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 - - 176.6 - - - - - - - - 178.2 - 34.3 - 2 ALA 2 l - - - - - - - - - - 177.0 - 31.2 - 3 ASP 3 B 60.7 - - - - - - - - - 180.1 - 32.7 - 4 THR 4 a - - -59.3 - - - - - - - 180.8 - 34.4 - 5 GLY 5 S - - - - - - - - - - - 181.0 - - - 6 GLU 6 l - 184.3 - - - - - - - - 177.6 - 31.2 - 7 VAL 7 E B - - -60.7 - - - - - - - 183.0 -2.1 33.9 - 8 GLN 8 E B 72.6 - - - - - - - - - 174.6 - 34.5 - 9 PHE 9 E B - 185.0 - - - - - - - - 181.1 -1.9 35.0 - 10 MET 10 E B - 182.9 - 180.7 - - - - - - 177.9 - 34.7 - 11 LYS 11 E B 70.9 - - - - - - - - - 183.7 -1.2 32.7 - * * 12 PRO 12 E - - - - - -62.2 - - - - - 178.4 - 38.2 - * * 13 PHE 13 e B - 179.4 - - - - - - - - 179.9 -.8 34.6 - +* +* 14 ILE 14 h B - - -57.7 176.3 - - - - - - 183.7 - 35.7 - 15 SER 15 H A - 181.4 - - - -58.2 -31.7 - - - 183.6 -.6 34.9 - +* +* 16 GLU 16 H A - 187.0 - 183.6 - -60.8 -37.3 - - - 183.1 - 35.6 - 17 LYS 17 H a - 184.8 - - - -110.1 -38.4 - - - 185.0 -1.2 33.9 - +*** * +*** 18 SER 18 H A - - -57.3 - - -79.6 6.9 - - - 169.3 -3.3 31.8 - * **** +* +* **** 19 SER 19 h A - - -66.2 - - - - - - - 181.1 -.8 32.7 - +* +* 20 LYS 20 T a 56.8 - - 173.7 - - - - - - 182.8 -1.7 33.0 - 21 SER 21 t B - - -55.5 - - - - - - - 179.9 -2.0 36.0 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 22 LEU 22 E B - 189.8 - - - - - - - - 181.0 -1.9 32.0 - 23 GLU 23 E B - - -53.8 - - - - - - - 176.4 -.7 36.8 - +* +* 24 ILE 24 E B - - -66.6 - - - - - - - 177.8 -1.8 34.4 - 25 PRO 25 h - - - - - -65.5 - - - - - 180.9 - 39.0 - * * 26 LEU 26 H A - 198.5 - 176.0 - -63.8 -33.4 - - - 178.0 - 34.7 - 27 GLY 27 H - - - - - - -63.1 -31.1 - - - 178.5 - - - 28 PHE 28 H A - 184.2 - - - -70.8 -38.9 - - - 176.0 -.7 35.3 - +* +* 29 ASN 29 H A - 172.9 - - - -64.4 -35.6 - - - 177.8 -1.6 34.3 - 30 GLU 30 H A - - -60.1 187.5 - -73.2 -18.0 - - - 181.2 -2.0 34.6 - +* +* 31 TYR 31 H A - 183.8 - - - -84.3 -29.1 - - - 174.6 -.6 33.9 - +* +* +* 32 PHE 32 h b 66.0 - - - - - - - - - 163.6 -1.4 33.9 - +** +** 33 PRO 33 - - - - - -98.3 - - - - - 181.4 - 38.6 - +** * +** 34 ALA 34 B - - - - - - - - - - 174.1 - 35.0 - * * 35 PRO 35 - - - - - -56.5 - - - - - 189.6 - 38.9 - +* * +* 36 PHE 36 B - 186.9 - - - - - - - - 179.2 - 33.8 - 37 PRO 37 - - - - - -91.9 - - - - - 177.8 - 39.3 - ** +* ** 38 ILE 38 S A - - -57.7 - - - - - - - 176.1 - 33.4 - 39 THR 39 B 47.2 - - - - - - - - - 180.4 - 33.2 - * * 40 VAL 40 E B - 178.1 - - - - - - - - 180.5 -3.3 35.6 - +* +* 41 ASP 41 E B - - -62.5 - - - - - - - 178.3 -2.1 32.9 - 42 LEU 42 E B - - -57.3 181.6 - - - - - - 182.0 -3.1 35.6 - * * 43 LEU 43 E B - - -66.2 - - - - - - - 178.5 -2.8 32.8 - * * 44 ASP 44 e B - 172.6 - - - - - - - - 183.4 -2.4 36.9 - 45 TYR 45 T A - 193.0 - - - - - - - - 180.9 - 34.4 - 46 SER 46 T A - 185.2 - - - - - - - - 176.2 - 34.0 - 47 GLY 47 t - - - - - - - - - - - 176.7 -2.2 - - 48 ARG 48 e B - - -63.4 - - - - - - - 184.1 - 32.2 - 49 SER 49 