Residue-by-residue listing for refined_10 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -65.3 - - - - - - - 179.0 - 33.5 - 2 GLY 2 - - - - - - - - - - - 179.6 - - - 3 HIS 3 B - - -67.6 - - - - - - - 175.7 - 34.6 - 4 HIS 4 B 60.9 - - - - - - - - - 182.1 - 33.0 - 5 HIS 5 b - - -63.9 - - - - - - - 174.8 - 33.0 - 6 HIS 6 b - 181.4 - - - - - - - - 181.3 -.9 32.2 - * * 7 HIS 7 b - 177.3 - - - - - - - - 177.6 -1.8 34.6 - 8 HIS 8 B - - -55.8 - - - - - - - 175.5 - 36.3 - 9 LEU 9 b - 191.4 - 173.9 - - - - - - 183.7 - 33.8 - 10 GLU 10 B - - -62.6 178.2 - - - - - - 174.6 -1.5 34.6 - 11 MET 11 B 58.2 - - - - - - - - - 181.7 - 34.2 - 12 ALA 12 B - - - - - - - - - - 177.5 - 33.2 - 13 SER 13 B - - -58.1 - - - - - - - 179.7 -.7 34.8 - +* +* 14 GLU 14 B 51.8 - - - - - - - - - 183.1 - 31.5 - 15 GLU 15 B 46.3 - - - - - - - - - 178.4 - 32.3 - * * 16 GLY 16 S - - - - - - - - - - - 181.0 -1.1 - - * * 17 GLN 17 B 52.0 - - 184.6 - - - - - - 183.9 - 31.9 - 18 VAL 18 B 64.1 - - - - - - - - - 181.6 - 34.7 - 19 ILE 19 E B - - -66.1 - - - - - - - 180.1 -3.1 32.6 - * * 20 ALA 20 E B - - - - - - - - - - 178.9 -.8 33.9 - +* +* 21 CYS 21 E B - - -55.5 - - - - - - - 179.4 -2.1 35.4 - Residue-by-residue listing for refined_10 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 HIS 22 S A - - -61.4 - - - - - - - 182.2 -.7 34.4 - +* +* 23 THR 23 h B 56.8 - - - - - - - - - 174.7 - 36.0 - 24 VAL 24 H A - 183.1 - - - -75.7 -25.6 - - - 179.3 - 34.8 - * * 25 GLU 25 H A - 180.6 - 188.3 - -58.6 -52.5 - - - 180.4 - 36.6 - * * 26 THR 26 H A - - -54.8 - - -67.7 -38.8 - - - 176.7 - 33.3 - 27 TRP 27 H A - 169.4 - - - -57.2 -52.8 - - - 179.4 -1.5 34.8 - * * 28 ASN 28 H A - 178.4 - - - -60.2 -43.3 - - - 179.3 -3.4 35.5 - +* +* 29 GLU 29 H A - 186.0 - 180.4 - -61.8 -46.6 - - - 182.0 -2.6 35.5 - 30 GLN 30 H A - - -70.4 - - -66.8 -33.1 - - - 176.0 -3.0 32.9 - * * 31 LEU 31 H A - - -67.4 179.8 - -65.6 -44.9 - - - 175.9 -1.8 34.3 - 32 GLN 32 H A - - -60.6 179.6 - -63.7 -37.4 - - - 174.4 -1.8 33.5 - 33 LYS 33 H A - 174.7 - - - -56.7 -48.0 - - - 180.8 -2.4 35.5 - 34 ALA 34 H A - - - - - -68.1 -41.9 - - - 180.4 -2.6 33.8 - 35 ASN 35 H A - 187.0 - - - -61.4 -53.1 - - - 180.3 -2.9 36.1 - * * * 36 GLU 36 H A - 182.9 - - - -58.9 -36.9 - - - 181.4 -3.2 34.8 - +* +* 37 SER 37 H A - - -57.5 - - -81.4 -8.5 - - - 183.4 -1.8 35.3 - * +** +** 38 LYS 38 h L - 188.1 - 181.6 - - - - - - 182.6 -1.3 33.2 - 39 THR 39 t B - - -49.9 - - - - - - - 180.8 -2.5 34.7 - * * 40 LEU 40 e B 66.8 - - 173.1 - - - - - - 182.8 - 33.4 - 41 VAL 41 E B 58.4 - - - - - - - - - 178.3 - 33.6 - 42 VAL 42 E B - 182.9 - - - - - - - - 185.2 -3.3 34.5 - +* +* 43 VAL 43 E B - 185.6 - - - - - - - - 176.6 -3.2 34.1 - +* +* 44 ASP 44 E B - 167.4 - - - - - - - - 174.2 -3.2 36.4 - * +* +* 45 PHE 45 E B - - -65.4 - - - - - - - 175.3 -3.0 36.9 - * * 46 THR 46 E B - 187.6 - - - - - - - - 172.5 -1.7 33.5 - * * 47 ALA 47 t B - - - - - - - - - - 181.4 - 34.5 - 48 SER 48 T A - 184.7 - - - - - - - - 182.8 - 33.5 - 49 TRP 49 T A 57.1 - - - - - - - - - 179.9 - 30.7 - 50 CYS 50 h B 43.6 - - - - - - - -115.5 2.8 184.9 -1.0 29.9 - * +** *7.8* * * *7.8* 51 GLY 51 H - - - - - - -54.6 -65.3 - - - 180.9 -.6 - - ** +* ** 52 PRO 52 H - - - - - -55.2 -55.2 -31.0 - - - 181.0 - 38.8 - * * 53 CYS 53 H A - - -48.6 153.6 - -72.1 -39.3 - -115.5 2.8 181.2 - 36.8 - * * +** *7.8* *7.8* 54 ARG 54 H A - 182.3 - 176.2 - -78.2 -29.3 - - - 177.8 -2.0 34.3 - * * 55 PHE 55 H A - 177.9 - - - -60.2 -38.5 - - - 185.8 -2.4 35.1 - * * 56 ILE 56 h A - 197.5 - - - - - - - - 179.8 -1.1 33.6 - * * Residue-by-residue listing for refined_10 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 57 ALA 57 H A - - - - - -57.4 -48.7 - - - 177.8 - 31.6 - 58 PRO 58 H - - - - - -60.8 -60.8 -29.0 - - - 180.2 - 38.5 - * * 59 PHE 59 H A - 185.3 - - - -68.2 -41.7 - - - 177.4 - 35.2 - 60 PHE 60 H A - 183.6 - - - -69.0 -33.3 - - - 177.4 -1.7 34.7 - 61 ALA 61 H A - - - - - -70.4 -27.9 - - - 175.9 -1.9 33.4 - * * 62 ASP 62 H A - 181.6 - - - -67.8 -39.9 - - - 175.4 -1.3 35.7 - * * 63 LEU 63 H A - - -68.2 180.6 - -60.4 -43.7 - - - 177.4 -1.5 34.8 - 64 ALA 64 H A - - - - - -61.8 -32.1 - - - 178.8 -1.8 33.9 - 65 LYS 65 H A - 175.9 - 182.3 - -71.2 -39.5 - - - 183.4 -1.2 35.2 - * * 66 LYS 66 H A - - -61.0 179.4 - -81.3 -24.9 - - - 178.4 -1.8 33.2 - * * * 67 LEU 67 h b - - -66.9 169.8 - - - - - - 181.4 -1.9 32.9 - 68 PRO 68 T - - - - - -74.2 - - - - - 183.8 - 39.3 - +* +* 69 ASN 69 T A - - -67.7 - - - - - - - 178.8 - 34.5 - 70 VAL 70 t B - 181.1 - - - - - - - - 180.9 -.7 34.1 - +* +* 71 LEU 71 E B - - -69.5 - - - - - - - 177.5 -1.5 34.6 - 72 PHE 72 E B - - -60.2 - - - - - - - 182.7 - 34.5 - 73 LEU 73 E B - - -77.8 - - - - - - - 174.4 -2.0 33.6 - 74 LYS 74 E B - - -72.4 - - - - - - - 175.8 -2.8 36.2 - 75 VAL 75 E B - 176.3 - - - - - - - - 179.5 -2.9 34.7 - * * 76 ASP 76 E B - 188.3 - - - - - - - - 184.7 -.5 33.5 - +* +* 77 THR 77 e A 49.9 - - - - - - - - - 177.4 -1.8 31.8 - 78 ASP 78 T A - 187.8 - - - - - - - - 177.6 - 34.8 - 79 GLU 79 T a - - -67.8 - - - - - - - 181.2 - 35.8 - 80 LEU 80 h b - - -67.6 177.9 - - - - - - 186.4 -3.3 34.1 - * +* +* 81 LYS 81 H A - 189.7 - 179.8 - -65.1 -33.2 - - - 178.1 -1.9 34.3 - 82 SER 82 H A - - -54.1 - - -69.1 -36.4 - - - 178.6 - 34.4 - 83 VAL 83 H A - 179.8 - - - -68.3 -36.8 - - - 177.9 - 34.2 - 84 ALA 84 H A - - - - - -59.5 -51.7 - - - 180.4 -2.0 34.5 - * * 85 SER 85 H A - - -57.0 - - -67.2 -30.7 - - - 180.8 -2.2 34.6 - 86 ASP 86 H A - 186.1 - - - -62.7 -36.1 - - - 177.8 -2.0 34.3 - 87 TRP 87 h A - - -63.9 - - - - - - - 176.9 -1.6 33.0 - 88 ALA 88 T l - - - - - - - - - - 178.5 -1.1 32.5 - * * 89 ILE 89 t B - - -54.9 - - - - - - - 182.5 -2.8 34.9 - * * 90 GLN 90 A - 186.5 - 184.0 - - - - - - 182.7 -.8 35.5 - +* +* 91 ALA 91 S B - - - - - - - - - - 179.2 - 33.8 - 92 MET 92 S B - - -58.4 180.9 - - - - - - -1.9 - 34.9 - 93 PRO 93 e cis - - - - - -91.7 - - - - - 174.9 - 40.1 - ** +* ** 94 THR 94 E B - - -61.1 - - - - - - - 178.6 -3.0 33.5 - * * 95 PHE 95 E B - - -56.0 - - - - - - - 182.3 -3.0 37.0 - * * Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 96 MET 96 E B - 180.7 - 170.3 - - - - - - 181.8 -3.3 31.3 - +* +* 97 PHE 97 E B - - -68.1 - - - - - - - 181.6 -2.2 36.5 - 98 LEU 98 E B - - -53.8 177.1 - - - - - - 171.5 -2.8 37.1 - * * 99 LYS 99 E B - 173.9 - 171.9 - - - - - - 183.3 -3.0 31.7 - * * 100 GLU 100 T l - - -59.2 183.3 - - - - - - 182.3 -.8 33.0 - +* +* 101 GLY 101 T - - - - - - - - - - - 178.0 - - - 102 LYS 102 E B - - -56.5 180.9 - - - - - - 186.9 -1.8 34.1 - * * 103 ILE 103 E B - - -58.7 178.0 - - - - - - 173.1 - 32.9 - * * 104 LEU 104 E a - - -65.4 185.2 - - - - - - 182.2 -2.2 33.8 - 105 ASP 105 E B - - -63.2 - - - - - - - 174.0 -2.8 35.3 - * * 106 LYS 106 E B - - -57.2 186.6 - - - - - - 177.2 - 34.9 - 107 VAL 107 E B - 181.4 - - - - - - - - 180.3 -3.3 35.2 - +* +* 108 VAL 108 E B 60.8 - - - - - - - - - 180.5 -.6 32.9 - +* +* 109 GLY 109 e - - - - - - - - - - - 178.9 -3.1 - - * * 110 ALA 110 B - - - - - - - - - - 181.5 - 34.4 - 111 LYS 111 h B - - -62.8 178.8 - - - - - - 177.4 -1.0 35.7 - * * 112 LYS 112 H A - - -68.8 180.0 - -69.6 -51.2 - - - 185.8 - 35.8 - * * * 113 ASP 113 H A - 176.7 - - - -72.0 -45.3 - - - 181.0 - 33.3 - 114 GLU 114 H A - 186.2 - 174.4 - -67.7 -29.9 - - - 177.8 - 32.6 - 115 LEU 115 H A - 189.1 - - - -66.4 -47.3 - - - 175.2 -.9 35.0 - +* +* 116 GLN 116 H A - - -68.8 - - -57.0 -36.9 - - - 178.3 -1.9 34.3 - 117 SER 117 H A - 180.9 - - - -66.7 -39.8 - - - 178.5 -2.0 34.4 - 118 THR 118 H A - - -54.0 - - -68.0 -34.8 - - - 175.6 -2.3 34.4 - 119 ILE 119 H A - - -61.0 - - -61.7 -50.4 - - - 180.2 -2.3 34.0 - 120 ALA 120 H A - - - - - -61.4 -31.4 - - - 176.9 -2.6 33.1 - 121 LYS 121 H A - 186.1 - 180.2 - -59.7 -42.1 - - - 180.7 -1.6 36.2 - 122 HIS 122 H A - - -71.3 - - -81.6 -35.3 - - - 181.6 -1.4 33.5 - * * 123 LEU 123 h B - - -83.1 - - - - - - - 179.9 -2.6 32.3 - * * 124 ALA 124 - - - - - - - - - - - - -1.1 34.2 - * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * ** * +** +** *7.8* * +* +* *7.8* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 55.9 182.6 -62.6 178.4 -70.5 -65.6 -39.1 - -115.5 2.8 179.5 -2.0 34.4 +** *7.8* *7.8* Standard deviations: 6.8 5.9 6.9 6.4 16.2 6.9 9.7 - .0 .0 3.1 .8 1.6 Numbers of values: 13 40 49 31 4 46 46 0 2 2 122 80 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_10 Page 5 ---------------------------------------- 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_10 Page 6 ---------------------------------------- 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 - 1.234 1.503 1.545 1.460 - 116.58 120.35 110.25 109.56 111.98 123.07 * * 2 GLY 2 1.303 1.233 1.499 - 1.431 121.03 116.86 120.39 - 111.10 - 122.75 +* * +* 3 HIS 3 1.298 1.231 1.503 1.545 1.450 122.20 115.53 120.88 108.44 110.07 112.19 123.58 ** * ** 4 HIS 4 1.298 1.235 1.510 1.560 1.434 123.03 117.14 120.25 111.85 107.80 112.10 122.56 ** * * * ** 5 HIS 5 1.300 1.232 1.491 1.531 1.443 120.39 116.51 120.80 109.75 112.01 112.32 122.67 ** +* * ** 6 HIS 6 1.302 1.238 1.523 1.541 1.434 120.10 114.44 121.75 112.26 108.24 112.39 123.56 +* * * * * +* 7 HIS 7 1.306 1.237 1.511 1.551 1.435 123.80 116.10 120.57 110.40 108.79 110.71 123.33 +* * * * +* 8 HIS 8 1.302 1.238 1.506 1.528 1.446 121.33 117.21 120.12 106.98 107.93 111.49 122.67 +* +* * +* 9 LEU 9 1.303 1.236 1.522 1.561 1.439 120.10 115.87 121.03 112.58 105.96 110.65 122.90 +* +* * * +* +* 10 GLU 10 1.304 1.246 1.503 1.532 1.439 121.77 115.05 121.12 108.90 111.21 111.27 