Residue-by-residue listing for refined_10 Page 1 ---------------------------------------- This listing highlights the residues in the structure which may need investigation. The ideal values and standard deviations against which the structure has been compared are shown in the following table: <------------------------------- I D E A L V A L U E S -------------------------------> Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha ------------------------------------------------------------------------------------------ Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9 Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5 ------------------------------------------------------------------------------------------ In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above. Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*. The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing. Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments. Full print-out. ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 1 MET 1 - - 179.9 - 178.8 - - - - - - 174.0 - 32.9 - * * 2 ALA 2 b - - - - - - - - - - 185.4 - 33.3 - 3 ASP 3 B - - -68.4 - - - - - - - 176.6 -.8 32.9 - +* +* 4 THR 4 ~a - - -59.6 - - - - - - - 177.8 - 34.6 - ** ** 5 GLY 5 - - - - - - - - - - - 178.9 - - - 6 GLU 6 S B 51.2 - - 188.3 - - - - - - 183.6 - 33.2 - 7 VAL 7 E B - - -61.4 - - - - - - - 180.1 -2.6 33.0 - 8 GLN 8 E B 58.4 - - 176.9 - - - - - - 177.8 - 34.5 - 9 PHE 9 E B - 179.9 - - - - - - - - 180.8 -1.6 35.0 - 10 MET 10 E B - 179.4 - 197.9 - - - - - - 167.4 - 36.7 - * ** ** 11 LYS 11 E B 72.7 - - - - - - - - - 173.2 -.9 32.7 - * +* +* 12 PRO 12 - - - - - -70.8 - - - - - 181.7 - 39.0 - * * 13 PHE 13 B - 197.4 - - - - - - - - 193.9 - 32.4 - ** ** 14 ILE 14 h B - - -58.2 178.7 - - - - - - 183.2 - 33.3 - 15 SER 15 H A - 184.7 - - - -61.2 -29.0 - - - 179.8 - 33.1 - 16 GLU 16 H A - - -58.8 180.9 - -60.4 -26.9 - - - 179.4 - 34.6 - * * 17 LYS 17 H a 60.0 - - 179.5 - -111.2 -36.3 - - - 182.1 -1.8 31.4 - +*** +*** 18 SER 18 H A - 181.3 - - - -61.9 -25.4 - - - 182.4 -3.5 34.0 - * +* +* Residue-by-residue listing for refined_10 Page 2 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 19 SER 19 h A - - -63.0 - - - - - - - 181.8 -2.0 32.5 - 20 LYS 20 T a - 190.3 - - - - - - - - 182.6 -1.7 33.2 - 21 SER 21 t B - - -59.7 - - - - - - - 175.6 -1.9 34.9 - 22 LEU 22 E B - 190.8 - 172.2 - - - - - - 180.4 -1.4 33.4 - 23 GLU 23 E B - - -54.8 194.8 - - - - - - 180.0 -.8 35.5 - +* +* 24 ILE 24 E B - - -60.8 180.8 - - - - - - 178.2 -2.5 33.2 - 25 PRO 25 h - - - - - -60.2 - - - - - 184.8 - 38.8 - * * 26 LEU 26 H A - - -67.1 - - -57.1 -40.0 - - - 180.9 - 32.5 - 27 GLY 27 H - - - - - - -67.8 -35.2 - - - 181.7 - - - 28 PHE 28 H A - 193.3 - - - -84.0 -23.3 - - - 175.8 - 34.1 - +* * +* 29 ASN 29 H A - 174.6 - - - -63.5 -43.8 - - - 180.3 -2.1 34.5 - 30 GLU 30 h A - - -60.2 - - - - - - - 182.3 -1.8 34.5 - 31 TYR 31 T A - 185.0 - - - - - - - - 176.2 - 33.8 - 32 PHE 32 t B - - -68.3 - - - - - - - 184.1 -1.6 33.1 - 33 PRO 33 - - - - - -62.6 - - - - - 183.1 - 39.5 - +* +* 34 ALA 34 b - - - - - - - - - - 177.2 - 34.5 - 35 PRO 35 S - - - - - -64.2 - - - - - 175.4 - 38.4 - * * 36 PHE 36 S b - 186.1 - - - - - - - - 178.8 - 32.4 - 37 PRO 37 - - - - - -87.0 - - - - - 177.1 - 39.5 - +* +* +* 38 ILE 38 e a - - -58.4 - - - - - - - 180.6 - 32.6 - 39 THR 39 E B 50.9 - - - - - - - - - 178.0 - 33.4 - 40 VAL 40 E B - - -63.6 - - - - - - - 182.1 -3.4 34.1 - +* +* 41 ASP 41 E B - - -66.8 - - - - - - - 179.1 -1.1 32.0 - * * 42 LEU 42 E B - - -80.1 - - - - - - - 179.7 -3.3 35.2 - +* +* 43 LEU 43 E B - - -64.6 - - - - - - - 180.8 -2.9 34.3 - * * 44 ASP 44 E B - 165.1 - - - - - - - - 182.0 -3.1 34.1 - * * * 45 TYR 45 e A - 188.0 - - - - - - - - 182.6 -1.4 35.2 - 46 SER 46 T A - - -54.9 - - - - - - - 175.5 - 33.6 - 47 GLY 47 t - - - - - - - - - - - 179.5 -2.0 - - 48 ARG 48 e B - 185.6 - - - - - - - - 180.2 - 35.1 - 49 SER 49 E B 55.5 - - - - - - - - - 178.3 - 32.4 - 50 TRP 50 E B - - -52.9 - - - - - - - 175.5 -2.9 37.5 - * * * 51 THR 51 E B - - -56.6 - - - - - - - 187.1 - 34.2 - * * 52 VAL 52 E B - 182.4 - - - - - - - - 178.2 -2.6 34.3 - 53 ARG 53 E B - 179.1 - 178.6 - - - - - - 182.3 -3.6 34.0 - ** ** 54 MET 54 E B - 177.1 - - - - - - - - 182.5 -1.9 35.7 - 55 LYS 55 E B - - -65.9 174.7 - - - - - - 174.3 -1.3 36.7 - * * 56 LYS 56 E B - - -59.8 194.7 - - - - - - 174.5 - 33.5 - 57 ARG 57 E B - 178.0 - 179.3 - - - - - - 179.5 -.6 32.2 - +* +* 58 GLY 58 T - - - - - - - - - - - 182.2 - - - 59 GLU 59 T A 61.7 - - - - - - - - - 184.5 - 34.3 - Residue-by-residue listing for refined_10 Page 3 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 60 LYS 60 E B - 183.3 - 183.6 - - - - - - 184.5 -.5 34.5 - ** ** 61 VAL 61 E B - - -54.1 - - - - - - - 181.8 -1.0 33.3 - * * 62 PHE 62 E B - - -57.3 - - - - - - - 168.0 -1.0 36.5 - ** * ** 63 LEU 63 E B - - -66.9 178.2 - - - - - - 189.9 -2.0 34.4 - +* +* 64 THR 64 e a 51.5 - - - - - - - - - 181.2 -1.4 34.2 - 65 VAL 65 T B - 181.2 - - - - - - - - 181.1 - 34.7 - 66 GLY 66 h - - - - - - - - - - - 173.3 - - - * * 67 TRP 67 H A - 174.9 - - - -67.1 -27.8 - - - 179.9 - 34.0 - * * 68 GLU 68 H A - 189.8 - 175.5 - -72.8 -29.6 - - - 174.0 -1.0 31.5 - * * * 69 ASN 69 H A - - -64.7 - - -67.6 -32.4 - - - 182.7 - 35.1 - 70 PHE 70 H A - 191.9 - - - -73.9 -53.3 - - - 184.2 -1.5 36.7 - * * 71 VAL 71 H A 71.8 - - - - -68.3 -38.2 - - - 179.8 -3.4 33.5 - +* +* 72 LYS 72 H A - 185.6 - - - -70.4 -37.0 - - - 185.2 -2.3 34.7 - 73 ASP 73 H A - 182.6 - - - -77.9 -42.9 - - - 180.2 -1.4 33.2 - * * 74 ASN 74 H A 64.7 - - - - -108.0 14.1 - - - 175.4 -2.5 30.0 - +*** *4.7* * *4.7* 75 ASN 75 h XX - 189.8 - - - - - - - - 175.7 -.6 31.8 - **** +* **** 76 LEU 76 l - - -80.1 181.9 - - - - - - 173.3 -2.3 29.7 - * * * 77 GLU 77 t B 58.9 - - 185.8 - - - - - - 182.3 - 30.9 - 78 ASP 78 T B 46.9 - - - - - - - - - 183.3 - 31.0 - * * 79 GLY 79 T - - - - - - - - - - - 174.9 - - - 80 LYS 80 t B - - -59.0 188.7 - - - - - - 184.8 -1.4 33.3 - 81 TYR 81 E B - - -57.0 - - - - - - - 181.2 -.9 33.7 - * * 82 LEU 82 E B 50.7 - - - - - - - - - 175.9 -.6 29.9 - +* * +* 83 GLN 83 E B - - -64.7 179.6 - - - - - - 