E B - - -60.5 - - - - - - - 180.6 -2.1 33.1 - 20 ALA 20 E B - - - - - - - - - - 182.4 -.8 33.6 - +* +* 21 CYS 21 E B - - -52.8 - - - - - - - 175.4 -2.0 35.9 - 22 HIS 22 a - - -67.9 - - - - - - - 181.9 - 33.2 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 23 THR 23 h B 59.8 - - - - - - - - - 176.2 - 36.0 - 24 VAL 24 H A - 183.4 - - - -76.3 -28.2 - - - 179.4 - 34.8 - 25 GLU 25 H A - 179.8 - - - -57.1 -52.9 - - - 179.8 - 35.7 - * * 26 THR 26 H A - - -53.6 - - -70.3 -35.0 - - - 178.5 - 33.7 - 27 TRP 27 H A - 169.7 - - - -59.7 -52.6 - - - 181.3 -1.3 34.2 - * * 28 ASN 28 H A - 185.1 - - - -62.9 -43.9 - - - 181.2 -3.3 34.5 - +* +* 29 GLU 29 H A - 179.4 - 172.2 - -58.8 -47.5 - - - 179.2 -2.0 32.8 - 30 GLN 30 H A - - -75.3 - - -64.7 -34.4 - - - 177.4 -2.4 33.2 - 31 LEU 31 H A - - -67.5 178.6 - -68.6 -42.1 - - - 176.5 -1.6 35.1 - 32 GLN 32 H A - 195.3 - - - -59.4 -47.2 - - - 178.0 -2.5 35.4 - 33 LYS 33 H A - 180.4 - 178.0 - -55.0 -46.9 - - - 180.8 -2.9 34.0 - * * 34 ALA 34 H A - - - - - -69.2 -39.0 - - - 180.9 -2.5 33.8 - 35 ASN 35 H A - 192.0 - - - -66.7 -51.9 - - - 180.7 -3.0 36.8 - * * * 36 GLU 36 H A - 180.7 - 187.0 - -58.9 -44.1 - - - 183.2 -3.7 36.2 - ** ** 37 SER 37 h A - - -55.0 - - - - - - - 179.3 -2.3 34.4 - 38 LYS 38 T L - 194.0 - 186.3 - - - - - - 183.2 -.9 34.2 - * * 39 THR 39 t B - - -46.9 - - - - - - - 179.7 -2.5 35.7 - * * 40 LEU 40 e B - 186.5 - 172.3 - - - - - - 182.4 - 34.7 - 41 VAL 41 E B 59.0 - - - - - - - - - 176.9 -.6 32.8 - +* +* 42 VAL 42 E B - 181.2 - - - - - - - - 182.8 -2.7 34.2 - 43 VAL 43 E B - 182.6 - - - - - - - - 175.9 -3.0 33.9 - * * 44 ASP 44 E B - 159.3 - - - - - - - - 172.2 -3.0 35.8 - * * * * 45 PHE 45 E B - - -65.1 - - - - - - - 181.8 -1.8 36.1 - 46 THR 46 E B - 188.9 - - - - - - - - 177.4 -2.0 33.8 - 47 ALA 47 t B - - - - - - - - - - 183.7 - 33.4 - 48 SER 48 T A - 183.3 - - - - - - - - 181.5 - 33.8 - 49 TRP 49 T A 55.9 - - - - - - - - - 181.0 - 31.7 - 50 CYS 50 h B - 175.5 - 223.3 - - - 51.2 - 2.0 183.2 -1.6 33.7 - ** *** *** 51 GLY 51 H - - - - - - -59.9 -67.2 - - - 179.5 -.6 - - ** +* ** 52 PRO 52 H - - - - - -57.5 -57.5 -30.3 - - - 179.4 - 38.7 - * * 53 CYS 53 H A - - -55.0 - - -70.4 -32.2 51.2 - 2.0 175.9 - 35.9 - *** *** 54 ARG 54 H A - 180.1 - 181.5 - -78.3 -34.7 - - - 179.9 -1.4 33.8 - * * 55 PHE 55 H A - 179.2 - - - -58.9 -31.4 - - - 184.4 -2.3 34.8 - 56 ILE 56 H A - 191.9 - - - -87.3 -20.5 - - - 184.4 -1.2 34.4 - +* +* * +* 57 ALA 57 H A - - - - - -64.0 -42.9 - - - 180.8 -.6 31.5 - +* +* 58 PRO 58 H - - - - - -61.1 -61.1 -26.6 - - - 179.9 - 38.9 - * * * 59 PHE 59 H A - 183.8 - - - -74.5 -40.6 - - - 178.7 -.6 33.6 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 60 PHE 60 H A - 183.1 - - - -66.5 -35.1 - - - 177.0 -1.3 34.3 - 61 ALA 61 H A - - - - - -67.5 -33.0 - - - 179.5 -2.2 33.8 - 62 ASP 62 H A - 190.8 - - - -72.2 -40.5 - - - 176.3 -1.3 35.2 - 