Residue-by-residue listing for refined_2 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 - 63.0 - - 178.7 - - - - - - 181.1 - 33.9 - 2 ALA 2 l - - - - - - - - - - 178.3 - 31.1 - 3 ASP 3 B - 180.7 - - - - - - - - 179.0 - 34.9 - 4 THR 4 A - - -57.3 - - - - - - - 179.5 - 34.1 - 5 GLY 5 - - - - - - - - - - - 181.0 - - - 6 GLU 6 b - 180.1 - 184.8 - - - - - - 175.1 -2.2 35.4 - 7 VAL 7 E B - - -64.2 - - - - - - - 187.4 -2.0 32.2 - * * 8 GLN 8 E B 64.6 - - - - - - - - - 175.3 - 34.3 - 9 PHE 9 E B - 171.7 - - - - - - - - 182.4 -2.7 35.9 - 10 MET 10 E B - 183.5 - - - - - - - - 174.3 - 35.0 - 11 LYS 11 E B 65.2 - - 165.2 - - - - - - 168.9 -1.4 33.7 - +* +* 12 PRO 12 E - - - - - -77.1 - - - - - 181.0 - 39.8 - * +* +* 13 PHE 13 e B 63.7 - - - - - - - - - 181.3 -.9 32.3 - * * 14 ILE 14 h B - - -63.0 - - - - - - - 186.9 - 34.1 - * * 15 SER 15 H A - - -53.7 - - -53.4 -25.3 - - - 180.8 -.6 34.0 - * +* +* 16 GLU 16 H A - 181.3 - 178.6 - -60.7 -40.5 - - - 177.1 - 34.9 - 17 LYS 17 H A - - -67.0 - - -103.0 -36.8 - - - 187.7 -2.1 33.2 - *** * *** 18 SER 18 H A 62.2 - - - - -66.0 -8.1 - - - 173.6 -3.2 32.9 - +** * +* +** 19 SER 19 h A - - -61.0 - - - - - - - 181.9 -1.0 33.2 - * * Residue-by-residue listing for refined_2 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 20 LYS 20 T a - - -63.3 - - - - - - - 188.3 -2.9 35.1 - * * * 21 SER 21 t B 54.4 - - - - - - - - - 179.6 -3.5 35.7 - +* +* 22 LEU 22 E B - 186.7 - - - - - - - - 181.7 -3.2 34.0 - +* +* 23 GLU 23 E B - - -30.0 - - - - - - - 177.6 - 35.6 - ** ** 24 ILE 24 E B - - -55.5 178.0 - - - - - - 179.8 -1.5 34.5 - 25 PRO 25 h - - - - - -57.2 - - - - - 180.6 - 38.8 - * * 26 LEU 26 H A - 190.5 - 171.4 - -62.7 -33.9 - - - 177.6 - 34.7 - 27 GLY 27 H - - - - - - -59.2 -36.0 - - - 179.9 - - - 28 PHE 28 H A - 188.5 - - - -80.1 -20.5 - - - 173.3 -.8 32.7 - * +* * +* +* 29 ASN 29 H A - 176.6 - - - -66.5 -43.3 - - - 178.2 -1.0 34.1 - * * 30 GLU 30 h A - - -61.5 185.3 - - - - - - 177.9 -2.1 33.3 - 31 TYR 31 T A - 186.2 - - - - - - - - 177.9 - 34.0 - 32 PHE 32 t b 66.7 - - - - - - - - - 174.2 -1.6 32.2 - 33 PRO 33 - - - - - -78.0 - - - - - 184.7 - 38.3 - * * * 34 ALA 34 B - - - - - - - - - - 172.8 - 35.1 - * * 35 PRO 35 - - - - - -63.6 - - - - - 184.0 - 39.1 - * * 36 PHE 36 B 62.7 - - - - - - - - - 176.2 - 32.6 - 37 PRO 37 - - - - - -78.7 - - - - - 178.7 - 38.6 - * * * 38 ILE 38 S A - - -57.4 - - - - - - - 179.1 - 34.2 - 39 THR 39 B - - -50.4 - - - - - - - 177.1 - 36.1 - * * 40 VAL 40 E B - - -61.0 - - - - - - - 180.3 -3.2 32.3 - +* +* 41 ASP 41 E B - - -67.5 - - - - - - - 176.7 -.9 33.5 - +* +* 42 LEU 42 E B - - -60.8 181.3 - - - - - - 180.7 -3.3 34.9 - +* +* 43 LEU 43 E B - - -59.2 179.9 - - - - - - 180.8 -3.8 34.4 - ** ** 44 ASP 44 E B - 162.9 - - - - - - - - 183.2 -2.6 34.3 - * * 45 TYR 45 e A - 183.1 - - - - - - - - 179.5 -1.3 34.5 - 46 SER 46 S A - - -55.0 - - - - - - - 178.3 - 33.6 - 47 GLY 47 S - - - - - - - - - - - 