174.7 -2.1 35.7 - 84 PHE 84 E B - - -65.9 - - - - - - - 178.5 -2.7 33.7 - 85 ILE 85 E B - - -54.0 - - - - - - - 182.8 -3.2 35.9 - +* +* 86 TYR 86 E B - 177.2 - - - - - - - - 173.7 -3.4 34.2 - * +* +* 87 ASP 87 e b - 191.6 - - - - - - - - 180.2 -.6 35.2 - +* +* 88 ARG 88 S a - - -74.2 - - - - - - - 180.4 - 31.1 - 89 ASP 89 S b - 187.5 - - - - - - - - 183.2 - 35.9 - 90 ARG 90 e A - - -61.9 173.2 - - - - - - 181.3 - 35.0 - 91 THR 91 E B - - -51.6 - - - - - - - 179.5 - 35.8 - * * 92 PHE 92 E B - - -64.2 - - - - - - - 180.2 -2.6 34.6 - 93 TYR 93 E B - 186.2 - - - - - - - - 182.9 -1.6 35.3 - 94 VAL 94 E B 63.5 - - - - - - - - - 177.1 -4.1 32.6 - +** +** 95 ILE 95 E B - - -58.2 179.5 - - - - - - 180.8 -2.4 33.8 - Residue-by-residue listing for refined_10 Page 4 ---------------------------------------- ................................................................................................................................... Residue Kabsch Region --------- Sander of No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev ----------------------------------------------------------------------------------------------------------------------------------- 96 ILE 96 E B - - -59.5 - - - - - - - 170.5 -.7 36.5 - +* +* +* 97 TYR 97 E B - - -66.1 - - - - - - - 183.2 -3.1 34.2 - * * 98 GLY 98 S - - - - - - - - - - - 179.5 -.8 - - +* +* 99 HIS 99 B - 180.9 - - - - - - - - 175.1 - 34.8 - 100 ASN 100 B - - -55.9 - - - - - - - 178.2 - 34.9 - 101 MET 101 b - 179.9 - 180.5 - - - - - - 182.0 - 32.3 - 102 CYS 102 - - - -54.5 - - - - - - - - -1.8 35.0 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: **** * * * * +* +*** *4.7* ** +** +* *4.7* ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 58.5 183.6 -61.8 181.8 -69.0 -73.3 -31.7 - - - 179.7 -1.9 34.1 Standard deviations: 7.9 6.5 6.5 6.8 10.8 15.7 14.5 - - - 4.1 .9 1.9 Numbers of values: 14 33 41 24 5 16 16 0 0 0 101 57 95 0 KEY TO CODES: ------------ Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander) -------------------------------- -------------------------------------------- A - Core alpha B - residue in isolated beta-bridge a - Allowed alpha E - extended strand, participates in beta-ladder ~a - Generous alpha ** Generous G - 3-helix (3/10 helix) B - Core beta H - 4-helix (alpha-helix) b - Allowed beta I - 5-helix (pi-helix) ~b - Generous beta ** Generous S - bend L - Core left-handed alpha T - hydrogen-bonded turn l - Allowed left-handed alpha ~l - Generous left-handed alpha ** Generous e - extension of beta-strand p - Allowed epsilon g - extension of 3/10 helix ~p - Generous epsilon ** Generous h - extension of alpha-helix XX - Outside major areas **** Disallowed Residue-by-residue listing for refined_10 Page 5 ---------------------------------------- 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 - 1.226 1.511 1.543 1.479 - 116.51 120.79 110.91 109.62 112.05 122.70 * * 2 ALA 2 1.310 1.236 1.500 1.524 1.432 121.16 115.66 121.01 111.49 107.43 111.80 123.19 * * * * * 3 ASP 3 1.309 1.232 1.507 1.541 1.441 121.39 114.78 121.42 110.75 111.99 111.63 