Residue-by-residue listing for analyzed_9 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 - - - -94.0 - - - - - - - 180.0 - 35.3 - +* +* 2 THR 2 B 74.9 - - - - - - - - - 180.0 - 33.8 - 3 GLU 3 e B - - -91.0 - - - - - - - 180.1 - 33.3 - +* +* 4 VAL 4 E B - - -84.9 - - - - - - - 180.0 - 32.8 1 * * * 5 TYR 5 E B 66.0 - - - - - - - - - 180.0 -3.5 38.0 - +* * +* 6 ASP 6 E B - - -24.0 - - - - - - - 180.1 - 35.5 - +** +** 7 LEU 7 E B 37.0 - - - - - - - - - 180.0 -2.5 32.0 1 +* * +* 8 GLU 8 E B - 171.4 - - - - - - - - 180.0 -1.1 33.4 1 * * * 9 ILE 9 E B - - -48.5 172.0 - - - - - - 180.0 -3.0 32.0 - * * * 10 THR 10 E B 10.1 - - - - - - - - - 180.0 -2.1 33.7 - *** *** 11 THR 11 E B - - -11.9 - - - - - - - 180.0 -.7 33.7 1 +*** +* * +*** 12 ASN 12 e A 69.2 - - - - - - - - - 180.0 -.7 35.5 - +* +* 13 ALA 13 S A - - - - - - - - - - 179.9 - 33.7 - 14 THR 14 B 46.0 - - - - - - - - - 180.0 - 33.7 - * * 15 ASP 15 a - - -42.8 - - - - - - - 180.0 - 35.5 - +* +* Residue-by-residue listing for analyzed_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 16 PHE 16 B - 212.4 - - - - - - - - 180.0 - 37.4 - +* +* 17 PRO 17 - - - - - -75.0 - - - - - 180.0 - 35.9 - 18 MET 18 E B - 206.0 - 187.9 - - - - - - 180.0 -1.8 35.3 - * * 19 GLU 19 E B - - -56.5 138.2 - - - - - - 180.1 - 33.4 - ** ** 20 LYS 20 E B - - -110.0 - - - - - - - 180.0 -3.3 32.0 - +** +* +** 21 LYS 21 E B - 210.0 - 218.7 - - - - - - 180.0 - 32.0 - +* ** ** 22 TYR 22 E B - - -85.9 - - - - - - - 180.0 -2.7 38.1 - * * * 23 PRO 23 E - - - - - -75.1 - - - - - 180.0 - 35.9 - 24 ALA 24 e A - - - - - - - - - - 180.0 -.9 33.7 - * * 25 GLY 25 T - - - - - - - - - - - 179.9 - - 1 * * 26 MET 26 t b - 208.0 - - - - - - - - 180.0 -.8 35.3 - * +* +* 27 SER 27 h B 12.9 - - - - - - - - - 180.0 - 33.9 - *** *** 28 LEU 28 H A - 233.1 - - - -54.7 -28.6 - - - 180.0 -.5 32.1 - +** ** +** 29 ASN 29 H A - - -92.3 - - -62.7 -51.2 - - - 180.0 - 35.5 - +* * +* 30 ASP 30 H A - 203.2 - - - -63.8 -39.2 - - - 180.0 - 35.5 - * * 31 LEU 31 H A - 223.2 - 175.6 - -61.7 -48.3 - - - 180.0 -2.6 32.0 - ** ** 32 LYS 32 H A - - -74.9 221.9 - -55.2 -37.1 - - - 180.0 -3.3 32.1 - ** +* ** 33 LYS 33 H A - 224.4 - - - -64.3 -44.6 - - - 180.0 -1.7 32.0 - ** ** 34 LYS 34 H A - 226.7 - - - -63.0 -39.1 - - - 180.0 -2.1 32.0 - +** +** 35 LEU 35 H A - - -99.6 169.6 - -73.0 -41.8 - - - 180.0 -2.8 32.0 1 ** * ** 36 GLU 36 H A - - -109.3 - - -58.6 -33.2 - - - 180.0 -3.8 33.3 1 +** ** * +** 37 LEU 37 H A - 192.1 - - - -64.5 -43.6 - - - 180.0 -1.9 32.1 - 38 VAL 38 H A - 170.7 - - - -75.2 -30.2 - - - 180.0 -1.2 32.9 - * * 39 VAL 39 H A - 186.7 - - - -80.5 -20.1 - - - 180.0 -2.8 32.9 - * +* * +* 40 GLY 40 h - - - - - - - - - - - 180.0 -1.7 - - 41 THR 41 t b - - -42.1 - - - - - - - 180.0 -.9 33.8 - +* * +* 42 THR 42 g B 60.4 - - - - - - - - - 180.0 - 33.8 - 43 VAL 43 G A - 179.7 - - - - - - - - 180.0 - 32.9 - 44 ASP 44 G A - 229.6 - - - - - - - - 180.0 - 35.5 - +** +** 45 SER 45 e a - 237.9 - - - - - - - - 180.0 -2.4 33.9 - *** *** 46 MET 46 E B - 218.4 - - - - - - - - 180.0 -.7 35.3 - ** +* ** Residue-by-residue listing for analyzed_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 47 ARG 47 E B - 192.4 - - - - - - - - 180.0 -2.8 34.5 - * * 48 ILE 48 E B - - -83.8 173.3 - - - - - - 180.0 - 32.0 - * * 49 GLN 49 E B - 227.6 - - - - - - - - 180.0 -3.4 33.3 - +** +* +** 50 LEU 50 E B - 185.4 - 175.5 - - - - - - 180.0 -1.4 32.0 - 51 PHE 51 E B - - -82.5 - - - - - - - 180.0 -2.1 37.4 - * * * 52 ASP 52 e b - 218.2 - - - - - - - - 180.0 -1.4 35.5 2 ** ** ** 53 GLY 53 G - - - - - - - - - - - 180.0 - - - 54 ASP 54 G XX - 198.1 - - - - - - - - 180.0 - 35.5 - **** **** 55 ASP 55 G ~b - 222.8 - - - - - - - - 180.0 -2.7 35.5 1 ** ** * ** 56 GLN 56 e b - - -55.1 195.1 - - - - - - 180.0 -.7 33.4 - +* +* 57 LEU 57 E B - 179.6 - - - - - - - - 180.0 - 32.1 - 58 LYS 58 E A - - -119.1 - - - - - - - 180.0 -1.9 32.1 - *** *** 59 GLY 59 E - - - - - - - - - - - 180.0 -1.1 - - * * 60 GLU 60 E B - 226.2 - - - - - - - - 180.0 - 33.4 - +** +** 61 LEU 61 e b - - -47.9 166.7 - - - - - - 180.1 -.9 32.0 1 * * * * 62 THR 62 ~l - 219.3 - - - - - - - - 180.0 - 33.8 - ** ** ** 63 ASP 63 a - - -83.9 - - - - - - - 180.0 - 35.5 - * * 64 GLY 64 - - - - - - - - - - - 180.0 - - - 65 ALA 65 S A - - - - - - - - - - 180.0 - 33.7 - 66 LYS 66 S b 62.0 - - 196.0 - - - - - - 180.0 - 32.0 - * * 67 SER 67 B B - - -19.1 - - - - - - - 180.0 - 33.8 - *** *** 68 LEU 68 T A - - -72.8 - - - - - - - 180.0 -1.1 32.1 - * * 69 LYS 69 T A - 182.3 - 206.9 - - - - - - 180.0 -2.5 32.0 - +* +* 70 ASP 70 T A - 211.2 - - - - - - - - 180.0 -1.0 35.5 - +* * +* 71 LEU 71 T A - - -91.9 176.2 - - - - - - 180.0 -2.8 32.1 - +* * +* 72 GLY 72 T - - - - - - - - - - - 180.0 -.5 - - ** ** 73 VAL 73 t b - 168.4 - - - - - - - - 180.0 -3.5 32.9 - ** ** 74 ARG 74 t b - - -64.3 - - - - - - - 180.0 -1.8 34.5 - 75 ASP 75 T B - - -29.1 - - - - - - - 180.0 - 35.5 - +** +** 76 GLY 76 T - - - - - - - - - - - 180.0 -3.2 - - +* +* 77 TYR 77 e B - - -83.3 - - - - - - - 180.0 -.8 38.1 - * +* * +* 78 ARG 78 E B 64.1 - - 178.3 - - - - - - 180.0 -1.5 34.5 - Residue-by-residue listing for analyzed_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 79 ILE 79 E B - - -81.0 167.6 - - - - - - 180.0 -3.4 32.1 - +* +* 80 HIS 80 E B - 163.6 - - - - - - - - 179.9 -3.4 32.4 - * +* +* 81 ALA 81 E B - - - - - - - - - - 180.0 -3.2 33.7 - +* +* 82 VAL 82 E B 82.3 - - - - - - - - - 180.0 -1.7 32.9 - * * 83 ASP 83 E B 9.6 - - - - - - - - - 180.0 - 35.5 1 *** * *** 84 VAL 84 e A - - -56.4 - - - - - - - 180.1 -2.2 32.9 - 85 THR 85 G A - - -43.4 - - - - - - - 180.0 -.6 33.7 - +* +* +* 86 GLY 86 G - - - - - - - - - - - 180.0 -1.2 - 1 * * * 87 GLY 87 g - - - - - - - - - - - 180.0 -.9 - - +* +* 88 ASN 88 t B - - -48.2 - - - - - - - 180.0 -.7 35.5 - * +* +* 89 