Residue-by-residue listing for refined_15 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - - -63.5 - - - - - - - 179.4 - 34.8 - 2 GLY 2 - - - - - - - - - - - 184.5 - - - 3 HIS 3 S A - 186.6 - - - - - - - - 178.8 - 34.2 - 4 HIS 4 S B - - -63.5 - - - - - - - 184.8 - 31.6 - 5 HIS 5 S l - 186.5 - - - - - - - - 179.6 - 30.8 - 6 HIS 6 B - 177.2 - - - - - - - - 181.7 - 35.7 - 7 HIS 7 b 62.7 - - - - - - - - - 181.7 -.6 29.4 - +* * +* 8 HIS 8 B 58.9 - - - - - - - - - 184.9 -.7 33.5 - +* +* 9 LEU 9 S l - - -61.0 179.6 - - - - - - 181.0 - 33.2 - 10 GLU 10 S B - 208.8 - - - - - - - - 181.9 - 35.8 - * * 11 MET 11 B - - -61.7 178.9 - - - - - - 180.9 - 33.9 - 12 ALA 12 b - - - - - - - - - - 176.6 - 32.6 - 13 SER 13 S B 57.5 - - - - - - - - - 178.9 -1.3 34.6 - 14 GLU 14 B - 181.6 - 176.2 - - - - - - 174.1 - 32.6 - * * 15 GLU 15 B 67.3 - - - - - - - - - 180.9 - 32.5 - 16 GLY 16 S - - - - - - - - - - - 179.3 -1.9 - - 17 GLN 17 S B 52.6 - - 181.8 - - - - - - 183.3 - 33.0 - 18 VAL 18 B - 182.9 - - - - - - - - 178.7 - 35.2 - 19 ILE 19 E B - - -69.2 - - - - - - - 179.8 -2.6 33.1 - 20 ALA 20 E B - - - - - - - - - - 181.3 -.8 33.8 - +* +* 21 CYS 21 E B - - -53.1 - - - - - - - 177.9 -.8 35.0 - +* +* Residue-by-residue listing for refined_15 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 - - -65.2 - - - - - - - 182.7 -.5 34.2 - +* +* 23 THR 23 h B 54.6 - - - - - - - - - 176.5 - 35.6 - 24 VAL 24 H A - 179.7 - - - -71.4 -26.9 - - - 179.3 - 34.0 - * * 25 GLU 25 H A - - -66.3 - - -57.1 -51.6 - - - 178.5 - 35.4 - * * 26 THR 26 H A - - -55.1 - - -70.9 -40.6 - - - 178.5 - 34.4 - 27 TRP 27 H A - 166.0 - - - -53.4 -54.8 - - - 181.4 -2.0 35.3 - * * * * 28 ASN 28 H A - 181.8 - - - -68.1 -38.4 - - - 180.8 -3.4 34.9 - +* +* 29 GLU 29 H A - 184.4 - 175.0 - -63.0 -46.3 - - - 180.5 -2.0 32.9 - 30 GLN 30 H A - - -69.8 - - -67.0 -42.2 - - - 178.9 -3.2 33.5 - +* +* 31 LEU 31 H A - - -68.7 180.9 - -65.2 -43.8 - - - 176.8 -2.1 34.0 - 32 GLN 32 H A - 184.3 - - - -61.5 -40.4 - - - 178.4 -2.5 34.0 - 33 LYS 33 H A - 186.2 - - - -61.7 -47.8 - - - 181.0 -2.3 33.3 - 34 ALA 34 H A - - - - - -66.5 -39.3 - - - 180.1 -3.0 33.8 - * * 35 ASN 35 H A - 184.7 - - - -64.9 -54.8 - - - 181.6 -3.1 37.5 - * * * * 36 GLU 36 H A - 185.6 - 179.1 - -63.3 -36.8 - - - 179.0 -3.3 33.5 - +* +* 37 SER 37 h A - - -56.6 - - - - - - - 175.9 -2.4 33.6 - 38 LYS 38 T L - 197.8 - 179.2 - - - - - - 183.2 -1.4 34.4 - 39 THR 39 t B - - -45.8 - - - - - - - 180.9 -2.7 35.2 - * * 40 LEU 40 e B - 186.4 - 170.7 - - - - - - 182.7 - 33.5 - 41 VAL 41 E B 59.2 - - - - - - - - - 178.6 - 34.2 - 42 VAL 42 E B 62.8 - - - - - - - - - 181.6 -2.8 33.1 - 43 VAL 43 E B - 179.9 - - - - - - - - 177.4 -3.2 34.0 - +* +* 44 ASP 44 E B - 172.1 - - - - - - - - 175.8 -3.0 36.2 - * * 45 PHE 45 E B - - -64.2 - - - - - - - 187.5 -3.2 34.8 - * +* +* 46 THR 46 E B - 181.6 - - - - - - - - 175.6 -3.2 35.4 - +* +* 47 ALA 47 t B - - - - - - - - - - 180.4 - 34.2 - 48 SER 48 T A - - -58.9 - - - - - - - 180.7 - 33.8 - 49 TRP 49 T A 54.4 - - - - - - - - - 181.8 - 33.3 - 50 CYS 50 h B - 172.3 - 216.8 - - - 71.1 - 2.8 180.2 -1.3 33.3 - ** +* *7.5* *7.5* 51 GLY 51 H - - - - - - -62.6 -65.6 - - - 178.1 - - - ** ** 52 PRO 52 H - - - - - -53.1 -53.1 -33.9 - - - 177.2 - 37.9 - * * * * 53 CYS 53 H A - - -65.1 - - -65.5 -41.5 71.1 - 2.8 180.9 - 34.4 - +* *7.5* *7.5* 54 ARG 54 H A - 183.8 - 181.1 - -71.9 -29.9 - - - 177.7 -1.9 34.9 - 55 PHE 55 H A - 177.3 - - - -72.5 -37.8 - - - 185.2 -2.1 34.3 - 56 ILE 56 H A - 195.3 - - - -86.8 -15.6 - - - 180.4 -2.1 33.7 - +* ** ** 57 ALA 57 H A - - - - - -54.4 -52.7 - - - 179.8 -1.4 31.2 - * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 58 PRO 58 H - - - - - -63.5 -63.5 -31.0 - - - 179.6 - 38.5 - * * 59 PHE 59 H A - 181.1 - - - -70.6 -42.1 - - - 179.8 -.5 33.8 - ** ** 60 PHE 60 H A - 190.0 - - - -69.6 -33.5 - - - 175.3 -2.7 33.9 - 61 ALA 61 H A - - - - - -69.8 -33.7 - - - 177.1 -2.3 33.8 - 62 ASP 62 H A - 185.2 - - - -66.1 -44.2 - - - 175.5 -1.8 35.4 - 63 LEU 63 H A - - -65.8 181.7 - -54.6 -44.3 - - - 179.3 -2.5 35.4 - 64 ALA 64 H A - - - - - -62.8 -32.8 - - - 178.2 -1.8 33.8 - 65 LYS 65 H A - 183.4 - 180.5 - -80.1 -28.8 - - - 183.5 -1.2 34.4 - * * * 66 LYS 66 H A - 186.8 - 175.0 - -78.4 -40.1 - - - 178.2 -2.1 34.8 - * * 67 LEU 67 h b - - -66.5 171.3 - - - - - - 184.0 -3.0 33.1 - * * 68 PRO 68 S - - - - - -71.1 - - - - - 185.3 - 39.0 - * * 69 ASN 69 S A - 188.5 - - - - - - - - 178.7 - 33.6 - 70 VAL 70 S B - 179.0 - - - - - - - - 181.6 - 33.4 - 71 LEU 71 E B - 184.1 - - - - - - - - 181.4 -2.0 34.8 - 72 PHE 72 E B - - -60.4 - - - - - - - 179.3 -.7 35.6 - +* +* 73 LEU 73 E B - - -70.5 - - - - - - - 174.6 -2.1 33.7 - 74 LYS 74 E B - - -98.2 179.8 - - - - - - 178.4 -2.4 33.9 - ** ** 75 VAL 75 E B - 176.9 - - - - - - - - 176.8 -3.7 35.0 - ** ** 76 ASP 76 E B - 182.4 - - - - - - - - 185.3 -.6 33.4 - +* +* 77 THR 77 e A 53.5 - - - - - - - - - 177.7 -2.7 32.0 - 78 ASP 78 T A - 187.8 - - - - - - - - 177.2 - 34.5 - 79 GLU 79 T A - - -62.3 - - - - - - - 182.6 - 35.9 - 80 LEU 80 h b - - -65.0 180.1 - - - - - - 181.3 -2.7 33.7 - 81 LYS 81 H A - - -59.4 180.5 - -68.9 -42.6 - - - 181.2 -1.0 33.7 - * * 82 SER 82 H A - - -55.4 - - -66.1 -31.0 - - - 178.5 - 33.8 - 83 VAL 83 H A - 179.3 - - - -74.1 -40.6 - - - 178.5 - 33.7 - 84 ALA 84 H A - - - - - -59.4 -45.1 - - - 179.0 -1.9 34.1 - 85 SER 85 H A - - -57.3 - - -71.5 -30.8 - - - 182.7 -2.4 34.1 - 86 ASP 86 H A - 182.8 - - - -67.0 -37.3 - - - 178.0 -1.5 34.5 - 87 TRP 87 h A - - -62.3 - - - - - - - 181.1 -2.0 33.6 - 88 ALA 88 T l - - - - - - - - - - 178.1 - 30.8 - 89 ILE 89 t B - - -57.0 - - - - - - - 184.2 -2.0 33.9 - 90 GLN 90 A - - -58.1 - - - - - - - 179.1 -.9 33.1 - * * 91 ALA 91 S B - - - - - - - - - - 179.3 - 33.4 - 92 MET 92 S B - - -63.2 176.7 - - - - - - 1.0 - 34.5 - 93 PRO 93 e cis - - - - - -90.0 - - - - - 174.4 - 39.6 - ** +* ** 94 THR 94 E B - - -57.6 - - - - - - - 181.4 -1.6 34.6 - 95 PHE 95 E B - - -48.1 - - - - - - - 179.6 -3.1 37.4 - * * * * 96 MET 96 E B - 181.4 - 174.0 - - - - - - 183.5 -3.5 