Residue-by-residue listing for refined_12 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 - - 181.4 - 181.9 - - - - - - 180.6 - 34.3 - 2 GLY 2 - - - - - - - - - - - 177.3 - - - 3 HIS 3 B - - -65.8 - - - - - - - 183.7 - 32.6 - 4 HIS 4 A - 180.6 - - - - - - - - 181.3 - 34.3 - 5 HIS 5 ~p 62.3 - - - - - - - - - 184.0 - 29.0 - ** * ** 6 HIS 6 XX - - -71.5 - - - - - - - 180.9 - 30.3 - **** * **** 7 HIS 7 l - 185.7 - - - - - - - - 179.6 - 32.8 - 8 HIS 8 b - 177.5 - - - - - - - - 179.5 - 33.5 - 9 LEU 9 B - - -63.5 - - - - - - - 176.2 -.8 34.5 - +* +* 10 GLU 10 A - 180.1 - 186.0 - - - - - - 179.6 - 35.9 - 11 MET 11 l - - -66.0 178.6 - - - - - - 171.9 - 30.5 - * * 12 ALA 12 b - - - - - - - - - - 185.8 - 33.6 - 13 SER 13 B - - -58.4 - - - - - - - 174.7 -1.4 34.6 - 14 GLU 14 b - 183.8 - 171.2 - - - - - - 187.1 -2.1 33.2 - * * 15 GLU 15 B 64.8 - - - - - - - - - 174.0 - 35.3 - * * 16 GLY 16 S - - - - - - - - - - - 182.2 -1.8 - - 17 GLN 17 B 53.8 - - 182.8 - - - - - - 175.0 -.6 33.5 - +* +* 18 VAL 18 B 68.2 - - - - - - - - - 179.7 - 34.6 - 19 ILE 19 E B - - -63.4 - - - - - - - 181.4 -2.7 33.1 - 20 ALA 20 E B - - - - - - - - - - 182.3 -.8 33.2 - +* +* Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B - - -51.3 - - - - - - - 174.5 -1.9 35.5 - * * 22 HIS 22 S A - - -66.7 - - - - - - - 181.8 -.6 34.0 - +* +* 23 THR 23 h B 54.0 - - - - - - - - - 176.6 - 35.4 - 24 VAL 24 H A 63.6 - - - - -74.0 -22.7 - - - 177.7 - 32.9 - * * 25 GLU 25 H A - 182.3 - 184.7 - -59.7 -51.6 - - - 179.7 - 35.8 - * * 26 THR 26 H A - - -54.5 - - -64.6 -40.6 - - - 176.4 - 34.3 - 27 TRP 27 H A - 177.5 - - - -53.6 -54.8 - - - 178.8 -1.5 34.6 - * * 28 ASN 28 H A - 181.1 - - - -60.9 -45.3 - - - 183.1 -3.1 35.0 - * * 29 GLU 29 H A - 183.3 - - - -55.6 -49.0 - - - 183.1 -2.8 36.2 - * * 30 GLN 30 H A - - -65.1 - - -72.6 -39.7 - - - 180.3 -2.7 34.3 - 31 LEU 31 H A - - -69.5 180.4 - -63.3 -42.6 - - - 176.8 -2.1 33.6 - 32 GLN 32 H A - 180.5 - 180.9 - -59.1 -44.7 - - - 178.5 -2.5 32.9 - 33 LYS 33 H A - - -61.5 - - -60.4 -37.4 - - - 178.9 -1.6 33.7 - 34 ALA 34 H A - - - - - -73.7 -38.0 - - - 183.7 -2.0 33.8 - 35 ASN 35 H A - 182.6 - - - -69.6 -55.7 - - - 183.5 -2.9 37.3 - * * * 36 GLU 36 H A 60.6 - - 174.6 - -72.8 -34.6 - - - 179.4 -3.0 29.9 - * * * 37 SER 37 H A - - -57.4 - - -87.3 -6.0 - - - 179.7 -1.2 34.0 - +* +** * +** 38 LYS 38 h l - - -77.4 170.5 - - - - - - 174.5 -.6 27.1 - +* +* +* 39 THR 39 t B - - -46.1 - - - - - - - 178.5 -2.2 36.5 - * * 40 LEU 40 e B 68.8 - - - - - - - - - 188.4 - 31.4 - * * 41 VAL 41 E B 60.0 - - - - - - - - - 177.4 - 33.7 - 42 VAL 42 E B - 183.5 - - - - - - - - 183.2 -2.9 34.5 - * * 43 VAL 43 E B - 185.2 - - - - - - - - 175.2 -3.1 34.6 - * * 44 ASP 44 E B - 163.2 - - - - - - - - 172.1 -3.2 35.1 - * * +* +* 45 PHE 45 E B - - -55.9 - - - - - - - 182.7 -2.5 36.7 - 46 THR 46 E B - 191.4 - - - - - - - - 181.9 -1.5 34.1 - 47 ALA 47 t B - - - - - - - - - - 181.3 - 33.8 - 48 SER 48 T A - - -56.7 - - - - - - - 185.7 - 33.5 - 49 TRP 49 T A 57.2 - - - - - - - - - 180.6 - 33.5 - 50 CYS 50 h B 40.7 - - - - - - - -115.2 2.8 