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 - - - -67.1 - - - - - - - 178.0 - 33.2 - 2 GLY 2 - - - - - - - - - - - 178.6 - - - 3 HIS 3 B - - -64.0 - - - - - - - 178.6 - 34.1 - 4 HIS 4 b 63.6 - - - - - - - - - 174.6 -.7 30.9 - +* +* 5 HIS 5 A - - -61.0 - - - - - - - 178.9 - 33.8 - 6 HIS 6 S B 66.9 - - - - - - - - - 176.8 - 34.6 - 7 HIS 7 B - - -62.7 - - - - - - - 181.9 - 33.9 - 8 HIS 8 B 58.1 - - - - - - - - - 177.8 - 34.1 - 9 LEU 9 B - - -61.8 178.2 - - - - - - 185.4 - 33.9 - 10 GLU 10 B 55.3 - - - - - - - - - 171.6 - 29.1 - * * * 11 MET 11 b 61.9 - - - - - - - - - 179.9 -1.0 32.3 - * * 12 ALA 12 B - - - - - - - - - - 180.5 - 34.7 - 13 SER 13 S p - - -56.5 - - - - - - - 175.6 - 34.7 - 14 GLU 14 S a - 184.1 - - - - - - - - 171.5 - 33.5 - * * 15 GLU 15 p - - -78.9 - - - - - - - 183.9 - 31.2 - 16 GLY 16 - - - - - - - - - - - 178.1 -.6 - - +* +* 17 GLN 17 S B 50.6 - - - - - - - - - 182.2 - 31.8 - 18 VAL 18 B - 187.1 - - - - - - - - 184.2 - 34.8 - 19 ILE 19 E B - - -60.6 - - - - - - - 178.4 -2.4 33.1 - 20 ALA 20 E B - - - - - - - - - - 182.8 -.7 33.9 - +* +* 21 CYS 21 E B - - -51.8 - - - - - - - 177.1 -2.6 35.6 - 22 HIS 22 A - - -64.8 - - - - - - - 183.6 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 23 THR 23 h B 58.5 - - - - - - - - - 175.4 - 35.8 - 24 VAL 24 H A 65.2 - - - - -74.2 -21.4 - - - 175.1 - 31.3 - +* +* 25 GLU 25 H A - - -60.5 - - -56.4 -51.8 - - - 179.4 - 35.6 - * * 26 THR 26 H A - - -55.9 - - -66.5 -42.0 - - - 178.0 - 34.5 - 27 TRP 27 H A - 176.6 - - - -55.1 -50.1 - - - 180.1 -1.7 34.9 - 28 ASN 28 H A - 185.4 - - - -59.9 -47.4 - - - 180.8 -3.3 35.2 - +* +* 29 GLU 29 H A - 178.8 - 177.9 - -57.8 -47.6 - - - 181.4 -2.1 34.1 - 30 GLN 30 H A - - -67.4 - - -67.2 -38.3 - - - 176.8 -2.5 33.4 - 31 LEU 31 H A - - -68.8 181.1 - -65.5 -44.5 - - - 176.4 -2.3 34.2 - 32 GLN 32 H A - 179.8 - 187.3 - -57.8 -46.8 - - - 181.5 -2.8 34.7 - * * 33 LYS 33 H A - 185.8 - 173.4 - -59.9 -40.5 - - - 178.6 -2.7 34.5 - 34 ALA 34 H A - - - - - -70.4 -38.8 - - - 182.0 -2.4 33.8 - 35 ASN 35 H A - 190.1 - - - -69.8 -53.5 - - - 183.6 -2.8 36.5 - * * 36 GLU 36 H A - 186.1 - 174.7 - -59.9 -41.1 - - - 179.6 -3.7 34.6 - ** ** 37 SER 37 h A - 184.4 - - - - - - - - 181.3 -1.8 33.9 - 38 LYS 38 T L - - -62.6 187.2 - - - - - - 178.8 -1.1 31.8 - * * 39 THR 39 t B - - -44.8 - - - - - - - 178.7 -2.5 36.0 - * * 40 LEU 40 e B 66.8 - - - - - - - - - 184.7 - 31.4 - 41 VAL 41 E B 59.8 - - - - - - - - - 178.9 - 32.8 - 42 VAL 42 E B - 181.1 - - - - - - - - 184.2 -2.7 34.5 - 43 VAL 43 E B - 182.6 - - - - - - - - 178.8 -2.3 33.7 - 44 ASP 44 E B - 182.6 - - - - - - - - 177.5 -3.5 37.2 - +* +* 45 PHE 45 E B - - -59.3 - - - - - - - 188.6 -3.4 35.8 - * +* +* 46 THR 46 E B - 189.6 - - - - - - - - 174.6 -2.6 35.7 - 47 ALA 47 t B - - - - - - - - - - 182.6 - 33.6 - 48 SER 48 T A - 184.5 - - - - - - - - 179.5 - 33.0 - 49 TRP 49 T A 52.1 - - - - - - - - - 178.1 - 30.9 - 50 CYS 50 h B - 175.6 - 222.1 - - - 53.5 - 2.0 183.6 -1.7 34.2 - ** +** +** 51 GLY 51 H - - - - - - -61.4 -66.2 - - - 180.9 -.5 - - ** +* ** 52 PRO 52 H - - - - - -58.7 -58.7 -30.5 - - - 179.5 - 38.9 - * * 53 CYS 53 H A - - -57.6 - - -65.5 -32.1 53.5 - 2.0 178.6 - 35.8 - +** +** 54 ARG 54 H A - 182.4 - 178.0 - -78.1 -31.9 - - - 179.7 -1.2 34.2 - * * * 55 PHE 55 H A - 177.9 - - - -72.1 -28.3 - - - 182.1 -1.5 33.6 - 56 ILE 56 H A - 191.2 - - - -86.8 -13.1 - - - 182.0 -1.6 34.5 - +* ** ** 57 ALA 57 H A - - - - - -57.5 -49.9 - - - 180.4 -.5 31.3 - ** ** 58 PRO 58 H - - - - - -61.8 -61.8 -33.4 - - - 181.1 - 38.5 - * * 59 PHE 59 H A - 185.9 - - - -73.3 -42.0 - - - 179.0 - 33.2 - 60 PHE 60 H A - 188.9 - - - -65.8 -33.2 - - - 177.2 -2.4 33.8 - 61 ALA 61 H A - - - - - -69.1 -30.4 - - - 179.0 -2.3 34.3 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 62 ASP 62 H A - 189.2 - - - -74.0 -42.7 - - - 175.2 -1.2 35.3 - * * 63 LEU 63 H A - - -68.0 181.9 - -53.8 -41.3 - - - 178.5 -2.5 35.3 - 64 ALA 64 H A - - - - - -63.1 -33.4 - - - 181.0 -1.8 34.1 - 65 LYS 65 H A - 188.4 - 172.1 - -80.4 -19.6 - - - 179.5 -.9 33.4 - * +* * +* 66 LYS 66 H A - - -56.9 - - -71.1 -39.6 - - - 181.2 -1.1 34.4 - * * 67 LEU 67 h B - - -65.8 171.3 - - - - - - 184.4 -1.4 33.3 - 68 PRO 68 S - - - - - -66.0 - - - - - 183.3 - 38.8 - * * 69 ASN 69 S A - 188.3 - - - - - - - - 185.0 - 33.9 - 70 VAL 70 S B - 178.2 - - - - - - - - 180.5 - 33.3 - 71 LEU 71 E B - - -63.1 177.6 - - - - - - 175.5 -.9 35.6 - +* +* 72 PHE 72 E B - - -62.2 - - - - - - - 184.1 - 34.2 - 73 LEU 73 E B - - -71.9 - - - - - - - 172.0 -2.1 34.3 - * * 74 LYS 74 E B - - -80.3 - - - - - - - 174.8 -2.7 36.5 - 75 VAL 75 E B - 176.7 - - - - - - - - 180.8 -3.3 33.7 - +* +* 76 ASP 76 E B - 186.0 - - - - - - - - 184.9 -1.2 33.0 - * * 77 THR 77 e A - 180.5 - - - - - - - - 177.2 -2.4 32.3 - 78 ASP 78 T A - 188.1 - - - - - - - - 175.1 - 34.5 - 79 GLU 79 T a - - -61.3 - - - - - - - 183.5 - 37.1 - 80 LEU 80 h b - - -67.5 177.2 - - - - - - 177.8 -3.2 34.1 - +* +* 81 LYS 81 H A 52.2 - - 178.4 - -69.1 -30.7 - - - 182.1 -1.3 33.5 - * * 82 SER 82 H A - - -52.9 - - -66.0 -33.9 - - - 177.7 - 34.4 - 83 VAL 83 H A - 179.9 - - - -69.6 -41.2 - - - 178.0 - 33.9 - 84 ALA 84 H A - - - - - -61.4 -42.1 - - - 177.7 -1.2 34.0 - * * 85 SER 85 H A - - -59.2 - - -67.0 -34.9 - - - 181.8 -2.3 33.8 - 86 ASP 86 H A - 179.3 - - - -70.0 -37.3 - - - 179.3 -1.8 34.0 - 87 TRP 87 h A - - -67.2 - - - - - - - 182.9 -2.3 34.1 - 88 ALA 88 T l - - - - - - - - - - 181.9 - 30.6 - 89 ILE 89 t B - - -56.5 176.8 - - - - - - 180.4 -2.7 35.4 - 90 GLN 90 A - 183.3 - - - - - - - - 180.2 -.6 34.5 - +* +* 91 ALA 91 S B - - - - - - - - - - 183.5 - 33.2 - 92 MET 92 S B - - -61.8 167.9 - - - - - - -3.4 -.6 36.5 - +* +* 93 PRO 93 e cis - - - - - -96.2 - - - - - 176.2 - 40.0 - +** +* +** 94 THR 94 E B - - -62.2 - - - - - - - 176.5 -2.0 34.1 - 95 PHE 95 E B - - -52.7 - - - - - - - 183.8 -3.4 37.3 - +* +* 96 MET 96 E B - 181.1 - - - - - - - - 180.1 -3.6 33.0 - ** ** 97 PHE 97 E B - - -66.6 - - - - - - - 175.1 -3.0 37.3 - * * 98 LEU 98 E B 64.5 - - - - - - - - - 176.4 -1.3 