123.83 +* * +* 11 MET 11 1.289 1.237 1.518 1.548 1.428 123.23 117.09 120.24 110.74 108.17 111.17 122.67 +** +* * +** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 12 ALA 12 1.301 1.231 1.514 1.517 1.438 120.82 115.56 121.30 111.14 110.76 110.94 123.08 +* * +* 13 SER 13 1.298 1.239 1.517 1.537 1.431 122.71 116.64 120.44 110.53 108.68 110.16 122.89 ** * ** 14 GLU 14 1.310 1.242 1.521 1.543 1.417 121.62 115.61 120.86 112.43 111.31 112.15 123.52 * ** * ** 15 GLU 15 1.310 1.234 1.527 1.555 1.446 122.92 116.25 120.49 112.34 112.24 110.69 123.23 * * * * 16 GLY 16 1.324 1.238 1.491 - 1.453 121.46 115.61 121.12 - 112.56 - 123.26 * * 17 GLN 17 1.297 1.231 1.492 1.516 1.425 121.85 114.34 121.64 112.04 111.52 111.70 124.02 ** +* +* * ** 18 VAL 18 1.272 1.239 1.544 1.547 1.424 123.15 117.42 120.32 112.16 110.03 108.31 122.22 **** +* * +* **** 19 ILE 19 1.325 1.231 1.526 1.572 1.443 120.73 116.43 121.12 110.43 110.06 113.19 122.44 * * 20 ALA 20 1.303 1.235 1.513 1.523 1.436 121.37 116.41 120.80 110.88 109.86 110.60 122.78 +* * +* 21 CYS 21 1.306 1.227 1.501 1.506 1.415 121.29 116.11 120.96 109.67 108.78 109.89 122.91 +* * * ** ** 22 HIS 22 1.290 1.219 1.503 1.534 1.441 121.40 115.88 121.02 109.58 109.24 111.46 123.10 +** * +** 23 THR 23 1.316 1.248 1.516 1.559 1.443 122.30 116.60 120.46 107.69 109.40 111.25 122.94 24 VAL 24 1.323 1.218 1.514 1.552 1.450 121.18 114.85 121.39 108.86 107.50 112.27 123.74 * * 25 GLU 25 1.326 1.222 1.520 1.518 1.444 123.74 116.36 120.61 108.59 110.26 108.63 122.99 * * * 26 THR 26 1.325 1.216 1.526 1.534 1.446 121.05 116.22 120.46 111.11 110.39 110.99 123.28 27 TRP 27 1.324 1.233 1.537 1.536 1.456 122.47 114.96 121.46 111.02 110.73 108.80 123.56 28 ASN 28 1.312 1.239 1.522 1.536 1.457 124.25 115.10 121.11 111.25 110.30 107.71 123.76 * * +* +* 29 GLU 29 1.317 1.228 1.541 1.526 1.449 123.45 116.54 120.71 110.04 110.83 108.67 122.74 * * 30 GLN 30 1.327 1.228 1.517 1.483 1.428 123.00 117.46 120.25 110.80 113.95 110.19 122.29 ** +* ** 31 LEU 31 1.307 1.230 1.512 1.488 1.414 121.33 115.84 120.83 111.03 110.44 109.41 123.31 +* ** ** ** 32 GLN 32 1.315 1.221 1.521 1.521 1.446 121.89 115.65 120.70 111.38 109.75 110.61 123.64 * * 33 LYS 33 1.327 1.227 1.533 1.546 1.457 123.52 116.65 120.44 110.24 109.66 109.05 122.89 * * 34 ALA 34 1.332 1.236 1.526 1.522 1.454 121.56 115.74 120.75 110.60 111.14 110.47 123.50 35 ASN 35 1.326 1.234 1.501 1.522 1.470 123.18 114.64 121.34 107.89 110.11 110.17 124.01 * * * 36 GLU 36 1.311 1.231 1.541 1.541 1.472 122.84 116.41 121.10 109.71 111.02 109.97 122.47 * * 37 SER 37 1.312 1.240 1.531 1.510 1.440 121.63 116.51 120.21 109.60 111.83 109.00 123.29 * * * 38 LYS 38 1.352 1.234 1.545 1.515 1.427 124.08 114.57 122.83 113.29 108.76 109.38 122.58 +* +* * * +* +* 39 THR 39 1.311 1.237 1.516 1.523 1.428 122.44 115.05 121.51 109.27 109.32 111.20 123.39 * +* +* 40 LEU 40 1.272 1.240 1.535 1.529 1.379 124.50 115.85 121.03 111.52 111.02 110.56 123.10 **** **** +* **** Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 41 VAL 41 1.307 1.232 1.541 1.566 1.437 122.12 116.22 121.06 111.24 110.73 110.73 122.69 +* * +* 42 VAL 42 1.305 1.236 1.515 1.532 