Residue-by-residue listing for refined_7 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -61.7 179.5 - - - - - - 177.6 - 34.3 - 2 ALA 2 B - - - - - - - - - - 183.2 - 34.4 - 3 ASP 3 S l - - -63.8 - - - - - - - 182.1 - 33.7 - 4 THR 4 A - - -53.4 - - - - - - - 175.7 - 34.1 - 5 GLY 5 S - - - - - - - - - - - 180.9 - - - 6 GLU 6 B 57.0 - - 179.2 - - - - - - 179.8 - 33.6 - 7 VAL 7 E B - - -59.0 - - - - - - - 181.0 -3.0 33.4 - * * 8 GLN 8 E B - 183.5 - 181.7 - - - - - - 181.6 - 34.6 - 9 PHE 9 E B - 181.2 - - - - - - - - 181.2 -2.2 35.2 - 10 MET 10 E B - 182.1 - 176.2 - - - - - - 181.3 - 34.1 - 11 LYS 11 E B - 180.1 - 186.6 - - - - - - 171.4 -2.9 36.0 - * * * 12 PRO 12 E - - - - - -79.3 - - - - - 178.0 - 38.8 - * * * 13 PHE 13 e B - 184.3 - - - - - - - - 178.4 -2.6 35.3 - 14 ILE 14 t B - - -58.1 177.5 - - - - - - 183.7 - 35.2 - 15 SER 15 T A - 187.0 - - - - - - - - 183.6 -.6 34.5 - +* +* 16 GLU 16 T A - 189.0 - 178.2 - - - - - - 182.2 - 32.7 - 17 LYS 17 T a - - -67.8 - - - - - - - 185.0 - 31.8 - 18 SER 18 T A - - -54.3 - - - - - - - 175.2 -2.2 34.1 - 19 SER 19 T A 49.9 - - - - - - - - - 183.2 - 33.7 - 20 LYS 20 T A 58.0 - - 182.9 - - - - - - 181.1 -1.9 32.8 - 21 SER 21 t B 51.9 - - - - - - - - - 177.6 -2.1 36.8 - 22 LEU 22 E B - 190.7 - - - - - - - - 185.4 -2.6 33.4 - 23 GLU 23 E B 74.3 - - - - - - - - - 180.0 -.8 31.8 - +* +* Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 24 ILE 24 e B - - -61.8 - - - - - - - 176.2 -2.5 35.2 - 25 PRO 25 h - - - - - -54.8 - - - - - 180.5 - 39.6 - +* +* 26 LEU 26 H A - 188.7 - 172.0 - -56.6 -42.1 - - - 179.5 - 34.5 - 27 GLY 27 H - - - - - - -63.9 -30.0 - - - 181.2 - - - 28 PHE 28 H A - 190.3 - - - -85.9 -25.0 - - - 172.7 -.6 32.2 - +* * * +* +* 29 ASN 29 H A - 172.4 - - - -65.3 -46.0 - - - 178.4 -2.1 35.5 - 30 GLU 30 H A - 177.2 - 182.4 - -65.8 -23.6 - - - 182.9 -2.5 36.5 - * * 31 TYR 31 H A - 190.6 - - - -68.9 -27.1 - - - 178.0 -.6 34.8 - * +* +* 32 PHE 32 h b 65.0 - - - - - - - - - 170.0 -1.1 30.6 - +* * +* 33 PRO 33 - - - - - -79.1 - - - - - 183.1 - 38.6 - * * * 34 ALA 34 B - - - - - - - - - - 170.9 - 35.2 - +* +* 35 PRO 35 - - - - - -57.2 - - - - - 185.6 - 39.3 - +* +* 36 PHE 36 B 58.8 - - - - - - - - - 179.0 - 31.1 - 37 PRO 37 - - - - - -77.6 - - - - - 173.3 - 39.4 - * * +* +* 38 ILE 38 S A - - -66.1 - - - - - - - 175.7 - 32.8 - 39 THR 39 B 44.7 - - - - - - - - - 180.9 - 32.5 - * * 40 VAL 40 E B 61.7 - - - - - - - - - 180.5 -3.6 35.3 - ** ** 41 ASP 41 E B - - -69.2 - - - - - - - 176.1 -1.5 31.6 - 42 LEU 42 E B - - -75.5 - - - - - - - 180.5 -3.1 34.8 - * * 43 LEU 43 E B - - -62.3 - - - - - - - 179.8 -2.8 34.1 - * * 44 ASP 44 E B - 150.1 - - - - - - - - 183.1 -2.5 33.4 - +* +* 45 TYR 45 e A - 182.3 - - - - - - - - 180.6 -.9 34.0 - +* +* 46 SER 46 S A - - -47.2 - - - - - - - 176.0 - 35.0 - * * 47 GLY 47 S - - - - - - - - - - - 179.9 - - - 48 ARG 48 e B - - -59.8 - - - - - - - 179.6 - 33.7 - 49 SER 49 E B 54.1 - - - - - - - - - 178.8 - 34.2 - 50 TRP 50 E B - - -64.6 - - - - - - - 171.6 -2.8 35.2 - * * * 51 THR 51 E B - - -60.0 - - - - - - - 186.4 - 33.6 - * * 52 VAL 52 E B - 179.6 - - - - - - - - 176.3 -2.9 34.7 - * * 53 ARG 53 e B - - -67.0 - - - - - - - 181.8 -2.8 34.0 - * * 54 MET 54 E B - 174.0 - 185.4 - - - - - - 181.3 -.6 35.9 - +* +* 55 LYS 55 E B - 194.0 - 176.1 - - - - - - 171.4 -1.3 37.0 - * * * 56 LYS 56 B - - -60.8 - - - - - - - 187.9 - 35.6 - * * Residue-by-residue listing for refined_7 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 ARG 57 t b - 186.3 - 179.1 - - - - - - 184.1 -.7 35.6 - +* +* 58 GLY 58 T - - - - - - - - - - - 177.7 - - - 59 GLU 59 T A - - -62.6 - - - - - - - 180.9 - 33.8 - 60 LYS 60 t B - 183.8 - 175.5 - - - - - - 186.5 -.6 34.0 - * +* +* 61 VAL 61 e B - - -55.9 - - - - - - - 185.5 - 32.0 - 62 PHE 62 E B - - -57.2 - - - - - - - 168.1 -1.0 36.4 - ** * ** 63 LEU 63 E B - - -65.5 - - - - - - - 192.0 -2.7 33.3 - ** ** 64 THR 64 e b - - -40.9 - - - - - - - 182.6 -2.0 36.5 - +* +* 65 VAL 65 T B - 181.4 - - - - - - - - 188.1 - 34.9 - * * 66 GLY 66 h - - - - - - - - - - - 174.3 - - - 67 TRP 67 H A - 172.4 - - - -67.0 -26.2 - - - 178.7 -2.1 34.8 - * * 68 GLU 68 H A - 168.6 - - - -62.6 -33.8 - - - 176.0 - 31.5 - 69 ASN 69 H A - - -67.1 - - -68.4 -30.8 - - - 179.6 -.5 32.7 - ** ** 70 PHE 70 H A - 176.7 - - - -72.9 -52.6 - - - 183.5 -.8 34.9 - * +* +* 71 VAL 71 H A 72.6 - - - - -60.2 -47.4 - - - 179.1 -3.0 32.4 - * * 72 LYS 72 H A 67.2 - - - - -72.7 -39.0 - - - 183.7 -2.6 27.6 - +* +* 73 ASP 73 H A - 181.4 - - - -77.6 -39.5 - - - 180.6 -2.1 31.5 - * * 74 ASN 74 H A - 191.4 - - - -84.5 -21.5 - - - 179.7 -2.9 35.5 - +* +* * +* 75 ASN 75 h l - 184.4 - - - - - - - - 179.6 -.9 30.0 - * * * 76 LEU 76 t B 47.6 - - - - - - - - - 187.7 -.7 29.1 - * * +* * +* 77 GLU 77 t B 52.2 - - 173.7 - - - - - - 176.8 - 35.2 - 78 ASP 78 T B - 185.2 - - - - - - - - 180.4 - 36.0 - 79 GLY 79 T - - - - - - - - - - - 178.5 -1.3 - - * * 80 LYS 80 e B - - -75.2 - - - - - - - 187.6 -1.4 31.6 - * * 81 TYR 81 E B - - -62.5 - - - - - - - 180.4 - 34.0 - 82 LEU 82 E B - - -58.0 176.3 - - - - - - 173.4 -3.0 36.7 - * * * 83 GLN 83 E B - - -68.7 197.0 - - - - - - 184.0 -1.7 30.9 - * * 84 PHE 84 E B - - -59.4 - - - - - - - 175.9 -2.5 35.3 - 85 ILE 85 E B - - -56.6 177.1 - - - - - - 180.3 -2.2 35.2 - 86 TYR 86 E B - 180.1 - - - - - - - - 182.1 -3.1 36.8 - * * 87 ASP 87 e A 71.4 - - - - - - - - - 182.0 -1.0 33.6 - * * 88 ARG 88 S ~b - - -103.5 - - - - - - - 179.9 - 33.9 - ** ** ** 89 ASP 89 S b - 198.8 - - - - - - - - 180.3 - 35.7 - 90 ARG 90 e a - - -70.9 - - - - - - - 177.6 - 34.0 - 91 THR 91 E B - - -54.2 - - - - - - - 181.2 - 35.9 - Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 92 PHE 92 E B - - -66.4 - - - - - - - 176.2 -2.5 34.3 - 93 TYR 93 E B - - -55.7 - - - - - - - 184.6 -1.8 34.5 - 94 VAL 94 E B 61.5 - - - - - - - - - 174.6 -3.1 33.3 - * * 95 ILE 95 E B - 183.8 - - - - - - - - 180.8 -1.8 32.4 - 96 ILE 96 E B 58.4 - - 177.0 - - - - - - 177.9 - 35.6 - 97 TYR 97 e B - - -69.5 - - - - - - - 183.9 -1.3 29.8 - * * 98 GLY 98 - - - - - - - - - - - 178.3 - - - 99 HIS 99 XX - - -73.6 - - - - - - - 184.4 - 30.1 - **** * **** 100 ASN 100 B - - -60.0 - - - - - - - 175.1 -2.7 34.5 - 101 MET 101 b - 181.9 - 178.6 - - - - - - 183.9 - 31.9 - 102 CYS 102 - - 182.6 - - - - - - - - - -1.4 34.9 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** * * +* +* ** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.2 182.3 -63.1 179.6 -69.6 -69.4 -34.6 - - - 180.0 -1.9 34.2 Standard deviations: 8.8 8.7 9.9 5.5 12.5 8.6 9.9 - - - 4.3 .9 2.2 Numbers of values: 17 33 38 20 5 14 14 0 0 0 101 56 95 0 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_7 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 - 1.232 1.514 1.544 1.464 - 115.93 120.84 109.65 109.90 111.25 123.20 2 ALA 2 1.306 1.231 1.504 1.524 1.440 123.24 116.88 119.65 110.77 107.59 110.70 123.42 +* * +* 3 ASP 3 1.333 1.230 1.521 1.556 1.487 122.56 115.49 121.24 109.47 109.28 112.53 123.25 * +* * +* 4 THR 4 1.322 1.236 1.551 1.548 1.444 122.81 115.78 121.48 111.66 110.58 109.34 122.73 * * * * 5 GLY 5 1.315 1.236 1.513 - 1.436 120.77 117.18 119.80 - 109.85 - 123.01 6 GLU 6 1.311 1.244 1.535 1.524 1.458 121.73 116.09 121.18 110.54 111.84 110.49 122.73 * * 7 VAL 7 1.303 1.233 1.518 1.568 1.444 121.88 116.83 120.55 110.15 109.31 112.69 122.62 +* * +* 8 GLN 8 1.299 1.236 1.517 1.530 1.439 121.41 116.71 120.28 111.05 108.74 109.85 123.00 ** ** 9 PHE 9 1.303 1.236 1.513 1.544 1.441 121.99 116.74 120.02 111.10 108.76 109.06 123.24 +* +* 10 MET 10 1.310 1.234 1.508 1.533 1.440 121.70 116.30 120.82 110.95 109.82 110.36 122.87 * * 11 LYS 11 1.300 1.234 1.526 1.521 1.426 121.03 117.60 120.42 108.63 111.31 109.41 121.95 ** +* ** 12 PRO 12 1.333 1.254 1.540 1.532 1.446 122.06 116.70 120.93 110.46 110.10 103.53 122.35 * * * Residue-by-residue listing for refined_7 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 PHE 13 1.299 1.236 1.526 1.543 1.449 121.36 117.47 119.72 110.61 108.37 109.35 122.79 ** * ** 14 ILE 14 1.332 1.224 1.513 1.555 1.436 121.16 117.05 119.79 109.96 107.54 110.65 123.16 * * * 15 SER 15 1.322 1.225 1.535 1.551 1.475 122.74 116.64 120.73 108.90 111.42 111.11 122.62 * * 16 GLU 16 1.314 1.223 1.535 1.516 1.432 120.97 118.07 120.28 111.03 112.63 110.94 121.64 * * * 17 LYS 17 1.324 1.234 1.496 1.538 1.466 118.22 116.17 120.28 109.10 112.56 114.34 123.45 * +* ** ** 18 SER 18 1.318 1.218 1.537 1.532 1.443 122.38 116.60 120.91 110.66 111.35 109.99 122.47 19 SER 19 1.313 1.230 1.535 1.526 1.434 121.66 116.83 120.61 111.39 111.31 109.83 122.55 * * * 20 LYS 20 1.332 1.232 1.525 1.540 1.463 120.78 116.10 120.91 111.45 112.49 110.68 122.99 21 SER 21 1.294 1.220 1.508 1.527 1.436 123.07 118.37 119.41 109.15 107.82 108.58 122.22 ** * * * * ** 22 LEU 22 1.288 1.239 1.523 1.556 1.446 119.43 116.12 120.60 112.81 106.71 110.71 123.26 +** * * * +* +** 23 GLU 23 1.314 1.239 1.540 1.565 1.437 121.77 115.54 121.70 113.20 112.37 110.63 122.75 * +* * +* +* 24 ILE 24 1.314 1.231 1.523 1.562 1.446 