Residue-by-residue listing for refined_16 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 - - - -62.6 180.3 - - - - - - 181.9 - 33.7 - 2 GLY 2 - - - - - - - - - - - 177.7 - - - 3 HIS 3 b 53.4 - - - - - - - - - 188.9 - 32.2 - +* +* 4 HIS 4 b - 190.8 - - - - - - - - 173.3 - 32.1 - * * 5 HIS 5 b - - -70.9 - - - - - - - 184.7 -1.4 33.3 - 6 HIS 6 b - 179.1 - - - - - - - - 176.3 - 32.6 - 7 HIS 7 B - 173.5 - - - - - - - - 176.7 - 35.2 - 8 HIS 8 B - - -68.8 - - - - - - - 183.9 - 32.3 - 9 LEU 9 b - 182.5 - - - - - - - - 176.2 - 34.2 - 10 GLU 10 B - - -60.4 179.5 - - - - - - 179.2 - 35.5 - 11 MET 11 B - - -61.9 - - - - - - - 179.1 - 33.7 - 12 ALA 12 B - - - - - - - - - - 178.0 -.7 33.0 - +* +* 13 SER 13 S B - - -58.1 - - - - - - - 177.6 -1.1 35.5 - * * 14 GLU 14 B - 181.9 - 179.5 - - - - - - 180.4 - 33.3 - 15 GLU 15 B - - -57.5 175.8 - - - - - - 177.7 -.7 36.3 - +* +* 16 GLY 16 S - - - - - - - - - - - 177.4 -1.1 - - * * 17 GLN 17 B - - -69.5 - - - - - - - 183.1 - 30.8 - 18 VAL 18 B - 180.5 - - - - - - - - 181.0 - 35.7 - 19 ILE 19 E B - - -64.9 - - - - - - - 180.1 -2.8 33.0 - * * 20 ALA 20 E B - - - - - - - - - - 178.2 -.7 33.9 - +* +* Residue-by-residue listing for refined_16 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 21 CYS 21 E B - - -57.1 - - - - - - - 181.3 -.9 34.9 - * * 22 HIS 22 a - - -60.6 - - - - - - - 177.1 - 33.5 - 23 THR 23 h B 57.2 - - - - - - - - - 179.1 - 34.1 - 24 VAL 24 H A 61.8 - - - - -68.7 -25.4 - - - 179.0 - 33.0 - * * 25 GLU 25 H A - 183.7 - 186.2 - -63.4 -51.7 - - - 179.7 - 35.7 - * * 26 THR 26 H A - - -55.8 - - -67.9 -34.8 - - - 174.7 - 33.0 - 27 TRP 27 H A - 167.8 - - - -59.2 -47.3 - - - 177.3 -2.0 33.7 - 28 ASN 28 H A - 182.1 - - - -59.1 -41.3 - - - 178.1 -2.9 35.5 - * * 29 GLU 29 H A - 184.0 - - - -58.2 -46.1 - - - 180.4 -2.1 36.3 - 30 GLN 30 H A - - -61.2 - - -63.8 -45.4 - - - 179.2 -2.4 35.1 - 31 LEU 31 H A - - -69.4 179.9 - -64.9 -41.8 - - - 176.6 -2.4 34.7 - 32 GLN 32 H A - 177.8 - - - -60.8 -39.8 - - - 179.2 -2.7 33.7 - 33 LYS 33 H A - 181.9 - 176.9 - -67.5 -44.5 - - - 180.3 -2.2 33.7 - 34 ALA 34 H A - - - - - -64.0 -37.6 - - - 180.4 -2.9 33.8 - * * 35 ASN 35 H A - 185.4 - - - -68.7 -53.8 - - - 184.8 -2.5 37.4 - * * * 36 GLU 36 H A - 179.5 - 182.0 - -70.6 -44.2 - - - 183.4 -2.8 34.6 - * * 37 SER 37 h A - - -59.7 - - - - - - - 178.6 -3.0 33.7 - * * 38 LYS 38 T L - - -57.8 183.0 - - - - - - 181.9 - 34.2 - 39 THR 39 t B - - -47.8 - - - - - - - 181.5 -.9 34.9 - * +* +* 40 LEU 40 e B - 191.4 - 173.2 - - - - - - 185.5 - 34.8 - 41 VAL 41 E B 59.9 - - - - - - - - - 174.1 -.7 33.8 - * +* +* 42 VAL 42 E B - 178.3 - - - - - - - - 185.3 -2.9 33.8 - * * 43 VAL 43 E B - 184.3 - - - - - - - - 177.4 -3.0 34.0 - * * 44 ASP 44 E B - 164.8 - - - - - - - - 174.8 -3.1 36.3 - * * * 45 PHE 45 E B - - -61.6 - - - - - - - 177.8 -3.1 36.9 - * * 46 THR 46 E B - 187.3 - - - - - - - - 176.9 -1.9 33.2 - 47 ALA 47 t B - - - - - - - - - - 184.9 - 33.4 - 48 SER 48 T A - 181.1 - - - - - - - - 181.2 - 32.8 - 49 TRP 49 T A 54.6 - - - - - - - - - 180.2 - 30.9 - 50 CYS 50 h B - 174.4 - 222.4 - - - 51.0 - 2.0 183.0 -1.9 33.8 - ** *** *** 51 GLY 51 H - - - - - - -61.0 -65.2 - - - 180.2 -.5 - - ** ** ** 52 PRO 52 H - - - - - -58.7 -58.7 -31.3 - - - 180.6 - 39.2 - +* +* 53 CYS 53 H A - - -53.3 - - -70.7 -36.8 51.0 - 2.0 177.2 - 36.1 - *** *** 54 ARG 54 H A - 183.1 - - - -76.6 -34.2 - - - 178.2 -1.8 33.8 - 55 PHE 55 H A - 175.4 - - - -59.7 -33.4 - - - 184.5 -2.7 35.0 - 56 ILE 56 H A - 196.2 - - - -87.8 -17.2 - - - 183.0 -1.3 34.3 - +* +* +* 57 ALA 57 H A - - - - - -58.6 -46.4 - - - 179.8 -.6 31.5 - +* +* Residue-by-residue listing for refined_16 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 - - - - - -58.2 -58.2 -27.6 - - - 180.7 - 39.0 - * * * 59 PHE 59 H A - 184.0 - - - -75.8 -31.5 - - - 179.9 -.7 33.5 - +* +* 60 PHE 60 H A - 188.4 - - - -70.5 -33.2 - - - 175.8 -1.1 33.9 - * * 61 ALA 61 H A - - - - - -69.1 -32.9 - - - 177.8 -1.5 34.3 - 62 ASP 62 H A - 181.6 - - - -67.5 -44.4 - - - 176.0 -1.2 36.0 - * * 63 LEU 63 H A - - -68.7 180.8 - -53.6 -41.8 - - - 178.8 -2.3 34.8 - 64 ALA 64 H A - - - - - -62.9 -32.1 - - - 180.4 -1.5 33.6 - 65 LYS 65 H A - 182.8 - 180.4 - -79.3 -27.9 - - - 182.2 -.9 34.1 - * * * * 66 LYS 66 H A - - -60.9 174.8 - -92.7 -14.4 - - - 173.7 -1.7 32.1 - ** ** * ** 67 LEU 67 h b - - -69.4 170.7 - - - - - - 183.7 -1.6 32.8 - 68 PRO 68 T - - - - - -65.1 - - - - - 183.4 - 39.0 - * * 69 ASN 69 T A - - -64.6 - - - - - - - 178.5 - 34.2 - 70 VAL 70 t B - 177.9 - - - - - - - - 178.8 -1.2 34.6 - * * 71 LEU 71 E B - - -71.0 - - - - - - - 178.7 -2.2 33.7 - 72 PHE 72 E B - - -61.5 - - - - - - - 181.2 -.6 34.3 - +* +* 73 LEU 73 E B - - -78.6 - - - - - - - 176.5 -2.5 33.1 - 74 LYS 74 E B - - -95.6 179.4 - - - - - - 176.6 -2.4 33.2 - +* +* 75 VAL 75 E B - 177.0 - - - - - - - - 179.5 -3.5 35.4 - +* +* 76 ASP 76 E B - 188.4 - - - - - - - - 185.2 -.7 33.2 - +* +* 77 THR 77 e A - 180.9 - - - - - - - - 178.3 -2.4 31.3 - 78 ASP 78 T A - 186.0 - - - - - - - - 178.2 - 34.0 - 79 GLU 79 T A - - -70.0 182.0 - - - - - - 180.7 - 34.3 - 80 LEU 80 h b - - -68.0 180.9 - - - - - - 184.0 -3.4 34.2 - +* +* 81 LYS 81 H A - 197.8 - 178.1 - -69.3 -30.8 - - - 176.3 -1.4 33.8 - 82 SER 82 H A 54.2 - - - - -64.1 -39.7 - - - 176.3 - 34.3 - 83 VAL 83 H A - 176.3 - - - -64.6 -44.6 - - - 178.3 - 35.0 - 84 ALA 84 H A - - - - - -58.4 -47.2 - - - 178.1 -2.2 34.4 - 85 SER 85 H A - 182.6 - - - -61.6 -38.7 - - - 181.9 -2.9 34.7 - * * 86 ASP 86 H A - 182.1 - - - -66.7 -37.0 - - - 178.9 -2.2 34.3 - 87 TRP 87 h A - - -68.4 - - - - - - - 177.5 -2.3 31.5 - 88 ALA 88 T l - - - - - - - - - - 180.8 -.8 32.9 - +* +* 89 ILE 89 t B - - -55.0 - - - - - - - 182.5 -2.8 34.8 - 90 GLN 90 A - 185.1 - 180.8 - - - - - - 179.5 -.9 34.8 - +* +* 91 ALA 91 S B - - - - - - - - - - 182.3 - 33.7 - 92 MET 92 S B - - -60.4 171.3 - - - - - - -4.1 - 35.7 - 93 PRO 93 e cis - - - - - -93.3 - - - - - 178.0 - 39.4 - ** +* ** 94 THR 94 E B - - -57.8 - - - - - - - 179.1 -2.8 33.6 - * * 95 PHE 95 E B - - -64.6 - - - - - - - 179.5 -3.2 35.8 - +* +* Residue-by-residue listing