1.443 122.25 116.95 120.71 109.35 108.37 111.77 122.33 +* * +* 43 VAL 43 1.299 1.235 1.524 1.547 1.434 120.38 114.86 121.24 109.48 111.71 111.33 123.90 ** * ** 44 ASP 44 1.301 1.247 1.511 1.534 1.448 124.34 116.87 120.14 108.73 109.92 109.17 122.97 +* * +* 45 PHE 45 1.315 1.246 1.519 1.524 1.415 120.95 116.12 120.81 108.20 109.00 109.19 123.07 * ** * ** 46 THR 46 1.300 1.228 1.523 1.556 1.424 122.36 117.10 119.92 111.12 108.70 111.71 122.98 ** +* ** 47 ALA 47 1.301 1.232 1.514 1.515 1.434 121.92 117.19 120.16 110.44 107.57 110.80 122.64 ** * * ** 48 SER 48 1.301 1.240 1.552 1.544 1.451 121.55 117.06 120.66 111.63 111.89 109.69 122.26 +* * +* 49 TRP 49 1.338 1.229 1.537 1.555 1.461 121.01 118.30 119.95 111.40 114.31 112.70 121.76 * * * * * 50 CYS 50 1.314 1.234 1.526 1.544 1.457 119.60 114.76 121.31 113.88 112.47 112.00 123.92 * * +* +* 51 GLY 51 1.338 1.224 1.528 - 1.469 123.80 119.29 119.44 - 115.50 - 121.27 * +* * * * +* 52 PRO 52 1.359 1.230 1.532 1.532 1.486 122.69 115.35 121.42 109.99 112.37 103.32 123.22 * * * * 53 CYS 53 1.304 1.227 1.529 1.500 1.444 123.05 115.22 121.53 108.81 110.02 108.00 123.26 +* +* * +* 54 ARG 54 1.310 1.226 1.534 1.529 1.444 123.32 115.91 121.15 112.21 110.39 108.46 122.94 * * * * 55 PHE 55 1.323 1.229 1.534 1.546 1.469 123.27 116.03 121.18 109.32 111.68 109.80 122.79 56 ILE 56 1.310 1.225 1.568 1.591 1.451 122.00 116.16 121.86 114.27 109.55 108.08 121.85 * ** +* ** ** ** 57 ALA 57 1.331 1.241 1.566 1.529 1.474 122.08 119.87 119.53 111.47 113.37 111.51 120.60 +* +* * +* 58 PRO 58 1.377 1.234 1.534 1.536 1.477 122.13 115.66 120.80 110.09 112.25 103.81 123.52 ** * ** 59 PHE 59 1.322 1.230 1.535 1.541 1.464 123.46 115.50 121.44 110.77 109.32 108.84 123.05 60 PHE 60 1.315 1.226 1.533 1.535 1.464 123.24 116.00 121.38 111.62 109.34 108.72 122.61 * * 61 ALA 61 1.315 1.235 1.540 1.511 1.451 121.54 115.94 121.17 111.29 110.49 110.25 122.89 62 ASP 62 1.328 1.228 1.501 1.523 1.480 123.12 114.06 121.78 109.60 108.42 109.40 124.16 * * * * 63 LEU 63 1.299 1.231 1.538 1.520 1.433 124.10 116.23 120.69 111.40 111.14 108.22 123.07 ** * * * ** 64 ALA 64 1.330 1.229 1.531 1.525 1.469 122.61 115.44 121.49 110.53 110.81 110.39 123.07 65 LYS 65 1.316 1.223 1.518 1.520 1.449 122.93 116.40 120.86 110.63 111.26 108.36 122.72 * * 66 LYS 66 1.303 1.230 1.511 1.507 1.449 120.98 116.93 120.24 110.44 112.56 110.83 122.82 +* * +* 67 LEU 67 1.311 1.224 1.521 1.511 1.428 121.56 116.71 121.19 112.13 111.40 110.11 122.05 * +* * +* 68 PRO 68 1.338 1.231 1.529 1.535 1.468 123.15 116.51 120.88 109.96 112.86 102.85 122.60 69 ASN 69 1.318 1.228 1.511 1.518 1.444 121.98 116.34 120.66 109.90 111.75 110.09 123.00 70 VAL 70 1.307 1.232 1.516 1.562 1.442 122.31 117.09 120.22 110.16 108.14 112.00 122.64 +* * +* Residue-by-residue listing for refined_10 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 ----------------------------------------------------------------------------------------------------------------------------------- 71 LEU 71 1.308 1.229 1.516 1.542 1.426 121.62 116.27 120.49 109.75 110.14 110.90 123.22 +* +* +* 72 PHE 72 1.313 1.237 1.506 1.528 1.450 122.44 116.32 120.46 