GLU 89 l - - -54.9 - - - - - - - 180.0 - 33.3 - 90 ASP 90 - - 221.8 - - - - - - - - - - 35.5 - ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** *** *** +*** ** * +* ** * ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 49.5 204.9 -68.3 182.5 -75.0 -64.8 -38.1 - - - 180.0 -1.9 33.9 * * Standard deviations: 26.1 21.7 27.8 21.2 .0 7.8 8.9 - - - .0 1.0 1.6 Numbers of values: 12 31 32 16 2 12 12 0 0 0 89 55 81 13 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 analyzed_9 Page 5 ---------------------------------------- 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 - 1.230 1.530 1.530 1.452 - 115.06 120.44 109.48 111.04 109.51 124.50 2 THR 2 1.324 1.230 1.530 1.531 1.453 121.02 114.96 120.52 113.39 110.41 107.97 124.52 +* ** ** 3 GLU 3 1.325 1.230 1.530 1.530 1.453 120.98 115.02 120.44 111.00 110.32 111.01 124.54 4 VAL 4 1.325 1.230 1.530 1.530 1.453 121.01 114.98 120.53 113.02 109.28 110.04 124.49 +* +* 5 TYR 5 1.325 1.231 1.530 1.530 1.454 120.98 115.01 120.49 109.02 111.00 105.99 124.50 +** +** 6 ASP 6 1.325 1.230 1.530 1.531 1.452 120.98 114.99 120.54 107.98 109.33 111.08 124.47 * * 7 LEU 7 1.326 1.230 1.530 1.530 1.453 121.01 115.02 120.49 113.73 109.27 110.53 124.50 +* +* 8 GLU 8 1.325 1.230 1.530 1.530 1.453 121.02 115.01 120.51 110.98 110.29 111.00 124.49 9 ILE 9 1.325 1.230 1.530 1.530 1.452 121.04 115.00 120.49 113.70 109.32 110.53 124.51 ** ** 10 THR 10 1.326 1.229 1.530 1.530 1.453 121.00 114.95 120.51 113.43 110.37 108.01 124.54 +* ** ** 11 THR 11 1.326 1.230 1.531 1.529 1.453 120.94 114.97 120.51 113.42 110.34 108.01 124.52 +* ** ** 12 ASN 12 1.326 1.230 1.530 1.529 1.452 121.01 115.02 120.50 107.98 109.28 111.12 124.48 * * Residue-by-residue listing for analyzed_9 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 13 ALA 13 1.325 1.230 1.530 1.530 1.452 121.02 115.00 120.55 112.36 109.30 109.52 124.45 * * 14 THR 14 1.325 1.230 1.530 1.529 1.454 121.01 114.96 120.50 113.40 110.40 107.99 124.54 +* ** ** 15 ASP 15 1.325 1.230 1.530 1.530 1.453 120.99 115.01 120.51 108.00 109.32 111.12 124.48 * * 16 PHE 16 1.324 1.229 1.530 1.530 1.454 121.01 114.97 120.53 109.01 110.99 106.97 124.50 ** ** 17 PRO 17 1.360 1.231 1.529 1.520 1.453 120.97 115.06 120.48 113.02 111.04 104.96 124.46 * * +* +* +* +* 18 MET 18 1.324 1.230 1.530 1.530 1.454 121.05 114.97 120.53 109.49 111.02 109.48 124.50 19 GLU 19 1.326 1.230 1.530 1.531 1.453 120.96 114.96 120.52 110.96 110.32 110.98 124.52 20 LYS 20 1.325 1.230 1.530 1.530 1.454 120.97 115.01 120.52 113.75 109.27 110.51 124.47 +* +* 21 LYS 21 1.325 1.230 1.530 1.529 1.453 121.02 114.96 120.52 113.73 109.26 110.52 124.52 +* +* 22 TYR 22 1.325 1.230 1.530 1.530 1.454 120.97 115.02 120.50 109.01 111.00 105.97 124.48 +** +** 23 PRO 23 1.360 1.230 1.530 1.520 1.453 121.01 114.96 120.51 113.01 110.98 104.98 124.53 * * +* +* +* +* 24 ALA 24 1.324 1.230 1.530 1.530 1.453 