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 - - - -65.7 178.7 - - - - - - 175.5 - 35.3 - 2 ALA 2 b - - - - - - - - - - 180.1 - 33.5 - 3 ASP 3 b - 182.5 - - - - - - - - 180.9 - 35.1 - 4 THR 4 A - - -50.1 - - - - - - - 183.4 - 35.5 - * * 5 GLY 5 S - - - - - - - - - - - 177.7 - - - 6 GLU 6 S b - 179.3 - 191.3 - - - - - - 182.1 - 36.2 - 7 VAL 7 E B - - -63.6 - - - - - - - 176.9 -2.5 33.0 - 8 GLN 8 E B 56.8 - - 180.9 - - - - - - 183.5 - 33.4 - 9 PHE 9 E B - 183.2 - - - - - - - - 177.1 -2.2 36.5 - 10 MET 10 E B 67.2 - - - - - - - - - 177.4 - 33.3 - 11 LYS 11 E B 78.3 - - - - - - - - - 178.7 -1.1 32.8 - * * 12 PRO 12 E - - - - - -60.1 - - - - - 177.6 - 38.2 - * * 13 PHE 13 e B - - -84.0 - - - - - - - 173.0 -.7 34.3 - * * +* +* 14 ILE 14 h B - - -59.1 179.5 - - - - - - 186.5 - 34.5 - * * 15 SER 15 H A - 186.2 - - - -61.0 -30.0 - - - 178.1 -.6 33.6 - +* +* 16 GLU 16 H A - 180.4 - 187.9 - -60.8 -44.0 - - - 182.4 - 34.9 - 17 LYS 17 H A - 183.7 - - - -80.6 -40.4 - - - 181.9 -.7 35.2 - * +* +* 18 SER 18 H A - 185.2 - - - -72.1 -5.5 - - - 178.3 -3.1 34.6 - +** * +** 19 SER 19 h A - 182.4 - - - - - - - - 185.0 -.6 35.1 - +* +* 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 T a - 197.0 - - - - - - - - 185.3 -1.8 35.1 - 21 SER 21 t B 54.7 - - - - - - - - - 178.1 -2.3 34.8 - 22 LEU 22 E B - 192.9 - 177.8 - - - - - - 180.1 -2.3 35.0 - 23 GLU 23 E B 57.4 - - 171.9 - - - - - - 174.2 -.8 34.3 - +* +* 24 ILE 24 e B - - -57.0 178.8 - - - - - - 177.7 -.7 35.1 - +* +* 25 PRO 25 h - - - - - -56.7 - - - - - 185.0 - 39.0 - * * 26 LEU 26 H A - 183.4 - - - -54.0 -38.7 - - - 179.8 - 33.2 - 27 GLY 27 H - - - - - - -63.1 -28.5 - - - 180.0 - - - 28 PHE 28 H A - 187.4 - - - -87.4 -23.0 - - - 175.4 -1.6 33.2 - +* * +* 29 ASN 29 H A - - -63.3 - - -73.7 -23.9 - - - 177.4 -1.5 33.3 - * * 30 GLU 30 h A - 180.0 - 179.2 - - - - - - 182.6 -1.4 35.6 - 31 TYR 31 T A - 181.8 - - - - - - - - 182.5 - 35.0 - 32 PHE 32 t b 64.1 - - - - - - - - - 168.4 -.5 31.0 - ** +* ** 33 PRO 33 - - - - - -77.8 - - - - - 186.6 - 38.7 - * * * * 34 ALA 34 B - - - - - - - - - - 173.6 - 35.1 - * * 35 PRO 35 - - - - - -59.1 - - - - - 183.6 - 38.5 - * * 36 PHE 36 B - - -64.0 - - - - - - - 177.3 - 34.8 - 37 PRO 37 - - - - - -93.9 - - - - - 175.7 - 39.4 - +** +* +** 38 ILE 38 e a - - -57.8 - - - - - - - 181.2 - 34.6 - 39 THR 39 E B 47.9 - - - - - - - - - 178.3 - 33.4 - * * 40 VAL 40 E B 60.3 - - - - - - - - - 183.8 -3.3 34.4 - +* +* 41 ASP 41 E B - - -62.4 - - - - - - - 179.2 -2.8 33.0 - * * 42 LEU 42 E B - - -64.2 181.5 - - - - - - 177.2 -3.2 34.1 - +* +* 43 LEU 43 E B - - -72.8 - - - - - - - 180.5 -2.5 33.5 - 44 ASP 44 E B - 165.5 - - - - - - - - 184.8 -2.3 34.9 - * * 45 TYR 45 e A - 187.8 - - - - - - - - 180.7 -.6 34.5 - +* +* 46 SER 46 T A - 183.7 - - - - - - - - 174.9 - 33.2 - 47 GLY 47 t - - - - - - - - - - - 181.5 -1.7 - - 48 ARG 48 e B - 181.1 - 174.3 - - - - - - 182.2 - 32.2 - 49 SER 49 E B 54.2 - - - - - - - - - 173.9 - 35.4 - * * 50 TRP 50 E B - - -66.9 - - - - - - - 175.1 -2.6 34.2 - 51 THR 51 E B - - -56.5 - - - - - - - 185.2 - 34.0 - 52 VAL 52 E B - 