108.90 108.46 112.08 123.21 * * 73 LEU 73 1.301 1.227 1.517 1.538 1.458 122.49 115.22 121.02 108.37 113.13 112.40 123.76 ** * ** 74 LYS 74 1.323 1.245 1.509 1.525 1.423 124.31 116.02 120.58 108.41 109.38 110.01 123.38 +* * +* 75 VAL 75 1.298 1.240 1.506 1.557 1.438 122.37 116.91 120.35 109.69 107.92 111.69 122.69 ** * * ** 76 ASP 76 1.307 1.223 1.502 1.507 1.435 120.09 116.16 120.63 110.64 108.34 111.70 123.17 +* * * * * +* 77 THR 77 1.295 1.235 1.529 1.527 1.440 122.53 117.54 120.06 111.55 114.76 110.95 122.40 ** * * ** 78 ASP 78 1.314 1.235 1.505 1.525 1.455 120.45 113.69 122.08 109.99 107.17 110.83 124.22 * * * * 79 GLU 79 1.314 1.233 1.515 1.504 1.422 124.62 116.12 120.87 109.69 110.73 108.64 122.94 * * +* +* * +* 80 LEU 80 1.319 1.237 1.503 1.519 1.410 122.84 113.25 122.56 112.53 108.19 109.43 124.19 * +** * * * * +** 81 LYS 81 1.303 1.235 1.528 1.525 1.424 124.48 116.39 120.65 111.78 111.39 108.68 122.94 +* +* +* * +* 82 SER 82 1.321 1.223 1.527 1.517 1.443 121.47 115.98 120.91 110.93 109.48 109.70 123.05 83 VAL 83 1.332 1.231 1.529 1.557 1.459 122.19 115.64 121.36 109.94 109.14 111.54 122.99 84 ALA 84 1.321 1.226 1.521 1.514 1.451 122.05 116.16 120.73 109.91 110.45 110.20 123.06 85 SER 85 1.317 1.243 1.536 1.520 1.446 122.19 115.52 121.05 110.86 110.94 109.12 123.40 86 ASP 86 1.323 1.235 1.531 1.531 1.464 123.48 116.09 121.04 110.67 111.33 109.57 122.86 87 TRP 87 1.322 1.237 1.526 1.518 1.451 122.17 115.46 120.96 110.98 111.41 111.01 123.58 88 ALA 88 1.336 1.230 1.533 1.534 1.473 124.18 116.55 120.65 111.27 112.62 110.96 122.77 * * 89 ILE 89 1.321 1.244 1.516 1.559 1.456 122.35 115.85 121.05 109.18 108.13 111.62 123.05 * * 90 GLN 90 1.297 1.234 1.520 1.521 1.434 121.67 115.96 121.11 109.83 110.07 109.28 122.92 ** * ** 91 ALA 91 1.308 1.236 1.511 1.521 1.442 121.06 116.34 120.92 110.81 110.51 110.56 122.72 +* +* 92 MET 92 1.304 1.240 1.515 1.527 1.429 121.37 117.95 120.20 109.68 109.24 110.66 121.85 +* * +* 93 PRO 93 1.335 1.235 1.535 1.526 1.461 123.58 116.66 120.71 109.65 111.97 101.99 122.62 94 THR 94 1.300 1.232 1.519 1.530 1.427 121.27 116.11 120.86 109.97 109.92 112.15 123.03 ** +* ** 95 PHE 95 1.301 1.225 1.493 1.518 1.414 122.60 117.54 120.26 108.90 106.87 108.96 122.20 +* +* ** +* ** 96 MET 96 1.276 1.233 1.505 1.534 1.419 119.57 114.91 121.54 113.25 111.08 111.62 123.55 +*** ** * +* +*** 97 PHE 97 1.298 1.240 1.488 1.515 1.398 123.33 115.36 121.29 109.33 108.11 109.05 123.34 ** +* *** * *** 98 LEU 98 1.273 1.228 1.519 1.544 1.407 121.75 116.24 120.95 107.42 108.45 110.07 122.81 **** +** * **** 99 LYS 99 1.287 1.226 1.470 1.516 1.423 121.84 114.15 121.07 111.35 108.53 113.91 124.65 +** +** +* * ** * +** 100 GLU 100 1.316 1.226 1.545 1.521 1.438 124.57 116.12 121.14 110.51 110.90 111.72 122.72 * +* +* 101 GLY 101 1.326 1.231 1.524 - 1.451 121.41 116.42 120.66 - 112.36 - 122.92 102 LYS 102 1.325 1.229 1.527 1.523 1.455 122.30 116.91 120.08 111.22 109.57 109.91 123.00 Residue-by-residue listing for refined_10 Page 10 ---------------------------------------- ................................................................................................................................... 