123.75 * * 4 THR 4 1.301 1.232 1.520 1.565 1.456 125.10 114.83 121.57 108.73 106.85 112.94 123.58 ** +* +* ** 5 GLY 5 1.317 1.241 1.500 - 1.423 121.74 115.57 120.73 - 112.29 - 123.69 +* +* 6 GLU 6 1.299 1.235 1.523 1.536 1.439 122.78 116.63 120.74 112.97 110.09 109.56 122.62 ** +* ** 7 VAL 7 1.303 1.232 1.506 1.562 1.441 121.37 116.28 120.83 110.40 110.33 112.56 122.88 +* +* 8 GLN 8 1.291 1.241 1.503 1.510 1.417 121.53 116.00 120.70 109.95 110.53 110.51 123.30 +** * ** +** 9 PHE 9 1.298 1.237 1.532 1.546 1.441 121.50 116.40 120.32 111.94 109.36 108.20 123.27 ** * ** 10 MET 10 1.323 1.235 1.511 1.541 1.458 123.00 116.36 120.24 105.75 110.46 111.46 123.37 ** ** 11 LYS 11 1.301 1.242 1.511 1.554 1.439 122.38 119.82 118.73 110.85 106.54 113.76 121.40 +* * * +* * +* +* +* Residue-by-residue listing for refined_10 Page 6 ---------------------------------------- ................................................................................................................................... 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 PRO 12 1.332 1.235 1.523 1.545 1.448 120.55 117.39 120.37 110.24 108.14 104.07 122.23 * * * 13 PHE 13 1.299 1.227 1.514 1.534 1.434 119.63 117.65 119.90 113.56 107.56 111.03 122.46 ** * * +* * ** 14 ILE 14 1.324 1.227 1.506 1.556 1.439 119.90 116.04 120.47 111.46 111.20 110.80 123.47 * * * 15 SER 15 1.321 1.225 1.520 1.538 1.455 122.89 116.03 120.44 111.44 111.56 110.63 123.43 16 GLU 16 1.317 1.223 1.523 1.534 1.456 122.87 116.53 120.82 109.68 110.45 110.55 122.63 17 LYS 17 1.328 1.233 1.518 1.543 1.446 120.10 115.37 121.13 112.50 111.13 112.13 123.43 * * 18 SER 18 1.315 1.221 1.520 1.540 1.441 123.39 117.12 119.84 111.30 111.91 109.52 122.96 19 SER 19 1.344 1.233 1.537 1.530 1.474 121.08 117.96 120.14 110.17 113.67 111.62 121.90 * * 20 LYS 20 1.318 1.236 1.527 1.537 1.436 118.82 117.56 120.33 111.16 112.07 110.70 122.10 * +* +* 21 SER 21 1.320 1.232 1.516 1.539 1.452 121.10 116.66 120.58 109.66 110.99 110.07 122.76 22 LEU 22 1.317 1.244 1.515 1.563 1.435 120.03 115.36 120.78 112.04 106.84 111.60 123.80 +* * * +* +* 23 GLU 23 1.313 1.235 1.509 1.521 1.436 122.58 116.86 120.14 108.59 110.12 110.42 123.00 * * * 24 ILE 24 1.307 1.244 1.531 1.551 1.442 121.04 116.90 120.43 110.41 110.59 112.00 122.64 +* +* 25 PRO 25 1.356 1.237 1.530 1.530 1.465 123.24 115.91 120.81 109.95 112.16 103.65 123.25 26 LEU 26 1.321 1.239 1.532 1.551 1.469 123.40 116.81 120.38 110.19 113.10 112.03 122.80 * * 27 GLY 27 1.318 1.228 1.511 - 1.454 120.97 116.08 121.00 - 112.62 - 122.89 28 PHE 28 1.316 1.215 1.530 1.541 1.450 121.41 115.65 121.35 112.02 108.45 109.61 122.98 * * 29 ASN 29 1.327 1.237 1.526 1.544 1.467 123.21 115.92 121.02 110.18 110.44 110.17 123.01 30 GLU 30 1.332 1.234 1.513 1.533 1.475 122.32 115.07 121.46 109.17 111.00 110.90 123.47 31 TYR 31 1.296 1.240 1.541 1.533 1.434 123.06 116.51 120.99 112.63 110.28 108.83 122.48 ** * * ** 32 PHE 32 1.327 1.235 1.525 1.531 1.451 121.22 117.52 120.01 110.36 110.11 112.08 122.47 33 PRO 33 1.346 1.227 1.515 1.533 1.475 123.61 114.73 121.09 108.98 