32.9 - +* +* 97 PHE 97 E B - - -66.8 - - - - - - - 179.3 -3.3 36.6 - +* +* 98 LEU 98 E B - - -54.0 - - - - - - - 174.6 -2.1 35.3 - Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 99 LYS 99 E B - 178.5 - 171.6 - - - - - - 177.3 -3.5 33.0 - +* +* 100 GLU 100 T l - - -54.9 169.5 - - - - - - 180.5 - 33.8 - 101 GLY 101 T - - - - - - - - - - - 178.0 - - - 102 LYS 102 E B - - -63.6 179.3 - - - - - - 182.3 -1.9 34.5 - 103 ILE 103 E B - - -58.1 176.0 - - - - - - 177.6 - 34.4 - 104 LEU 104 E a - - -67.9 185.3 - - - - - - 186.1 -2.1 34.0 - * * 105 ASP 105 E B 55.3 - - - - - - - - - 178.9 -2.1 33.4 - 106 LYS 106 E B 57.9 - - 182.0 - - - - - - 181.9 - 32.7 - 107 VAL 107 E B - 181.7 - - - - - - - - 178.3 -3.1 35.6 - * * 108 VAL 108 E B 60.9 - - - - - - - - - 180.9 - 32.9 - 109 GLY 109 e - - - - - - - - - - - 183.0 -3.3 - - +* +* 110 ALA 110 B - - - - - - - - - - 172.3 - 34.2 - * * 111 LYS 111 h B - - -68.0 180.4 - - - - - - 188.2 -.8 34.7 - * +* +* 112 LYS 112 H A - 181.0 - 180.6 - -56.2 -50.8 - - - 183.7 - 33.2 - * * 113 ASP 113 H A - 181.5 - - - -72.6 -35.8 - - - 182.5 - 33.5 - 114 GLU 114 H A - 200.8 - - - -72.3 -41.8 - - - 178.0 - 35.1 - * * 115 LEU 115 H A - 187.2 - - - -61.8 -42.3 - - - 178.4 -3.2 36.2 - +* +* 116 GLN 116 H A - 185.4 - - - -56.5 -34.9 - - - 177.4 -2.0 35.4 - 117 SER 117 H A - - -57.5 - - -70.1 -32.5 - - - 176.2 -1.2 33.5 - * * 118 THR 118 H A - - -53.9 - - -73.8 -29.7 - - - 174.5 -1.3 34.0 - 119 ILE 119 H A - - -58.2 177.7 - -66.4 -46.3 - - - 177.3 -2.0 33.8 - 120 ALA 120 H A - - - - - -62.9 -29.7 - - - 176.2 -2.6 33.2 - 121 LYS 121 H A - 183.2 - 179.4 - -56.9 -40.5 - - - 177.4 -1.3 37.4 - 122 HIS 122 H A - - -69.6 - - -86.6 -48.2 - - - 181.7 -1.1 35.0 - +* * +* 123 LEU 123 h b - - -78.8 - - - - - - - 177.6 -3.6 34.7 - ** ** 124 ALA 124 - - - - - - - - - - - - -1.3 34.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * ** ** ** +* ** +* *7.5* * ** +* *7.5* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.3 183.8 -62.4 179.3 -69.4 -66.5 -39.8 71.1 - 2.8 179.8 -2.1 34.2 +* *7.5* *7.5* Standard deviations: 4.3 7.1 8.4 8.0 15.6 7.8 8.9 .0 - .0 2.9 .9 1.5 Numbers of values: 13 45 44 30 4 46 46 2 0 2 122 77 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_15 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_15 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 1.505 1.538 1.450 - 116.93 120.34 109.44 108.81 111.09 122.73 2 GLY 2 1.306 1.235 1.500 - 1.429 120.03 115.98 120.65 - 112.12 - 123.36 +* * +* 3 HIS 3 1.306 1.228 1.533 1.546 1.442 122.25 116.95 120.87 111.76 110.88 109.09 122.17 +* +* 4 HIS 4 1.324 1.246 1.510 1.543 1.457 120.03 115.17 120.65 110.95 110.04 113.73 124.18 +* +* 5 HIS 5 1.314 1.235 1.525 1.546 1.452 124.38 114.39 121.98 112.35 109.97 113.52 123.47 * * * +* +* 6 HIS 6 1.297 1.224 1.510 1.545 1.437 123.62 117.25 119.84 110.53 107.77 109.13 122.90 ** * * * ** 7 HIS 7 1.313 1.234 1.532 1.560 1.443 120.75 114.78 121.94 113.54 111.75 113.54 123.24 * +* +* +* +* 8 HIS 8 1.306 1.227 1.504 1.556 1.452 