Residue-by-residue listing for refined_14 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 - - - -62.7 182.3 - - - - - - 175.1 - 34.7 - 2 ALA 2 b - - - - - - - - - - 184.1 - 33.7 - 3 ASP 3 b - 185.9 - - - - - - - - 174.2 -.6 33.0 - * +* +* 4 THR 4 A - - -52.4 - - - - - - - 180.9 -.9 35.1 - * * 5 GLY 5 - - - - - - - - - - - 178.4 - - - 6 GLU 6 B 62.2 - - 177.7 - - - - - - 175.6 - 33.8 - 7 VAL 7 E B - - -66.4 - - - - - - - 179.7 -3.3 33.2 - +* +* 8 GLN 8 E B - 175.1 - - - - - - - - 178.1 - 35.0 - 9 PHE 9 E B 56.4 - - - - - - - - - 179.4 -1.9 33.7 - 10 MET 10 E B 65.6 - - 176.6 - - - - - - 166.9 - 34.8 - ** ** 11 LYS 11 E B 94.4 - - - - - - - - - 173.6 -1.2 31.2 - +* * * +* 12 PRO 12 E - - - - - -60.8 - - - - - 184.9 - 38.9 - * * 13 PHE 13 e B - 221.6 - - - - - - - - 182.3 -1.4 33.8 - ** ** 14 ILE 14 h B - - -65.2 - - - - - - - 184.9 - 32.9 - 15 SER 15 H A 47.3 - - - - -60.5 -19.0 - - - 176.6 -.5 33.1 - * +* +* +* 16 GLU 16 H A - 175.9 - 181.6 - -63.5 -44.8 - - - 178.1 - 34.6 - 17 LYS 17 H A - - -76.9 - - -87.7 -40.4 - - - 184.5 -1.4 32.1 - +* +* 18 SER 18 H A - 182.7 - - - -62.0 -10.0 - - - 174.5 -2.8 32.2 - +** +** Residue-by-residue listing for refined_14 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 SER 19 h A 54.8 - - - - - - - - - 179.7 -.7 34.5 - +* +* 20 LYS 20 T a - - -77.0 184.2 - - - - - - 182.1 -2.0 33.2 - 21 SER 21 t B - - -58.2 - - - - - - - 176.9 -3.0 34.5 - * * 22 LEU 22 E B - 187.4 - 172.3 - - - - - - 178.4 -3.7 33.6 - ** ** 23 GLU 23 E B - 175.4 - 191.6 - - - - - - 177.1 -.8 36.4 - +* +* 24 ILE 24 e B - - -63.0 179.9 - - - - - - 181.4 -1.0 33.2 - * * 25 PRO 25 h - - - - - -53.7 - - - - - 179.2 - 39.2 - * +* +* 26 LEU 26 H A - 189.6 - 169.9 - -64.7 -32.4 - - - 178.4 - 33.9 - 27 GLY 27 H - - - - - - -62.5 -29.4 - - - 176.9 - - - 28 PHE 28 H A - 175.3 - - - -65.4 -49.6 - - - 179.1 -.8 36.2 - +* +* 29 ASN 29 H A - 178.0 - - - -65.8 -39.7 - - - 178.7 -1.3 34.5 - 30 GLU 30 H A - 178.6 - 183.4 - -62.1 -38.2 - - - 183.1 -2.8 35.7 - * * 31 TYR 31 H A - 183.4 - - - -73.1 -28.6 - - - 175.9 -1.9 33.8 - 32 PHE 32 h b 62.6 - - - - - - - - - 168.7 -1.4 33.4 - +* +* 33 PRO 33 - - - - - -73.4 - - - - - 183.7 - 38.3 - * * 34 ALA 34 B - - - - - - - - - - 175.5 - 34.8 - 35 PRO 35 - - - - - -59.6 - - - - - 181.4 - 38.6 - * * 36 PHE 36 B 51.1 - - - - - - - - - 178.9 - 31.8 - 37 PRO 37 - - - - - -87.8 - - - - - 179.9 - 38.9 - +* * +* 38 ILE 38 S A - - -58.6 - - - - - - - 176.6 - 33.2 - 39 THR 39 B 52.7 - - - - - - - - - 179.8 - 33.2 - 40 VAL 40 E B - 178.1 - - - - - - - - 181.9 -3.3 35.8 - +* +* 41 ASP 41 E B - 187.6 - - - - - - - - 183.4 -2.9 33.5 - * * 42 LEU 42 E B - - -54.9 181.6 - - - - - - 177.8 -3.3 36.5 - +* +* 43 LEU 43 E B - - -67.9 - - - - - - - 174.0 -2.9 34.3 - * * * 44 ASP 44 E B - 180.7 - - - - - - - - 184.4 -2.2 35.2 - 45 TYR 45 e A - - -67.3 - - - - - - - 173.1 -.8 29.9 - * +* * +* 46 SER 46 T A - 183.9 - - - - - - - - 174.7 - 33.4 - 47 GLY 47 t - - - - - - - - - - - 183.4 -2.4 - - 48 ARG 48 e B - 188.3 - 176.6 - - - - - - 181.9 - 31.1 - 49 SER 49 E B 52.7 - - - - - - - - - 178.5 - 35.6 - 50 TRP 50 E B - - -64.2 - - - - - - - 178.5 -2.5 34.5 - 51 THR 51 E B - - -54.3 - - - - - - - 187.3 - 33.6 - * * 52 VAL 52 E B - - -61.5 - - - - - - - 175.9 -2.9 35.2 - * * 53 ARG 53 e B - - -64.5 182.7 - - - - - - 178.6 -2.0 34.2 - 54 MET 54 E B - 170.8 - 182.0 - - - - - - 184.6 -.8 36.0 - +* +* 55 LYS 55 E B - - -63.1 181.7 - - - - - - 174.7 -2.8 34.2 - Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 56 LYS 56 E B - 169.9 - 171.5 - - - - - - 179.5 -.5 32.1 - ** ** 57 ARG 57 e b - 184.8 - 179.2 - - - - - - 178.7 -1.2 34.0 - * * 58 GLY 58 S - - - - - - - - - - - 184.4 - - - 59 GLU 59 S A - - -55.5 180.0 - - - - - - 180.6 - 34.8 - 60 LYS 60 e B - - -63.3 182.8 - - - - - - 177.4 - 34.9 - 61 VAL 61 E B - 184.7 - - - - - - - - 179.0 - 34.9 - 62 PHE 62 E B - - -62.4 - - - - - - - 175.8 -2.4 34.9 - 63 LEU 63 E B - 179.9 - 165.9 - - - - - - 190.8 -2.0 34.0 - +* +* 64 THR 64 e a 58.9 - - - - - - - - - 187.6 -1.6 30.9 - * * 65 VAL 65 T B - - -65.2 - - - - - - - 183.0 - 31.0 - 66 GLY 66 h - - - - - - - - - - - 179.4 - - - 67 TRP 67 H A - 169.6 - - - -59.2 -26.5 - - - 184.0 -1.5 34.2 - * * 68 GLU 68 H A 65.9 - - 181.1 - -71.2 -26.5 - - - 177.9 - 30.0 - * * * 69 ASN 69 H A - - -61.3 - - -69.0 -29.5 - - - 178.5 -1.4 33.4 - 70 PHE 70 H A - 183.4 - - - -73.9 -49.1 - - - 180.9 -.8 35.1 - +* +* 71 VAL 71 H A 72.4 - - - - -63.5 -37.9 - - - 175.6 -2.3 32.4 - 72 LYS 72 H A - - -68.0 175.8 - -65.3 -46.7 - - - 187.6 -2.4 34.7 - * * 73 ASP 73 H A - 188.2 - - - -77.6 -40.8 - - - 181.6 -2.0 31.9 - * * 74 ASN 74 H A - - -64.4 - - -86.8 -15.1 - - - 185.2 -3.4 33.7 - +* ** +* ** 75 ASN 75 h l - - -60.3 - - - - - - - 179.1 -1.0 30.4 - * * * 76 LEU 76 t B 62.2 - - - - - - - - - 183.4 -.6 29.6 - +* * +* 77 GLU 77 t B - - -57.8 168.5 - - - - - - 178.4 - 36.4 - 78 ASP 78 T B 62.1 - - - - - - - - - 180.7 - 32.7 - 79 GLY 79 T - - - - - - - - - - - 178.5 - - - 80 LYS 80 e B - - -76.0 176.8 - - - - - - 185.9 -1.3 31.8 - * * 81 TYR 81 E B - - -64.5 - - - - - - - 174.2 -1.0 35.5 - * * 82 LEU 82 E B - - -69.5 - - - - - - - 179.5 -1.6 32.7 - 83 GLN 83 E B - 176.6 - 183.7 - - - - - - 179.7 -2.5 35.7 - 84 PHE 84 E B - - -57.9 - - - - - - - 177.6 -3.0 34.9 - * * 85 ILE 85 E B - - -53.6 177.4 - - - - - - 181.4 -2.4 34.8 - 86 TYR 86 E B - 176.7 - - - - - - - - 175.1 -3.3 35.6 - +* +* 87 ASP 87 e ~a - - -60.9 - - - - - - - 173.7 -.8 33.0 - ** * +* ** 88 ARG 88 S a - - -62.3 - - - - - - - 187.6 - 35.7 - * * 89 ASP 89 S b - 190.9 - - - - - - - - 181.4 - 36.5 - 90 ARG 90 e a - - -72.6 - - - - - - - 182.3 - 35.0 - 91 THR 91 E B - - -56.2 - - - - - - - 173.4 - 36.2 - * * 92 PHE 92 E B - - -76.1 - - - - - - - 175.2 -2.3 34.7 - Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 TYR 93 E B - - -51.9 - - - - - - - 185.9 -1.8 35.2 - * * 94 VAL 94 