113.61 103.44 124.18 * +* +* 34 ALA 34 1.310 1.234 1.531 1.518 1.465 124.16 117.52 120.22 109.65 112.59 109.75 122.25 * * * 35 PRO 35 1.354 1.231 1.523 1.536 1.462 122.42 116.27 121.01 110.40 110.42 104.16 122.71 * * 36 PHE 36 1.320 1.243 1.526 1.535 1.434 121.05 116.23 121.31 111.54 109.57 112.28 122.36 * * * 37 PRO 37 1.326 1.241 1.529 1.527 1.454 123.61 116.52 120.76 110.18 111.73 102.55 122.69 38 ILE 38 1.311 1.233 1.538 1.564 1.440 121.43 117.36 120.48 111.19 109.71 112.47 122.09 * * 39 THR 39 1.318 1.235 1.517 1.553 1.449 121.06 115.30 121.17 109.65 112.00 111.98 123.53 40 VAL 40 1.309 1.234 1.520 1.565 1.444 124.15 117.85 120.21 109.95 107.96 112.16 121.94 * * * * 41 ASP 41 1.294 1.234 1.499 1.535 1.449 119.94 115.07 120.92 111.01 111.97 112.40 124.01 +** * * +** 42 LEU 42 1.313 1.233 1.508 1.553 1.447 123.54 115.77 120.90 109.20 109.03 110.86 123.32 * * * * 43 LEU 43 1.294 1.190 1.502 1.547 1.438 122.19 116.51 120.12 109.41 109.23 112.02 123.35 ** ** * * ** 44 ASP 44 1.283 1.241 1.505 1.553 1.458 123.95 114.44 121.10 110.22 110.75 110.99 124.46 *** * * *** Residue-by-residue listing for refined_10 Page 7 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 45 TYR 45 1.306 1.232 1.551 1.543 1.448 125.56 117.29 120.42 111.23 112.23 107.60 122.26 +* * ** +* ** 46 SER 46 1.329 1.239 1.557 1.522 1.447 121.16 117.71 120.29 110.95 112.80 109.64 121.99 +* +* 47 GLY 47 1.337 1.240 1.527 - 1.471 119.77 117.28 120.34 - 115.21 - 122.38 * * 48 ARG 48 1.308 1.225 1.536 1.538 1.467 121.57 118.01 119.72 111.07 108.44 108.83 122.24 +* +* 49 SER 49 1.315 1.234 1.542 1.540 1.457 120.67 115.09 121.57 111.66 113.15 110.70 123.32 * * 50 TRP 50 1.316 1.241 1.530 1.523 1.433 124.97 117.44 120.26 108.45 108.68 107.97 122.28 * +* * +* 51 THR 51 1.302 1.234 1.525 1.544 1.445 120.98 116.14 120.87 110.50 107.82 111.34 122.99 +* * +* 52 VAL 52 1.303 1.224 1.524 1.564 1.437 121.89 116.26 120.97 110.68 110.77 110.37 122.77 +* * +* 53 ARG 53 1.300 1.245 1.515 1.533 1.424 122.31 114.90 121.29 110.52 109.57 111.10 123.80 ** +* ** 54 MET 54 1.297 1.220 1.511 1.542 1.436 123.51 116.48 120.53 110.80 107.49 108.87 122.97 ** * * * ** 55 LYS 55 1.300 1.235 1.499 1.512 1.439 121.91 117.01 120.05 107.61 110.86 109.39 122.93 ** * * * ** 56 LYS 56 1.314 1.232 1.498 1.514 1.418 120.10 115.80 120.66 107.69 109.87 114.29 123.52 * * ** * ** ** 57 ARG 57 1.288 1.231 1.500 1.544 1.438 122.61 116.39 120.55 111.17 108.58 113.51 123.01 +** * * +* +** 58 GLY 58 1.287 1.232 1.490 - 1.419 119.83 115.58 120.94 - 112.01 - 123.47 *** * +* *** 59 GLU 59 1.290 1.227 1.523 1.554 1.438 122.85 116.33 120.96 110.39 110.92 110.52 122.67 +** * * +** 60 LYS 60 1.312 1.230 1.494 1.529 1.450 121.01 116.71 120.41 110.10 108.63 110.97 122.88 * * * 61 VAL 61 1.296 1.244 1.527 1.540 1.430 120.49 116.03 121.04 111.89 111.44 110.00 122.90 ** * * ** 62 PHE 62 1.314 1.245 1.527 1.539 1.452 121.72 116.40 120.51 106.72 111.52 110.47 123.08 * +* +* 63 LEU 63 1.324 1.227 1.509 1.534 1.457 121.32 116.17 120.33 109.57 106.21 112.20 123.49 +* +* 64 THR 64 1.301 1.242 1.536 1.541 