185.6 -.9 30.7 - * +** *7.8* +* *7.8* 51 GLY 51 H - - - - - - -52.4 -63.2 - - - 180.9 -.5 - - * ** ** ** 52 PRO 52 H - - - - - -57.6 -57.6 -30.7 - - - 181.5 - 39.0 - * * 53 CYS 53 H A - - -46.8 151.7 - -72.6 -42.6 - -115.2 2.8 178.2 - 35.7 - * * +** *7.8* *7.8* 54 ARG 54 H A - 177.6 - 176.4 - -67.7 -35.4 - - - 178.6 -2.5 33.7 - 55 PHE 55 H A - 172.7 - - - -65.3 -33.2 - - - 186.6 -2.5 34.2 - * * Residue-by-residue listing for refined_12 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 ILE 56 H A - 194.7 - - - -87.5 -23.5 - - - 181.3 -1.3 33.4 - +* * +* 57 ALA 57 H A - - - - - -54.7 -46.4 - - - 178.9 -1.4 31.9 - 58 PRO 58 H - - - - - -61.6 -61.6 -26.5 - - - 179.5 - 38.8 - * * * 59 PHE 59 H A - 181.4 - - - -72.9 -32.2 - - - 177.3 -.8 33.1 - +* +* 60 PHE 60 H A - 188.3 - - - -69.0 -33.3 - - - 175.1 -1.2 34.1 - * * 61 ALA 61 H A - - - - - -69.6 -28.2 - - - 177.1 -1.4 33.8 - 62 ASP 62 H A - 183.4 - - - -69.9 -43.4 - - - 175.1 -1.1 35.1 - * * 63 LEU 63 H A - - -66.0 182.2 - -56.8 -47.4 - - - 177.4 -2.2 35.1 - 64 ALA 64 H A - - - - - -60.1 -32.0 - - - 178.4 -2.3 33.8 - 65 LYS 65 H A - 180.1 - - - -76.4 -31.0 - - - 183.3 -1.2 32.8 - * * 66 LYS 66 H A - 186.7 - 181.9 - -84.8 -38.9 - - - 179.2 -1.8 33.3 - +* +* 67 LEU 67 h B - - -66.4 - - - - - - - 183.7 -2.9 33.2 - * * 68 PRO 68 S - - - - - -84.4 - - - - - 183.7 - 39.6 - +* +* +* 69 ASN 69 S A - 178.8 - - - - - - - - 179.6 - 33.0 - 70 VAL 70 S B - 175.9 - - - - - - - - 181.2 - 34.1 - 71 LEU 71 E B - - -60.6 177.7 - - - - - - 179.0 -1.3 36.0 - 72 PHE 72 E B - - -60.2 - - - - - - - 178.7 - 34.7 - 73 LEU 73 E B - - -75.6 - - - - - - - 180.6 -2.3 32.7 - 74 LYS 74 E B - 203.2 - - - - - - - - 183.1 -2.8 36.8 - * * * 75 VAL 75 E B - 179.6 - - - - - - - - 177.5 -3.6 33.8 - ** ** 76 ASP 76 E B - 187.0 - - - - - - - - 185.8 -1.4 34.5 - 77 THR 77 e A - 178.0 - - - - - - - - 175.9 -1.0 30.3 - * * * 78 ASP 78 T A - 183.7 - - - - - - - - 177.5 - 34.4 - 79 GLU 79 T A - - -61.1 - - - - - - - 178.5 - 36.3 - 80 LEU 80 h b - - -70.7 - - - - - - - 186.0 -2.5 34.2 - * * 81 LYS 81 H A - 208.4 - - - -68.9 -44.7 - - - 180.4 -1.0 34.6 - * * * 82 SER 82 H A - - -56.2 - - -67.6 -35.3 - - - 179.2 - 34.0 - 83 VAL 83 H A - 182.6 - - - -66.2 -42.3 - - - 177.6 - 34.2 - 84 ALA 84 H A - - - - - -58.9 -51.1 - - - 179.3 -2.2 34.1 - * * 85 SER 85 H A - - -57.4 - - -61.4 -34.6 - - - 180.2 -2.4 34.3 - 86 ASP 86 H A - 183.7 - - - -69.3 -36.2 - - - 177.6 -2.2 34.0 - 87 TRP 87 h A - - -70.3 - - - - - - - 177.1 -2.2 32.8 - 88 ALA 88 T l - - - - - - - - - - 180.1 -1.1 33.1 - * * 89 ILE 89 t b - - -54.3 176.7 - - - - - - 183.0 -3.3 34.2 - +* +* 90 GLN 90 A - 187.7 - - - - - - - - 181.4 -1.4 35.6 - 91 ALA 91 S B - - - - - - - - - - 180.6 - 33.7 - 92 MET 92 S B - - -59.6 168.5 - - - - - - -2.6 - 36.9 - 93 PRO 93 e cis - - - - - -90.6 - - - - - 177.2 - 39.8 - ** +* ** Residue-by-residue listing for refined_12 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 THR 94 E B - - -60.8 - - - - - - - 177.9 -2.9 33.6 - * * 95 PHE 95 E B - - -63.0 - - - - - - - 181.4 -2.9 36.4 - * * 96 MET 96 E B - 