for refined_16 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 96 MET 96 E B - 181.8 - 180.0 - - - - - - 181.9 -3.4 34.2 - +* +* 97 PHE 97 E B - - -63.4 - - - - - - - 182.1 -2.8 36.2 - * * 98 LEU 98 E B - - -52.4 178.0 - - - - - - 174.5 -2.1 36.8 - 99 LYS 99 E B - 179.4 - 176.6 - - - - - - 178.2 -3.4 32.0 - +* +* 100 GLU 100 T l - - -61.4 184.5 - - - - - - 180.0 - 31.5 - 101 GLY 101 T - - - - - - - - - - - 178.3 -.6 - - +* +* 102 LYS 102 E B - 194.2 - - - - - - - - 182.1 -2.0 35.1 - 103 ILE 103 E B - - -59.3 177.8 - - - - - - 174.0 - 34.1 - * * 104 LEU 104 E a - - -67.7 184.3 - - - - - - 186.1 -2.0 34.4 - * * 105 ASP 105 E B 45.8 - - - - - - - - - 184.9 -2.1 31.0 - * * 106 LYS 106 E B - 190.0 - 184.4 - - - - - - 178.2 - 36.5 - 107 VAL 107 E B - 179.3 - - - - - - - - 180.5 -3.4 34.7 - +* +* 108 VAL 108 E B 60.9 - - - - - - - - - 179.7 -.5 32.4 - ** ** 109 GLY 109 e - - - - - - - - - - - 180.6 -2.6 - - 110 ALA 110 B - - - - - - - - - - 172.8 - 34.3 - * * 111 LYS 111 h B - - -60.5 179.5 - - - - - - 182.7 -.9 36.3 - * * 112 LYS 112 H A - 183.1 - 182.4 - -61.6 -49.2 - - - 183.7 - 34.1 - 113 ASP 113 H A - 178.4 - - - -66.0 -48.0 - - - 179.4 - 33.0 - 114 GLU 114 H A - 178.7 - 177.0 - -64.4 -33.4 - - - 177.4 - 32.8 - 115 LEU 115 H A - 185.8 - - - -62.7 -49.9 - - - 179.8 -2.0 35.2 - 116 GLN 116 H A - - -53.8 - - -57.3 -40.0 - - - 180.1 -2.4 33.9 - 117 SER 117 H A - 179.9 - - - -64.9 -40.2 - - - 178.9 -2.3 34.0 - 118 THR 118 H A - - -54.2 - - -71.3 -33.2 - - - 177.3 -2.4 34.0 - 119 ILE 119 H A - - -58.0 - - -66.8 -44.2 - - - 178.9 -2.6 33.1 - 120 ALA 120 H A - - - - - -63.4 -31.5 - - - 177.1 -2.8 33.2 - * * 121 LYS 121 H A - 187.6 - 186.8 - -60.8 -44.1 - - - 181.4 -1.5 36.9 - 122 HIS 122 H A - - -69.8 - - -85.4 -18.7 - - - 180.5 -1.5 33.9 - +* +* +* 123 LEU 123 h B - 197.0 - 170.9 - - - - - - 180.2 -1.7 34.9 - 124 ALA 124 - - - - - - - - - - - - -.5 34.1 - ** ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: * * +* ** ** ** ** *** +* ** +* *** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 56.0 182.7 -63.0 180.6 -68.8 -66.3 -38.6 51.0 - 2.0 179.7 -2.0 34.2 *** *** Standard deviations: 5.2 6.5 8.0 8.5 16.6 8.0 9.7 .0 - .0 3.0 .9 1.6 Numbers of values: 8 50 44 33 4 46 46 2 0 2 122 82 119 0 Number of cis-peptides (labelled cis): 1 Residue-by-residue listing for refined_16 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_16 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 - 1.229 1.497 1.537 1.463 - 117.54 119.70 110.87 108.40 111.39 122.75 * * 2 GLY 2 1.307 1.238 1.495 - 1.421 119.58 114.87 121.08 - 112.85 - 124.04 +* * +* +* 3 HIS 3 1.298 1.231 1.516 1.568 1.444 124.45 116.16 121.18 112.93 107.65 112.23 122.62 ** +* +* * * * ** 4 HIS 4 1.308 1.237 1.528 1.540 1.439 120.83 114.39 121.78 112.01 112.75 111.06 123.79 +* * * +* 5 HIS 5 1.295 1.237 1.488 1.545 1.450 124.88 115.32 120.08 109.92 106.53 113.77 124.51 ** +* +* +* +* ** 6 HIS 6 1.322 1.232 1.519 1.547 1.451 123.60 114.89 121.37 111.39 112.76 111.00 123.73 * * 7 HIS 7 1.306 1.218 1.513 