33.2 - * * 99 LYS 99 E B - 184.5 - 175.1 - - - - - - 180.8 -3.6 33.6 - ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 100 GLU 100 T L - - -62.2 181.0 - - - - - - 177.1 - 32.1 - 101 GLY 101 T - - - - - - - - - - - 180.5 - - - 102 LYS 102 E B - - -74.0 - - - - - - - 182.9 -1.8 35.4 - 103 ILE 103 E B - - -56.5 - - - - - - - 178.9 -.5 34.5 - ** ** 104 LEU 104 E a - - -63.9 182.5 - - - - - - 184.8 -2.1 34.3 - 105 ASP 105 E B 49.7 - - - - - - - - - 178.0 -2.3 33.1 - 106 LYS 106 E B 62.8 - - 172.7 - - - - - - 177.0 - 34.1 - 107 VAL 107 E B - 182.1 - - - - - - - - 179.8 -3.1 35.4 - * * 108 VAL 108 E B - 182.8 - - - - - - - - 184.4 -.6 34.0 - +* +* 109 GLY 109 e - - - - - - - - - - - 183.3 -3.4 - - +* +* 110 ALA 110 B - - - - - - - - - - 172.7 - 34.0 - * * 111 LYS 111 h B - - -69.2 181.4 - - - - - - 181.5 -1.0 35.4 - * * 112 LYS 112 H A - 183.7 - 175.3 - -66.6 -39.9 - - - 180.6 - 33.4 - 113 ASP 113 H A - 179.3 - - - -66.0 -41.7 - - - 181.0 - 34.9 - 114 GLU 114 H A - 192.3 - - - -67.4 -40.4 - - - 178.1 - 36.4 - 115 LEU 115 H A - 186.1 - - - -60.1 -43.5 - - - 177.8 -2.2 35.6 - 116 GLN 116 H A - - -57.5 - - -56.3 -39.3 - - - 180.7 -2.1 33.6 - 117 SER 117 H A - - -55.4 - - -68.8 -36.0 - - - 177.4 -1.6 33.8 - 118 THR 118 H A - - -58.0 - - -70.8 -37.3 - - - 178.6 -2.0 34.2 - 119 ILE 119 H A - - -60.4 176.9 - -63.6 -43.2 - - - 179.6 -2.9 32.9 - * * 120 ALA 120 H A - - - - - -66.5 -30.8 - - - 177.3 -2.4 32.4 - 121 LYS 121 H A - 189.2 - 186.6 - -64.7 -44.3 - - - 181.9 -1.3 36.5 - 122 HIS 122 H A - - -66.4 - - -90.5 -2.0 - - - 182.7 -2.0 35.3 - ** *** *** 123 LEU 123 h B - 193.9 - - - - - - - - 179.5 -.7 34.5 - +* +* 124 ALA 124 - - - - - - - - - - - - - 34.7 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * ** +** ** *** +** * ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 59.2 184.1 -62.3 179.8 -70.7 -66.5 -38.0 53.5 - 2.0 179.7 -2.0 34.3 +** +** Standard deviations: 6.0 4.6 6.8 10.1 17.2 7.7 10.6 .0 - .0 3.1 .9 1.7 Numbers of values: 15 42 45 25 4 46 46 2 0 2 122 76 119 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 - 1.238 1.510 1.534 1.466 - 116.02 120.80 110.06 111.31 111.86 123.17 2 GLY 2 1.320 1.230 1.510 - 1.444 121.24 115.73 121.22 - 110.93 - 123.04 3 HIS 3 1.312 1.227 1.498 1.536 1.447 122.05 116.50 120.72 109.25 109.34 112.22 122.76 * * * * 4 HIS 4 1.301 1.221 1.518 1.563 1.433 120.85 115.52 121.91 112.39 111.07 113.18 122.38 ** +* * * +* ** 5 HIS 5 1.295 1.235 1.510 1.540 1.450 121.16 114.61 121.51 110.40 107.92 111.89 123.84 ** * ** 6 HIS 6 1.324 1.242 1.519 1.567 1.451 122.88 116.13 120.75 109.48 109.86 111.37 123.11 +* +* 7 HIS 7 1.295 1.230 1.517 1.536 1.439 121.72 116.58 120.30 110.98 108.66 111.00 123.12 ** ** 8 HIS 8 1.298 1.220 1.509 1.554 1.458 122.26 117.73 119.28 110.71 108.83 111.06 122.99 ** * ** 9 LEU 9 1.320 1.240 1.519 1.528 1.456 120.92 116.60 120.47 110.66 108.82 111.04 122.91 10 GLU 10 1.305 1.241 1.521 1.561 1.437 121.08 114.19 121.91 112.66 114.13 113.71 123.82 +* +* * * * * +* +* 11 MET 