184.4 - 174.9 - - - - - - 181.7 -3.2 32.5 - +* +* 97 PHE 97 E B - - -65.5 - - - - - - - 183.0 -3.2 36.3 - +* +* 98 LEU 98 E B - - -52.3 178.6 - - - - - - 173.5 -3.2 37.1 - * +* +* 99 LYS 99 E B - 173.7 - 176.3 - - - - - - 178.5 -3.2 32.7 - +* +* 100 GLU 100 T l - - -55.8 170.6 - - - - - - 182.5 - 34.2 - 101 GLY 101 T - - - - - - - - - - - 177.1 - - - 102 LYS 102 E B - 177.6 - 175.3 - - - - - - 182.2 -2.5 33.2 - 103 ILE 103 E B - - -58.7 179.4 - - - - - - 173.5 - 33.4 - * * 104 LEU 104 E a - - -69.8 183.0 - - - - - - 185.8 -1.9 34.5 - 105 ASP 105 E B 47.0 - - - - - - - - - 183.2 -2.3 31.6 - * * 106 LYS 106 E B 63.3 - - 177.6 - - - - - - 172.3 - 35.9 - * * 107 VAL 107 E B - 181.5 - - - - - - - - 180.7 -3.2 35.3 - +* +* 108 VAL 108 E B 59.6 - - - - - - - - - 183.0 - 31.9 - 109 GLY 109 e - - - - - - - - - - - 179.3 -3.1 - - * * 110 ALA 110 B - - - - - - - - - - 179.7 - 34.2 - 111 LYS 111 h B - - -59.8 - - - - - - - 184.4 -1.1 37.5 - * * * 112 LYS 112 H A - 179.9 - 176.8 - -63.4 -50.8 - - - 183.1 -.5 32.9 - * +* +* 113 ASP 113 H A - 183.7 - - - -72.1 -46.2 - - - 181.5 - 33.1 - 114 GLU 114 H A - 181.3 - 181.8 - -62.4 -33.3 - - - 178.2 - 32.8 - 115 LEU 115 H A - 185.0 - - - -61.3 -50.1 - - - 179.8 -1.8 35.2 - 116 GLN 116 H A - - -54.7 - - -58.0 -40.0 - - - 180.3 -1.5 34.1 - 117 SER 117 H A - - -55.1 - - -65.2 -37.3 - - - 178.9 -2.1 34.4 - 118 THR 118 H A - - -53.5 - - -71.4 -35.7 - - - 177.0 -2.2 34.6 - 119 ILE 119 H A - - -59.7 175.2 - -66.3 -48.3 - - - 180.3 -2.4 33.8 - 120 ALA 120 H A - - - - - -60.8 -31.5 - - - 178.5 -3.2 33.5 - +* +* 121 LYS 121 H A - 189.8 - 177.8 - -59.7 -44.2 - - - 180.2 -1.6 36.4 - 122 HIS 122 H A - - -69.5 - - -88.8 -15.1 - - - 181.7 -1.3 34.7 - +* ** ** 123 LEU 123 h B - 195.9 - 168.4 - - - - - - 177.9 -1.5 34.5 - 124 ALA 124 - - - - - - - - - - - - - 34.5 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * * ** +* +** +** *7.8* * ** +* *7.8* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.9 183.2 -61.3 176.7 -73.5 -66.5 -38.9 - -115.2 2.8 179.9 -2.0 34.2 +** *7.8* *7.8* Standard deviations: 7.9 7.4 7.1 6.6 16.4 8.7 10.6 - .0 .0 3.3 .8 1.9 Numbers of values: 14 45 43 30 4 47 47 0 2 2 122 79 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_12 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_12 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 - 1.236 1.518 1.537 1.463 - 116.23 120.68 109.86 110.19 110.85 123.09 2 GLY 2 1.317 1.237 1.500 - 1.434 121.17 116.73 120.40 - 110.75 - 122.87 * * 3 HIS 3 1.300 1.242 1.505 1.540 1.442 121.87 115.80 120.28 111.07 109.70 112.52 123.92 ** * ** 4 HIS 4 1.317 1.228 1.524 1.538 1.460 123.32 116.20 120.00 110.20 111.73 110.03 123.80 5 HIS 5 1.339 1.236 1.546 1.579 1.486 124.78 116.88 120.17 113.62 112.51 113.55 122.93 * ** * +* +* +* ** 6 HIS 6 1.335 1.248 1.518 1.556 1.487 123.63 115.55 120.67 110.70 112.21 114.83 123.78 * +* * +** +** 7 HIS 7 1.343 1.234 1.547 1.566 1.477 123.95 115.46 122.19 112.44 109.56 110.81 122.30 * * +* * * +* 8 HIS 8 1.313 1.228 1.527 1.546 1.440 122.10 116.10 121.10 111.45 110.01 110.74 