E B - 186.2 - - - - - - - - 176.1 -2.9 34.8 - * * 95 ILE 95 E B - - -57.7 179.2 - - - - - - 176.0 -1.8 34.6 - 96 ILE 96 E B - - -67.0 - - - - - - - 177.1 - 34.4 - 97 TYR 97 E B - - -60.2 - - - - - - - 180.7 -3.0 33.5 - * * 98 GLY 98 S - - - - - - - - - - - 178.2 -.6 - - +* +* 99 HIS 99 S b - - -66.0 - - - - - - - 177.7 - 31.0 - 100 ASN 100 S a - 184.5 - - - - - - - - 177.4 -.9 35.3 - +* +* 101 MET 101 B - 195.8 - - - - - - - - 183.6 - 35.0 - 102 CYS 102 - - - -58.1 - - - - - - - - - 33.9 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* ** +* +* +** ** ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.4 182.9 -63.0 178.7 -67.1 -68.5 -33.6 - - - 179.4 -1.9 34.2 Standard deviations: 11.3 9.6 6.5 5.5 13.6 8.4 11.5 - - - 4.1 .9 1.9 Numbers of values: 15 31 42 27 5 18 18 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_14 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 1.502 1.547 1.462 - 115.92 120.67 108.29 109.42 112.29 123.40 * * * 2 ALA 2 1.300 1.238 1.506 1.521 1.428 122.49 115.82 121.23 111.11 107.51 111.46 122.82 ** +* * ** 3 ASP 3 1.306 1.238 1.497 1.540 1.435 120.62 115.17 121.65 110.75 110.26 112.18 122.96 +* * * +* 4 THR 4 1.288 1.225 1.515 1.539 1.416 121.09 114.70 121.18 109.71 106.90 111.20 124.07 +** ** +* +** 5 GLY 5 1.331 1.222 1.498 - 1.429 121.95 116.93 120.23 - 110.90 - 122.80 * * 6 GLU 6 1.303 1.236 1.509 1.541 1.439 121.09 115.74 120.84 110.13 110.38 111.60 123.37 +* +* 7 VAL 7 1.295 1.234 1.511 1.565 1.436 123.20 116.22 121.10 109.85 108.83 113.50 122.65 ** * * ** 8 GLN 8 1.280 1.228 1.502 1.563 1.426 121.42 116.55 120.26 113.87 108.05 107.11 123.18 +*** * +* +* +* * +* +*** 9 PHE 9 1.304 1.243 1.516 1.551 1.450 121.13 116.08 120.65 111.16 110.60 110.64 123.26 +* * +* 10 MET 10 1.322 1.236 1.523 1.543 1.445 121.96 117.30 120.25 108.67 111.39 111.18 122.42 11 LYS 11 1.307 1.245 1.509 1.566 1.435 121.11 119.62 118.57 112.13 107.60 114.55 121.71 +* +* * +* * * * ** ** Residue-by-residue listing for refined_14 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 1.350 1.235 1.513 1.533 1.452 120.96 117.16 120.35 110.34 108.27 103.95 122.50 * * 13 PHE 13 1.293 1.210 1.501 1.513 1.429 119.72 117.11 120.03 110.60 109.34 111.11 122.85 +** * * +* * +** 14 ILE 14 1.307 1.242 1.520 1.589 1.421 121.15 115.94 120.62 111.59 107.97 112.70 123.44 +* +* +* * * +* 15 SER 15 1.324 1.236 1.541 1.528 1.456 123.80 115.42 121.46 112.34 112.73 109.08 123.11 * * * 16 GLU 16 1.320 1.230 1.526 1.519 1.443 123.12 117.31 120.42 110.01 110.66 110.01 122.26 17 LYS 17 1.333 1.228 1.476 1.538 1.456 119.25 115.51 120.28 109.31 110.53 114.69 124.08 ** * ** ** 18 SER 18 1.326 1.220 1.541 1.544 1.447 122.81 116.46 120.63 112.77 112.30 110.25 122.91 * * 19 SER 19 1.324 1.235 1.553 1.531 1.435 122.41 117.05 120.50 111.00 110.90 109.27 122.45 * * * 20 LYS 20 1.344 1.225 1.521 1.529 1.464 121.42 118.95 119.49 108.00 114.73 112.59 121.55 * * * * * * 21 SER 