Residue-by-residue listing for refined_20 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 - - - -63.0 - - - - - - - 181.3 - 34.1 - 2 ALA 2 b - - - - - - - - - - 179.9 - 33.6 - 3 GLU 3 b - 185.4 - 183.8 - - - - - - 180.4 -.9 34.8 - +* +* 4 VAL 4 B - 187.8 - - - - - - - - 178.6 - 35.2 - 5 HIS 5 b - - -62.9 - - - - - - - 178.9 - 33.9 - 6 ASN 6 S A - - -74.8 - - - - - - - 184.1 - 33.9 - 7 GLN 7 B - - -67.6 - - - - - - - 178.6 - 32.1 - 8 LEU 8 E B - - -66.2 - - - - - - - 179.4 -2.8 34.7 - * * 9 GLU 9 E B - - -71.2 - - - - - - - 178.2 -1.1 33.4 - * * 10 ILE 10 E B - - -61.8 179.8 - - - - - - 175.0 -2.6 34.9 - 11 LYS 11 E B 63.3 - - 175.6 - - - - - - 184.2 -2.7 33.2 - 12 PHE 12 E B - - -55.5 - - - - - - - 175.1 -.6 35.5 - +* +* 13 ARG 13 E B - 172.6 - 174.4 - - - - - - 183.1 -3.2 31.9 - +* +* 14 LEU 14 E B - - -66.5 - - - - - - - 177.9 -3.5 34.5 - +* +* 15 THR 15 e A - 184.9 - - - - - - - - 178.8 -1.8 34.7 - 16 ASP 16 T A - - -62.6 - - - - - - - 177.6 - 34.3 - 17 GLY 17 t - - - - - - - - - - - 178.1 -1.6 - - 18 SER 18 e B - - -55.8 - - - - - - - 180.3 - 35.2 - 19 ASP 19 E B 64.3 - - - - - - - - - 178.4 - 33.6 - 20 ILE 20 E B - - -58.3 177.6 - - - - - - 180.7 -2.8 35.7 - * * 21 GLY 21 E - - - - - - - - - - - 183.6 - - - Residue-by-residue listing for refined_20 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 22 PRO 22 E - - - - - -80.6 - - - - - 176.6 - 38.2 - * * * 23 LYS 23 E B - - -80.6 - - - - - - - 183.5 -1.9 31.1 - 24 ALA 24 E B - - - - - - - - - - 177.5 - 34.3 - 25 PHE 25 E B - - -53.4 - - - - - - - 175.2 -3.3 36.5 - +* +* 26 PRO 26 t - - - - - -60.5 - - - - - 177.9 - 39.2 - +* +* 27 ASP 27 T A - 173.4 - - - - - - - - 182.9 - 35.1 - 28 ALA 28 T A - - - - - - - - - - 180.3 - 33.8 - 29 THR 29 t B - - -56.9 - - - - - - - 178.1 -1.7 34.9 - 30 THR 30 h B - 178.2 - - - - - - - - 178.6 - 33.2 - 31 VAL 31 H A - 180.9 - - - -66.6 -26.1 - - - 175.5 -3.2 33.2 - * +* +* 32 SER 32 H A - 182.3 - - - -57.6 -46.9 - - - 180.2 -.9 34.2 - * * 33 ALA 33 H A - - - - - -71.5 -29.6 - - - 177.1 - 34.0 - 34 LEU 34 H A - 175.1 - - - -66.2 -45.8 - - - 176.9 -1.6 35.5 - 35 LYS 35 H A - - -64.1 165.2 - -67.2 -39.4 - - - 174.7 -3.1 32.4 - * * 36 GLU 36 H A - - -68.7 - - -57.9 -38.4 - - - 180.9 -2.6 34.0 - 37 THR 37 H A - - -56.0 - - -73.4 -41.2 - - - 180.6 -1.9 33.6 - 38 VAL 38 H A 68.1 - - - - -63.4 -36.5 - - - 175.7 -2.3 31.9 - 39 ILE 39 H A - - -60.0 173.6 - -63.5 -35.8 - - - 180.7 -2.2 35.5 - 40 SER 40 H A - 181.0 - - - -71.3 -27.5 - - - 182.1 -1.2 34.7 - * * * 41 GLU 41 h A - - -60.9 - - - - - - - 185.5 -1.4 36.7 - 42 TRP 42 t B - 206.1 - - - - - - - - 177.6 -.8 37.0 - * +* +* 43 PRO 43 t - - - - - -62.3 - - - - - 181.9 - 38.3 - * * 44 ARG 44 T A - 186.8 - 187.1 - - - - - - 182.6 - 36.4 - 45 GLU 45 T A - - -58.4 177.8 - - - - - - 181.7 - 34.5 - 46 LYS 46 t B - 184.8 - 172.9 - - - - - - 180.3 -1.0 33.5 - * * 47 GLU 47 S B 51.6 - - 179.2 - - - - - - 