1.547 1.436 122.75 116.73 120.41 110.84 108.82 109.29 122.81 +* * +* 8 HIS 8 1.299 1.231 1.504 1.537 1.437 120.30 115.66 120.15 112.00 108.61 112.33 124.14 ** * * * * ** 9 LEU 9 1.313 1.231 1.524 1.536 1.450 123.25 115.46 121.10 110.14 112.20 110.19 123.43 * * 10 GLU 10 1.305 1.233 1.508 1.521 1.437 122.47 117.12 120.11 109.09 108.01 110.58 122.76 +* * * +* 11 MET 11 1.296 1.228 1.507 1.545 1.442 121.12 116.76 120.52 109.79 109.33 112.37 122.71 ** * ** Residue-by-residue listing for refined_16 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 1.303 1.237 1.514 1.519 1.434 121.18 115.22 121.55 111.31 110.14 111.39 123.06 +* * +* 13 SER 13 1.301 1.241 1.517 1.539 1.442 123.46 117.74 119.47 109.59 107.67 110.22 122.78 ** * ** 14 GLU 14 1.310 1.230 1.513 1.526 1.442 120.51 115.94 120.84 110.19 109.41 112.23 123.20 * * * 15 GLU 15 1.301 1.224 1.503 1.532 1.440 122.58 117.45 119.78 108.51 107.50 110.12 122.77 ** * * ** 16 GLY 16 1.299 1.234 1.501 - 1.441 120.11 117.22 120.27 - 113.87 - 122.51 ** ** 17 GLN 17 1.308 1.239 1.497 1.521 1.434 119.92 114.49 121.49 110.61 111.41 114.60 124.02 * * * ** ** 18 VAL 18 1.290 1.233 1.517 1.554 1.438 123.48 117.11 120.04 109.25 108.53 110.27 122.84 +** * +** 19 ILE 19 1.310 1.224 1.524 1.569 1.441 121.23 116.75 120.74 109.99 109.78 113.19 122.49 * * * 20 ALA 20 1.301 1.233 1.513 1.525 1.439 121.53 116.30 120.79 110.74 110.09 110.65 122.89 +* +* 21 CYS 21 1.303 1.231 1.515 1.513 1.422 121.98 116.53 120.72 110.78 109.08 109.42 122.72 +* +* +* 22 HIS 22 1.306 1.241 1.519 1.540 1.447 121.44 116.17 120.87 110.87 110.67 111.08 122.96 +* +* 23 THR 23 1.327 1.246 1.520 1.561 1.450 122.07 116.89 120.28 109.17 109.27 112.47 122.82 24 VAL 24 1.328 1.225 1.532 1.571 1.456 121.32 115.40 121.33 110.97 109.59 112.26 123.22 * * 25 GLU 25 1.329 1.235 1.529 1.512 1.444 122.56 116.43 120.58 108.92 110.26 109.60 122.97 26 THR 26 1.331 1.212 1.535 1.547 1.450 121.08 116.31 120.89 111.19 109.86 111.61 122.78 27 TRP 27 1.319 1.237 1.543 1.531 1.458 122.04 115.93 120.85 111.64 110.88 109.56 123.21 28 ASN 28 1.324 1.238 1.531 1.534 1.466 122.87 114.66 121.40 109.52 109.67 109.50 123.93 29 GLU 29 1.329 1.238 1.545 1.541 1.459 124.65 116.05 120.87 110.15 109.78 107.72 123.07 +* +* +* 30 GLN 30 1.332 1.226 1.519 1.499 1.430 123.51 116.86 120.44 109.82 111.80 109.14 122.70 +* * * +* 31 LEU 31 1.328 1.234 1.503 1.489 1.422 122.28 115.89 120.68 110.11 111.46 109.51 123.42 * ** +* ** 32 GLN 32 1.308 1.232 1.527 1.534 1.434 121.87 115.96 120.64 111.34 109.57 110.54 123.35 +* * +* 33 LYS 33 1.318 1.229 1.529 1.536 1.446 122.28 116.82 120.47 111.07 110.76 110.41 122.69 34 ALA 34 1.335 1.225 1.523 1.520 1.459 121.45 115.35 121.12 110.49 110.83 110.55 123.52 35 ASN 35 1.311 1.238 1.511 1.522 1.458 123.30 114.47 121.68 107.71 110.48 108.30 123.84 * * * * 36 GLU 36 1.302 1.229 1.530 1.518 1.459 122.93 117.11 120.40 109.61 113.47 109.42 122.48 +* +* 37 SER 37 1.308 1.237 1.523 1.518 1.434 120.96 116.07 120.21 111.49 112.15 109.47 123.72 * * * 38 LYS 38 1.346 