11 1.308 1.239 1.505 1.560 1.441 124.49 116.56 120.20 110.05 107.62 114.88 123.22 * +* +* * +** +** 12 ALA 12 1.297 1.237 1.501 1.525 1.441 122.18 116.76 119.42 110.46 108.49 110.29 123.79 ** * ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 SER 13 1.332 1.244 1.546 1.542 1.461 122.47 117.20 120.66 111.01 109.81 109.23 122.10 * * 14 GLU 14 1.303 1.237 1.508 1.537 1.434 121.02 115.50 120.16 111.77 106.98 111.39 124.30 +* * +* +* 15 GLU 15 1.341 1.234 1.522 1.535 1.456 123.76 116.49 120.94 114.35 114.13 109.09 122.48 * ** * ** 16 GLY 16 1.296 1.230 1.495 - 1.438 119.91 114.75 121.50 - 110.71 - 123.75 ** * ** 17 GLN 17 1.297 1.234 1.486 1.552 1.418 123.20 116.09 120.46 113.04 109.36 112.13 123.45 ** +* * ** +* ** 18 VAL 18 1.279 1.231 1.520 1.546 1.426 121.26 117.42 120.03 110.36 108.05 110.60 122.54 +*** +* * +*** 19 ILE 19 1.319 1.230 1.523 1.574 1.450 120.64 116.61 120.56 109.46 110.78 113.20 122.82 * * * 20 ALA 20 1.311 1.233 1.510 1.524 1.446 121.79 116.27 120.82 110.59 109.31 110.96 122.90 * * 21 CYS 21 1.301 1.232 1.511 1.505 1.418 121.53 115.67 121.11 109.57 110.18 109.25 123.20 +* * ** ** 22 HIS 22 1.299 1.235 1.507 1.535 1.447 122.47 115.90 121.28 108.99 109.23 111.09 122.82 ** ** 23 THR 23 1.311 1.250 1.500 1.550 1.434 121.25 116.30 120.44 107.97 109.41 111.25 123.26 * * * * 24 VAL 24 1.309 1.216 1.541 1.575 1.426 120.82 116.05 120.99 112.75 108.28 113.43 122.96 * * +* +* * * +* 25 GLU 25 1.353 1.238 1.545 1.540 1.420 123.50 116.43 120.60 108.68 110.50 110.24 122.96 +* +* +* 26 THR 26 1.342 1.235 1.537 1.554 1.458 121.54 115.07 121.23 110.07 109.64 110.72 123.69 27 TRP 27 1.325 1.234 1.545 1.536 1.458 123.68 115.94 120.87 111.51 111.21 108.03 123.17 * * * 28 ASN 28 1.326 1.237 1.527 1.546 1.469 123.37 115.75 120.72 110.31 110.09 109.26 123.51 29 GLU 29 1.326 1.241 1.530 1.528 1.458 122.64 116.39 120.47 110.32 111.73 110.08 123.13 30 GLN 30 1.321 1.230 1.521 1.492 1.417 122.48 117.17 120.34 111.51 112.62 109.49 122.49 +* ** ** 31 LEU 31 1.325 1.235 1.502 1.486 1.416 121.76 116.41 120.06 110.01 111.19 110.35 123.53 * ** ** ** 32 GLN 32 1.331 1.208 1.506 1.524 1.446 121.26 115.23 120.84 108.37 109.12 112.09 123.90 * * 33 LYS 33 1.312 1.238 1.527 1.524 1.443 123.49 116.58 120.69 111.83 110.77 108.46 122.70 * * * 34 ALA 34 1.326 1.221 1.530 1.521 1.442 120.94 116.30 120.83 110.79 110.54 110.43 122.85 35 ASN 35 1.315 1.237 1.516 1.533 1.466 122.60 113.84 121.88 108.47 110.07 109.05 124.27 * * * 36 GLU 36 1.296 1.225 1.530 1.530 1.453 125.00 116.96 120.64 111.55 111.76 108.22 122.38 ** +* * ** 37 SER 37 1.319 1.236 1.547 1.542 1.451 120.91 116.03 120.94 111.51 110.58 109.73 123.03 * * 38 LYS 38 1.349 1.235 1.518 1.511 1.477 124.01 115.12 122.00 111.22 112.09 112.06 122.86 * * * * 39 THR 39 1.287 1.234 1.512 1.515 1.413 122.30 116.28 120.83 108.13 107.34 110.95 122.85 *** ** * *** 40 LEU 40 1.272 1.233 1.516 1.521 1.367 122.73 115.90 120.68 113.45 110.06 111.94 123.35 **** *4.8* +* *4.8* 41 VAL 41 1.278 1.240 1.526 1.571 1.440 