Residue-by-residue listing for refined_17 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 - - - -62.1 180.4 - - - - - - 178.5 - 34.4 - 2 ALA 2 B - - - - - - - - - - 180.4 - 34.1 - 3 GLU 3 b - 181.0 - 181.8 - - - - - - 177.5 - 33.8 - 4 VAL 4 S A - 183.1 - - - - - - - - 175.7 - 32.6 - 5 HIS 5 S b 55.3 - - - - - - - - - 186.4 - 28.1 - * +* +* 6 ASN 6 B - 174.7 - - - - - - - - 177.5 -1.7 34.4 - 7 GLN 7 e b - - -70.0 - - - - - - - 174.7 - 35.0 - 8 LEU 8 E B - - -64.3 - - - - - - - 175.0 -1.6 34.2 - 9 GLU 9 E B - - -62.4 184.0 - - - - - - 179.8 -3.3 33.8 - +* +* 10 ILE 10 E B - - -58.1 179.2 - - - - - - 177.4 -2.6 33.5 - 11 LYS 11 E B 58.2 - - 184.6 - - - - - - 185.4 -2.3 32.2 - 12 PHE 12 E B - - -60.5 - - - - - - - 179.9 -.7 34.2 - +* +* 13 ARG 13 E B - 173.9 - 181.2 - - - - - - 179.6 -3.1 34.5 - * * 14 LEU 14 e B - - -68.5 - - - - - - - 181.2 -3.4 34.2 - +* +* 15 THR 15 T A 47.5 - - - - - - - - - 180.6 - 34.7 - * * 16 ASP 16 T A - - -57.1 - - - - - - - 184.7 - 35.7 - 17 GLY 17 t - - - - - - - - - - - 177.8 -1.5 - - 18 SER 18 e B - 182.1 - - - - - - - - 181.2 - 35.4 - 19 ASP 19 E B 66.1 - - - - - - - - - 172.1 - 35.5 - * * 20 ILE 20 E B - - -58.9 179.4 - - - - - - 182.5 -1.6 34.9 - 21 GLY 21 E - - - - - - - - - - - 181.1 - - - Residue-by-residue listing for refined_17 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 PRO 22 E - - - - - -57.8 - - - - - 180.8 - 38.1 - * * 23 LYS 23 E B - 187.9 - 180.8 - - - - - - 181.4 -2.1 35.2 - 24 ALA 24 E B - - - - - - - - - - 177.9 - 34.0 - 25 PHE 25 E B - - -55.3 - - - - - - - 171.8 -3.8 36.5 - * ** ** 26 PRO 26 t - - - - - -59.2 - - - - - 176.3 - 40.3 - +* +* 27 ASP 27 T A - - -60.0 - - - - - - - 184.0 - 36.3 - 28 ALA 28 T A - - - - - - - - - - 178.1 - 33.9 - 29 THR 29 t B - - -62.6 - - - - - - - 180.3 -2.3 33.2 - 30 THR 30 h B 51.1 - - - - - - - - - 178.4 - 34.7 - 31 VAL 31 H A - 177.7 - - - -66.5 -26.3 - - - 175.5 -3.2 32.6 - * +* +* 32 SER 32 H A 51.2 - - - - -57.6 -49.3 - - - 179.4 -.9 34.5 - +* +* 33 ALA 33 H A - - - - - -69.4 -31.4 - - - 176.6 - 33.9 - 34 LEU 34 H A - 172.7 - - - -64.2 -49.3 - - - 178.0 -1.7 35.9 - 35 LYS 35 H A - 177.5 - - - -59.3 -46.8 - - - 176.4 -3.4 34.2 - +* +* 36 GLU 36 H A - - -68.7 - - -56.9 -39.8 - - - 176.8 -2.6 34.5 - 37 THR 37 H A - - -61.5 - - -67.7 -40.3 - - - 180.2 -2.0 33.5 - 38 VAL 38 H A - 179.9 - - - -58.7 -51.4 - - - 180.1 -2.4 34.7 - * * 39 ILE 39 H A - - -59.7 179.8 - -61.2 -33.4 - - - 179.9 -2.6 33.9 - 40 SER 40 H A - - -56.9 - - -76.0 -39.3 - - - 180.9 -1.4 32.7 - 41 GLU 41 H A - - -58.5 - - -76.9 -28.5 - - - 176.4 -3.0 34.6 - * * 42 TRP 42 h B - 197.8 - - - - - - - - 180.3 -2.4 36.5 - 43 PRO 43 t - - - - - -62.3 - - - - - 178.9 - 38.0 - * * 44 ARG 44 T A - - -57.4 184.4 - - - - - - 177.6 -.6 34.0 - +* +* 45 GLU 45 T A - 182.4 - 182.3 - - - - - - 180.6 - 35.6 - 46 LYS 46 t B - 189.9 - - - - - - - - 177.6 -1.5 