185.0 - 30.1 - * * 48 ASN 48 S l - 187.1 - - - - - - - - 180.6 - 30.6 - 49 GLY 49 S - - - - - - - - - - - 179.4 - - - 50 PRO 50 - - - - - -57.3 - - - - - 185.4 - 39.9 - +* +* 51 LYS 51 A - 185.3 - 175.1 - - - - - - 179.6 -.9 33.0 - +* +* 52 THR 52 t B 56.3 - - - - - - - - - 186.8 - 30.8 - * * 53 VAL 53 T A 55.8 - - - - - - - - - 183.2 - 31.8 - 54 LYS 54 T A - - -59.3 174.0 - - - - - - 186.0 - 35.2 - * * 55 GLU 55 e A - - -57.1 172.2 - - - - - - 181.6 -1.8 35.4 - 56 VAL 56 E B - 183.0 - - - - - - - - 181.4 -1.2 35.2 - * * 57 LYS 57 E B - 182.9 - 175.4 - - - - - - 183.7 -2.1 34.3 - 58 LEU 58 E B - - -64.4 - - - - - - - 174.7 - 34.1 - 59 ILE 59 E B - - -63.0 181.9 - - - - - - 181.3 -2.7 33.4 - 60 SER 60 E B - 181.7 - - - - - - - - 180.0 -3.0 34.7 - * * 61 ALA 61 T l - - - - - - - - - - 180.1 - 32.7 - Residue-by-residue listing for refined_20 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 62 GLY 62 T - - - - - - - - - - - 179.7 - - - 63 LYS 63 E B - 179.1 - - - - - - - - 178.0 -1.6 34.4 - 64 VAL 64 E B 60.9 - - - - - - - - - 179.7 - 32.9 - 65 LEU 65 e B - - -65.9 - - - - - - - 182.1 -3.3 33.4 - +* +* 66 GLU 66 t B - 186.1 - 174.6 - - - - - - 184.9 - 34.0 - 67 ASN 67 T A 62.6 - - - - - - - - - 180.7 - 32.9 - 68 SER 68 T A - - -52.5 - - - - - - - 179.6 - 35.0 - 69 LYS 69 t B - - -65.6 - - - - - - - 175.2 -2.7 35.4 - 70 THR 70 B B 56.7 - - - - - - - - - 177.2 - 35.4 - 71 VAL 71 g A - 180.7 - - - - - - - - 178.6 -3.8 34.1 - ** ** 72 LYS 72 G A - 182.5 - - - - - - - - 180.5 -.6 34.8 - +* +* 73 ASP 73 G A - 182.5 - - - - - - - - 179.4 - 33.5 - 74 TYR 74 G A - - -60.0 - - - - - - - 178.1 -1.5 34.0 - 75 ARG 75 g B - - -70.7 - - - - - - - 178.7 -1.2 36.2 - * * 76 SER 76 B - - -56.8 - - - - - - - 182.9 - 34.5 - 77 PRO 77 S - - - - - -49.6 - - - - - 183.6 - 38.4 - * * * 78 VAL 78 S l - 178.3 - - - - - - - - 179.1 - 31.5 - 79 SER 79 B 54.6 - - - - - - - - - 179.9 - 33.7 - 80 ASN 80 b - - -63.8 - - - - - - - 174.6 - 35.4 - 81 LEU 81 B 49.5 - - - - - - - - - 182.9 - 33.2 - 82 ALA 82 b - - - - - - - - - - 174.3 -.6 35.3 - +* +* 83 GLY 83 - - - - - - - - - - - 182.1 - - - 84 ALA 84 e B - - - - - - - - - - 180.3 - 34.7 - 85 VAL 85 E B - 182.7 - - - - - - - - 180.5 - 34.2 - 86 THR 86 E B - - -49.9 - - - - - - - 184.0 -3.7 35.3 - * ** ** 87 THR 87 E B - - -52.5 - - - - - - - 176.0 -.5 34.8 - +* +* 88 MET 88 E B - - -77.2 - - - - - - - 178.1 -2.5 33.6 - 89 HIS 89 E B - - -62.3 - - - - - - - 179.8 -3.6 34.0 - ** ** 90 VAL 90 E B - 181.5 - - - - - - - - 179.1 -2.7 33.7 - 91 ILE 91 E B - - -74.7 - - - - - - - 183.6 -3.0 33.8 - * * 92 ILE 92 E B - - -58.2 - - - - - - - 174.2 -.6 34.4 - * +* +* 93 GLN 93 e B - 181.2 - 173.9 - - - - - - 189.1 -1.6 34.5 - +* +* 94 ALA 94 B - - - - - - - - - - 182.6 -.6 33.9 - +* +* 95 PRO 95 - - - - - -75.4 - - - - - 179.6 - 38.2 - * * 96 VAL 96 b - 186.0 - - - - - - - - 182.6 -.5 33.2 - ** ** 97 THR 97 B - - -58.5 - - - - - - - 