123.29 116.56 119.42 111.46 108.94 111.29 124.02 +* * * +* 9 LEU 9 1.337 1.229 1.532 1.546 1.485 123.19 115.28 121.81 110.56 109.64 111.85 122.88 * * 10 GLU 10 1.313 1.238 1.548 1.553 1.439 122.61 118.60 119.02 112.86 105.72 107.06 122.37 * * * * * * * +* ** ** 11 MET 11 1.314 1.237 1.525 1.535 1.470 122.19 116.51 120.90 109.95 111.09 111.05 122.59 * * Residue-by-residue listing for refined_15 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 1.314 1.236 1.514 1.518 1.439 121.07 114.70 121.23 111.21 111.06 111.65 123.97 * * * 13 SER 13 1.300 1.253 1.511 1.540 1.437 124.75 117.98 119.19 110.80 106.52 110.77 122.83 ** * * +* +* ** 14 GLU 14 1.305 1.233 1.511 1.523 1.428 120.47 114.37 121.47 111.19 111.58 111.62 124.10 +* +* +* 15 GLU 15 1.296 1.245 1.513 1.564 1.426 124.33 117.99 119.35 111.97 106.11 113.31 122.65 ** +* +* * +* +* ** 16 GLY 16 1.306 1.234 1.503 - 1.452 119.77 115.46 121.01 - 112.31 - 123.53 +* +* 17 GLN 17 1.301 1.238 1.483 1.530 1.426 122.71 115.24 120.89 111.16 109.40 111.99 123.87 +* +* +* +* 18 VAL 18 1.276 1.236 1.514 1.553 1.434 121.84 116.96 120.21 109.67 109.23 110.54 122.82 +*** * +*** 19 ILE 19 1.316 1.224 1.518 1.569 1.429 120.63 116.41 121.07 110.75 109.28 112.60 122.51 * +* +* 20 ALA 20 1.295 1.229 1.503 1.524 1.434 121.32 116.46 120.71 111.15 109.34 110.77 122.81 ** * * ** 21 CYS 21 1.303 1.231 1.513 1.508 1.418 121.11 115.82 121.19 109.88 109.70 109.91 122.97 +* * ** ** 22 HIS 22 1.299 1.225 1.510 1.539 1.445 121.65 115.56 120.97 109.96 109.39 111.37 123.46 ** ** 23 THR 23 1.323 1.249 1.518 1.553 1.449 122.56 116.47 120.29 108.02 109.70 111.23 123.24 24 VAL 24 1.328 1.224 1.519 1.547 1.452 121.70 115.38 121.18 109.78 108.98 111.92 123.40 25 GLU 25 1.328 1.232 1.530 1.530 1.412 123.62 116.30 120.36 110.36 110.34 108.95 123.27 ** * ** 26 THR 26 1.335 1.225 1.535 1.537 1.453 122.03 115.99 120.54 110.14 110.43 110.33 123.45 27 TRP 27 1.331 1.238 1.528 1.543 1.468 123.08 115.39 121.10 110.95 111.09 108.08 123.46 * * 28 ASN 28 1.304 1.234 1.521 1.526 1.446 122.71 115.85 120.91 111.06 110.58 108.69 123.22 +* * +* 29 GLU 29 1.321 1.235 1.530 1.538 1.458 122.15 116.72 120.09 111.21 111.26 111.14 123.17 30 GLN 30 1.327 1.227 1.507 1.494 1.424 122.62 117.18 120.16 110.59 112.95 110.24 122.66 +* +* +* 31 LEU 31 1.321 1.219 1.497 1.486 1.411 121.40 116.42 120.16 110.42 111.42 110.17 123.42 * ** ** ** 32 GLN 32 1.315 1.218 1.516 1.523 1.441 121.32 116.16 120.52 110.53 109.55 110.90 123.29 33 LYS 33 1.325 1.228 1.525 1.561 1.445 121.91 117.15 119.87 112.41 109.56 110.27 122.94 +* * +* 34 ALA 34 1.335 1.230 1.522 1.516 1.457 121.45 115.72 120.77 110.42 111.02 110.54 123.51 35 ASN 35 1.321 1.229 1.503 1.520 1.465 123.31 114.71 121.49 106.90 109.98 109.01 123.79 * +* +* 36 GLU 36 1.308 1.226 1.535 1.533 1.457 122.65 117.14 120.76 111.15 111.24 110.26 122.08 +* +* 37 SER 37 1.317 1.231 1.533 1.512 1.445 120.99 116.11 120.35 111.12 111.41 109.94 123.54 38 LYS 38 1.354 1.235 1.548 1.505 1.431 124.57 114.59 122.32 113.35 