63 LEU 63 H A - - -70.2 181.3 - -53.0 -37.8 - - - 179.3 -2.4 34.6 - * * 64 ALA 64 H A - - - - - -66.3 -35.5 - - - 180.2 -1.3 33.8 - 65 LYS 65 H A - 184.5 - 179.5 - -79.7 -32.0 - - - 180.3 -.9 35.0 - * * * 66 LYS 66 H A - 180.0 - - - -69.4 -41.0 - - - 183.5 -2.5 36.4 - 67 LEU 67 h B - - -67.0 170.9 - - - - - - 173.6 -2.5 34.0 - * * 68 PRO 68 S - - - - - -74.1 - - - - - 179.0 - 39.0 - * * 69 ASN 69 S A - 183.7 - - - - - - - - 183.0 - 36.0 - 70 VAL 70 S B - 181.0 - - - - - - - - 179.0 - 34.1 - 71 LEU 71 E B - 196.3 - 175.5 - - - - - - 182.4 -2.9 35.4 - * * 72 PHE 72 E B - - -59.1 - - - - - - - 175.4 - 34.0 - 73 LEU 73 E B - - -79.5 - - - - - - - 179.0 -2.1 33.0 - 74 LYS 74 E B - 190.7 - - - - - - - - 180.1 -2.9 36.0 - * * 75 VAL 75 E B - 178.8 - - - - - - - - 178.6 -3.3 33.9 - +* +* 76 ASP 76 E B - 183.8 - - - - - - - - 184.6 -.9 34.2 - +* +* 77 THR 77 e A 54.3 - - - - - - - - - 178.6 -2.4 33.4 - 78 ASP 78 T A - 180.7 - - - - - - - - 176.4 - 35.2 - 79 GLU 79 T a - 193.4 - - - - - - - - 181.3 - 37.3 - 80 LEU 80 h b - - -69.1 - - - - - - - 179.0 -3.4 34.1 - +* +* 81 LYS 81 H A - - -63.0 182.6 - -69.4 -39.5 - - - 180.9 -1.4 32.7 - 82 SER 82 H A - - -57.1 - - -65.3 -34.3 - - - 178.3 - 33.7 - 83 VAL 83 H A - 178.4 - - - -72.3 -46.1 - - - 178.7 - 34.1 - 84 ALA 84 H A - - - - - -59.3 -36.1 - - - 179.5 -2.2 34.3 - 85 SER 85 H A - 189.1 - - - -70.8 -43.7 - - - 184.3 -2.3 34.7 - 86 ASP 86 H A - 180.1 - - - -68.9 -36.6 - - - 181.8 -2.1 34.2 - 87 TRP 87 h A - - -64.5 - - - - - - - 177.6 -2.6 32.4 - 88 ALA 88 T l - - - - - - - - - - 175.9 -.8 31.2 - +* +* 89 ILE 89 t b - - -58.5 - - - - - - - 182.3 -1.1 33.8 - * * 90 GLN 90 A - 179.2 - 182.5 - - - - - - 184.7 -.7 34.8 - +* +* 91 ALA 91 S B - - - - - - - - - - 175.4 - 33.1 - 92 MET 92 S B - - -56.2 168.1 - - - - - - 1.1 - 35.4 - 93 PRO 93 e cis - - - - - -93.7 - - - - - 176.7 - 39.9 - +** +* +** 94 THR 94 E B - - -66.5 - - - - - - - 179.1 -2.5 33.3 - 95 PHE 95 E B - - -64.6 - - - - - - - 180.7 -2.5 35.2 - 96 MET 96 E B - 180.3 - 179.5 - - - - - - 180.4 -3.1 33.9 - * * 97 PHE 97 E B - - -68.0 - - - - - - - 177.9 -2.9 36.5 - * * 98 LEU 98 E B 66.4 - - - - - - - - - 183.9 -1.8 31.4 - 99 LYS 99 E B - 178.4 - 175.8 - - - - - - 174.8 -3.5 33.6 - ** ** 100 GLU 100 T l - - -55.2 173.2 - - - - - - 180.8 - 33.5 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 GLY 101 T - - - - - - - - - - - 176.4 - - - 102 LYS 102 E B - 186.9 - 175.9 - - - - - - 186.1 -1.2 33.7 - * * * 103 ILE 103 E B - - -57.6 178.8 - - - - - - 179.1 - 32.6 - 104 LEU 104 E a - - -75.8 181.1 - - - - - - 189.8 -2.0 34.0 - +* +* 105 ASP 105 E B - 186.6 - - - - - - - - 183.5 -2.8 34.8 - 106 LYS 106 E B - 188.5 - 185.9 - - - - - - 179.4 - 35.0 - 107 VAL 107 E B - 180.9 - - - - - - - - 182.7 -3.1 35.2 - * * 108 VAL 108 E B 56.7 - - - - - - - - - 182.4 -.6 33.5 - +* +* 109 GLY 109 e - - - - - - - - - - - 