122.69 * * 9 LEU 9 1.306 1.237 1.519 1.561 1.445 122.44 116.22 120.32 108.46 109.18 112.68 123.45 +* +* * +* 10 GLU 10 1.320 1.231 1.520 1.540 1.457 122.76 114.36 121.29 109.66 108.21 109.34 124.33 * * 11 MET 11 1.327 1.228 1.504 1.543 1.448 124.49 116.22 121.14 111.13 113.65 113.62 122.59 +* +* +* 12 ALA 12 1.301 1.223 1.500 1.520 1.428 120.42 115.91 121.07 111.31 106.15 111.84 122.75 +* * +* +* +* Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 SER 13 1.296 1.236 1.513 1.529 1.420 121.08 115.25 121.13 111.02 111.78 109.08 123.57 ** +* ** 14 GLU 14 1.305 1.228 1.516 1.531 1.434 123.65 115.34 121.13 112.51 107.30 110.98 123.44 +* * * * * +* 15 GLU 15 1.308 1.241 1.510 1.549 1.442 122.54 114.62 121.38 108.45 111.66 110.74 124.00 +* +* 16 GLY 16 1.315 1.231 1.487 - 1.434 121.92 116.70 120.37 - 112.85 - 122.93 * +* * +* 17 GLN 17 1.302 1.230 1.467 1.502 1.424 120.62 113.18 122.27 109.75 112.57 111.51 124.53 +* +** * +* +* +** 18 VAL 18 1.250 1.244 1.526 1.546 1.406 123.21 118.10 119.69 111.67 107.55 109.95 122.17 *5.7* +** * * *5.7* 19 ILE 19 1.309 1.237 1.518 1.571 1.433 119.50 116.63 120.66 110.23 108.89 113.23 122.70 * * * * * * 20 ALA 20 1.311 1.232 1.503 1.512 1.438 121.06 116.19 120.97 110.99 110.29 111.30 122.84 * * * * 21 CYS 21 1.298 1.236 1.512 1.504 1.410 121.48 115.53 121.16 109.47 110.23 109.57 123.28 ** * +** +** 22 HIS 22 1.301 1.224 1.505 1.543 1.446 122.12 115.48 121.23 110.12 108.23 111.95 123.28 ** * ** 23 THR 23 1.331 1.248 1.508 1.555 1.442 122.58 116.64 120.14 108.20 109.19 111.63 123.22 24 VAL 24 1.318 1.230 1.537 1.567 1.444 121.10 115.25 121.50 111.29 108.88 112.20 123.23 * * 25 GLU 25 1.335 1.233 1.523 1.507 1.448 123.00 116.23 120.37 108.67 110.72 109.45 123.40 * * 26 THR 26 1.335 1.230 1.532 1.544 1.455 121.61 115.34 121.04 110.11 109.54 110.91 123.61 27 TRP 27 1.327 1.231 1.548 1.543 1.461 123.06 116.20 120.83 111.85 110.49 108.25 122.92 * * * 28 ASN 28 1.327 1.243 1.531 1.552 1.475 123.09 115.42 120.63 110.26 110.60 109.38 123.94 * * 29 GLU 29 1.324 1.232 1.532 1.539 1.466 123.74 116.11 120.88 109.36 111.26 108.37 122.94 * * * 30 GLN 30 1.317 1.232 1.515 1.489 1.418 122.31 116.82 120.53 110.76 112.68 108.96 122.64 ** ** ** 31 LEU 31 1.321 1.223 1.507 1.483 1.414 122.05 117.01 119.99 110.68 112.64 109.97 122.99 ** ** ** 32 GLN 32 1.319 1.232 1.519 1.530 1.447 120.92 116.09 120.32 110.73 110.08 112.06 123.54 33 LYS 33 1.327 1.232 1.529 1.532 1.456 122.00 116.73 120.70 110.12 110.98 111.18 122.56 34 ALA 34 1.322 1.227 1.530 1.524 1.445 120.91 115.91 120.76 110.62 110.87 110.60 123.29 35 ASN 35 1.318 1.232 1.503 1.521 1.468 123.17 115.85 121.09 107.21 111.92 108.64 123.05 * +* * +* 36 GLU 36 1.308 1.240 1.534 1.530 1.473 120.04 117.55 120.26 111.41 114.01 113.52 122.19 +* * +* +* 37 SER 37 1.320 1.241 1.533 1.510 1.442 120.54 116.00 120.79 110.78 111.10 109.94 123.21 38 LYS 38 1.335 1.237 1.493 1.502 1.449 122.80 114.29 122.17 114.43 114.90 113.49 123.39 * * ** * +* ** 39 THR 39 1.281 1.240 1.500 1.516 1.406 122.20 116.58 120.70 107.73 105.62 111.00 122.68 *** * +** +* *** 