Residue-by-residue listing for refined_16 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 - - 183.8 - 181.0 - - - - - - 183.6 - 34.3 - 2 ALA 2 b - - - - - - - - - - 176.0 - 32.2 - 3 GLU 3 l - 184.1 - 178.9 - - - - - - 178.3 -1.8 31.1 - 4 VAL 4 A - 185.3 - - - - - - - - 180.4 - 33.4 - 5 HIS 5 b 62.2 - - - - - - - - - 172.6 - 29.2 - * * * 6 ASN 6 S A - 180.7 - - - - - - - - 174.5 -.7 34.4 - +* +* 7 GLN 7 S B 50.1 - - 191.6 - - - - - - 188.6 - 34.3 - * * 8 LEU 8 E B 62.8 - - 169.8 - - - - - - 181.2 -1.3 30.0 - * * 9 GLU 9 E B - - -57.6 179.2 - - - - - - 181.1 -2.6 34.3 - 10 ILE 10 E B - - -60.5 179.0 - - - - - - 175.1 -2.8 34.9 - * * 11 LYS 11 E B 69.4 - - - - - - - - - 186.9 -2.5 29.7 - * * * 12 PHE 12 E B - - -59.2 - - - - - - - 176.8 - 34.0 - 13 ARG 13 E B - 178.1 - - - - - - - - 180.0 -3.5 35.5 - ** ** 14 LEU 14 E B - - -63.5 176.3 - - - - - - 176.6 -3.1 35.5 - * * 15 THR 15 e A - 187.9 - - - - - - - - 179.0 -1.7 34.4 - 16 ASP 16 T A - - -64.4 - - - - - - - 177.4 - 35.4 - 17 GLY 17 t - - - - - - - - - - - 178.6 -2.0 - - 18 SER 18 B - - -55.0 - - - - - - - 180.6 - 35.6 - 19 ASP 19 B B 69.5 - - - - - - - - - 180.1 - 33.2 - 20 ILE 20 B - - -57.3 177.3 - - - - - - 180.4 -2.8 36.0 - Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 GLY 21 - - - - - - - - - - - 185.7 - - - 22 PRO 22 - - - - - -65.2 - - - - - 179.6 - 37.3 - 23 LYS 23 E B - 191.3 - - - - - - - - 184.6 -2.4 35.7 - 24 ALA 24 E B - - - - - - - - - - 179.9 - 32.5 - 25 PHE 25 E B - - -59.9 - - - - - - - 176.1 -3.7 36.1 - ** ** 26 PRO 26 t - - - - - -78.2 - - - - - 178.1 - 39.4 - * +* +* 27 ASP 27 T A 62.9 - - - - - - - - - 178.7 - 32.8 - 28 ALA 28 T A - - - - - - - - - - 178.9 - 33.4 - 29 THR 29 t B - 196.0 - - - - - - - - 181.5 -2.2 32.4 - 30 THR 30 h B 58.4 - - - - - - - - - 176.1 - 35.1 - 31 VAL 31 H A - 179.6 - - - -59.4 -29.4 - - - 178.6 -2.2 34.4 - 32 SER 32 H A - 180.3 - - - -60.2 -49.6 - - - 181.2 -.9 34.2 - +* +* 33 ALA 33 H A - - - - - -72.7 -26.9 - - - 176.0 - 33.2 - * * 34 LEU 34 H A - 174.8 - - - -62.6 -47.3 - - - 174.8 -1.8 35.6 - 35 LYS 35 H A - - -92.5 - - -68.8 -35.3 - - - 177.0 -2.5 31.2 - +* +* 36 GLU 36 H A - - -67.7 - - -57.4 -36.8 - - - 179.5 -2.1 34.3 - 37 THR 37 H A - - -54.8 - - -64.4 -41.9 - - - 179.0 -1.8 34.2 - 38 VAL 38 H A - 183.3 - - - -61.9 -39.8 - - - 181.6 -1.1 35.3 - * * 39 ILE 39 H A - - -54.6 173.5 - -72.1 -49.3 - - - 184.4 -1.9 35.0 - 40 SER 40 H A 53.5 - - - - -71.1 -38.4 - - - 180.6 -3.2 32.5 - +* +* 41 GLU 41 h A - - -69.5 - - - - - - - 178.8 -2.7 33.1 - 42 TRP 42 t B - 193.6 - - - - - - - - 178.8 -.6 36.3 - +* +* 43 PRO 43 t - - - - - -49.7 - - - - - 181.6 - 38.5 - * * * 44 ARG 44 T A 61.7 - - 177.7 - - - - - - 179.5 - 35.2 - 45 GLU 45 T A - 185.2 - 185.1 - - - - - - 181.9 - 35.8 - 46 LYS 46 T a - 201.6 - 183.4 - - - - - - 177.1 -1.4 35.3 - * * 47 GLU 47 t b - - -68.3 - - - - - - - 173.2 -1.8 34.8 - * * 48 ASN 48 S A - 184.4 - - - - - - - - 