122.32 117.81 119.88 108.92 109.56 111.09 122.29 * * 25 PRO 25 1.352 1.241 1.531 1.534 1.466 122.70 116.41 120.34 109.43 111.12 103.14 123.24 26 LEU 26 1.328 1.234 1.532 1.567 1.465 122.83 115.57 121.04 111.92 108.89 109.24 123.35 +* +* 27 GLY 27 1.325 1.227 1.519 - 1.444 121.37 117.24 120.14 - 113.08 - 122.61 28 PHE 28 1.328 1.216 1.537 1.543 1.452 120.65 116.01 121.23 112.55 109.60 111.42 122.74 * * 29 ASN 29 1.321 1.238 1.525 1.535 1.470 122.20 114.18 121.90 109.63 108.92 109.61 123.89 * * 30 GLU 30 1.315 1.245 1.539 1.526 1.453 124.60 115.17 121.54 110.34 110.49 106.89 123.27 +* ** ** 31 TYR 31 1.317 1.242 1.538 1.538 1.446 123.33 117.08 120.55 111.41 110.10 108.70 122.36 * * 32 PHE 32 1.336 1.240 1.548 1.565 1.450 120.37 117.29 121.88 111.85 113.42 112.89 120.74 * +* * * +* 33 PRO 33 1.327 1.241 1.508 1.520 1.434 121.85 115.38 121.30 109.59 108.96 105.05 123.31 ** * * +* ** 34 ALA 34 1.270 1.242 1.494 1.532 1.433 122.27 119.02 118.94 110.26 108.53 109.92 122.04 **** * * * * **** 35 PRO 35 1.344 1.251 1.508 1.526 1.451 121.22 117.14 119.83 109.91 106.93 103.91 122.99 +* +* 36 PHE 36 1.301 1.238 1.515 1.537 1.394 120.35 116.35 121.16 113.26 111.43 111.92 122.42 +* *** +* *** 37 PRO 37 1.321 1.229 1.510 1.534 1.436 122.41 116.63 120.86 110.24 110.39 103.22 122.44 * +* +* 38 ILE 38 1.287 1.236 1.518 1.575 1.428 120.47 114.76 121.76 111.25 106.64 113.48 123.42 *** * +* +* * *** 39 THR 39 1.313 1.239 1.531 1.551 1.427 122.94 115.62 120.99 111.56 110.82 111.81 123.38 * +* * +* 40 VAL 40 1.293 1.243 1.526 1.575 1.439 124.12 117.71 119.95 110.27 107.39 110.47 122.32 +** * * * * +** 41 ASP 41 1.297 1.239 1.493 1.532 1.440 119.93 114.51 121.55 110.55 112.67 113.24 123.94 ** +* +* ** Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 LEU 42 1.309 1.243 1.494 1.556 1.433 123.09 115.52 120.97 109.58 107.73 111.79 123.50 * * * * * * 43 LEU 43 1.292 1.228 1.497 1.555 1.429 121.76 115.79 120.55 109.77 109.16 112.18 123.65 +** * * +* +** 44 ASP 44 1.288 1.238 1.514 1.540 1.435 123.02 115.30 121.15 112.31 110.48 109.93 123.53 +** * * +** 45 TYR 45 1.312 1.235 1.532 1.541 1.449 123.17 116.53 120.75 111.24 111.29 109.71 122.71 * * 46 SER 46 1.314 1.240 1.546 1.526 1.445 121.74 115.90 121.17 110.63 109.35 109.19 122.93 * * * 47 GLY 47 1.327 1.235 1.520 - 1.446 121.43 116.93 120.77 - 113.02 - 122.30 48 ARG 48 1.313 1.241 1.534 1.531 1.454 121.49 116.54 120.83 110.66 110.72 110.66 122.62 * * 49 SER 49 1.315 1.235 1.531 1.536 1.443 121.72 116.60 120.42 111.23 110.75 109.52 122.94 50 TRP 50 1.323 1.242 1.519 1.546 1.456 122.07 116.53 120.64 107.64 110.48 111.81 122.81 * * 51 THR 51 1.304 1.232 1.534 1.545 1.433 121.43 115.62 121.52 111.11 107.72 111.64 122.86 +* * * +* 52 VAL 52 1.292 1.207 1.525 1.569 1.448 123.38 118.15 119.93 111.02 109.47 109.87 121.86 +** * * +** 53 ARG 53 1.306 1.217 1.513 1.562 1.438 120.37 115.72 120.91 109.94 107.86 112.47 123.36 +* +* * * * +* 54 MET 54 1.299 1.214 1.482 1.531 1.452 123.20 117.39 119.52 108.94 