Residue-by-residue listing for refined_1 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 - - 181.0 - 181.4 - - - - - - 180.0 - 35.4 - 2 ALA 2 B - - - - - - - - - - 180.4 - 34.0 - 3 ASP 3 B - 179.4 - - - - - - - - 180.4 - 33.9 - 4 THR 4 a 48.0 - - - - - - - - - 179.5 -.6 34.2 - * +* +* 5 GLY 5 - - - - - - - - - - - 180.1 - - - 6 GLU 6 B 61.0 - - - - - - - - - 179.1 - 34.0 - 7 VAL 7 E B - - -59.8 - - - - - - - 180.1 -2.7 33.2 - 8 GLN 8 E B 55.8 - - 183.1 - - - - - - 180.9 - 34.2 - 9 PHE 9 E B - 181.2 - - - - - - - - 178.1 -2.0 35.5 - 10 MET 10 E B - - -62.5 182.9 - - - - - - 179.9 - 34.5 - 11 LYS 11 E B - 190.9 - 196.7 - - - - - - 175.4 -2.4 36.3 - * * 12 PRO 12 E - - - - - -65.6 - - - - - 177.3 - 38.5 - * * 13 PHE 13 e B - 177.9 - - - - - - - - 175.8 -2.4 35.9 - 14 ILE 14 t B - - -58.1 - - - - - - - 187.8 -.7 35.4 - * +* +* 15 SER 15 T A - 188.6 - - - - - - - - 181.4 -.9 33.6 - +* +* 16 GLU 16 T A - 182.4 - 188.5 - - - - - - 186.2 - 35.2 - * * 17 LYS 17 T A - 186.2 - - - - - - - - 184.9 - 35.1 - 18 SER 18 T A - - -55.6 - - - - - - - 168.6 -3.5 32.7 - +* +* +* 19 SER 19 T A - - -59.9 - - - - - - - 182.4 - 35.6 - 20 LYS 20 T a - 178.2 - 177.9 - - - - - - 184.3 -1.4 34.5 - 21 SER 21 t B - - -57.7 - - - - - - - 176.0 -2.1 35.4 - Residue-by-residue listing for refined_1 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 LEU 22 E B - - -72.7 179.4 - - - - - - 172.3 -2.4 33.3 - * * 23 GLU 23 E B - 166.9 - 167.5 - - - - - - 180.3 - 33.2 - 24 ILE 24 e B - - -55.0 - - - - - - - 177.2 -1.4 34.9 - 25 PRO 25 h - - - - - -56.2 - - - - - 185.9 - 38.7 - * * * 26 LEU 26 H A - 192.1 - 170.3 - -54.2 -39.0 - - - 180.4 - 32.8 - 27 GLY 27 H - - - - - - -59.5 -35.3 - - - 180.7 - - - 28 PHE 28 H A - 189.6 - - - -88.4 -25.1 - - - 176.9 -1.4 33.0 - +* * +* 29 ASN 29 H A - - -63.8 - - -62.7 -46.3 - - - 181.9 -2.0 35.5 - 30 GLU 30 h A - 182.1 - 182.4 - - - - - - 185.0 -2.6 35.4 - 31 TYR 31 T A - 176.6 - - - - - - - - 184.0 - 33.7 - 32 PHE 32 t b 62.1 - - - - - - - - - 169.6 -.8 28.8 - +* +* * +* 33 PRO 33 - - - - - -57.0 - - - - - 184.9 - 38.1 - * * 34 ALA 34 B - - - - - - - - - - 167.7 - 35.8 - ** ** 35 PRO 35 S - - - - - -56.5 - - - - - 188.1 - 39.2 - * +* +* 36 PHE 36 B 69.2 - - - - - - - - - 180.7 - 32.0 - 37 PRO 37 - - - - - -96.8 - - - - - 174.6 - 40.5 - +** +* +** 38 ILE 38 e A - - -59.1 - - - - - - - 181.6 - 33.3 - 39 THR 39 E B 57.0 - - - - - - - - - 173.8 - 34.5 - * * 40 VAL 40 E B 58.6 - - - - - - - - - 186.9 -3.0 33.3 - * * * 41 ASP 41 E B - 189.7 - - - - - - - - 181.8 -1.4 33.5 - 42 LEU 42 E B - - -56.6 180.7 - - - - - - 180.5 -3.1 35.5 - * * 43 LEU 43 E B - - -66.5 - - - - - - - 173.6 -2.4 33.9 - * * 44 ASP 44 e B - 181.0 - - - - - - - - 184.9 -1.6 35.6 - 45 TYR 45 S A - - -63.4 - - - - - - - 180.1 - 32.5 - 46 SER 46 S A - 183.0 - - - - - - - - 178.7 - 32.8 - 47 GLY 47 S - - - - - - - - - - - 184.0 - - - 48 ARG 48 e B - - -58.9 196.6 - - - - - - 180.8 - 29.4 - * * * 49 SER 49 E B - - -55.6 - - - - - - - 183.1 - 34.3 - 50 TRP 50 E B - - -53.4 - - - - - - - 174.9 -2.8 35.7 - * * 51 THR 51 E B - - -53.4 - - - - - - - 185.7 - 34.3 - 52 VAL 52 E B - - -55.6 - - - - - - - 181.6 -2.6 32.6 - 53 ARG 53 E B - - -69.0 180.1 - - - - - - 182.5 - 33.5 - 54 MET 54 E B - 181.9 - 181.6 - - - - - - 180.8 -.6 35.0 - +* +* 55 LYS 55 E B - 190.5 - - - - - - - - 173.3 -3.2 36.6 - * +* +* 56 LYS 56 E B - - -62.5 - - - - - - - 181.7 - 36.1 - 57 ARG 57 E b - 202.7 - - - - - - - - 177.7 -2.5 34.5 - * * 58 GLY 58 T - - - - - - - - - - - 185.0 - - - 59 GLU 59 T A 57.7 - - 180.7 - - - - - - 187.4 - 36.3 - * * 60 LYS 60 E B - 189.4 - 172.8 - - - - - - 177.5 -2.7 33.7 - Residue-by-residue listing for refined_1 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 61 VAL 61 E B - 179.9 - - - - - - - - 178.5 - 35.3 - 62 PHE 62 E B - - -56.9 - - - - - - - 168.9 -2.7 37.0 - +* +* 63 LEU 63 E B - - -65.8 - - - - - - - 189.4 -2.1 30.5 - +* +* 64 THR 64 e b - 182.7 - - - - - - - - 184.1 -1.3 34.2 - 65 VAL 65 T B - 181.5 - - - - - - - - 190.8 - 33.3 - +* +* 66 GLY 66 h - - - - - - - - - - - 175.2 - - - 67 TRP 67 H A - 171.1 - - - -65.5 -24.9 - - - 181.5 -2.5 34.0 - * * 68 GLU 68 H A - 183.8 - 184.5 - -61.3 -30.3 - - - 176.2 - 33.3 - 69 ASN 69 H A - - -63.6 - - -58.6 -44.6 - - - 183.9 -1.0 34.8 - * * 70 PHE 70 H A - 183.3 - - - -73.0 -46.5 - - - 184.9 -.6 35.1 - +* +* 71 VAL 71 H A 71.3 - - - - -62.8 -43.2 - - - 179.1 -2.6 32.6 - 72 LYS 72 H A - 192.4 - - - -72.1 -43.2 - - - 185.0 -2.5 34.1 - 73 ASP 73 H A - 173.7 - - - -75.9 -40.4 - - - 181.7 -2.5 32.4 - 74 ASN 74 H A - 190.0 - - - -86.2 -21.0 - - - 181.8 -3.3 34.1 - +* +* +* +* 75 ASN 75 h ~l - 178.8 - - - - - - - - 181.4 -.9 32.6 - ** +* ** 76 LEU 76 t B 63.7 - - 171.4 - - - - - - 178.0 -.9 32.1 - +* +* 77 GLU 77 t B 53.2 - - - - - - - - - 181.4 - 32.3 - 78 ASP 78 T B - 185.6 - - - - - - - - 177.4 - 35.8 - 79 GLY 79 T - - - - - - - - - - - 177.9 -1.6 - - 80 LYS 80 e B - - -64.3 185.5 - - - - - - 183.1 -1.0 31.8 - * * 81 TYR 81 E B - - -69.4 - - - - - - - 181.2 - 33.5 - 82 LEU 82 E B - - -63.5 - - - - - - - 177.8 -1.9 34.2 - 83 GLN 83 E B - - -59.2 181.2 - - - - - - 179.5 -3.2 36.3 - +* +* 84 PHE 84 E B - - -60.7 - - - - - - - 176.6 -3.2 34.8 - +* +* 85 ILE 85 E B - - -58.5 178.4 - - - - - - 181.6 -2.5 33.8 - 86 TYR 86 E B - 176.6 - - - - - - - - 181.4 -3.2 37.2 - +* +* 87 ASP 87 e b - 178.1 - - - - - - - - 170.8 -1.2 31.1 - +* * +* 88 ARG 88 S L - - -56.8 - - - - - - - 182.9 -.5 35.8 - ** ** 89 ASP 89 S b - 190.9 - - - - - - - - 179.1 - 36.2 - 90 ARG 90 e a - 185.1 - 177.9 - - - - - - 180.1 - 37.0 - 91 THR 91 E B - - -58.9 - - - - - - - 179.5 - 36.0 - 92 PHE 92 E B - - -66.5 - - - - - - - 174.6 -2.5 34.3 - 93 TYR 93 E B - - -57.5 - - - - - - - 186.9 -2.0 34.7 - * * 94 VAL 94 E B - 182.1 - - - - - - - - 174.5 -2.8 34.1 - 95 ILE 95 E B - - -54.9 176.3 - - - - - - 182.1 -2.4 35.0 - 96 ILE 96 E B - 178.3 - 180.5 - - - - - - 174.9 -.5 34.3 - ** ** 97 TYR 