182.4 - 34.1 - 49 GLY 49 - - - - - - - - - - - 183.8 - - - 50 PRO 50 S - - - - - -91.4 - - - - - 183.9 - 39.8 - ** +* ** 51 LYS 51 XX - - -77.6 - - - - - - - 182.8 -1.0 23.7 - **** * +** **** 52 THR 52 t B 54.7 - - - - - - - - - 187.8 - 34.4 - * * 53 VAL 53 T A 68.2 - - - - - - - - - 180.6 - 33.4 - 54 LYS 54 T A - - -61.2 176.7 - - - - - - 184.5 - 35.0 - 55 GLU 55 T A - - -52.6 - - - - - - - 185.2 -1.2 36.8 - * * 56 VAL 56 t B - 172.8 - - - - - - - - 180.4 -3.2 33.5 - +* +* 57 LYS 57 E B - - -74.3 - - - - - - - 179.5 -1.8 33.7 - 58 LEU 58 E B - 194.1 - - - - - - - - 184.2 - 35.7 - 59 ILE 59 E B - - -63.4 179.2 - - - - - - 177.8 -3.3 33.8 - +* +* 60 SER 60 E B - 186.8 - - - - - - - - 181.8 -2.8 34.3 - Residue-by-residue listing for refined_16 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 ALA 61 T l - - - - - - - - - - 181.1 - 33.0 - 62 GLY 62 T - - - - - - - - - - - 182.8 - - - 63 LYS 63 E B - 183.3 - 183.0 - - - - - - 176.5 -2.0 35.4 - 64 VAL 64 E B 59.1 - - - - - - - - - 179.4 -.5 33.0 - ** ** 65 LEU 65 e B - - -80.5 - - - - - - - 177.7 -3.4 33.6 - +* +* 66 GLU 66 t B - 190.8 - - - - - - - - 189.6 - 33.7 - +* +* 67 ASN 67 T A - - -51.7 - - - - - - - 185.3 -.6 34.5 - * +* +* 68 SER 68 T A - - -48.1 - - - - - - - 183.6 - 34.9 - * * 69 LYS 69 t B - - -55.4 175.9 - - - - - - 173.7 -2.3 34.9 - * * 70 THR 70 h B 55.5 - - - - - - - - - 176.7 - 35.6 - 71 VAL 71 H A - 180.6 - - - -60.1 -41.5 - - - 179.1 -2.4 33.8 - 72 LYS 72 H A - 186.3 - - - -67.3 -42.7 - - - 180.6 -3.0 33.6 - * * 73 ASP 73 H A - 181.4 - - - -66.8 -27.5 - - - 179.5 - 33.2 - * * 74 TYR 74 H A - 177.8 - - - -82.7 -28.5 - - - 183.8 -1.9 34.8 - * * 75 ARG 75 h B - 194.8 - - - - - - - - 174.2 -1.5 36.7 - * * 76 SER 76 B - - -59.1 - - - - - - - 185.3 -.8 34.8 - +* +* 77 PRO 77 S - - - - - -48.0 - - - - - 180.4 - 36.8 - +* +* 78 VAL 78 S a 64.3 - - - - - - - - - 180.9 - 34.2 - 79 SER 79 b - - -59.1 - - - - - - - 177.0 - 34.6 - 80 ASN 80 B - 177.8 - - - - - - - - 179.8 - 33.3 - 81 LEU 81 B - 179.4 - - - - - - - - 178.9 -.8 35.3 - +* +* 82 ALA 82 S B - - - - - - - - - - 181.2 - 33.8 - 83 GLY 83 S - - - - - - - - - - - 178.9 -.7 - - +* +* 84 ALA 84 e B - - - - - - - - - - 178.3 - 34.2 - 85 VAL 85 E B - 182.2 - - - - - - - - 182.6 - 33.5 - 86 THR 86 E B - - -53.3 - - - - - - - 176.8 -2.6 35.1 - 87 THR 87 E B - - -61.6 - - - - - - - 179.2 - 34.7 - 88 MET 88 E B - - -66.9 - - - - - - - 179.1 -2.6 34.1 - 89 HIS 89 E B - - -60.0 - - - - - - - 182.9 -2.4 33.6 - 90 VAL 90 E B - 185.6 - - - - - - - - 181.5 -3.4 34.8 - +* +* 91 ILE 91 E B - - -74.2 - - - - - - - 184.1 -2.9 34.0 - * * 92 ILE 92 B - - -50.2 - - - - - - - 178.9 -.7 35.6 - * +* +* 93 GLN 93 B - - -65.9 - - - - - - - 182.0 -1.0 33.5 - * * 94 ALA 94 B - - - - - - - - - - 172.8 -.9 35.0 - * +* +* 95 PRO 95 - - - - - -70.7 - - - - - 179.6 - 39.0 - * * 96 VAL 96 S b - 179.5 - - - - - - - - 179.9 - 32.6 - 97 THR 97 b - 188.0 - - - - - - - - 179.3 -1.5 35.3 - Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 GLU 98 XX - - -64.0 - - - - - - - 183.9 - 30.6 - **** **** 99 LYS 99 B - 180.8 - 181.3 - - - - - - 178.1 - 34.2 - 100 GLU 100 B 61.1 - - 173.0 - - - - - - 175.6 - 34.2 - 101 LYS 101 - - 183.1 - 179.4 - - - - - - - - 34.