Residue-by-residue listing for refined_11 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -64.9 180.3 - - - - - - 176.3 - 34.9 - 2 THR 2 B - - -54.0 - - - - - - - 179.3 - 35.1 - 3 GLU 3 e B - 184.1 - - - - - - - - 185.5 -.8 34.7 - +* +* 4 VAL 4 E B - - -66.3 - - - - - - - 178.6 - 32.6 - 5 TYR 5 E B 59.0 - - - - - - - - - 170.1 -3.0 34.2 - +* * +* 6 ASP 6 E B - - -71.2 - - - - - - - 180.4 - 33.3 - 7 LEU 7 E B - - -67.7 182.7 - - - - - - 168.0 -2.2 36.4 - ** ** 8 GLU 8 E B - 179.8 - 177.7 - - - - - - 184.9 -1.6 34.2 - 9 ILE 9 E B - - -57.4 - - - - - - - 176.6 -3.5 34.0 - +* +* 10 THR 10 E B 52.7 - - - - - - - - - 176.9 -2.9 34.3 - * * 11 THR 11 E B - - -43.3 - - - - - - - 178.1 - 35.7 - +* +* 12 ASN 12 e A 63.7 - - - - - - - - - 176.8 -.9 33.4 - +* +* 13 ALA 13 S A - - - - - - - - - - 178.6 - 34.3 - 14 THR 14 B 52.1 - - - - - - - - - 178.9 - 34.5 - 15 ASP 15 S A - 179.2 - - - - - - - - 180.8 - 33.5 - 16 PHE 16 S B - 179.9 - - - - - - - - 174.1 - 34.8 - * * 17 PRO 17 - - - - - -68.4 - - - - - 185.1 - 38.8 - * * 18 MET 18 E B - 177.1 - - - - - - - - 178.6 -2.2 35.1 - 19 GLU 19 E B 65.3 - - - - - - - - - 178.7 - 31.9 - Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 LYS 20 E B - 183.2 - 170.2 - - - - - - 180.9 -1.6 32.6 - 21 LYS 21 E B - 180.3 - 179.1 - - - - - - 179.2 - 35.1 - 22 TYR 22 E B - - -63.9 - - - - - - - 178.2 -2.4 34.4 - 23 PRO 23 E - - - - - -77.1 - - - - - 179.5 - 38.5 - * * * 24 ALA 24 e A - - - - - - - - - - 181.8 -2.0 32.8 - 25 GLY 25 T - - - - - - - - - - - 179.7 -.6 - - +* +* 26 MET 26 t B - 182.6 - 181.1 - - - - - - 177.1 -.8 35.2 - +* +* 27 SER 27 h B 55.2 - - - - - - - - - 175.4 - 35.6 - 28 LEU 28 H A - 182.9 - - - -64.7 -32.8 - - - 181.7 -.9 35.4 - +* +* 29 ASN 29 H A - - -67.5 - - -61.3 -30.6 - - - 175.1 - 30.8 - 30 ASP 30 H A - 185.7 - - - -69.0 -45.0 - - - 180.5 -.5 34.9 - ** ** 31 LEU 31 H A - 191.5 - - - -65.9 -40.9 - - - 173.7 -1.3 35.3 - * * * 32 LYS 32 H A - - -73.1 - - -55.1 -49.1 - - - 182.7 -3.4 36.2 - +* +* 33 LYS 33 H A - 204.2 - - - -60.1 -34.8 - - - 176.0 -2.2 35.5 - * * 34 LYS 34 H A - - -90.6 - - -68.9 -43.2 - - - 175.2 -1.5 34.9 - +* +* 35 LEU 35 H A - - -68.8 180.2 - -62.6 -47.4 - - - 177.2 -2.5 35.7 - 36 GLU 36 H A - - -72.8 175.7 - -56.7 -35.6 - - - 179.4 -3.8 35.2 - ** ** 37 LEU 37 H A - 181.9 - - - -73.2 -37.6 - - - 181.9 -1.5 34.6 - 38 VAL 38 H A - 179.3 - - - -80.1 -41.5 - - - 182.9 -1.7 33.4 - * * 39 VAL 39 H A - 184.8 - - - -90.5 -27.3 - - - 179.8 -3.4 32.1 - ** * +* ** 40 GLY 40 h - - - - - - - - - - - 181.2 -1.5 - - 41 THR 41 B - - -46.6 - - - - - - - 176.4 - 35.3 - * * 42 THR 42 b 52.2 - - - - - - - - - 184.1 - 35.4 - 43 VAL 43 S A - 177.5 - - - - - - - - 185.1 - 33.6 - 44 ASP 44 S A - 179.4 - - - - - - - - 179.1 - 32.3 - 45 SER 45 e A - - -58.5 - - - - - - - 175.7 - 33.9 - 46 MET 46 E B - 196.0 - 176.4 - - - - - - 184.6 - 35.2 - 47 ARG 47 E B - 219.7 - - - - - - - - 184.5 -2.9 33.2 - ** * ** 48 ILE 48 E B - - -51.1 - - - - - - - 179.4 -.7 35.3 - * +* +* 49 GLN 49 E B - - -63.3 180.1 - - - - - - 180.4 -3.8 33.9 - ** ** 50 LEU 50 E B - 180.9 - 164.4 - - - - - - 174.3 -2.1 32.5 - 51 PHE 51 E B - - -56.5 - - - - - - - 185.9 -1.8 34.4 - * * 52 ASP 52 e b - 194.4 - - - - - - - - 175.9 -1.5 35.9 - 53 GLY 53 S - - - - - - - - - - - 176.5 - - - 54 ASP 54 S B - 184.4 - - - - - - - - 184.1 - 35.3 - 55 ASP 55 S A - 187.0 - - - - - - - - 180.0 - 34.6 - 56 GLN 56 e B - - -65.8 182.9 - - - - - - 181.5 - 31.9 - 57 LEU 57 E B - 181.1 - - - - - - - - 176.6 - 35.9 - 58 LYS 58 E A - - -73.0 - - - - - - - 179.8 -2.7 33.2 - Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 GLY 59 E - - - - - - - - - - - 183.0 -1.1 - - * * 60 GLU 60 E B - 183.3 - 179.9 - - - - - - 178.9 - 35.1 - 61 LEU 61 E b 59.7 - - 175.8 - - - - - - 191.1 -2.0 31.2 - +* +* 62 THR 62 ~l - 197.0 - - - - - - - - 177.3 - 31.0 - ** ** 63 ASP 63 a - - -57.1 - - - - - - - 178.6 - 35.9 - 64 GLY 64 - - - - - - - - - - - 177.1 - - - 65 ALA 65 S A - - - - - - - - - - 179.5 - 34.3 - 66 LYS 66 S B 50.3 - - 190.3 - - - - - - 186.6 - 34.7 - * * 67 SER 67 h B 55.5 - - - - - - - - - 177.2 - 34.1 - 68 LEU 68 H A - - -68.0 163.3 - -69.5 -27.7 - - - 179.8 -2.2 35.1 - * * 69 LYS 69 H A - 194.0 - - - -72.2 -40.2 - - - 180.2 -2.3 35.2 - 70 ASP 70 H A - 193.7 - - - -73.0 -29.3 - - - 176.3 - 35.0 - 71 LEU 71 H A - - -71.8 172.1 - -73.8 -14.2 - - - 179.1 -1.8 34.7 - ** ** 72 GLY 72 h - - - - - - - - - - - 178.6 -.6 - - +* +* 73 VAL 73 t b - 182.4 - - - - - - - - 181.1 -3.2 33.6 - +* +* 74 ARG 74 t b - - -55.1 176.5 - - - - - - 177.6 -1.4 36.3 - 75 ASP 75 T B - - -65.6 - - - - - - - 176.8 - 34.2 - 76 GLY 76 T - - - - - - - - - - - 178.6 -1.9 - - 77 TYR 77 E B - - -76.0 - - - - - - - 177.1 -1.1 33.3 - * * 78 ARG 78 E B 63.2 - - 175.8 - - - - - - 180.0 -1.3 33.5 - * * 79 ILE 79 E B - - -63.8 - - - - - - - 182.7 -2.2 32.6 - 80 HIS 80 E B - 174.2 - - - - - - - - 176.4 -2.7 35.0 - 81 ALA 81 E B - - - - - - - - - - 178.8 -2.2 33.9 - 82 VAL 82 E B 58.2 - - - - - - - - - 179.5 -2.7 33.2 - 83 ASP 83 E B - 176.4 - - - - - - - - 177.6 - 34.4 - 84 VAL 84 e A - - -61.5 - - - - - - - 182.3 -2.4 33.7 - 85 THR 85 T A - - -46.8 - - - - - - - 177.0 - 36.7 - * * 86 GLY 86 T - - - - - - - - - - - 183.4 - - - 87 GLY 87 T - - - - - - - - - - - 184.5 - - - 88 ASN 88 t B - - -66.3 - - - - - - - 175.8 -1.1 34.3 - * * 89 GLU 89 a 56.4 - - 183.6 - - - - - - 178.7 -.5 32.5 - ** ** 90 ASP 90 - - 177.9 - - - - - - - - - - 34.3 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** ** +* * ** ** ** ** * ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 57.2 185.5 -63.6 177.4 -72.7 -68.5 -36.1 - - - 179.3 -1.9 34.4 Standard deviations: 4.8 