120.99 115.00 120.49 112.37 109.31 109.52 124.51 * * 25 GLY 25 1.325 1.230 1.531 - 1.453 120.99 114.97 120.50 - 111.03 - 124.53 26 MET 26 1.326 1.230 1.530 1.529 1.453 120.96 114.99 120.53 109.52 111.00 109.48 124.48 27 SER 27 1.325 1.230 1.530 1.530 1.452 120.98 114.98 120.52 110.23 110.00 111.12 124.51 28 LEU 28 1.325 1.230 1.529 1.531 1.453 120.98 115.00 120.52 113.68 109.34 110.50 124.48 +* +* 29 ASN 29 1.325 1.230 1.529 1.530 1.453 120.99 115.04 120.52 108.01 109.31 111.06 124.43 * * 30 ASP 30 1.325 1.231 1.530 1.530 1.453 121.07 115.02 120.47 108.02 109.28 111.13 124.51 * * 31 LEU 31 1.324 1.230 1.531 1.530 1.453 121.03 114.97 120.47 113.67 109.29 110.54 124.56 +* +* 32 LYS 32 1.325 1.230 1.531 1.530 1.453 120.95 115.00 120.47 113.66 109.30 110.50 124.53 +* +* 33 LYS 33 1.324 1.230 1.530 1.530 1.453 121.01 114.99 120.52 113.69 109.31 110.52 124.50 +* +* 34 LYS 34 1.324 1.230 1.529 1.530 1.453 121.00 115.02 120.52 113.70 109.32 110.49 124.46 +* +* 35 LEU 35 1.325 1.230 1.530 1.530 1.453 121.03 114.99 120.49 113.69 109.30 110.51 124.51 +* +* 36 GLU 36 1.325 1.230 1.530 1.529 1.454 121.03 115.01 120.52 111.03 110.28 111.03 124.47 37 LEU 37 1.325 1.230 1.530 1.530 1.453 121.01 115.03 120.50 113.67 109.27 110.49 124.48 +* +* 38 VAL 38 1.325 1.230 1.530 1.531 1.454 120.98 115.02 120.50 113.00 109.29 109.99 124.48 +* +* 39 VAL 39 1.325 1.230 1.530 1.529 1.453 121.03 114.95 120.54 113.00 109.32 110.03 124.51 +* +* 40 GLY 40 1.325 1.231 1.530 - 1.454 120.99 115.07 120.47 - 110.96 - 124.46 41 THR 41 1.325 1.231 1.529 1.530 1.452 121.03 115.05 120.48 113.40 110.45 107.98 124.47 +* ** ** 42 THR 42 1.325 1.230 1.530 1.530 1.453 121.00 114.97 120.49 113.41 110.38 107.99 124.54 +* ** ** 43 VAL 43 1.325 1.229 1.530 1.530 1.454 120.95 115.03 120.53 113.00 109.31 109.94 124.44 +* +* Residue-by-residue listing for analyzed_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.325 1.230 1.531 1.530 1.452 121.06 115.00 120.50 108.00 109.29 111.16 124.50 * * 45 SER 45 1.325 1.230 1.530 1.531 1.453 120.98 115.03 120.52 110.28 109.95 111.10 124.45 46 MET 46 1.325 1.230 1.530 1.530 1.454 121.01 114.97 120.50 109.53 110.98 109.47 124.53 47 ARG 47 1.325 1.230 1.530 1.530 1.453 120.95 115.00 120.49 109.16 110.29 111.12 124.52 48 ILE 48 1.325 1.231 1.530 1.530 1.452 121.01 115.07 120.48 113.69 109.36 110.49 124.45 ** ** 49 GLN 49 1.325 1.230 1.530 1.529 1.453 121.05 114.97 120.53 111.00 110.30 110.99 124.49 50 LEU 50 1.325 1.230 1.530 1.530 1.453 121.01 115.07 120.45 113.72 109.31 110.53 124.48 +* +* 51 PHE 51 1.325 1.230 1.530 1.531 1.453 121.02 114.96 120.57 108.99 110.99 106.98 124.47 ** ** 52 ASP 52 1.326 1.230 1.531 1.529 1.454 120.95 114.98 120.50 107.99 109.23 111.11 124.52 * * 53 GLY 53 1.324 1.230 1.530 - 1.453 120.99 114.98 120.49 - 110.99 - 124.53 54 ASP 54 1.325 1.230 1.529 1.530 1.453 120.95 115.00 120.56 108.02 109.33 111.10 