182.4 - - - - - - - - 180.2 -3.0 34.5 - * * 53 ARG 53 E B - - -64.1 174.4 - - - - - - 186.2 -.5 35.7 - * ** ** 54 MET 54 E B - 178.3 - 180.9 - - - - - - 183.9 -.9 35.3 - +* +* 55 LYS 55 E B - - -67.9 175.0 - - - - - - 176.8 -2.1 34.2 - 56 LYS 56 E B - - -59.1 - - - - - - - 178.1 - 36.6 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 57 ARG 57 E b - 181.8 - 179.0 - - - - - - 175.8 -3.0 32.2 - * * 58 GLY 58 T - - - - - - - - - - - 184.9 - - - 59 GLU 59 T A - - -55.0 177.6 - - - - - - 191.8 -.6 37.6 - ** +* * ** 60 LYS 60 E B 58.6 - - 187.9 - - - - - - 179.1 -2.5 34.9 - 61 VAL 61 E B - 184.4 - - - - - - - - 175.0 - 35.7 - 62 PHE 62 E B - - -67.6 - - - - - - - 172.1 -1.5 35.0 - * * 63 LEU 63 E B - - -67.6 - - - - - - - 186.7 -2.1 31.0 - * * 64 THR 64 e b 56.7 - - - - - - - - - 187.7 -1.5 34.0 - * * 65 VAL 65 T B 63.2 - - - - - - - - - 186.6 - 32.1 - * * 66 GLY 66 h - - - - - - - - - - - 173.3 - - - * * 67 TRP 67 H A - 166.9 - - - -60.9 -26.9 - - - 179.3 -1.8 35.5 - * * 68 GLU 68 H A - 180.3 - 187.2 - -56.6 -36.7 - - - 179.9 -.6 36.3 - +* +* 69 ASN 69 H A - - -63.6 - - -66.4 -36.2 - - - 180.3 -1.2 33.0 - * * 70 PHE 70 H A - 177.1 - - - -72.7 -44.9 - - - 181.4 -.7 33.9 - +* +* 71 VAL 71 H A 74.1 - - - - -62.6 -43.8 - - - 177.8 -2.6 32.3 - 72 LYS 72 H A 66.6 - - - - -72.4 -38.5 - - - 180.9 -2.5 26.7 - ** ** 73 ASP 73 H A - - -76.7 - - -77.5 -39.3 - - - 182.8 -2.7 31.1 - * * 74 ASN 74 H A - 186.4 - - - -84.2 -19.6 - - - 180.9 -3.1 34.8 - +* +* * +* 75 ASN 75 h l - 182.1 - - - - - - - - 182.3 -.9 32.1 - +* +* 76 LEU 76 t B - - -63.5 175.4 - - - - - - 172.4 -1.5 35.2 - * * 77 GLU 77 t B 56.2 - - - - - - - - - 182.3 - 31.8 - 78 ASP 78 T B 61.4 - - - - - - - - - 184.4 - 31.9 - 79 GLY 79 T - - - - - - - - - - - 174.1 - - - * * 80 LYS 80 e B - - -68.7 167.0 - - - - - - 181.7 -1.4 35.2 - 81 TYR 81 E B - - -57.2 - - - - - - - 182.6 -.8 34.3 - +* +* 82 LEU 82 E B - - -67.3 - - - - - - - 177.6 -1.0 33.1 - * * 83 GLN 83 E B - 176.0 - 184.9 - - - - - - 179.5 -3.1 36.2 - * * 84 PHE 84 E B - - -58.9 - - - - - - - 175.9 -3.2 34.8 - * * 85 ILE 85 E B - - -57.0 177.7 - - - - - - 183.4 -2.9 34.3 - * * 86 TYR 86 E B - - -54.6 - - - - - - - 172.0 -3.7 37.1 - * ** ** 87 ASP 87 e b 65.4 - - - - - - - - - 186.0 -.7 30.6 - * +* +* 88 ARG 88 S A - - -45.4 - - - - - - - 176.9 - 33.0 - * * Residue-by-residue listing for refined_11 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 ----------------------------------------------------------------------------------------------------------------------------------- 89 ASP 89 S b - 190.6 - - - - - - - - 179.7 - 36.1 - 90 ARG 90 e a - - -64.7 - - - - - - - 182.6 - 34.5 - 91 THR 91 E B - - -53.7 - - - - - - - 182.8 - 36.3 - 92 PHE 92 E B - - -54.3 - - - - - - - 181.9 -3.2 33.4 - +* +* 93 TYR 93 E B - - -57.9 - - - - - - - 179.6 -1.9 34.8 - 94 VAL 94 E B 57.4 - - - - - - - - - 175.2 -2.8 32.7 - * * 95 ILE 95 E B - - -59.1 178.3 - - - - - - 181.3 -3.2 34.3 - +* +* 96 ILE 96 E B 57.5 - - 177.0 - - - - - - 173.5 -.5 35.4 - * ** ** 97 TYR 97 E B - - -66.3 - - - - - - - 182.0 -3.1 33.6 - * * 98 GLY 