Residue-by-residue listing for refined_1 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 - - 174.6 - - - - - - - - 175.7 - 33.2 - 2 GLY 2 - - - - - - - - - - - 180.1 - - - 3 HIS 3 S B - - -68.3 - - - - - - - 181.8 - 32.5 - 4 HIS 4 S l - - -64.1 - - - - - - - 177.5 - 29.9 - * * 5 HIS 5 S b - - -67.0 - - - - - - - 172.0 - 35.6 - * * 6 HIS 6 S B 63.7 - - - - - - - - - 182.8 - 32.6 - 7 HIS 7 S B - 182.7 - - - - - - - - 184.5 - 32.0 - 8 HIS 8 B 58.5 - - - - - - - - - 175.6 - 35.7 - 9 LEU 9 b 59.9 - - 172.1 - - - - - - 185.2 - 30.6 - 10 GLU 10 B - 186.4 - - - - - - - - 179.1 - 33.4 - 11 MET 11 B 62.9 - - - - - - - - - 181.0 -.6 34.1 - +* +* 12 ALA 12 B - - - - - - - - - - 175.9 - 33.6 - 13 SER 13 B 49.8 - - - - - - - - - 181.4 -1.1 33.8 - * * 14 GLU 14 B - 183.7 - 174.5 - - - - - - 182.6 -.5 32.4 - ** ** 15 GLU 15 B - - -56.8 174.3 - - - - - - 175.5 -1.0 36.8 - * * 16 GLY 16 S - - - - - - - - - - - 182.3 -.8 - - +* +* 17 GLN 17 B 53.1 - - 184.2 - - - - - - 180.4 - 32.0 - 18 VAL 18 B 61.9 - - - - - - - - - 185.3 - 34.5 - 19 ILE 19 E B - - -58.7 180.5 - - - - - - 176.8 -2.6 33.7 - 20 ALA 20 E B - - - - - - - - - - 182.8 -.6 34.2 - +* +* Residue-by-residue listing for refined_1 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B - - -56.2 - - - - - - - 177.8 -.9 35.3 - +* +* 22 HIS 22 a - - -64.0 - - - - - - - 182.2 - 34.1 - 23 THR 23 h B 53.2 - - - - - - - - - 177.5 - 35.0 - 24 VAL 24 H A 63.8 - - - - -71.2 -22.1 - - - 175.1 - 32.3 - +* +* 25 GLU 25 H A - - -70.8 - - -56.3 -51.2 - - - 180.0 - 37.2 - * * 26 THR 26 H A - - -52.6 - - -73.6 -37.1 - - - 178.0 - 35.0 - 27 TRP 27 H A - 174.0 - - - -53.3 -52.7 - - - 179.8 -2.0 34.5 - * * * 28 ASN 28 H A - 180.3 - - - -62.1 -44.2 - - - 182.2 -2.8 34.9 - * * 29 GLU 29 H A - 185.5 - - - -57.8 -46.0 - - - 181.9 -1.6 34.5 - 30 GLN 30 H A - - -65.5 - - -67.6 -39.3 - - - 175.9 -2.7 33.0 - 31 LEU 31 H A - - -66.2 180.4 - -66.2 -41.7 - - - 174.3 -1.8 35.2 - 32 GLN 32 H A - 172.2 - 176.1 - -57.1 -46.6 - - - 177.2 -2.9 33.4 - * * 33 LYS 33 H A - - -66.3 - - -65.9 -34.0 - - - 176.2 -2.7 31.2 - 34 ALA 34 H A - - - - - -65.9 -38.4 - - - 179.5 -2.2 33.8 - 35 ASN 35 H A - 185.6 - - - -72.2 -54.2 - - - 182.7 -2.5 36.9 - * * 36 GLU 36 H A - 183.4 - 178.3 - -58.9 -43.5 - - - 183.0 -3.9 34.6 - ** ** 37 SER 37 h A - - -57.5 - - - - - - - 178.9 -2.5 35.0 - 38 LYS 38 T L - - -78.1 170.4 - - - - - - 179.4 -1.0 32.6 - * * 39 THR 39 e B - - -45.3 - - - - - - - 181.1 -1.3 35.6 - * * 40 LEU 40 E B - 182.9 - 168.4 - - - - - - 186.6 -.9 33.8 - * +* +* 41 VAL 41 E B 60.5 - - - - - - - - - 177.5 -1.1 33.2 - * * 42 VAL 42 E B - 182.1 - - - - - - - - 183.4 -2.4 34.0 - 43 VAL 43 E B - 183.3 - - - - - - - - 174.7 -3.2 34.1 - +* +* 44 ASP 44 E B - 163.3 - - - - - - - - 176.8 -3.4 35.4 - * +* +* 45 PHE 45 E B - - -61.3 - - - - - - - 189.9 -3.3 34.6 - +* +* +* 46 THR 46 E B - 182.1 - - - - - - - - 171.1 -2.7 37.2 - +* +* 47 ALA 47 t B - - - - - - - - - - 179.7 - 33.5 - 48 SER 48 T A - - -55.0 - - - - - - - 177.5 - 34.1 - 49 TRP 49 