182.8 -1.3 35.0 - * * 98 GLU 98 B - 183.6 - 182.1 - - - - - - 184.2 - 34.5 - 99 LYS 99 b - 186.8 - - - - - - - - 183.0 -1.1 35.2 - * * 100 GLU 100 A - 180.5 - 186.7 - - - - - - 183.6 - 34.7 - 101 LYS 101 - - 175.6 - - - - - - - - - - 31.4 - Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * * +* ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.5 182.7 -62.5 177.2 -64.3 -65.9 -36.7 - - - 180.2 -1.9 34.4 Standard deviations: 5.7 5.8 7.0 5.3 11.6 5.4 7.2 - - - 3.1 1.0 1.7 Numbers of values: 11 32 39 20 6 10 10 0 0 0 100 52 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_20 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 - 1.231 1.506 1.550 1.465 - 116.63 120.24 109.31 109.13 112.27 123.14 * * 2 ALA 2 1.312 1.243 1.513 1.520 1.442 121.77 115.57 120.79 110.79 110.58 110.85 123.60 * * 3 GLU 3 1.315 1.235 1.520 1.528 1.439 123.48 116.72 120.40 109.50 108.69 111.06 122.87 * * 4 VAL 4 1.307 1.229 1.512 1.546 1.451 121.47 116.01 120.74 107.45 109.21 112.38 123.25 +* +* 5 HIS 5 1.297 1.238 1.530 1.551 1.467 122.98 116.86 120.48 109.21 109.63 112.40 122.65 ** * * ** 6 ASN 6 1.324 1.233 1.514 1.545 1.474 122.20 117.49 119.91 107.84 112.72 112.71 122.59 * * * 7 GLN 7 1.315 1.238 1.515 1.528 1.433 120.62 114.40 121.52 109.92 112.66 113.08 124.07 * +* +* 8 LEU 8 1.299 1.229 1.518 1.551 1.458 124.50 118.67 119.40 108.68 109.10 112.01 121.93 ** * +* * ** 9 GLU 9 1.324 1.229 1.498 1.539 1.454 118.88 114.36 121.76 107.24 110.44 114.80 123.88 * +* +* +** +** 10 ILE 10 1.289 1.245 1.503 1.563 1.435 123.30 115.88 120.65 108.92 108.94 111.90 123.44 +** * * +** 11 LYS 11 1.291 1.243 1.511 1.529 1.420 121.66 116.64 120.49 110.86 108.12 112.41 122.87 +** ** * * +** Residue-by-residue listing for refined_20 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 1.294 1.213 1.512 1.532 1.438 120.87 117.08 120.25 109.30 110.51 109.75 122.67 +** * +** 13 ARG 13 1.306 1.221 1.508 1.550 1.449 121.47 115.63 121.03 111.89 109.06 112.96 123.34 +* * * +* 14 LEU 14 1.299 1.240 1.518 1.548 1.442 122.94 115.58 121.05 109.29 111.12 111.19 123.37 ** ** 15 THR 15 1.318 1.222 1.536 1.556 1.453 123.24 115.22 121.71 110.47 110.24 109.93 123.06 16 ASP 16 1.312 1.229 1.527 1.533 1.461 122.98 116.17 121.19 110.05 111.04 110.43 122.63 * * 17 GLY 17 1.324 1.230 1.510 - 1.449 121.32 116.38 120.82 - 113.03 - 122.80 18 SER 18 1.303 1.232 1.521 1.525 1.439 121.71 117.20 120.11 110.44 108.59 109.42 122.66 +* * +* 19 ASP 19 1.303 1.234 1.502 1.536 1.428 121.34 115.03 121.33 109.94 110.90 111.88 123.63 +* * +* +* 20 ILE 20 1.291 1.237 1.523 1.564 1.436 123.82 116.45 119.60 109.50 107.73 110.32 123.94 +** * * * +** 21 GLY 21 1.332 1.243 1.527 - 1.461 122.34 117.79 120.11 - 112.93 - 122.09 * * 22 PRO 22 1.337 1.231 1.529 1.525 1.452 122.77 114.63 121.76 110.34 114.62 103.69 123.61 +* * * +* 23 LYS 23 1.304 1.213 1.494 1.557 1.471 124.30 117.33 119.54 110.28 109.46 115.47 123.13 +* * * * +** +** 24 ALA 24 1.306 1.243 1.520 1.523 1.441 121.33 115.19 121.33 110.39 111.01 110.11 123.46 +* +* 25 PHE 25 1.306 1.234 1.507 1.536 1.441 123.58 118.31 119.80 107.09 106.82 111.32 121.78 +* * * +* +* +* 26 PRO 26 1.319 1.240 1.536 1.526 1.462 122.16 115.21 121.04 109.30 112.45 103.62 123.74 * * * * 27 ASP 27 1.311 1.226 1.539 1.547 1.473 124.20 116.30 121.12 110.65 111.32 108.52 122.51 * * * * 28 ALA 28 1.324 1.232 1.541 1.520 1.463 121.95 117.55 120.17 110.21 113.28 109.96 122.27 29 THR 29 1.317 1.219 1.519 1.539 1.460 121.35 116.89 120.17 109.46 110.36 110.39 122.93 30 THR 30 1.309 1.245 1.534 1.561 1.438 121.32 116.31 120.80 110.78 110.43 111.74 122.89 * * * 31 VAL 31 1.323 1.220 1.517 1.554 1.445 122.13 116.36 120.77 110.88 109.01 112.18 122.86 32 SER 32 1.330 1.223 1.538 1.535 1.443 121.31 116.31 120.65 110.62 109.35 110.60 122.93 33 ALA 33 1.333 1.235 1.523 1.518 1.459 122.45 115.89 121.02 110.49 110.71 110.35 123.09 34 LEU 34 1.321 1.236 1.539 1.530 1.419 123.25 115.53 121.24 111.83 109.01 107.54 123.19 ** +* ** 35 LYS 35 1.324 1.207 1.523 1.539 1.451 122.75 117.18 120.27 113.19 110.37 110.24 122.50 * +* +* 36 GLU 36 1.324 1.237 1.529 1.530 1.462 121.50 115.93 121.00 109.67 111.06 111.02 123.05 37 THR 37 1.317 1.227 1.540 1.541 1.437 121.84 117.37 120.18 110.30 111.35 111.16 122.42 * * 38 VAL 38 1.334 1.221 1.538 1.570 1.466 120.76 115.54 120.96 111.75 110.22 112.57 123.44 * * * 39 ILE 39 1.328 1.234 1.541 1.558 1.479 123.28 115.62 121.59 108.60 109.82 110.44 122.79 * * 40 SER 40 1.311 1.245 1.548 1.548 1.449 123.13 116.09 121.11 111.34 110.79 108.72 122.78 * * * * 41 GLU 41 1.327 1.242 1.529 1.515 1.448 123.07 115.60 121.10 108.25 111.22 108.52 123.31 * * 42 TRP 42 1.296 1.244 1.529 1.523 1.441 122.47 118.29 119.69 109.43 109.04 107.60 122.01 ** * +* ** 43 PRO 43 1.349 1.232 1.530 1.535 1.464 122.63 115.43 121.29 110.42 111.59 104.03 123.27 Residue-by-residue listing for refined_20 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 1.314 1.239 1.534 1.525 1.456 123.42 115.27 121.47 109.33 110.17 108.21 123.26 * * * 45 GLU 45 1.318 1.240 1.533 1.532 1.459 123.31 116.65 120.68 110.23 111.79 109.64 122.67 46 LYS 46 1.325 1.237 1.522 1.537 1.451 121.70 116.32 120.81 111.08 110.41 110.75 122.83 47 GLU 47 1.315 1.242 1.514 1.522 1.429 121.45 114.22 121.00 112.87 112.67 112.68 124.77 * +* * * * +* 48 ASN 48 1.327 1.245 1.520 1.547 1.477 125.60 115.17 121.70 111.32 111.00 114.28 122.98 ** ** ** 49 GLY 49 1.293 1.230 1.489 - 1.417 121.50 117.92 119.02 - 109.80 - 123.02 +** * ** +** 50 PRO 50 1.336 1.205 1.524 1.526 1.478 123.79 117.51 120.51 109.37 113.12 102.37 121.98 * * 51 LYS 51 1.300 1.228 1.526 1.543 1.437 119.73 117.10 120.95 112.37 111.39 110.04 121.95 ** * * * ** 52 THR 52 1.315 1.244 1.560 1.550 1.436 120.25 115.51 121.10 112.34 113.10 112.19 123.39 * +* * * +* 53 VAL 53 1.333 1.238 1.548 1.576 1.485 125.40 