Protein Data Bank File : crambin Title : CRAMBIN Number of Amino Acid Residues : 46 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR THR CYS CYS PRO SER ILE VAL ALA ARG 10 SER ASN PHE ASN VAL CYS ARG LEU PRO GLY 20 THR PRO GLU ALA ILE CYS ALA THR TYR THR 30 GLY CYS ILE ILE ILE PRO GLY ALA THR CYS 40 PRO GLY ASP TYR ALA ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 147.7 178.9 -59.3 2 THR -107.8 144.3 -179.5 56.1 3 CYS -131.2 133.3 -177.9 -51.1 4 CYS -118.9 151.2 -176.9 -64.6 5 PRO -76.2 -19.0 -179.4 32.0 -41.4 6 SER -157.9 166.0 177.6 69.2 7 ILE -63.6 -42.1 178.3 -74.1 172.8 8 VAL -55.9 -44.6 -178.4 159.7 9 ALA -61.4 -43.8 178.1 10 ARG -63.2 -43.3 -179.8 176.7 64.0 67.2 177.4 11 SER -61.2 -42.4 179.8 -65.8 12 ASN -64.9 -39.5 177.3 -69.6 -22.9 13 PHE -59.1 -47.2 -177.9 -174.9 -90.0 14 ASN -62.8 -35.2 177.3 -73.0 -24.2 15 VAL -69.2 -41.2 179.5 171.0 16 CYS -56.7 -36.0 -178.7 179.5 17 ARG -77.1 -16.1 -176.7 -67.1 -79.8 -72.1 157.4 18 LEU -53.2 -46.2 179.9 -76.1 176.6 19 PRO -77.2 -7.6 -179.9 12.8 -13.9 20 GLY 106.3 7.3 -179.1 21 THR -52.7 136.3 178.2 -45.0 22 PRO -57.0 146.6 177.3 -24.1 32.5 23 GLU -56.4 -36.2 -175.8 -72.5 -172.0 -21.6 24 ALA -63.4 -34.9 179.0 25 ILE -74.8 -37.9 176.0 -75.4 -72.0 26 CYS -64.9 -31.7 178.6 -65.3 27 ALA -62.0 -54.0 -178.8 28 THR -68.8 -25.5 177.3 53.5 29 TYR -67.6 -36.3 -171.8 -177.6 55.3 30 THR -109.0 -18.5 -171.6 61.2 31 GLY 91.8 -3.1 171.5 32 CYS -69.5 164.4 -178.1 -54.3 33 ILE -129.8 157.0 174.8 65.1 170.6 34 ILE -111.6 129.6 176.3 -60.3 168.4 35 ILE -124.1 158.1 -179.0 64.7 169.3 36 PRO -78.2 -24.4 -177.7 4.2 -3.8 37 GLY -89.7 -161.7 -176.4 38 ALA -120.8 1.2 -174.7 39 THR -114.6 104.5 -178.6 -51.7 40 CYS -75.5 145.4 176.7 -63.2 41 PRO -71.2 162.7 -176.9 27.6 -34.5 42 GLY -61.9 -23.1 178.3 43 ASP -89.7 -2.0 174.9 59.2 -24.4 44 TYR -130.3 60.0 -168.7 -73.6 86.4 45 ALA -88.8 -2.5 -174.3 46 ASN -112.9 13.7 0.0 -56.5 113.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 16.967 12.784 4.338 2 THR 13.856 11.469 6.066 3 CYS 13.660 10.707 9.787 4 CYS 10.646 8.991 11.408 5 PRO 9.448 9.034 15.012 6 SER 8.673 5.314 15.279 7 ILE 8.912 2.083 13.258 8 VAL 5.145 2.209 12.453 9 ALA 5.598 5.767 11.082 10 ARG 8.496 4.609 8.837 11 SER 6.500 1.584 7.565 12 ASN 3.545 3.935 6.751 13 PHE 