108.04 110.28 123.08 ** ** * ** 55 LYS 55 1.303 1.237 1.521 1.526 1.418 120.21 117.36 119.89 110.47 108.84 106.82 122.74 +* ** ** ** 56 LYS 56 1.321 1.231 1.510 1.540 1.433 120.32 116.84 120.07 107.63 103.42 113.15 123.08 * * +** +* +** 57 ARG 57 1.279 1.222 1.507 1.538 1.445 121.42 116.56 120.69 110.90 108.93 108.50 122.72 +*** * +*** 58 GLY 58 1.300 1.236 1.503 - 1.430 119.94 117.18 119.91 - 109.49 - 122.91 ** * * ** 59 GLU 59 1.303 1.237 1.516 1.522 1.455 121.29 115.79 121.24 110.32 110.72 110.91 122.96 +* +* 60 LYS 60 1.305 1.219 1.499 1.530 1.427 121.80 116.46 120.56 111.51 107.86 110.61 122.98 +* * +* * +* 61 VAL 61 1.292 1.240 1.489 1.517 1.428 121.15 115.65 121.17 111.75 111.93 111.68 123.16 +** +* +* * +** 62 PHE 62 1.295 1.241 1.502 1.548 1.434 120.81 116.38 120.64 107.68 110.48 110.38 122.97 ** * * * ** 63 LEU 63 1.305 1.222 1.495 1.547 1.433 120.28 115.10 120.97 110.91 103.85 113.73 123.87 +* * * +** +* +** 64 THR 64 1.286 1.236 1.573 1.551 1.429 123.58 116.72 120.68 112.09 110.68 105.54 122.59 *** ** +* * * +*** +*** 65 VAL 65 1.325 1.228 1.528 1.561 1.469 124.00 116.03 121.30 109.35 109.94 110.77 122.66 * * 66 GLY 66 1.298 1.224 1.485 - 1.423 120.97 114.83 121.47 - 108.53 - 123.69 ** +* +* * ** 67 TRP 67 1.332 1.232 1.510 1.537 1.443 122.40 114.43 121.98 110.19 108.25 110.62 123.56 * * 68 GLU 68 1.302 1.214 1.528 1.555 1.429 122.35 115.96 120.89 115.76 109.80 109.40 122.95 +* * +* +** +** 69 ASN 69 1.318 1.201 1.506 1.533 1.454 122.31 116.35 120.70 110.85 110.86 112.02 122.91 * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 70 PHE 70 1.300 1.231 1.495 1.552 1.447 122.74 115.40 120.67 109.88 108.84 110.90 123.90 ** * * ** 71 VAL 71 1.324 1.224 1.522 1.578 1.437 121.79 116.51 120.70 111.66 110.31 112.36 122.77 * * * * 72 LYS 72 1.317 1.233 1.536 1.547 1.446 120.56 117.86 120.15 114.54 114.26 113.35 121.98 ** * +* ** 73 ASP 73 1.338 1.228 1.518 1.534 1.485 119.54 116.93 120.68 111.09 112.66 112.52 122.36 * * * * 74 ASN 74 1.315 1.227 1.531 1.554 1.466 120.72 114.46 121.28 111.02 107.88 108.75 124.17 * * * * * 75 ASN 75 1.328 1.238 1.525 1.539 1.469 125.51 115.70 121.60 112.16 113.55 113.02 122.68 ** * * ** 76 LEU 76 1.303 1.239 1.521 1.553 1.432 121.43 116.11 120.47 114.88 112.21 112.43 123.41 +* * * +** * +** 77 GLU 77 1.306 1.242 1.525 1.529 1.454 122.49 114.68 121.18 109.30 112.64 109.33 124.15 +* +* 78 ASP 78 1.332 1.235 1.519 1.536 1.472 124.33 116.24 120.74 109.74 109.78 108.59 123.00 * * * 79 GLY 79 1.304 1.228 1.498 - 1.436 120.69 115.49 121.10 - 111.02 - 123.41 +* * +* 80 LYS 80 1.307 1.252 1.513 1.550 1.436 122.00 116.66 120.58 113.09 110.04 111.87 122.76 +* * * +* +* 81 TYR 81 1.305 1.239 1.480 1.531 1.426 120.68 114.86 120.84 110.26 110.52 111.26 124.31 +* ** +* ** 82 LEU 82 1.288 1.238 1.502 1.530 1.413 123.01 116.75 120.41 108.63 108.32 109.42 122.81 +** * ** * +** 83 GLN 83 1.292 1.232 1.487 1.530 1.435 120.20 115.39 120.71 111.71 109.89 114.11 123.88 +** +* * ** +** 84 PHE 84 1.298 1.235 