E B 53.7 - - - - - - - - - 174.2 - 34.2 - 50 TRP 50 E B - - -66.0 - - - - - - - 176.8 -2.9 34.5 - * * 51 THR 51 E B - - -54.4 - - - - - - - 185.0 - 34.0 - 52 VAL 52 E B - - -58.2 - - - - - - - 177.6 -3.3 34.9 - +* +* 53 ARG 53 e B - 186.8 - 176.9 - - - - - - 181.6 -1.2 34.2 - * * 54 MET 54 E B - 176.0 - - - - - - - - 179.2 - 34.9 - 55 LYS 55 E B - - -65.7 184.5 - - - - - - 174.5 -2.1 35.1 - 56 LYS 56 E B - 170.7 - 173.6 - - - - - - 180.8 - 32.9 - 57 ARG 57 E b - 181.0 - 177.4 - - - - - - 180.6 -2.4 34.0 - 58 GLY 58 T - - - - - - - - - - - 184.2 - - - 59 GLU 59 T A 62.6 - - - - - - - - - 186.1 -.5 35.0 - * ** ** 60 LYS 60 E B 62.8 - - 182.3 - - - - - - 176.3 -1.5 34.5 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 61 VAL 61 E B - 176.5 - - - - - - - - 175.6 -.6 35.4 - +* +* 62 PHE 62 E B 57.0 - - - - - - - - - 174.2 -2.3 32.0 - 63 LEU 63 E B - - -68.7 - - - - - - - 186.4 -2.9 33.0 - * * * 64 THR 64 e b - - -36.8 - - - - - - - 183.0 -2.4 36.1 - +* +* 65 VAL 65 T B - 183.8 - - - - - - - - 186.3 - 33.2 - * * 66 GLY 66 h - - - - - - - - - - - 174.9 - - - 67 TRP 67 H A - 161.5 - - - -58.5 -26.5 - - - 182.0 -1.8 34.0 - * * * 68 GLU 68 H A 59.8 - - 175.4 - -61.8 -29.3 - - - 181.3 -.5 33.3 - ** ** 69 ASN 69 H A - - -61.6 - - -68.6 -29.2 - - - 181.0 -1.5 33.0 - 70 PHE 70 H A - 179.6 - - - -73.6 -54.0 - - - 182.8 -1.1 36.0 - * * * 71 VAL 71 H A - 166.9 - - - -68.9 -38.9 - - - 176.9 -1.8 30.1 - * * 72 LYS 72 H A - - -61.5 - - -71.7 -37.0 - - - 182.8 -2.7 31.4 - 73 ASP 73 H A - 178.9 - - - -77.3 -39.0 - - - 179.0 -1.5 31.8 - * * 74 ASN 74 H A - 180.7 - - - -83.8 -20.1 - - - 181.3 -2.8 35.1 - +* +* * +* 75 ASN 75 h l - 183.8 - - - - - - - - 178.0 -1.0 30.0 - * * * 76 LEU 76 t B 55.3 - - - - - - - - - 185.8 -1.0 30.6 - * * * 77 GLU 77 t B 52.4 - - 184.3 - - - - - - 180.6 - 33.3 - 78 ASP 78 T B 65.7 - - - - - - - - - 184.2 - 33.5 - 79 GLY 79 T - - - - - - - - - - - 175.8 -.7 - - +* +* 80 LYS 80 e B - - -60.7 - - - - - - - 179.8 -1.3 34.5 - 81 TYR 81 E B - - -62.2 - - - - - - - 180.8 -.6 34.4 - +* +* 82 LEU 82 E B - - -65.2 - - - - - - - 175.9 -.8 34.1 - +* +* 83 GLN 83 E B - - -60.4 183.0 - - - - - - 181.8 -2.8 35.0 - * * 84 PHE 84 E B - - -59.8 - - - - - - - 178.0 -3.1 35.2 - * * 85 ILE 85 E B - - -58.9 183.1 - - - - - - 180.2 -3.6 34.0 - ** ** 86 TYR 86 E B - 182.2 - - - - - - - - 183.5 -3.4 35.7 - +* +* 87 ASP 87 e A - 181.4 - - - - - - - - 188.1 -1.2 35.1 - * * * 88 ARG 88 S ~l - - -63.2 186.6 - - - - - - 186.5 - 29.8 - ** * * ** 89 ASP 89 S ~b - 185.6 - - - - - - - - 180.7 - 36.4 - ** ** 90 ARG 90 e a - 187.9 - 180.6 - - - - - - 183.0 - 35.5 - 91 THR 91 E B 46.0 - - - - - - - - - 175.8 - 34.3 - * * 92 PHE 92 E B - - -65.5 - - - - - - - 178.2 -2.2 34.9 - 93 TYR 93 E B - 180.4 - - - - - - - - 184.7 -3.2 34.9 - +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 VAL 94 E B - 185.4 - - - - - - - - 176.7 -1.7 33.8 - 95 ILE 95 E B - - -61.2 180.3 - - - - - - 175.8 -3.0 34.3 - * * 96 ILE 96 E B - - -57.7 - - - - - - - 178.7 - 35.2 - 97 TYR 97 E B 64.8 - - - - - - - - - 182.5 -1.1 32.6 - * * 98 GLY 98 S - - - - - - - - - - - 182.8 - - - 99 HIS 99 b - 184.4 - - - - - - - - 178.4 - 33.9 - 100 ASN 100 B 57.7 - - - - - - - - - 182.2 -1.1 32.5 - * * 101 MET 101 a - 181.2 - 180.9 - - - - - - 175.2 - 35.3 - 102 CYS 102 - - - -58.5 - - - - - - - - - 34.4 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +* +** +*** **** +** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.5 181.6 -60.3 180.4 -74.9 -71.8 -31.1 - - - 179.9 -1.8 34.2 Standard deviations: 7.4 6.8 5.7 4.1 18.9 12.5 12.4 - - - 3.9 .9 1.8 Numbers of values: 17 38 33 20 5 18 18 0 0 0 101 60 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 - 1.236 1.520 1.541 1.464 - 115.72 120.01 110.67 110.00 110.24 124.27 2 ALA 2 1.337 1.240 1.533 1.527 1.463 124.66 115.72 121.36 111.71 113.28 112.05 122.90 +* * +* 3 ASP 3 1.316 1.236 1.511 1.551 1.456 122.65 116.16 120.75 110.28 109.78 113.19 123.06 * +* +* 4 THR 4 1.298 1.235 1.522 1.552 1.443 122.14 115.03 121.48 110.20 110.41 110.69 123.48 ** ** 5 GLY 5 1.286 1.232 1.491 - 1.430 122.24 116.63 119.17 - 109.64 - 124.20 *** * * *** 6 GLU 6 1.330 1.236 1.540 1.568 1.468 123.31 115.34 121.78 114.20 111.04 110.76 122.73 +* ** ** 7 VAL 7 1.314 1.221 1.519 1.574 1.446 122.49 117.56 120.02 110.32 108.53 112.08 122.42 * * * 8 GLN 8 1.300 1.234 1.513 1.541 1.410 121.44 115.80 120.89 109.49 111.44 111.01 123.31 ** +** +** 9 PHE 9 1.301 1.224 1.512 1.535 1.435 122.58 117.22 120.26 110.90 107.24 109.89 122.52 +* * * +* 10 MET 10 1.288 1.241 1.500 1.528 1.446 120.87 116.28 120.50 109.67 109.96 110.64 123.21 +** * +** 11 LYS 11 1.307 1.240 1.552 1.562 1.430 121.31 118.56 119.43 114.32 108.72 109.55 122.00 +* * +* * * ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 PRO 12 1.357 1.250 1.547 1.539 1.486 123.30 115.50 121.87 110.08 114.64 103.64 122.62 * * * * * 13 PHE 13 1.313 1.231 1.521 1.540 1.440 122.60 116.54 120.68 110.27 109.25 110.54 122.78 * * 14 ILE 14 1.318 1.228 1.508 1.554 1.420 121.90 116.56 119.86 109.65 106.59 110.55 123.57 +* +* +* 15 SER 15 1.314 1.216 1.522 1.541 1.460 123.22 115.12 121.30 110.51 110.47 109.40 123.43 * * 16 GLU 16 1.299 1.227 1.518 1.511 1.436 123.72 116.98 120.64 109.28 111.35 109.18 122.38 ** * * ** 17 LYS 17 1.317 1.239 1.512 1.535 1.446 119.35 115.63 121.31 111.02 110.71 110.29 123.00 * * 18 SER 18 1.304 1.216 1.533 1.516 1.426 121.58 117.74 120.18 112.86 113.41 110.06 122.07 +* +* * +* 19 SER 19 1.332 1.238 1.545 1.536 1.466 119.11 116.76 120.63 110.21 110.78 112.50 122.61 * * * 20 LYS 20 1.338 1.224 1.535 1.539 1.459 121.14 117.06 120.56 110.24 112.91 111.39 122.38 21 SER 21 1.314 1.241 1.528 1.530 1.446 121.72 117.39 120.43 109.52 109.41 108.93 122.19 * * 22 LEU 22 1.305 1.240 1.509 1.557 1.442 120.21 114.24 121.52 112.89 109.14 111.90 124.24 +* * * +* 23 