180.2 -2.5 - - 110 ALA 110 B - - - - - - - - - - 176.7 - 34.0 - 111 LYS 111 h B - 187.6 - - - - - - - - 186.1 -.9 36.8 - * +* +* 112 LYS 112 H A - 187.2 - 180.8 - -64.0 -39.6 - - - 180.1 - 34.1 - 113 ASP 113 H A - 176.0 - - - -69.8 -46.5 - - - 180.6 - 33.6 - 114 GLU 114 H A - 185.6 - - - -66.3 -30.8 - - - 177.6 - 34.3 - 115 LEU 115 H A - 180.8 - - - -57.4 -54.4 - - - 179.5 -2.0 37.2 - * * 116 GLN 116 H A - - -65.5 - - -62.4 -40.2 - - - 180.7 -1.7 33.7 - 117 SER 117 H A - - -55.1 - - -67.2 -36.7 - - - 178.8 -2.2 34.1 - 118 THR 118 H A - - -58.3 - - -71.9 -28.9 - - - 172.8 -2.7 31.4 - * * 119 ILE 119 H A - - -59.4 178.1 - -62.7 -50.0 - - - 180.4 -1.7 34.3 - 120 ALA 120 H A - - - - - -60.8 -30.8 - - - 178.3 -2.2 32.8 - 121 LYS 121 H A - - -75.1 180.8 - -57.2 -35.6 - - - 182.8 -1.6 36.9 - 122 HIS 122 H A - - -64.7 - - -105.2 -24.7 - - - 181.6 -1.3 34.7 - *** * *** 123 LEU 123 h B - - -85.5 - - - - - - - 176.4 -2.5 33.8 - * * 124 ALA 124 - - - - - - - - - - - - -1.1 33.9 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * ** +** *** ** *** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.4 183.3 -63.8 180.3 -71.6 -66.6 -39.2 51.2 - 2.0 179.7 -2.0 34.3 *** *** Standard deviations: 5.1 6.5 8.1 9.4 16.4 9.1 8.9 .0 - .0 3.0 .8 1.7 Numbers of values: 12 53 37 29 4 46 46 2 0 2 122 78 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_11 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_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 - 1.241 1.527 1.542 1.457 - 115.42 120.70 111.38 111.12 110.94 123.74 2 GLY 2 1.341 1.238 1.530 - 1.466 123.32 114.77 120.74 - 114.65 - 124.48 +* +* 3 HIS 3 1.330 1.225 1.506 1.565 1.489 127.37 114.15 121.36 107.35 106.46 115.59 124.45 +* +* *** * * +* +** *** 4 HIS 4 1.336 1.226 1.523 1.544 1.454 125.13 117.11 120.49 109.79 107.28 112.15 122.32 +* * +* 5 HIS 5 1.309 1.229 1.515 1.565 1.454 120.69 114.79 121.23 111.84 112.73 113.02 123.92 * +* * +* 6 HIS 6 1.311 1.236 1.519 1.556 1.462 124.85 117.86 119.86 107.83 108.60 112.93 122.24 * * +* * * +* 7 HIS 7 1.324 1.235 1.521 1.570 1.458 119.69 115.25 121.77 112.71 109.37 114.42 122.92 ** * * ** ** 8 HIS 8 1.297 1.232 1.501 1.546 1.432 122.17 116.02 120.26 109.73 109.94 109.55 123.71 ** * * ** 9 LEU 9 1.315 1.236 1.521 1.562 1.435 121.26 116.72 120.64 114.21 109.65 111.33 122.54 * +* * ** ** 10 GLU 10 1.299 1.233 1.517 1.537 1.429 120.30 114.62 122.09 113.32 113.09 111.59 123.23 ** +* +* ** 11 MET 11 1.300 1.234 1.496 1.549 1.443 123.91 116.69 120.52 109.22 107.88 112.47 122.74 ** * * * * ** 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 1.299 1.240 1.511 1.519 1.430 120.29 116.27 120.80 110.94 109.55 111.06 122.89 ** * ** 13 SER 13 1.288 1.234 1.517 1.532 1.418 121.46 116.97 119.39 112.33 108.38 109.26 123.60 +** ** * * +** 14 GLU 14 1.324 1.241 1.525 1.533 1.454 122.68 115.85 120.37 110.84 110.03 110.11 