180.6 - - - 48 ARG 48 e B - - -59.6 180.8 - - - - - - 179.3 - 32.9 - 49 SER 49 E B 54.6 - - - - - - - - - 180.2 - 34.6 - 50 TRP 50 E B - - -55.6 - - - - - - - 177.2 -3.3 35.0 - +* +* 51 THR 51 E B - - -56.9 - - - - - - - 185.8 - 34.7 - * * 52 VAL 52 E B - - -57.2 - - - - - - - 181.2 -2.4 34.0 - 53 ARG 53 e B - 189.2 - 160.9 - - - - - - 181.4 -2.2 32.9 - 54 MET 54 E B - 178.1 - - - - - - - - 182.8 -.5 34.2 - ** ** 55 LYS 55 E B - - -65.5 176.2 - - - - - - 169.3 -2.8 36.2 - +* +* Residue-by-residue listing for refined_2 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 - - -55.6 - - - - - - - 190.0 - 36.2 - +* +* 57 ARG 57 E b - 187.7 - 183.8 - - - - - - 178.9 -2.7 35.3 - 58 GLY 58 T - - - - - - - - - - - 181.5 - - - 59 GLU 59 T A 64.3 - - - - - - - - - 182.9 -.6 34.1 - +* +* 60 LYS 60 E B - 181.6 - 185.3 - - - - - - 172.5 -2.2 35.7 - * * 61 VAL 61 E B - - -59.6 - - - - - - - 186.4 -.8 31.5 - * +* +* 62 PHE 62 E B - 188.5 - - - - - - - - 176.1 -2.4 36.1 - 63 LEU 63 E B - 191.5 - 171.6 - - - - - - 189.4 -2.7 34.1 - +* +* 64 THR 64 e b - 180.6 - - - - - - - - 187.0 -2.0 33.6 - * * 65 VAL 65 T B - - -64.3 - - - - - - - 183.3 - 32.7 - 66 GLY 66 h - - - - - - - - - - - 177.1 - - - 67 TRP 67 H A - 170.6 - - - -54.6 -27.1 - - - 184.5 -1.5 35.5 - * * 68 GLU 68 H A 60.7 - - 179.9 - -63.8 -26.6 - - - 178.4 -.6 31.2 - * +* +* 69 ASN 69 H A - - -64.7 - - -61.5 -37.8 - - - 182.2 -2.0 33.7 - 70 PHE 70 H A - 175.7 - - - -73.9 -48.2 - - - 182.8 -1.0 34.3 - * * 71 VAL 71 H A 72.9 - - - - -65.6 -42.2 - - - 178.4 -1.9 33.0 - 72 LYS 72 H A - - -62.0 178.4 - -71.3 -39.8 - - - 183.7 -2.8 32.6 - 73 ASP 73 H A - 179.6 - - - -71.8 -38.6 - - - 181.1 -2.0 32.0 - 74 ASN 74 H A - - -70.4 - - -95.6 .2 - - - 181.1 -2.5 32.0 - +** +*** +*** 75 ASN 75 h l - 184.8 - - - - - - - - 186.9 -.6 32.6 - * +* +* 76 LEU 76 t B - - -60.9 178.4 - - - - - - 175.6 -1.9 34.5 - 77 GLU 77 t B 54.5 - - 174.7 - - - - - - 180.2 - 34.3 - 78 ASP 78 T B 61.6 - - - - - - - - - 183.4 - 31.8 - 79 GLY 79 T - - - - - - - - - - - 175.2 - - - 80 LYS 80 e B - - -65.5 181.5 - - - - - - 185.4 -1.5 32.5 - 81 TYR 81 E B - - -49.6 - - - - - - - 178.3 -.8 35.7 - * +* +* 82 LEU 82 E B - - -54.0 - - - - - - - 171.8 -1.9 34.8 - * * 83 GLN 83 E B - 187.7 - 184.7 - - - - - - 179.0 -2.4 35.8 - 84 PHE 84 E B - - -59.5 - - - - - - - 179.1 -3.4 36.1 - +* +* 85 ILE 85 E B - - -53.9 179.2 - - - - - - 173.6 -2.9 36.1 - * * * 86 TYR 86 E B 73.1 - - - - - - - - - 181.2 -2.9 30.3 - * * * 87 ASP 87 e a - 178.9 - - - - - - - - 178.5 -.6 33.0 - +* +* 88 ARG 88 S a - - -67.7 - - - - - - - 185.3 - 34.9 - 89 ASP 89 S b - 186.4 - - - - - - - - 182.2 - 34.8 - 90 ARG 90 e a 39.0 - - - - - - - - - 174.5 - 32.5 - +* +* 91 THR 91 E B - 186.2 - - - - - - - - 183.8 - 32.5 - 92 PHE 92 E B - - -59.0 - - - - - - - 175.5 -2.7 35.2 - 93 TYR 93 E B - - -53.9 - - - - - - - 186.2 -3.6 35.7 - * ** ** Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 