110.24 106.89 123.02 +* * * * +* +* ** ** 39 THR 39 1.318 1.239 1.538 1.525 1.443 123.29 115.95 120.93 109.03 109.83 110.46 123.07 40 LEU 40 1.301 1.243 1.549 1.565 1.457 123.19 115.75 121.07 112.88 109.78 109.36 123.18 +* * +* * +* 41 VAL 41 1.320 1.238 1.541 1.567 1.446 122.76 116.70 120.65 110.88 110.30 110.39 122.63 42 VAL 42 1.309 1.235 1.531 1.558 1.443 121.74 116.31 120.95 110.99 110.06 111.76 122.71 * * 43 VAL 43 1.305 1.228 1.524 1.550 1.442 121.58 115.46 120.94 109.37 110.94 111.76 123.60 +* +* Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 44 ASP 44 1.295 1.226 1.520 1.537 1.453 123.87 117.14 120.21 109.69 109.43 108.54 122.60 ** * * ** 45 PHE 45 1.308 1.244 1.514 1.520 1.429 121.46 116.17 120.42 110.41 108.38 110.18 123.38 +* +* * +* 46 THR 46 1.306 1.233 1.537 1.567 1.428 121.49 115.33 121.39 109.88 111.53 109.37 123.26 +* +* * +* 47 ALA 47 1.309 1.244 1.510 1.513 1.430 123.46 116.41 120.52 110.18 108.39 111.29 123.07 * * * * 48 SER 48 1.304 1.224 1.544 1.531 1.450 122.34 116.66 120.98 111.12 111.82 109.78 122.34 +* +* 49 TRP 49 1.319 1.227 1.533 1.543 1.462 121.81 116.81 120.79 111.14 112.15 110.37 122.39 50 CYS 50 1.308 1.236 1.525 1.527 1.449 121.19 115.75 120.53 110.90 111.63 110.68 123.71 +* +* 51 GLY 51 1.337 1.228 1.528 - 1.459 122.51 118.87 119.50 - 113.08 - 121.64 * * * 52 PRO 52 1.368 1.226 1.535 1.541 1.476 122.87 116.48 120.83 110.63 112.59 104.18 122.69 +* * +* 53 CYS 53 1.322 1.228 1.534 1.527 1.461 121.88 116.28 120.95 109.20 110.71 111.03 122.75 54 ARG 54 1.321 1.235 1.520 1.520 1.455 122.27 115.46 121.33 110.43 109.61 109.53 123.20 55 PHE 55 1.311 1.232 1.528 1.537 1.440 122.09 116.76 120.90 110.17 111.00 110.46 122.31 * * 56 ILE 56 1.313 1.230 1.538 1.567 1.449 120.15 115.98 121.06 110.38 110.57 111.43 122.94 * * * 57 ALA 57 1.325 1.230 1.549 1.524 1.460 122.54 120.10 119.04 111.75 113.79 111.65 120.84 * +* * * +* 58 PRO 58 1.377 1.231 1.523 1.536 1.468 121.81 116.19 120.81 110.12 111.51 104.11 122.98 ** * ** 59 PHE 59 1.324 1.217 1.523 1.540 1.451 121.71 115.86 121.01 111.08 109.67 110.63 123.10 60 PHE 60 1.315 1.231 1.539 1.539 1.455 122.48 116.23 121.06 112.22 109.61 109.32 122.71 * * 61 ALA 61 1.324 1.234 1.533 1.523 1.459 121.80 115.72 121.16 110.72 109.81 110.70 123.11 62 ASP 62 1.330 1.227 1.494 1.519 1.467 122.73 114.66 121.05 108.88 108.56 110.54 124.28 * * 63 LEU 63 1.323 1.225 1.527 1.524 1.431 123.94 116.24 120.57 109.62 110.74 109.38 123.18 * * * 64 ALA 64 1.324 1.230 1.530 1.519 1.458 122.55 116.30 121.02 110.61 111.59 110.25 122.66 65 LYS 65 1.316 1.241 1.527 1.534 1.456 121.66 115.10 121.47 110.51 110.39 109.95 123.44 66 LYS 66 1.307 1.232 1.524 1.530 1.440 123.17 116.43 120.52 111.43 110.65 108.51 123.05 +* * +* 67 LEU 67 1.315 1.229 1.522 1.512 1.431 122.28 116.30 121.15 111.94 110.91 110.16 122.53 * * 68 PRO 68 1.333 1.234 1.539 1.534 1.470 123.45 117.52 120.39 109.89 114.87 102.91 122.09 * * 69 ASN 69 1.325 1.226 1.527 1.534 1.464 120.56 116.39 121.45 110.79 111.07 110.56 122.16 