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 - 62.8 - - 178.7 - - - - - - 181.1 - 33.9 - 2 GLY 2 - - - - - - - - - - - 181.2 - - - 3 HIS 3 b 58.7 - - - - - - - - - 167.7 - 25.0 - ** +** +** 4 HIS 4 A - - -75.1 - - - - - - - 174.3 -2.0 32.3 - 5 HIS 5 S B 58.7 - - - - - - - - - 184.5 - 32.7 - 6 HIS 6 b - 188.2 - - - - - - - - 179.0 -.9 32.7 - * * 7 HIS 7 t B - - -69.9 - - - - - - - 175.4 -2.1 35.2 - 8 HIS 8 T b - - -68.4 - - - - - - - 178.9 - 31.2 - 9 LEU 9 T a - 182.7 - - - - - - - - 182.0 -2.0 35.4 - 10 GLU 10 t B - 181.9 - 181.9 - - - - - - 181.1 -.8 35.1 - +* +* 11 MET 11 a 60.1 - - 179.6 - - - - - - 179.7 -.8 33.1 - +* +* 12 ALA 12 S l - - - - - - - - - - 177.1 - 30.0 - * * 13 SER 13 S B - - -57.2 - - - - - - - 174.1 - 36.3 - * * 14 GLU 14 S b 51.4 - - 179.9 - - - - - - 183.0 - 32.0 - 15 GLU 15 B 57.3 - - 169.8 - - - - - - 176.7 -1.7 35.4 - 16 GLY 16 S - - - - - - - - - - - 181.2 -1.0 - - * * 17 GLN 17 e B 51.5 - - 176.1 - - - - - - 180.5 - 30.3 - * * 18 VAL 18 E B - 179.3 - - - - - - - - 181.2 - 35.7 - 19 ILE 19 E B - - -58.7 - - - - - - - 179.9 -3.0 34.0 - * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 20 ALA 20 E B - - - - - - - - - - 180.8 -.9 34.0 - +* +* 21 CYS 21 E B 46.3 - - - - - - - - - 174.0 -1.7 32.9 - * * * 22 HIS 22 S a - - -65.4 - - - - - - - 177.6 - 33.2 - 23 THR 23 h B 60.1 - - - - - - - - - 178.1 - 35.4 - 24 VAL 24 H A - 184.5 - - - -76.0 -28.1 - - - 178.9 - 33.9 - 25 GLU 25 H A - 179.3 - 182.1 - -57.9 -51.7 - - - 178.9 - 35.5 - * * 26 THR 26 H A - - -58.4 - - -61.1 -42.9 - - - 179.3 - 34.3 - 27 TRP 27 H A - 176.4 - - - -61.9 -49.1 - - - 182.4 -1.4 34.7 - 28 ASN 28 H A - 190.7 - - - -61.7 -44.5 - - - 180.7 -3.5 35.6 - +* +* 29 GLU 29 H A - 180.0 - 180.6 - -57.7 -45.5 - - - 180.5 -2.5 34.8 - 30 GLN 30 H A - - -74.9 - - -64.6 -44.5 - - - 181.3 -1.9 34.0 - 31 LEU 31 H A - - -66.2 180.4 - -64.3 -46.5 - - - 178.4 -2.1 34.1 - 32 GLN 32 H A - 183.8 - - - -62.5 -39.0 - - - 180.1 -2.5 33.0 - 33 LYS 33 H A - 188.1 - - - -66.5 -40.5 - - - 180.4 -2.2 33.9 - 34 ALA 34 H A - - - - - -69.4 -29.9 - - - 180.5 -2.9 33.8 - * * 35 ASN 35 H A - 184.7 - - - -75.6 -54.0 - - - 184.2 -2.1 37.7 - * * * 36 GLU 36 H A - 186.4 - - - -62.2 -44.3 - - - 181.1 -3.3 35.3 - +* +* 37 SER 37 h A - - -56.3 - - - - - - - 181.3 -2.3 34.6 - 38 LYS 38 T l - - -64.7 185.4 - - - - - - 179.9 - 30.3 - * * 39 THR 39 t B - - -48.6 - - - - - - - 180.1 -1.7 35.4 - * * 40 LEU 40 E B - 188.8 - 174.5 - - - - - - 181.3 -.6 35.0 - +* +* 41 VAL 41 E B 58.3 - - - - - - - - - 175.1 -.8 32.7 - +* +* 42 VAL 42 E B - 181.3 - - - - - - - - 184.7 -3.0 34.3 - * * 43 VAL 43 E B - 185.5 - - - - - - - - 175.9 -2.4 34.1 - 44 ASP 44 E B - 165.7 - - - - - - - - 177.9 -2.9 35.3 - * * * 45 PHE 45 E B - - -60.7 - - - - - - - 175.2 -3.0 37.4 - * * 46 THR 46 E B - 186.4 - - - - - - - - 175.1 -2.6 33.1 - 47 ALA 47 t B - - - - - - - - - - 182.5 - 34.1 - 48 SER 48 T A - 185.7 - - - - - - - - 180.4 - 33.6 - 49 TRP 49 T A 54.9 - - - - - - - - - 