94 VAL 94 E B - 184.2 - - - - - - - - 175.1 -3.6 34.0 - ** ** 95 ILE 95 E B - - -58.0 177.5 - - - - - - 183.3 -2.2 34.7 - 96 ILE 96 E B - - -60.0 - - - - - - - 178.2 - 33.3 - 97 TYR 97 E B - - -65.9 - - - - - - - 176.8 -3.5 36.3 - +* +* 98 GLY 98 - - - - - - - - - - - 178.3 - - - 99 HIS 99 S a - 182.5 - - - - - - - - 184.6 - 33.5 - 100 ASN 100 S A - - -60.6 - - - - - - - 179.2 - 34.2 - 101 MET 101 ~b - 183.3 - 178.1 - - - - - - 170.4 - 35.3 - ** +* ** 102 CYS 102 - - - -63.2 - - - - - - - - - 34.6 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** +* * ** * *** +*** +* ** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 61.5 182.3 -59.3 178.1 -70.9 -69.4 -31.5 - - - 179.9 -2.1 34.3 Standard deviations: 8.1 6.3 6.7 6.0 9.9 13.6 13.1 - - - 4.4 1.0 1.7 Numbers of values: 16 30 42 24 5 16 16 0 0 0 101 58 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_2 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 - 1.237 1.529 1.543 1.475 - 116.19 120.34 109.79 110.94 111.26 123.47 2 ALA 2 1.342 1.243 1.520 1.531 1.460 123.76 115.37 121.85 111.75 111.67 112.79 122.70 * +* +* 3 ASP 3 1.300 1.236 1.510 1.539 1.446 121.72 117.24 119.60 110.46 108.43 110.19 123.15 ** ** 4 THR 4 1.319 1.246 1.548 1.547 1.447 122.27 116.12 121.03 110.77 111.08 110.00 122.81 * * 5 GLY 5 1.324 1.225 1.498 - 1.456 122.60 113.90 121.33 - 112.69 - 124.77 * * * * * 6 GLU 6 1.289 1.253 1.538 1.536 1.439 125.89 115.75 121.16 110.54 111.80 108.21 123.00 +** * * ** * +** 7 VAL 7 1.311 1.233 1.514 1.564 1.439 122.16 116.84 120.65 111.48 108.63 113.18 122.51 * * * 8 GLN 8 1.294 1.229 1.512 1.533 1.402 121.18 114.21 121.53 109.62 113.39 110.46 124.25 ** +** +** 9 PHE 9 1.299 1.233 1.521 1.539 1.440 124.57 117.31 119.90 110.56 107.52 108.78 122.79 ** +* * * ** 10 MET 10 1.310 1.238 1.523 1.551 1.447 121.31 117.48 120.06 111.98 109.88 108.09 122.45 * * * * 11 LYS 11 1.322 1.245 1.520 1.543 1.447 120.54 116.96 120.43 107.77 111.50 113.55 122.59 * +* +* Residue-by-residue listing for refined_2 Page 6 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 12 PRO 12 1.347 1.239 1.518 1.544 1.456 122.80 117.48 120.14 108.93 108.68 104.06 122.37 * * 13 PHE 13 1.299 1.227 1.511 1.541 1.439 120.15 116.11 120.65 111.89 110.18 111.87 123.22 ** ** 14 ILE 14 1.299 1.242 1.516 1.587 1.441 122.15 116.63 119.44 109.92 107.67 112.67 123.89 ** +* * ** 15 SER 15 1.345 1.234 1.537 1.534 1.480 124.01 115.19 121.09 110.43 112.62 109.80 123.65 * * * * 16 GLU 16 1.311 1.226 1.528 1.524 1.444 124.31 116.87 120.73 110.67 110.66 108.97 122.40 * * * 17 LYS 17 1.324 1.225 1.492 1.539 1.451 119.99 116.27 120.23 107.54 110.54 114.87 123.46 +* * +** +** 18 SER 18 1.327 1.214 1.517 1.514 1.449 122.37 117.44 120.35 110.87 113.16 110.67 122.20 19 SER 19 1.309 1.231 1.546 1.524 1.439 119.36 117.08 120.47 110.91 110.80 111.07 122.44 * * * * * 20 LYS 20 1.344 1.229 1.544 1.543 1.462 121.42 117.26 119.98 108.79 