70 VAL 70 1.303 1.240 1.526 1.555 1.446 120.93 116.45 120.53 110.84 109.29 111.82 122.98 +* +* 71 LEU 71 1.316 1.235 1.528 1.540 1.449 121.79 116.45 120.56 110.74 109.77 109.56 122.98 72 PHE 72 1.320 1.243 1.516 1.530 1.457 121.90 115.87 120.95 107.38 109.89 111.49 123.18 * * 73 LEU 73 1.295 1.225 1.507 1.546 1.444 122.96 115.38 120.83 108.13 111.45 113.30 123.79 ** * +* ** 74 LYS 74 1.308 1.233 1.492 1.500 1.415 123.78 116.01 120.91 109.92 110.44 111.38 123.06 +* +* * ** * ** 75 VAL 75 1.280 1.229 1.497 1.554 1.421 121.81 116.35 120.54 109.47 108.66 111.26 123.11 +*** * +* +*** Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 76 ASP 76 1.303 1.240 1.499 1.518 1.433 120.44 116.23 120.51 111.05 107.66 111.85 123.24 +* * * * +* 77 THR 77 1.295 1.219 1.531 1.538 1.437 122.33 118.04 119.79 111.34 114.23 111.12 122.17 ** * * * ** 78 ASP 78 1.326 1.227 1.491 1.509 1.458 119.92 114.46 121.66 108.98 108.25 111.91 123.88 +* * * +* 79 GLU 79 1.305 1.233 1.520 1.516 1.410 122.96 116.00 121.08 109.37 109.87 109.22 122.90 +* +** +** 80 LEU 80 1.316 1.236 1.519 1.513 1.400 122.00 114.95 121.58 111.85 111.42 109.56 123.44 *** *** 81 LYS 81 1.309 1.232 1.517 1.534 1.454 122.87 116.08 121.19 110.94 110.89 110.41 122.69 * * 82 SER 82 1.317 1.229 1.525 1.513 1.441 121.83 116.22 120.50 111.22 110.97 109.78 123.26 83 VAL 83 1.326 1.227 1.528 1.556 1.450 121.80 115.95 120.95 110.61 109.33 111.46 123.06 84 ALA 84 1.326 1.239 1.524 1.520 1.459 122.13 116.06 120.81 110.27 110.60 110.48 123.11 85 SER 85 1.325 1.230 1.539 1.526 1.442 121.61 116.52 120.72 110.88 111.02 109.86 122.71 86 ASP 86 1.328 1.237 1.521 1.525 1.471 122.21 116.07 121.02 109.79 111.40 110.04 122.88 87 TRP 87 1.317 1.238 1.518 1.519 1.441 121.56 114.96 120.83 110.43 110.91 111.02 124.21 88 ALA 88 1.327 1.239 1.521 1.531 1.453 124.56 115.51 121.53 112.23 112.22 112.60 122.83 +* * * +* 89 ILE 89 1.308 1.240 1.507 1.553 1.439 121.46 115.85 121.06 110.56 108.04 111.82 123.03 +* * +* 90 GLN 90 1.302 1.231 1.511 1.525 1.426 121.15 116.74 120.44 111.48 111.48 110.65 122.82 +* +* +* 91 ALA 91 1.310 1.228 1.507 1.518 1.446 121.37 116.00 120.96 110.66 110.42 111.32 123.03 * * 92 MET 92 1.293 1.237 1.524 1.530 1.441 121.84 118.33 120.13 110.67 109.55 110.07 121.54 +** * +** 93 PRO 93 1.338 1.240 1.535 1.528 1.461 123.82 115.79 121.47 109.74 113.26 102.47 122.72 94 THR 94 1.301 1.232 1.515 1.529 1.429 122.02 116.81 120.27 109.59 107.92 111.51 122.93 ** +* * ** 95 PHE 95 1.301 1.222 1.502 1.534 1.413 121.88 117.61 119.83 108.55 106.79 108.82 122.55 +* * ** +* ** 96 MET 96 1.288 1.230 1.504 1.536 1.433 120.64 114.91 121.33 112.45 109.51 110.76 123.76 +** * * * +** 97 PHE 97 1.290 1.247 1.507 1.513 1.410 124.33 116.34 121.17 109.17 110.14 108.37 122.49 +** +** * * +** 98 LEU 98 1.288 1.220 1.512 1.559 1.422 120.54 116.93 120.49 107.68 107.73 112.86 122.59 +** * +* * * * +** 99 LYS 99 1.288 1.239 1.485 1.525 1.426 121.41 114.75 120.77 111.49 109.14 111.75 124.44 +** +* +* +** 100 GLU 100 1.327 1.226 1.538 