Residue-by-residue listing for refined_1 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 GLU 1 - 55.5 - - 179.5 - - - - - - 179.1 - 33.4 - 2 ALA 2 B - - - - - - - - - - 179.9 - 34.2 - 3 GLU 3 S B 53.0 - - - - - - - - - 184.9 - 30.9 - 4 VAL 4 S ~l 58.0 - - - - - - - - - 185.5 - 25.5 - ** ** ** 5 HIS 5 b 55.2 - - - - - - - - - 173.9 - 28.2 - * +* +* 6 ASN 6 b - - -70.8 - - - - - - - 172.7 -2.0 30.9 - * * 7 GLN 7 b - - -68.5 - - - - - - - 180.7 -.6 34.3 - +* +* 8 LEU 8 E B - - -65.4 - - - - - - - 188.1 -.9 31.4 - * +* +* 9 GLU 9 E B - - -59.4 178.4 - - - - - - 178.7 -.6 33.7 - +* +* 10 ILE 10 E B - - -56.3 179.5 - - - - - - 169.9 -2.7 35.8 - +* +* 11 LYS 11 E B 70.0 - - 171.3 - - - - - - 185.6 -2.4 30.6 - 12 PHE 12 E B - - -55.6 - - - - - - - 174.0 -.5 35.7 - * ** ** 13 ARG 13 E B - - -63.3 197.5 - - - - - - 179.6 -3.3 32.8 - * +* +* 14 LEU 14 E B - - -67.3 - - - - - - - 181.1 -3.2 34.2 - +* +* 15 THR 15 e A - 185.6 - - - - - - - - 179.8 -2.2 34.7 - 16 ASP 16 T A 64.1 - - - - - - - - - 175.4 - 32.9 - 17 GLY 17 t - - - - - - - - - - - 177.3 -2.4 - - 18 SER 18 e B - - -54.1 - - - - - - - 181.4 - 35.1 - Residue-by-residue listing for refined_1 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 ASP 19 E B 73.4 - - - - - - - - - 177.9 - 33.3 - 20 ILE 20 E B - - -58.8 178.3 - - - - - - 181.8 -3.0 35.4 - * * 21 GLY 21 E - - - - - - - - - - - 182.2 - - - 22 PRO 22 E - - - - - -68.7 - - - - - 177.7 - 38.5 - * * 23 LYS 23 E B - 176.2 - 184.5 - - - - - - 178.6 -2.4 36.1 - 24 ALA 24 E B - - - - - - - - - - 180.4 - 33.8 - 25 PHE 25 E B - - -58.5 - - - - - - - 172.3 -3.0 35.8 - * * * 26 PRO 26 t - - - - - -61.0 - - - - - 177.8 - 40.0 - +* +* 27 ASP 27 T A - - -59.5 - - - - - - - 181.9 - 34.9 - 28 ALA 28 T A - - - - - - - - - - 177.1 - 34.4 - 29 THR 29 t B - - -52.8 - - - - - - - 177.5 -1.8 35.2 - 30 THR 30 h B 55.2 - - - - - - - - - 176.9 - 35.2 - 31 VAL 31 H A - 175.8 - - - -64.7 -26.6 - - - 174.2 -3.3 31.4 - * +* +* 32 SER 32 H A - - -61.8 - - -57.5 -48.9 - - - 179.3 -1.4 33.6 - 33 ALA 33 H A - - - - - -69.4 -34.0 - - - 177.7 - 33.6 - 34 LEU 34 H A - 172.8 - - - -63.3 -46.4 - - - 179.7 -2.1 36.6 - 35 LYS 35 H A - 194.2 - 176.5 - -62.3 -43.6 - - - 175.2 -3.2 35.5 - +* +* 36 GLU 36 H A - - -71.3 - - -59.3 -42.7 - - - 180.7 -2.3 35.9 - 37 THR 37 H A - - -58.3 - - -56.5 -41.8 - - - 180.3 -2.4 34.6 - 38 VAL 38 H A - 184.3 - - - -63.9 -43.1 - - - 182.8 -1.7 34.6 - 39 ILE 39 H A - - -48.8 - - -60.8 -33.5 - - - 178.3 -1.6 34.1 - * * 40 SER 40 H A - - -55.0 - - -75.3 -33.0 - - - 180.2 -1.6 34.2 - 41 GLU 41 H A - - -65.0 - - -79.5 -36.8 - - - 184.1 -1.5 36.0 - * * 42 TRP 42 h B - 200.9 - - - - - - - - 179.6 -3.2 36.6 - * +* +* 43 PRO 43 t - - - - - -65.1 - - - - - 177.5 - 38.8 - * * 44 ARG 44 T A 63.3 - - 185.4 - - - - - - 176.6 - 32.4 - 45 GLU 45 T A 58.1 - - 174.5 - - - - - - 183.0 - 35.5 - 46 LYS 46 t B - 182.1 - 182.9 - - - - - - 169.2 -1.1 35.9 - +* * +* 