9.4 9.9 6.4 6.1 9.0 9.0 - - - 3.6 .9 1.4 Numbers of values: 13 32 30 20 2 16 16 0 0 0 89 50 81 0 Residue-by-residue listing for refined_11 Page 4 ---------------------------------------- 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_11 Page 5 ---------------------------------------- M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S ..................................... Small molecule data ......................................... <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N --------------------------------------------------------------------------------------------------- Any - 1.231 - - - - - - - - - - ( .020) Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00 ( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40) Except Pro 1.329 - - - - - - - - - - 123.00 ( .014) ( 1.60) Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - - ( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90) Except Gly - - 1.525 - - - - 120.80 - - - - ( .021) ( 1.70) Ala - - - 1.521 - - - - 110.50 - 110.40 - ( .033) ( 1.50) ( 1.50) Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 - ( .027) ( 2.20) ( 1.70) Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - - ( .019) ( 1.80) ( 2.00) ( 2.80) The rest - - - 1.530 - - - - 110.10 - 110.50 - ( .020) ( 1.90) ( 1.70) Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets are standard deviations ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - 1.235 1.503 1.542 1.467 - 116.54 120.48 108.65 109.79 111.43 122.98 * * 2 THR 2 1.306 1.237 1.529 1.544 1.425 121.60 115.76 121.06 109.32 108.60 111.05 123.17 +* +* +* 3 GLU 3 1.295 1.216 1.495 1.512 1.418 123.02 117.38 119.74 111.13 107.53 109.94 122.87 ** * ** * ** 4 VAL 4 1.292 1.235 1.515 1.566 1.441 121.97 114.91 121.28 110.38 111.76 112.62 123.77 +** +** 5 TYR 5 1.296 1.242 1.542 1.557 1.460 123.44 117.02 120.42 110.69 110.89 110.17 122.41 ** * ** 6 ASP 6 1.307 1.245 1.520 1.528 1.468 120.81 115.92 120.58 108.87 109.82 113.22 123.50 +* +* +* 7 LEU 7 1.314 1.237 1.495 1.513 1.451 123.57 114.89 121.02 105.03 111.98 112.01 124.08 * * * +** +** 8 GLU 8 1.304 1.230 1.515 1.518 1.435 122.74 115.65 121.12 110.97 106.09 111.10 123.17 +* * +* +* 9 ILE 9 1.290 1.244 1.515 1.588 1.445 121.90 115.51 120.74 108.64 109.78 113.31 123.74 +** +* * +** 10 THR 10 1.304 1.237 1.508 1.541 1.433 122.97 115.65 121.56 108.51 110.30 112.48 122.78 +* * +* 11 THR 11 1.279 1.224 1.502 1.552 1.413 123.65 116.97 119.91 108.56 104.16 112.24 123.10 +*** * ** * +** +*** Residue-by-residue listing for refined_11 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 ASN 12 1.264 1.225 1.519 1.526 1.431 121.80 115.49 121.57 111.09 109.60 111.18 122.94 *4.6* * *4.6* 13 ALA 13 1.323 1.231 1.525 1.520 1.443 122.66 115.50 121.21 110.53 110.00 110.15 123.28 14 THR 14 1.309 1.235 1.519 