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 - - 183.0 - - - - - - - - 182.5 - 34.3 - 2 ALA 2 A - - - - - - - - - - 178.3 - 33.2 - 3 ASP 3 S B - 185.6 - - - - - - - - 179.0 - 35.2 - 4 THR 4 S A - - -55.0 - - - - - - - 181.0 - 33.8 - 5 GLY 5 - - - - - - - - - - - 182.4 - - - 6 GLU 6 B - 181.8 - 188.0 - - - - - - 175.6 - 35.5 - 7 VAL 7 E B - - -64.5 - - - - - - - 178.0 -1.2 32.7 - * * 8 GLN 8 E B 57.3 - - 181.9 - - - - - - 179.6 - 33.8 - 9 PHE 9 E B 62.2 - - - - - - - - - 176.6 -2.7 33.8 - 10 MET 10 E B 62.2 - - 175.8 - - - - - - 181.1 - 34.0 - 11 LYS 11 E B 78.1 - - 178.4 - - - - - - 178.0 -1.2 34.9 - * * 12 PRO 12 - - - - - -60.7 - - - - - 175.0 - 37.8 - * * 13 PHE 13 B - 177.8 - - - - - - - - 175.7 - 36.6 - 14 ILE 14 t B - 178.2 - - - - - - - - 183.1 - 33.3 - 15 SER 15 T A - - -53.7 - - - - - - - 181.6 - 34.4 - 16 GLU 16 T A - 188.5 - 178.5 - - - - - - 179.6 - 34.3 - 17 LYS 17 T A - - -73.0 - - - - - - - 183.9 - 31.6 - 18 SER 18 T a - - -55.5 - - - - - - - 171.7 -2.7 33.3 - * * 19 SER 19 T A - 182.0 - - - - - - - - 179.1 - 35.6 - 20 LYS 20 T a 69.6 - - - - - - - - - 184.8 -2.1 32.7 - 21 SER 21 t B 52.0 - - - - - - - - - 171.6 -2.5 36.6 - * * 22 LEU 22 E B - - -76.9 178.8 - - - - - - 182.9 -2.6 30.9 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 23 GLU 23 E B - 207.0 - - - - - - - - 183.9 -.6 37.9 - * +* * +* 24 ILE 24 E B - - -63.2 179.7 - - - - - - 180.4 -1.7 33.4 - 25 PRO 25 h - - - - - -61.4 - - - - - 179.8 - 38.9 - * * 26 LEU 26 H A - 174.6 - - - -53.7 -39.2 - - - 182.1 - 34.0 - 27 GLY 27 H - - - - - - -57.5 -36.9 - - - 179.8 - - - 28 PHE 28 H A - 187.0 - - - -88.5 -29.2 - - - 175.1 -1.0 32.6 - +* * +* 29 ASN 29 H A - 178.0 - - - -61.1 -45.6 - - - 180.5 -2.0 35.7 - 30 GLU 30 h A - 179.6 - 183.6 - - - - - - 181.6 -3.4 36.2 - +* +* 31 TYR 31 T A - 172.4 - - - - - - - - 177.6 - 33.5 - 32 PHE 32 t b 67.1 - - - - - - - - - 175.2 -.9 30.9 - * * 33 PRO 33 - - - - - -86.6 - - - - - 182.5 - 38.8 - +* * +* 34 ALA 34 B - - - - - - - - - - 170.1 - 35.5 - +* +* 35 PRO 35 S - - - - - -55.3 - - - - - 188.7 - 39.3 - +* +* +* 36 PHE 36 B 61.3 - - - - - - - - - 172.6 - 32.0 - * * 37 PRO 37 - - - - - -84.9 - - - - - 180.8 - 39.0 - +* * +* 38 ILE 38 e A - - -70.3 - - - - - - - 185.3 - 31.5 - 39 THR 39 E B - - -42.0 - - - - - - - 178.9 - 35.6 - +* +* 40 VAL 40 E B - - -64.2 - - - - - - - 183.9 -3.2 33.1 - +* +* 41 ASP 41 E B - - -67.9 - - - - - - - 175.5 -2.5 32.7 - 42 LEU 42 E B - - -57.0 177.6 - - - - - - 183.7 -2.9 36.2 - * * 43 LEU 43 E B - - -60.0 - - - - - - - 178.9 -3.8 33.9 - ** ** 44 ASP 44 e B - 177.1 - - - - - - - - 182.7 -2.5 34.8 - 45 TYR 45 T A - - -65.4 - - - - - - - 179.5 - 33.8 - 46 SER 46 T A - - -55.0 - - - - - - - 179.4 - 34.3 - 47 GLY 47 t - - - - - - - - - - - 179.3 -1.0 - - * * 48 ARG 48 e B - - -62.6 - - - - - - - 180.5 - 33.9 - 49 SER 49 E B 53.8 - - - - - - - - - 181.6 - 33.9 - 50 TRP 50 E B - - -53.3 - - - - - - - 177.4 -2.9 35.0 - * * 51 THR 51 E B - - -55.5 - - - - - - - 187.4 - 34.6 - * * 52 VAL 52 E B 60.6 - - - - - - - - - 180.1 -2.6 33.4 - 53 ARG 53 E B - - -66.9 182.1 - - - - - - 187.2 -2.5 32.6 - * * 54 MET 54 E B - 176.4 - 182.0 - - - - - - 175.4 -1.5 36.7 - 55 LYS 55 E B - - -65.5 - - - - - - - 169.6 -2.1 33.8 - +* +* 56 LYS 56 E B - - -63.0 - - - - - - - 183.6 - 37.2 - 57 ARG 57 E b - 188.5 - 181.1 - - - - - - 176.6 -3.0 33.6 - * * 58 GLY 58 T - - - - - - - - - - - 184.9 - - - 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 ----------------------------------------------------------------------------------------------------------------------------------- 59 GLU 59 T A - - -60.5 176.9 - - - - - - 187.7 -.6 36.2 - * +* +* 60 LYS 60 E B - - -68.9 184.2 - - - - - - 174.5 -2.1 33.3 - 61 VAL 61 E B - 180.8 - - - - - - - - 178.2 -1.2 35.9 - * * 62 PHE 62 E B - - -58.2 - - - - - - - 175.5 -2.5 34.6 - 63 LEU 63 E B - - -60.7 178.3 - - - - - - 188.6 -2.2 33.4 - * * 64 THR 64 e ~b 55.2 - - - - - - - - - 184.0 -2.7 33.0 - ** ** 65 VAL 65 T B 61.3 - - - - - - - - - 187.9 - 32.4 - * * 66 GLY 66 h - - - - - - - - - - - 175.5 - - - 67 TRP 67 H A - 173.9 - - - -68.0 -28.0 - - - 180.2 -2.0 34.4 - * * 68 GLU 68 H A 45.0 - - - - -68.1 -26.4 - - - 174.0 -.5 27.9 - * * * +* +* +* 69 ASN 69 H A - - -66.2 - - -72.2 -32.8 - - - 180.2 -.5 34.0 - +* +* 70 PHE 70 H A - 174.3 - - - -70.7 -51.7 - - - 183.1 -1.0 34.5 - * * * 71 VAL 71 H A 69.9 - - - - -59.6 -39.5 - - - 175.0 -2.9 32.8 - * * 72 LYS 72 H A - - -60.3 - - -72.6 -48.0 - - - 185.1 -1.5 31.5 - 73 ASP 73 H A - 173.9 - - - -70.5 -39.7 - - - 181.0 -3.0 32.3 - * * 74 ASN 74 h A - 195.2 - - - - - - - - 180.7 -3.4 34.2 - +* +* 75 ASN 75 T l - 182.5 - - - - - - - - 181.8 -.8 31.1 - +* +* 76 LEU 76 t B - - -62.1 178.0 - - - - - - 179.7 -1.0 33.5 - * * 77 GLU 77 t B 56.3 - - 184.0 - - - - - - 178.8 - 34.9 - 78 ASP 78 T B 67.4 - - - - - - - - - 183.2 - 32.5 - 79 GLY 79 T - - - - - - - - - - - 175.8 - - - 80 LYS 80 t B - - -55.5 182.0 - - - - - - 189.1 -1.4 34.0 - +* +* 81 TYR 81 E B - - -63.3 - - - - - - - 182.4 -.6 31.8 - +* +* 82 LEU 82 E B - - -57.6 - - - - - - - 169.9 -.9 36.8 - +* +* +* 83 GLN 83 E B 65.5 - - 175.3 - - - - - - 181.4 -2.9 32.4 - * * 84 PHE 84 E B - - -61.8 - - - - - - - 174.9 -3.5 34.7 - +* +* 85 ILE 85 E B - - -56.5 178.0 - - - - - - 185.0 -3.1 34.8 - * * 86 TYR 86 E B - 180.1 - - - - - - - - 