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * +* ** * * +* ** +** **** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.9 184.6 -62.6 179.0 -67.2 -66.2 -38.2 - - - 180.1 -2.0 34.3 Standard deviations: 5.8 6.4 9.5 4.8 16.7 6.9 7.9 - - - 3.4 .9 2.1 Numbers of values: 15 34 33 19 6 14 14 0 0 0 100 54 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_16 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 - 1.235 1.527 1.539 1.458 - 116.23 120.90 111.28 108.58 109.95 122.84 2 ALA 2 1.324 1.238 1.520 1.524 1.450 122.12 114.39 120.81 111.26 112.46 111.49 124.67 * * 3 GLU 3 1.330 1.238 1.536 1.528 1.469 125.79 115.82 121.64 111.58 114.30 111.74 122.55 ** * ** 4 VAL 4 1.298 1.230 1.540 1.570 1.449 121.77 115.08 122.76 111.90 108.28 111.10 122.09 ** * * * * ** 5 HIS 5 1.306 1.225 1.526 1.564 1.443 120.65 115.41 121.48 112.87 112.63 114.07 122.90 +* +* * ** ** 6 ASN 6 1.316 1.231 1.519 1.544 1.469 122.34 113.27 122.67 110.90 106.39 110.88 124.05 * * +* +* 7 GLN 7 1.319 1.240 1.522 1.533 1.428 124.51 119.20 119.13 113.40 107.31 108.40 121.64 +* +* +* +* * * +* 8 LEU 8 1.303 1.220 1.505 1.544 1.446 117.89 115.42 121.44 111.54 113.05 114.09 123.14 +* ** ** ** 9 GLU 9 1.302 1.227 1.505 1.520 1.429 122.22 115.80 121.31 110.19 109.25 110.93 122.89 +* +* +* 10 ILE 10 1.275 1.237 1.505 1.559 1.427 121.95 116.63 120.36 109.40 109.46 111.24 122.98 +*** +* +*** 11 LYS 11 1.305 1.251 1.519 1.559 1.421 120.18 116.59 120.48 114.87 109.35 113.06 122.92 +* * * +* +** +* +** Residue-by-residue listing for refined_16 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 1.304 1.218 1.504 1.526 1.448 121.24 115.64 120.99 109.99 112.57 110.54 123.37 +* +* 13 ARG 13 1.297 1.225 1.518 1.535 1.436 122.65 116.68 120.35 109.87 108.54 109.80 122.96 ** * ** 14 LEU 14 1.305 1.239 1.507 1.532 1.445 121.83 115.48 120.99 108.00 110.46 111.08 123.51 +* * +* 15 THR 15 1.310 1.225 1.551 1.552 1.455 123.69 114.86 121.92 111.11 110.08 109.53 123.16 * * * * * 16 ASP 16 1.322 1.230 1.527 1.538 1.465 123.68 116.67 120.87 108.65 111.00 110.23 122.45 * * 17 GLY 17 1.321 1.220 1.504 - 1.450 120.36 116.27 121.00 - 113.03 - 122.73 18 SER 18 1.294 1.228 1.510 1.523 1.434 121.95 117.73 119.81 110.52 108.07 109.04 122.44 +** * * +** 19 ASP 19 1.299 1.232 1.511 1.535 1.427 120.65 115.44 121.01 110.83 110.37 111.69 123.55 ** +* ** 20 ILE 20 1.294 1.221 1.518 1.564 1.444 123.97 117.30 119.00 109.15 107.40 110.28 123.66 ** * * * ** 21 GLY 21 1.334 1.239 1.530 - 1.461 122.00 117.76 119.97 - 112.74 - 122.25 22 PRO 22 1.342 1.246 1.531 1.529 1.467 123.27 114.43 121.93 111.01 115.00 103.96 123.64 +* * * +* 23 LYS 