121.74 115.75 120.88 111.62 110.82 111.50 123.34 +*** * * +*** 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 VAL 42 1.314 1.239 1.511 1.538 1.440 122.50 116.72 120.68 109.62 108.37 111.65 122.59 * * * 43 VAL 43 1.300 1.225 1.520 1.547 1.438 120.51 115.24 120.85 109.88 111.35 111.55 123.90 ** * ** 44 ASP 44 1.300 1.240 1.523 1.538 1.447 124.26 117.23 120.21 109.17 107.76 107.88 122.49 ** * * +* ** 45 PHE 45 1.306 1.246 1.513 1.518 1.428 121.25 116.60 120.40 109.82 107.59 109.45 122.97 +* +* * +* 46 THR 46 1.305 1.226 1.538 1.548 1.430 120.71 116.33 120.65 110.25 110.55 108.60 122.95 +* * +* +* 47 ALA 47 1.312 1.242 1.512 1.514 1.444 122.93 117.26 119.77 110.73 108.35 111.49 122.95 * * * 48 SER 48 1.315 1.225 1.536 1.541 1.454 121.62 117.17 120.70 111.15 111.25 111.08 122.08 * * 49 TRP 49 1.329 1.232 1.534 1.552 1.459 120.86 116.24 120.82 112.15 112.62 112.40 122.92 * * * * 50 CYS 50 1.314 1.237 1.536 1.529 1.444 122.49 116.03 120.55 111.12 109.93 109.78 123.43 * * 51 GLY 51 1.329 1.235 1.534 - 1.470 122.70 118.82 119.80 - 114.55 - 121.37 * * * * * * 52 PRO 52 1.365 1.235 1.524 1.535 1.483 122.88 114.81 121.69 110.05 111.38 103.55 123.49 +* * * * +* 53 CYS 53 1.308 1.230 1.538 1.512 1.447 123.70 116.12 121.51 109.81 110.89 108.32 122.37 * * * * 54 ARG 54 1.307 1.229 1.532 1.525 1.446 121.73 115.99 121.03 111.13 109.95 109.76 122.94 +* +* 55 PHE 55 1.319 1.231 1.534 1.540 1.459 122.19 116.85 120.95 110.64 111.60 110.64 122.18 56 ILE 56 1.312 1.238 1.550 1.573 1.458 120.69 115.37 121.53 110.33 109.42 110.71 123.05 * * * * 57 ALA 57 1.336 1.236 1.554 1.529 1.461 122.98 120.41 118.76 111.58 114.09 111.54 120.83 * ** * * * ** 58 PRO 58 1.382 1.233 1.524 1.536 1.471 121.74 116.47 120.68 110.05 111.93 104.15 122.82 +** * +** 59 PHE 59 1.321 1.222 1.526 1.538 1.446 120.83 116.31 120.69 111.33 109.90 111.25 122.97 60 PHE 60 1.323 1.230 1.541 1.545 1.463 121.90 115.95 121.24 111.73 109.77 109.91 122.79 61 ALA 61 1.326 1.235 1.524 1.517 1.459 122.10 115.86 121.24 110.00 110.41 110.46 122.89 62 ASP 62 1.317 1.226 1.499 1.507 1.453 121.95 114.71 121.14 109.34 108.34 110.19 124.13 * * * * 63 LEU 63 1.328 1.234 1.523 1.525 1.440 123.96 115.82 120.78 109.69 110.99 109.44 123.39 * * 64 ALA 64 1.321 1.221 1.517 1.521 1.454 122.33 115.99 121.21 110.36 111.18 110.30 122.81 65 LYS 65 1.303 1.229 1.534 1.533 1.439 121.79 116.50 120.85 112.39 110.83 109.45 122.65 +* * +* 66 LYS 66 1.332 1.235 1.516 1.544 1.461 121.52 116.16 120.79 108.82 110.07 111.89 123.05 67 LEU 67 1.318 1.224 1.523 1.513 1.425 121.69 116.48 120.85 112.17 111.14 109.67 122.67 +* * +* 68 PRO 68 1.344 1.232 1.536 1.534 1.476 123.49 117.49 120.61 109.91 114.58 103.20 121.90 * * 69 ASN 69 1.318 1.230 1.520 1.534 1.459 119.73 116.11 121.12 109.85 110.57 111.31 122.68 * * 70 VAL 70 1.308 1.232 1.519 1.554 1.443 121.54 115.23 121.38 110.79 111.21 111.38 123.39 +* +* 71 LEU 71 1.311 1.240 1.517 1.526 1.415 122.82 115.83 120.86 109.85 110.27 109.23 123.29 * ** ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 72 PHE 72 1.304 1.242 1.500 1.522 1.437 122.44 115.87 120.94 109.59 107.84 112.12 123.18 +* * * * +* 73 LEU 73 1.283 1.223 1.506 1.544 1.441 122.12 115.08 121.09 108.08 112.38 112.23 123.83 *** * * *** 74 LYS 74 1.306 1.235 1.497 1.531 1.414 124.18 117.04 120.35 107.88 107.33 110.69 122.58 +* * ** * * * ** 75 VAL 75 1.276 1.237 1.480 1.550 1.421 119.96 115.87 120.75 110.47 107.05 112.82 123.37 +*** ** +* * +*** 76 ASP 76 1.295 1.228 1.498 1.513 1.416 120.14 115.42 120.91 111.74 108.38 111.63 123.64 ** * ** * ** 77 THR 77 1.307 1.234 1.532 1.566 1.447 123.09 117.10 120.38 111.42 112.49 111.61 122.52 +* * +* 78 ASP 78 1.318 1.241 1.516 1.526 1.452 120.77 114.57 121.51 110.57 107.30 110.76 123.90 * * 79 GLU 79 1.326 1.240 1.532 1.529 1.428 123.93 115.24 121.38 107.70 109.10 109.24 123.36 +* * * +* 80 LEU 80 1.326 1.240 1.514 1.511 1.411 123.61 114.86 121.79 110.90 111.93 109.66 123.30 ** * ** 81 LYS 81 1.295 1.229 1.529 1.531 1.446 122.62 115.59 121.19 111.62 110.98 110.07 123.17 ** ** 82 SER 82 1.318 1.241 1.533 1.513 1.444 122.80 116.28 120.69 111.43 111.36 108.64 123.01 * * 83 VAL 83 1.332 1.230 1.528 1.558 1.454 121.74 115.86 121.10 110.32 109.13 111.56 122.98 84 ALA 84 1.327 1.214 1.523 1.513 1.454 121.95 116.77 120.62 110.49 110.33 110.47 122.60 85 SER 85 1.313 1.231 1.542 1.523 1.444 121.42 117.10 120.40 110.80 111.65 110.03 122.48 * * 86 ASP 86 1.332 1.231 1.520 1.538 1.476 121.44 115.93 120.89 109.83 111.43 110.83 123.15 87 TRP 87 1.316 1.234 1.533 1.531 1.450 122.62 115.28 120.80 110.46 111.29 110.19 123.91 88 ALA 88 1.336 1.236 1.522 1.524 1.467 124.68 114.80 121.97 112.18 111.63 112.91 123.15 +* * +* +* 89 ILE 89 1.296 1.240 1.508 1.545 1.429 123.13 115.76 120.91 109.47 109.40 110.36 123.30 ** +* ** 90 GLN 90 1.297 1.230 1.518 1.529 1.433 121.65 116.01 121.14 110.89 109.83 109.78 122.84 ** * ** 91 ALA 91 1.310 1.239 1.522 1.511 1.433 121.35 115.37 121.52 111.78 109.90 110.52 123.10 * * * 92 MET 92 1.298 1.235 1.523 1.519 1.446 122.61 118.47 120.00 108.72 110.74 108.63 121.53 ** * * ** 93 PRO 93 1.340 1.235 1.541 1.528 1.457 124.28 117.18 120.76 109.91 111.62 101.99 122.02 94 THR 94 1.296 1.225 1.519 1.534 1.431 120.19 116.43 120.46 109.75 109.95 111.49 123.11 ** * ** 95 PHE 95 1.310 1.219 1.501 1.534 1.416 122.31 117.41 119.94 108.31 105.13 109.56 122.64 * * ** ** ** 96 MET 96 1.279 1.243 1.496 1.546 1.437 120.87 115.07 120.84 112.72 110.43 110.13 124.07 +*** * * * +*** 97 PHE 97 1.305 1.251 1.522 1.518 1.399 123.53 116.20 121.28 108.65 109.85 107.95 122.52 +* *** * * *** 98 LEU 98 1.292 1.233 1.513 1.561 1.412 121.50 117.17 120.24 112.20 108.90 111.18 122.59 +** +* ** * +** 99 LYS 99 1.298 1.242 1.505 1.516 1.421 120.59 114.60 121.10 111.83 109.20 110.36 124.28 ** +* ** 100 GLU 100 1.327 1.230 1.538 1.512 1.458 124.30 115.39 121.78 111.88 112.11 110.89 122.83 * * 101 GLY 101 1.312 1.225 1.509 - 1.446 121.79 117.23 120.26 - 113.81 - 122.51 * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 