180.4 - 32.0 - 50 CYS 50 h B - 176.2 - 219.4 - - - 56.2 - 2.0 182.7 -2.1 33.8 - ** +** +** 51 GLY 51 H - - - - - - -65.1 -64.9 - - - 179.9 -.5 - - ** ** ** 52 PRO 52 H - - - - - -57.3 -57.3 -31.3 - - - 178.4 - 38.7 - * * 53 CYS 53 H A - - -52.6 - - -67.2 -39.6 56.2 - 2.0 177.8 - 35.6 - +** +** 54 ARG 54 H A - 176.1 - 173.8 - -70.5 -30.6 - - - 178.6 -1.6 34.1 - 55 PHE 55 H A - 179.2 - - - -70.5 -35.7 - - - 183.5 -1.9 34.4 - 56 ILE 56 H A - 192.4 - - - -87.4 -17.5 - - - 182.1 -1.8 34.5 - +* +* +* 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 - - - - - -56.1 -46.8 - - - 180.3 -1.3 31.7 - * * 58 PRO 58 H - - - - - -60.7 -60.7 -28.4 - - - 178.6 - 38.3 - * * 59 PHE 59 H A - 180.4 - - - -75.0 -35.1 - - - 178.0 -.6 33.7 - +* +* 60 PHE 60 H A - 187.6 - - - -68.9 -33.6 - - - 176.4 -1.4 34.5 - 61 ALA 61 H A - - - - - -69.2 -27.5 - - - 177.6 -2.0 34.0 - * * 62 ASP 62 H A - 184.4 - - - -74.0 -46.0 - - - 174.9 -.9 35.4 - +* +* 63 LEU 63 H A - - -76.0 175.2 - -53.6 -41.5 - - - 179.4 -2.5 35.2 - 64 ALA 64 H A - - - - - -60.8 -36.9 - - - 178.4 -1.9 33.2 - 65 LYS 65 H A - 185.9 - - - -79.4 -33.9 - - - 183.1 -.9 33.1 - * * * 66 LYS 66 H A - 182.9 - 180.4 - -65.6 -38.9 - - - 178.1 -2.5 33.8 - 67 LEU 67 h b - - -67.9 170.5 - - - - - - 182.2 -2.5 33.0 - 68 PRO 68 T - - - - - -69.5 - - - - - 184.0 - 38.4 - * * 69 ASN 69 e A - 187.1 - - - - - - - - 178.1 - 33.6 - 70 VAL 70 E B - 178.0 - - - - - - - - 180.3 -.6 33.5 - +* +* 71 LEU 71 E B - - -61.5 178.0 - - - - - - 177.3 -2.8 35.8 - * * 72 PHE 72 E B - - -62.8 - - - - - - - 182.5 -.5 33.2 - ** ** 73 LEU 73 E B - - -81.1 - - - - - - - 178.0 -2.5 33.3 - 74 LYS 74 E B - 191.5 - - - - - - - - 179.3 -3.0 35.2 - * * 75 VAL 75 E B - 181.2 - - - - - - - - 176.8 -3.3 35.3 - +* +* 76 ASP 76 E B - 186.7 - - - - - - - - 185.1 -1.4 32.7 - 77 THR 77 e A 52.6 - - - - - - - - - 176.0 -1.6 33.1 - 78 ASP 78 T A - 186.8 - - - - - - - - 177.6 - 34.7 - 79 GLU 79 T a - 193.3 - - - - - - - - 182.1 - 37.7 - * * 80 LEU 80 h a - - -72.6 - - - - - - - 182.9 -3.3 35.5 - +* +* 81 LYS 81 H A 56.3 - - 183.7 - -58.4 -37.4 - - - 180.1 -1.3 32.3 - 82 SER 82 H A - - -59.5 - - -77.6 -26.2 - - - 175.0 - 32.8 - * * * 83 VAL 83 H A - 181.3 - - - -75.1 -40.4 - - - 179.4 - 34.0 - 84 ALA 84 H A - - - - - -58.0 -46.4 - - - 179.1 -3.0 34.2 - * * 85 SER 85 H A 55.7 - - - - -64.3 -31.6 - - - 180.9 -2.0 33.3 - 86 ASP 86 H A - 181.3 - - - -72.1 -37.0 - - - 178.1 -.9 34.6 - * * 87 TRP 87 h A - - -72.8 - - - - - - - 177.9 -2.2 32.7 - 88 ALA 88 T l - - - - - - - - - - 179.6 -.9 33.3 - +* +* 89 ILE 89 t b - - -53.9 - - - - - - - 181.6 -3.1 34.2 - * * 90 GLN 90 A - - -63.1 179.8 - - - - - - 182.1 -1.1 34.7 - * * 91 ALA 91 S B - - - - - - - - - - 179.5 - 34.1 - 92 MET 92 S B - - -58.9 178.3 - - - - - - -2.2 - 35.1 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 PRO 93 e cis - - - - - -95.7 - - - - - 174.2 - 40.3 - +** * +* +** 94 THR 94 E B - - -58.9 - - - - - - - 179.9 -2.5 33.4 - 95 PHE 95 E B - - -62.0 - - - - - - - 