177.7 -2.8 34.2 - * * 87 ASP 87 e b - 193.7 - - - - - - - - 177.8 -1.8 35.8 - 88 ARG 88 S A - - -59.0 - - - - - - - 174.8 - 31.2 - 89 ASP 89 S b - - -72.7 - - - - - - - 189.6 - 32.6 - +* +* 90 ARG 90 e a - - -57.5 177.8 - - - - - - 178.3 - 35.7 - 91 THR 91 E B 50.9 - - - - - - - - - 178.2 - 33.4 - 92 PHE 92 E B - - -62.8 - - - - - - - 178.9 -2.7 35.8 - 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 ----------------------------------------------------------------------------------------------------------------------------------- 93 TYR 93 E B - - -47.2 - - - - - - - 188.2 -3.0 34.6 - * * * * 94 VAL 94 E B 58.8 - - - - - - - - - 172.7 -2.2 32.5 - * * 95 ILE 95 E B - - -64.5 - - - - - - - 181.2 -2.8 33.6 - 96 ILE 96 E B 62.8 - - 179.4 - - - - - - 174.6 -.5 35.7 - ** ** 97 TYR 97 E B - - -64.0 - - - - - - - 177.3 -3.1 34.7 - * * 98 GLY 98 - - - - - - - - - - - 183.5 -.7 - - +* +* 99 HIS 99 B - 191.0 - - - - - - - - 179.5 -2.4 34.0 - 100 ASN 100 S ~a - 182.2 - - - - - - - - 173.4 -.9 35.1 - ** * +* ** 101 MET 101 a 59.7 - - 171.7 - - - - - - 177.7 - 31.6 - 102 CYS 102 - - - -61.4 - - - - - - - - - 34.4 - ----------------------------------------------------------------------------------------------------------------------------------- Max deviations: ** * * +* +* +* * +* ** +* ** ----------------------------------------------------------------------------------------------------------------------------------- Mean values: 60.8 182.5 -61.2 179.7 -69.8 -67.5 -37.9 - - - 179.8 -2.0 34.2 Standard deviations: 7.5 8.0 6.7 3.5 14.8 9.5 8.3 - - - 4.5 .9 1.9 Numbers of values: 21 26 41 23 5 11 11 0 0 0 101 58 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 - 1.229 1.530 1.546 1.465 - 116.35 120.93 111.27 109.07 109.88 122.69 2 ALA 2 1.334 1.226 1.522 1.521 1.472 122.30 115.90 121.07 110.86 112.28 110.50 123.03 3 ASP 3 1.294 1.226 1.524 1.542 1.450 122.10 118.93 119.31 110.82 107.24 109.63 121.76 +** * * +** 4 THR 4 1.314 1.240 1.545 1.546 1.448 120.27 116.16 121.08 110.05 110.41 111.46 122.75 * * 5 GLY 5 1.311 1.238 1.492 - 1.438 121.12 115.12 121.06 - 110.85 - 123.82 * * * 6 GLU 6 1.292 1.243 1.524 1.524 1.448 123.19 116.60 120.63 108.58 111.06 110.04 122.77 +** +** 7 VAL 7 1.309 1.229 1.524 1.566 1.441 121.57 116.45 120.93 110.59 109.57 113.12 122.54 * * 8 GLN 8 1.296 1.231 1.508 1.522 1.414 122.58 117.30 119.88 111.55 109.09 110.44 122.82 ** ** ** 9 PHE 9 1.304 1.227 1.513 1.547 1.442 120.99 116.04 120.70 110.49 110.77 111.00 123.26 +* +* 10 MET 10 1.299 1.240 1.505 1.545 1.443 122.31 117.27 120.15 110.07 107.96 112.15 122.57 ** * ** 11 LYS 11 1.304 1.240 1.532 1.539 1.435 120.31 