T A 51.0 - - - - - - - - - 181.9 - 32.0 - 50 CYS 50 h B - 176.3 - 215.6 - - - 57.2 - 2.0 183.0 -2.3 33.7 - ** +** +** 51 GLY 51 H - - - - - - -68.3 -75.0 - - - 180.6 - - - *** *** 52 PRO 52 H - - - - - -53.2 -53.2 -33.8 - - - 179.0 - 38.5 - * * * * 53 CYS 53 H A - - -54.0 - - -60.5 -44.8 57.2 - 2.0 181.5 - 35.5 - +** +** 54 ARG 54 H A - 181.1 - 183.2 - -74.5 -29.9 - - - 181.0 -1.4 34.5 - 55 PHE 55 H A - 181.4 - - - -67.0 -41.3 - - - 183.2 -1.9 33.8 - 56 ILE 56 H A - 187.7 - 175.4 - -90.8 -14.2 - - - 180.3 -2.0 33.2 - ** ** ** Residue-by-residue listing for refined_1 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 - - - - - -52.1 -46.1 - - - 179.9 -1.1 32.3 - * * * 58 PRO 58 H - - - - - -57.7 -57.7 -32.3 - - - 179.9 - 38.3 - * * 59 PHE 59 H A - 181.0 - - - -72.7 -36.1 - - - 178.1 -.9 33.1 - +* +* 60 PHE 60 H A - 184.3 - - - -68.5 -35.8 - - - 175.9 -1.4 33.9 - 61 ALA 61 H A - - - - - -67.9 -32.2 - - - 178.3 -2.2 33.9 - 62 ASP 62 H A - 185.9 - - - -69.1 -43.8 - - - 176.1 -1.5 35.3 - 63 LEU 63 H A - - -69.9 180.0 - -53.2 -39.1 - - - 178.6 -2.5 34.7 - * * 64 ALA 64 H A - - - - - -64.9 -33.1 - - - 178.3 -1.4 34.0 - 65 LYS 65 H A - 182.1 - 179.2 - -80.2 -32.7 - - - 182.7 -.9 34.1 - * * * 66 LYS 66 H A - 184.9 - 180.2 - -74.5 -40.4 - - - 177.5 -2.4 34.6 - 67 LEU 67 h b - - -66.3 - - - - - - - 183.3 -3.0 34.0 - * * 68 PRO 68 T - - - - - -83.3 - - - - - 180.2 - 39.1 - +* * +* 69 ASN 69 e A - - -54.8 - - - - - - - 181.8 - 35.6 - 70 VAL 70 E B - 178.7 - - - - - - - - 181.1 -1.0 34.0 - * * 71 LEU 71 E B - 205.5 - 184.9 - - - - - - 181.0 -3.3 36.0 - * +* +* 72 PHE 72 E B - - -61.3 - - - - - - - 178.2 -.7 34.8 - +* +* 73 LEU 73 E B - - -66.8 - - - - - - - 173.6 -2.6 34.4 - * * 74 LYS 74 E B - - -63.0 190.1 - - - - - - 183.6 -2.5 35.5 - 75 VAL 75 E B - 176.7 - - - - - - - - 178.0 -3.7 33.7 - ** ** 76 ASP 76 E B - 184.9 - - - - - - - - 183.6 -.9 33.7 - * * 77 THR 77 e A 51.0 - - - - - - - - - 176.2 -3.7 33.0 - ** ** 78 ASP 78 T A - 184.6 - - - - - - - - 173.4 - 34.3 - * * 79 GLU 79 T A - - -67.4 - - - - - - - 183.6 - 36.1 - 80 LEU 80 h b - - -67.8 - - - - - - - 177.6 -3.2 33.9 - +* +* 81 LYS 81 H A - - -64.6 - - -69.8 -40.8 - - - 182.4 -1.5 32.4 - 82 SER 82 H A - - -57.3 - - -66.1 -38.7 - - - 179.1 - 33.2 - 83 VAL 83 H A - 179.7 - - - -67.0 -42.4 - - - 179.5 - 33.8 - 84 ALA 84 H A - - - - - -62.0 -37.5 - - - 178.4 -1.6 33.7 - 85 SER 85 H A - 184.6 - - - -75.9 -44.3 - - - 185.0 -2.0 34.1 - 86 ASP 86 H A - 180.5 - - - -61.3 -36.3 - - - 180.0 -3.1 34.1 - * * 87 TRP 87 h A - - -62.0 - - - - - - - 180.5 -2.2 32.7 - 88 ALA 88 T l - - - - - - - - - - 182.3 -1.2 31.6 - * * 89 ILE 89 t B - - -55.2 179.1 - - - - - - 180.8 -2.2 34.1 - 90 GLN 90 A - 183.0 - 181.9 - - - - - - 180.8 -.7 34.2 - +* +* 91 ALA 91 S B - - - - - - - - - - 184.1 - 33.6 - 92 MET 92 S B - - -59.1 174.4 - - - - - - -2.7 - 36.5 - 93 PRO 93 e cis - - - - - -86.2 - - - - - 175.6 - 39.4 - +* +* +* Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 THR 94 E B - - -64.0 - - - - - - - 176.5 -1.8 34.1 - 95 PHE 95 E B - - -59.8 - - - - - - - 182.8 -2.8 36.6 - * * 96 MET 96 E B - 183.8 - 166.0 - - - - - - 185.5 -3.4 31.8 - +* +* 97 PHE 97 E B - - -66.1 - - - - - - - 179.9 -3.1 36.6 - * * 98 LEU 98 E B - - -53.6 - - - - - - - 177.1 -3.1 34.9 - * * 99 LYS 99 E B - 171.4 - 176.6 - - - - - - 185.3 -3.1 33.8 - * * 100 GLU 100 e l - - -58.7 181.1 - - - - - - 184.5 -1.0 33.5 - * * 101 GLY 101 T - - - - - - - - - - - 179.5 - - - 102 LYS 102 E B - - -53.4 169.2 - - - - - - 186.1 -2.0 36.2 - * * 103 ILE 103 E B - - -64.3 170.7 - - - - - - 175.4 - 34.1 - 104 LEU 104 E a - - -67.0 183.1 - - - - - - 184.0 -1.8 33.9 - 105 ASP 105 E B 49.0 - - - - - - - - - 178.5 -2.4 32.7 - 106 LYS 106 E B 60.8 - - 167.4 - - - - - - 172.6 - 34.5 - * * 107 VAL 107 E B - 182.4 - - - - - - - - 179.1 -3.5 35.9 - +* +* 108 VAL 108 E B 62.3 - - - - - - - - - 180.7 -.5 32.1 - ** ** 109 GLY 109 e - - - - - - - - - - - 180.3 -2.3 - - 110 ALA 110 B - - - - - - - - - - 176.8 -.6 34.2 - +* +* 111 LYS 111 h B - - -64.9 182.6 - - - - - - 185.9 -.9 33.3 - * +* +* 112 LYS 112 H A - 204.6 - - - -63.4 -50.3 - - - 179.2 - 35.7 - * * 113 ASP 113 H A - 178.4 - - - -74.0 -48.0 - - - 185.2 - 33.5 - 114 GLU 114 H A - 183.8 - - - -57.1 -36.0 - - - 178.1 - 33.8 - 115 LEU 115 H A - 183.0 - - - -58.9 -51.4 - - - 178.8 -1.8 35.1 - * * 116 GLN 116 H A - - -56.0 179.2 - -59.5 -40.5 - - - 178.8 -.9 34.9 - * * 117 SER 117 H A - - -56.1 - - -63.2 -33.8 - - - 178.9 -2.4 34.2 - 118 THR 118 H A - - -52.0 - - -74.0 -31.9 - - - 175.9 -2.1 34.4 - 119 ILE 119 H A - - -58.8 - - -63.2 -46.1 - - - 178.6 -1.8 33.9 - 120 ALA 120 H A - - - - - -64.3 -31.7 - - - 176.4 -2.3 33.3 - 121 LYS 121 H A - 185.2 - 182.7 - -59.5 -42.2 - - - 180.5 -1.5 36.4 - 122 HIS 122 H A - - -73.8 - - -80.2 -27.7 - - - 178.4 -1.7 31.9 - * * * 123 LEU 123 h b - - -91.4 - - - - - - - 179.2 -1.8 32.4 - +* +* 124 ALA 124 - - - - - - - - - - - - -1.3 34.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * +* ** +* ** *** +** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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: 57.4 182.4 -62.2 178.8 -70.1 -65.7 -40.0 57.2 - 2.0 179.8 -2.0 34.2 +** +** Standard deviations: 5.5 7.0 7.8 8.9 17.0 8.1 9.5 .0 - .0 3.4 .9 1.6 Numbers of values: 15 41 46 31 4 46 46 2 0 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_1 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 - 1.233 1.516 1.537 1.457 - 116.42 120.71 110.57 111.47 111.33 122.87 2 GLY 2 1.310 1.232 1.505 - 1.434 120.63 117.18 120.13 - 109.96 - 122.69 * * * 3 HIS 3 1.302 1.232 1.508 1.531 1.454 121.27 115.23 120.66 110.89 111.67 111.92 124.11 +* +* 4 HIS 4 1.321 1.226 1.510 1.541 1.460 124.36 114.85 121.81 112.02 112.35 114.01 123.18 * * ** ** 5 HIS 5 1.299 1.239 1.499 1.553 1.449 123.53 116.56 120.31 107.86 107.87 111.98 123.13 ** * * * * * ** 6 HIS 6 1.306 1.255 1.528 1.559 1.436 120.63 117.78 119.08 112.45 107.42 112.04 123.14 +* * * * * * * +* 7 HIS 7 1.332 1.238 1.524 1.538 1.470 121.56 115.44 121.23 111.19 111.41 