178.4 -3.0 36.1 - * * 96 MET 96 E B - 181.7 - 178.3 - - - - - - 179.2 -2.9 33.3 - * * 97 PHE 97 E B - - -67.8 - - - - - - - 178.0 -2.9 36.6 - * * 98 LEU 98 E B 62.8 - - - - - - - - - 184.7 -1.6 31.1 - 99 LYS 99 E B - 178.2 - 179.4 - - - - - - 176.3 -3.3 34.2 - +* +* 100 GLU 100 T l - - -58.6 178.6 - - - - - - 181.6 - 33.4 - 101 GLY 101 T - - - - - - - - - - - 178.0 - - - 102 LYS 102 E B - - -62.2 - - - - - - - 183.7 -2.2 34.4 - 103 ILE 103 E B - - -58.8 178.6 - - - - - - 178.6 - 32.6 - 104 LEU 104 E a - - -62.7 180.8 - - - - - - 182.3 -1.8 34.5 - 105 ASP 105 E B 56.8 - - - - - - - - - 183.0 -2.3 31.6 - 106 LYS 106 E B - - -56.4 174.8 - - - - - - 176.7 - 36.3 - 107 VAL 107 E B - 182.1 - - - - - - - - 179.6 -3.6 35.0 - ** ** 108 VAL 108 E B 58.9 - - - - - - - - - 179.9 -.6 32.4 - +* +* 109 GLY 109 e - - - - - - - - - - - 177.7 -3.0 - - * * 110 ALA 110 B - - - - - - - - - - 178.5 - 34.6 - 111 LYS 111 h B - - -64.1 180.2 - - - - - - 184.3 -1.0 35.5 - * * 112 LYS 112 H A - 182.6 - 180.9 - -61.0 -50.9 - - - 184.3 - 34.7 - * * 113 ASP 113 H A - 180.4 - - - -72.0 -41.1 - - - 179.5 - 32.6 - 114 GLU 114 H A - - -64.3 - - -64.1 -40.6 - - - 179.6 - 33.6 - 115 LEU 115 H A - 186.3 - - - -62.8 -52.3 - - - 179.6 -2.3 34.9 - * * 116 GLN 116 H A - - -59.2 - - -58.3 -34.3 - - - 178.7 -2.2 32.7 - 117 SER 117 H A - - -57.7 - - -72.0 -38.0 - - - 176.6 -2.2 33.2 - 118 THR 118 H A - - -60.8 - - -66.8 -38.9 - - - 178.0 -2.5 34.5 - 119 ILE 119 H A - - -59.0 177.2 - -66.6 -36.3 - - - 176.9 -2.9 32.7 - * * 120 ALA 120 H A - - - - - -69.2 -33.4 - - - 175.8 -2.0 32.9 - 121 LYS 121 H A - - -79.5 182.1 - -64.9 -37.5 - - - 178.4 -1.9 35.2 - 122 HIS 122 H A - - -75.3 - - -84.9 -23.3 - - - 181.5 -1.9 33.7 - +* * +* 123 LEU 123 h B - 191.9 - - - - - - - - 179.3 -1.9 35.3 - 124 ALA 124 - - - - - - - - - - - - - 34.2 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * * ** +** +* ** +** ** ** +** +** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.7 183.5 -63.8 180.0 -70.8 -66.8 -39.0 56.2 - 2.0 179.4 -2.0 34.1 +** +** Standard deviations: 4.3 5.2 7.5 8.2 17.3 7.5 8.9 .0 - .0 2.8 .8 1.9 Numbers of values: 17 44 41 30 4 46 46 2 0 2 122 84 119 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 - 1.247 1.526 1.538 1.469 - 116.85 120.69 109.71 111.03 111.26 122.46 2 GLY 2 1.324 1.236 1.510 - 1.432 120.11 118.01 120.24 - 113.14 - 121.74 * * 3 HIS 3 1.326 1.220 1.521 1.570 1.447 118.80 115.33 121.89 113.39 115.51 116.87 122.68 ** +* +* +* +*** +*** 4 HIS 4 1.319 1.220 1.503 1.538 1.462 121.39 114.15 122.20 110.79 107.74 113.79 123.64 * * * +* +* 5 HIS 5 1.310 1.232 1.509 1.572 1.423 123.06 116.13 120.86 112.84 107.53 111.78 122.92 * ** +* * * ** 6 HIS 6 1.312 1.234 1.525 1.545 1.450 121.09 114.72 121.32 111.48 110.51 111.54 123.80 * * 7 HIS 7 1.309 1.241 1.501 1.556 1.450 125.06 117.18 120.05 107.85 108.28 112.57 122.76 * * * +* * * * +* 8 HIS 8 1.313 1.237 1.510 1.532 1.441 120.29 114.35 121.83 111.48 110.23 113.75 123.59 * +* +* 9 LEU 9 1.294 1.232 1.528 1.540 1.439 123.43 114.99 121.52 110.97 108.64 108.80 123.44 ** ** 10 GLU 10 1.321 1.226 1.522 1.543 1.438 122.94 116.36 120.94 110.65 109.07 109.56 122.70 * * 11 MET 11 1.305 1.230 1.523 1.540 1.455 122.28 114.61 121.01 111.22 110.24 111.25 124.26 +* +* 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 1.330 1.234 1.509 1.534 1.465 125.50 114.55 121.80 112.40 112.17 113.45 123.56 ** * ** ** 13 SER 13 1.303 1.235 1.501 1.539 1.439 124.94 118.07 119.12 108.21 105.74 110.94 122.79 +* * * +* +* +* 14 GLU 14 1.301 1.243 1.530 1.518 1.409 120.47 114.82 121.82 113.35 109.95 110.80 123.22 +* +** +* +** 15 GLU 15 1.310 1.232 1.511 1.533 1.444 122.85 116.46 120.85 108.59 110.51 110.58 122.69 * * 16 GLY 16 1.300 1.237 1.499 - 1.431 120.21 116.77 120.51 - 112.77 - 122.71 ** * ** 17 GLN 17 1.301 1.233 1.479 1.519 1.417 119.92 113.12 122.37 111.64 112.31 114.00 124.50 +* ** ** +* ** ** 18 VAL 18 1.270 1.233 1.497 1.560 1.422 123.82 117.39 119.89 109.47 106.61 110.87 122.70 **** * +* * +* **** 19 ILE 19 1.293 1.230 1.513 1.541 1.423 119.68 115.89 121.01 110.49 109.40 111.31 123.09 +** +* * +** 20 ALA 20 1.301 1.239 1.505 1.521 1.432 121.73 116.18 120.87 110.79 109.62 110.65 122.95 ** * ** 21 CYS 21 1.298 1.237 1.497 1.515 1.411 121.44 114.41 121.95 111.16 112.23 111.01 123.58 ** * ** ** 22 HIS 22 1.292 1.226 1.518 1.543 1.427 122.97 115.19 121.48 111.60 108.17 111.78 123.33 +** +* * +** 23 THR 23 1.335 1.252 1.513 1.562 1.439 122.83 117.13 119.93 108.17 107.36 112.27 122.94 * * * 24 VAL 24 1.308 1.219 1.529 1.548 1.440 121.13 115.85 120.89 110.22 108.76 111.74 123.23 +* +* 25 GLU 25 1.333 1.242 1.532 1.529 1.466 122.89 115.88 120.70 109.36 110.55 109.32 123.41 26 THR 26 1.329 1.242 1.535 1.550 1.455 122.47 115.52 120.84 110.50 110.51 110.21 123.62 27 TRP 27 1.324 1.239 1.541 1.541 1.457 123.06 115.66 120.97 111.33 111.30 108.55 123.35 * * 28 ASN 28 1.319 1.242 1.527 1.532 1.465 123.22 115.12 121.14 109.04 110.54 109.64 123.73 29 GLU 29 1.328 1.235 1.527 1.524 1.452 123.30 116.05 120.67 110.28 111.02 109.33 123.28 30 GLN 30 1.323 1.220 1.508 1.486 1.422 122.64 117.11 120.19 110.41 113.14 109.62 122.70 ** +* ** 31 LEU 31 1.319 1.235 1.498 1.487 1.414 121.77 116.68 120.00 110.29 112.19 110.03 123.32 * ** ** ** 32 GLN 32 1.315 1.220 1.528 1.533 1.436 120.55 116.35 120.64 110.90 109.74 111.87 122.94 * * 33 LYS 33 1.328 1.236 1.532 1.537 1.452 121.42 116.87 120.39 110.19 110.39 111.00 122.71 34 ALA 34 1.338 1.223 1.517 1.522 1.452 121.15 115.55 120.97 110.64 110.50 110.65 123.47 35 ASN 35 1.316 1.224 1.505 1.519 1.461 123.02 114.33 121.72 107.09 110.17 108.59 123.95 +* * +* 36 GLU 36 1.305 1.238 1.537 1.532 1.455 123.64 116.77 120.97 110.16 111.74 108.59 122.21 +* * * +* 37 SER 37 1.308 1.235 1.528 1.515 1.435 120.77 115.80 120.64 110.97 111.06 108.99 123.56 +* * +* 38 LYS 38 1.340 1.231 1.514 1.511 1.457 123.61 114.90 121.92 112.36 112.74 112.73 123.16 * * * * 39 THR 39 1.290 1.236 1.523 