118.19 119.69 110.05 109.04 110.31 122.09 +* * +* 12 PRO 12 1.345 1.258 1.545 1.537 1.463 122.86 114.29 121.94 110.27 114.47 104.31 123.73 * +* * * * +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 13 PHE 13 1.318 1.237 1.529 1.554 1.444 124.42 117.85 119.99 109.67 107.00 108.70 122.14 * +* +* * +* 14 ILE 14 1.307 1.213 1.527 1.569 1.445 120.26 117.38 120.08 111.31 108.90 111.70 122.54 +* * * +* 15 SER 15 1.324 1.215 1.538 1.535 1.467 122.19 116.06 121.18 110.39 111.32 109.75 122.73 16 GLU 16 1.315 1.232 1.543 1.516 1.437 122.23 117.91 120.37 110.89 111.47 109.23 121.72 * * 17 LYS 17 1.340 1.229 1.492 1.534 1.477 118.93 116.02 120.81 109.18 112.11 114.68 123.07 +* +* ** ** 18 SER 18 1.309 1.215 1.520 1.513 1.437 122.16 115.35 120.96 112.33 111.30 109.42 123.69 * * * * 19 SER 19 1.318 1.237 1.534 1.541 1.421 123.00 116.58 120.93 110.53 107.75 109.18 122.49 +* * +* 20 LYS 20 1.349 1.226 1.523 1.541 1.438 119.54 116.94 120.32 110.10 112.86 112.12 122.74 * * * * 21 SER 21 1.308 1.233 1.537 1.529 1.438 120.99 116.76 121.13 109.13 112.76 107.63 122.11 * * +* +* 22 LEU 22 1.313 1.236 1.480 1.531 1.450 120.50 114.27 121.32 110.36 110.13 115.42 124.41 * ** +** +** 23 GLU 23 1.281 1.239 1.548 1.539 1.419 123.30 117.69 120.12 110.88 105.87 105.63 122.11 *** * ** +* +** *** 24 ILE 24 1.312 1.221 1.535 1.553 1.462 121.20 117.37 120.24 110.23 112.00 111.25 122.40 * * 25 PRO 25 1.359 1.249 1.540 1.535 1.474 123.49 114.81 121.51 109.30 114.16 103.76 123.65 * * * * 26 LEU 26 1.333 1.214 1.521 1.541 1.463 124.18 117.11 119.91 110.01 112.36 110.45 122.96 * * 27 GLY 27 1.322 1.234 1.523 - 1.454 121.07 116.94 120.31 - 113.72 - 122.72 28 PHE 28 1.324 1.223 1.531 1.535 1.451 120.58 116.12 120.99 112.15 109.77 111.17 122.87 * * 29 ASN 29 1.326 1.236 1.523 1.536 1.471 122.02 114.25 121.69 108.66 109.11 110.27 124.03 30 GLU 30 1.313 1.235 1.527 1.522 1.445 124.89 116.08 120.92 110.03 110.78 107.74 122.98 * +* +* +* 31 TYR 31 1.322 1.230 1.526 1.545 1.447 121.95 117.09 120.42 111.33 111.24 110.39 122.45 32 PHE 32 1.316 1.240 1.538 1.568 1.442 120.03 117.57 121.75 112.83 111.70 112.41 120.41 +* * * +* +* 33 PRO 33 1.335 1.246 1.510 1.517 1.434 121.93 114.04 121.80 109.92 111.53 103.98 124.15 ** +* +* ** 34 ALA 34 1.275 1.248 1.505 1.532 1.432 124.28 119.36 118.30 110.34 107.14 109.79 122.32 +*** * * +* * * +*** 35 PRO 35 1.354 1.243 1.522 1.529 1.462 121.55 117.76 119.73 110.10 107.58 103.52 122.51 +* +* 36 PHE 36 1.308 1.237 1.529 1.533 1.413 120.87 116.18 121.28 111.88 113.87 110.94 122.46 +* ** ** 37 PRO 37 1.338 1.231 1.524 1.528 1.444 123.03 117.82 120.07 110.75 108.78 103.28 122.06 * * * 38 ILE 38 1.298 