40 LEU 40 1.259 1.243 1.520 1.526 1.357 121.62 115.88 120.80 113.78 108.50 112.24 123.27 *5.0* *5.3* +* * *5.3* 41 VAL 41 1.270 1.233 1.529 1.562 1.438 121.59 116.20 120.84 111.42 111.67 110.03 122.94 **** * * **** 42 VAL 42 1.310 1.238 1.519 1.536 1.440 122.12 116.85 120.66 109.25 108.33 111.90 122.48 * * * Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.306 1.235 1.531 1.553 1.444 120.92 115.54 120.54 108.82 111.19 111.41 123.91 +* +* 44 ASP 44 1.312 1.241 1.504 1.536 1.459 124.23 116.39 120.78 108.31 110.75 111.22 122.80 * * * * 45 PHE 45 1.294 1.224 1.504 1.520 1.399 121.57 117.21 120.20 108.80 106.20 109.75 122.56 ** * *** +* *** 46 THR 46 1.290 1.252 1.515 1.580 1.434 120.58 116.53 120.17 110.74 108.58 111.53 123.29 +** * * * +** 47 ALA 47 1.302 1.229 1.510 1.501 1.423 121.90 115.33 121.17 110.87 110.56 110.33 123.50 +* +* +* 48 SER 48 1.295 1.239 1.547 1.525 1.438 123.41 117.42 120.29 111.41 113.03 109.35 122.29 ** * * ** 49 TRP 49 1.340 1.230 1.537 1.544 1.437 121.44 116.39 120.73 111.45 111.95 110.08 122.88 * * 50 CYS 50 1.315 1.239 1.535 1.542 1.445 121.88 114.81 121.27 114.11 112.41 110.84 123.92 * ** ** 51 GLY 51 1.336 1.233 1.528 - 1.468 123.89 119.24 119.43 - 115.31 - 121.33 * +* * * +* 52 PRO 52 1.362 1.231 1.524 1.535 1.479 122.49 115.40 121.41 109.68 111.90 103.65 123.18 * * * 53 CYS 53 1.305 1.227 1.529 1.506 1.439 122.67 115.94 121.12 109.94 109.72 108.61 122.94 +* * * +* 54 ARG 54 1.323 1.218 1.522 1.534 1.450 122.07 115.92 120.83 111.22 110.18 110.47 123.24 55 PHE 55 1.319 1.239 1.534 1.545 1.461 122.68 117.01 120.77 109.93 112.61 110.29 122.21 56 ILE 56 1.313 1.237 1.548 1.564 1.449 120.08 115.97 120.96 110.95 111.11 110.95 123.01 * * * 57 ALA 57 1.330 1.235 1.566 1.530 1.469 123.10 120.17 119.64 111.38 114.01 110.98 120.19 +* +* * +* +* 58 PRO 58 1.378 1.235 1.528 1.521 1.471 121.99 116.45 120.78 109.61 112.47 103.74 122.76 ** ** 59 PHE 59 1.322 1.223 1.525 1.538 1.450 121.39 116.18 121.12 111.14 109.98 111.50 122.68 60 PHE 60 1.312 1.230 1.534 1.531 1.455 121.85 115.73 121.36 111.80 108.65 109.63 122.89 * * 61 ALA 61 1.327 1.235 1.537 1.520 1.459 121.84 115.97 121.23 110.86 109.96 110.48 122.80 62 ASP 62 1.334 1.238 1.490 1.515 1.470 122.34 114.04 121.45 108.73 108.73 111.13 124.51 +* * +* 63 LEU 63 1.311 1.229 1.526 1.524 1.427 124.26 115.84 120.71 111.05 110.36 108.60 123.42 * +* * * +* 64 ALA 64 1.325 1.223 1.531 1.523 1.463 122.94 116.18 121.24 110.55 111.25 110.28 122.56 65 LYS 65 1.317 1.227 1.538 1.569 1.452 122.21 116.88 120.79 113.23 111.19 109.65 122.31 +* +* +* 66 LYS 66 1.312 1.232 1.540 1.532 1.455 120.65 117.10 120.62 110.82 111.64 110.80 122.28 * * 67 LEU 67 1.319 1.229 1.532 1.545 1.439 121.38 117.50 120.71 110.71 110.09 111.83 121.78 * * 68 PRO 68 1.344 1.236 1.531 1.525 1.462 122.75 117.20 120.22 109.62 114.44 102.36 122.58 * * 69 ASN 69 1.320 1.235 1.521 1.532 1.463 120.94 115.89 121.26 111.58 111.85 110.35 122.82 70 VAL 70 1.301 1.223 1.515 1.554 1.442 121.80 116.34 120.41 110.40 109.38 111.26 123.23 +* +* 71 LEU 71 1.310 1.240 1.514 