1.526 1.421 122.52 116.10 121.08 109.36 108.37 110.48 122.79 +** +* * +** 40 LEU 40 1.285 1.236 1.540 1.565 1.441 121.96 117.34 120.02 111.95 106.51 109.13 122.59 *** +* +* *** 41 VAL 41 1.311 1.230 1.534 1.570 1.436 121.40 116.05 120.83 111.92 111.37 111.10 123.05 * * * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.310 1.243 1.518 1.539 1.441 122.81 116.97 120.49 109.36 107.71 112.22 122.53 * * * 43 VAL 43 1.309 1.237 1.531 1.554 1.446 120.26 115.17 120.87 109.23 111.78 111.51 123.95 * * 44 ASP 44 1.316 1.234 1.518 1.545 1.465 124.86 117.33 120.35 109.99 109.96 109.41 122.25 +* +* 45 PHE 45 1.314 1.245 1.526 1.530 1.424 120.65 116.83 120.28 107.37 109.07 109.27 122.88 * +* * +* 46 THR 46 1.316 1.230 1.538 1.537 1.439 121.62 117.22 120.42 110.74 110.67 111.57 122.34 47 ALA 47 1.303 1.233 1.520 1.512 1.438 122.14 116.56 120.32 110.51 108.57 110.89 123.12 +* * +* 48 SER 48 1.314 1.241 1.562 1.545 1.465 123.30 117.11 120.78 111.41 112.72 109.30 122.08 * +* +* 49 TRP 49 1.327 1.239 1.540 1.546 1.457 121.69 117.16 120.38 111.39 113.11 111.49 122.43 50 CYS 50 1.317 1.233 1.534 1.532 1.460 121.44 115.51 120.82 110.39 111.03 110.62 123.66 51 GLY 51 1.332 1.230 1.528 - 1.462 122.94 119.15 119.49 - 114.32 - 121.36 * * * * 52 PRO 52 1.366 1.229 1.528 1.533 1.484 122.66 115.31 121.49 110.32 111.56 103.39 123.19 +* * * +* 53 CYS 53 1.308 1.222 1.533 1.505 1.446 122.84 115.92 121.56 110.27 109.79 108.28 122.50 +* * * +* 54 ARG 54 1.316 1.230 1.529 1.531 1.449 122.28 115.59 121.07 111.69 110.02 109.36 123.32 55 PHE 55 1.319 1.233 1.538 1.543 1.455 122.89 116.70 120.69 110.60 111.30 109.69 122.60 56 ILE 56 1.322 1.241 1.556 1.577 1.462 121.36 115.37 121.60 110.53 110.19 110.24 123.00 * * * 57 ALA 57 1.327 1.238 1.561 1.525 1.469 123.74 120.59 119.04 111.10 115.14 110.99 120.36 +* * ** * * +* ** 58 PRO 58 1.378 1.239 1.535 1.535 1.478 122.08 116.19 120.93 110.49 112.38 103.67 122.87 ** ** 59 PHE 59 1.321 1.229 1.528 1.536 1.451 121.83 115.99 121.16 110.99 110.05 110.75 122.84 60 PHE 60 1.315 1.229 1.536 1.539 1.459 122.26 115.48 121.52 111.68 108.64 109.21 122.99 61 ALA 61 1.325 1.241 1.535 1.517 1.458 122.45 115.60 121.05 110.50 110.27 110.30 123.34 62 ASP 62 1.325 1.234 1.501 1.521 1.467 122.88 114.56 121.22 109.52 108.51 110.02 124.21 * * 63 LEU 63 1.323 1.232 1.521 1.532 1.441 124.03 115.75 120.78 110.21 110.94 109.17 123.45 * * 64 ALA 64 1.321 1.234 1.530 1.515 1.449 122.66 117.28 120.68 111.01 112.18 110.43 122.05 65 LYS 65 1.324 1.227 1.520 1.555 1.449 120.05 115.69 121.02 112.50 109.13 110.64 123.25 * * * 66 LYS 66 1.312 1.229 1.534 1.529 1.443 122.18 116.91 120.48 111.40 111.42 109.66 122.62 * * 67 LEU 67 1.317 1.228 1.530 1.510 1.436 121.63 116.85 121.02 111.92 111.56 109.96 122.11 * * 68 PRO 68 1.344 1.231 1.540 1.533 1.472 123.49 117.56 120.27 110.26 114.77 103.36 122.17 * * 69 ASN 69 1.322 1.228 1.534 1.543 1.470 120.85 115.81 122.01 111.16 110.36 110.55 122.18 70 VAL 70 1.298 1.234 1.517 1.556 