98 - - - - - - - - - - - 179.5 -.8 - - +* +* 99 HIS 99 t b 58.6 - - - - - - - - - 177.4 - 33.6 - 100 ASN 100 T b - - -71.2 - - - - - - - 183.0 - 32.8 - 101 MET 101 T ~b - 182.2 - - - - - - - - 176.9 - 35.5 - ** ** 102 CYS 102 t - 51.4 - - - - - - - - - - -1.1 33.3 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * +** +* +** ** ** ** +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.4 182.4 -62.4 179.3 -69.5 -69.1 -32.5 - - - 179.9 -1.8 34.4 Standard deviations: 7.2 6.2 7.4 5.5 16.0 10.0 10.8 - - - 4.1 1.0 1.9 Numbers of values: 21 30 37 24 5 16 16 0 0 0 101 61 95 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_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 - 1.232 1.499 1.538 1.461 - 116.00 120.64 108.35 109.59 111.18 123.36 * * 2 ALA 2 1.307 1.229 1.505 1.518 1.431 122.43 115.98 120.79 111.12 108.42 111.34 123.03 +* * +* 3 ASP 3 1.302 1.227 1.500 1.529 1.444 122.08 116.53 120.61 109.51 108.82 110.67 122.83 +* * +* 4 THR 4 1.297 1.224 1.544 1.544 1.444 121.04 116.33 121.33 109.98 110.36 109.07 122.33 ** * ** 5 GLY 5 1.324 1.230 1.511 - 1.461 120.76 114.07 121.90 - 110.97 - 124.04 * * 6 GLU 6 1.290 1.231 1.505 1.522 1.432 125.56 117.56 119.78 108.51 105.62 110.69 122.63 +** * ** +* +** 7 VAL 7 1.291 1.221 1.502 1.566 1.446 120.36 116.61 120.59 110.18 110.65 112.80 122.76 +** * +** 8 GLN 8 1.296 1.235 1.508 1.526 1.411 121.07 116.44 120.55 112.01 109.20 110.70 123.01 ** ** * ** 9 PHE 9 1.298 1.233 1.509 1.547 1.437 121.34 116.43 120.27 110.77 108.79 107.46 123.29 ** * +* ** 10 MET 10 1.301 1.232 1.509 1.564 1.446 122.30 117.56 119.82 110.25 108.77 112.92 122.58 ** +* * ** 11 LYS 11 1.312 1.244 1.529 1.558 1.443 120.77 118.18 119.45 111.68 109.48 111.81 122.36 * * * 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 PRO 12 1.347 1.241 1.538 1.533 1.466 123.10 115.21 121.55 110.34 113.12 103.88 123.19 * * 13 PHE 13 1.307 1.225 1.498 1.528 1.445 123.41 115.95 120.57 108.75 111.45 111.71 123.45 +* * +* 14 ILE 14 1.309 1.233 1.518 1.551 1.428 121.93 116.89 119.98 110.46 106.35 111.58 123.13 * +* +* +* 15 SER 15 1.321 1.218 1.531 1.533 1.459 122.13 116.75 120.40 110.95 111.59 110.31 122.84 16 GLU 16 1.326 1.234 1.536 1.525 1.452 121.61 116.24 121.08 108.92 110.43 110.72 122.67 17 LYS 17 1.319 1.244 1.515 1.531 1.445 121.38 114.87 121.37 110.05 109.53 109.58 123.66 18 SER 18 1.318 1.212 1.531 1.536 1.444 123.20 116.62 120.88 110.71 110.94 109.50 122.50 19 SER 19 1.303 1.239 1.529 1.533 1.431 121.64 116.71 120.93 110.29 110.11 109.38 122.35 +* * +* 20 LYS 20 1.323 1.237 1.527 1.528 1.430 119.51 116.59 120.52 109.69 111.63 109.63 122.88 * * * 21 SER 21 1.324 1.234 1.522 1.534 1.445 121.15 116.26 120.75 110.26 112.14 109.25 122.98 22 LEU 22 1.315 1.245 1.506 1.554 1.445 121.44 115.62 120.73 110.09 106.34 111.06 123.62 * +* +* 23 GLU 23 1.296 1.247 1.530 1.537 1.433 121.79 116.13 121.02 109.91 110.93 110.74 122.81 ** * ** 24 ILE 24 1.299 1.225 1.534 1.558 1.446 121.64 118.99 119.18 108.93 107.96 111.53 121.81 ** * * ** 25 PRO 25 1.356 1.238 1.535 1.533 1.480 122.60 116.67 120.25 110.06 111.15 