123.77 15 GLU 15 1.331 1.248 1.528 1.536 1.456 123.48 115.17 121.83 110.93 113.42 111.13 122.98 16 GLY 16 1.307 1.229 1.486 - 1.426 121.07 116.14 120.83 - 110.88 - 123.03 +* +* +* +* 17 GLN 17 1.311 1.228 1.473 1.509 1.422 119.95 113.01 122.43 111.31 113.14 113.40 124.53 * ** * +* +* +* ** 18 VAL 18 1.258 1.232 1.515 1.551 1.423 124.11 118.84 119.15 109.39 106.04 110.90 122.00 *5.0* +* * * +* *5.0* 19 ILE 19 1.307 1.239 1.518 1.545 1.444 118.73 115.97 120.79 110.81 110.24 111.90 123.24 +* +* +* 20 ALA 20 1.312 1.233 1.505 1.522 1.437 122.01 115.73 121.15 110.89 109.62 111.07 123.13 * * * 21 CYS 21 1.296 1.237 1.512 1.510 1.409 121.71 115.92 120.90 109.68 109.87 108.89 123.14 ** +** +** 22 HIS 22 1.302 1.227 1.502 1.540 1.449 122.26 115.26 121.32 110.64 109.28 112.18 123.40 +* * +* 23 THR 23 1.315 1.246 1.516 1.555 1.439 122.44 116.91 120.04 108.28 108.54 110.88 123.06 * * 24 VAL 24 1.319 1.232 1.518 1.545 1.458 121.49 114.12 121.83 109.28 107.91 111.46 124.02 * * * 25 GLU 25 1.319 1.237 1.534 1.547 1.446 124.46 116.45 120.65 112.57 110.62 106.19 122.84 +* * +** +** 26 THR 26 1.316 1.240 1.539 1.541 1.455 120.97 115.56 121.08 110.87 110.57 110.59 123.33 27 TRP 27 1.323 1.233 1.534 1.539 1.452 122.97 115.93 120.92 111.71 111.54 108.78 123.14 * * 28 ASN 28 1.317 1.243 1.529 1.548 1.457 122.57 115.71 120.63 111.11 110.12 109.53 123.64 29 GLU 29 1.328 1.235 1.534 1.528 1.460 122.89 117.16 120.43 111.40 112.45 110.52 122.39 30 GLN 30 1.324 1.231 1.521 1.484 1.426 121.53 116.92 120.49 110.83 112.92 110.16 122.58 ** +* ** 31 LEU 31 1.318 1.221 1.503 1.486 1.415 121.79 115.81 120.56 110.04 110.62 109.28 123.63 * ** ** ** 32 GLN 32 1.317 1.208 1.518 1.544 1.448 122.92 116.05 120.35 111.23 107.19 108.98 123.54 * * * 33 LYS 33 1.327 1.237 1.534 1.542 1.455 122.68 116.74 120.44 110.55 111.03 110.38 122.80 34 ALA 34 1.332 1.226 1.526 1.514 1.451 121.22 116.02 120.71 110.43 111.41 110.43 123.27 35 ASN 35 1.315 1.239 1.516 1.525 1.466 123.26 114.47 121.47 108.34 109.23 108.89 124.06 * * 36 GLU 36 1.315 1.233 1.529 1.528 1.469 123.71 116.61 120.74 108.21 111.73 109.18 122.63 * * 37 SER 37 1.308 1.248 1.531 1.508 1.438 121.24 115.78 120.75 111.18 111.65 108.69 123.46 +* * * * +* 38 LYS 38 1.350 1.225 1.553 1.513 1.429 124.43 115.00 122.32 112.58 109.44 108.37 122.65 +* * * +* * * +* 39 THR 39 1.307 1.241 1.527 1.525 1.436 123.05 115.68 121.28 108.77 109.86 110.06 123.03 +* * +* 40 LEU 40 1.287 1.237 1.534 1.564 1.437 122.36 116.96 120.32 112.31 106.99 109.17 122.71 +** +* * * +* +** 41 VAL 41 1.309 1.241 1.528 1.568 1.435 121.39 115.43 121.19 111.48 111.53 111.40 123.34 * * * * * 42 VAL 42 1.309 1.242 1.511 1.538 1.436 122.66 116.61 120.69 109.51 108.26 112.16 122.69 * * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.298 1.239 1.519 1.546 1.432 120.95 114.90 120.94 109.47 111.24 111.74 124.15 ** * ** 44 ASP 