1.523 1.424 122.22 116.26 120.58 109.62 109.49 109.01 123.15 * +* +* 72 PHE 72 1.308 1.240 1.500 1.518 1.442 121.61 115.40 121.24 108.19 109.96 112.07 123.36 * * * * Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 73 LEU 73 1.281 1.221 1.494 1.535 1.436 122.71 115.52 120.90 109.81 110.61 113.36 123.58 *** * * +* *** 74 LYS 74 1.291 1.221 1.529 1.567 1.429 122.87 117.12 120.63 112.42 104.28 106.61 122.20 +** +* +* * ** ** +** 75 VAL 75 1.299 1.243 1.518 1.556 1.446 121.45 115.79 121.25 110.17 110.84 111.35 122.91 ** ** 76 ASP 76 1.305 1.238 1.521 1.510 1.441 121.89 116.36 120.56 110.46 108.25 110.32 123.07 +* * +* 77 THR 77 1.312 1.224 1.537 1.559 1.453 122.12 118.15 119.78 112.03 114.64 112.55 122.06 * * * * 78 ASP 78 1.309 1.237 1.504 1.523 1.471 119.95 113.75 121.85 109.36 108.06 111.77 124.40 * * * * 79 GLU 79 1.316 1.223 1.523 1.512 1.426 124.34 116.50 120.70 109.87 110.18 107.95 122.80 +* * +* +* 80 LEU 80 1.322 1.236 1.521 1.533 1.420 122.37 114.89 121.67 110.83 109.18 110.67 123.44 +* +* 81 LYS 81 1.308 1.235 1.536 1.540 1.447 123.23 116.45 120.73 111.96 110.18 108.45 122.79 +* * +* 82 SER 82 1.325 1.227 1.521 1.513 1.448 121.74 115.94 120.81 110.88 110.64 109.92 123.21 83 VAL 83 1.328 1.228 1.524 1.554 1.455 121.96 115.87 120.99 109.97 109.23 111.47 123.11 84 ALA 84 1.324 1.222 1.523 1.517 1.450 122.09 116.54 120.53 110.61 110.16 110.27 122.89 85 SER 85 1.321 1.242 1.546 1.525 1.449 122.09 116.42 120.63 110.72 111.31 109.54 122.93 86 ASP 86 1.329 1.232 1.528 1.535 1.470 122.69 115.96 121.20 110.37 111.12 110.44 122.84 87 TRP 87 1.315 1.233 1.531 1.530 1.448 122.58 116.07 120.47 111.07 111.78 111.21 123.46 88 ALA 88 1.343 1.231 1.525 1.528 1.479 124.10 116.16 121.11 110.82 112.09 110.74 122.68 * * * 89 ILE 89 1.307 1.241 1.517 1.542 1.436 122.01 115.39 121.32 110.26 108.87 111.29 123.21 +* * +* 90 GLN 90 1.302 1.233 1.520 1.532 1.434 121.90 115.88 121.10 109.85 109.87 109.24 123.02 +* * +* 91 ALA 91 1.310 1.237 1.515 1.515 1.438 121.97 115.31 121.44 110.76 111.03 110.52 123.25 * * * 92 MET 92 1.296 1.231 1.522 1.530 1.431 123.31 119.04 119.57 108.74 107.61 108.88 121.37 ** * * * * ** 93 PRO 93 1.327 1.223 1.537 1.522 1.448 123.93 117.17 120.82 109.91 111.37 102.37 122.00 * * 94 THR 94 1.286 1.227 1.517 1.532 1.425 121.02 116.03 120.73 110.39 110.06 111.63 123.24 *** +* *** 95 PHE 95 1.304 1.223 1.492 1.517 1.419 122.71 117.36 120.16 108.96 107.54 109.62 122.47 +* +* ** * ** 96 MET 96 1.282 1.234 1.510 1.525 1.426 119.80 114.71 121.35 112.56 110.90 110.56 123.93 *** +* * * *** 97 PHE 97 1.298 1.248 1.512 1.525 1.409 124.39 116.06 121.30 109.99 108.53 108.53 122.63 ** +** * * +** 98 LEU 98 1.291 1.227 1.527 1.545 1.431 121.15 116.25 120.75 106.88 109.20 110.25 122.97 +** * +* +** 99 LYS 99 1.301 1.227 1.479 1.521 1.439 122.31 114.79 120.58 110.30 109.30 113.20 124.55 +* ** * +* ** 100 GLU 100 1.321 1.230 1.548 1.528 1.457 124.36 115.79 121.08 110.15 110.53 110.47 123.07 * * * 101 GLY 101 1.328 1.225 1.535 - 1.449 121.74 117.88 120.06 - 113.64 - 122.06 * * 102 LYS 102 1.324 1.233 1.525 