102 LYS 102 1.320 1.223 1.507 1.559 1.451 120.72 116.96 120.00 108.72 107.81 111.50 123.03 * * * 103 ILE 103 1.311 1.237 1.515 1.555 1.456 121.45 116.45 120.62 109.17 109.81 111.69 122.92 * * 104 LEU 104 1.304 1.235 1.503 1.527 1.426 121.06 115.88 120.90 109.94 110.28 110.94 123.20 +* * +* +* 105 ASP 105 1.310 1.219 1.493 1.528 1.442 122.23 115.75 121.05 109.99 111.95 112.00 123.16 * +* +* 106 LYS 106 1.297 1.232 1.516 1.543 1.432 121.66 116.23 120.83 109.54 109.66 111.98 122.95 ** * ** 107 VAL 107 1.292 1.224 1.507 1.559 1.437 122.10 116.64 120.47 108.74 107.12 111.75 122.85 +** * * +** 108 VAL 108 1.292 1.236 1.510 1.530 1.428 121.26 116.11 120.51 110.40 108.93 111.31 123.37 +** +* +** 109 GLY 109 1.302 1.237 1.502 - 1.437 121.43 117.99 119.84 - 108.96 - 122.16 +* * +* 110 ALA 110 1.314 1.228 1.504 1.525 1.430 118.90 114.65 121.66 110.67 110.39 110.67 123.67 * * +* +* 111 LYS 111 1.294 1.234 1.490 1.504 1.413 124.15 117.87 119.43 108.79 107.67 111.14 122.70 ** +* * ** * * ** 112 LYS 112 1.303 1.229 1.530 1.520 1.427 120.56 115.82 120.65 111.97 110.26 110.07 123.42 +* +* +* 113 ASP 113 1.328 1.233 1.528 1.532 1.476 123.32 115.62 121.03 109.58 111.45 109.77 123.34 114 GLU 114 1.325 1.236 1.509 1.522 1.471 122.75 114.76 121.60 108.75 108.30 109.16 123.64 * * 115 LEU 115 1.320 1.211 1.496 1.503 1.429 122.19 115.59 120.64 109.10 108.88 110.02 123.75 * * * +* +* 116 GLN 116 1.323 1.234 1.524 1.544 1.474 121.83 116.44 120.59 108.36 110.67 113.16 122.95 +* +* 117 SER 117 1.326 1.241 1.530 1.526 1.454 120.94 115.41 121.22 111.40 109.94 110.04 123.34 118 THR 118 1.311 1.235 1.544 1.539 1.432 122.16 116.64 120.96 111.03 109.99 109.99 122.37 * * * 119 ILE 119 1.326 1.210 1.520 1.551 1.449 121.63 116.97 120.13 110.11 110.49 112.75 122.85 * * 120 ALA 120 1.329 1.237 1.521 1.519 1.465 121.30 115.93 120.85 111.51 111.12 111.44 123.22 121 LYS 121 1.316 1.228 1.526 1.503 1.447 122.53 115.33 121.43 108.10 109.54 109.13 123.24 * * * 122 HIS 122 1.319 1.237 1.536 1.532 1.450 122.91 117.75 119.62 108.16 112.99 110.24 122.60 * * 123 LEU 123 1.338 1.242 1.525 1.515 1.430 122.14 114.64 121.35 112.37 110.94 107.84 123.99 * * +* +* 124 ALA 124 1.307 - 1.508 1.528 1.437 124.46 - - 110.12 107.54 110.98 - +* * +* * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * ** ** *4.8* +* ** * ** ** +** * *4.8* ----------------------------------------------------------------------------------------------------------------------------------- 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 1.272 1.353 1.312 .015 **** +* * C-N (Pro) 1.341 .016 4 1.340 1.382 1.358 .017 +** * C-O C-O 1.231 .020 123 1.208 1.251 1.233 .008 * CA-C CH1E-C (except Gly) 1.525 .021 119 1.480 1.554 1.520 .014 ** * CH2G*-C (Gly) 1.516 .018 5 1.495 1.534 1.510 .013 * * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.511 1.529 1.521 .005 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.515 1.575 1.552 .015 * CH1E-CH2E (the rest) 1.530 .020 84 1.486 1.567 1.530 .016 