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 ----------------------------------------------------------------------------------------------------------------------------------- 103 ILE 103 1.314 1.238 1.531 1.557 1.471 122.75 115.85 121.06 109.84 114.13 111.59 123.08 * * * 104 LEU 104 1.329 1.225 1.512 1.519 1.434 122.05 116.61 120.65 109.27 110.17 112.20 122.72 * * 105 ASP 105 1.323 1.225 1.489 1.527 1.463 121.04 115.25 121.06 106.12 111.39 112.84 123.69 +* ** * ** 106 LYS 106 1.301 1.223 1.511 1.542 1.446 123.32 117.13 120.10 108.20 107.67 112.51 122.75 +* * * * +* 107 VAL 107 1.293 1.227 1.509 1.561 1.442 121.74 116.62 120.26 109.26 107.70 111.34 123.11 +** * +** 108 VAL 108 1.299 1.246 1.532 1.565 1.433 121.61 115.82 121.12 111.64 110.04 111.61 123.01 ** * * ** 109 GLY 109 1.306 1.238 1.503 - 1.431 121.49 117.53 120.08 - 110.61 - 122.37 +* * +* 110 ALA 110 1.326 1.238 1.508 1.523 1.444 119.04 115.19 121.24 110.67 108.39 110.54 123.52 * * * 111 LYS 111 1.301 1.217 1.506 1.521 1.416 123.14 117.78 119.59 110.50 110.39 108.44 122.62 ** ** * ** 112 LYS 112 1.308 1.236 1.530 1.509 1.418 121.26 115.30 121.40 109.03 111.18 109.13 123.21 +* * ** ** 113 ASP 113 1.325 1.234 1.517 1.536 1.467 122.60 116.89 120.48 110.81 112.50 110.52 122.61 114 GLU 114 1.318 1.235 1.524 1.523 1.453 120.93 116.64 120.67 111.25 110.98 111.50 122.67 115 LEU 115 1.325 1.221 1.507 1.507 1.447 120.75 115.29 120.97 109.34 108.32 110.76 123.73 * * * 116 GLN 116 1.324 1.234 1.520 1.520 1.477 122.70 115.85 120.86 109.37 111.13 110.75 123.28 117 SER 117 1.309 1.237 1.529 1.535 1.447 122.28 115.61 121.19 111.08 109.48 109.78 123.15 * * 118 THR 118 1.318 1.235 1.543 1.549 1.440 122.31 115.96 121.18 110.51 109.34 110.47 122.85 119 ILE 119 1.330 1.224 1.529 1.568 1.454 122.24 116.16 120.72 109.69 109.49 112.01 123.07 * * 120 ALA 120 1.325 1.230 1.526 1.516 1.463 122.48 116.32 120.48 111.01 111.74 110.67 123.20 121 LYS 121 1.324 1.222 1.517 1.500 1.456 122.42 115.10 121.67 108.21 109.99 109.39 123.23 +* +* 122 HIS 122 1.302 1.235 1.527 1.525 1.436 122.46 117.42 120.20 110.42 112.93 110.58 122.39 +* * +* 123 LEU 123 1.322 1.240 1.520 1.513 1.412 121.83 114.56 121.63 112.22 113.12 110.34 123.81 ** * ** 124 ALA 124 1.311 - 1.513 1.529 1.440 123.97 - - 110.51 108.29 110.98 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** +** ** **** +* +* * ** +* ** * **** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 11 ---------------------------------------- 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 .014 119 1.272 1.352 1.312 .014 **** +* * C-N (Pro) 1.341 .016 4 1.335 1.377 1.352 .017 ** C-O C-O 1.231 .020 123 1.216 1.248 1.232 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.470 1.568 1.521 .015 +** ** CH2G*-C (Gly) 1.516 .018 5 1.491 1.528 1.509 .015 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.511 1.534 1.521 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.523 1.591 1.553 .016 +* CH1E-CH2E (the rest) 1.530 .020 84 1.483 1.561 1.527 .015 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.379 1.480 1.442 .017 **** * NH1-CH2G* (Gly) 1.451 .016 5 1.431 1.469 