112.79 109.98 122.75 * * 21 SER 21 1.327 1.229 1.538 1.517 1.462 121.93 116.64 120.57 109.67 112.33 108.16 122.79 * * 22 LEU 22 1.326 1.239 1.541 1.566 1.436 122.27 115.84 121.17 113.33 107.85 109.03 122.95 +* * +* * +* 23 GLU 23 1.317 1.233 1.513 1.551 1.458 122.69 117.47 120.02 107.07 108.95 112.26 122.50 * +* * +* 24 ILE 24 1.298 1.235 1.545 1.541 1.438 120.49 118.39 119.72 110.52 108.88 110.40 121.82 ** * * ** 25 PRO 25 1.353 1.245 1.539 1.532 1.477 123.14 115.28 121.27 109.53 113.37 103.65 123.42 * * * 26 LEU 26 1.326 1.232 1.538 1.563 1.457 124.06 115.89 120.98 112.57 108.87 108.20 123.09 +* * * * +* 27 GLY 27 1.327 1.232 1.527 - 1.454 121.45 116.84 120.72 - 112.47 - 122.42 28 PHE 28 1.328 1.225 1.529 1.537 1.455 120.98 116.37 121.33 111.80 109.56 111.50 122.30 29 ASN 29 1.324 1.232 1.519 1.536 1.460 120.78 115.32 121.20 109.45 108.54 112.02 123.43 30 GLU 30 1.329 1.234 1.525 1.523 1.459 122.61 116.22 120.97 109.91 111.50 111.58 122.79 31 TYR 31 1.318 1.231 1.538 1.545 1.446 121.95 116.49 120.46 111.44 109.19 110.18 123.03 32 PHE 32 1.346 1.238 1.557 1.571 1.461 121.88 118.47 121.07 111.43 111.69 111.89 120.34 * +* ** * +* ** 33 PRO 33 1.340 1.238 1.517 1.521 1.448 121.87 115.35 121.39 109.96 110.19 104.80 123.26 * * +* +* 34 ALA 34 1.280 1.230 1.505 1.532 1.441 122.89 119.39 118.81 110.63 108.38 109.65 121.79 +*** +* * * +*** 35 PRO 35 1.345 1.251 1.522 1.536 1.459 121.44 117.84 119.73 110.20 108.34 103.77 122.43 * * * 36 PHE 36 1.314 1.241 1.524 1.540 1.411 120.31 116.78 120.94 111.90 111.43 111.19 122.18 * ** ** 37 PRO 37 1.330 1.242 1.519 1.532 1.436 122.17 116.37 121.06 110.83 110.30 103.78 122.55 ** ** 38 ILE 38 1.292 1.227 1.518 1.553 1.429 121.13 115.95 121.37 110.16 108.64 111.60 122.68 +** * +** 39 THR 39 1.309 1.234 1.538 1.552 1.438 122.62 117.50 120.06 109.10 107.69 109.87 122.44 * * * * 40 VAL 40 1.306 1.237 1.518 1.566 1.456 122.32 116.89 120.52 110.09 109.28 114.11 122.58 +* +* +* 41 ASP 41 1.298 1.241 1.492 1.539 1.448 120.77 115.58 120.87 108.95 110.89 113.01 123.55 ** +* * ** Residue-by-residue listing for refined_2 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 1.294 1.228 1.490 1.537 1.429 122.11 115.90 121.05 109.16 107.37 111.90 123.02 ** +* +* * ** 43 LEU 43 1.272 1.223 1.496 1.532 1.413 121.70 115.61 120.99 110.85 109.10 110.44 123.40 **** * ** **** 44 ASP 44 1.270 1.239 1.502 1.525 1.439 122.99 114.24 121.20 111.05 111.12 109.47 124.55 **** * * **** 45 TYR 45 1.307 1.227 1.542 1.538 1.446 124.75 116.96 120.67 111.74 111.80 108.25 122.36 +* +* * +* 46 SER 46 1.314 1.231 1.546 1.518 1.439 121.08 117.55 120.25 111.62 111.04 109.66 122.20 * * 47 GLY 47 1.327 1.233 1.525 - 1.462 119.37 117.18 120.24 - 114.65 - 122.57 48 ARG 48 1.318 1.235 1.536 1.531 1.466 121.94 116.52 120.88 110.58 111.48 111.55 122.54 49 SER 49 1.310 1.238 1.528 1.531 1.444 122.08 116.90 119.93 111.09 109.82 109.30 123.15 * * 50 TRP 50 1.315 1.233 