112.25 123.33 * * 8 HIS 8 1.301 1.218 1.508 1.551 1.440 122.88 116.39 120.20 109.84 109.86 109.41 123.42 +* * +* 9 LEU 9 1.293 1.238 1.509 1.562 1.436 122.01 114.21 122.36 112.82 108.56 114.25 123.29 +** +* * * ** +** 10 GLU 10 1.294 1.243 1.509 1.564 1.421 122.24 114.30 121.77 114.09 108.12 109.33 123.70 +** +* +* ** * +** 11 MET 11 1.293 1.240 1.506 1.551 1.426 123.36 116.49 120.60 110.84 108.32 111.25 122.86 +** * +* * +** Residue-by-residue listing for refined_1 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 1.291 1.237 1.513 1.521 1.430 121.25 115.93 120.79 111.13 110.56 110.62 123.18 +** * +** 13 SER 13 1.311 1.244 1.521 1.544 1.429 122.13 116.92 120.40 112.33 108.98 109.84 122.64 * +* * +* 14 GLU 14 1.315 1.235 1.520 1.528 1.441 120.68 115.03 121.29 112.38 110.04 111.14 123.62 * * 15 GLU 15 1.317 1.236 1.518 1.539 1.450 123.49 117.41 119.82 108.29 107.90 109.44 122.75 * * 16 GLY 16 1.319 1.230 1.512 - 1.449 119.95 117.23 120.25 - 113.98 - 122.52 17 GLN 17 1.312 1.229 1.493 1.524 1.443 120.49 114.03 121.53 111.16 113.11 111.85 124.44 * +* * +* 18 VAL 18 1.294 1.246 1.537 1.549 1.431 123.61 117.34 120.39 111.69 109.41 109.28 122.26 ** * * * * ** 19 ILE 19 1.318 1.218 1.525 1.554 1.450 121.03 116.56 120.94 110.14 111.78 111.20 122.50 20 ALA 20 1.308 1.235 1.519 1.525 1.445 121.24 116.63 120.51 110.60 108.74 110.73 122.85 * * 21 CYS 21 1.310 1.228 1.513 1.511 1.430 121.85 115.72 120.95 109.57 111.03 109.40 123.32 * * * 22 HIS 22 1.312 1.218 1.517 1.543 1.454 122.63 116.69 120.64 109.52 110.18 111.68 122.66 * * 23 THR 23 1.323 1.251 1.518 1.554 1.452 121.79 116.72 120.26 108.86 110.21 111.15 123.03 * * 24 VAL 24 1.327 1.240 1.543 1.566 1.453 121.30 115.06 121.73 111.69 109.13 112.47 123.21 * * 25 GLU 25 1.329 1.240 1.530 1.531 1.423 124.92 115.38 121.22 109.24 109.78 107.55 123.37 +* +* +* +* 26 THR 26 1.323 1.229 1.533 1.539 1.444 122.41 115.64 120.88 110.14 109.98 109.68 123.46 * * 27 TRP 27 1.329 1.233 1.533 1.535 1.463 123.07 116.05 120.78 110.87 111.45 109.14 123.15 28 ASN 28 1.324 1.227 1.520 1.531 1.463 121.90 115.53 120.72 109.25 110.48 110.41 123.73 29 GLU 29 1.323 1.221 1.536 1.531 1.458 122.94 116.84 120.59 109.99 111.43 109.94 122.55 30 GLN 30 1.321 1.228 1.523 1.486 1.421 122.00 116.97 120.47 111.92 112.82 109.40 122.55 ** +* ** 31 LEU 31 1.322 1.227 1.512 1.490 1.422 122.06 115.10 121.15 110.20 109.86 109.15 123.75 +* +* +* 32 GLN 32 1.308 1.202 1.508 1.521 1.437 123.40 117.46 119.74 111.82 110.71 110.07 122.79 * * * * 33 LYS 33 1.313 1.231 1.523 1.532 1.451 121.13 117.16 120.30 112.35 111.93 112.04 122.51 * * * 34 ALA 34 1.328 1.224 1.528 1.520 1.448 120.63 115.57 121.18 110.76 109.58 110.70 123.23 35 ASN 35 1.314 1.229 1.508 1.530 1.460 122.98 114.26 121.63 108.37 109.98 108.59 124.11 * * * 36 GLU 36 1.302 1.233 1.535 1.537 1.469 124.02 116.90 120.48 110.07 112.81 109.36 122.62 +* * +* 37 SER 37 1.311 1.239 1.535 1.516 1.436 121.25 117.35 119.73 110.09 112.60 108.76 122.92 * * * * 38 LYS 38 1.350 1.243 1.510 