103.22 123.07 26 LEU 26 1.336 1.231 1.527 1.535 1.465 123.39 116.63 120.18 110.53 112.14 110.98 123.13 27 GLY 27 1.325 1.227 1.523 - 1.455 121.28 116.64 120.81 - 112.54 - 122.54 28 PHE 28 1.324 1.212 1.537 1.540 1.449 121.27 117.23 120.78 111.84 109.73 110.74 121.96 29 ASN 29 1.334 1.230 1.508 1.537 1.484 120.38 114.79 121.80 108.84 109.43 113.45 123.41 * +* +* 30 GLU 30 1.311 1.237 1.538 1.533 1.449 123.45 115.02 121.70 110.72 109.40 108.24 123.25 * * * 31 TYR 31 1.314 1.245 1.536 1.544 1.444 123.40 117.53 120.40 110.98 111.10 108.56 122.06 * * * 32 PHE 32 1.329 1.232 1.540 1.562 1.447 119.22 117.16 121.38 111.68 114.58 112.06 121.39 +* * * * +* 33 PRO 33 1.335 1.247 1.511 1.523 1.439 122.00 116.07 120.83 109.73 108.05 104.94 123.10 +* +* +* +* 34 ALA 34 1.280 1.240 1.510 1.529 1.438 121.13 117.52 119.89 110.01 110.68 109.58 122.58 *** * *** 35 PRO 35 1.342 1.241 1.534 1.538 1.462 122.85 117.03 120.10 110.55 110.12 103.87 122.87 36 PHE 36 1.312 1.232 1.532 1.517 1.429 122.61 117.00 120.83 110.06 111.90 109.32 122.13 * +* +* 37 PRO 37 1.335 1.232 1.529 1.528 1.441 123.34 116.63 120.72 110.26 111.15 102.72 122.54 +* +* 38 ILE 38 1.300 1.237 1.523 1.559 1.442 120.81 115.65 121.66 109.59 108.18 111.63 122.66 ** * ** 39 THR 39 1.312 1.235 1.527 1.546 1.431 121.58 115.03 121.62 110.38 112.34 111.21 123.35 * * * 40 VAL 40 1.300 1.233 1.527 1.566 1.436 124.07 117.84 120.01 111.15 107.20 110.79 122.13 ** * * * ** 41 ASP 41 1.298 1.230 1.499 1.530 1.450 120.27 115.70 120.92 110.72 111.43 111.62 123.37 ** * ** 42 LEU 42 1.306 1.238 1.505 1.528 1.439 122.29 115.62 120.84 109.74 110.71 111.20 123.53 +* +* 43 LEU 43 1.305 1.238 1.504 1.549 1.444 122.09 115.57 120.67 109.86 110.26 112.40 123.70 +* * +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.299 1.236 1.503 1.536 1.451 123.02 114.65 121.03 110.05 110.41 109.98 124.32 ** * ** 45 TYR 45 1.314 1.230 1.541 1.543 1.450 124.96 117.11 120.22 111.04 111.99 108.92 122.66 * +* +* 46 SER 46 1.330 1.240 1.545 1.537 1.447 121.32 116.78 120.74 111.90 110.78 110.22 122.47 47 GLY 47 1.331 1.230 1.515 - 1.452 120.21 118.13 119.90 - 115.27 - 121.97 48 ARG 48 1.311 1.234 1.536 1.545 1.457 119.92 116.83 120.32 112.92 110.22 110.83 122.81 * * * 49 SER 49 1.317 1.237 1.522 1.523 1.442 121.91 115.98 120.61 109.86 111.53 108.89 123.38 50 TRP 50 1.312 1.235 1.512 1.541 1.463 122.62 116.59 120.64 108.20 109.84 112.86 122.76 * * * 51 THR 51 1.297 1.231 1.534 1.540 1.423 121.06 115.33 121.56 111.46 108.19 110.59 123.10 ** +* * * ** 52 VAL 52 1.292 1.220 1.527 1.567 1.438 123.70 117.06 120.28 111.05 109.26 110.24 122.64 +** * * +** 53 ARG 53 1.299 1.224 1.516 1.531 1.443 122.09 116.05 120.72 111.19 107.91 108.20 123.22 ** * * ** 54 MET 54 1.309 1.211 1.508 1.534 1.461 122.79 117.05 120.10 110.16 109.97 109.20 122.85 * * 55 LYS 55 1.320 1.237 1.514 1.509 1.436 121.12 115.67 120.84 110.29 112.75 109.63 123.49 * * * 56 LYS 56 1.315 1.233 1.515 1.528 1.444 123.00 117.41 119.96 107.28 107.36 110.72 122.60 * * * 57 ARG 57 1.289 1.239 1.516 1.527 1.444 120.20 114.94 121.01 110.41 112.15 112.53 124.03 +** * +** 58 GLY 58 1.312 1.236 1.497 - 1.443 123.21 115.56 120.87 - 114.59 - 123.53 * * +* +* 59 GLU 59 1.300 1.234 1.512 1.533 1.444 122.39 116.57 120.77 106.79 110.54 109.22 122.63 ** +* ** 60 LYS 60 1.312 1.237 1.520 1.510 1.429 120.09 115.06 121.61 110.80 113.92 107.84 123.31 * +* +* +* 61 VAL 61 1.317 1.241 1.524 1.562 1.440 123.51 116.08 120.81 108.24 108.81 111.34 123.10 * * 62 PHE 62 1.303 1.246 1.488 1.543 1.444 122.61 116.76 120.40 107.73 108.47 112.85 122.83 +* +* * * +* 63 LEU 63 1.298 1.220 1.491 1.538 1.441 118.71 114.95 120.73 111.52 107.39 115.23 124.29 ** +* +* * +** +** 64 THR 64 1.296 1.248 1.548 1.545 1.438 124.16 115.49 121.42 111.16 113.16 109.15 123.08 ** * * * * ** 65 VAL 65 1.328 1.234 1.539 1.561 1.440 123.13 115.10 121.76 112.63 111.16 111.20 123.13 +* +* 66 GLY 66 1.298 1.225 1.485 - 1.438 121.82 114.37 121.59 - 108.56 - 124.02 ** +* * ** 67 TRP 67 1.333 1.234 1.522 1.538 1.459 123.32 113.74 122.09 110.45 108.84 108.93 124.12 * * 68 GLU 68 1.308 1.219 1.538 1.520 1.448 124.28 115.96 121.20 109.65 109.93 107.96 122.83 +* * * +* 69 ASN 69 1.317 1.201 1.503 1.536 1.448 122.10 115.99 120.96 110.88 110.64 111.81 122.97 +* * +* 70 PHE 70 1.295 1.225 1.502 1.539 1.433 122.74 116.62 120.22 110.76 109.89 111.01 123.13 ** * * ** 71 VAL 71 1.330 1.236 1.528 1.577 1.446 120.50 115.94 120.89 111.22 109.65 113.07 123.16 * * 72 LYS 72 1.327 1.230 1.539 1.559 1.442 120.95 117.69 120.02 114.94 114.24 114.07 122.29 * +** * ** +** 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 ASP 73 1.350 1.226 1.505 1.538 1.488 120.26 117.16 120.20 109.35 113.88 114.24 122.63 * +* ** ** 74 ASN 74 1.308 1.234 1.521 1.546 1.463 120.75 114.92 121.15 110.19 108.92 110.33 123.88 +* +* 75 ASN 75 1.332 1.248 1.521 1.537 1.464 124.74 115.52 121.55 111.19 110.95 112.38 122.89 +* * +* 76 LEU 76 1.311 1.229 1.504 1.528 1.442 121.82 114.85 121.19 108.40 111.87 110.73 123.95 * * * 77 GLU 77 1.295 1.246 1.508 1.555 1.423 124.16 116.95 119.88 111.38 107.89 114.28 123.16 ** * +* * * ** ** 78 ASP 78 1.311 1.229 1.508 1.536 1.455 121.14 115.35 121.23 111.43 110.65 112.65 123.39 * * * 79 GLY 79 1.295 1.229 1.493 - 1.436 121.43 114.66 121.36 - 109.03 - 123.99 ** * * ** 80 LYS 80 1.311 1.242 1.514 1.528 1.440 123.31 116.77 120.24 110.47 108.33 109.56 122.99 * * * 81 TYR 81 1.300 1.234 1.494 1.536 1.438 121.16 116.93 120.15 110.70 107.90 110.99 122.90 ** * * * ** 82 LEU 82 1.295 1.238 1.504 1.546 1.436 120.77 114.99 120.85 109.88 111.16 112.51 124.15 ** * * * ** 83 GLN 83 1.301 1.226 1.512 1.529 1.436 124.02 116.82 120.36 109.05 108.15 109.56 122.82 +* * * * +* 84 PHE 84 1.293 1.231 1.502 1.530 1.436 121.40 116.26 120.38 109.26 109.72 111.07 123.35 +** * * +** 85 ILE 85 1.302 1.241 1.518 1.551 1.441 121.76 116.20 120.44 109.94 107.75 111.84 123.33 +* * +* 86 TYR 86 1.308 1.246 1.523 1.549 1.438 122.15 117.41 120.07 106.93 110.28 110.02 122.52 +* * +* +* 87 ASP 87 1.318 1.240 1.529 1.558 1.449 119.83 119.26 119.37 113.29 107.69 113.86 121.36 * * +* +* * +* * +* 88 ARG 88 1.314 1.232 1.541 1.538 1.461 119.29 116.99 120.53 110.51 