1.506 1.536 1.431 122.44 115.95 120.60 109.22 110.01 110.42 123.43 ** * ** 85 ILE 85 1.300 1.232 1.521 1.549 1.438 121.91 115.76 120.30 108.90 108.23 111.42 123.93 ** * * ** 86 TYR 86 1.302 1.236 1.520 1.546 1.449 124.10 117.61 119.96 110.84 106.85 107.15 122.42 +* * +* +* +* 87 ASP 87 1.317 1.230 1.514 1.561 1.462 119.99 114.55 120.44 110.28 109.60 111.98 125.00 +* * +* 88 ARG 88 1.333 1.231 1.507 1.533 1.470 127.04 116.15 121.07 108.60 108.86 113.06 122.78 +** +* +** 89 ASP 89 1.321 1.223 1.525 1.546 1.419 121.16 116.43 120.73 110.49 107.15 109.41 122.82 ** * ** 90 ARG 90 1.287 1.225 1.520 1.539 1.433 123.63 115.86 121.42 110.49 109.80 110.97 122.68 *** * * *** 91 THR 91 1.304 1.233 1.522 1.538 1.418 120.85 116.30 120.63 109.12 107.77 110.26 123.06 +* ** * ** 92 PHE 92 1.311 1.236 1.507 1.533 1.436 121.33 115.88 121.21 109.59 110.67 111.26 122.89 * * * 93 TYR 93 1.298 1.227 1.513 1.538 1.443 121.43 116.77 120.37 110.37 107.41 111.14 122.85 ** * ** 94 VAL 94 1.299 1.235 1.530 1.571 1.442 121.76 116.09 121.04 110.90 110.93 111.39 122.74 ** * ** 95 ILE 95 1.307 1.242 1.539 1.580 1.438 121.78 115.67 121.04 111.69 108.95 112.73 123.21 +* * * * +* 96 ILE 96 1.312 1.244 1.518 1.551 1.436 123.69 116.02 121.15 109.21 110.34 110.02 122.80 * * * * Residue-by-residue listing for refined_7 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 ----------------------------------------------------------------------------------------------------------------------------------- 97 TYR 97 1.299 1.231 1.507 1.528 1.432 121.22 114.72 121.42 114.07 112.27 112.14 123.83 ** * ** ** 98 GLY 98 1.309 1.234 1.512 - 1.434 122.55 115.33 120.84 - 109.95 - 123.83 * * * * 99 HIS 99 1.346 1.230 1.531 1.547 1.493 124.67 117.10 119.91 110.28 115.40 113.85 122.98 * +* +* * +* +* 100 ASN 100 1.310 1.238 1.504 1.536 1.465 122.42 116.67 120.76 108.56 111.74 111.42 122.57 * * 101 MET 101 1.308 1.236 1.517 1.536 1.433 119.89 115.01 121.45 112.10 108.81 112.73 123.42 * * * * * * 102 CYS 102 1.309 - 1.513 1.543 1.433 123.52 - - 110.51 107.76 110.32 - * * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** +* *** +** * * +** +** +*** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 Page 10 ---------------------------------------- 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 96 1.270 1.346 1.309 .014 **** * * C-N (Pro) 1.341 .016 5 1.321 1.352 1.335 .011 * C-O C-O 1.231 .020 101 1.201 1.254 1.233 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 95 1.480 1.573 1.519 .016 ** ** CH2G*-C (Gly) 1.516 .018 7 1.485 1.520 1.507 .012 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.524 1.532 1.528 .004 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.517 1.580 1.558 .016 * CH1E-CH2E (the rest) 1.530 .020 75 1.516 1.567 1.539 .011 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.394 1.493 1.444 .017 *** +* NH1-CH2G* (Gly) 1.451 .016 7 1.423 1.446 1.435 .007 +* N-CH1E (Pro) 1.466 .015 5 1.434 1.466 1.447 .012 ** * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_7 