44 1.301 1.232 1.510 1.537 1.451 124.31 116.86 120.25 109.33 110.81 109.17 122.83 ** * ** 45 PHE 45 1.315 1.240 1.523 1.524 1.415 121.11 116.25 120.78 108.89 107.98 109.98 122.95 ** * ** 46 THR 46 1.300 1.233 1.533 1.572 1.437 122.01 117.67 119.71 111.62 108.45 110.87 122.60 ** * * * ** 47 ALA 47 1.316 1.241 1.511 1.513 1.451 121.67 115.95 120.46 110.45 109.80 111.61 123.57 48 SER 48 1.319 1.234 1.541 1.541 1.456 123.03 117.09 120.52 110.95 112.23 109.82 122.38 49 TRP 49 1.329 1.232 1.535 1.551 1.465 121.34 117.03 120.56 111.35 113.24 111.87 122.40 * * 50 CYS 50 1.308 1.231 1.531 1.538 1.449 121.49 116.06 120.37 111.84 110.32 109.74 123.56 * * 51 GLY 51 1.334 1.232 1.530 - 1.469 123.05 119.11 119.65 - 114.19 - 121.24 * * * * * 52 PRO 52 1.361 1.232 1.527 1.534 1.482 122.71 114.90 121.82 110.33 111.39 103.42 123.27 * * * * 53 CYS 53 1.303 1.222 1.535 1.505 1.441 123.27 116.44 121.11 109.51 110.28 108.55 122.43 +* * * +* 54 ARG 54 1.312 1.211 1.516 1.533 1.444 121.38 115.90 120.60 110.26 109.20 111.55 123.48 * * * 55 PHE 55 1.328 1.234 1.534 1.548 1.470 123.50 116.47 121.08 109.79 111.90 109.79 122.44 56 ILE 56 1.306 1.238 1.560 1.566 1.446 121.12 115.74 121.36 110.69 110.85 109.98 122.80 +* +* +* 57 ALA 57 1.324 1.236 1.566 1.517 1.466 122.99 120.78 119.02 111.38 115.47 110.83 120.21 +* ** * +* +* ** 58 PRO 58 1.387 1.238 1.518 1.531 1.477 121.93 115.77 121.23 109.67 111.80 103.89 122.99 +** +** 59 PHE 59 1.316 1.222 1.525 1.533 1.436 121.25 116.03 120.95 111.17 109.57 110.84 122.99 * * 60 PHE 60 1.322 1.232 1.529 1.537 1.462 122.39 115.83 121.36 111.33 109.59 109.58 122.80 61 ALA 61 1.319 1.237 1.529 1.521 1.450 121.51 115.90 121.17 110.74 110.22 110.50 122.92 62 ASP 62 1.327 1.222 1.498 1.510 1.465 122.03 114.81 121.13 109.00 109.05 110.54 124.05 * * 63 LEU 63 1.322 1.230 1.529 1.525 1.439 123.90 116.45 120.46 110.16 111.85 109.61 123.08 * * * 64 ALA 64 1.323 1.227 1.521 1.514 1.453 121.80 115.99 121.02 110.44 111.38 110.52 122.99 65 LYS 65 1.316 1.236 1.525 1.530 1.451 122.03 114.90 121.54 110.78 109.60 109.13 123.56 66 LYS 66 1.318 1.240 1.525 1.538 1.444 123.50 116.09 121.05 109.24 110.73 108.47 122.85 * * 67 LEU 67 1.313 1.223 1.510 1.511 1.416 121.76 116.88 120.86 110.61 113.24 109.61 122.24 * ** ** 68 PRO 68 1.337 1.237 1.540 1.537 1.472 122.80 114.64 121.69 110.15 110.60 103.38 123.66 +* * +* 69 ASN 69 1.324 1.229 1.526 1.551 1.459 124.31 115.53 121.47 110.43 109.49 108.22 122.97 * * * * 70 VAL 70 1.307 1.229 1.524 1.553 1.440 122.08 116.18 120.65 110.15 110.04 111.18 123.13 +* +* 71 LEU 71 1.307 1.229 1.551 1.563 1.445 122.15 118.07 119.95 112.65 106.48 107.81 121.90 +* * +* * +* +* +* 72 PHE 72 1.323 1.250 1.530 1.526 1.469 120.82 115.19 121.39 108.55 112.95 111.51 123.42 73 LEU 73 1.317 1.222 1.498 1.535 1.464 123.78 115.15 120.87 107.76 111.14 114.49 123.97 * * * ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 LYS 74 1.302 1.228 1.515 1.568 1.433 123.41 116.20 121.07 113.12 105.67 106.92 122.70 +* +* * +* +* ** ** 75 VAL 75 1.301 1.235 1.512 1.558 1.442 122.26 115.88 121.23 110.02 109.41 111.90 122.80 +* +* 76 ASP 76 1.297 1.225 1.506 1.519 1.439 120.97 116.85 120.10 111.19 107.80 110.47 123.03 ** * ** 77 THR 77 1.311 1.220 1.512 1.535 1.453 121.88 116.62 120.66 109.84 112.66 111.43 122.71 * * 78 ASP 78 1.308 1.234 1.513 1.524 1.455 121.52 113.69 122.28 110.75 107.82 109.25 124.02 +* * * +* 79 GLU 79 1.300 1.230 1.525 1.518 1.438 123.88 115.31 121.54 108.09 108.55 108.42 123.14 ** * * * * ** 80 LEU 80 1.317 1.241 1.524 1.529 1.419 122.83 116.42 120.83 109.02 111.91 111.56 122.73 ** ** 81 LYS 81 1.310 1.231 1.517 1.523 1.454 121.31 116.07 120.98 110.85 111.26 111.71 122.94 * * 82 SER 82 1.320 1.231 1.531 1.517 1.443 121.99 116.42 120.60 111.33 111.13 109.85 122.95 83 VAL 83 1.325 1.229 1.521 1.551 1.454 121.55 115.78 121.00 109.92 109.40 111.60 123.19 84 ALA 84 1.327 1.228 1.524 1.523 1.455 122.28 115.80 121.23 110.31 110.62 110.15 122.97 85 SER 85 1.315 1.238 1.542 1.536 1.429 121.82 116.14 120.73 110.82 110.38 109.41 123.08 +* +* 86 ASP 86 1.332 1.244 1.532 1.539 1.474 122.79 116.39 120.97 109.92 112.47 110.09 122.63 87 TRP 87 1.316 1.243 1.526 1.525 1.447 121.80 115.07 120.81 112.01 112.19 110.63 124.11 * * 88 ALA 88 1.332 1.242 1.526 1.531 1.461 124.72 115.28 121.44 111.58 113.29 112.12 123.23 +* * +* 89 ILE 89 1.305 1.236 1.510 1.562 1.446 122.86 114.98 121.43 110.84 108.29 111.71 123.47 +* * +* 90 GLN 90 1.308 1.234 1.526 1.528 1.449 122.67 116.18 120.83 109.91 111.73 109.61 122.98 +* +* 91 ALA 91 1.307 1.211 1.494 1.519 1.448 121.11 116.80 120.97 110.60 111.39 111.42 122.19 +* * * +* 92 MET 92 1.277 1.236 1.521 1.513 1.430 120.49 118.99 119.72 110.08 107.36 109.74 121.29 +*** * * * * +*** 93 PRO 93 1.335 1.228 1.558 1.520 1.454 124.33 116.74 121.03 109.95 112.71 101.77 122.21 +* * +* 94 THR 94 1.303 1.223 1.525 1.531 1.446 122.04 116.38 120.85 110.12 110.62 111.87 122.75 +* +* 95 PHE 95 1.303 1.234 1.505 1.518 1.416 122.28 116.63 120.58 110.17 109.05 109.80 122.79 +* ** ** 96 MET 96 1.296 1.234 1.499 1.521 1.436 120.82 114.99 121.26 110.18 110.19 111.20 123.75 ** * * ** 97 PHE 97 1.292 1.245 1.509 1.522 1.402 123.24 116.49 121.03 109.55 109.45 108.49 122.48 +** +** * +** 98 LEU 98 1.286 1.227 1.506 1.563 1.416 120.52 117.52 120.19 114.49 108.76 111.52 122.29 *** +* ** ** *** 99 LYS 99 1.283 1.236 1.492 1.520 1.419 120.20 114.19 121.13 111.19 111.59 110.31 124.62 *** +* ** * * *** 100 GLU 100 1.331 1.223 1.531 1.516 1.452 124.80 115.58 121.32 111.61 111.48 109.58 123.01 +* +* 101 GLY 101 1.319 1.225 1.522 - 1.446 121.40 117.11 120.15 - 113.30 - 122.73 102 LYS 102 1.326 1.232 1.542 1.526 1.456 121.23 116.91 120.17 111.87 109.37 109.88 122.92 103 ILE 103 1.330 1.237 