47 GLU 47 S B - - -66.1 - - - - - - - 181.5 - 33.3 - 48 ASN 48 S l - 180.9 - - - - - - - - 174.2 - 29.5 - * * * 49 GLY 49 S - - - - - - - - - - - 175.6 - - - 50 PRO 50 - - - - - -55.4 - - - - - 172.8 - 40.4 - * +* +* 51 LYS 51 ~b 54.9 - - 186.7 - - - - - - 169.7 - 29.8 - ** +* * ** 52 THR 52 g B 60.4 - - - - - - - - - 188.0 - 31.9 - * * 53 VAL 53 G A 58.7 - - - - - - - - - 185.9 - 31.9 - * * 54 LYS 54 G A 61.5 - - 187.7 - - - - - - 185.5 - 33.9 - 55 GLU 55 e A - - -61.0 176.3 - - - - - - 187.1 -1.1 34.3 - * * * 56 VAL 56 E B 61.8 - - - - - - - - - 178.8 -.9 33.1 - +* +* Residue-by-residue listing for refined_1 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 LYS 57 E B - - -79.4 - - - - - - - 178.2 -1.1 33.7 - * * 58 LEU 58 E B - - -60.8 - - - - - - - 182.9 - 34.7 - 59 ILE 59 E B - - -62.8 176.0 - - - - - - 180.5 -3.0 33.3 - * * 60 SER 60 E B - 181.2 - - - - - - - - 180.2 -2.6 34.9 - 61 ALA 61 T l - - - - - - - - - - 181.1 - 32.4 - 62 GLY 62 T - - - - - - - - - - - 181.1 - - - 63 LYS 63 E B - 183.4 - 181.5 - - - - - - 176.9 -1.0 36.0 - * * 64 VAL 64 E B 61.2 - - - - - - - - - 181.0 - 32.5 - 65 LEU 65 e B - - -70.5 - - - - - - - 173.8 -3.2 32.6 - * +* +* 66 GLU 66 t B - 179.4 - - - - - - - - 185.4 -.9 34.3 - +* +* 67 ASN 67 T A 70.1 - - - - - - - - - 182.9 - 33.1 - 68 SER 68 T A - 184.1 - - - - - - - - 179.5 - 34.7 - 69 LYS 69 t B - - -60.8 177.7 - - - - - - 179.7 -1.6 35.1 - 70 THR 70 B B 58.2 - - - - - - - - - 177.4 - 34.6 - 71 VAL 71 G A - 181.4 - - - - - - - - 178.9 -3.2 33.8 - +* +* 72 LYS 72 G A - 182.7 - 176.5 - - - - - - 178.9 -2.6 34.5 - 73 ASP 73 G A - - -75.0 - - - - - - - 183.8 -.5 35.5 - ** ** 74 TYR 74 G A - - -56.8 - - - - - - - 185.6 -2.0 36.2 - 75 ARG 75 g B - - -83.0 - - - - - - - 176.2 -.8 35.8 - * +* +* 76 SER 76 B - - -52.6 - - - - - - - 178.9 - 37.3 - 77 PRO 77 t - - - - - -64.0 - - - - - 182.4 - 38.7 - * * 78 VAL 78 T A - 185.5 - - - - - - - - 178.7 - 33.4 - 79 SER 79 T a 49.9 - - - - - - - - - 179.5 - 34.0 - 80 ASN 80 t B - 184.3 - - - - - - - - 183.8 -.6 34.8 - +* +* 81 LEU 81 t b - - -61.1 179.3 - - - - - - 180.4 - 36.0 - 82 ALA 82 T a - - - - - - - - - - 180.7 - 34.1 - 83 GLY 83 T - - - - - - - - - - - 180.4 - - - 84 ALA 84 t B - - - - - - - - - - 176.6 -.9 34.0 - +* +* 85 VAL 85 B 57.8 - - - - - - - - - 182.9 -.7 32.8 - +* +* 86 THR 86 E B - - -52.2 - - - - - - - 176.5 -3.5 36.1 - ** ** 87 THR 87 E B - - -53.1 - - - - - - - 184.6 - 35.2 - 88 MET 88 E B - 178.7 - 174.0 - - - - - - 180.1 -2.9 33.2 - * * 89 HIS 89 E B - - -76.2 - - - - - - - 174.7 -1.7 32.6 - 90 VAL 90 E B - 178.1 - - - - - - - - 180.5 -2.6 34.5 - 91 ILE 91 E B - - -69.1 186.9 - - - - - - 186.4 -1.7 31.5 - * * 92 ILE 92 E B - - -55.6 - - - - - - - 176.5 - 36.2 - 93 GLN 93 e B - - -60.7 182.6 - - - - - - 182.6 -.8 33.3 - +* +* 94 ALA 94 B - - - - - - - - - - 177.5 -.6 34.2 - +* +* 95 PRO 95 - - - - - -74.8 - - - - - 178.7 - 38.9 - * * Residue-by-residue