1.436 121.70 116.39 120.52 110.98 108.92 111.77 123.05 ** * ** 71 LEU 71 1.305 1.229 1.510 1.520 1.423 122.42 116.68 120.59 109.34 109.54 109.58 122.71 +* +* +* 72 PHE 72 1.295 1.236 1.491 1.516 1.435 121.14 115.10 121.27 110.15 109.30 112.58 123.62 ** +* * * ** 73 LEU 73 1.280 1.230 1.495 1.540 1.443 122.78 114.87 121.18 109.17 111.79 112.74 123.95 +*** * * +*** 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 ----------------------------------------------------------------------------------------------------------------------------------- 74 LYS 74 1.296 1.231 1.516 1.554 1.423 123.23 116.16 120.95 111.43 106.60 109.45 122.87 ** * +* +* ** 75 VAL 75 1.291 1.234 1.494 1.550 1.434 121.81 116.94 120.11 108.68 108.07 111.64 122.91 +** * * * +** 76 ASP 76 1.303 1.217 1.506 1.513 1.434 119.95 115.92 120.60 111.50 108.82 111.99 123.45 +* * +* 77 THR 77 1.311 1.227 1.520 1.534 1.452 122.97 117.13 120.45 110.47 113.43 110.82 122.40 * * 78 ASP 78 1.313 1.232 1.504 1.526 1.447 120.00 114.05 121.78 109.89 107.14 111.26 124.17 * * * * 79 GLU 79 1.312 1.225 1.519 1.513 1.436 123.92 114.87 121.85 107.88 109.05 108.04 123.24 * * * * * * 80 LEU 80 1.315 1.228 1.532 1.539 1.435 124.44 115.95 120.80 109.61 110.88 109.42 123.17 * +* +* 81 LYS 81 1.317 1.227 1.547 1.536 1.461 123.34 117.76 120.24 111.86 113.57 110.33 121.96 * * 82 SER 82 1.325 1.242 1.536 1.517 1.456 120.40 116.06 121.35 111.73 111.11 110.56 122.59 83 VAL 83 1.318 1.230 1.532 1.554 1.449 121.35 115.45 121.23 110.22 108.65 111.64 123.29 84 ALA 84 1.329 1.235 1.519 1.520 1.458 123.15 116.26 120.80 110.27 111.10 110.23 122.93 85 SER 85 1.325 1.232 1.534 1.536 1.443 121.73 116.44 120.73 111.60 111.39 110.21 122.79 86 ASP 86 1.327 1.234 1.524 1.525 1.465 121.86 115.66 121.25 110.06 110.58 109.94 123.05 87 TRP 87 1.319 1.235 1.523 1.530 1.448 122.62 115.81 120.46 111.09 111.94 111.26 123.73 88 ALA 88 1.344 1.239 1.526 1.532 1.469 123.94 116.11 121.12 111.06 111.40 110.62 122.73 * * * 89 ILE 89 1.313 1.231 1.519 1.554 1.440 121.41 115.91 120.94 109.46 108.62 112.24 123.08 * * 90 GLN 90 1.306 1.232 1.510 1.517 1.438 121.90 116.35 120.64 109.66 111.15 110.19 123.00 +* * +* 91 ALA 91 1.310 1.232 1.512 1.519 1.438 121.63 116.46 120.91 110.45 110.43 110.44 122.62 * * * 92 MET 92 1.302 1.240 1.514 1.517 1.432 121.01 118.12 119.89 109.08 109.39 110.68 121.98 +* * +* 93 PRO 93 1.332 1.233 1.537 1.525 1.453 123.66 117.24 120.83 109.70 111.55 101.77 121.89 * * 94 THR 94 1.286 1.230 1.513 1.528 1.426 119.91 116.24 120.51 110.37 109.32 112.07 123.25 *** +* *** 95 PHE 95 1.306 1.230 1.498 1.525 1.411 122.48 116.82 120.57 108.90 108.28 110.02 122.60 +* * ** * ** 96 MET 96 1.284 1.240 1.492 1.522 1.428 120.19 115.14 121.06 110.75 109.65 111.80 123.79 *** +* +* *** 97 PHE 97 1.291 1.246 1.506 1.518 1.395 122.63 116.50 121.12 109.42 108.74 108.72 122.38 +** *** * *** 98 LEU 98 1.291 1.224 1.515 1.566 1.397 120.30 117.43 120.31 114.28 109.46 111.90 122.26 +** +* *** ** *** 99 