34.3 - 47 GLU 47 b - - -67.2 - - - - - - - 181.5 - 34.2 - 48 ASN 48 S b - - -68.7 - - - - - - - 167.2 - 27.5 - ** +* ** 49 GLY 49 S - - - - - - - - - - - 168.8 -2.6 - - +* +* 50 PRO 50 S - - - - - -65.9 - - - - - 178.0 - 39.3 - +* +* 51 LYS 51 a - 185.0 - 174.3 - - - - - - 178.5 - 33.5 - 52 THR 52 t B 61.3 - - - - - - - - - 181.2 - 33.3 - 53 VAL 53 T A 59.6 - - - - - - - - - 180.1 - 32.8 - 54 LYS 54 T A - - -59.1 179.9 - - - - - - 178.1 - 33.7 - 55 GLU 55 e a - - -53.4 - - - - - - - 184.7 -2.4 34.0 - 56 VAL 56 E B 58.0 - - - - - - - - - 176.7 -2.7 32.5 - 57 LYS 57 E B - - -75.3 179.3 - - - - - - 183.5 -1.2 29.9 - * * * 58 LEU 58 E B - - -56.8 - - - - - - - 180.9 -.5 34.8 - ** ** 59 ILE 59 E B - - -65.7 184.7 - - - - - - 176.4 -3.2 33.3 - +* +* 60 SER 60 E B - - -61.9 - - - - - - - 178.0 -2.9 34.6 - * * 61 ALA 61 T l - - - - - - - - - - 180.9 - 32.6 - Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 62 GLY 62 T - - - - - - - - - - - 180.7 - - - 63 LYS 63 E B - 180.6 - - - - - - - - 183.8 -.9 35.4 - +* +* 64 VAL 64 E B 64.3 - - - - - - - - - 178.1 - 32.4 - 65 LEU 65 E B - - -66.1 - - - - - - - 178.8 -3.1 34.6 - * * 66 GLU 66 t B - - -57.0 179.6 - - - - - - 186.6 -.8 33.7 - * +* +* 67 ASN 67 T A 67.2 - - - - - - - - - 182.6 - 33.4 - 68 SER 68 T A - - -53.9 - - - - - - - 182.6 - 34.8 - 69 LYS 69 t B - - -73.3 - - - - - - - 177.1 -2.5 33.1 - 70 THR 70 B B - - -45.3 - - - - - - - 180.4 - 36.5 - * * 71 VAL 71 G A - 176.9 - - - - - - - - 178.4 -3.0 33.3 - * * 72 LYS 72 G A - 183.1 - 182.0 - - - - - - 179.8 -2.0 34.7 - 73 ASP 73 G A - 179.1 - - - - - - - - 183.4 -.7 34.8 - +* +* 74 TYR 74 G A - - -64.0 - - - - - - - 180.5 -.9 34.2 - +* +* 75 ARG 75 g b - 184.1 - - - - - - - - 181.3 -.8 36.0 - +* +* 76 SER 76 B - - -56.8 - - - - - - - 176.5 -1.1 35.8 - * * 77 PRO 77 - - - - - -70.7 - - - - - 181.5 - 38.1 - * * 78 VAL 78 B - 179.2 - - - - - - - - 180.9 -.6 36.2 - +* +* 79 SER 79 b - - -56.9 - - - - - - - 184.0 - 34.5 - 80 ASN 80 B - - -65.1 - - - - - - - 175.7 - 33.9 - 81 LEU 81 b - - -78.2 - - - - - - - 180.6 -.8 35.2 - +* +* 82 ALA 82 S b - - - - - - - - - - 180.0 - 32.8 - 83 GLY 83 S - - - - - - - - - - - 181.0 -1.6 - - 84 ALA 84 E B - - - - - - - - - - 177.2 -1.5 34.4 - 85 VAL 85 E B - 180.3 - - - - - - - - 181.6 - 33.9 - 86 THR 86 E B - - -53.7 - - - - - - - 178.7 -3.6 35.0 - ** ** 87 THR 87 E B - - -52.9 - - - - - - - 181.9 - 35.3 - 88 MET 88 E B - 177.6 - 172.1 - - - - - - 183.8 -2.6 33.2 - 89 HIS 89 E B - 190.9 - - - - - - - - 178.3 -2.2 35.2 - 90 VAL 90 E B - 181.2 - - - - - - - - 179.6 -3.1 34.4 - * * 91 ILE 91 E B - - -66.8 - - - - - - - 181.3 -2.8 35.0 - * * 92 ILE 92 E B - - -70.6 - - - - - - - 174.2 -.7 32.4 - * +* +* 93 GLN 93 e B - - -62.0 177.0 - - - - - - 183.6 -.8 34.4 - +* +* 94 ALA 94 B - - - - - - - - - - 174.9 -.8 34.1 - +* +* 95 PRO 95 - - - - - -91.6 - - - - - 175.8 - 39.3 - ** +* ** 96 VAL 96 B - 180.4 - - - - - - - - 181.2 - 34.0 - 97 THR 97 B - - -55.4 - - - - - - - 182.2 - 33.5 - 98 GLU 98 B - 183.9 - 179.3 - - - - - - 180.4 - 35.2 - Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 LYS 99 S XX - 184.8 - 181.1 - - - - - - 179.2 - 32.1 - **** **** 100 GLU 100 l - - -58.4 182.4 - - - - - - 174.8 - 30.9 - 101 LYS 101 - - 183.4 - 179.8 - - - - - - - - 33.