97 e B - - -62.4 - - - - - - - 182.2 -2.4 33.9 - 98 GLY 98 S - - - - - - - - - - - 179.4 -.8 - - +* +* 99 HIS 99 B 56.0 - - - - - - - - - 181.1 - 31.6 - Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 ASN 100 B - 180.4 - - - - - - - - 180.5 -.7 33.3 - +* +* 101 MET 101 A - 181.5 - 177.4 - - - - - - 180.5 - 34.2 - 102 CYS 102 - - 184.1 - - - - - - - - - - 34.1 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * * +** +* +* ** ** +* +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.5 183.2 -60.5 180.6 -66.4 -68.3 -36.6 - - - 180.1 -2.0 34.4 Standard deviations: 6.5 6.5 4.8 6.8 17.4 10.9 9.1 - - - 4.5 .9 1.9 Numbers of values: 12 41 35 25 5 12 12 0 0 0 101 56 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_1 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 - 1.226 1.510 1.538 1.459 - 117.29 119.44 110.04 108.10 109.72 123.27 * * 2 ALA 2 1.326 1.235 1.520 1.523 1.456 121.72 116.41 120.67 110.37 110.52 110.52 122.91 3 ASP 3 1.303 1.237 1.506 1.533 1.446 121.93 115.86 120.83 110.53 110.00 111.03 123.29 +* +* 4 THR 4 1.306 1.242 1.531 1.531 1.409 122.40 116.09 120.64 111.74 110.97 109.08 123.21 +* +** * * +** 5 GLY 5 1.307 1.234 1.494 - 1.440 121.07 114.64 121.51 - 111.74 - 123.85 +* * +* 6 GLU 6 1.271 1.238 1.518 1.550 1.439 123.24 116.68 120.56 109.68 109.73 111.90 122.76 **** **** 7 VAL 7 1.309 1.235 1.515 1.562 1.448 121.60 116.76 120.48 110.05 109.58 112.89 122.75 * * 8 GLN 8 1.300 1.237 1.520 1.517 1.424 121.95 116.58 120.61 111.55 110.28 109.30 122.79 ** +* ** 9 PHE 9 1.303 1.231 1.523 1.545 1.446 121.90 116.85 120.12 111.04 109.43 108.31 123.02 +* * +* 10 MET 10 1.316 1.235 1.503 1.538 1.458 122.14 116.97 120.42 108.64 109.03 112.36 122.61 * * * 11 LYS 11 1.305 1.248 1.520 1.523 1.439 119.95 117.63 119.85 107.40 110.08 110.38 122.51 +* * +* 12 PRO 12 1.338 1.247 1.533 1.538 1.460 122.85 116.14 121.16 110.25 111.08 104.09 122.57 Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 PHE 13 1.291 1.240 1.530 1.544 1.433 121.74 117.59 119.90 110.86 109.12 108.07 122.50 +** * * +** 14 ILE 14 1.340 1.229 1.495 1.560 1.424 120.73 116.89 119.51 110.19 105.07 111.08 123.57 * +* ** ** 15 SER 15 1.324 1.215 1.508 1.526 1.459 121.75 115.97 120.29 110.10 111.40 111.24 123.63 16 GLU 16 1.318 1.229 1.517 1.529 1.440 123.10 116.92 120.53 108.91 110.64 110.53 122.48 17 LYS 17 1.330 1.232 1.496 1.536 1.445 119.60 114.78 121.58 110.22 109.15 109.93 123.49 * * * 18 SER 18 1.296 1.224 1.526 1.505 1.411 122.11 116.71 120.34 113.27 112.51 108.93 122.95 ** * ** +* ** 19 SER 19 1.345 1.244 1.530 1.545 1.460 120.42 115.29 121.23 107.81 108.20 111.63 123.47 * * * * 20 LYS 20 1.338 1.232 1.533 1.535 1.444 121.72 117.71 120.48 110.34 112.51 109.48 121.80 21 SER 21 1.319 1.226 1.543 1.536 1.450 120.21 116.98 120.92 109.90 112.21 108.68 122.10 * * 22 LEU 22 1.316 1.238 1.481 1.528 1.450 120.74 114.55 121.13 107.33 111.69 114.49 124.32 ** * ** ** 23 GLU 23 1.288 1.238 1.521 1.532 1.408 122.43 