117.49 120.03 111.45 115.55 110.87 122.46 * * * ** * +* ** 54 LYS 54 1.314 1.232 1.529 1.531 1.469 121.90 116.50 120.87 108.99 111.85 109.84 122.62 * * 55 GLU 55 1.308 1.238 1.531 1.509 1.452 121.92 116.64 120.76 110.05 112.23 108.26 122.60 +* * * +* 56 VAL 56 1.317 1.227 1.521 1.554 1.454 121.05 116.91 120.24 108.40 109.54 111.42 122.84 57 LYS 57 1.310 1.229 1.529 1.528 1.453 121.64 116.81 120.34 111.51 110.19 109.19 122.84 * * 58 LEU 58 1.328 1.232 1.529 1.560 1.463 121.65 116.09 120.81 108.84 112.04 111.75 123.10 * * 59 ILE 59 1.315 1.232 1.526 1.567 1.460 122.78 116.37 120.75 110.55 108.92 112.28 122.86 * * * 60 SER 60 1.303 1.241 1.513 1.535 1.434 122.12 115.77 120.31 111.09 108.92 109.63 123.87 +* * +* 61 ALA 61 1.335 1.234 1.536 1.529 1.466 124.11 116.29 121.07 111.56 111.55 110.79 122.59 * * 62 GLY 62 1.317 1.235 1.513 - 1.441 121.00 116.69 120.80 - 112.64 - 122.51 63 LYS 63 1.307 1.232 1.499 1.541 1.433 121.59 116.11 120.52 110.66 108.58 110.83 123.33 +* * * +* 64 VAL 64 1.302 1.241 1.531 1.566 1.436 121.42 116.24 121.12 111.34 109.84 111.94 122.59 +* * * +* 65 LEU 65 1.300 1.236 1.507 1.546 1.426 121.41 116.56 120.53 110.49 109.02 112.30 122.92 ** +* * ** 66 GLU 66 1.300 1.226 1.508 1.537 1.433 121.47 116.02 119.95 112.09 108.01 110.05 124.01 ** * * * ** 67 ASN 67 1.323 1.221 1.531 1.547 1.488 124.59 117.10 120.19 110.04 114.28 111.08 122.71 +* +* * +* 68 SER 68 1.310 1.225 1.539 1.510 1.444 121.86 116.54 120.97 110.44 111.52 108.62 122.49 * * * 69 LYS 69 1.306 1.223 1.506 1.531 1.438 122.41 116.58 120.58 109.29 109.66 110.18 122.83 +* * +* 70 THR 70 1.297 1.240 1.524 1.541 1.421 121.92 117.73 119.87 109.78 108.54 110.17 122.40 ** +* ** 71 VAL 71 1.326 1.222 1.517 1.560 1.448 120.70 114.18 121.21 110.21 107.54 111.97 124.49 * * * 72 LYS 72 1.331 1.226 1.533 1.549 1.459 125.60 116.80 120.71 112.06 111.58 107.62 122.48 ** * +* ** 73 ASP 73 1.321 1.237 1.532 1.534 1.467 121.46 115.84 121.49 110.87 110.62 110.73 122.64 Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 TYR 74 1.318 1.239 1.544 1.528 1.438 122.46 115.84 121.23 111.16 110.69 109.81 122.93 * * 75 ARG 75 1.319 1.232 1.518 1.526 1.437 124.26 116.55 120.32 109.83 109.21 108.44 123.12 * * * * 76 SER 76 1.307 1.243 1.543 1.519 1.437 122.05 117.15 120.10 111.48 110.65 108.70 122.75 +* * * +* 77 PRO 77 1.362 1.250 1.531 1.527 1.479 123.97 114.65 121.16 110.24 114.18 103.35 124.15 * * +* +* 78 VAL 78 1.331 1.241 1.527 1.525 1.442 125.28 114.77 122.25 112.01 111.62 112.13 122.87 +* * +* 79 SER 79 1.286 1.249 1.530 1.536 1.433 122.34 116.03 120.95 111.66 110.80 109.85 123.02 *** * *** 80 ASN 80 1.310 1.241 1.510 1.550 1.453 123.06 116.86 120.37 109.21 107.89 110.89 122.74 * * * 81 LEU 81 1.307 1.251 1.521 1.523 1.392 121.90 116.26 120.07 113.30 110.02 109.40 123.66 +* * *** +* *** 82 ALA 82 1.320 1.227 1.496 1.528 1.444 122.93 115.84 120.82 108.27 109.71 111.31 123.34 * * * 83 