1.230 1.531 1.582 1.443 120.13 117.51 120.44 111.42 111.88 113.08 122.01 ** +* * ** 39 THR 39 1.311 1.234 1.541 1.537 1.443 119.67 115.65 120.61 109.32 110.71 109.46 123.74 * * * * 40 VAL 40 1.316 1.229 1.534 1.575 1.473 125.50 118.58 119.74 109.87 107.84 113.60 121.67 * ** * * * ** 41 ASP 41 1.314 1.236 1.507 1.539 1.469 119.81 114.78 121.50 109.51 113.55 112.36 123.72 * * * * 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 ----------------------------------------------------------------------------------------------------------------------------------- 42 LEU 42 1.313 1.235 1.519 1.537 1.442 123.78 116.79 120.44 108.72 106.65 110.27 122.75 * * +* +* 43 LEU 43 1.300 1.242 1.511 1.553 1.440 121.73 115.38 121.04 109.65 110.78 111.83 123.58 ** * ** 44 ASP 44 1.302 1.244 1.526 1.522 1.440 122.88 116.10 120.60 110.47 109.89 109.53 123.29 +* +* 45 TYR 45 1.317 1.224 1.529 1.524 1.462 123.17 117.67 120.17 109.31 113.12 110.95 122.16 46 SER 46 1.315 1.233 1.528 1.526 1.452 120.82 116.03 121.26 110.71 110.36 109.92 122.71 * * 47 GLY 47 1.321 1.237 1.497 - 1.441 120.79 115.85 120.89 - 111.59 - 123.26 * * 48 ARG 48 1.316 1.238 1.513 1.531 1.432 121.49 115.91 120.98 110.09 109.39 111.58 123.10 * * 49 SER 49 1.281 1.247 1.510 1.533 1.421 122.10 116.29 120.68 111.95 109.34 109.92 122.99 *** +* *** 50 TRP 50 1.306 1.229 1.504 1.535 1.437 121.35 115.98 120.86 109.65 109.46 110.57 123.13 +* * * +* 51 THR 51 1.287 1.238 1.537 1.534 1.421 121.95 115.91 121.10 112.12 108.16 108.90 122.98 *** +* * * +* *** 52 VAL 52 1.312 1.223 1.522 1.574 1.444 122.17 116.14 121.24 111.60 111.38 110.58 122.61 * * * * 53 ARG 53 1.296 1.241 1.506 1.519 1.430 121.49 114.52 121.42 111.99 110.79 111.01 124.04 ** * ** 54 MET 54 1.302 1.222 1.506 1.539 1.444 124.16 116.70 120.56 109.02 110.17 108.42 122.66 +* * * +* 55 LYS 55 1.310 1.230 1.522 1.551 1.432 121.17 116.13 120.53 108.58 110.94 112.86 123.32 * * * * * 56 LYS 56 1.312 1.234 1.493 1.520 1.448 122.37 117.47 119.73 106.69 104.02 111.05 122.77 * +* +* +** +** 57 ARG 57 1.268 1.236 1.509 1.537 1.434 119.78 115.08 120.97 110.80 111.10 110.90 123.92 **** * * **** 58 GLY 58 1.308 1.243 1.498 - 1.430 122.09 115.12 121.34 - 114.82 - 123.53 +* * * +* 59 GLU 59 1.300 1.226 1.496 1.520 1.429 122.30 117.88 120.08 107.50 111.46 110.26 122.02 ** * +* * ** 60 LYS 60 1.305 1.242 1.516 1.513 1.429 118.85 113.73 122.13 110.23 115.45 110.08 124.11 +* +* +* * +* +* 61 VAL 61 1.321 1.232 1.495 1.560 1.436 123.85 117.35 120.16 107.01 106.28 112.96 122.48 * * * +* +* 62 PHE 62 1.280 1.241 1.490 1.532 1.415 119.08 116.18 120.68 110.65 108.94 110.49 123.12 *** +* ** * *** 63 LEU 63 1.298 