21 1.302 1.225 1.521 1.533 1.453 119.78 116.03 121.52 109.95 112.49 109.76 122.45 +* * +* 22 LEU 22 1.296 1.246 1.506 1.561 1.404 121.30 114.68 121.28 112.50 106.35 111.28 123.97 ** +* +** * +* +** 23 GLU 23 1.294 1.247 1.513 1.520 1.431 123.32 115.95 120.73 109.16 109.16 108.79 123.29 ** * * ** 24 ILE 24 1.287 1.240 1.528 1.554 1.418 121.41 117.28 120.16 112.22 108.54 111.14 122.48 +** ** * +** 25 PRO 25 1.354 1.236 1.524 1.536 1.464 122.94 116.31 120.83 109.79 112.17 103.39 122.86 26 LEU 26 1.321 1.227 1.531 1.563 1.456 121.72 115.34 121.17 112.80 108.06 109.44 123.40 +* * * +* 27 GLY 27 1.331 1.218 1.520 - 1.450 122.22 116.16 120.38 - 112.64 - 123.45 28 PHE 28 1.323 1.227 1.526 1.546 1.469 123.63 115.38 121.13 111.03 108.47 107.49 123.46 * +* +* 29 ASN 29 1.326 1.226 1.523 1.535 1.463 122.42 115.52 121.23 109.94 110.58 110.35 123.24 30 GLU 30 1.318 1.242 1.522 1.527 1.457 123.20 115.14 121.37 109.35 110.39 109.19 123.48 31 TYR 31 1.310 1.234 1.531 1.532 1.432 122.48 117.06 120.10 112.54 110.95 108.82 122.77 * * * * 32 PHE 32 1.329 1.234 1.514 1.558 1.456 121.38 118.07 120.62 109.27 111.65 112.56 121.25 * * * * 33 PRO 33 1.336 1.240 1.504 1.520 1.419 120.70 115.95 120.91 109.77 107.87 105.78 123.13 *** +* +** *** 34 ALA 34 1.267 1.243 1.490 1.527 1.430 121.35 117.97 119.48 110.51 108.96 110.10 122.47 **** +* * **** 35 PRO 35 1.335 1.233 1.510 1.532 1.447 122.02 116.53 120.17 110.19 109.88 104.38 123.29 * * * 36 PHE 36 1.306 1.247 1.528 1.539 1.408 121.68 116.81 121.15 113.46 111.27 110.73 121.95 +* +** +* +** 37 PRO 37 1.335 1.216 1.521 1.536 1.441 122.53 116.88 120.51 110.54 111.60 103.28 122.60 +* +* 38 ILE 38 1.321 1.226 1.525 1.548 1.455 120.64 116.68 120.77 110.18 110.19 112.31 122.55 39 THR 39 1.312 1.239 1.523 1.549 1.428 120.26 114.96 121.27 110.56 110.89 111.77 123.77 * +* +* 40 VAL 40 1.293 1.224 1.516 1.570 1.436 125.24 118.27 119.58 110.05 106.15 110.23 122.14 +** * * +* * +* +** 41 ASP 41 1.293 1.243 1.522 1.531 1.435 120.32 115.99 120.73 112.55 109.64 109.56 123.26 +** * * +** Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 LEU 42 1.309 1.234 1.501 1.541 1.447 122.51 116.41 120.33 107.16 109.13 110.84 123.26 * * +* +* 43 LEU 43 1.300 1.241 1.508 1.555 1.434 121.22 115.41 120.94 109.00 110.18 112.21 123.66 ** * * * ** 44 ASP 44 1.298 1.235 1.496 1.532 1.444 122.33 116.79 120.09 109.19 106.74 111.38 123.12 ** * +* ** 45 TYR 45 1.303 1.238 1.534 1.529 1.459 121.91 117.17 120.42 113.14 114.51 111.64 122.41 +* +* * +* 46 SER 46 1.329 1.242 1.538 1.543 1.441 120.72 116.13 121.28 111.40 108.47 111.29 122.59 47 GLY 47 1.335 1.230 1.521 - 1.440 120.26 118.72 119.62 - 115.54 - 121.65 * * * 48 ARG 48 1.323 1.240 1.538 1.553 1.455 118.76 116.23 120.72 112.71 110.82 112.45 123.04 * +* * * +* 49 SER 49 1.314 1.240 1.539 1.521 1.437 123.21 116.69 120.37 110.74 110.95 107.78 122.92 * * +* +* 50 TRP 50 1.322 1.223 1.519 1.549 1.476 122.39 116.79 120.53 