23 1.306 1.220 1.531 1.558 1.439 124.39 119.17 118.94 113.40 104.99 106.94 121.86 +* * * * * +* ** ** ** 24 ALA 24 1.311 1.224 1.518 1.529 1.464 119.49 115.90 121.10 111.11 111.57 111.58 123.00 * * * 25 PHE 25 1.305 1.223 1.498 1.531 1.444 123.65 118.12 120.24 107.70 108.12 111.05 121.59 +* * * * * +* 26 PRO 26 1.303 1.219 1.516 1.538 1.442 121.89 117.07 120.35 109.59 110.02 103.84 122.58 ** +* ** 27 ASP 27 1.302 1.235 1.536 1.546 1.468 121.54 116.00 121.11 111.25 110.85 111.37 122.86 +* +* 28 ALA 28 1.318 1.238 1.547 1.518 1.447 122.02 118.18 119.80 110.57 112.80 110.39 122.02 * * 29 THR 29 1.338 1.247 1.549 1.586 1.464 119.71 116.62 120.72 111.13 109.19 113.08 122.62 * +* * +* 30 THR 30 1.311 1.243 1.527 1.551 1.448 121.88 116.35 120.69 108.70 110.77 110.96 122.95 * * 31 VAL 31 1.330 1.236 1.539 1.555 1.471 122.22 116.04 121.02 109.65 110.23 111.02 122.91 32 SER 32 1.325 1.235 1.539 1.538 1.443 121.98 116.67 120.40 110.96 110.24 109.90 122.82 33 ALA 33 1.339 1.244 1.525 1.514 1.464 121.84 115.52 121.04 110.98 110.95 110.73 123.43 34 LEU 34 1.321 1.232 1.542 1.531 1.416 123.55 115.97 121.30 112.44 108.61 106.97 122.69 ** * * ** ** 35 LYS 35 1.323 1.234 1.521 1.524 1.450 121.81 117.16 119.53 111.66 112.95 112.29 123.31 * * 36 GLU 36 1.337 1.224 1.514 1.533 1.467 122.20 115.94 120.82 109.32 110.39 111.30 123.22 37 THR 37 1.316 1.224 1.541 1.538 1.443 122.33 116.39 120.59 110.59 110.52 110.24 122.96 38 VAL 38 1.331 1.215 1.532 1.561 1.471 122.02 115.27 121.39 108.22 109.82 111.34 123.34 39 ILE 39 1.313 1.231 1.544 1.553 1.454 123.11 115.99 121.00 110.20 111.06 109.37 122.99 * * * 40 SER 40 1.319 1.228 1.537 1.536 1.457 122.61 117.39 120.45 111.73 113.67 110.20 122.15 41 GLU 41 1.320 1.232 1.521 1.515 1.441 121.37 116.39 120.62 111.13 112.67 110.33 122.98 42 TRP 42 1.306 1.240 1.511 1.522 1.444 121.82 118.41 119.10 109.51 107.72 108.94 122.46 +* * * +* 43 PRO 43 1.346 1.232 1.533 1.530 1.463 122.59 115.55 120.84 110.48 111.84 103.54 123.60 * * Residue-by-residue listing for refined_16 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 44 ARG 44 1.327 1.230 1.526 1.535 1.467 123.93 115.48 121.19 109.21 110.52 110.10 123.32 * * 45 GLU 45 1.322 1.232 1.532 1.534 1.442 123.04 115.68 121.29 110.32 109.08 108.58 123.02 * * 46 LYS 46 1.319 1.233 1.506 1.539 1.433 121.85 113.22 122.36 110.16 107.87 110.11 124.37 * * * * 47 GLU 47 1.265 1.217 1.514 1.553 1.414 125.67 116.02 121.07 107.49 108.06 113.67 122.90 *4.6* * ** ** * * +* *4.6* 48 ASN 48 1.305 1.228 1.530 1.542 1.450 122.34 112.57 123.33 112.04 107.11 109.97 124.09 +* +* * * * +* 49 GLY 49 1.289 1.232 1.498 - 1.416 125.30 119.67 119.23 - 107.67 - 121.10 +** * ** +** +* +* * +** 50 PRO 50 1.311 1.221 1.505 1.512 1.447 122.23 114.80 121.09 111.65 109.96 100.71 124.07 +* * * ** * ** 51 LYS 51 1.318 1.258 1.483 1.547 1.378 124.91 111.32 123.72 116.08 113.52 116.95 124.93 * ** **** +* ** +* *** +*** * **** 