124.44 * * 55 ASP 55 1.326 1.231 1.529 1.530 1.453 121.02 115.05 120.50 108.03 109.29 111.07 124.44 * * 56 GLN 56 1.325 1.230 1.530 1.530 1.452 121.03 115.00 120.51 110.98 110.29 111.00 124.50 57 LEU 57 1.325 1.230 1.530 1.530 1.453 121.00 115.00 120.48 113.68 109.29 110.50 124.53 +* +* 58 LYS 58 1.325 1.230 1.530 1.530 1.453 120.98 115.01 120.50 113.68 109.34 110.46 124.49 +* +* 59 GLY 59 1.325 1.230 1.531 - 1.453 121.00 114.97 120.49 - 111.00 - 124.53 60 GLU 60 1.325 1.230 1.530 1.530 1.453 120.94 114.99 120.53 111.00 110.29 110.96 124.48 61 LEU 61 1.325 1.229 1.531 1.530 1.453 120.99 114.99 120.49 113.69 109.29 110.51 124.52 +* +* 62 THR 62 1.325 1.230 1.530 1.531 1.453 121.00 114.98 120.50 113.38 110.44 107.98 124.53 +* ** ** 63 ASP 63 1.325 1.231 1.530 1.530 1.453 120.98 115.03 120.49 107.98 109.33 111.11 124.47 * * 64 GLY 64 1.325 1.230 1.530 - 1.453 121.01 114.98 120.55 - 111.06 - 124.47 65 ALA 65 1.326 1.230 1.530 1.530 1.452 120.99 115.01 120.52 112.41 109.29 109.49 124.47 * * 66 LYS 66 1.325 1.231 1.529 1.530 1.453 121.01 115.02 120.51 113.72 109.32 110.50 124.46 +* +* 67 SER 67 1.325 1.230 1.530 1.530 1.452 121.00 115.04 120.50 110.28 109.98 111.12 124.46 68 LEU 68 1.325 1.229 1.530 1.531 1.452 121.02 114.97 120.50 113.67 109.35 110.48 124.53 +* +* 69 LYS 69 1.325 1.230 1.530 1.531 1.453 121.00 114.98 120.52 113.68 109.28 110.52 124.50 +* +* 70 ASP 70 1.326 1.231 1.530 1.530 1.453 120.98 115.05 120.44 108.03 109.27 111.10 124.51 * * 71 LEU 71 1.324 1.230 1.530 1.530 1.453 121.02 115.03 120.53 113.71 109.29 110.45 124.44 +* +* 72 GLY 72 1.325 1.230 1.530 - 1.452 121.06 115.00 120.55 - 111.04 - 124.44 73 VAL 73 1.325 1.230 1.531 1.530 1.452 121.02 114.98 120.52 112.97 109.27 109.99 124.50 +* +* 74 ARG 74 1.325 1.230 1.530 1.530 1.453 120.99 114.99 120.53 109.24 110.31 111.07 124.48 75 ASP 75 1.325 1.230 1.530 1.530 1.453 121.01 115.01 120.52 107.97 109.29 111.11 124.47 * * 76 GLY 76 1.325 1.230 1.530 - 1.453 121.02 114.99 120.52 - 110.98 - 124.50 77 TYR 77 1.325 1.230 1.530 1.530 1.453 120.99 114.97 120.53 108.99 110.99 106.01 124.49 +** +** Residue-by-residue listing for analyzed_9 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 ----------------------------------------------------------------------------------------------------------------------------------- 78 ARG 78 1.325 1.230 1.530 1.530 1.453 120.98 115.02 120.48 109.16 110.30 111.12 124.49 79 ILE 79 1.325 1.230 1.531 1.530 1.452 121.01 114.99 120.49 113.68 109.31 110.50 124.52 ** ** 80 HIS 80 1.325 1.230 1.529 1.530 1.453 120.99 115.02 120.51 112.85 109.58 110.80 124.46 * * 81 ALA 81 1.326 1.230 1.530 1.531 1.452 121.03 115.00 120.50 112.39 109.33 109.50 124.51 * * 82 VAL 82 1.324 1.230 1.530 1.531 1.453 120.99 115.04 120.47 112.95 109.32 110.02 124.48 +* +* 83 ASP 83 1.325 1.231 1.529 1.531 1.453 121.04 115.01 120.51 108.02 109.32 111.08 124.48 * * 