111.89 111.48 122.48 * * * 89 ASP 89 1.321 1.229 1.549 1.560 1.444 123.09 117.23 120.41 111.20 106.52 108.14 122.35 * * +* * +* 90 ARG 90 1.288 1.232 1.520 1.563 1.467 123.75 115.28 121.65 108.72 107.91 112.65 123.05 +** +* * * * +** 91 THR 91 1.298 1.225 1.517 1.534 1.420 122.33 117.39 120.02 109.70 107.72 109.05 122.56 ** ** * * ** 92 PHE 92 1.310 1.242 1.513 1.540 1.438 120.34 115.83 121.14 110.71 110.30 111.45 123.03 * * * 93 TYR 93 1.302 1.233 1.501 1.527 1.441 121.83 116.38 120.27 110.12 109.98 110.06 123.35 +* * +* 94 VAL 94 1.304 1.240 1.536 1.567 1.441 121.68 115.53 121.48 110.81 111.48 112.06 122.92 +* * +* 95 ILE 95 1.302 1.235 1.520 1.559 1.433 122.88 116.42 120.65 109.93 107.82 111.97 122.89 +* * * +* 96 ILE 96 1.301 1.234 1.515 1.553 1.420 122.25 115.96 121.08 109.11 110.57 110.46 122.89 +* +* +* 97 TYR 97 1.297 1.237 1.506 1.528 1.430 121.44 115.54 120.69 110.46 108.52 112.04 123.75 ** * ** 98 GLY 98 1.305 1.237 1.508 - 1.431 121.42 116.52 120.30 - 110.67 - 123.18 +* * +* 99 HIS 99 1.307 1.237 1.520 1.558 1.457 122.68 117.28 119.35 111.22 109.20 111.10 123.36 +* * +* Residue-by-residue listing for refined_11 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 100 ASN 100 1.332 1.231 1.506 1.540 1.475 122.29 115.01 120.90 109.97 111.05 112.65 124.09 * * 101 MET 101 1.308 1.230 1.513 1.543 1.459 124.56 114.17 122.12 109.22 106.62 110.93 123.71 +* +* * +* +* 102 CYS 102 1.306 - 1.532 1.538 1.425 123.21 - - 112.89 109.20 109.74 - +* +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* +* +* ** ** +* +** +* +** * *** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 Page 10 ---------------------------------------- A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S +------------------+ | BOND LENGTHS | +------------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Bond X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- C-N C-NH1 (except Pro) 1.329 .014 96 1.280 1.350 1.309 .013 *** * * C-N (Pro) 1.341 .016 5 1.335 1.356 1.343 .008 C-O C-O 1.231 .020 101 1.201 1.248 1.233 .008 +* CA-C CH1E-C (except Gly) 1.525 .021 95 1.488 1.549 1.519 .014 +* * CH2G*-C (Gly) 1.516 .018 7 1.485 1.523 1.505 .012 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.518 1.529 1.523 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.534 1.577 1.556 .011 * CH1E-CH2E (the rest) 1.530 .020 75 1.509 1.564 1.537 .012 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.411 1.488 1.444 .013 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.431 1.461 1.445 .010 * N-CH1E (Pro) 1.466 .015 5 1.439 1.480 1.458 .016 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_11 Page 11 ---------------------------------------- +-----------------+ | BOND ANGLES | +-----------------+ ------------------------------------------------------------------------------------------------------------- (Small molecule data) Number of Min Max Mean Standard Angle X-PLOR labelling Mean St. dev values value value value deviation ------------------------------------------------------------------------------------------------------------- CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 