52 THR 52 1.240 1.238 1.554 1.535 1.437 125.31 116.12 120.59 110.98 112.20 108.95 123.24 *6.4* * * ** +* *6.4* 53 VAL 53 1.347 1.233 1.537 1.567 1.487 124.47 116.25 120.91 109.71 113.11 111.40 122.84 * +* +* +* 54 LYS 54 1.309 1.230 1.525 1.522 1.448 121.91 115.56 121.18 109.89 110.94 109.50 123.24 * * 55 GLU 55 1.306 1.227 1.526 1.526 1.449 122.28 115.13 121.70 107.85 110.18 109.15 123.16 +* * +* 56 VAL 56 1.312 1.232 1.504 1.541 1.443 122.64 114.47 121.25 110.45 112.80 110.79 124.26 * * 57 LYS 57 1.304 1.241 1.514 1.548 1.431 123.50 115.52 121.04 110.83 110.47 111.03 123.43 +* * +* 58 LEU 58 1.294 1.227 1.534 1.559 1.426 122.76 117.05 120.42 112.26 106.03 108.05 122.50 +** * +* * +* * +** 59 ILE 59 1.308 1.238 1.523 1.564 1.452 121.93 115.43 121.43 110.86 111.58 110.51 123.13 * * 60 SER 60 1.306 1.235 1.516 1.530 1.429 122.58 116.55 119.77 110.85 107.81 110.74 123.59 +* +* * +* 61 ALA 61 1.341 1.243 1.528 1.527 1.482 123.52 115.10 121.52 111.03 110.51 111.17 123.34 * * * 62 GLY 62 1.321 1.230 1.505 - 1.438 121.61 116.39 120.82 - 112.25 - 122.78 63 LYS 63 1.309 1.239 1.500 1.531 1.424 121.44 116.01 120.42 109.67 109.26 110.00 123.54 * * +* +* 64 VAL 64 1.301 1.238 1.532 1.566 1.434 121.76 115.79 121.15 111.30 109.78 111.81 122.99 +* * * +* 65 LEU 65 1.299 1.243 1.506 1.531 1.430 122.79 115.10 121.07 110.89 111.45 110.70 123.82 ** * ** 66 GLU 66 1.308 1.235 1.523 1.553 1.434 122.19 114.80 120.82 113.74 106.31 109.42 124.37 * * * +* +* +* 67 ASN 67 1.319 1.242 1.533 1.543 1.479 125.40 116.72 120.31 108.82 114.08 110.38 122.95 * ** * ** 68 SER 68 1.318 1.245 1.533 1.523 1.453 122.19 116.74 120.61 109.61 112.30 109.46 122.65 69 LYS 69 1.310 1.243 1.516 1.533 1.435 121.08 115.41 121.35 109.75 110.62 110.18 123.21 * * * 70 THR 70 1.294 1.248 1.509 1.547 1.413 122.25 117.68 119.39 109.47 106.58 110.82 122.92 +** ** +* +** 71 VAL 71 1.312 1.224 1.536 1.548 1.449 120.41 115.69 121.01 109.97 109.38 111.93 123.25 * * Residue-by-residue listing for refined_16 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 1.214 1.529 1.544 1.449 122.94 117.47 120.07 112.26 110.91 109.35 122.44 * * 73 ASP 73 1.332 1.233 1.520 1.539 1.483 121.20 115.75 121.41 110.01 110.90 111.90 122.84 * * 74 TYR 74 1.304 1.237 1.524 1.534 1.430 121.85 115.65 121.11 110.96 110.21 109.31 123.23 +* * +* 75 ARG 75 1.306 1.233 1.527 1.511 1.411 122.59 116.30 120.89 109.17 110.40 107.99 122.78 +* ** * ** 76 SER 76 1.297 1.241 1.529 1.521 1.418 121.31 117.38 119.81 111.42 107.57 109.47 122.80 ** ** * ** 77 PRO 77 1.350 1.241 1.520 1.524 1.468 123.84 114.58 121.82 111.07 114.51 104.80 123.59 +* * +* * +* 78 VAL 78 1.307 1.241 1.540 1.559 1.448 122.93 115.88 121.67 110.47 110.60 110.48 122.45 +* +* 79 SER 79 1.306 1.242 1.529 1.541 1.445 122.34 116.32 120.78 110.17 110.60 110.13 122.85 +* +* 80 ASN 80 1.311 1.241 1.513 1.538 1.450 121.67 115.57 121.31 110.53 109.87 111.89 123.10 * * 81 LEU 81 