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.367 1.477 1.442 .018 *4.8* * NH1-CH2G* (Gly) 1.451 .016 5 1.437 1.470 1.447 .012 * N-CH1E (Pro) 1.466 .015 4 1.457 1.483 1.472 .010 * ------------------------------------------------------------------------------------------------------------- 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 2.0 114 113.84 120.41 116.11 .91 * ** CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.75 118.82 116.91 1.48 * CH1E-C-N (Pro) 116.9 1.5 4 114.81 117.49 116.49 1.04 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.83 124.30 123.05 .57 * O-C-N (Pro) 122.0 1.4 4 121.90 123.49 122.56 .64 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 118.90 125.00 122.09 1.17 +* +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.91 122.70 121.41 .90 * C-N-CH1E (Pro) 122.6 5.0 4 121.74 124.28 123.10 .93 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 118.76 122.00 120.81 .56 * CH2G*-C-O (Gly) 120.8 2.1 5 119.80 121.50 120.52 .71 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.00 112.18 110.87 .65 * CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 107.97 112.75 110.10 1.07 +* CH2E-CH1E-C (the rest) 110.1 1.9 84 107.70 114.35 110.41 1.43 * ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.13 114.13 110.02 1.61 ** * NH1-CH2G*-C (Gly) 112.5 2.9 5 108.96 114.55 111.79 2.08 * N-CH1E-C (Pro) 111.8 2.5 4 111.38 114.58 112.38 1.29 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.29 112.91 110.96 .71 +* NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 108.60 113.43 111.40 1.05 +* * N-CH1E-CH2E (Pro) 103.0 1.1 4 101.99 104.15 103.22 .79 * NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.84 114.88 110.46 1.41 +* +** ------------------------------------------------------------------------------------------------------------- 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] 104 92.0% Residues in additional allowed regions [a,b,l,p] 9 8.0% 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 92.0 83.8 10.0 .8 Inside b. Omega angle st dev 122 3.1 6.0 3.0 -1.0 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 119 1.7 3.1 1.6 -.9 Inside e. H-bond energy st dev 76 .9 .8 .2 .4 Inside f. Overall G-factor 124 .1 -.4 .3 1.6 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 15 6.0 18.1 6.5 -1.9 BETTER b. Chi-1 trans st dev 42 4.6 19.0 5.3 -2.7 BETTER c. Chi-1 gauche plus st dev 45 6.8 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 102 6.6 18.2 4.8 -2.4 BETTER e. Chi-2 trans st dev 25 10.1 20.4 5.0 -2.1 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% 92.0 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.1 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .90 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 -.21 Chi1 only -.04 Chi3 & chi4 .65 Omega .08 ------ .01 ===== Main-chain covalent forces:- Main-chain bond lengths -.06 Main-chain bond angles .45 ------ .24 ===== OVERALL AVERAGE .08 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.