108.41 110.20 112.15 122.68 51 THR 51 1.301 1.235 1.548 1.529 1.437 121.57 115.18 121.38 111.95 109.76 109.90 123.41 +* * * * +* 52 VAL 52 1.309 1.216 1.535 1.542 1.453 124.75 117.42 120.26 109.08 111.57 110.03 122.27 * +* +* 53 ARG 53 1.317 1.224 1.532 1.522 1.466 120.93 116.03 120.51 108.65 111.09 111.61 123.45 54 MET 54 1.316 1.209 1.514 1.541 1.472 124.09 118.13 120.16 109.57 108.34 109.22 121.71 * * * * 55 LYS 55 1.303 1.241 1.505 1.515 1.431 119.30 115.58 120.98 110.13 112.76 109.91 123.44 +* * * +* 56 LYS 56 1.314 1.242 1.479 1.513 1.435 121.98 113.48 122.17 110.52 110.04 113.55 124.32 * ** * * +* ** 57 ARG 57 1.247 1.234 1.508 1.528 1.420 123.12 116.15 120.46 111.30 108.41 110.62 123.28 *5.8* +* *5.8* 58 GLY 58 1.299 1.241 1.503 - 1.425 120.40 115.88 120.82 - 112.01 - 123.26 ** +* ** 59 GLU 59 1.310 1.232 1.529 1.526 1.450 122.16 116.64 120.70 109.86 111.63 109.63 122.66 * * 60 LYS 60 1.317 1.244 1.515 1.523 1.434 121.84 115.61 121.00 109.13 110.84 110.63 123.39 * * 61 VAL 61 1.316 1.232 1.515 1.562 1.437 122.83 116.88 120.41 108.59 107.55 112.48 122.70 * * * 62 PHE 62 1.299 1.233 1.489 1.539 1.439 121.15 115.61 120.94 109.26 108.88 111.33 123.43 ** +* ** 63 LEU 63 1.276 1.203 1.509 1.548 1.425 122.06 117.78 119.95 114.93 105.51 108.10 122.23 +*** * +* +** ** * +*** 64 THR 64 1.302 1.242 1.540 1.553 1.437 119.22 115.96 121.04 111.68 115.78 111.60 122.94 +* * * * +* +* 65 VAL 65 1.318 1.246 1.513 1.552 1.447 122.28 115.11 121.55 111.67 112.96 112.77 123.34 * * 66 GLY 66 1.311 1.230 1.488 - 1.425 121.01 115.61 120.68 - 111.51 - 123.70 * +* +* +* 67 TRP 67 1.337 1.236 1.503 1.544 1.462 122.49 115.82 121.48 110.04 110.40 110.96 122.62 * * 68 GLU 68 1.303 1.206 1.520 1.518 1.431 119.01 116.49 120.77 112.56 111.34 113.67 122.68 +* * * * * +* +* 69 ASN 69 1.319 1.222 1.515 1.535 1.458 121.81 114.70 121.40 111.35 109.63 110.87 123.89 70 PHE 70 1.311 1.229 1.523 1.546 1.442 124.59 116.74 120.40 110.56 109.39 109.48 122.85 * +* +* Residue-by-residue listing for refined_14 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 VAL 71 1.348 1.231 1.513 1.565 1.469 121.15 115.04 121.25 110.52 110.00 113.33 123.70 * * * 72 LYS 72 1.313 1.220 1.509 1.537 1.447 122.02 116.86 120.49 108.11 110.59 112.04 122.64 * * * 73 ASP 73 1.325 1.230 1.522 1.522 1.453 119.06 117.48 120.15 110.67 113.76 112.01 122.31 * * 74 ASN 74 1.308 1.223 1.504 1.552 1.469 120.68 116.07 120.14 108.74 111.12 112.73 123.78 * * * * * 75 ASN 75 1.331 1.247 1.511 1.516 1.439 124.41 115.65 121.30 111.37 112.62 113.76 122.96 +* +* +* 76 LEU 76 1.304 1.231 1.494 1.584 1.431 120.97 115.40 121.08 113.64 109.75 114.60 123.47 +* * +** * +* ** +** 77 GLU 77 1.281 1.246 1.502 1.511 1.424 122.31 115.85 120.16 109.63 108.90 108.42 123.99 *** * +* * *** 78 ASP 78 1.314 1.239 1.524 1.543 1.457 122.47 115.56 121.19 111.09 111.89 111.47 123.20 * * 79 GLY 79 1.311 1.228 1.506 - 1.444 121.52 116.18 120.93 - 