1.297 1.233 1.505 1.516 1.411 122.95 115.36 120.73 110.65 108.94 109.11 123.91 ** ** ** 82 ALA 82 1.282 1.238 1.503 1.518 1.415 123.74 115.57 120.97 111.29 107.77 111.16 123.35 *** * ** * * *** 83 GLY 83 1.288 1.240 1.505 - 1.426 121.17 116.14 121.02 - 110.85 - 122.83 +** +* +** 84 ALA 84 1.310 1.223 1.514 1.522 1.447 121.29 117.25 120.20 110.57 109.44 110.57 122.53 * * 85 VAL 85 1.309 1.241 1.512 1.548 1.445 120.50 115.79 120.97 109.79 109.15 112.76 123.25 * * 86 THR 86 1.285 1.237 1.535 1.549 1.431 121.97 116.30 121.02 109.86 110.14 110.01 122.66 *** * *** 87 THR 87 1.301 1.233 1.528 1.549 1.427 121.70 116.31 120.91 109.93 109.06 110.89 122.78 +* +* +* 88 MET 88 1.305 1.227 1.497 1.526 1.444 121.21 116.70 120.34 109.81 109.52 111.52 122.95 +* * +* 89 HIS 89 1.303 1.228 1.501 1.542 1.440 121.01 116.31 120.63 111.05 108.38 111.54 123.05 +* * * +* 90 VAL 90 1.295 1.242 1.499 1.556 1.433 121.29 114.65 121.68 109.90 108.97 110.95 123.66 ** * * ** 91 ILE 91 1.290 1.234 1.504 1.570 1.412 122.18 114.84 121.68 111.88 108.85 110.60 123.47 +** * ** * +** 92 ILE 92 1.299 1.235 1.515 1.563 1.426 122.19 116.72 120.42 109.16 108.21 110.76 122.75 ** +* * ** 93 GLN 93 1.307 1.237 1.502 1.529 1.436 121.10 114.75 121.60 111.59 109.58 110.69 123.64 +* * * +* 94 ALA 94 1.289 1.239 1.512 1.520 1.428 122.56 117.71 120.28 110.03 110.79 109.58 121.98 +** +* +** 95 PRO 95 1.328 1.240 1.523 1.538 1.451 122.06 116.80 120.12 109.94 109.23 104.06 123.06 * * * 96 VAL 96 1.313 1.247 1.534 1.547 1.448 121.71 114.77 121.41 111.21 110.98 111.76 123.65 * * 97 THR 97 1.315 1.253 1.538 1.563 1.426 124.68 116.65 119.53 110.26 107.10 110.37 123.81 * +* +* * +* 98 GLU 98 1.333 1.238 1.528 1.534 1.469 124.17 115.76 121.60 112.14 113.44 112.25 122.63 * * * * Residue-by-residue listing for refined_16 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 LYS 99 1.310 1.233 1.510 1.535 1.412 121.89 116.34 120.50 110.38 110.36 110.89 123.15 * ** ** 100 GLU 100 1.305 1.253 1.527 1.536 1.439 121.34 116.08 121.01 109.76 110.08 111.23 122.90 +* * +* 101 LYS 101 1.305 - 1.514 1.538 1.429 121.70 - - 111.09 107.78 110.97 - +* +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *6.4* * ** +* **** +** ** +* *** ** +*** * *6.4* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 1.240 1.347 1.309 .016 *6.4* * * C-N (Pro) 1.341 .016 6 1.303 1.350 1.330 .018 ** C-O C-O 1.231 .020 100 1.214 1.258 1.234 .009 * CA-C CH1E-C (except Gly) 1.525 .021 96 1.483 1.554 1.522 .014 ** * CH2G*-C (Gly) 1.516 .018 5 1.498 1.530 1.508 .011 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.514 1.529 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.535 1.586 1.556 .011 +* CH1E-CH2E (the rest) 1.530 .020 62 1.511 1.564 1.535 .011 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.378 1.487 1.442 .019 **** +* NH1-CH2G* (Gly) 1.451 .016 5 1.416 1.461 1.438 .016 ** N-CH1E (Pro) 1.466 .015 6 1.442 1.468 1.456 .010 