1.549 1.429 123.00 117.22 120.33 110.23 108.88 111.01 122.37 * +* +* 15 ASP 15 1.297 1.232 1.518 1.534 1.455 121.17 115.65 121.44 111.24 110.36 110.58 122.89 ** ** 16 PHE 16 1.310 1.232 1.533 1.537 1.437 122.05 117.37 120.58 110.29 110.79 109.72 122.01 * * * 17 PRO 17 1.338 1.249 1.531 1.534 1.461 122.62 116.08 121.01 109.82 110.27 104.24 122.89 * * 18 MET 18 1.297 1.229 1.507 1.541 1.451 122.22 117.12 120.05 110.14 109.89 109.77 122.82 ** ** 19 GLU 19 1.315 1.237 1.513 1.553 1.432 120.38 116.24 120.84 111.24 110.35 113.16 122.90 * * * +* +* 20 LYS 20 1.303 1.242 1.513 1.534 1.435 121.90 115.91 120.26 112.25 109.99 111.17 123.80 +* * * +* 21 LYS 21 1.308 1.234 1.525 1.532 1.434 123.02 116.38 120.57 110.87 109.86 108.90 123.03 +* * +* 22 TYR 22 1.316 1.235 1.533 1.538 1.460 122.51 118.58 119.81 109.14 109.94 111.41 121.61 * * 23 PRO 23 1.356 1.237 1.531 1.537 1.459 122.35 116.06 120.87 109.51 112.71 104.58 123.06 * * 24 ALA 24 1.323 1.232 1.528 1.518 1.467 122.01 115.75 121.31 111.23 112.34 110.67 122.92 25 GLY 25 1.300 1.232 1.516 - 1.458 121.15 116.03 120.79 - 112.67 - 123.18 ** ** 26 MET 26 1.313 1.242 1.541 1.536 1.450 122.44 116.64 120.70 110.94 110.28 108.49 122.64 * * * 27 SER 27 1.318 1.241 1.494 1.523 1.432 122.24 115.83 121.07 109.12 109.66 110.06 123.10 * * * 28 LEU 28 1.306 1.186 1.500 1.492 1.435 120.90 115.89 120.46 109.16 110.00 109.81 123.64 +* ** * +* * ** 29 ASN 29 1.305 1.236 1.510 1.525 1.488 122.49 117.27 120.01 112.42 113.05 111.83 122.71 +* +* * +* 30 ASP 30 1.326 1.221 1.527 1.533 1.464 120.57 114.73 121.62 109.42 108.43 110.81 123.57 31 LEU 31 1.320 1.224 1.536 1.558 1.472 123.96 115.26 121.17 112.46 108.52 107.37 123.58 * * * +* +* 32 LYS 32 1.314 1.179 1.488 1.523 1.464 123.96 116.99 119.58 107.41 110.39 110.45 123.43 * +** +* * * +** 33 LYS 33 1.323 1.225 1.539 1.545 1.452 122.50 115.46 121.28 110.41 109.58 108.84 123.26 34 LYS 34 1.316 1.230 1.541 1.529 1.421 123.72 116.21 120.87 112.57 110.20 107.34 122.89 +* * * +* +* 35 LEU 35 1.322 1.234 1.528 1.527 1.452 123.57 114.90 121.36 109.86 110.05 108.84 123.73 * * 36 GLU 36 1.316 1.224 1.524 1.536 1.437 125.43 116.22 121.03 111.00 111.15 108.35 122.73 * ** * ** 37 LEU 37 1.306 1.234 1.538 1.532 1.447 122.09 116.61 120.97 110.27 110.99 109.74 122.41 +* +* 38 VAL 38 1.314 1.234 1.535 1.562 1.457 121.32 116.91 120.66 110.07 111.80 111.60 122.42 * * 39 VAL 39 1.313 1.235 1.528 1.560 1.455 120.96 116.89 120.82 111.69 111.96 111.74 122.25 * * * 40 GLY 40 1.312 1.231 1.511 - 1.448 119.98 115.90 120.96 - 112.05 - 123.14 * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 THR 41 1.306 1.239 1.564 1.546 1.450 121.84 115.78 121.05 110.13 111.11 108.91 123.13 +* +* +* +* 42 THR 42 1.318 1.237 1.547 1.534 1.433 124.44 117.82 120.34 110.24 109.40 109.12 121.84 * * +* * +* 43 VAL 43 