1.227 1.516 1.514 1.470 123.24 115.76 121.46 109.86 110.41 110.60 122.75 * * 39 THR 39 1.294 1.243 1.534 1.515 1.424 121.58 115.48 121.53 109.74 109.90 110.12 122.99 +** +* +** 40 LEU 40 1.286 1.242 1.531 1.556 1.434 123.00 116.28 120.82 112.38 106.79 109.00 122.88 *** * * * +* *** 41 VAL 41 1.303 1.234 1.533 1.564 1.432 121.33 115.91 121.03 110.95 111.93 110.30 123.03 +* * +* 42 VAL 42 1.309 1.240 1.514 1.537 1.440 122.79 116.57 120.59 110.06 107.75 112.36 122.83 * * * Residue-by-residue listing for refined_16 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 43 VAL 43 1.304 1.235 1.525 1.551 1.437 121.29 114.80 121.25 109.52 111.55 111.45 123.95 +* * +* 44 ASP 44 1.296 1.236 1.516 1.531 1.451 124.66 117.14 120.21 109.46 110.15 108.49 122.62 ** +* * ** 45 PHE 45 1.315 1.247 1.526 1.526 1.419 120.79 116.52 120.58 107.99 108.58 109.52 122.89 ** * ** 46 THR 46 1.306 1.220 1.532 1.559 1.432 122.17 117.47 119.86 111.64 108.91 111.47 122.66 +* * * +* 47 ALA 47 1.309 1.243 1.506 1.519 1.450 122.44 116.50 119.89 110.68 108.61 111.75 123.59 * * 48 SER 48 1.316 1.225 1.543 1.543 1.461 122.75 118.15 119.90 111.07 113.69 110.50 121.94 49 TRP 49 1.324 1.230 1.535 1.545 1.464 120.59 116.62 120.79 111.72 113.32 112.46 122.59 * * 50 CYS 50 1.309 1.228 1.523 1.532 1.448 121.52 116.11 120.29 111.40 110.38 110.06 123.60 * * 51 GLY 51 1.328 1.231 1.522 - 1.468 122.83 118.88 119.62 - 114.24 - 121.50 * * * * 52 PRO 52 1.363 1.230 1.518 1.533 1.480 122.75 114.69 121.81 109.43 111.10 103.68 123.49 * * * * 53 CYS 53 1.297 1.222 1.537 1.500 1.432 123.46 116.55 120.95 109.86 110.65 107.75 122.50 ** +* * +* ** 54 ARG 54 1.319 1.218 1.528 1.564 1.450 121.97 115.50 121.12 113.19 108.40 109.18 123.35 +* +* * +* 55 PHE 55 1.321 1.233 1.537 1.546 1.465 123.91 116.76 120.76 110.33 111.87 108.97 122.47 * * 56 ILE 56 1.316 1.237 1.555 1.569 1.455 120.89 115.96 121.17 110.35 110.66 110.50 122.82 * * * 57 ALA 57 1.331 1.235 1.561 1.529 1.466 123.12 120.02 119.16 111.53 114.51 111.18 120.82 +* +* * * +* 58 PRO 58 1.380 1.240 1.529 1.527 1.480 122.37 116.23 121.00 109.66 112.85 103.30 122.76 ** ** 59 PHE 59 1.321 1.219 1.529 1.535 1.445 121.10 116.18 121.02 111.15 110.08 110.79 122.76 60 PHE 60 1.315 1.230 1.535 1.539 1.459 122.19 115.86 121.23 112.14 109.26 109.50 122.90 * * * 61 ALA 61 1.324 1.236 1.532 1.517 1.462 121.77 115.26 121.38 110.25 109.94 110.32 123.36 62 ASP 62 1.325 1.230 1.497 1.514 1.471 123.16 114.28 121.53 109.05 109.17 109.33 124.18 * * 63 LEU 63 1.311 1.227 1.520 1.521 1.433 123.88 116.08 120.48 110.72 111.28 109.05 123.41 * * * * 64 ALA 64 1.318 1.227 1.529 1.519 1.450 122.49 116.49 121.11 110.81 111.58 110.37 122.40 65 LYS 65 1.321 1.242 1.533 1.540 1.452 121.55 116.15 121.21 110.81 110.74 110.09 122.63 66 LYS 66 1.314 1.235 1.531 1.534 1.447 121.61 116.51 120.82 113.17 111.90 110.03 122.67 * +* +* 67 LEU 67 1.314 1.227 1.529 1.517 1.432 122.68 116.55 121.25 112.11 110.42 110.65 122.14 * * * * 68 PRO 68 1.348 1.233 1.532 1.534 1.476 123.62 116.73 120.64 109.68 114.10 