listing for refined_1 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 96 VAL 96 S B - 179.4 - - - - - - - - 182.4 - 33.7 - 97 THR 97 S l - - -58.1 - - - - - - - 179.9 -1.0 31.5 - * * 98 GLU 98 b - 179.8 - - - - - - - - 184.6 - 34.5 - 99 LYS 99 b - 170.4 - 187.0 - - - - - - 176.4 - 34.8 - 100 GLU 100 XX - 182.6 - - - - - - - - 166.5 - 30.9 - **** ** **** 101 LYS 101 - 77.3 - - - - - - - - - - - 25.7 - ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * * * ** ** ** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.8 181.9 -62.2 180.9 -64.8 -64.8 -39.1 - - - 179.4 -1.9 34.1 Standard deviations: 6.9 6.3 8.0 5.9 6.6 7.2 6.8 - - - 4.1 .9 2.4 Numbers of values: 21 23 38 23 6 11 11 0 0 0 100 52 96 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_1 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 GLU 1 - 1.233 1.509 1.533 1.452 - 116.47 120.37 111.20 110.08 110.95 123.15 2 ALA 2 1.311 1.241 1.515 1.521 1.435 121.22 116.39 120.36 110.85 109.46 110.27 123.25 * * * 3 GLU 3 1.309 1.238 1.516 1.559 1.432 121.88 115.37 120.10 112.57 110.62 113.21 124.52 * * * * +* +* 4 VAL 4 1.336 1.241 1.511 1.558 1.464 125.41 114.00 122.64 114.17 113.75 116.43 123.35 ** * * ** +** +** 5 HIS 5 1.289 1.230 1.510 1.558 1.448 121.90 114.82 122.10 113.00 114.16 114.41 123.00 +** * +* * ** +** 6 ASN 6 1.296 1.240 1.486 1.541 1.421 121.80 114.26 121.56 111.74 110.29 114.21 123.89 ** +* +* ** ** 7 GLN 7 1.296 1.238 1.503 1.541 1.418 123.76 118.26 119.73 110.26 106.59 111.94 122.00 ** * ** * * +* ** 8 LEU 8 1.298 1.233 1.495 1.525 1.428 118.13 115.85 121.08 112.17 108.71 113.48 123.07 ** * +* +* * +* ** 9 GLU 9 1.280 1.210 1.493 1.517 1.430 121.63 115.66 120.93 110.67 111.96 110.46 123.38 *** * +* * *** 10 ILE 10 1.298 1.239 1.504 1.570 1.431 122.29 116.45 120.32 107.44 108.45 112.29 123.18 ** * * * ** 11 LYS 11 1.296 1.245 1.503 1.529 1.436 119.81 116.27 120.62 111.01 109.26 115.34 123.11 ** * * * +** +** Residue-by-residue listing for refined_1 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 PHE 12 1.292 1.224 1.517 1.532 1.437 121.51 117.24 120.22 109.18 110.93 109.51 122.53 +** * +** 13 ARG 13 1.315 1.230 1.487 1.519 1.428 120.93 115.44 120.87 109.20 109.86 113.94 123.69 +* +* ** ** 14 LEU 14 1.285 1.238 1.517 1.545 1.424 122.70 115.72 120.65 110.23 109.43 111.27 123.63 *** +* *** 15 THR 15 1.312 1.232 1.543 1.551 1.460 124.06 115.72 121.49 110.36 111.89 109.40 122.79 * * * * 16 ASP 16 1.309 1.226 1.538 1.528 1.459 121.94 117.05 120.63 110.48 111.98 111.41 122.32 * * 17 GLY 17 1.324 1.240 1.526 - 1.461 121.05 117.37 120.26 - 114.75 - 122.37 18 SER 18 1.309 1.228 1.531 1.526 1.461 121.01 118.59 119.62 110.43 108.58 109.37 121.77 * * * 19 ASP 19 1.323 1.228 1.514 1.528 1.435 120.04 114.83 121.33 110.28 112.30 111.22 123.83 * * 20 ILE 20 1.303 1.232 1.525 1.566 1.448 124.40 116.91 119.34 109.48 107.71 110.80 123.72 +* * * +* 21 GLY 21 1.330 1.243 