1.504 1.484 122.28 115.39 121.35 110.81 113.22 110.79 123.21 +* * * +* 39 THR 39 1.290 1.237 1.519 1.523 1.408 121.54 116.09 121.26 109.47 107.32 110.33 122.64 +** +** * +** 40 LEU 40 1.264 1.228 1.528 1.566 1.433 121.37 117.52 119.89 114.03 106.36 109.11 122.59 *4.6* +* * ** +* *4.6* 41 VAL 41 1.308 1.230 1.531 1.566 1.441 120.62 116.03 121.31 111.30 111.95 110.79 122.64 * * * Residue-by-residue listing for refined_1 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.302 1.237 1.504 1.535 1.438 121.93 116.51 120.67 109.30 108.59 112.56 122.81 +* * +* 43 VAL 43 1.296 1.230 1.522 1.546 1.430 120.78 115.03 121.00 109.32 111.59 111.51 123.96 ** * ** 44 ASP 44 1.297 1.225 1.506 1.534 1.449 124.32 116.80 120.59 109.70 109.43 109.87 122.54 ** * ** 45 PHE 45 1.296 1.238 1.512 1.508 1.412 121.40 115.58 120.87 111.13 108.26 109.82 123.49 ** * ** * ** 46 THR 46 1.296 1.222 1.524 1.564 1.436 122.44 116.06 120.84 108.87 109.67 108.28 122.97 ** * +* ** 47 ALA 47 1.297 1.234 1.500 1.514 1.429 123.28 116.50 119.86 110.57 107.28 112.31 123.63 ** * +* * * ** 48 SER 48 1.296 1.234 1.552 1.530 1.446 123.42 116.65 120.64 111.56 111.49 108.93 122.69 ** * ** 49 TRP 49 1.340 1.226 1.540 1.555 1.464 121.88 117.24 120.57 111.01 113.06 111.93 122.18 * * 50 CYS 50 1.314 1.238 1.522 1.535 1.458 121.26 115.97 120.62 110.98 110.49 110.50 123.41 * * 51 GLY 51 1.326 1.233 1.520 - 1.452 122.20 118.38 119.84 - 113.69 - 121.77 52 PRO 52 1.362 1.232 1.526 1.542 1.475 123.18 115.73 120.78 110.09 112.24 104.05 123.47 * * * 53 CYS 53 1.324 1.223 1.534 1.521 1.452 122.74 116.20 121.03 109.44 110.22 109.41 122.72 54 ARG 54 1.329 1.234 1.530 1.533 1.454 121.94 116.12 120.92 109.99 110.65 110.24 122.96 55 PHE 55 1.316 1.233 1.534 1.542 1.455 122.04 116.67 120.71 110.61 111.74 110.37 122.61 56 ILE 56 1.320 1.239 1.551 1.566 1.461 121.12 115.45 121.40 111.74 110.93 110.48 123.09 * * * 57 ALA 57 1.329 1.235 1.561 1.525 1.471 123.65 120.26 119.10 110.78 114.35 110.85 120.64 +* * ** * * * ** 58 PRO 58 1.383 1.236 1.525 1.528 1.473 122.05 116.71 120.47 110.14 112.81 103.91 122.80 +** +** 59 PHE 59 1.326 1.217 1.518 1.538 1.450 121.09 116.31 120.81 111.40 109.88 111.32 122.85 60 PHE 60 1.319 1.232 1.530 1.536 1.458 121.74 115.92 121.23 111.35 109.51 110.16 122.85 61 ALA 61 1.322 1.233 1.531 1.519 1.454 121.52 115.53 121.26 110.84 109.78 110.42 123.20 62 ASP 62 1.327 1.221 1.492 1.513 1.464 122.50 114.78 120.93 108.85 108.97 110.68 124.29 +* +* 63 LEU 63 1.318 1.225 1.530 1.527 1.435 124.20 116.45 120.37 110.56 111.64 109.21 123.16 * * * 64 ALA 64 1.326 1.228 1.526 1.523 1.464 122.25 115.67 121.62 110.35 111.16 110.31 122.70 65 LYS 65 1.309 1.238 1.535 1.538 1.441 121.75 115.39 121.30 111.70 110.11 109.39 123.30 * * 66 LYS 66 1.315 1.233 1.535 1.538 1.449 123.29 116.79 120.61 111.04 111.02 109.07 122.60 67 LEU 67 1.321 1.219 1.526 1.548 1.436 122.15 118.18 120.42 109.41 109.42 112.24 121.40 * * * 68 PRO 68 1.339 1.233 1.528 1.524 1.462 122.24 116.50 120.75 110.41 112.88 102.59 122.75 