84 VAL 84 1.325 1.231 1.531 1.530 1.453 121.01 114.99 120.47 112.99 109.28 110.00 124.53 +* +* 85 THR 85 1.324 1.230 1.531 1.530 1.453 120.99 114.97 120.55 113.38 110.38 108.03 124.49 +* ** ** 86 GLY 86 1.325 1.230 1.531 - 1.453 120.98 115.00 120.47 - 110.96 - 124.54 87 GLY 87 1.325 1.230 1.530 - 1.453 120.95 114.98 120.50 - 111.05 - 124.53 88 ASN 88 1.324 1.231 1.530 1.530 1.453 121.00 115.05 120.47 108.00 109.33 111.13 124.47 * * 89 GLU 89 1.325 1.230 1.530 1.530 1.452 121.01 115.03 120.49 111.03 110.34 111.00 124.49 90 ASP 90 1.326 - 1.530 1.530 1.453 120.99 - - 108.02 109.27 111.11 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * ** +** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for analyzed_9 Page 9 ---------------------------------------- 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 87 1.324 1.326 1.325 .000 C-N (Pro) 1.341 .016 2 1.360 1.360 1.360 .000 * * * C-O C-O 1.231 .020 89 1.229 1.231 1.230 .000 CA-C CH1E-C (except Gly) 1.525 .021 81 1.529 1.531 1.530 .000 CH2G*-C (Gly) 1.516 .018 9 1.530 1.531 1.530 .000 CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.530 1.531 1.530 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.529 1.531 1.530 .000 CH1E-CH2E (the rest) 1.530 .020 59 1.520 1.531 1.530 .002 N-CA NH1-CH1E (except Gly,Pro)1.458 .019 79 1.452 1.454 1.453 .000 NH1-CH2G* (Gly) 1.451 .016 9 1.452 1.454 1.453 .000 N-CH1E (Pro) 1.466 .015 2 1.453 1.453 1.453 .000 ------------------------------------------------------------------------------------------------------------- +-----------------+ | 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 78 114.95 115.07 115.00 .03 CH2G*-C-NH1 (Gly) 116.4 2.1 9 114.97 115.07 114.99 .03 CH1E-C-N (Pro) 116.9 1.5 2 114.96 115.06 115.01 .05 * * * O-C-N O-C-NH1 (except Pro) 123.0 1.6 87 124.43 124.56 124.49 .03 O-C-N (Pro) 122.0 1.4 2 124.46 124.53 124.49 .03 +* +* +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 78 120.94 121.07 121.00 .03 C-NH1-CH2G* (Gly) 120.6 1.7 9 120.95 121.06 121.00 .03 C-N-CH1E (Pro) 122.6 5.0 2 120.97 121.01 120.99 .02 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 80 120.44 120.57 120.51 .03 CH2G*-C-O (Gly) 120.8 2.1 9 120.47 120.55 120.50 .03 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 112.36 112.41 112.38 .02 * * * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 112.95 113.70 113.29 .26 +* ** +* CH2E-CH1E-C (the rest) 110.1 1.9 59 107.97 113.75 110.76 2.31 * +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 79 109.23 111.04 109.77 .62 NH1-CH2G*-C (Gly) 112.5 2.9 9 110.96 111.06 111.01 .03 N-CH1E-C (Pro) 111.8 2.5 2 110.98 111.04 111.01 .03 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.49 109.52 109.51 .01 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 107.97 110.53 109.19 1.09 ** * N-CH1E-CH2E (Pro) 103.0 1.1 2 104.96 104.98 104.97 .01 +* +* +* Residue-by-residue