1.526 - 1.459 122.18 117.15 120.40 - 113.87 - 122.44 22 PRO 22 1.348 1.238 1.517 1.533 1.461 123.32 114.74 121.52 109.75 113.62 104.07 123.74 * * * 23 LYS 23 1.295 1.220 1.513 1.540 1.441 124.12 118.37 119.10 109.69 106.81 109.49 122.53 ** * * * +* ** 24 ALA 24 1.308 1.239 1.511 1.519 1.441 120.58 116.34 120.55 110.81 109.35 110.86 123.05 +* +* 25 PHE 25 1.318 1.250 1.500 1.533 1.437 121.44 117.39 120.50 107.08 109.35 111.90 122.09 * * +* +* 26 PRO 26 1.317 1.237 1.528 1.526 1.443 121.88 116.60 120.42 108.17 109.74 104.24 122.98 +* +* * * +* 27 ASP 27 1.304 1.223 1.527 1.535 1.464 122.57 115.87 121.24 109.00 110.33 110.77 122.83 +* +* 28 ALA 28 1.319 1.231 1.531 1.518 1.452 122.37 117.09 120.43 110.00 111.82 109.93 122.48 29 THR 29 1.321 1.236 1.534 1.550 1.449 120.91 116.86 120.56 108.80 108.82 111.09 122.55 30 THR 30 1.304 1.244 1.524 1.543 1.433 121.53 117.42 120.25 109.41 109.25 110.51 122.34 +* * +* 31 VAL 31 1.321 1.218 1.532 1.558 1.448 120.65 116.45 120.73 112.15 109.88 113.08 122.79 * * 32 SER 32 1.333 1.232 1.538 1.534 1.454 121.55 116.57 120.43 110.92 110.26 110.67 122.94 33 ALA 33 1.337 1.224 1.528 1.521 1.463 122.04 116.45 120.60 110.61 110.99 110.60 122.94 34 LEU 34 1.325 1.230 1.529 1.525 1.431 123.62 114.90 121.35 110.82 109.34 106.85 123.72 * * ** ** 35 LYS 35 1.315 1.220 1.544 1.541 1.447 124.24 115.98 120.68 112.42 108.58 107.07 123.29 * * * ** ** 36 GLU 36 1.340 1.235 1.534 1.533 1.479 123.59 115.82 120.95 108.39 111.06 109.60 123.22 * * * 37 THR 37 1.329 1.245 1.529 1.553 1.454 122.94 115.51 120.88 109.78 110.46 110.63 123.57 38 VAL 38 1.321 1.212 1.518 1.546 1.445 122.47 116.18 120.35 109.07 109.99 111.55 123.41 39 ILE 39 1.326 1.223 1.529 1.563 1.472 122.93 116.11 121.16 109.74 110.56 111.36 122.73 40 SER 40 1.315 1.235 1.556 1.524 1.441 121.69 116.91 120.81 111.13 111.45 109.15 122.28 * * 41 GLU 41 1.335 1.244 1.525 1.523 1.445 122.40 114.85 121.30 108.45 111.07 109.60 123.85 42 TRP 42 1.304 1.231 1.525 1.528 1.438 124.09 118.36 120.07 110.18 108.97 107.58 121.54 +* * * * +* +* 43 PRO 43 1.334 1.225 1.530 1.538 1.456 122.09 116.59 120.67 109.74 112.21 103.99 122.74 44 ARG 44 1.320 1.231 1.531 1.536 1.463 122.02 114.83 122.01 112.04 109.53 111.59 123.16 * * Residue-by-residue listing for refined_1 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 45 GLU 45 1.324 1.241 1.544 1.528 1.460 123.22 116.20 120.72 108.79 111.05 109.73 123.08 46 LYS 46 1.324 1.227 1.517 1.536 1.450 122.70 116.65 120.54 108.32 111.66 109.87 122.78 47 GLU 47 1.301 1.247 1.500 1.511 1.417 121.05 115.17 120.45 109.71 108.13 113.13 124.38 ** * ** * +* ** 48 ASN 48 1.293 1.242 1.529 1.548 1.457 124.19 114.16 122.39 113.08 112.57 113.27 123.18 +** * * +* +* +** 49 GLY 49 1.291 1.235 1.479 - 1.396 124.16 119.19 118.21 - 106.21 - 122.55 +** ** *** ** * * ** *** 50 PRO 50 1.323 1.236 1.531 1.530 1.466 122.55 115.18 120.70 108.66 112.39 102.55 124.10 * * * * 51 LYS 51 1.317 1.227 1.492 1.528 1.466 124.89 116.02 121.09 112.05 110.52 114.79 122.85 +* +* * +** +** 52 THR 52 1.311 1.249 1.528 1.538 1.414 120.09 116.16 120.47 111.44 108.82 113.44 123.36 * ** * * ** 53 VAL 53 1.313 1.234 1.543 1.563 1.458 123.49 116.63 120.64 111.79 114.24 110.99 122.63 * * * * 54 LYS 54 1.306 1.227 1.531 1.529 1.455 121.96 117.11 120.43 110.60 113.25 109.68 122.45 +* +* 55 GLU 55 1.316 1.233 1.531 1.515 1.467 121.01 116.98 120.63 109.21 113.14 110.27 122.37 56 VAL 56 1.308 1.238 1.543 1.559 1.455 120.51 115.58 121.25 110.74 112.51 111.04 123.15 +* +* 57 LYS 57 1.326 1.240 1.519 1.543 1.454 123.29 115.54 120.74 109.58 111.40 111.71 123.72 58 LEU 58 1.316 1.232 1.522 1.561 1.451 122.87 117.42 119.89 109.68 108.26 111.40 122.68 +* * +* 59 ILE 59 1.320 1.240 1.528 1.561 1.462 121.54 115.38 121.27 110.91 111.79 110.99 123.35 60 SER 60 1.315 1.239 1.527 1.540 1.440 122.86 116.44 120.02 110.52 109.10 109.80 123.51 * * 61 ALA 61 1.344 1.242 1.529 1.529 1.481 124.32 115.61 121.21 111.32 111.62 111.32 123.11 * * * * 62 GLY 62 1.315 1.235 1.506 - 1.443 121.32 115.84 121.04 - 111.64 - 123.11 63 LYS 63 1.306 1.235 1.511 1.533 1.434 122.12 116.82 119.95 109.69 108.90 109.11 123.20 +* * +* 64 VAL 64 1.314 1.239 1.529 1.570 1.445 120.90 116.21 120.86 111.39 109.45 112.58 122.87 * * * * 65 LEU 65 1.300 1.240 1.514 1.540 1.417 122.09 115.53 121.03 110.65 112.28 112.01 123.41 ** ** ** 66 GLU 66 1.323 1.240 1.528 1.541 1.446 121.99 116.45 120.32 110.76 108.56 110.52 123.21 67 ASN 67 1.326 1.233 1.524 1.551 1.471 122.66 115.33 120.96 110.31 111.48 111.82 123.70 * * 68 SER 68 1.320 1.245 1.547 1.537 1.453 123.93 116.29 120.94 111.31 112.00 108.29 122.77 * * * * 69 LYS 69 1.305 1.229 1.521 1.515 1.427 123.74 117.77 119.92 111.07 108.70 108.84 122.28 +* +* * +* 70 THR 70 1.302 1.236 1.510 1.538 1.414 121.15 117.13 120.02 109.64 109.04 111.41 122.84 +* ** ** 71 VAL 71 1.315 1.228 1.538 1.560 1.442 121.03 115.43 121.07 110.84 108.75 111.44 123.43 * * 72 LYS 72 1.340 1.237 1.530 1.541 1.470 124.60 115.67 120.75 110.67 111.16 109.46 123.53 +* +* 73 ASP 73 1.329 1.230 1.535 1.541 1.456 123.91 116.71 120.80 108.87 112.15 109.57 122.49 * * 74 TYR 74 1.322 1.230 1.530 1.527 1.449 122.36 115.88 121.19 109.21 111.06 108.42 122.93 * * 75 ARG 75 1.299 1.230 1.504 1.493 1.434 123.46 114.02 121.76 109.31 114.24 107.85 124.22 ** +* * * * +* ** Residue-by-residue listing for refined_1 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 76 SER 76 1.310 1.237 1.540 1.523 1.421 124.20 118.92 119.45 109.76 107.90 107.09 121.62 * +* * * * ** ** 77 PRO 77 1.347 1.237 1.549 1.539 1.475 122.56 116.54 121.11 110.16 112.37 103.52 122.30 * * 78 VAL 78 1.330 1.232 1.550 1.558 1.473 122.64 115.43 122.25 111.05 110.69 110.79 122.23 * * 79 SER 79 1.313 1.240 1.538 1.518 1.454 123.59 114.17 122.37 112.17 110.99 108.51 123.41 * * * * * * 80 ASN 80 1.289 1.241 1.521 