69 ASN 69 1.323 1.227 1.513 1.519 1.434 122.01 115.54 121.47 108.89 109.46 110.16 122.99 * * 70 VAL 70 1.306 1.226 1.514 1.555 1.431 122.15 116.31 120.59 110.47 108.97 111.59 123.08 +* * +* 71 LEU 71 1.303 1.235 1.539 1.546 1.429 121.65 116.94 120.58 110.59 106.65 108.77 122.44 +* +* +* * +* 72 PHE 72 1.307 1.246 1.513 1.521 1.454 121.34 115.53 121.07 108.15 110.92 111.59 123.40 +* * +* 73 LEU 73 1.304 1.221 1.501 1.540 1.440 123.12 115.83 120.62 107.15 110.55 113.55 123.55 +* * +* +* +* Residue-by-residue listing for refined_1 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 1.304 1.228 1.507 1.479 1.389 123.71 116.69 120.72 110.23 107.80 109.24 122.54 +* +** +*** * * +*** 75 VAL 75 1.285 1.239 1.500 1.554 1.436 121.63 115.54 121.02 110.38 110.63 111.60 123.43 *** * * *** 76 ASP 76 1.310 1.226 1.520 1.516 1.434 121.45 115.24 121.41 111.06 108.87 110.95 123.33 * * * 77 THR 77 1.298 1.234 1.537 1.543 1.451 124.18 116.91 120.95 111.11 113.35 110.39 122.14 ** * ** 78 ASP 78 1.319 1.232 1.506 1.521 1.451 120.42 114.42 121.78 110.52 106.98 111.12 123.80 +* +* 79 GLU 79 1.311 1.238 1.541 1.519 1.422 123.77 116.18 120.81 109.57 110.34 108.49 123.00 * +* * * +* 80 LEU 80 1.326 1.241 1.525 1.529 1.422 122.86 116.12 120.96 109.44 112.69 111.16 122.87 +* +* 81 LYS 81 1.311 1.239 1.520 1.527 1.457 121.86 116.20 120.84 111.06 112.20 111.62 122.94 * * 82 SER 82 1.315 1.226 1.517 1.516 1.441 121.43 116.42 120.28 111.36 111.19 110.50 123.26 83 VAL 83 1.325 1.232 1.535 1.558 1.454 122.03 116.26 120.93 110.43 110.04 111.33 122.76 84 ALA 84 1.328 1.239 1.525 1.522 1.460 121.89 116.23 120.97 110.64 111.00 110.51 122.80 85 SER 85 1.316 1.234 1.545 1.538 1.438 121.33 115.93 120.99 111.17 110.65 109.74 123.03 * * 86 ASP 86 1.330 1.236 1.529 1.533 1.477 123.94 116.76 120.76 110.29 113.18 109.63 122.47 * * * 87 TRP 87 1.312 1.237 1.521 1.523 1.447 121.15 115.32 120.55 111.48 111.89 110.90 124.11 * * 88 ALA 88 1.337 1.233 1.518 1.525 1.462 124.28 115.73 121.55 111.67 111.79 112.13 122.66 * * * 89 ILE 89 1.301 1.234 1.518 1.546 1.437 121.35 115.85 120.97 110.81 110.25 110.48 123.14 ** * ** 90 GLN 90 1.313 1.233 1.532 1.534 1.449 121.95 116.49 120.84 110.31 110.69 110.46 122.67 * * 91 ALA 91 1.314 1.234 1.517 1.516 1.449 121.33 116.56 120.72 111.21 109.87 110.54 122.72 * * 92 MET 92 1.310 1.227 1.514 1.518 1.436 122.01 118.63 119.75 108.53 109.65 109.19 121.62 * * * * 93 PRO 93 1.331 1.235 1.529 1.527 1.461 123.92 116.63 120.96 110.22 111.39 102.61 122.34 94 THR 94 1.288 1.222 1.507 1.536 1.421 120.51 116.54 120.46 109.67 109.22 111.94 123.00 +** +* +** 95 PHE 95 1.298 1.220 1.489 1.523 1.405 121.52 117.33 120.29 109.06 105.71 109.85 122.37 ** +* +** +* +** 96 MET 96 1.273 1.232 1.498 1.533 1.420 119.93 114.12 121.65 114.80 109.99 109.83 124.21 **** * ** * ** **** 97 PHE 97 1.289 1.249 1.510 1.515 1.402 124.75 115.54 121.53 109.62 110.19 108.01 122.92 +** +** +* * +** 98 LEU 98 1.285 1.213 1.527 1.563 1.416 121.48 117.28 120.61 108.50 108.02 112.54 122.08 *** +* ** * * *** 99 LYS 99 1.285 1.209 1.461 1.514 1.441 121.83 114.66 120.66 109.96 108.12 112.41 124.61 *** * *** * * * *** 100 GLU 100 1.311 1.218 1.547 1.536 1.449 124.43 116.36 121.23 108.53 109.51 113.41 122.41 * * +* +* +* 101 GLY 101 1.315 1.220 1.525 - 1.447 121.06 116.13 120.84 - 111.53 - 123.03 102 LYS 102 1.323 1.229 1.528 1.533 1.463 123.30 116.94 119.91 109.87 107.87 108.62 123.16 * * * 103 ILE 103 1.315 1.231 1.526 1.554 1.472 122.95 115.71 121.06 109.67 113.06 110.49 123.22 * * Residue-by-residue listing for refined_1 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 1.322 1.230 1.514 1.523 1.430 121.93 116.37 120.53 109.69 110.94 111.50 123.10 * * 105 ASP 105 1.325 1.221 1.508 1.529 1.458 122.09 116.26 120.89 110.30 112.55 111.93 122.77 106 LYS 106 1.313 1.238 1.523 1.544 1.450 121.56 115.19 121.36 108.14 111.38 112.14 123.45 * * * 107 VAL 107 1.302 1.231 1.511 1.554 1.434 123.45 117.07 120.19 108.08 106.37 111.74 122.72 +* * +* +* 108 VAL 108 1.294 1.248 1.531 1.564 1.432 120.60 115.77 121.03 112.09 110.47 112.04 123.15 ** * * ** 109 GLY 109 1.310 1.240 1.501 - 1.434 121.46 117.35 120.06 - 110.08 - 122.59 * * * 110 ALA 110 1.315 1.239 1.500 1.525 1.436 119.95 115.54 121.26 110.42 109.23 110.99 123.15 * * * 111 LYS 111 1.292 1.234 1.509 1.509 1.410 122.58 115.28 120.72 112.17 109.18 110.38 124.00 +** * +** * +** 112 LYS 112 1.307 1.233 1.549 1.537 1.444 123.76 116.33 120.91 112.19 110.14 106.57 122.76 +* * * * ** ** 113 ASP 113 1.326 1.229 1.521 1.527 1.468 122.26 115.75 120.88 109.34 112.47 111.63 123.37 114 GLU 114 1.326 1.230 1.529 1.527 1.474 122.96 117.07 120.20 110.54 111.94 110.20 122.73 115 LEU 115 1.329 1.228 1.512 1.516 1.457 121.09 114.68 121.36 108.86 109.48 110.70 123.94 116 GLN 116 1.311 1.234 1.528 1.516 1.467 123.00 115.88 120.97 109.20 110.38 110.27 123.14 * * 117 SER 117 1.326 1.233 1.538 1.535 1.450 122.02 116.03 121.12 111.02 110.34 109.85 122.82 118 THR 118 1.314 1.237 1.533 1.531 1.442 122.14 116.25 121.17 110.25 109.79 110.43 122.57 * * 119 ILE 119 1.324 1.226 1.528 1.562 1.446 121.33 116.08 120.88 110.16 108.65 111.98 122.97 120 ALA 120 1.327 1.224 1.527 1.510 1.460 122.08 116.08 120.67 110.95 111.26 110.60 123.25 121 LYS 121 1.328 1.228 1.523 1.513 1.462 122.87 114.79 121.79 108.67 109.54 108.79 123.42 * * 122 HIS 122 1.311 1.229 1.524 1.517 1.440 122.73 118.17 119.74 111.14 114.29 111.28 122.09 * * * 123 LEU 123 1.317 1.235 1.517 1.516 1.417 120.75 114.88 121.40 112.03 111.89 110.83 123.68 ** * ** 124 ALA 124 1.309 - 1.513 1.523 1.434 123.53 - - 111.01 108.37 110.43 - * * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * *** +** +*** +* ** * ** +* ** * *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 1.264 1.350 1.312 .014 *4.6* +* * C-N (Pro) 1.341 .016 4 1.331 1.383 1.354 .020 +** C-O C-O 1.231 .020 123 1.202 1.255 1.232 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 119 1.461 1.561 1.521 .014 *** +* CH2G*-C (Gly) 1.516 .018 5 1.501 1.525 1.513 .009 