111.08 - 122.88 * * 80 LYS 80 1.317 1.237 1.510 1.523 1.452 121.40 115.49 120.78 111.57 111.92 111.97 123.72 81 TYR 81 1.317 1.236 1.486 1.538 1.440 122.60 115.86 120.58 108.19 110.28 111.07 123.55 +* * +* 82 LEU 82 1.291 1.233 1.493 1.542 1.423 121.24 115.67 120.52 110.37 108.99 113.54 123.80 +** +* +* +* +** 83 GLN 83 1.295 1.234 1.487 1.527 1.430 122.36 115.66 120.52 109.01 108.33 110.45 123.80 ** +* * * ** 84 PHE 84 1.291 1.238 1.499 1.527 1.420 121.93 115.88 120.70 110.27 108.91 110.30 123.36 +** * +* +** 85 ILE 85 1.299 1.237 1.514 1.548 1.436 121.46 116.14 120.33 109.37 107.79 111.75 123.49 ** * * ** 86 TYR 86 1.299 1.223 1.512 1.540 1.446 122.47 116.92 120.17 110.20 110.13 108.93 122.89 ** ** 87 ASP 87 1.319 1.228 1.531 1.558 1.454 120.19 115.45 121.25 110.09 109.13 113.05 123.28 * * * 88 ARG 88 1.318 1.231 1.504 1.549 1.473 125.07 114.24 122.20 108.02 105.75 111.89 123.53 +* * +* +* 89 ASP 89 1.310 1.222 1.514 1.548 1.404 123.19 115.94 120.87 110.77 107.81 108.06 123.15 * +** * * +** 90 ARG 90 1.265 1.235 1.521 1.550 1.448 124.26 115.19 121.33 110.01 108.52 110.51 123.44 *4.6* * * *4.6* 91 THR 91 1.305 1.234 1.544 1.549 1.424 122.72 116.51 120.38 109.38 110.27 108.87 123.07 +* +* +* +* 92 PHE 92 1.322 1.239 1.502 1.536 1.462 122.48 115.90 120.71 106.90 109.54 113.50 123.39 * +* +* +* 93 TYR 93 1.293 1.241 1.516 1.529 1.441 122.08 117.17 119.74 110.60 106.61 109.88 123.05 +** +* +** 94 VAL 94 1.320 1.233 1.532 1.560 1.457 121.31 116.05 120.77 108.82 111.42 111.04 123.17 95 ILE 95 1.325 1.234 1.535 1.566 1.458 122.48 116.63 120.17 108.45 109.50 112.36 123.18 96 ILE 96 1.320 1.239 1.520 1.595 1.469 122.83 116.42 120.68 108.58 108.66 113.09 122.88 ** ** 97 TYR 97 1.305 1.240 1.507 1.524 1.441 121.44 115.71 120.64 110.50 109.85 111.57 123.63 +* +* 98 GLY 98 1.307 1.234 1.500 - 1.431 121.83 117.37 120.07 - 110.19 - 122.56 +* * +* 99 HIS 99 1.309 1.238 1.503 1.539 1.448 120.77 114.81 121.60 111.47 110.94 113.77 123.44 * * +* +* Residue-by-residue listing for refined_14 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 1.298 1.232 1.507 1.548 1.441 122.75 115.40 121.40 110.38 106.92 110.21 123.17 ** +* ** 101 MET 101 1.307 1.236 1.515 1.549 1.433 122.03 116.69 120.47 111.03 105.64 110.31 122.79 +* * +* +* 102 CYS 102 1.290 - 1.529 1.526 1.434 121.40 - - 111.73 110.89 109.41 - +** * +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.8* * ** +** *** +* +* * +** ** +** * *5.8* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 1.247 1.348 1.309 .017 *5.8* * * C-N (Pro) 1.341 .016 5 1.335 1.354 1.342 .008 C-O C-O 1.231 .020 101 1.203 1.247 1.233 .009 * CA-C CH1E-C (except Gly) 1.525 .021 95 1.476 1.553 1.516 .015 ** * CH2G*-C (Gly) 1.516 .018 7 1.488 1.521 1.505 .011 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.521 1.527 1.524 .003 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.529 1.595 1.558 .016 ** CH1E-CH2E (the rest) 1.530 .020 