1.444 121.72 115.73 121.29 110.57 114.06 109.23 122.98 +* * * +* 65 VAL 65 1.304 1.223 1.508 1.557 1.446 122.71 116.93 120.23 110.46 108.53 110.61 122.75 +* +* 66 GLY 66 1.303 1.223 1.494 - 1.432 120.55 116.34 120.86 - 111.43 - 122.81 +* * * +* 67 TRP 67 1.329 1.224 1.496 1.539 1.441 120.99 115.72 121.46 109.63 107.92 112.48 122.76 * * * * 68 GLU 68 1.311 1.208 1.548 1.532 1.422 119.06 116.09 120.95 113.98 108.45 111.43 122.82 * * * +* * ** ** 69 ASN 69 1.343 1.209 1.495 1.553 1.488 123.35 114.58 121.36 108.54 109.32 111.41 124.04 * * * +* +* 70 PHE 70 1.294 1.230 1.535 1.560 1.434 124.83 115.71 121.14 111.10 108.22 106.97 123.05 ** * * +* * ** ** 71 VAL 71 1.329 1.223 1.518 1.569 1.459 122.31 115.85 121.38 110.18 110.94 111.78 122.78 * * Residue-by-residue listing for refined_10 Page 8 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 72 LYS 72 1.296 1.236 1.524 1.535 1.434 121.79 116.72 120.51 110.66 110.07 109.69 122.74 ** * ** 73 ASP 73 1.333 1.221 1.535 1.523 1.469 119.70 118.52 119.93 110.86 114.16 109.88 121.51 * * * * 74 ASN 74 1.322 1.250 1.518 1.526 1.470 118.97 115.32 121.09 112.09 112.70 113.37 123.59 +* * +* +* 75 ASN 75 1.329 1.231 1.532 1.526 1.486 124.87 115.58 120.85 111.81 113.05 111.07 123.58 * +* +* 76 LEU 76 1.303 1.244 1.512 1.505 1.493 123.21 118.40 119.90 108.59 117.91 114.59 121.65 +* * +* * ** ** ** 77 GLU 77 1.276 1.247 1.489 1.521 1.430 117.57 114.80 120.75 112.10 109.71 113.80 124.43 +*** +* * ** * +* +*** 78 ASP 78 1.304 1.240 1.508 1.534 1.445 122.84 114.28 121.60 112.74 112.11 111.99 124.05 +* * +* 79 GLY 79 1.306 1.232 1.495 - 1.428 123.03 115.35 121.16 - 108.75 - 123.48 +* * * * * +* 80 LYS 80 1.327 1.241 1.516 1.549 1.445 121.57 117.54 119.99 111.35 107.92 111.79 122.47 * * 81 TYR 81 1.305 1.234 1.490 1.535 1.441 119.92 115.99 120.50 110.70 109.83 111.27 123.51 +* +* +* 82 LEU 82 1.298 1.238 1.520 1.583 1.422 121.68 115.46 121.01 113.22 112.54 113.16 123.46 ** +** +* +* +* +** 83 GLN 83 1.309 1.227 1.489 1.528 1.447 122.58 116.79 120.04 106.97 109.12 112.13 123.17 * +* +* +* 84 PHE 84 1.289 1.239 1.493 1.535 1.431 120.43 115.92 120.51 109.82 108.44 112.71 123.54 +** +* * * +** 85 ILE 85 1.300 1.248 1.507 1.550 1.425 121.67 116.30 120.52 108.04 106.78 111.71 123.18 ** +* +* ** 86 TYR 86 1.293 1.235 1.523 1.545 1.428 121.38 115.38 121.47 111.18 111.93 109.48 123.15 +** +* +** 87 ASP 87 1.305 1.210 1.533 1.550 1.443 122.58 119.89 119.29 111.37 104.51 109.80 120.81 +* * +* ** * ** 88 ARG 88 1.288 1.232 1.528 1.552 1.457 119.96 115.10 121.43 112.59 111.02 112.42 123.32 +** * * * +** 89 ASP 89 1.324 1.239 1.547 1.558 1.424 123.99 117.56 120.27 111.84 106.58 107.93 122.15 * * +* * +* +* +* 90 ARG 90 1.286 1.233 1.521 1.530 1.464 123.11 115.69 121.25 110.03 110.24 109.66 123.04 *** *** 91 THR 91 1.306 1.234 1.529 1.541 1.435 121.65 116.79 120.52 109.13 109.21 109.89 122.66 +* * +* 92 PHE 92 1.307 1.228 1.508 1.528 1.437 121.92 116.23 120.91 109.95 109.57 110.64 122.85 +* * +* 93 TYR 93 1.291 1.230 1.520 1.536 1.438 121.69 117.29 120.10 111.85 107.34 108.42 122.57 +** * * * +** 