1.518 1.541 1.473 121.95 116.27 120.82 108.23 110.38 111.50 122.90 51 THR 51 1.297 1.241 1.545 1.537 1.436 121.92 116.17 121.05 111.03 108.91 109.53 122.76 ** * * ** 52 VAL 52 1.320 1.227 1.535 1.560 1.464 122.57 118.29 120.15 109.94 110.37 111.34 121.56 * * 53 ARG 53 1.316 1.218 1.521 1.546 1.446 119.23 115.79 121.09 111.13 110.26 111.84 123.11 * * 54 MET 54 1.311 1.228 1.509 1.553 1.449 123.27 116.87 119.83 112.84 108.09 109.01 123.26 * * * * * 55 LYS 55 1.320 1.243 1.521 1.528 1.437 121.95 115.77 121.04 107.88 111.91 109.68 123.20 * * * 56 LYS 56 1.315 1.232 1.506 1.531 1.437 122.19 117.63 119.86 109.06 102.83 110.74 122.47 * +** +** 57 ARG 57 1.280 1.241 1.518 1.538 1.441 119.86 115.80 120.90 110.45 111.41 108.72 123.29 *** * * *** 58 GLY 58 1.308 1.235 1.505 - 1.435 121.43 115.96 120.77 - 111.96 - 123.24 * * * 59 GLU 59 1.305 1.225 1.522 1.554 1.444 122.42 116.10 120.99 110.32 110.27 110.99 122.89 +* * +* 60 LYS 60 1.305 1.231 1.530 1.557 1.440 122.10 116.90 120.89 110.24 109.26 109.15 122.17 +* * +* 61 VAL 61 1.302 1.240 1.508 1.553 1.427 121.63 116.43 120.72 111.77 108.10 114.18 122.83 +* +* * * +* +* 62 PHE 62 1.287 1.240 1.495 1.539 1.427 120.68 115.54 121.05 111.10 109.46 107.63 123.38 *** * +* +* *** 63 LEU 63 1.290 1.219 1.516 1.549 1.413 121.69 115.81 120.75 113.94 104.64 109.27 123.40 +** ** ** ** +** 64 THR 64 1.288 1.239 1.561 1.588 1.434 122.96 116.44 120.48 113.44 111.10 108.57 123.08 +** +* +* * +* +* +** 65 VAL 65 1.324 1.238 1.513 1.548 1.444 124.36 115.00 121.83 110.45 112.82 111.83 123.14 * * 66 GLY 66 1.298 1.232 1.477 - 1.421 120.75 115.13 120.80 - 110.26 - 124.05 ** ** +* ** 67 TRP 67 1.332 1.241 1.513 1.532 1.458 123.46 114.98 121.61 109.62 110.45 109.39 123.32 68 GLU 68 1.307 1.213 1.533 1.517 1.432 121.27 117.10 120.35 112.17 112.21 112.03 122.53 +* * * +* 69 ASN 69 1.331 1.200 1.502 1.542 1.472 121.64 115.35 120.96 109.24 110.09 112.54 123.62 +* * * +* 70 PHE 70 1.298 1.237 1.521 1.541 1.439 123.81 115.95 120.92 111.65 110.78 109.05 123.11 ** * ** Residue-by-residue listing for refined_2 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 1.327 1.236 1.530 1.569 1.457 121.49 115.53 121.11 111.15 110.32 111.73 123.36 * * 72 LYS 72 1.321 1.227 1.526 1.543 1.454 122.04 117.22 120.29 110.91 111.74 111.80 122.48 73 ASP 73 1.336 1.239 1.523 1.529 1.480 120.29 117.07 120.57 110.95 112.95 111.81 122.34 * * 74 ASN 74 1.310 1.229 1.512 1.543 1.465 120.67 116.61 119.71 110.71 112.91 112.30 123.66 * * * 75 ASN 75 1.336 1.245 1.523 1.546 1.479 123.51 115.58 121.98 111.01 109.65 112.31 122.34 * * * * 76 LEU 76 1.294 1.233 1.521 1.528 1.426 120.69 115.08 121.46 110.44 112.92 109.37 123.46 ** +* ** 77 GLU 77 1.314 1.251 1.494 1.518 1.441 123.90 115.80 119.84 109.04 108.38 112.27 124.36 * * * * * * 78 ASP 78 1.310 1.232 1.523 1.553 1.465 122.34 115.67 121.22 111.49 111.01 112.56 123.06 * * * * 79 GLY 79 1.304 1.227 1.494 - 1.440 