LYS 99 1.289 1.232 1.493 1.527 1.427 120.56 114.68 120.84 110.59 110.95 110.27 124.44 +** +* +* +** 100 GLU 100 1.326 1.238 1.544 1.532 1.458 124.44 115.72 121.10 111.03 111.64 110.34 123.10 +* +* 101 GLY 101 1.326 1.228 1.527 - 1.453 121.88 117.14 120.48 - 113.38 - 122.39 102 LYS 102 1.323 1.227 1.520 1.543 1.465 121.54 117.25 119.88 108.44 109.03 112.56 122.87 * * 103 ILE 103 1.317 1.237 1.528 1.558 1.460 121.93 116.07 120.84 110.80 111.94 111.88 123.08 104 LEU 104 1.327 1.240 1.505 1.522 1.434 122.16 116.00 120.56 109.70 110.38 110.87 123.42 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 105 ASP 105 1.317 1.232 1.508 1.531 1.435 121.87 115.31 121.44 111.29 112.40 112.50 123.23 * * * 106 LYS 106 1.304 1.237 1.522 1.541 1.449 122.53 117.08 120.27 108.51 109.36 109.73 122.65 +* +* 107 VAL 107 1.306 1.228 1.515 1.560 1.446 121.51 116.58 120.50 108.73 108.22 111.94 122.91 +* * +* 108 VAL 108 1.303 1.243 1.533 1.566 1.435 121.35 115.76 121.05 111.96 110.83 111.60 123.14 +* * * +* 109 GLY 109 1.315 1.241 1.507 - 1.433 121.46 117.13 120.42 - 111.32 - 122.44 * * 110 ALA 110 1.320 1.243 1.499 1.526 1.429 119.96 114.65 121.49 110.50 108.00 110.73 123.82 * +* * +* 111 LYS 111 1.287 1.234 1.498 1.515 1.413 123.73 116.87 119.68 110.36 107.50 109.54 123.45 *** * ** * * *** 112 LYS 112 1.306 1.232 1.535 1.520 1.436 122.15 116.79 120.47 110.51 111.95 108.99 122.64 +* * +* 113 ASP 113 1.324 1.230 1.516 1.530 1.462 120.95 116.55 120.67 110.89 111.73 111.64 122.77 114 GLU 114 1.318 1.239 1.513 1.521 1.469 121.53 116.74 120.20 109.53 111.44 111.63 123.06 115 LEU 115 1.324 1.220 1.497 1.513 1.442 120.74 115.45 120.93 108.88 108.89 111.32 123.59 * * 116 GLN 116 1.316 1.237 1.530 1.532 1.463 121.98 117.04 120.32 110.34 111.82 112.00 122.63 117 SER 117 1.328 1.217 1.530 1.521 1.444 120.63 116.34 120.89 112.05 110.20 110.19 122.73 * * 118 THR 118 1.316 1.232 1.531 1.541 1.450 122.25 116.49 121.02 110.39 109.84 110.30 122.45 119 ILE 119 1.317 1.213 1.528 1.546 1.440 120.95 116.91 120.41 111.24 110.01 112.02 122.63 120 ALA 120 1.328 1.232 1.527 1.518 1.463 121.70 116.18 120.81 111.03 110.58 111.29 123.01 121 LYS 121 1.326 1.231 1.525 1.504 1.408 123.52 116.09 121.06 111.37 111.01 107.77 122.85 * +** * +* +** 122 HIS 122 1.315 1.225 1.528 1.525 1.438 122.03 116.79 120.20 110.14 112.07 110.88 123.01 * * 123 LEU 123 1.334 1.236 1.518 1.522 1.429 123.23 115.32 120.87 111.97 110.22 107.40 123.80 +* +* +* 124 ALA 124 1.309 - 1.505 1.536 1.440 123.87 - - 110.59 107.60 111.29 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- 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 1.270 1.344 1.313 .014 **** * * C-N (Pro) 1.341 .016 4 1.332 1.378 1.355 .018 ** C-O C-O 1.231 .020 123 1.213 1.252 1.233 .007 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.479 1.562 1.521 .015 ** +* CH2G*-C (Gly) 1.516 .018 5 1.499 1.528 1.514 .012 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.512 1.536 1.523 