1.536 1.462 121.10 116.29 120.45 110.85 110.49 111.40 123.26 103 ILE 103 1.323 1.237 1.523 1.565 1.457 122.93 115.62 121.02 109.83 112.48 111.73 123.34 Residue-by-residue listing for refined_12 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 ----------------------------------------------------------------------------------------------------------------------------------- 104 LEU 104 1.322 1.230 1.495 1.527 1.433 121.82 115.65 121.01 108.18 109.97 112.47 123.34 * * * * * 105 ASP 105 1.309 1.227 1.500 1.535 1.448 121.93 116.05 120.98 111.67 112.49 112.14 122.92 * * * 106 LYS 106 1.310 1.230 1.522 1.539 1.442 121.58 115.76 120.99 108.32 110.77 110.08 123.25 * * 107 VAL 107 1.300 1.235 1.509 1.559 1.437 122.98 117.00 120.10 108.66 106.21 112.16 122.88 ** * +* ** 108 VAL 108 1.298 1.244 1.528 1.559 1.432 120.64 115.45 121.58 112.60 110.79 111.73 122.92 ** * +* ** 109 GLY 109 1.301 1.242 1.501 - 1.427 121.43 117.83 119.99 - 109.67 - 122.17 ** * ** 110 ALA 110 1.312 1.231 1.502 1.525 1.429 118.84 114.97 121.21 110.80 108.52 110.84 123.82 * * +* +* +* 111 LYS 111 1.299 1.226 1.501 1.520 1.419 123.91 118.05 119.28 107.89 106.39 109.11 122.67 ** * ** * * +* ** 112 LYS 112 1.312 1.236 1.531 1.525 1.440 120.78 116.84 120.34 111.25 112.93 110.49 122.78 * * 113 ASP 113 1.313 1.237 1.522 1.529 1.462 121.13 116.51 120.51 110.35 111.96 111.43 122.96 * * 114 GLU 114 1.333 1.241 1.523 1.535 1.465 121.43 116.69 120.58 110.48 111.32 111.89 122.73 115 LEU 115 1.323 1.222 1.501 1.509 1.443 120.93 115.19 120.95 108.95 109.05 110.75 123.83 * * * 116 GLN 116 1.314 1.232 1.520 1.530 1.467 122.39 116.34 120.50 108.89 110.87 111.77 123.14 * * 117 SER 117 1.328 1.242 1.528 1.525 1.457 121.66 115.44 121.23 110.49 110.28 109.96 123.31 118 THR 118 1.313 1.239 1.538 1.536 1.436 122.41 116.08 121.32 110.64 109.75 109.88 122.58 * * * 119 ILE 119 1.326 1.216 1.520 1.549 1.446 121.36 116.38 120.33 109.87 109.40 112.05 123.22 120 ALA 120 1.336 1.226 1.520 1.519 1.466 122.50 115.59 120.92 110.68 111.26 110.59 123.48 121 LYS 121 1.315 1.229 1.524 1.502 1.446 123.13 115.36 121.42 109.27 109.90 108.10 123.20 * * * 122 HIS 122 1.312 1.235 1.533 1.527 1.446 122.75 116.58 120.51 109.30 112.14 110.27 122.90 * * 123 LEU 123 1.319 1.239 1.521 1.534 1.426 122.70 115.23 121.11 112.14 110.09 108.48 123.65 +* * * +* 124 ALA 124 1.304 - 1.513 1.531 1.438 123.76 - - 110.65 107.68 110.73 - +* * * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *5.7* * +** ** *5.3* +* +* ** ** +** +* *5.7* ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 1.250 1.343 1.313 .016 *5.7* * * C-N (Pro) 1.341 .016 4 1.327 1.378 1.353 .019 ** C-O C-O 1.231 .020 123 1.216 1.252 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.467 1.566 1.521 .015 +** +* CH2G*-C (Gly) 1.516 .018 5 1.487 1.535 1.510 .018 +* * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.501 1.531 1.520 .008 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.516 1.580 1.553 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.483 1.579 1.530 .017 