115.80 120.78 112.32 108.81 110.72 123.34 +** +** * +** 24 ILE 24 1.308 1.246 1.549 1.558 1.441 122.05 117.79 119.92 109.90 109.51 110.46 122.19 +* * +* 25 PRO 25 1.366 1.246 1.534 1.533 1.477 123.21 115.63 120.77 110.22 112.06 103.43 123.56 +* * +* 26 LEU 26 1.335 1.238 1.539 1.564 1.471 123.99 116.68 120.35 113.04 111.76 109.46 122.93 +* * +* +* 27 GLY 27 1.323 1.239 1.522 - 1.455 121.38 116.64 120.79 - 112.92 - 122.55 28 PHE 28 1.318 1.221 1.535 1.541 1.445 120.88 116.18 121.00 112.30 109.50 110.54 122.77 * * 29 ASN 29 1.333 1.233 1.503 1.539 1.481 122.24 114.53 121.60 107.28 110.05 111.78 123.85 * * * * 30 GLU 30 1.312 1.241 1.543 1.542 1.445 123.53 116.06 121.02 110.81 110.62 108.31 122.88 * * * * 31 TYR 31 1.325 1.241 1.533 1.550 1.445 122.10 118.66 119.80 110.41 113.29 110.32 121.51 * * 32 PHE 32 1.326 1.233 1.546 1.564 1.457 117.65 118.41 120.63 112.76 116.32 112.70 120.78 * +* ** * * +* * * ** 33 PRO 33 1.358 1.249 1.508 1.513 1.454 121.98 114.30 121.79 109.64 111.01 105.14 123.91 * +* +* * +* 34 ALA 34 1.278 1.242 1.502 1.523 1.435 122.93 119.20 118.74 109.85 108.62 109.20 122.01 +*** * * +* * +*** 35 PRO 35 1.345 1.250 1.535 1.535 1.462 121.15 118.69 119.10 110.48 106.67 103.29 122.21 * * ** ** 36 PHE 36 1.322 1.240 1.537 1.536 1.412 120.03 116.24 121.60 112.45 111.68 111.22 122.05 ** * ** 37 PRO 37 1.329 1.242 1.515 1.509 1.442 123.65 115.71 121.33 109.02 112.73 102.00 122.93 * +* +* 38 ILE 38 1.295 1.231 1.528 1.555 1.431 121.30 116.54 120.77 110.70 109.25 112.14 122.64 ** * ** 39 THR 39 1.323 1.232 1.531 1.553 1.444 121.73 115.12 121.17 108.78 111.92 111.37 123.70 40 VAL 40 1.305 1.236 1.530 1.571 1.441 124.93 118.09 119.97 111.94 106.14 112.00 121.89 +* * +* * +* +* 41 ASP 41 1.297 1.244 1.520 1.528 1.450 119.52 115.72 120.65 111.96 111.17 109.53 123.60 ** * ** 42 LEU 42 1.323 1.242 1.518 1.536 1.452 122.94 116.37 120.58 108.73 109.95 110.40 123.05 Residue-by-residue listing for refined_1 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 LEU 43 1.309 1.242 1.515 1.552 1.455 121.69 114.94 121.08 108.52 111.90 112.45 123.97 * * * * 44 ASP 44 1.314 1.239 1.513 1.533 1.447 124.17 117.98 119.62 109.78 105.91 110.23 122.39 * * +* +* 45 TYR 45 1.295 1.235 1.523 1.530 1.450 120.71 117.99 120.05 110.74 113.28 111.47 121.96 ** ** 46 SER 46 1.316 1.235 1.521 1.534 1.439 119.89 117.13 120.24 111.30 110.91 111.49 122.63 * * * 47 GLY 47 1.324 1.225 1.510 - 1.439 118.86 117.85 119.99 - 114.18 - 122.15 * * 48 ARG 48 1.321 1.232 1.503 1.529 1.461 119.89 115.52 121.45 111.74 113.10 114.45 122.92 * * ** ** 49 SER 49 1.295 1.240 1.522 1.532 1.447 121.92 116.94 120.31 111.39 109.29 109.67 122.74 ** ** 50 TRP 50 1.313 1.230 1.511 1.546 1.447 121.27 116.91 120.51 108.41 109.93 110.69 122.58 * * 51 THR 51 1.295 1.238 1.526 1.533 1.420 120.33 115.87 121.22 111.02 107.19 110.85 122.89 ** ** * ** 52 VAL 52 1.295 1.226 1.521 1.569 1.437 122.41 117.56 120.40 111.58 109.66 112.29 121.99 ** * * * ** 53 ARG 53 1.295 1.216 1.507 1.534 1.440 120.24 115.74 121.03 111.47 110.50 110.56 123.21 ** ** 54 MET 54 1.311 1.229 1.500 1.530 1.449 122.35 116.30 120.60 109.45 109.42 110.66 123.10 * * * 55 LYS 55 1.291 1.233 1.513 1.526 1.414 121.84 116.32 120.54 108.94 108.90 108.98 123.11 +** ** +** 56 LYS 56 1.301 1.229 1.483 1.515 1.433 121.43 117.24 119.87 107.37 105.67 111.90 122.88 +* +* * * +* +* 57 ARG 57 1.270 1.234 1.524 1.554 1.428 119.97 115.56 120.77 111.51 108.72 109.78 123.63 **** * +* **** 58 GLY 58 1.317 1.237 1.516 - 1.448 122.70 115.26 121.06 - 114.32 - 123.65 * * 59 GLU 59 1.309 1.235 1.528 1.534 1.456 123.37 117.83 120.36 108.64 112.19 108.66 121.81 * * * 60 LYS 60 1.316 1.236 1.526 1.535 1.432 118.52 115.15 121.30 112.41 112.90 108.38 123.50 * +* * * +* 61 VAL 61 1.313 1.239 1.507 1.557 1.436 123.32 116.20 120.71 108.76 108.24 111.59 123.08 * * * * 62 PHE 62 1.293 1.228 1.498 1.541 1.428 121.41 117.94 119.92 106.86 108.35 110.78 122.13 +** * +* +* * +** 63 LEU 63 1.293 1.211 1.497 1.552 1.449 118.15 114.82 120.93 112.30 107.29 115.21 124.25 +** * * +* * * +** +** 64 THR 64 1.300 1.250 1.556 1.586 1.441 124.56 116.28 120.56 112.66 111.27 108.41 123.15 ** * +* +* +* +* ** 65 VAL 65 1.335 1.218 1.504 1.551 1.452 123.48 114.45 121.79 110.57 109.14 112.21 123.75 66 GLY 66 1.273 1.220 1.471 - 1.405 122.06 114.77 121.53 - 107.24 - 123.68 +*** +** +** +* +*** 67 TRP 67 1.331 1.241 1.515 1.540 1.445 122.12 115.24 121.34 110.20 109.61 111.29 123.36 68 GLU 68 1.317 1.222 1.540 1.528 1.446 121.54 115.70 121.06 111.12 109.38 111.22 123.19 69 ASN 69 1.331 1.198 1.501 1.545 1.463 123.09 116.03 120.52 108.52 109.74 111.81 123.34 +* * +* 70 PHE 70 1.315 1.228 1.507 1.548 1.448 123.08 116.49 120.27 109.48 110.01 110.42 123.24 71 VAL 71 1.327 1.238 1.512 1.572 1.453 120.85 114.67 121.58 111.03 110.09 112.62 123.74 * * Residue-by-residue listing for refined_1 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.297 1.227 1.547 1.542 1.424 122.97 117.09 120.62 113.52 110.30 107.69 122.25 ** * +* +* +* ** 73 ASP 73 1.333 1.229 1.521 1.532 1.483 120.67 117.70 120.36 110.65 114.21 111.09 121.93 * * * 74 ASN 74 1.301 1.231 1.526 1.556 1.455 119.76 115.11 121.06 111.95 108.61 109.83 123.61 +* * * +* 75 ASN 75 1.342 1.233 1.535 1.551 1.481 123.95 117.14 121.10 110.92 111.62 111.65 121.74 * * * * 76 LEU 76 1.317 1.239 1.511 1.558 1.452 120.22 114.93 121.28 110.17 111.97 113.27 123.78 * +* +* 77 GLU 77 1.306 1.242 1.518 1.548 1.434 123.45 114.99 120.83 110.85 111.17 112.59 124.18 +* * * +* 78 ASP 78 1.316 1.243 1.526 1.528 1.464 124.52 116.25 120.95 108.84 111.98 109.07 122.80 +* +* 79 GLY 79 1.313 1.229 1.506 - 1.445 120.39 117.04 120.37 - 113.42 - 122.57 * * 80 LYS 80 1.312 1.247 1.514 1.530 1.449 120.07 116.01 120.79 111.49 111.38 112.35 123.20 * * * 81 TYR 81 1.314 1.245 1.481 1.534 1.427 122.26 115.21 120.94 110.58 109.47 112.00 123.81 * ** +* ** 82 LEU 82 1.293 1.245 1.502 1.554 1.419 