GLU 23 1.300 1.243 1.520 1.517 1.438 123.93 116.08 120.60 108.35 110.35 108.61 123.32 ** * * * ** 24 ILE 24 1.299 1.240 1.524 1.558 1.439 122.17 117.94 119.90 109.98 109.03 111.32 122.12 ** * ** 25 PRO 25 1.346 1.243 1.528 1.540 1.461 122.35 116.52 120.52 109.71 110.77 104.02 122.96 26 LEU 26 1.318 1.223 1.545 1.556 1.457 122.15 115.60 121.44 112.02 107.83 108.91 122.89 * * * * 27 GLY 27 1.330 1.224 1.525 - 1.454 121.66 116.38 120.90 - 112.50 - 122.70 28 PHE 28 1.318 1.225 1.526 1.537 1.461 122.34 115.14 121.28 111.25 107.80 108.71 123.52 * * * 29 ASN 29 1.324 1.232 1.532 1.544 1.460 122.85 116.11 121.21 110.64 110.46 110.09 122.68 30 GLU 30 1.329 1.227 1.509 1.519 1.461 121.62 116.21 120.75 107.99 110.89 111.95 123.03 * * 31 TYR 31 1.307 1.241 1.530 1.539 1.430 120.88 115.94 120.45 113.02 109.02 108.88 123.50 +* * +* +* 32 PHE 32 1.346 1.231 1.531 1.566 1.465 123.12 118.01 120.92 108.28 111.35 112.94 120.87 * +* * * +* 33 PRO 33 1.318 1.238 1.525 1.504 1.414 121.66 116.35 121.22 110.61 109.81 103.69 122.43 * * *** *** 34 ALA 34 1.272 1.234 1.507 1.531 1.439 121.28 119.11 118.82 110.75 108.42 109.64 122.00 **** * * **** 35 PRO 35 1.355 1.237 1.514 1.529 1.464 121.81 117.57 119.06 110.68 108.40 103.43 123.34 * * * 36 PHE 36 1.322 1.234 1.516 1.542 1.458 121.18 116.64 120.91 110.47 111.12 110.83 122.43 37 PRO 37 1.331 1.230 1.519 1.531 1.430 122.98 116.23 121.31 110.35 111.77 102.85 122.46 ** ** 38 ILE 38 1.296 1.227 1.517 1.553 1.433 120.53 115.66 121.26 111.29 108.28 111.72 123.05 ** * * ** 39 THR 39 1.318 1.234 1.531 1.551 1.433 121.96 115.69 121.21 110.55 110.65 111.81 123.09 * * 40 VAL 40 1.302 1.224 1.513 1.570 1.447 124.19 117.73 119.66 109.53 107.17 110.70 122.60 +* * * * +* 41 ASP 41 1.302 1.242 1.505 1.539 1.443 120.39 115.42 121.05 110.62 110.39 112.23 123.51 +* * +* 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 1.298 1.229 1.496 1.534 1.436 122.78 116.59 120.31 108.72 107.68 111.06 123.09 ** * * * ** 43 LEU 43 1.288 1.237 1.516 1.547 1.431 121.16 113.99 121.61 110.27 112.29 112.09 124.39 +** * * +** 44 ASP 44 1.298 1.232 1.510 1.542 1.448 125.23 115.97 120.28 108.80 108.70 108.73 123.74 ** +* * ** 45 TYR 45 1.311 1.235 1.549 1.542 1.459 123.76 116.77 120.77 110.87 111.38 109.25 122.44 * * * * 46 SER 46 1.326 1.231 1.543 1.541 1.448 121.97 116.80 120.77 111.22 110.69 109.78 122.43 47 GLY 47 1.326 1.230 1.522 - 1.452 120.74 117.12 120.45 - 114.32 - 122.41 48 ARG 48 1.312 1.221 1.515 1.531 1.460 120.94 117.56 119.89 111.54 109.69 112.35 122.53 * * * 49 SER 49 1.302 1.235 1.529 1.531 1.434 120.55 115.69 121.14 111.21 112.65 109.04 123.11 +* * +* 50 TRP 50 1.308 1.225 1.513 1.527 1.464 122.41 116.76 120.42 108.13 110.42 112.20 122.82 +* * +* 51 THR 51 1.298 1.236 1.543 1.536 1.433 121.59 115.44 121.41 111.01 109.00 110.60 123.14 ** * ** 52 VAL 52 1.299 1.233 1.522 1.560 1.448 124.12 117.69 119.99 109.31 109.93 110.94 122.31 ** * ** 53 ARG 53 1.312 1.223 1.520 1.536 1.445 119.63 116.11 120.77 109.03 108.79 112.33 123.11 * * * * 54 MET 54 1.300 1.224 1.510 1.553 1.451 123.26 116.86 120.18 112.83 108.30 107.93 122.88 ** * * * +* ** 55 LYS 55 1.312 1.238 1.507 1.509 1.421 121.51 115.73 120.69 108.30 111.10 110.97 123.59 * * +* +* 56 LYS 56 1.297 1.240 1.478 1.515 1.441 123.02 113.98 121.60 109.94 109.69 113.07 124.42 ** ** * +* ** 57 ARG 57 1.260 1.233 1.500 1.526 1.425 122.88 115.96 120.77 111.01 108.96 110.79 123.22 *5.0* * +* *5.0* 58 GLY 58 1.297 1.235 1.502 - 1.427 120.43 115.76 120.91 - 111.79 - 123.26 ** +* ** 59 GLU 59 1.294 1.230 1.518 1.547 1.443 122.72 116.57 120.88 109.06 111.05 110.63 122.54 ** ** 60 LYS 60 1.308 1.250 1.509 1.526 1.420 120.27 114.08 121.69 110.14 112.24 109.85 124.22 +* +* * +* 61 VAL 61 1.304 1.238 1.512 1.559 1.431 124.28 117.26 120.06 108.58 107.28 111.81 122.57 +* * * * +* 62 PHE 62 1.291 1.245 1.507 1.551 1.434 120.90 116.29 120.60 112.14 110.89 112.02 123.07 +** * * * +** 63 LEU 63 1.308 1.222 1.485 1.546 1.439 120.84 115.73 120.56 110.29 106.91 113.89 123.70 * +* +* +* +* 64 THR 64 1.278 1.248 1.559 1.544 1.421 122.52 116.87 120.36 111.55 108.82 107.08 122.77 +*** +* +* * +** +*** 65 VAL 65 1.321 1.242 1.532 1.564 1.449 123.11 115.70 121.16 111.34 109.57 111.47 123.10 * * 66 GLY 66 1.302 1.230 1.474 - 1.422 120.82 114.85 121.23 - 109.20 - 123.90 +* ** +* * ** 67 TRP 67 1.334 1.239 1.520 1.551 1.449 122.66 115.26 121.49 110.80 109.87 110.65 123.16 * * 68 GLU 68 1.317 1.219 1.528 1.528 1.455 121.16 115.65 121.14 110.44 110.42 111.47 123.11 69 ASN 69 1.321 1.196 1.511 1.541 1.449 122.98 116.07 120.73 111.40 110.95 111.15 123.18 +* +* 70 PHE 70 1.304 1.231 1.514 1.553 1.450 123.58 115.53 121.09 109.65 109.23 109.26 123.34 +* * * +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.320 1.224 1.510 1.563 1.447 121.55 117.16 120.35 113.20 112.43 112.80 122.49 +* +* 72 LYS 72 1.308 1.226 1.530 1.527 1.442 120.11 117.35 120.30 112.06 112.03 112.04 122.33 +* * +* 73 ASP 73 1.334 1.243 1.520 1.516 1.482 120.04 116.52 120.67 110.74 113.32 112.02 122.81 * * 74 ASN 74 1.314 1.234 1.518 1.544 1.465 121.18 114.04 121.50 110.16 108.66 110.01 124.39 * * * 75 ASN 75 1.326 1.252 1.524 1.537 1.460 125.47 114.95 121.85 112.54 113.11 112.83 123.16 * ** * * ** 76 LEU 76 1.308 1.239 1.523 1.561 1.432 122.28 116.19 120.50 114.21 110.54 111.95 123.31 +* +* * ** ** 77 GLU 77 1.304 1.243 1.512 1.525 1.444 122.74 115.63 120.36 111.57 111.44 110.21 123.97 +* +* 78 ASP 78 1.329 1.235 1.515 1.539 1.473 123.37 115.80 121.17 110.32 110.50 111.40 123.01 79 GLY 79 1.300 1.222 1.505 - 1.437 120.74 115.79 121.64 - 110.47 - 122.55 ** ** 80 LYS 80 1.308 1.239 1.521 1.524 1.444 121.87 116.55 120.33 110.02 109.04 110.68 123.12 +* +* 81 TYR 81 1.310 1.238 1.499 1.542 1.436 122.16 116.03 120.47 110.10 108.56 111.31 123.49 * * * * 82 LEU 82 1.303 1.244 1.502 1.559 1.435 