103.22 122.62 69 ASN 69 1.322 1.234 1.513 1.523 1.441 122.13 115.84 121.15 110.23 111.34 110.25 123.00 70 VAL 70 1.304 1.235 1.515 1.554 1.433 122.14 116.65 120.63 109.71 108.85 111.39 122.69 +* * +* 71 LEU 71 1.306 1.229 1.503 1.533 1.417 121.34 116.02 120.91 110.35 110.06 111.57 123.05 +* * ** ** 72 PHE 72 1.297 1.244 1.497 1.516 1.434 121.47 115.24 121.11 109.41 109.25 111.69 123.64 ** * * ** 73 LEU 73 1.283 1.229 1.501 1.545 1.443 123.06 115.32 120.96 109.19 111.56 113.07 123.72 *** * +* *** Residue-by-residue listing for refined_16 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 1.303 1.237 1.493 1.498 1.405 123.15 115.20 121.15 110.71 111.78 111.14 123.62 +* +* +* +** +** 75 VAL 75 1.292 1.243 1.499 1.551 1.427 122.70 116.69 120.48 109.29 107.42 111.21 122.80 +** * +* * +** 76 ASP 76 1.299 1.218 1.497 1.500 1.430 119.69 116.19 120.74 110.37 108.86 112.28 123.06 ** * * * * * ** 77 THR 77 1.292 1.235 1.532 1.557 1.440 122.22 118.25 119.59 111.25 113.97 112.39 122.14 +** * +** 78 ASP 78 1.308 1.236 1.499 1.515 1.455 119.73 114.15 122.03 110.08 108.15 111.54 123.83 +* * * * * +* 79 GLU 79 1.300 1.229 1.512 1.495 1.417 123.48 116.72 120.53 110.82 111.84 109.26 122.71 ** +* ** ** 80 LEU 80 1.309 1.235 1.500 1.511 1.414 122.42 114.02 122.28 111.95 108.97 109.53 123.69 * * ** * ** 81 LYS 81 1.299 1.228 1.533 1.517 1.424 123.05 116.27 120.88 112.28 110.33 109.09 122.82 ** +* * ** 82 SER 82 1.326 1.237 1.532 1.529 1.451 121.98 115.34 121.21 111.29 109.62 109.48 123.43 83 VAL 83 1.329 1.230 1.516 1.550 1.454 123.41 115.39 121.25 109.29 109.32 110.86 123.35 84 ALA 84 1.319 1.219 1.514 1.505 1.447 122.26 116.00 120.48 110.09 110.29 110.24 123.51 85 SER 85 1.319 1.231 1.536 1.543 1.444 122.57 116.11 120.84 110.65 110.21 109.67 123.01 86 ASP 86 1.326 1.229 1.523 1.540 1.462 122.51 116.46 121.15 110.40 111.28 110.01 122.37 87 TRP 87 1.306 1.237 1.524 1.523 1.440 121.25 115.99 120.31 111.92 112.67 111.74 123.70 +* +* 88 ALA 88 1.341 1.235 1.532 1.530 1.476 124.14 116.15 120.81 111.22 112.17 110.55 122.95 * * 89 ILE 89 1.320 1.236 1.527 1.558 1.453 122.69 116.26 120.75 109.00 109.28 111.59 122.94 90 GLN 90 1.306 1.231 1.525 1.533 1.449 121.69 116.00 121.40 110.68 110.05 109.45 122.61 +* +* 91 ALA 91 1.309 1.234 1.505 1.514 1.436 121.54 116.38 120.86 110.92 109.32 110.98 122.76 * * * 92 MET 92 1.292 1.239 1.513 1.516 1.425 121.23 118.16 120.19 109.30 109.79 109.58 121.63 +** +* +** 93 PRO 93 1.327 1.232 1.546 1.526 1.457 124.03 117.67 120.59 110.36 111.20 102.37 121.70 94 THR 94 1.302 1.229 1.526 1.526 1.440 120.10 116.20 120.67 110.19 110.69 111.42 123.13 +* +* 95 PHE 95 1.315 1.232 1.510 1.517 1.425 122.87 116.76 120.63 109.15 109.26 109.72 122.61 +* +* 96 MET 96 1.291 1.230 1.507 1.518 1.436 121.08 115.53 121.12 111.03 109.66 110.08 123.35 +** * +** 97 PHE 97 1.290 1.247 1.512 1.512 1.407 123.27 116.59 121.02 109.79 109.26 108.49 122.39 +** +** * +** 98 LEU 98 1.293 1.226 1.523 1.546 1.428 120.58 117.07 120.33 107.71 108.19 110.14 122.60 +** +* * * +** 99 LYS 