121.83 114.90 121.46 - 109.72 - 123.64 +* * +* 80 LYS 80 1.308 1.226 1.519 1.542 1.440 122.66 118.27 119.55 113.20 108.27 111.06 122.15 +* * +* * +* 81 TYR 81 1.307 1.226 1.518 1.542 1.459 120.06 118.13 119.68 109.53 109.19 109.55 122.19 +* +* 82 LEU 82 1.323 1.243 1.500 1.543 1.454 119.92 115.42 120.88 106.62 110.43 113.57 123.69 * +* +* +* 83 GLN 83 1.297 1.229 1.513 1.526 1.423 122.02 117.14 119.86 108.85 106.37 110.83 122.98 ** +* +* ** 84 PHE 84 1.298 1.218 1.498 1.537 1.442 121.55 117.11 120.07 108.37 108.11 110.50 122.82 ** * * ** 85 ILE 85 1.287 1.219 1.501 1.556 1.440 121.09 118.20 119.72 107.43 108.53 111.55 122.07 +** * +** 86 TYR 86 1.294 1.237 1.496 1.555 1.441 118.00 116.53 120.26 112.41 108.83 114.85 123.18 +** * * ** * +** +** 87 ASP 87 1.303 1.228 1.516 1.538 1.449 120.23 116.52 120.85 111.84 110.29 110.83 122.59 +* +* 88 ARG 88 1.309 1.230 1.512 1.545 1.453 122.54 116.37 120.87 109.17 110.05 110.95 122.71 * * 89 ASP 89 1.313 1.223 1.529 1.557 1.419 121.64 115.52 120.83 111.69 109.00 109.19 123.62 * * ** ** 90 ARG 90 1.286 1.229 1.526 1.564 1.448 125.42 116.02 121.36 112.81 111.78 110.27 122.61 *** +* ** * *** 91 THR 91 1.311 1.240 1.532 1.571 1.426 120.85 116.54 120.65 112.24 107.35 112.63 122.75 * * +* * * +* 92 PHE 92 1.307 1.219 1.507 1.540 1.445 121.25 116.20 120.42 109.19 110.18 110.50 123.37 +* +* 93 TYR 93 1.300 1.233 1.521 1.546 1.442 123.07 117.16 120.04 109.84 106.04 110.22 122.76 ** +* ** 94 VAL 94 1.304 1.235 1.534 1.560 1.445 121.35 115.20 121.35 109.65 112.28 111.09 123.44 +* +* 95 ILE 95 1.317 1.238 1.533 1.561 1.452 123.49 117.44 119.99 109.91 107.45 111.31 122.56 * * 96 ILE 96 1.321 1.240 1.533 1.591 1.454 121.29 115.85 120.66 109.39 110.46 113.26 123.49 +* * +* 97 TYR 97 1.322 1.239 1.506 1.530 1.452 122.55 115.11 121.03 105.80 109.88 112.04 123.83 ** ** 98 GLY 98 1.292 1.234 1.495 - 1.417 122.58 117.16 120.13 - 109.62 - 122.70 +** * ** * +** Residue-by-residue listing for refined_2 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 HIS 99 1.303 1.222 1.516 1.539 1.454 120.17 116.27 120.87 109.94 111.53 111.54 122.86 +* +* 100 ASN 100 1.308 1.231 1.521 1.535 1.470 121.72 114.07 121.36 110.54 110.62 110.15 124.57 * * * 101 MET 101 1.312 1.231 1.492 1.537 1.463 127.03 111.81 122.75 109.54 103.27 111.58 125.44 * +* +** ** * +** +* +** 102 CYS 102 1.309 - 1.527 1.542 1.417 126.41 - - 110.40 104.74 111.82 - * ** +** ** +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +* ** ** +** +** ** * ** +** +** +* **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 1.270 1.346 1.310 .016 **** * * C-N (Pro) 1.341 .016 5 1.330 1.353 1.343 .008 C-O C-O 1.231 .020 101 1.200 1.253 1.233 .008 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.490 1.561 1.521 .015 +* +* CH2G*-C (Gly) 1.516 .018 7 1.477 1.527 1.503 .017 ** CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.531 1.532 1.532 .001 