5.929 6.358 5.055 14 ASN 7.331 3.607 2.791 15 VAL 3.782 2.599 1.742 16 CYS 2.890 6.285 1.126 17 ARG 5.895 6.489 -1.213 18 LEU 4.933 3.431 -3.326 19 PRO 2.792 5.376 -5.797 20 GLY 5.366 8.191 -6.018 21 THR 3.767 10.609 -3.513 22 PRO 6.143 13.513 -2.696 23 GLU 8.114 13.103 0.500 24 ALA 6.614 16.317 1.913 25 ILE 3.074 14.894 1.756 26 CYS 4.180 11.549 3.187 27 ALA 5.879 13.502 6.026 28 THR 2.691 15.221 7.194 29 TYR 0.715 12.045 6.657 30 THR 2.986 9.994 8.950 31 GLY 4.769 12.336 11.360 32 CYS 8.140 11.694 9.635 33 ILE 10.280 14.760 8.823 34 ILE 12.552 15.877 6.036 35 ILE 15.930 17.454 6.941 36 PRO 18.635 18.861 4.738 37 GLY 21.452 16.969 6.513 38 ALA 22.019 13.242 7.020 39 THR 21.936 12.911 10.809 40 CYS 18.504 12.312 12.298 41 PRO 17.924 13.421 15.877 42 GLY 17.334 10.956 18.691 43 ASP 13.564 11.573 18.836 44 TYR 13.257 10.745 15.081 45 ALA 15.445 7.667 15.246 46 ASN 13.512 5.395 12.878 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S/H H H H H 10 H H H H H H H H S S 20 S S/H H H H H H H H H 30 H/S S S S S S/S S S S C 40 T T T T/S S S Kabash-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E B S h H H H H 10 H H H H H H H h T T 20 t h H H H H H H H H 30 h E E e S S S 40 g G G G g B Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 54.7 51.2 70.2 2 THR 94.2 88.2 55.4 3 CYS 99.2 100.0 41.4 4 CYS 99.2 100.0 40.9 5 PRO 88.3 70.9 60.5 6 SER 36.2 43.3 68.9 7 ILE 16.9 11.8 83.1 8 VAL 13.9 11.7 83.4 9 ALA 65.4 90.1 59.3 10 ARG 148.0 70.9 67.5 11 SER 26.1 31.2 75.2 12 ASN 50.0 41.3 60.1 13 PHE 159.6 95.7 46.1 14 ASN 42.2 34.9 66.4 15 VAL 21.3 17.9 76.6 16 CYS 79.9 80.5 47.0 17 ARG 123.7 59.2 65.5 18 LEU 29.9 20.2 77.1 19 PRO 41.9 33.6 83.6 20 GLY 5.2 15.0 85.4 21 THR 73.6 68.9 48.1 22 PRO 39.9 32.1 73.2 23 GLU 82.9 59.8 58.1 24 ALA 15.9 21.9 64.0 25 ILE 38.8 27.1 71.0 26 CYS 99.2 100.0 39.1 27 ALA 62.7 86.4 57.4 28 THR 12.3 11.5 81.7 29 TYR 44.4 24.5 75.8 30 THR 101.4 94.8 49.7 31 GLY 2.3 6.5 80.1 32 CYS 99.0 99.8 38.9 33 ILE 89.8 62.6 52.8 34 ILE 89.9 62.7 60.7 35 ILE 111.3 77.5 48.8 36 PRO 7.5 6.0 83.7 37 GLY 0.0 0.0 74.3 38 ALA 10.7 14.8 78.5 39 THR 0.0 0.0 86.2 40 CYS 77.6 78.3 54.3 41 PRO 66.4 53.3 66.3 42 GLY 0.0 0.0 79.8 43 ASP 17.7 16.1 72.8 44 TYR 123.9 68.5 59.9 45 ALA 29.0 40.0 83.3 46 ASN 70.7 58.5 67.1