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * ** * ** ** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.2 181.8 -61.6 180.4 -67.9 -65.0 -39.6 - - - 179.3 -2.0 34.3 Standard deviations: 6.5 5.3 6.6 3.0 12.5 7.1 8.9 - - - 3.3 1.0 1.9 Numbers of values: 11 28 43 23 6 11 11 0 0 0 100 55 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_17 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 - 1.236 1.519 1.523 1.458 - 116.32 120.78 109.15 110.69 111.22 122.90 2 ALA 2 1.306 1.232 1.511 1.523 1.438 122.06 116.36 120.58 110.69 109.22 110.70 123.03 +* * +* 3 GLU 3 1.303 1.232 1.510 1.525 1.419 122.15 115.70 121.00 110.16 110.17 111.56 123.27 +* ** ** 4 VAL 4 1.298 1.229 1.508 1.542 1.444 121.61 114.58 122.19 111.75 109.34 111.95 123.20 ** * ** 5 HIS 5 1.282 1.232 1.513 1.568 1.452 121.12 113.66 122.70 114.25 109.69 115.57 123.53 *** +* * * ** +** *** 6 ASN 6 1.285 1.245 1.519 1.550 1.427 123.17 115.41 120.86 112.74 111.28 107.91 123.67 *** +* * +* *** 7 GLN 7 1.320 1.227 1.535 1.551 1.454 123.79 118.71 120.09 110.49 108.20 109.92 121.11 * * * * * * 8 LEU 8 1.303 1.214 1.491 1.517 1.442 118.55 117.10 120.42 107.46 109.45 113.64 122.48 +* +* +* * +* +* 9 GLU 9 1.278 1.226 1.483 1.510 1.418 119.82 115.69 121.08 108.74 108.10 113.52 123.22 +*** +* ** * * +* +*** 10 ILE 10 1.266 1.236 1.490 1.559 1.424 121.16 115.09 121.01 109.88 108.69 113.23 123.86 **** +* +* * **** 11 LYS 11 1.283 1.247 1.503 1.540 1.423 122.00 115.75 120.94 112.57 108.68 112.11 123.29 *** * +* * *** Residue-by-residue listing for refined_17 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 1.288 1.224 1.516 1.529 1.433 121.74 115.94 120.54 111.11 111.01 109.68 123.51 +** * +** 13 ARG 13 1.319 1.238 1.527 1.537 1.453 122.93 116.01 120.65 110.22 110.63 110.18 123.34 14 LEU 14 1.312 1.235 1.520 1.555 1.454 122.85 115.80 120.85 109.15 110.40 111.87 123.29 * * * 15 THR 15 1.318 1.227 1.535 1.534 1.450 123.46 116.24 121.06 110.15 112.41 109.35 122.70 * * 16 ASP 16 1.322 1.223 1.510 1.533 1.466 122.10 116.48 120.81 107.77 110.64 110.84 122.70 * * 17 GLY 17 1.314 1.231 1.512 - 1.441 120.19 115.02 121.52 - 110.25 - 123.45 * * 18 SER 18 1.310 1.238 1.516 1.542 1.433 123.00 117.37 119.97 110.88 107.58 109.29 122.65 * * * * 19 ASP 19 1.293 1.236 1.498 1.527 1.412 121.30 115.12 121.12 108.69 110.47 110.63 123.74 +** * ** +** 20 ILE 20 1.289 1.250 1.506 1.563 1.434 122.61 116.89 118.87 109.88 105.28 111.97 124.21 +** * * ** +** 21 GLY 21 1.334 1.239 