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.510 1.525 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.523 1.566 1.551 .012 CH1E-CH2E (the rest) 1.530 .020 84 1.479 1.566 1.530 .016 +** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.389 1.484 1.444 .017 +*** * NH1-CH2G* (Gly) 1.451 .016 5 1.434 1.452 1.443 .008 * N-CH1E (Pro) 1.466 .015 4 1.461 1.475 1.468 .006 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 2.0 114 114.03 120.26 116.13 .97 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.13 118.38 117.25 .72 CH1E-C-N (Pro) 116.9 1.5 4 115.73 116.71 116.39 .39 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.64 124.61 123.01 .59 * * O-C-N (Pro) 122.0 1.4 4 122.34 123.47 122.84 .41 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.93 124.92 122.20 1.10 +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.95 122.20 121.06 .76 C-N-CH1E (Pro) 122.6 5.0 4 122.05 123.92 122.85 .75 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.08 122.36 120.82 .54 * CH2G*-C-O (Gly) 120.8 2.1 5 119.84 120.84 120.22 .34 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.35 111.67 110.84 .35 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.08 112.09 110.26 1.04 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.15 114.80 110.45 1.42 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.71 114.35 110.26 1.74 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.96 113.98 111.85 1.72 N-CH1E-C (Pro) 111.8 2.5 4 111.39 112.88 112.33 .60 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.31 112.31 110.86 .61 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.28 112.56 110.99 1.03 +* N-CH1E-CH2E (Pro) 103.0 1.1 4 102.59 104.05 103.29 .69 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.57 114.25 110.45 1.44 ** ** ------------------------------------------------------------------------------------------------------------- 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_1 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] 103 91.2% Residues in additional allowed regions [a,b,l,p] 10 8.8% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 113 91.2 83.8 10.0 .7 Inside b. Omega angle st dev 122 3.4 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 1.6 3.1 1.6 -1.0 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 15 5.5 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 41 7.0 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 46 7.8 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 102 8.2 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 31 8.9 20.4 5.0 -2.3 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% 91.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 3 Residue-by-residue listing for refined_1 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.15 Chi1-chi2 distribution -.16 Chi1 only -.08 Chi3 & chi4 .49 Omega .03 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths .01 Main-chain bond angles .45 ------ .27 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.