121.52 115.82 120.82 108.90 109.64 112.82 123.36 +* * * * * +* 83 GLN 83 1.295 1.231 1.503 1.536 1.429 121.44 116.10 120.56 109.04 107.50 111.80 123.33 ** * * * ** 84 PHE 84 1.289 1.235 1.508 1.541 1.429 122.16 116.26 120.50 109.98 108.83 110.24 123.19 +** +* +** 85 ILE 85 1.300 1.231 1.505 1.552 1.419 121.69 115.88 121.01 109.90 108.74 112.31 123.11 ** ** ** 86 TYR 86 1.282 1.233 1.504 1.536 1.413 121.62 115.64 121.11 111.48 107.20 108.41 123.26 *** * ** * * *** 87 ASP 87 1.303 1.232 1.508 1.539 1.462 121.96 114.34 121.31 110.35 110.13 109.42 124.20 +* +* 88 ARG 88 1.324 1.235 1.501 1.543 1.443 124.17 113.41 122.02 113.35 108.33 114.67 124.40 * * * +* * ** ** 89 ASP 89 1.315 1.219 1.525 1.565 1.436 126.11 118.70 118.99 110.67 103.15 109.21 122.25 * +* * ** * * +** +** 90 ARG 90 1.281 1.243 1.553 1.539 1.456 122.35 115.37 122.17 111.61 108.17 107.75 122.44 *** * * +* *** 91 THR 91 1.320 1.248 1.538 1.546 1.441 122.88 115.40 121.17 109.78 112.47 110.42 123.41 92 PHE 92 1.324 1.228 1.516 1.542 1.454 123.25 116.66 120.53 108.15 108.79 112.24 122.81 * * * 93 TYR 93 1.292 1.215 1.507 1.527 1.444 122.24 117.50 120.24 111.02 107.67 109.69 122.25 +** * +** 94 VAL 94 1.294 1.231 1.523 1.547 1.444 119.83 115.88 120.83 109.75 111.40 111.48 123.27 +** * +** 95 ILE 95 1.315 1.240 1.517 1.562 1.447 122.28 115.80 120.75 108.73 109.53 112.53 123.43 * * 96 ILE 96 1.306 1.241 1.510 1.583 1.437 122.47 116.98 120.30 107.89 106.37 113.25 122.69 +* +* * +* * +* 97 TYR 97 1.302 1.230 1.500 1.547 1.439 120.32 117.14 119.69 111.51 108.93 112.50 123.17 +* * * +* 98 GLY 98 1.309 1.237 1.498 - 1.435 120.06 115.22 121.11 - 109.41 - 123.63 * * * * 99 HIS 99 1.316 1.242 1.519 1.540 1.440 122.46 115.20 121.17 111.02 110.41 110.47 123.60 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 ASN 100 1.308 1.230 1.512 1.553 1.444 122.62 115.38 121.37 111.54 110.35 112.03 123.21 +* * +* 101 MET 101 1.292 1.226 1.507 1.535 1.443 122.39 115.33 121.31 110.86 108.17 109.16 123.35 +** * +** 102 CYS 102 1.301 - 1.515 1.535 1.424 122.39 - - 110.90 107.24 110.79 - +* +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.0* +* ** +* *** ** * * ** +** +** * *5.0* ----------------------------------------------------------------------------------------------------------------------------------- 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 1.260 1.346 1.308 .015 *5.0* * * C-N (Pro) 1.341 .016 5 1.318 1.357 1.342 .015 * * C-O C-O 1.231 .020 101 1.196 1.252 1.233 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.478 1.559 1.519 .014 ** +* CH2G*-C (Gly) 1.516 .018 7 1.474 1.525 1.502 .016 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.527 1.531 1.529 .002 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.536 1.583 1.557 .011 +* CH1E-CH2E (the rest) 1.530 .020 75 1.504 1.568 1.538 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.410 1.482 1.444 .014 +** * NH1-CH2G* (Gly) 