1.512 - 1.450 121.48 117.96 119.87 - 112.39 - 122.15 22 PRO 22 1.345 1.237 1.514 1.531 1.455 122.63 115.75 121.27 110.17 112.17 104.57 122.98 * * 23 LYS 23 1.287 1.220 1.503 1.532 1.431 121.47 117.77 119.47 110.75 107.29 109.70 122.75 *** * * * *** 24 ALA 24 1.299 1.246 1.515 1.512 1.435 120.44 115.36 121.23 110.55 110.84 110.33 123.41 ** * ** 25 PHE 25 1.305 1.233 1.520 1.537 1.435 123.62 117.47 120.49 107.20 108.43 110.94 121.92 +* * * +* +* 26 PRO 26 1.312 1.238 1.538 1.519 1.466 122.89 116.31 120.48 108.20 112.25 102.99 123.21 +* * +* 27 ASP 27 1.336 1.233 1.538 1.550 1.489 123.25 115.42 121.64 106.97 110.33 110.67 122.93 +* +* +* 28 ALA 28 1.327 1.241 1.538 1.517 1.453 122.95 117.61 120.13 110.37 113.19 109.75 122.26 29 THR 29 1.320 1.230 1.527 1.552 1.450 120.69 116.25 120.92 110.94 110.18 111.56 122.79 30 THR 30 1.301 1.242 1.531 1.531 1.419 122.15 116.62 120.75 110.61 110.98 109.45 122.63 ** ** * ** 31 VAL 31 1.325 1.222 1.525 1.554 1.457 121.64 116.05 121.09 111.08 109.98 112.39 122.85 32 SER 32 1.317 1.230 1.540 1.527 1.437 122.01 115.98 120.72 111.68 110.09 108.82 123.16 * * 33 ALA 33 1.335 1.230 1.525 1.519 1.459 122.73 116.19 120.78 110.67 110.78 110.29 123.03 34 LEU 34 1.327 1.213 1.524 1.526 1.423 123.29 115.46 120.74 111.69 108.55 107.22 123.74 +* +* +* 35 LYS 35 1.322 1.232 1.519 1.546 1.460 124.22 115.47 120.92 112.22 110.74 108.58 123.61 * * * * 36 GLU 36 1.312 1.234 1.522 1.525 1.462 122.80 115.47 121.28 111.07 110.48 109.22 123.23 * * 37 THR 37 1.311 1.209 1.537 1.547 1.432 122.32 117.19 119.89 111.18 110.88 110.68 122.86 * * * * 38 VAL 38 1.333 1.220 1.511 1.551 1.468 122.36 115.47 120.72 108.78 109.78 111.75 123.76 39 ILE 39 1.320 1.224 1.536 1.565 1.466 122.47 115.83 121.55 110.54 110.31 111.01 122.62 40 SER 40 1.312 1.234 1.549 1.519 1.438 121.50 117.36 120.29 111.59 112.86 110.24 122.36 * * * * 41 GLU 41 1.334 1.234 1.522 1.518 1.437 122.03 115.89 120.98 110.07 110.60 110.04 123.13 * * 42 TRP 42 1.316 1.234 1.525 1.544 1.441 122.16 119.39 119.37 110.11 105.41 108.81 121.16 +* ** * ** Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 PRO 43 1.332 1.223 1.526 1.532 1.448 121.37 116.67 120.79 110.45 111.70 104.61 122.54 * * * 44 ARG 44 1.324 1.227 1.517 1.528 1.457 121.51 114.34 121.77 110.23 108.89 111.32 123.88 45 GLU 45 1.327 1.225 1.540 1.532 1.441 123.86 117.02 120.60 109.92 110.50 108.84 122.37 * * 46 LYS 46 1.330 1.241 1.531 1.553 1.454 121.53 115.89 120.58 110.53 109.39 110.69 123.51 * * 47 GLU 47 1.313 1.239 1.530 1.540 1.445 123.93 116.34 120.99 110.21 111.28 110.39 122.67 * * * 48 ASN 48 1.316 1.233 1.495 1.536 1.436 122.22 112.30 122.74 112.35 114.31 115.68 124.58 * * +* * * * *** *** 49 GLY 49 1.264 1.245 1.488 - 1.416 124.25 119.29 119.40 - 105.83 - 121.31 *4.6* +* ** ** * ** * *4.6* 50 PRO 50 1.304 1.227 1.522 1.531 1.441 120.81 117.58 119.92 110.15 108.04 