99 1.307 1.239 1.496 1.517 1.439 120.99 114.80 120.90 110.79 110.85 113.02 124.26 +* * * * +* 100 GLU 100 1.319 1.222 1.533 1.529 1.451 124.39 115.91 121.10 112.27 112.60 111.43 122.92 * * * 101 GLY 101 1.323 1.224 1.516 - 1.444 121.22 117.27 120.74 - 112.87 - 121.99 102 LYS 102 1.311 1.230 1.545 1.542 1.448 120.99 117.59 119.79 110.48 108.07 109.66 122.62 * * * 103 ILE 103 1.323 1.236 1.530 1.573 1.470 122.03 116.57 120.54 109.19 111.66 111.69 122.87 * * 104 LEU 104 1.328 1.236 1.499 1.532 1.440 121.52 115.76 120.89 108.27 109.88 112.64 123.32 * * * Residue-by-residue listing for refined_16 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 1.318 1.225 1.487 1.540 1.430 122.07 116.11 120.92 112.26 111.43 113.02 122.93 +* * * * +* 106 LYS 106 1.295 1.226 1.524 1.523 1.419 121.03 116.66 120.46 110.04 109.40 107.85 122.86 ** ** +* ** 107 VAL 107 1.306 1.234 1.518 1.559 1.450 122.68 116.70 120.58 109.40 108.60 111.60 122.71 +* +* 108 VAL 108 1.303 1.246 1.537 1.566 1.433 121.20 115.85 121.46 112.02 110.82 111.59 122.63 +* * * +* 109 GLY 109 1.308 1.235 1.502 - 1.434 120.99 117.14 120.45 - 111.13 - 122.42 +* * +* 110 ALA 110 1.310 1.235 1.502 1.525 1.428 119.71 114.78 121.51 110.21 110.02 110.70 123.66 * * +* * +* 111 LYS 111 1.286 1.231 1.491 1.512 1.413 123.42 117.82 119.22 108.68 105.74 110.44 122.94 *** +* ** +* *** 112 LYS 112 1.302 1.236 1.525 1.518 1.430 121.10 115.94 120.64 110.36 110.64 110.48 123.35 +* * +* 113 ASP 113 1.321 1.244 1.524 1.523 1.460 122.19 116.56 120.48 110.61 112.42 111.07 122.95 114 GLU 114 1.330 1.241 1.517 1.531 1.463 121.38 116.27 120.69 111.01 110.75 111.56 123.02 115 LEU 115 1.324 1.212 1.496 1.510 1.441 120.99 115.57 120.53 108.51 108.64 111.29 123.87 * * 116 GLN 116 1.329 1.228 1.525 1.546 1.476 121.78 115.93 120.88 108.44 110.03 112.85 123.16 * * 117 SER 117 1.322 1.236 1.533 1.543 1.447 121.94 115.96 121.14 111.50 110.12 109.86 122.88 118 THR 118 1.312 1.235 1.537 1.541 1.435 121.99 116.56 120.95 110.89 109.95 110.56 122.47 * * * 119 ILE 119 1.328 1.217 1.516 1.555 1.446 120.96 116.53 120.30 110.00 109.55 113.02 123.10 120 ALA 120 1.330 1.226 1.522 1.516 1.461 121.96 115.91 120.79 111.05 110.88 110.78 123.30 121 LYS 121 1.322 1.231 1.523 1.503 1.459 122.78 114.87 121.78 107.53 109.74 109.03 123.34 * * * 122 HIS 122 1.316 1.235 1.533 1.535 1.442 122.94 117.01 120.22 110.33 112.60 110.29 122.76 123 LEU 123 1.326 1.233 1.520 1.532 1.431 122.36 115.60 120.83 111.55 109.10 108.87 123.57 * * 124 ALA 124 1.304 - 1.499 1.533 1.442 123.57 - - 110.54 107.73 111.49 - +* * * * +* ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: *** +* ** +** +* +* +* +* ** * *** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 1.283 1.346 1.312 .013 *** * * C-N (Pro) 1.341 .016 4 1.327 1.380 1.354 .019 ** C-O C-O 1.231 .020 123 1.212 1.247 1.232 .007 CA-C CH1E-C (except Gly) 1.525 .021 119 1.487 1.561 1.520 .015 +* +* CH2G*-C (Gly) 1.516 .018 5 1.495 1.522 1.507 .010 * CA-CB CH1E-CH3E (Ala) 1.521 .033 13 1.505 1.533 1.521 .007 