121.63 115.44 120.50 109.68 109.29 112.06 124.07 +** * * ** +** 83 GLN 83 1.297 1.236 1.486 1.525 1.428 122.99 115.85 120.39 107.37 107.31 111.38 123.75 ** +* +* * * ** 84 PHE 84 1.285 1.237 1.497 1.535 1.420 121.90 116.10 120.66 110.15 108.67 110.66 123.18 *** * +* *** 85 ILE 85 1.296 1.231 1.510 1.555 1.429 121.15 115.63 120.68 110.14 108.34 112.31 123.69 ** +* * ** 86 TYR 86 1.292 1.237 1.506 1.546 1.434 123.49 116.80 120.38 110.24 107.18 107.42 122.82 +** * * +* +** 87 ASP 87 1.306 1.230 1.501 1.542 1.442 120.03 114.77 121.06 111.59 112.86 112.79 123.92 +* * * +* 88 ARG 88 1.333 1.234 1.538 1.531 1.476 123.97 117.52 120.34 109.53 113.30 107.92 122.12 * +* +* 89 ASP 89 1.310 1.226 1.503 1.564 1.424 121.49 115.16 120.82 109.87 106.95 109.62 123.92 * * +* +* +* +* 90 ARG 90 1.265 1.235 1.542 1.525 1.430 125.78 114.28 122.64 111.44 106.17 106.13 123.07 *4.6* * ** * +* +** *4.6* 91 THR 91 1.303 1.241 1.536 1.545 1.426 123.60 116.92 120.07 109.57 108.80 109.38 123.00 +* +* * * +* 92 PHE 92 1.321 1.233 1.514 1.541 1.452 121.77 115.83 121.09 108.51 110.85 112.19 123.07 93 TYR 93 1.297 1.238 1.507 1.527 1.441 121.87 117.17 119.75 110.52 106.58 110.83 123.06 ** +* ** 94 VAL 94 1.309 1.231 1.520 1.552 1.446 120.81 115.60 121.13 109.29 112.34 111.31 123.27 * * 95 ILE 95 1.310 1.222 1.527 1.557 1.449 122.34 117.33 120.21 109.02 107.12 111.88 122.44 * * * 96 ILE 96 1.297 1.243 1.518 1.566 1.457 121.70 115.69 120.94 110.27 110.68 110.68 123.32 ** ** 97 TYR 97 1.311 1.238 1.502 1.525 1.437 121.67 115.67 120.81 110.26 108.55 111.70 123.48 * * * * 98 GLY 98 1.299 1.227 1.500 - 1.423 120.62 116.08 121.09 - 110.38 - 122.81 ** +* ** 99 HIS 99 1.301 1.230 1.516 1.563 1.442 121.62 115.98 120.97 112.63 110.39 112.22 123.02 +* +* * * +* Residue-by-residue listing for refined_1 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 1.311 1.227 1.515 1.539 1.452 121.80 115.80 120.86 110.69 110.91 111.38 123.34 * * 101 MET 101 1.308 1.238 1.535 1.542 1.448 122.22 115.87 121.57 111.75 110.11 109.27 122.55 * * 102 CYS 102 1.309 - 1.529 1.540 1.436 121.76 - - 111.46 109.23 110.05 - * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *4.6* +* +** +* +** ** +* * +* ** +** * *4.6* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 1.265 1.345 1.309 .016 *4.6* * * C-N (Pro) 1.341 .016 5 1.329 1.366 1.347 .013 +* C-O C-O 1.231 .020 101 1.198 1.250 1.234 .009 +* CA-C CH1E-C (except Gly) 1.525 .021 95 1.481 1.556 1.518 .016 ** * CH2G*-C (Gly) 1.516 .018 7 1.471 1.522 1.503 .016 +** CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.523 1.523 1.523 .000 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.531 1.586 1.557 .013 +* CH1E-CH2E (the rest) 1.530 .020 75 1.505 1.564 1.537 .012 * +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.408 1.483 1.443 .015 +** * NH1-CH2G* (Gly) 1.451 .016 7 1.405 1.455 1.436 .016 +** N-CH1E (Pro) 1.466 .015 5 1.442 1.477 1.459 .012 +* ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_1 