103.64 122.40 ** +* +* ** 51 LYS 51 1.293 1.216 1.500 1.538 1.441 120.05 116.02 121.23 111.36 109.64 110.94 122.75 +** * +** 52 THR 52 1.300 1.240 1.530 1.548 1.414 121.20 115.40 120.88 110.67 110.38 111.86 123.72 ** ** ** 53 VAL 53 1.314 1.251 1.549 1.555 1.472 125.34 116.54 121.26 111.64 112.81 110.34 122.20 * * * ** * ** 54 LYS 54 1.324 1.224 1.524 1.524 1.440 121.37 116.77 120.53 110.54 110.28 111.00 122.69 55 GLU 55 1.324 1.229 1.511 1.530 1.439 120.76 116.31 120.84 108.10 110.37 113.11 122.85 * +* +* 56 VAL 56 1.308 1.235 1.538 1.571 1.443 120.79 115.19 121.74 111.54 112.11 111.39 123.03 +* * * +* 57 LYS 57 1.315 1.236 1.514 1.515 1.437 123.15 115.74 120.75 113.43 112.94 112.19 123.50 * +* +* 58 LEU 58 1.316 1.235 1.531 1.556 1.450 122.75 116.95 120.31 109.72 110.11 110.63 122.74 * * 59 ILE 59 1.324 1.231 1.529 1.571 1.461 122.39 115.56 121.39 110.11 111.96 111.75 123.05 * * 60 SER 60 1.311 1.233 1.523 1.529 1.437 122.69 116.39 120.03 110.29 109.29 110.39 123.51 * * * 61 ALA 61 1.339 1.229 1.533 1.532 1.480 123.99 116.40 120.80 111.03 112.64 111.02 122.71 * * * 62 GLY 62 1.310 1.230 1.513 - 1.455 120.65 115.78 121.06 - 111.76 - 123.16 * * 63 LYS 63 1.307 1.238 1.524 1.539 1.437 122.67 116.74 120.14 111.92 107.67 108.16 123.09 +* * * * +* 64 VAL 64 1.322 1.243 1.531 1.579 1.456 121.66 115.43 121.52 110.93 111.71 112.37 123.02 * * 65 LEU 65 1.301 1.233 1.517 1.547 1.417 122.87 116.44 120.73 109.96 109.02 111.13 122.79 +* ** ** 66 GLU 66 1.312 1.238 1.523 1.523 1.443 121.39 116.48 120.21 111.42 109.41 110.34 123.31 * * 67 ASN 67 1.332 1.230 1.538 1.548 1.489 123.72 117.11 120.14 109.05 113.96 111.51 122.75 +* * +* 68 SER 68 1.315 1.222 1.536 1.516 1.456 122.55 115.97 121.14 110.23 112.24 108.95 122.88 69 LYS 69 1.295 1.243 1.520 1.520 1.436 122.92 114.90 121.43 110.79 113.40 110.46 123.63 ** * ** 70 THR 70 1.308 1.239 1.545 1.542 1.441 123.56 118.23 119.30 109.33 106.76 109.09 122.47 +* * * +* * +* 71 VAL 71 1.334 1.229 1.527 1.570 1.476 121.13 114.84 121.35 110.36 109.72 112.22 123.76 * * Residue-by-residue listing for refined_17 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.321 1.232 1.544 1.525 1.457 124.41 116.95 120.41 110.16 112.15 109.23 122.63 +* +* 73 ASP 73 1.336 1.228 1.517 1.544 1.480 121.81 115.53 121.33 109.15 110.37 110.88 123.07 * * 74 TYR 74 1.312 1.233 1.518 1.521 1.438 122.34 115.90 120.99 110.76 111.75 109.55 123.10 * * * 75 ARG 75 1.306 1.239 1.519 1.500 1.406 123.00 114.85 121.47 111.76 108.92 106.72 123.54 +* * +** ** +** 76 SER 76 1.291 1.239 1.526 1.517 1.423 123.07 117.98 120.06 110.20 110.92 108.24 121.95 +** +* * +** 77 PRO 77 1.350 1.239 1.515 1.528 1.443 121.94 114.54 121.42 110.07 110.39 105.17 124.03 +* +* +* * +* 78 VAL 78 1.286 1.235 1.485 1.568 1.404 127.02 116.89 118.18 108.21 102.00 112.63 124.86 *** +* * +** +** +* *** * *** 79 SER 79 1.296 1.237 1.533 