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 22 1.515 1.573 1.554 .014 * CH1E-CH2E (the rest) 1.530 .020 84 1.489 1.568 1.528 .015 ** +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 115 1.405 1.476 1.443 .015 +** NH1-CH2G* (Gly) 1.451 .016 5 1.421 1.468 1.442 .015 +* * N-CH1E (Pro) 1.466 .015 4 1.457 1.480 1.473 .010 ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_16 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 2.0 114 114.02 120.02 116.17 .92 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 5 114.87 118.88 117.07 1.28 * CH1E-C-N (Pro) 116.9 1.5 4 114.69 117.67 116.33 1.08 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 119 120.82 124.51 123.01 .57 * O-C-N (Pro) 122.0 1.4 4 121.70 123.49 122.64 .64 * C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 114 119.69 124.88 122.14 1.12 * +* C-NH1-CH2G* (Gly) 120.6 1.7 5 119.58 122.83 120.94 1.11 * C-N-CH1E (Pro) 122.6 5.0 4 122.37 124.03 123.20 .66 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 118 119.16 122.28 120.78 .55 CH2G*-C-O (Gly) 120.8 2.1 5 119.62 121.08 120.43 .49 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 13 110.09 111.53 110.76 .43 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 22 109.00 112.02 110.14 .87 * CH2E-CH1E-C (the rest) 110.1 1.9 84 107.53 113.19 110.43 1.25 * +* N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 115 105.74 114.51 110.14 1.61 +* * NH1-CH2G*-C (Gly) 112.5 2.9 5 111.13 114.24 112.99 1.08 N-CH1E-C (Pro) 111.8 2.5 4 111.10 114.10 112.31 1.24 N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 13 110.24 111.75 110.84 .46 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 22 110.12 113.19 111.51 .84 N-CH1E-CH2E (Pro) 103.0 1.1 4 102.37 103.68 103.14 .48 NH1-CH1E-CH2E (the rest) 110.5 1.7 80 107.72 114.60 110.40 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_16 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] 102 90.3% Residues in additional allowed regions [a,b,l,p] 11 9.7% 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 90.3 83.8 10.0 .6 Inside b. Omega angle st dev 122 3.0 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 1.6 3.1 1.6 -.9 Inside e. H-bond energy st dev 82 .9 .8 .2 .4 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 8 5.2 18.1 6.5 -2.0 BETTER b. Chi-1 trans st dev 50 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 44 8.0 17.5 4.9 -1.9 BETTER d. Chi-1 pooled st dev 102 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 33 8.5 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% 90.3 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.8 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .88 3 Residue-by-residue listing for refined_16 Page 14 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.10 Chi1-chi2 distribution .05 Chi1 only .10 Chi3 & chi4 .37 Omega .09 ------ .06 ===== Main-chain covalent forces:- Main-chain bond lengths .04 Main-chain bond angles .47 ------ .29 ===== OVERALL AVERAGE .13 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.