1.451 .016 7 1.422 1.454 1.437 .011 +* N-CH1E (Pro) 1.466 .015 5 1.414 1.486 1.451 .026 *** * ------------------------------------------------------------------------------------------------------------- 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 89 113.41 119.11 116.16 1.07 * * CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.85 117.12 115.97 .74 CH1E-C-N (Pro) 116.9 1.5 5 115.50 117.57 116.43 .67 O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.87 124.42 123.07 .63 * O-C-N (Pro) 122.0 1.4 5 122.43 123.34 122.76 .34 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 119.11 126.11 122.15 1.33 * ** C-NH1-CH2G* (Gly) 120.6 1.7 7 120.06 122.24 120.96 .69 C-N-CH1E (Pro) 122.6 5.0 5 121.66 123.30 122.42 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.82 122.17 120.75 .65 * CH2G*-C-O (Gly) 120.8 2.1 7 119.17 121.64 120.77 .73 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.75 111.71 111.23 .48 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.89 113.20 110.14 1.21 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 107.99 114.32 110.64 1.41 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 103.15 113.41 109.74 1.80 +** NH1-CH2G*-C (Gly) 112.5 2.9 7 109.20 114.32 111.05 1.76 * N-CH1E-C (Pro) 111.8 2.5 5 108.40 114.64 111.08 2.10 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.64 112.05 110.84 1.21 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 107.08 113.25 111.31 1.30 +** * N-CH1E-CH2E (Pro) 103.0 1.1 5 102.85 104.02 103.53 .39 NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.75 114.67 110.78 1.49 +* ** ------------------------------------------------------------------------------------------------------------- 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] 74 84.1% Residues in additional allowed regions [a,b,l,p] 12 13.6% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% Residues in disallowed regions [XX] 0 .0% ---- ------ 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 84.1 83.8 10.0 .0 Inside b. Omega angle st dev 101 3.9 6.0 3.0 -.7 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.8 3.1 1.6 -.8 Inside e. H-bond energy st dev 60 .9 .8 .2 .5 Inside f. Overall G-factor 102 -.1 -.4 .3 1.1 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 17 7.4 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 38 6.8 19.0 5.3 -2.3 BETTER c. Chi-1 gauche plus st dev 33 5.7 17.5 4.9 -2.4 BETTER d. Chi-1 pooled st dev 88 8.0 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 20 4.1 20.4 5.0 -3.3 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% 84.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 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 -.57 Chi1-chi2 distribution -.27 Chi1 only .09 Chi3 & chi4 .36 Omega -.05 ------ -.20 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .39 ------ .17 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.