1.211 1.481 1.531 1.442 120.35 115.83 120.47 111.16 106.75 112.29 123.68 ** * ** +* * ** 64 THR 64 1.283 1.237 1.544 1.543 1.436 121.58 115.51 121.09 111.48 113.96 109.87 123.39 *** * * *** 65 VAL 65 1.324 1.239 1.529 1.563 1.451 123.63 115.84 120.82 112.11 110.67 111.43 123.32 * * * 66 GLY 66 1.310 1.234 1.484 - 1.417 121.54 114.97 121.36 - 108.91 - 123.64 * +* ** * ** 67 TRP 67 1.332 1.236 1.508 1.537 1.438 121.84 115.18 121.66 110.01 108.67 111.33 123.11 * * 68 GLU 68 1.307 1.223 1.532 1.549 1.433 120.57 115.92 121.28 115.39 111.97 113.43 122.75 +* * +** +* +** 69 ASN 69 1.319 1.196 1.506 1.539 1.450 121.92 116.11 120.78 109.65 109.24 111.96 123.07 +* +* 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 ----------------------------------------------------------------------------------------------------------------------------------- 70 PHE 70 1.318 1.228 1.498 1.547 1.454 122.98 115.90 120.63 109.52 110.17 111.26 123.46 * * 71 VAL 71 1.325 1.218 1.517 1.560 1.443 121.54 115.62 121.01 111.19 110.18 112.04 123.36 72 LYS 72 1.313 1.227 1.545 1.536 1.457 121.52 117.39 120.03 111.11 112.48 112.53 122.57 * * * 73 ASP 73 1.336 1.227 1.513 1.542 1.493 121.35 117.12 120.52 110.30 113.75 111.82 122.35 +* +* 74 ASN 74 1.302 1.227 1.532 1.559 1.446 120.52 115.05 120.89 112.35 108.00 109.59 123.98 +* * * * +* 75 ASN 75 1.336 1.233 1.526 1.543 1.487 125.07 116.35 121.22 111.42 112.96 112.63 122.42 +* +* * +* 76 LEU 76 1.313 1.240 1.519 1.538 1.447 121.29 115.08 121.04 110.18 111.50 111.32 123.88 * * 77 GLU 77 1.310 1.244 1.507 1.525 1.448 124.35 116.37 119.97 109.84 108.66 110.51 123.66 * * * 78 ASP 78 1.316 1.234 1.518 1.552 1.461 121.19 116.11 120.82 110.83 109.52 112.91 123.06 * * * 79 GLY 79 1.300 1.240 1.498 - 1.440 121.06 115.28 121.14 - 110.06 - 123.58 ** * ** 80 LYS 80 1.314 1.234 1.519 1.551 1.439 122.33 118.42 119.55 112.67 105.91 110.12 122.03 * * * * * +* +* 81 TYR 81 1.314 1.236 1.484 1.537 1.448 119.24 114.88 121.12 111.22 112.53 112.46 123.99 * +* * * +* 82 LEU 82 1.302 1.241 1.508 1.551 1.423 122.75 116.76 120.12 107.01 109.55 110.74 123.11 +* * +* +* +* 83 GLN 83 1.300 1.242 1.518 1.557 1.430 120.37 116.55 120.84 111.40 106.40 113.85 122.52 ** * * +* +* ** 84 PHE 84 1.285 1.227 1.487 1.532 1.427 121.04 116.03 120.53 108.99 109.50 111.71 123.43 *** +* +* *** 85 ILE 85 1.286 1.233 1.505 1.554 1.422 121.50 116.34 120.44 110.15 105.50 111.82 123.17 *** +* ** *** 86 TYR 86 1.290 1.239 1.510 1.549 1.428 121.41 115.78 120.69 112.00 109.88 109.40 123.48 +** +* * +** 87 ASP 87 1.314 1.217 1.535 1.549 1.459 122.26 119.46 119.76 110.72 106.24 108.99 120.77 * +* +* * +* 88 ARG 88 1.298 1.237 