GLY 83 1.294 1.242 1.508 - 1.441 121.27 114.76 121.73 - 109.60 - 123.51 ** * ** 84 ALA 84 1.309 1.242 1.497 1.517 1.428 123.11 115.94 120.77 110.27 109.97 110.14 123.29 * * +* +* 85 VAL 85 1.298 1.239 1.509 1.545 1.422 121.01 115.34 121.39 109.86 108.69 111.92 123.26 ** +* ** 86 THR 86 1.277 1.237 1.521 1.542 1.419 122.53 117.03 120.40 110.91 107.35 109.56 122.52 +*** ** * * +*** 87 THR 87 1.305 1.243 1.524 1.543 1.428 120.15 115.67 121.03 109.96 111.06 110.11 123.30 +* +* +* 88 MET 88 1.307 1.236 1.494 1.545 1.441 122.14 116.00 120.67 109.88 109.40 112.53 123.31 +* * * +* 89 HIS 89 1.296 1.238 1.485 1.534 1.429 121.52 115.88 120.43 110.03 108.39 112.11 123.66 ** +* +* * ** 90 VAL 90 1.294 1.245 1.496 1.547 1.425 121.17 113.79 121.97 110.01 109.65 112.23 124.24 ** * +* * ** 91 ILE 91 1.275 1.243 1.494 1.565 1.410 123.68 114.86 121.22 111.53 107.64 111.62 123.89 +*** * +** * * * +*** 92 ILE 92 1.290 1.240 1.505 1.551 1.413 121.76 115.40 121.00 109.87 110.31 111.27 123.57 +** ** +** 93 GLN 93 1.296 1.243 1.501 1.533 1.405 122.02 115.73 120.23 112.48 104.90 109.92 124.04 ** * +** * ** +** 94 ALA 94 1.300 1.239 1.503 1.521 1.456 122.60 116.55 120.88 110.48 111.05 110.51 122.53 ** * ** 95 PRO 95 1.333 1.245 1.490 1.521 1.431 122.64 114.69 121.39 109.84 111.79 105.14 123.92 +* ** * +* * ** 96 VAL 96 1.284 1.240 1.508 1.546 1.418 121.47 114.45 121.76 110.81 107.80 112.80 123.66 *** ** * *** 97 THR 97 1.292 1.243 1.509 1.556 1.421 123.31 115.57 120.95 110.15 107.75 110.78 123.44 +** +* * +** 98 GLU 98 1.302 1.242 1.510 1.508 1.426 122.34 115.10 121.07 110.94 109.26 109.79 123.80 +* * +* +* 99 LYS 99 1.293 1.237 1.512 1.543 1.411 123.59 116.32 119.98 111.08 107.03 109.72 123.67 +** ** * * +** 100 GLU 100 1.315 1.235 1.520 1.528 1.454 122.39 115.66 120.28 109.41 111.13 110.48 124.05 * * Residue-by-residue listing for refined_20 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 ----------------------------------------------------------------------------------------------------------------------------------- 101 LYS 101 1.334 - 1.527 1.555 1.454 123.32 - - 112.40 110.43 112.50 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * +* * *** ** +* +* ** +** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 1.275 1.335 1.310 .014 +*** * C-N (Pro) 1.341 .016 6 1.319 1.362 1.339 .013 * * C-O C-O 1.231 .020 100 1.205 1.251 1.235 .009 * * CA-C CH1E-C (except Gly) 1.525 .021 96 1.485 1.560 1.521 .015 +* +* CH2G*-C (Gly) 1.516 .018 5 1.489 1.527 1.510 .012 * CA-CB CH1E-CH3E (Ala) 1.521 .033 8 1.517 1.529 1.522 .004 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 26 1.525 1.576 1.553 .011 * CH1E-CH2E (the rest) 1.530 .020 62 1.508 1.560 1.535 .012 * * N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.392 1.488 1.444 .018 *** +* NH1-CH2G* (Gly) 1.451 .016 5 1.417 1.461 1.442 .014 ** N-CH1E (Pro) 1.466 .015 6 1.431 1.479 1.461 .016 ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_20 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 89 113.79 118.67 116.16 .93 * * CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.76 117.92 116.71 1.14 CH1E-C-N (Pro) 116.9 1.5 6 114.63 117.51 115.35 1.01 +* * O-C-N O-C-NH1 (except Pro) 123.0 1.6 94 121.78 124.77 123.06 .57 * O-C-N (Pro) 122.0 1.4 6 121.98 124.15 123.45 .71 +* * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.88 125.60 122.36 1.27 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 5 121.00 122.34 121.49 .46 * C-N-CH1E (Pro) 122.6 5.0 6 122.16 123.97 122.99 .66 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 95 119.40 122.25 120.76 .57 CH2G*-C-O (Gly) 120.8 2.1 5 119.02 121.73 120.50 .90 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 8 108.27 111.56 110.31 .87 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 26 107.45 112.34 110.28 1.13 * CH2E-CH1E-C (the rest) 110.1 1.9 62 107.09 113.30 110.35 1.32 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.90 115.55 110.07 1.68 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 5 109.60 113.03 111.60 1.56 * N-CH1E-C (Pro) 111.8 2.5 6 111.59 114.62 112.96 1.14 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 8 109.96 111.31 110.50 .43 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 26 109.56 112.80 111.40 .91 * N-CH1E-CH2E (Pro) 103.0 1.1 6 102.37 105.14 103.70 .82 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 56 107.54 115.47 110.64 1.79 +* +** ------------------------------------------------------------------------------------------------------------- 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_20 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] 78 88.6% 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] 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 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 88.6 83.8 10.0 .5 Inside b. Omega angle st dev 100 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 96 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 52 1.0 .8 .2 .9 Inside f. Overall G-factor 101 .0 -.4 .3 1.3 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 11 5.7 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 32 5.8 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 39 7.0 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 82 7.3 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 20 5.3 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% 88.6 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 1.00 3 Residue-by-residue listing for refined_20 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.47 Chi1-chi2 distribution -.20 Chi1 only .11 Chi3 & chi4 .16 Omega .06 ------ -.13 ===== Main-chain covalent forces:- Main-chain bond lengths -.03 Main-chain bond angles .41 ------ .22 ===== OVERALL AVERAGE -.01 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.