1.325 1.231 1.522 1.563 1.465 120.64 116.97 120.03 109.27 112.40 112.00 122.95 44 ASP 44 1.304 1.236 1.516 1.528 1.457 120.97 116.51 120.69 111.60 112.01 111.27 122.77 +* +* 45 SER 45 1.318 1.239 1.528 1.496 1.423 121.84 116.43 121.17 111.59 111.96 108.94 122.40 +* +* +* 46 MET 46 1.305 1.234 1.491 1.517 1.436 119.92 116.90 120.42 109.51 106.90 110.99 122.67 +* +* * +* +* 47 ARG 47 1.284 1.231 1.504 1.525 1.426 119.35 116.65 120.40 111.82 108.61 111.17 122.92 *** * +* * *** 48 ILE 48 1.306 1.233 1.526 1.562 1.439 121.22 116.61 120.34 109.03 109.02 110.93 123.05 +* * +* 49 GLN 49 1.308 1.240 1.512 1.520 1.434 121.95 115.98 120.63 110.40 110.42 110.93 123.39 * * * 50 LEU 50 1.310 1.251 1.503 1.568 1.460 121.74 114.87 121.62 111.86 111.23 111.49 123.51 * * +* +* 51 PHE 51 1.291 1.242 1.504 1.525 1.420 121.93 116.53 120.00 111.03 106.03 111.05 123.46 +** * ** +* +** 52 ASP 52 1.296 1.230 1.529 1.543 1.462 122.00 116.71 120.79 110.91 108.88 107.85 122.49 ** +* ** 53 GLY 53 1.304 1.233 1.511 - 1.447 121.04 114.17 121.79 - 109.19 - 124.05 +* * * +* 54 ASP 54 1.312 1.231 1.538 1.534 1.436 124.05 116.93 120.17 110.71 108.05 109.15 122.90 * * * * * 55 ASP 55 1.314 1.240 1.534 1.525 1.456 123.17 116.27 121.06 110.25 112.29 109.27 122.67 * * 56 GLN 56 1.317 1.243 1.527 1.512 1.457 121.38 113.98 122.16 109.90 114.07 112.48 123.85 * * * * 57 LEU 57 1.309 1.244 1.517 1.540 1.444 124.40 116.28 120.75 109.49 110.35 109.08 122.97 * * * 58 LYS 58 1.310 1.237 1.505 1.523 1.450 121.36 115.91 120.84 110.62 110.84 111.41 123.23 * * 59 GLY 59 1.298 1.246 1.487 - 1.425 120.43 116.11 120.29 - 111.33 - 123.59 ** +* +* ** 60 GLU 60 1.298 1.238 1.509 1.526 1.404 122.09 115.52 121.11 111.11 108.63 109.28 123.35 ** +** +** 61 LEU 61 1.282 1.217 1.514 1.571 1.434 122.32 116.96 118.22 113.79 108.51 112.55 124.46 *** ** * +* +* * *** 62 THR 62 1.345 1.231 1.545 1.603 1.510 127.40 115.00 121.46 110.36 109.97 115.28 123.44 * ** +** *** ** *** 63 ASP 63 1.330 1.216 1.535 1.538 1.471 124.06 115.93 121.30 108.63 111.15 109.42 122.75 * * 64 GLY 64 1.334 1.221 1.524 - 1.466 122.56 117.29 120.06 - 114.74 - 122.64 * * 65 ALA 65 1.323 1.226 1.525 1.507 1.473 122.20 113.24 122.63 110.64 109.25 109.87 124.12 * * * 66 LYS 66 1.286 1.256 1.506 1.543 1.417 126.57 118.12 119.04 112.90 104.95 109.18 122.84 *** * ** +** * * ** *** 67 SER 67 1.301 1.236 1.482 1.518 1.415 119.99 114.12 121.69 110.08 111.27 110.93 124.18 +* ** ** * ** 68 LEU 68 1.273 1.215 1.507 1.505 1.424 123.10 115.14 121.36 112.19 109.67 107.45 123.39 **** * +* * +* **** Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 69 LYS 69 1.304 1.234 1.530 1.554 1.440 122.45 115.35 121.22 111.84 107.56 108.66 123.38 +* * * * +* 70 ASP 70 1.330 1.225 1.520 1.518 1.464 122.34 115.39 121.41 109.85 109.61 109.85 123.19 71 LEU 71 1.325 1.231 1.526 