1.544 1.564 1.482 123.07 116.01 121.08 110.85 113.33 111.24 122.89 * * 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 1.345 1.226 1.524 1.528 1.448 122.90 117.40 120.49 108.65 113.56 111.33 122.10 * * 105 ASP 105 1.315 1.235 1.476 1.540 1.444 120.54 115.87 120.80 110.90 108.66 110.05 123.32 ** ** 106 LYS 106 1.253 1.229 1.518 1.539 1.422 120.91 116.85 120.42 110.31 109.42 109.94 122.72 *5.5* +* *5.5* 107 VAL 107 1.308 1.228 1.501 1.559 1.442 121.16 115.36 120.91 108.70 107.81 111.88 123.72 +* * * +* 108 VAL 108 1.297 1.239 1.532 1.569 1.426 122.67 115.80 121.31 112.39 110.14 110.10 122.84 ** * +* * ** 109 GLY 109 1.310 1.243 1.507 - 1.434 121.09 117.37 120.39 - 110.04 - 122.24 * * * 110 ALA 110 1.308 1.233 1.512 1.524 1.431 119.71 115.85 121.29 110.74 109.38 110.78 122.77 +* * * +* 111 LYS 111 1.294 1.228 1.515 1.504 1.401 122.95 117.21 119.73 110.31 106.47 107.61 123.05 ** * +** +* +* +** 112 LYS 112 1.315 1.233 1.547 1.523 1.446 122.20 116.33 121.02 110.97 111.71 109.39 122.62 * * 113 ASP 113 1.319 1.236 1.521 1.529 1.468 122.01 116.25 121.00 109.94 111.80 111.11 122.75 114 GLU 114 1.320 1.224 1.522 1.532 1.468 121.94 115.82 120.67 110.33 109.71 110.40 123.50 115 LEU 115 1.323 1.228 1.515 1.516 1.454 123.07 115.02 121.18 108.52 109.46 107.95 123.74 * * 116 GLN 116 1.315 1.235 1.514 1.530 1.464 122.53 116.34 120.58 110.01 111.50 111.14 123.05 * * 117 SER 117 1.315 1.220 1.531 1.515 1.439 121.08 116.31 120.96 111.23 110.62 109.50 122.71 * * * 118 THR 118 1.314 1.246 1.529 1.540 1.441 122.07 116.95 120.44 113.20 111.31 111.35 122.60 * +* +* 119 ILE 119 1.331 1.228 1.530 1.555 1.444 119.95 115.64 121.04 109.20 107.77 112.48 123.21 * * 120 ALA 120 1.327 1.225 1.528 1.517 1.462 122.80 116.86 120.18 110.89 112.31 111.02 122.95 121 LYS 121 1.334 1.234 1.531 1.503 1.413 123.43 116.42 120.86 108.96 111.72 107.49 122.72 * ** +* ** 122 HIS 122 1.324 1.232 1.521 1.519 1.433 121.95 116.87 120.55 109.66 112.22 109.83 122.58 * * 123 LEU 123 1.312 1.233 1.503 1.512 1.406 122.11 115.45 121.09 111.03 112.22 109.95 123.43 * * +** +** 124 ALA 124 1.299 - 1.515 1.524 1.428 122.11 - - 111.41 108.10 110.73 - ** +* * ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.5* * ** ** +** *** ** * ** +* +** +* *5.5* ----------------------------------------------------------------------------------------------------------------------------------- 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 1.253 1.350 1.313 .015 *5.5* +* * C-N (Pro) 1.341 .016 4 1.335 1.387 1.355 .021 +** C-O C-O 1.231 .020 123 1.208 1.250 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.473 1.566 1.522 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.486 1.530 1.515 .016 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.513 1.531 1.520 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.572 1.551 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.484 1.570 1.531 .017 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.401 1.489 1.444 .017 +** +* NH1-CH2G* (Gly) 1.451 .016 5 1.426 1.469 1.448 .017 +* * N-CH1E (Pro) 1.466 .015 4 1.454 1.482 1.471 .