Page 11 ---------------------------------------- +-----------------+ | 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 89 114.18 119.02 116.24 .95 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.83 117.24 116.31 .97 CH1E-C-N (Pro) 116.9 1.5 5 115.38 117.14 116.45 .58 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.74 125.00 122.99 .61 * * O-C-N (Pro) 122.0 1.4 5 122.35 123.31 122.87 .40 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.22 127.04 121.96 1.42 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.94 122.55 121.10 .75 * C-N-CH1E (Pro) 122.6 5.0 5 121.22 122.70 122.05 .51 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.94 121.98 120.74 .59 * CH2G*-C-O (Gly) 120.8 2.1 7 119.80 121.47 120.57 .59 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.26 110.77 110.52 .25 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.90 112.09 110.59 1.08 * CH2E-CH1E-C (the rest) 110.1 1.9 75 107.63 115.76 110.68 1.57 * +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 103.42 115.40 109.80 2.03 +** * NH1-CH2G*-C (Gly) 112.5 2.9 7 108.53 113.08 110.71 1.63 * N-CH1E-C (Pro) 111.8 2.5 5 106.93 111.12 109.50 1.46 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.92 110.70 110.31 .39 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 105.54 113.48 110.96 1.69 +*** * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.14 105.05 103.77 .70 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.82 114.34 110.83 1.68 ** ** ------------------------------------------------------------------------------------------------------------- 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_7 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] 77 87.5% Residues in additional allowed regions [a,b,l,p] 9 10.2% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.1% Residues in disallowed regions [XX] 1 1.1% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 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 88 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 101 4.3 6.0 3.0 -.6 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 2.2 3.1 1.6 -.6 Inside e. H-bond energy st dev 56 .9 .8 .2 .4 Inside f. Overall G-factor 102 -.1 -.4 .3 1.0 Inside 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 17 8.8 18.1 6.5 -1.4 BETTER b. Chi-1 trans st dev 33 8.7 19.0 5.3 -1.9 BETTER c. Chi-1 gauche plus st dev 38 9.9 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 88 9.8 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 20 5.5 20.4 5.0 -3.0 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% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_7 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.45 Chi1-chi2 distribution -.43 Chi1 only -.11 Chi3 & chi4 .49 Omega -.17 ------ -.23 ===== Main-chain covalent forces:- Main-chain bond lengths -.10 Main-chain bond angles .34 ------ .16 ===== OVERALL AVERAGE -.09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.