listing for analyzed_9 Page 10 ---------------------------------------- ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- NH1-CH1E-CH2E (the rest) 110.5 1.7 57 105.97 111.16 110.37 1.32 +** ------------------------------------------------------------------------------------------------------------- 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 analyzed_9 Page 11 ---------------------------------------- B A D C O N T A C T S L I S T I N G ....................................................................... Residue Residue ----------- ----------- No. Type No. Type Contact Distance Chain Atom Chain Atom type (Angstroms) ----------------------------------------------------------------------- 1. 4 VAL O --> 75 ASP OD2 Main-Side 2.6 2. 7 LEU CB --> 77 TYR O Side-Main 2.6 3. 8 GLU OE2 --> 9 ILE O Side-Main 2.6 4. 11 THR O --> 14 THR O Main-Main 2.6 5. 25 GLY O --> 26 MET O Main-Main 2.5 6. 35 LEU O --> 39 VAL CG2 Main-Side 2.6 7. 36 GLU OE1 --> 41 THR O Side-Main 2.4 8. 52 ASP O --> 53 GLY C Main-Main 2.6 9. 52 ASP OD2 --> 77 TYR CE1 Side-Side 2.5 10. 55 ASP O --> 56 GLN O Main-Main 2.4 11. 61 LEU O --> 62 THR CB Main-Side 2.6 12. 83 ASP O --> 88 ASN OD1 Main-Side 2.6 13. 86 GLY O --> 87 GLY C Main-Main 2.6 Residue-by-residue listing for analyzed_9 Page 12 ---------------------------------------- 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] 62 80.5% Residues in additional allowed regions [a,b,l,p] 12 15.6% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.6% Residues in disallowed regions [XX] 1 1.3% ---- ------ Number of non-glycine and non-proline residues 77 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 9 Number of proline residues 2 ---- Total number of residues 90 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 77 80.5 83.8 10.0 -.3 Inside b. Omega angle st dev 89 .0 6.0 3.0 -2.0 BETTER c. Bad contacts / 100 residues 13 14.4 4.2 10.0 1.0 WORSE d. Zeta angle st dev 81 1.6 3.1 1.6 -.9 Inside e. H-bond energy st dev 55 1.0 .8 .2 1.0 Inside f. Overall G-factor 90 .0 -.4 .3 1.2 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 26.1 18.1 6.5 1.2 WORSE b. Chi-1 trans st dev 31 21.7 19.0 5.3 .5 Inside c. Chi-1 gauche plus st dev 32 27.8 17.5 4.9 2.1 WORSE d. Chi-1 pooled st dev 75 29.4 18.2 4.8 2.3 WORSE e. Chi-2 trans st dev 16 21.2 20.4 5.0 .2 Inside 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% 80.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 27.8 4 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 1.01 3 Residue-by-residue listing for analyzed_9 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.67 Chi1-chi2 distribution -1.63 Chi1 only -.47 Chi3 & chi4 .20 Omega .72 ------ -.31 ===== Main-chain covalent forces:- Main-chain bond lengths .66 Main-chain bond angles .23 ------ .41 ===== OVERALL AVERAGE -.02 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.