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.357 1.487 1.444 .019 *5.3* +* NH1-CH2G* (Gly) 1.451 .016 5 1.427 1.468 1.442 .015 * * N-CH1E (Pro) 1.466 .015 4 1.448 1.479 1.465 .011 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_12 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 2.0 114 113.18 120.17 116.08 .95 +* +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.70 119.24 117.68 .93 * CH1E-C-N (Pro) 116.9 1.5 4 115.40 117.20 116.55 .73 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.19 124.55 123.03 .64 +* O-C-N (Pro) 122.0 1.4 4 122.00 123.18 122.63 .42 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.84 124.78 122.13 1.15 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 121.17 123.89 122.03 .96 +* C-N-CH1E (Pro) 122.6 5.0 4 121.99 123.93 122.79 .71 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.28 122.27 120.83 .51 CH2G*-C-O (Gly) 120.8 2.1 5 119.43 120.40 120.05 .35 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.55 111.38 110.84 .25 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.73 112.60 110.24 1.18 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 106.88 114.43 110.40 1.48 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 104.28 114.90 110.27 1.87 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 109.67 115.31 112.44 2.02 N-CH1E-C (Pro) 111.8 2.5 4 111.37 114.44 112.54 1.16 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.27 111.84 110.73 .42 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.88 113.23 111.45 .79 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.36 103.74 103.03 .67 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.61 114.83 110.53 1.56 ** +** ------------------------------------------------------------------------------------------------------------- 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_12 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] 100 88.5% Residues in additional allowed regions [a,b,l,p] 11 9.7% Residues in generously allowed regions [~a,~b,~l,~p] 1 .9% Residues in disallowed regions [XX] 1 .9% ---- ------ 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 88.5 83.8 10.0 .5 Inside b. Omega angle st dev 122 3.3 6.0 3.0 -.9 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 79 .8 .8 .2 .2 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 14 7.9 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 45 7.4 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 43 7.1 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 102 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 30 6.6 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% 88.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.0 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2 Residue-by-residue listing for refined_12 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.19 Chi1-chi2 distribution -.15 Chi1 only -.04 Chi3 & chi4 .43 Omega .05 ------ -.02 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .44 ------ .23 ===== OVERALL AVERAGE .06 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.