1.505 1.520 1.442 118.54 114.94 121.50 112.21 109.78 113.12 123.56 ** +* * +* ** 89 ASP 89 1.313 1.217 1.507 1.536 1.409 122.73 116.30 120.87 112.18 109.21 111.72 122.78 * +** * +** 90 ARG 90 1.283 1.242 1.523 1.520 1.457 122.70 115.90 121.07 110.53 111.71 107.61 122.99 *** +* *** 91 THR 91 1.307 1.240 1.542 1.552 1.430 122.07 116.05 121.25 111.18 110.94 110.84 122.67 +* * +* 92 PHE 92 1.319 1.219 1.510 1.536 1.453 122.33 117.24 120.01 108.09 108.52 111.00 122.74 * * 93 TYR 93 1.300 1.232 1.518 1.536 1.453 121.47 116.97 120.19 111.53 107.50 109.64 122.83 ** * ** 94 VAL 94 1.310 1.236 1.540 1.566 1.452 121.13 115.22 121.75 110.80 114.54 111.12 123.03 * * * 95 ILE 95 1.317 1.241 1.529 1.556 1.443 122.88 116.10 120.79 110.07 108.45 112.57 123.09 96 ILE 96 1.309 1.235 1.520 1.561 1.425 122.84 116.15 121.05 109.39 110.25 109.88 122.76 * +* +* 97 TYR 97 1.301 1.245 1.502 1.535 1.437 121.25 116.68 120.18 108.64 108.56 112.19 123.13 ** * * ** 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 ----------------------------------------------------------------------------------------------------------------------------------- 98 GLY 98 1.311 1.230 1.506 - 1.445 120.98 115.82 121.16 - 110.58 - 123.01 * * 99 HIS 99 1.311 1.230 1.510 1.530 1.427 121.38 114.98 120.93 110.41 110.09 111.04 124.09 * +* +* 100 ASN 100 1.296 1.238 1.508 1.538 1.455 124.60 114.08 121.60 109.79 106.31 110.98 124.30 ** +* * +* ** 101 MET 101 1.318 1.230 1.522 1.557 1.450 124.58 115.69 121.02 111.34 108.51 114.08 123.26 * +* ** ** 102 CYS 102 1.316 - 1.513 1.544 1.438 124.07 - - 110.32 107.18 111.48 - * * * * ----------------------------------------------------------------------------------------------------------------------------------- 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 1.268 1.349 1.309 .014 **** * * C-N (Pro) 1.341 .016 5 1.335 1.359 1.346 .009 * C-O C-O 1.231 .020 101 1.196 1.258 1.233 .009 +* * CA-C CH1E-C (except Gly) 1.525 .021 95 1.480 1.548 1.519 .016 ** * CH2G*-C (Gly) 1.516 .018 7 1.484 1.523 1.500 .011 +* CA-CB CH1E-CH3E (Ala) 1.521 .033 2 1.521 1.532 1.527 .006 CH1E-CH1E (Ile,Thr,Val) 1.540 .027 18 1.534 1.582 1.558 .013 +* CH1E-CH2E (the rest) 1.530 .020 75 1.513 1.568 1.536 .011 +* N-CA NH1-CH1E (except Gly,Pro)1.458 .019 90 1.409 1.493 1.443 .016 +** +* NH1-CH2G* (Gly) 1.451 .016 7 1.417 1.454 1.438 .011 ** N-CH1E (Pro) 1.466 .015 5 1.434 1.474 1.456 .014 ** ------------------------------------------------------------------------------------------------------------- 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 89 113.73 119.46 116.37 1.11 * +* CH2G*-C-NH1 (Gly) 116.4 2.1 7 114.97 