1.527 1.469 124.25 115.50 121.32 110.37 111.30 109.56 123.13 ** * ** 80 ASN 80 1.312 1.230 1.507 1.543 1.447 122.18 116.11 120.83 109.94 111.44 111.26 123.01 * * 81 LEU 81 1.308 1.247 1.519 1.514 1.396 122.64 115.97 120.75 110.07 109.89 109.59 123.27 * *** *** 82 ALA 82 1.308 1.234 1.512 1.523 1.419 122.54 114.75 121.70 111.65 110.11 111.49 123.35 * ** ** 83 GLY 83 1.294 1.234 1.500 - 1.432 121.51 116.13 120.86 - 111.09 - 123.00 ** * ** 84 ALA 84 1.302 1.228 1.510 1.521 1.441 121.81 116.55 120.53 110.23 110.28 110.39 122.92 +* +* 85 VAL 85 1.305 1.234 1.505 1.551 1.441 121.66 115.88 120.87 109.56 108.34 112.75 123.23 +* * +* 86 THR 86 1.282 1.238 1.532 1.545 1.424 122.68 116.32 120.91 110.49 109.53 109.76 122.74 *** +* * *** 87 THR 87 1.304 1.239 1.525 1.544 1.431 121.67 116.77 120.52 109.74 108.30 110.28 122.70 +* * * +* 88 MET 88 1.304 1.235 1.517 1.526 1.442 121.29 115.97 120.67 112.32 110.67 109.89 123.35 +* * +* 89 HIS 89 1.320 1.233 1.512 1.537 1.442 122.44 115.56 121.05 109.84 109.78 109.93 123.39 90 VAL 90 1.285 1.234 1.504 1.551 1.437 122.40 114.97 121.18 110.20 109.05 111.18 123.82 *** * * *** 91 ILE 91 1.283 1.241 1.502 1.537 1.422 123.36 114.75 121.39 110.74 109.38 109.59 123.83 *** * +* * *** 92 ILE 92 1.302 1.243 1.523 1.581 1.424 122.12 115.36 121.45 110.62 111.07 113.18 123.17 +* +* +* +* 93 GLN 93 1.299 1.232 1.500 1.527 1.420 121.96 115.31 120.84 111.20 106.56 110.80 123.78 ** * ** +* ** 94 ALA 94 1.287 1.245 1.519 1.521 1.437 122.62 117.15 120.85 110.43 111.38 110.16 121.96 *** * *** 95 PRO 95 1.330 1.236 1.528 1.528 1.435 122.65 116.72 120.88 110.65 110.71 102.59 122.38 ** ** 96 VAL 96 1.299 1.238 1.526 1.548 1.442 121.24 117.23 119.99 110.42 108.28 111.57 122.75 ** * ** 97 THR 97 1.315 1.237 1.529 1.540 1.438 121.11 116.43 120.62 110.90 110.01 111.15 122.93 * * * 98 GLU 98 1.315 1.230 1.514 1.522 1.439 121.89 115.69 120.22 110.59 109.64 109.03 124.08 * * * 99 LYS 99 1.327 1.239 1.548 1.565 1.464 124.36 116.34 120.50 112.90 110.40 111.04 123.08 * +* * * +* Residue-by-residue listing for refined_17 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 GLU 100 1.338 1.232 1.533 1.542 1.469 124.15 115.34 121.34 112.83 111.85 111.96 123.29 * * * 101 LYS 101 1.311 - 1.516 1.542 1.437 124.25 - - 110.74 107.61 112.86 - * * * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* * +* +* *** +** +* +* ** *** *** * *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 94 1.264 1.339 1.309 .016 *4.6* * C-N (Pro) 1.341 .016 6 1.304 1.350 1.329 .016 ** C-O C-O 1.231 .020 100 1.209 1.251 1.233 .008 * * CA-C CH1E-C (except Gly) 1.525 .021 96 1.483 1.549 1.521 .014 +* * CH2G*-C (Gly) 1.516 .018 5 1.488 1.513 1.505 .010 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.512 1.532 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.531 1.581 1.554 .013 +* CH1E-CH2E (the rest) 1.530 .020 62 