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 89 111.32 119.20 116.01 1.22 ** +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.14 119.67 117.25 1.35 +* CH1E-C-N (Pro) 116.9 1.5 6 114.43 117.07 115.54 1.05 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.10 124.93 123.03 .63 * * O-C-N (Pro) 122.0 1.4 6 122.58 124.07 123.42 .48 * * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.89 125.79 122.32 1.35 ** ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.36 125.30 122.09 1.69 +** C-N-CH1E (Pro) 122.6 5.0 6 121.89 123.84 122.65 .70 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 118.94 123.72 120.90 .82 * +* CH2G*-C-O (Gly) 120.8 2.1 5 119.23 121.02 120.41 .71 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 110.03 111.29 110.86 .40 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 108.22 111.90 110.20 .91 * CH2E-CH1E-C (the rest) 110.1 1.9 62 107.49 116.08 110.77 1.58 * *** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.99 114.30 109.98 1.96 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 107.67 113.03 111.31 1.97 +* N-CH1E-C (Pro) 111.8 2.5 6 109.23 115.00 111.76 2.26 * * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.58 111.58 110.83 .62 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 108.95 113.08 110.88 .92 +* N-CH1E-CH2E (Pro) 103.0 1.1 6 100.71 104.80 103.49 1.30 ** +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 106.94 116.95 110.55 1.72 ** +*** ------------------------------------------------------------------------------------------------------------- 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_16 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] 76 86.4% Residues in additional allowed regions [a,b,l,p] 10 11.4% Residues in generously allowed regions [~a,~b,~l,~p] 0 .0% Residues in disallowed regions [XX] 2 2.3% ---- ------ 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 86.4 83.8 10.0 .3 Inside b. Omega angle st dev 100 3.4 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 2.1 3.1 1.6 -.7 Inside e. H-bond energy st dev 54 .9 .8 .2 .4 Inside f. Overall G-factor 101 -.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 15 5.8 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 34 6.4 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 33 9.5 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 82 8.1 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 19 4.8 20.4 5.0 -3.1 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% 86.4 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 10.4 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 3 Residue-by-residue listing for refined_16 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.54 Chi1-chi2 distribution -.34 Chi1 only .13 Chi3 & chi4 .26 Omega .01 ------ -.17 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .33 ------ .14 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.