Protein Data Bank File : 2bi6h Title : CYSTEINE PROTEASE INHIBITOR 07-DEC-95 2BI6 Number of Amino Acid Residues : 41 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU GLU TYR LYS CYS TYR CYS THR ASP THR 10 TYR SER ASP CYS PRO GLY PHE CYS LYS THR 20 CYS LYS ALA GLU PHE GLY LYS TYR ILE CYS 30 LEU ASP LEU ILE SER PRO ASN ASP CYS VAL 40 LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 -64.4 -179.8 -68.0 -127.9 61.7 2 GLU -146.4 53.2 -179.9 179.0 143.8 -89.2 3 TYR 175.6 -177.8 179.8 -139.2 78.8 4 LYS -59.4 -33.2 179.9 -96.5 170.2 -108.9 -65.4 5 CYS 68.5 158.0 -179.7 -51.5 6 TYR -132.5 128.0 179.6 29.6 -83.5 7 CYS -73.9 132.7 -179.6 166.5 8 THR -137.4 18.1 179.2 47.1 9 ASP -59.3 161.6 -179.5 -141.6 -51.0 10 THR -104.2 153.3 -179.6 43.0 11 TYR -146.0 -177.4 178.8 -31.1 -85.6 12 SER -106.9 6.5 -180.0 -60.1 13 ASP -167.1 165.1 -179.9 -114.9 77.4 14 CYS -71.9 119.2 -179.4 -37.1 15 PRO -77.2 148.8 179.6 22.4 -20.5 16 GLY -61.7 -29.3 179.6 17 PHE -77.8 -22.2 178.8 49.8 70.7 18 CYS -125.8 74.8 179.8 -149.1 19 LYS -50.2 -30.7 179.6 50.9 -133.6 -107.7 110.4 20 THR -86.9 81.6 -179.2 -67.4 21 CYS -90.5 135.6 179.5 69.7 22 LYS -116.0 102.5 -179.5 -143.9 -155.1 -155.5 -100.5 23 ALA -79.9 106.0 179.7 24 GLU -130.7 153.0 180.0 -62.1 -99.2 -32.7 25 PHE 49.8 17.4 178.8 3.5 -78.9 26 GLY 99.7 -29.1 -179.6 27 LYS -98.5 -165.5 -179.9 67.7 -141.6 63.2 -132.6 28 TYR -118.6 174.1 178.7 -96.9 -74.2 29 ILE -151.5 124.7 -179.6 -32.4 -173.1 30 CYS -81.0 140.1 179.1 -179.3 31 LEU -128.8 41.7 -178.9 -41.7 171.3 32 ASP -94.7 164.5 179.7 171.3 87.1 33 LEU -140.6 99.1 -179.6 -140.5 133.1 34 ILE -166.0 154.2 179.9 -86.0 107.2 35 SER -163.2 95.5 -179.8 146.7 36 PRO -76.9 -11.9 179.8 22.2 -21.1 37 ASN -139.1 -51.7 180.0 29.3 -61.2 38 ASP 164.0 -55.9 180.0 -112.7 -16.6 39 CYS -171.3 149.9 -180.0 -100.3 40 VAL -92.1 39.4 179.9 -168.7 41 LYS 179.1 -68.0 0.0 -162.9 -86.7 143.2 64.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 5.746 -8.363 -1.461 2 GLU 3.324 -11.151 -0.505 3 TYR -0.146 -9.621 -0.052 4 LYS -2.467 -6.813 -1.205 5 CYS 0.033 -4.351 0.314 6 TYR -0.999 -0.794 1.214 7 CYS 0.181 2.420 -0.467 8 THR 1.376 4.977 2.110 9 ASP 3.459 7.434 0.058 10 THR 2.930 11.103 0.996 11 TYR 1.534 13.803 -1.326 12 SER 0.306 17.411 -1.445 13 ASP -3.232 16.367 -2.454 14 CYS -5.462 13.260 -2.591 15 PRO -4.118 11.062 -5.412 16 GLY -6.505 9.277 -7.783 17 PHE -4.803 6.039 -6.727 18 CYS -5.445 6.879 -3.050 19 LYS -8.927 8.424 -2.804 20 THR -8.371 8.179 0.966 21 CYS -5.807 10.979 1.329 22 LYS -4.620 11.877 4.847 23 ALA -3.121 15.382 5.030 24 GLU -0.799 15.332 8.063 25 PHE 2.285 17.413 8.989 26 GLY 1.452 19.375 5.809 27 LYS 1.924 16.444 3.392 28 TYR -0.404 13.557 2.560 29 ILE -0.415 9.844 3.375 30 CYS -1.999 6.995 1.397 31 LEU -3.955 4.414 3.398 32 ASP -4.976 2.082 0.564 33 LEU -4.561 -1.718 0.450 34 ILE -4.263 -3.382 -2.980 35 SER -1.659 -5.085 -5.202 36 PRO -2.479 -6.260 -8.736 37 ASN 1.173 -7.281 -9.231 38 ASP 3.235 -6.740 -6.058 39 CYS 4.779 -3.245 -5.937 40 VAL 5.572 -0.331 -8.274 41 LYS 9.254 -0.458 -7.324 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C S S S S S S S 10 C C C C T T T T S S 20 S S S/T T T T/S S S S S 30 S S S S T T T T/S S S/S 40 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 S S t T T t S S 20 B B T T B B 30 S S S 40 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.0 0.0 85.8 2 GLU 0.0 0.0 88.4 3 TYR 20.1 11.1 80.4 4 LYS 58.2 33.6 67.0 5 CYS 72.7 73.3 64.3 6 TYR 56.5 31.2 68.8 7 CYS 52.5 53.0 63.4 8 THR 49.2 46.0 63.4 9 ASP 18.8 17.0 78.2 10 THR 60.9 57.0 53.2 11 TYR 139.8 77.2 49.4 12 SER 1.9 2.3 76.3 13 ASP 10.5 9.5 77.3 14 CYS 57.5 58.0 61.9 15 PRO 108.0 86.8 45.4 16 GLY 0.0 0.0 84.2 17 PHE 56.5 33.9 65.6 18 CYS 98.5 99.3 45.1 19 LYS 11.1 6.4 91.2 20 THR 35.9 33.6 65.8 21 CYS 84.2 84.9 54.4 22 LYS 78.1 45.0 65.6 23 ALA 36.0 49.6 68.3 24 GLU 78.8 56.9 63.7 25 PHE 58.3 35.0 66.8 26 GLY 0.0 0.0 82.4 27 LYS 81.3 46.9 69.9 28 TYR 147.5 81.5 49.4 29 ILE 111.5 77.7 44.8 30 CYS 99.2 100.0 40.4 31 LEU 86.2 58.3 53.1 32 ASP 75.2 68.1 57.2 33 LEU 68.7 46.5 59.4 34 ILE 49.2 34.3 74.5 35 SER 76.8 91.9 56.7 36 PRO 29.8 24.0 81.6 37 ASN 44.3 36.7 71.0 38 ASP 43.5 39.4 81.2 39 CYS 40.1 40.5 75.6 40 VAL 0.0 0.0 88.1 41 LYS 0.0 0.0 93.3