94 VAL 94 1.303 1.235 1.519 1.577 1.436 120.85 115.85 121.42 111.23 110.43 112.43 122.67 +* * * +* 95 ILE 95 1.298 1.235 1.516 1.553 1.429 121.10 115.56 120.74 110.45 108.62 111.99 123.68 ** +* ** 96 ILE 96 1.303 1.235 1.516 1.563 1.445 122.93 116.22 120.46 107.65 109.77 110.44 123.29 +* +* 97 TYR 97 1.300 1.241 1.499 1.531 1.434 121.59 115.60 120.64 110.29 107.12 111.70 123.74 ** * * * ** 98 GLY 98 1.296 1.235 1.502 - 1.423 121.49 116.97 120.33 - 109.67 - 122.70 ** +* ** Residue-by-residue listing for refined_10 Page 9 ---------------------------------------- ................................................................................................................................... Residue ------------- <---------- Bond lengths ----------> <---------------------- Bond angles ----------------------> No. Type Seq Max Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev ----------------------------------------------------------------------------------------------------------------------------------- 99 HIS 99 1.293 1.238 1.513 1.543 1.442 121.15 116.39 120.50 110.75 109.54 109.79 123.07 +** +** 100 ASN 100 1.305 1.236 1.503 1.544 1.437 121.08 117.76 119.72 108.87 107.04 112.25 122.47 +* * * * * +* 101 MET 101 1.313 1.224 1.512 1.540 1.449 119.96 115.29 121.48 111.20 109.65 112.72 123.12 * * * 102 CYS 102 1.294 - 1.513 1.529 1.422 121.95 - - 110.80 108.81 109.53 - ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: +*** ** +* +** ** ** +* * ** ** ** +* +*** ----------------------------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 10 ---------------------------------------- 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 96 1.276 1.344 1.308 .014 +*** * * C-N (Pro) 1.341 .016 5 1.326 1.356 1.343 .012 C-O C-O 1.231 .020 101 1.190 1.250 1.233 .009 ** CA-C CH1E-C (except Gly) 1.525 .021 95 1.489 1.557 1.518 .014 +* +* CH2G*-C (Gly) 1.516 .018 7 1.490 1.527 1.503 .012 * CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.518 1.524 1.521 .003 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.540 1.577 1.556 .010 * CH1E-CH2E (the rest) 1.530 .020 75 1.505 1.583 1.538 .012 * +** N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.417 1.493 1.445 .015 ** +* NH1-CH2G* (Gly) 1.451 .016 7 1.419 1.471 1.436 .018 +* * N-CH1E (Pro) 1.466 .015 5 1.448 1.475 1.461 .009 * ------------------------------------------------------------------------------------------------------------- Residue-by-residue listing for refined_10 Page 11 ---------------------------------------- +-----------------+ | 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 89 114.28 119.89 116.36 1.07 +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 115.35 117.28 116.17 .69 CH1E-C-N (Pro) 116.9 1.5 5 114.73 117.39 116.17 .87 * O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.81 124.46 122.96 .63 * O-C-N (Pro) 122.0 1.4 5 122.23 124.18 123.01 .67 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 117.57 125.56 121.83 1.50 ** ** C-NH1-CH2G* (Gly) 120.6 1.7 7 119.77 123.03 121.05 1.07 * C-N-CH1E (Pro) 122.6 