1.447 .014 * * N-CH1E (Pro) 1.466 .015 4 1.461 1.486 1.473 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 12 ---------------------------------------- +-----------------+ | 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 2.0 114 113.25 119.87 116.07 .96 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.61 119.29 117.14 1.24 * CH1E-C-N (Pro) 116.9 1.5 4 115.35 116.66 116.04 .55 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.60 124.65 123.01 .58 * * O-C-N (Pro) 122.0 1.4 4 122.60 123.52 122.99 .40 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.04 124.62 122.22 1.16 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 121.03 123.80 121.84 1.00 +* C-N-CH1E (Pro) 122.6 5.0 4 122.13 123.58 122.89 .54 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.53 122.83 120.87 .54 * CH2G*-C-O (Gly) 120.8 2.1 5 119.44 121.12 120.34 .56 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 109.91 111.47 110.81 .41 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.69 114.27 110.29 1.35 ** CH2E-CH1E-C (the rest) 110.1 1.9 84 106.12 113.88 110.31 1.46 ** +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.96 114.76 110.15 1.68 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 110.61 115.50 112.42 1.70 * N-CH1E-C (Pro) 111.8 2.5 4 111.97 112.86 112.37 .32 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.20 111.51 110.68 .34 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.08 113.19 111.26 1.12 ** N-CH1E-CH2E (Pro) 103.0 1.1 4 101.99 103.81 102.99 .67 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.71 113.91 110.33 1.35 +* ** ------------------------------------------------------------------------------------------------------------- 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_10 Page 13 ---------------------------------------- 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] 103 91.2% Residues in additional allowed regions [a,b,l,p] 10 8.8% 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 113 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 5 Number of proline residues 4 ---- Total number of residues 124 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 113 91.2 83.8 10.0 .7 Inside b. Omega angle st dev 122 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 119 1.6 3.1 1.6 -.9 Inside e. H-bond energy st dev 80 .8 .8 .2 .1 Inside f. Overall G-factor 124 .1 -.4 .3 1.5 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 13 6.8 18.1 6.5 -1.7 BETTER b. Chi-1 trans st dev 40 5.9 19.0 5.3 -2.5 BETTER c. Chi-1 gauche plus st dev 49 6.9 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 7.6 18.2 4.8 -2.2 BETTER e. Chi-2 trans st dev 31 6.4 20.4 5.0 -2.8 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% 91.2 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .83 2 Residue-by-residue listing for refined_10 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.14 Chi1-chi2 distribution -.11 Chi1 only .05 Chi3 & chi4 .24 Omega .03 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths -.03 Main-chain bond angles .45 ------ .25 ===== OVERALL AVERAGE .06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.