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 2.0 114 113.01 120.78 116.10 1.03 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.77 119.11 116.90 1.43 * CH1E-C-N (Pro) 116.9 1.5 4 114.64 116.74 115.51 .82 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.21 124.62 123.02 .65 +* * O-C-N (Pro) 122.0 1.4 4 122.21 123.66 123.03 .53 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.73 127.37 122.21 1.32 +* *** C-NH1-CH2G* (Gly) 120.6 1.7 5 121.07 123.32 121.99 .99 +* C-N-CH1E (Pro) 122.6 5.0 4 121.93 124.33 122.94 .87 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.02 122.43 120.85 .58 * CH2G*-C-O (Gly) 120.8 2.1 5 119.65 120.83 120.35 .43 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.31 111.58 110.83 .39 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.28 113.20 110.24 1.19 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 107.35 114.49 110.55 1.39 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.67 115.47 110.26 1.88 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 5 110.04 114.65 112.61 1.83 N-CH1E-C (Pro) 111.8 2.5 4 110.60 112.71 111.62 .76 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.15 112.12 110.94 .52 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.98 112.48 111.30 .67 N-CH1E-CH2E (Pro) 103.0 1.1 4 101.77 103.89 103.11 .80 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.19 115.59 110.14 1.65 +** +** ------------------------------------------------------------------------------------------------------------- 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] 98 86.7% Residues in additional allowed regions [a,b,l,p] 13 11.5% Residues in generously allowed regions [~a,~b,~l,~p] 2 1.8% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 113 86.7 83.8 10.0 .3 Inside b. Omega angle st dev 122 3.0 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 78 .8 .8 .2 .2 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 12 5.1 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 53 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 37 8.1 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 102 7.6 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 29 9.4 20.4 5.0 -2.2 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 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 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 -.21 Chi1-chi2 distribution -.12 Chi1 only -.11 Chi3 & chi4 .52 Omega .07 ------ -.01 ===== Main-chain covalent forces:- Main-chain bond lengths .00 Main-chain bond angles .40 ------ .23 ===== OVERALL AVERAGE .07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.