5.0 5 120.55 123.61 122.69 1.15 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.73 121.60 120.67 .54 * CH2G*-C-O (Gly) 120.8 2.1 7 120.33 121.16 120.76 .30 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 109.65 111.49 110.57 .92 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.65 111.89 110.14 1.10 * CH2E-CH1E-C (the rest) 110.1 1.9 75 105.75 113.98 110.56 1.53 ** ** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.51 117.91 110.00 2.12 ** ** NH1-CH2G*-C (Gly) 112.5 2.9 7 108.75 115.21 111.71 1.95 * N-CH1E-C (Pro) 111.8 2.5 5 108.14 113.61 111.21 1.84 * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.75 111.80 110.78 1.02 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 109.23 112.94 111.37 1.05 * N-CH1E-CH2E (Pro) 103.0 1.1 5 102.55 104.16 103.58 .58 * NH1-CH1E-CH2E (the rest) 110.5 1.7 70 106.97 114.59 110.94 1.62 ** ** ------------------------------------------------------------------------------------------------------------- The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber. Residue-by-residue listing for refined_10 Page 12 ---------------------------------------- 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] 74 84.1% Residues in additional allowed regions [a,b,l,p] 12 13.6% Residues in generously allowed regions [~a,~b,~l,~p] 1 1.1% Residues in disallowed regions [XX] 1 1.1% ---- ------ Number of non-glycine and non-proline residues 88 100.0% Number of end-residues (excl. Gly and Pro) 2 Number of glycine residues 7 Number of proline residues 5 ---- Total number of residues 102 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 88 84.1 83.8 10.0 .0 Inside b. Omega angle st dev 101 4.1 6.0 3.0 -.6 Inside c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside d. Zeta angle st dev 95 1.9 3.1 1.6 -.8 Inside e. H-bond energy st dev 57 .9 .8 .2 .7 Inside f. Overall G-factor 102 -.1 -.4 .3 1.1 BETTER S T E R E O C H E M I S T R Y O F S I D E - C H A I N Comparison values No. of No. of Parameter Typical Band band widths Stereochemical parameter data pts value value width from mean ------------------------ -------- ----- ----- ----- --------- a. Chi-1 gauche minus st dev 14 7.9 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 33 6.5 19.0 5.3 -2.4 BETTER c. Chi-1 gauche plus st dev 41 6.5 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 88 7.8 18.2 4.8 -2.1 BETTER e. Chi-2 trans st dev 24 6.8 20.4 5.0 -2.7 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% 84.1 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.2 1 H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .95 3 Residue-by-residue listing for refined_10 Page 13 ---------------------------------------- G - F A C T O R S Average Parameter Score Score --------- ----- ----- Dihedral angles:- Phi-psi distribution -.51 Chi1-chi2 distribution -.25 Chi1 only -.02 Chi3 & chi4 .34 Omega -.09 ------ -.20 ===== Main-chain covalent forces:- Main-chain bond lengths -.07 Main-chain bond angles .36 ------ .18 ===== OVERALL AVERAGE -.07 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.