1.547 1.474 122.32 116.61 120.76 108.83 110.99 111.12 122.61 72 GLY 72 1.316 1.227 1.498 - 1.441 120.54 116.41 120.71 - 112.56 - 122.88 * * 73 VAL 73 1.307 1.233 1.523 1.556 1.432 121.39 114.86 121.62 110.71 108.21 112.10 123.32 +* * * +* 74 ARG 74 1.303 1.235 1.512 1.529 1.441 122.60 116.83 120.38 108.61 108.29 109.73 122.79 +* * +* 75 ASP 75 1.313 1.245 1.496 1.519 1.449 121.08 114.57 121.49 107.85 110.78 112.83 123.95 * * * * * 76 GLY 76 1.283 1.238 1.519 - 1.459 121.48 116.59 120.51 - 114.01 - 122.90 *** *** 77 TYR 77 1.306 1.240 1.511 1.536 1.449 122.03 115.91 121.36 110.63 111.20 111.28 122.71 +* +* 78 ARG 78 1.297 1.244 1.518 1.545 1.430 120.97 116.40 120.83 110.90 108.20 111.88 122.75 ** * * ** 79 ILE 79 1.293 1.234 1.501 1.557 1.436 121.28 115.17 121.31 111.18 109.52 112.73 123.51 +** * * +** 80 HIS 80 1.292 1.210 1.514 1.535 1.425 122.18 116.68 120.52 110.54 110.60 109.38 122.80 +** * +* +** 81 ALA 81 1.294 1.229 1.518 1.510 1.437 121.32 116.42 120.64 110.90 110.27 110.26 122.92 +** * +** 82 VAL 82 1.300 1.240 1.532 1.568 1.434 122.20 116.02 120.74 111.88 110.07 110.96 123.18 ** * * * ** 83 ASP 83 1.312 1.235 1.504 1.526 1.460 122.18 115.76 121.13 108.91 111.15 111.39 123.12 * * * 84 VAL 84 1.297 1.229 1.528 1.545 1.434 121.49 116.07 120.98 109.87 110.30 111.95 122.91 ** * ** 85 THR 85 1.323 1.230 1.527 1.529 1.456 122.38 115.69 121.36 108.09 109.82 109.19 122.90 * * 86 GLY 86 1.312 1.230 1.497 - 1.437 120.46 115.33 120.89 - 110.81 - 123.78 * * * 87 GLY 87 1.329 1.231 1.501 - 1.442 121.66 115.74 120.85 - 111.00 - 123.40 88 ASN 88 1.316 1.228 1.498 1.530 1.442 121.91 115.39 120.99 109.76 111.30 110.77 123.60 * * 89 GLU 89 1.300 1.228 1.522 1.544 1.450 123.22 114.98 121.55 112.23 109.77 111.41 123.46 ** * ** 90 ASP 90 1.316 - 1.514 1.539 1.448 123.16 - - 110.78 108.39 110.60 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* +** ** ** +** *** * +* +** +** ** *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 87 1.264 1.345 1.307 .014 *4.6* * +* C-N (Pro) 1.341 .016 2 1.338 1.356 1.347 .009 C-O C-O 1.231 .020 89 1.179 1.256 1.232 .011 +** * CA-C CH1E-C (except Gly) 1.525 .021 81 1.482 1.564 1.519 .015 ** +* CH2G*-C (Gly) 1.516 .018 9 1.487 1.524 1.507 .011 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.507 1.520 1.514 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.529 1.603 1.557 .017 ** CH1E-CH2E (the rest) 1.530 .020 59 1.492 1.571 1.532 .015 +* ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 79 1.404 1.510 1.445 .018 +** +** NH1-CH2G* (Gly) 1.451 .016 9 1.425 1.466 1.447 .012 +* N-CH1E (Pro) 1.466 .015 2 1.459 1.461 1.460 .001 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 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 78 113.24 118.58 116.06 .94 * * CH2G*-C-NH1 (Gly) 116.4 2.1 9 114.17 117.29 