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.537 1.591 1.561 .015 +* CH1E-CH2E (the rest) 1.530 .020 75 1.514 1.571 1.539 .012 ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.402 1.480 1.446 .016 +** * NH1-CH2G* (Gly) 1.451 .016 7 1.417 1.462 1.441 .016 ** N-CH1E (Pro) 1.466 .015 5 1.436 1.477 1.455 .013 ** ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_2 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 89 111.81 119.39 116.37 1.10 ** +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 113.90 117.18 115.87 1.18 * CH1E-C-N (Pro) 116.9 1.5 5 115.28 117.84 116.46 1.06 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.34 125.44 122.97 .71 +* +* O-C-N (Pro) 122.0 1.4 5 122.37 123.42 122.81 .44 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.00 127.03 122.04 1.56 ** +** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.37 122.60 121.43 1.04 * C-N-CH1E (Pro) 122.6 5.0 5 121.44 123.14 122.28 .61 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.81 122.75 120.67 .64 * * CH2G*-C-O (Gly) 120.8 2.1 7 120.13 121.46 120.78 .46 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.63 111.75 111.19 .56 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.43 113.44 110.47 1.28 +* CH2E-CH1E-C (the rest) 110.1 1.9 75 105.80 113.94 110.36 1.55 ** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 102.83 113.39 109.85 2.09 +** NH1-CH2G*-C (Gly) 112.5 2.9 7 109.62 114.65 111.62 1.72 N-CH1E-C (Pro) 111.8 2.5 5 108.34 113.37 110.18 1.78 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.65 112.79 111.22 1.57 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.57 114.18 111.60 1.51 +* +* N-CH1E-CH2E (Pro) 103.0 1.1 5 103.65 104.80 104.01 .42 +* NH1-CH1E-CH2E (the rest) 110.5 1.7 70 107.63 114.87 110.73 1.57 +* +** ------------------------------------------------------------------------------------------------------------- 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_2 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 4.4 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 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 58 1.0 .8 .2 .7 Inside f. Overall G-factor 102 -.1 -.4 .3 .9 Inside 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 16 8.1 18.1 6.5 -1.5 BETTER b. Chi-1 trans st dev 30 6.3 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 42 6.7 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 88 8.5 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 24 6.0 20.4 5.0 -2.9 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 10.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .96 3 Residue-by-residue listing for refined_2 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.53 Chi1-chi2 distribution -.34 Chi1 only -.02 Chi3 & chi4 .31 Omega -.20 ------ -.26 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .33 ------ .17 ===== OVERALL AVERAGE -.11 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.