1.500 1.568 1.533 .013 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.396 1.489 1.442 .018 *** +* NH1-CH2G* (Gly) 1.451 .016 5 1.416 1.455 1.439 .014 ** N-CH1E (Pro) 1.466 .015 6 1.435 1.466 1.448 .010 ** * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_17 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 89 112.30 119.39 116.09 1.03 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.02 119.29 116.84 1.56 * CH1E-C-N (Pro) 116.9 1.5 6 114.54 117.58 116.26 .94 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.11 124.86 123.06 .63 * * O-C-N (Pro) 122.0 1.4 6 122.38 124.03 122.92 .58 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.55 127.02 122.40 1.23 +* +** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.19 124.25 121.61 1.41 ** C-N-CH1E (Pro) 122.6 5.0 6 120.81 122.89 122.05 .76 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.18 122.74 120.80 .68 +* * CH2G*-C-O (Gly) 120.8 2.1 5 119.40 121.52 120.54 .79 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.23 111.65 110.70 .42 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.21 111.75 110.39 .82 * CH2E-CH1E-C (the rest) 110.1 1.9 62 106.97 114.25 110.47 1.46 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 102.00 114.31 110.06 1.90 *** * NH1-CH2G*-C (Gly) 112.5 2.9 5 105.83 112.39 110.27 2.33 ** N-CH1E-C (Pro) 111.8 2.5 6 108.04 112.25 110.88 1.45 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.75 111.49 110.52 .51 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.09 113.23 111.32 1.18 * * N-CH1E-CH2E (Pro) 103.0 1.1 6 102.59 105.17 103.93 .93 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.72 115.68 110.51 1.73 ** *** ------------------------------------------------------------------------------------------------------------- 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_17 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] 13 14.8% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% 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 3.3 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 55 1.0 .8 .2 .7 Inside f. Overall G-factor 101 .0 -.4 .3 1.2 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 11 6.5 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 28 5.3 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 43 6.6 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 82 7.5 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 23 3.0 20.4 5.0 -3.5 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 8.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for refined_17 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.56 Chi1-chi2 distribution -.17 Chi1 only .05 Chi3 & chi4 .23 Omega .07 ------ -.14 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .38 ------ .17 ===== OVERALL AVERAGE -.04 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.