1.544 1.437 124.44 117.43 119.86 111.48 106.77 109.75 122.67 +** * +* +* +** 81 LEU 81 1.309 1.223 1.530 1.496 1.402 122.78 116.40 121.13 110.69 111.79 106.99 122.46 * +* +** ** +** 82 ALA 82 1.315 1.235 1.528 1.510 1.444 122.35 115.83 121.36 110.62 111.23 109.84 122.79 * * 83 GLY 83 1.307 1.240 1.508 - 1.439 120.97 116.16 121.00 - 112.05 - 122.84 +* +* 84 ALA 84 1.310 1.234 1.515 1.518 1.437 121.52 115.88 120.92 110.33 110.79 110.63 123.18 * * * 85 VAL 85 1.306 1.242 1.532 1.573 1.441 121.68 116.86 120.41 112.05 108.43 111.92 122.69 +* * * +* 86 THR 86 1.294 1.231 1.524 1.550 1.422 122.18 116.73 120.90 109.05 109.07 109.80 122.35 ** +* ** 87 THR 87 1.287 1.229 1.530 1.527 1.421 121.45 117.08 120.45 109.67 108.02 110.46 122.46 *** +* * *** 88 MET 88 1.305 1.230 1.518 1.531 1.449 121.26 116.39 120.38 112.04 111.38 109.85 123.20 +* * +* 89 HIS 89 1.327 1.237 1.497 1.533 1.452 121.70 114.15 121.64 108.96 113.05 113.27 124.20 * * +* +* 90 VAL 90 1.296 1.240 1.494 1.548 1.427 123.48 115.05 121.54 109.73 107.70 112.02 123.40 ** * +* * ** 91 ILE 91 1.273 1.238 1.508 1.540 1.404 121.38 114.82 121.35 113.77 110.15 111.32 123.83 +*** +** ** +*** 92 ILE 92 1.301 1.220 1.502 1.551 1.427 122.80 116.48 120.70 108.43 110.12 110.07 122.79 +* * +* +* 93 GLN 93 1.301 1.235 1.509 1.530 1.428 120.47 115.68 121.02 111.61 108.61 111.33 123.30 ** +* ** 94 ALA 94 1.296 1.237 1.523 1.524 1.439 121.97 117.42 120.50 110.62 110.87 110.08 122.05 ** ** 95 PRO 95 1.329 1.238 1.531 1.523 1.465 122.68 116.20 120.83 109.89 112.48 103.38 122.97 96 VAL 96 1.325 1.242 1.519 1.552 1.456 121.67 115.23 120.61 109.84 109.54 112.25 124.15 97 THR 97 1.317 1.239 1.540 1.529 1.437 124.44 114.54 122.08 112.49 112.27 111.37 123.30 * +* +* +* 98 GLU 98 1.302 1.243 1.507 1.539 1.435 123.95 116.43 119.83 111.04 107.22 110.54 123.73 +* * * * +* 99 LYS 99 1.308 1.220 1.518 1.541 1.434 123.01 116.43 119.05 109.28 110.85 110.77 124.52 * * * * 100 GLU 100 1.351 1.241 1.569 1.550 1.486 124.78 117.66 119.30 115.58 112.47 108.78 123.03 +* ** * +* +** * +** 101 LYS 101 1.351 - 1.526 1.587 1.470 123.26 - - 114.09 111.16 117.98 - +* +** ** **** **** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * ** +** *** ** * * +** ** **** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 94 1.273 1.351 1.312 .015 +*** +* * C-N (Pro) 1.341 .016 6 1.317 1.348 1.333 .011 +* C-O C-O 1.231 .020 100 1.210 1.250 1.234 .008 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.486 1.569 1.523 .015 +* ** CH2G*-C (Gly) 1.516 .018 5 1.479 1.526 1.509 .017 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.510 1.529 1.520 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.527 1.573 1.553 .012 * CH1E-CH2E (the rest) 1.530 .020 62 1.493 1.587 1.533 .014 +* +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.402 1.486 1.444 .017 +** * NH1-CH2G* (Gly) 1.451 .016 5 1.396 1.461 1.440 .023 *** N-CH1E (Pro) 1.466 .015 6 1.443 1.475 1.461 .010 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 Page 10 ---------------------------------------- +-----------------+ | 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 89 114.00 118.92 116.17 1.06 * * CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.84 119.19 117.14 1.17 * CH1E-C-N (Pro) 116.9 1.5 6 114.74 116.60 115.97 .74 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.54 124.52 123.04 .61 O-C-N (Pro) 122.0 1.4 6 122.30 124.10 123.14 .61 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.13 125.41 122.42 1.35 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.97 124.16 121.94 1.19 ** C-N-CH1E (Pro) 122.6 5.0 6 121.88 123.32 122.51 .46 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 119.05 122.64 120.75 .70 * * CH2G*-C-O (Gly) 120.8 2.1 5 118.21 121.04 120.18 1.03 * CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.00 111.32 110.64 .36 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 107.44 114.17 110.51 1.57 ** CH2E-CH1E-C (the rest) 110.1 1.9 62 107.08 115.58 110.47 1.50 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 106.59 114.24 110.34 1.75 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 106.21 114.75 111.70 2.98 ** N-CH1E-C (Pro) 111.8 2.5 6 109.74 113.62 112.14 1.17 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.84 111.32 110.44 .47 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.40 116.43 111.50 1.35 * +** N-CH1E-CH2E (Pro) 103.0 1.1 6 102.55 104.24 103.62 .57 * NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.85 117.98 110.70 2.26 ** **** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_1 Page 11 ---------------------------------------- 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] 11 12.5% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% 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 5 Number of proline residues 6 ---- Total number of residues 101 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 100 4.1 6.0 3.0 -.6 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 2.4 3.1 1.6 -.4 Inside e. H-bond energy st dev 52 .9 .8 .2 .7 Inside f. Overall G-factor 101 -.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 21 6.9 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 23 6.3 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 38 8.0 17.5 4.9 -2.0 BETTER d. Chi-1 pooled st dev 82 8.1 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 23 5.9 20.4 5.0 -2.9 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 9.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for refined_1 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.57 Chi1-chi2 distribution -.25 Chi1 only -.03 Chi3 & chi4 .08 Omega -.11 ------ -.24 ===== Main-chain covalent forces:- Main-chain bond lengths -.01 Main-chain bond angles .33 ------ .19 ===== OVERALL AVERAGE -.09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.