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 89 114.28 119.20 116.32 1.05 +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.64 117.85 116.04 1.12 CH1E-C-N (Pro) 116.9 1.5 5 114.30 118.69 116.09 1.44 +* * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.78 124.32 122.99 .68 * O-C-N (Pro) 122.0 1.4 5 122.21 123.91 123.03 .63 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.65 125.78 121.80 1.48 ** ** C-NH1-CH2G* (Gly) 120.6 1.7 7 118.86 122.70 121.01 1.15 * * C-N-CH1E (Pro) 122.6 5.0 5 121.15 123.65 122.57 .90 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.74 122.64 120.67 .61 * * CH2G*-C-O (Gly) 120.8 2.1 7 119.99 121.53 120.91 .53 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 109.85 110.37 110.11 .26 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 108.76 112.66 110.40 1.09 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 106.86 113.52 110.32 1.54 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 105.07 116.32 109.97 2.03 ** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 107.24 114.32 112.03 2.34 +* N-CH1E-C (Pro) 111.8 2.5 5 106.67 112.73 110.71 2.12 ** N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.20 110.52 109.86 .66 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.41 112.89 111.25 1.22 +* N-CH1E-CH2E (Pro) 103.0 1.1 5 102.00 105.14 103.59 1.03 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.13 115.21 110.66 1.69 +** +** ------------------------------------------------------------------------------------------------------------- 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_1 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] 79 89.8% Residues in additional allowed regions [a,b,l,p] 8 9.1% 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 89.8 83.8 10.0 .6 Inside b. Omega angle st dev 101 4.5 6.0 3.0 -.5 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 56 .9 .8 .2 .4 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 12 6.5 18.1 6.5 -1.8 BETTER b. Chi-1 trans st dev 41 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 35 4.8 17.5 4.9 -2.6 BETTER d. Chi-1 pooled st dev 88 7.3 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 25 6.8 20.4 5.0 -2.7 BETTER M O R R I S E T A L . C L A S S I F I C A T I O N Mean St.dev Classification Parameter m s 1 2 3 4 Value Class --------- ---- --- ------------------------------------ ----- ----- Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 89.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 7.9 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3 Residue-by-residue listing for refined_1 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.48 Chi1-chi2 distribution -.11 Chi1 only -.19 Chi3 & chi4 .34 Omega -.23 ------ -.21 ===== Main-chain covalent forces:- Main-chain bond lengths -.13 Main-chain bond angles .35 ------ .15 ===== OVERALL AVERAGE -.09 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.