116.94 115.59 .64 CH1E-C-N (Pro) 116.9 1.5 5 114.04 117.82 115.75 1.69 +* O-C-N O-C-NH1 (except Pro) 123.0 1.6 96 120.41 124.41 122.95 .69 +* O-C-N (Pro) 122.0 1.4 5 122.06 124.15 123.22 .80 +* C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 89 118.54 125.50 121.86 1.52 +* ** C-NH1-CH2G* (Gly) 120.6 1.7 7 120.79 122.09 121.24 .40 C-N-CH1E (Pro) 122.6 5.0 5 121.55 123.49 122.57 .72 CA-C-O CH1E-C-O (except Gly) 120.8 1.7 94 118.30 122.13 120.71 .64 * CH2G*-C-O (Gly) 120.8 2.1 7 120.31 121.36 121.04 .33 CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 2 110.34 110.86 110.60 .26 CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 18 107.01 112.12 110.55 1.19 * CH2E-CH1E-C (the rest) 110.1 1.9 75 106.69 115.39 110.40 1.38 +* +** N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 90 104.02 115.45 109.92 2.25 +** +* NH1-CH2G*-C (Gly) 112.5 2.9 7 108.91 114.82 111.50 1.93 * N-CH1E-C (Pro) 111.8 2.5 5 107.58 114.47 111.30 2.77 +* * N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 2 109.79 110.50 110.15 .35 NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 18 108.90 113.60 111.43 1.31 +* * N-CH1E-CH2E (Pro) 103.0 1.1 5 103.28 104.31 103.77 .36 * NH1-CH1E-CH2E (the rest) 110.5 1.7 70 105.63 115.42 110.89 1.68 +** +** ------------------------------------------------------------------------------------------------------------- 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] 77 87.5% Residues in additional allowed regions [a,b,l,p] 9 10.2% Residues in generously allowed regions [~a,~b,~l,~p] 2 2.3% Residues in disallowed regions [XX] 0 .0% ---- ------ 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 87.5 83.8 10.0 .4 Inside b. Omega angle st dev 101 4.5 6.0 3.0 -.5 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 -.7 Inside e. H-bond energy st dev 58 .9 .8 .2 .7 Inside f. Overall G-factor 102 -.1 -.4 .3 .9 Inside 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 21 7.5 18.1 6.5 -1.6 BETTER b. Chi-1 trans st dev 26 8.0 19.0 5.3 -2.1 BETTER c. Chi-1 gauche plus st dev 41 6.7 17.5 4.9 -2.2 BETTER d. Chi-1 pooled st dev 88 8.4 18.2 4.8 -2.0 BETTER e. Chi-2 trans st dev 23 3.5 20.4 5.0 -3.4 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% 87.5 1 Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.7 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 -.52 Chi1-chi2 distribution -.28 Chi1 only -.30 Chi3 & chi4 .44 Omega -.28 ------ -.27 ===== Main-chain covalent forces:- Main-chain bond lengths -.09 Main-chain bond angles .33 ------ .16 ===== OVERALL AVERAGE -.12 ===== Ideally, scores should be above -0.5. Values below -1.0 may need investigation.