89 113.74 119.26 116.28 1.00 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.07 118.13 115.71 1.36 * CH1E-C-N (Pro) 116.9 1.5 5 115.21 117.03 116.32 .64 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.36 124.32 123.02 .60 * O-C-N (Pro) 122.0 1.4 5 122.54 123.19 122.95 .23 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.71 125.56 122.01 1.39 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 7 120.21 123.21 121.45 .87 +* C-N-CH1E (Pro) 122.6 5.0 5 122.00 123.34 122.78 .46 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 119.18 122.12 120.70 .61 CH2G*-C-O (Gly) 120.8 2.1 7 119.90 121.90 120.96 .66 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.01 111.12 110.56 .55 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.24 112.63 110.33 1.02 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 106.79 114.94 110.27 1.35 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.62 114.58 109.90 1.86 +* * NH1-CH2G*-C (Gly) 112.5 2.9 7 108.56 115.27 111.66 2.40 * N-CH1E-C (Pro) 111.8 2.5 5 108.05 113.12 110.72 1.65 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.58 111.34 110.46 .88 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.05 113.07 111.09 1.14 * N-CH1E-CH2E (Pro) 103.0 1.1 5 102.72 104.94 103.73 .75 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.46 115.23 110.85 1.70 +* +** ------------------------------------------------------------------------------------------------------------- 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 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] 73 83.0% Residues in additional allowed regions [a,b,l,p] 14 15.9% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.1% Residues in disallowed regions [XX] 0 .0% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions [E,H,L]. S T E R E O C H E M I S T R Y O F M A I N - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. %-tage residues in A, B, L 88 83.0 83.8 10.0 -.1 Inside b. Omega angle st dev 101 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 95 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 61 1.0 .8 .2 .8 Inside f. Overall G-factor 102 -.1 -.4 .3 1.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 21 7.2 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 30 6.2 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 37 7.4 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 88 7.7 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 24 5.5 20.4 5.0 -3.0 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% 83.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.6 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .99 3 Residue-by-residue listing for refined_11 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.46 Chi1-chi2 distribution -.23 Chi1 only -.23 Chi3 & chi4 .36 Omega -.20 ------ -.22 ===== Main-chain covalent forces:- Main-chain bond lengths .01 Main-chain bond angles .38 ------ .23 ===== OVERALL AVERAGE -.06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.