115.95 .82 * CH1E-C-N (Pro) 116.9 1.5 2 116.06 116.08 116.07 .01 O-C-N O-C-NH1 (except Pro) 123.0 1.6 87 121.61 124.46 123.10 .52 O-C-N (Pro) 122.0 1.4 2 122.89 123.06 122.98 .08 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 78 119.35 127.40 122.32 1.34 * *** C-NH1-CH2G* (Gly) 120.6 1.7 9 119.98 122.56 121.03 .74 * C-N-CH1E (Pro) 122.6 5.0 2 122.35 122.62 122.48 .13 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 80 118.22 122.63 120.84 .66 +* * CH2G*-C-O (Gly) 120.8 2.1 9 120.06 121.79 120.76 .46 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.53 111.23 110.83 .27 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.09 111.88 109.90 1.06 * CH2E-CH1E-C (the rest) 110.1 1.9 59 105.03 113.79 110.43 1.46 +** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 79 104.16 114.07 109.90 1.70 +** * NH1-CH2G*-C (Gly) 112.5 2.9 9 109.19 114.74 112.04 1.60 * N-CH1E-C (Pro) 111.8 2.5 2 110.27 112.71 111.49 1.22 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.87 110.67 110.24 .29 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.91 115.28 111.62 1.51 +* ** N-CH1E-CH2E (Pro) 103.0 1.1 2 104.24 104.58 104.41 .17 * * * NH1-CH1E-CH2E (the rest) 110.5 1.7 57 107.34 113.22 110.32 1.42 +* +* ------------------------------------------------------------------------------------------------------------- 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_11 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] 69 89.6% Residues in additional allowed regions [a,b,l,p] 7 9.1% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.3% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 77 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 9 Number of proline residues 2 ---- Total number of residues 90 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 77 89.6 83.8 10.0 .6 Inside b. Omega angle st dev 89 3.6 6.0 3.0 -.8 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 81 1.4 3.1 1.6 -1.0 BETTER e. H-bond energy st dev 50 .9 .8 .2 .5 Inside f. Overall G-factor 90 .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 13 4.8 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 32 9.4 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 30 9.9 17.5 4.9 -1.6 BETTER d. Chi-1 pooled st dev 75 9.7 18.2 4.8 -1.7 BETTER e. Chi-2 trans st dev 20 6.4 20.4 5.0 -2.8 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% 89.6 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 .91 3 Residue-by-residue listing for refined_11 Page 12 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.36 Chi1-chi2 distribution -.36 Chi1 only -.24 Chi3 & chi4 .42 Omega .03 ------ -.14 ===== Main-chain covalent forces:- Main-chain bond lengths -.15 Main-chain bond angles .42 ------ .18 ===== OVERALL AVERAGE -.03 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.