1.510 1.453 124.39 115.40 121.51 112.10 110.81 108.75 123.02 * * * * 101 GLY 101 1.324 1.230 1.524 - 1.451 121.70 117.00 120.30 - 113.28 - 122.69 102 LYS 102 1.322 1.225 1.506 1.528 1.457 121.56 116.55 120.20 109.60 109.55 111.03 123.25 103 ILE 103 1.306 1.229 1.519 1.551 1.450 122.11 116.39 120.93 109.85 110.77 110.86 122.67 +* +* 104 LEU 104 1.306 1.239 1.497 1.528 1.427 120.82 115.58 120.79 109.31 110.59 111.90 123.61 +* * +* +* 105 ASP 105 1.310 1.209 1.496 1.523 1.443 121.82 116.17 120.78 109.68 111.96 111.84 123.02 * * * * 106 LYS 106 1.298 1.229 1.518 1.537 1.447 121.68 115.97 120.47 111.54 110.75 111.41 123.56 ** ** 107 VAL 107 1.314 1.230 1.520 1.558 1.461 123.13 117.13 120.14 108.35 109.43 110.94 122.73 * * Residue-by-residue listing for refined_15 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 ----------------------------------------------------------------------------------------------------------------------------------- 108 VAL 108 1.312 1.240 1.549 1.557 1.441 121.61 116.46 121.08 111.63 111.00 110.98 122.45 * * * * 109 GLY 109 1.321 1.238 1.512 - 1.452 120.98 117.47 120.18 - 111.08 - 122.35 110 ALA 110 1.316 1.241 1.524 1.521 1.439 119.98 114.95 121.61 110.09 112.27 110.17 123.44 * * 111 LYS 111 1.303 1.214 1.505 1.520 1.428 124.51 117.86 119.21 111.00 106.92 110.23 122.92 +* +* +* +* +* 112 LYS 112 1.324 1.227 1.541 1.527 1.457 121.71 117.06 120.10 110.73 113.77 110.18 122.81 113 ASP 113 1.319 1.232 1.514 1.536 1.477 121.44 115.53 121.32 110.05 111.46 111.30 123.14 * * 114 GLU 114 1.305 1.230 1.540 1.536 1.449 122.02 116.21 120.93 111.93 108.59 108.14 122.82 +* * +* 115 LEU 115 1.329 1.223 1.490 1.510 1.457 122.07 114.49 121.44 107.75 108.87 110.41 124.07 +* * +* 116 GLN 116 1.309 1.235 1.538 1.501 1.411 124.08 116.80 120.44 111.61 110.80 107.16 122.72 * * ** * +* ** 117 SER 117 1.326 1.234 1.541 1.514 1.446 121.25 116.71 120.76 111.65 110.64 109.86 122.50 118 THR 118 1.326 1.235 1.533 1.536 1.451 121.61 116.03 121.62 109.96 109.40 111.48 122.35 119 ILE 119 1.316 1.211 1.528 1.551 1.437 120.95 116.01 120.68 110.55 108.12 111.86 123.23 * * * 120 ALA 120 1.327 1.225 1.543 1.522 1.473 123.47 115.64 121.25 110.91 111.48 110.69 123.07 121 LYS 121 1.319 1.225 1.522 1.505 1.469 124.13 114.74 121.83 109.47 109.22 106.47 123.42 * * ** ** 122 HIS 122 1.306 1.239 1.536 1.527 1.442 122.91 115.94 121.24 109.57 110.95 109.84 122.82 +* +* 123 LEU 123 1.319 1.238 1.505 1.512 1.403 123.70 115.32 121.16 110.22 111.78 109.69 123.46 +** * +** 124 ALA 124 1.291 - 1.504 1.518 1.421 122.30 - - 111.40 108.23 110.51 - +** * +* * +** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** * +* ** *** +* +* * +* +* ** * +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 1.276 1.354 1.313 .013 +*** +* * C-N (Pro) 1.341 .016 4 1.333 1.377 1.354 .019 ** C-O C-O 1.231 .020 123 1.209 1.253 1.232 .007 * * CA-C CH1E-C (except Gly) 1.525 .021 119 1.483 1.549 1.521 .015 +* * CH2G*-C (Gly) 1.516 .018 5 1.500 1.528 1.513 .011 CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.513 1.531 1.521 .004 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.525 1.569 1.551 .012 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.565 1.529 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.400 1.485 1.443 .016 *** * NH1-CH2G* (Gly) 1.451 .016 5 1.429 1.459 1.448 .010 * N-CH1E (Pro) 1.466 .015 4 1.461 1.476 1.469 .005 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_15 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 2.0 114 114.37 120.10 116.14 .94 +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.46 118.87 116.95 1.19 * CH1E-C-N (Pro) 116.9 1.5 4 115.79 117.52 116.50 .64 O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.84 124.44 123.04 .56 * O-C-N (Pro) 122.0 1.4 4 122.09 122.98 122.62 .32 C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.92 124.75 122.19 1.11 +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.77 122.51 121.00 1.02 * C-N-CH1E (Pro) 122.6 5.0 4 121.81 123.82 122.99 .76 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.02 122.32 120.79 .60 * CH2G*-C-O (Gly) 120.8 2.1 5 119.50 121.01 120.33 .51 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.09 112.23 110.89 .61 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 108.02 111.63 110.07 .88 * CH2E-CH1E-C (the rest) 110.1 1.9 84 106.90 113.54 110.59 1.27 +* +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.72 114.23 110.13 1.49 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 111.08 113.28 112.37 .78 N-CH1E-C (Pro) 111.8 2.5 4 111.51 114.87 113.06 1.22 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.17 112.60 110.97 .67 * NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 109.37 112.60 111.22 .69 * N-CH1E-CH2E (Pro) 103.0 1.1 4 102.47 104.18 103.42 .74 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 106.47 113.73 110.31 1.48 ** +* ------------------------------------------------------------------------------------------------------------- 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_15 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 2.9 6.0 3.0 -1.0 BETTER c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.5 3.1 1.6 -1.0 BETTER e. H-bond energy st dev 77 .9 .8 .2 .3 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 13 4.3 18.1 6.5 -2.1 BETTER b. Chi-1 trans st dev 45 7.1 19.0 5.3 -2.2 BETTER c. Chi-1 gauche plus st dev 44 8.4 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 102 8.2 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 30 8.0 20.4 5.0 -2.5 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 9.5 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 3 Residue-by-residue listing for refined_15 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.15 Chi1-chi2 distribution -.08 Chi1 only .16 Chi3 & chi4 .42 Omega .12 ------ .03 ===== Main-chain covalent forces:- Main-chain bond lengths .06 Main-chain bond angles .47 ------ .30 ===== OVERALL AVERAGE .12 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.