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.526 1.577 1.551 .013 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.572 1.530 .015 ** ** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.395 1.470 1.443 .016 *** NH1-CH2G* (Gly) 1.451 .016 5 1.431 1.462 1.442 .013 * N-CH1E (Pro) 1.466 .015 4 1.453 1.484 1.472 .012 * ------------------------------------------------------------------------------------------------------------- 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 2.0 114 113.12 120.59 116.10 1.02 +* ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 116.77 119.15 117.64 .86 * CH1E-C-N (Pro) 116.9 1.5 4 115.31 117.56 116.57 .89 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.36 124.50 122.99 .62 +* O-C-N (Pro) 122.0 1.4 4 121.89 123.19 122.53 .52 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.80 125.50 122.10 1.29 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 5 120.11 122.94 121.32 1.06 * C-N-CH1E (Pro) 122.6 5.0 4 122.08 123.66 122.97 .64 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.04 122.37 120.85 .58 * CH2G*-C-O (Gly) 120.8 2.1 5 119.49 120.51 120.23 .38 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.27 112.40 110.83 .52 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.17 111.96 110.15 .97 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.09 114.28 110.54 1.33 +* ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.74 115.51 110.20 1.75 +* +* NH1-CH2G*-C (Gly) 112.5 2.9 5 111.32 114.32 112.98 .98 N-CH1E-C (Pro) 111.8 2.5 4 111.55 114.77 112.57 1.32 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.23 113.45 110.92 .80 ** NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 110.21 112.27 111.43 .66 N-CH1E-CH2E (Pro) 103.0 1.1 4 101.77 103.67 103.05 .75 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.40 116.87 110.54 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_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] 97 85.8% Residues in additional allowed regions [a,b,l,p] 16 14.2% 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 85.8 83.8 10.0 .2 Inside b. Omega angle st dev 122 2.8 6.0 3.0 -1.1 BETTER 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 84 .8 .8 .2 .1 Inside f. Overall G-factor 124 .1 -.4 .3 1.7 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 17 4.3 18.1 6.5 -2.1 BETTER b. Chi-1 trans st dev 44 5.2 19.0 5.3 -2.6 BETTER c. Chi-1 gauche plus st dev 41 7.5 17.5 4.9 -2.1 BETTER d. Chi-1 pooled st dev 102 7.0 18.2 4.8 -2.3 BETTER e. Chi-2 trans st dev 30 8.2 20.4 5.0 -2.4 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% 85.8 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.0 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 -.22 Chi1-chi2 distribution -.11 Chi1 only .22 Chi3 & chi4 .31 Omega .21 ------ .03 ===== Main-chain covalent forces:- Main-chain bond lengths .04 Main-chain bond angles .43 ------ .27 ===== OVERALL AVERAGE .11 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.