75 1.511 1.584 1.537 .014 +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.404 1.476 1.443 .016 +** NH1-CH2G* (Gly) 1.451 .016 7 1.425 1.450 1.435 .009 +* * N-CH1E (Pro) 1.466 .015 5 1.419 1.464 1.445 .015 *** * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_14 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 89 113.48 119.62 116.19 1.00 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 115.61 118.72 116.69 1.00 * CH1E-C-N (Pro) 116.9 1.5 5 115.95 117.16 116.57 .42 O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 121.25 124.32 123.05 .60 * O-C-N (Pro) 122.0 1.4 5 122.50 123.29 122.88 .30 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.76 125.24 121.88 1.35 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 7 120.26 122.22 121.31 .72 C-N-CH1E (Pro) 122.6 5.0 5 120.70 122.94 121.83 .87 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.57 122.20 120.71 .58 * CH2G*-C-O (Gly) 120.8 2.1 7 119.62 120.93 120.39 .43 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.51 111.11 110.81 .30 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.45 112.22 110.13 1.22 * CH2E-CH1E-C (the rest) 110.1 1.9 75 106.90 114.93 110.48 1.59 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.51 115.78 109.86 2.00 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 110.19 115.54 111.98 1.63 * N-CH1E-C (Pro) 111.8 2.5 5 107.87 112.17 109.96 1.72 +* N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 110.10 111.46 110.78 .68 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.87 113.50 111.67 1.26 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.28 105.78 104.16 .90 +** * NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.11 114.69 110.96 1.75 +* ** ------------------------------------------------------------------------------------------------------------- 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_14 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] 75 85.2% Residues in additional allowed regions [a,b,l,p] 12 13.6% 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 85.2 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 .9 .8 .2 .6 Inside f. Overall G-factor 102 -.1 -.4 .3 1.0 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 11.3 18.1 6.5 -1.1 BETTER b. Chi-1 trans st dev 31 9.6 19.0 5.3 -1.8 BETTER c. Chi-1 gauche plus st dev 42 6.5 17.5 4.9 -2.3 BETTER d. Chi-1 pooled st dev 88 8.9 18.2 4.8 -1.9 BETTER e. Chi-2 trans st dev 27 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% 85.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3 Residue-by-residue listing for refined_14 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.43 Chi1-chi2 distribution -.26 Chi1 only -.09 Chi3 & chi4 .47 Omega -.18 ------ -.19 ===== Main-chain covalent forces:- Main-chain bond lengths -.18 Main-chain bond angles .36 ------ .13 ===== OVERALL AVERAGE -.08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.