Protein Data Bank File : 1fzca Title : BLOOD COAGULATION 19-MAY-98 1FZC Number of Amino Acid Residues : 74 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU 10 LYS VAL GLN HIS ILE GLN LEU LEU GLN LYS 20 ASN VAL ARG ALA GLN LEU VAL ASP MET LYS 30 ARG LEU GLU VAL ASP ILE ASP ILE LYS ILE 40 ARG SER CYS ARG GLY SER CYS SER ARG ALA 50 LEU ALA ARG GLU VAL ASP LEU LYS ASP TYR 60 GLU ASP GLN GLN LYS GLN LEU GLU GLN VAL 70 ILE ALA LYS ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ILE 0.0 -45.4 178.0 -148.8 60.3 2 GLU -47.0 -56.7 178.3 178.2 -148.8 29.1 3 VAL -65.8 15.6 176.1 -45.4 4 LEU -142.7 -121.7 -178.7 -148.6 53.7 5 LYS -34.9 -24.3 179.5 -67.6 160.9 176.4 -150.3 6 ARG -81.8 -43.6 -179.9 -116.9 75.5 -72.0 144.9 7 LYS -64.3 -32.1 178.6 -73.7 -60.4 118.3 -167.5 8 VAL -61.8 -58.5 -179.4 178.2 9 ILE -51.4 -41.0 176.8 -81.2 162.0 10 GLU -57.3 -37.5 -175.2 -146.9 -119.4 -43.7 11 LYS -82.1 -39.2 175.8 -61.2 -66.1 79.6 -150.1 12 VAL -53.2 -34.2 -178.7 138.4 13 GLN -72.2 -32.9 179.6 73.7 -147.3 6.7 14 HIS -73.1 -31.4 177.9 -69.5 -115.9 15 ILE -70.0 -40.7 -179.4 -71.1 126.5 16 GLN -63.7 -33.9 175.3 -68.6 176.6 -59.5 17 LEU -68.0 -55.3 177.6 171.2 -72.9 18 LEU -49.6 -51.6 -177.2 -103.2 176.8 19 GLN -47.3 -58.9 176.3 -73.9 -175.2 -20.6 20 LYS -56.3 -42.5 -177.1 -62.7 -51.9 163.7 -38.5 21 ASN -61.1 -47.9 -177.2 -79.4 -27.2 22 VAL -71.8 -23.6 174.5 -49.9 23 ARG -62.1 -46.2 177.3 166.0 147.5 89.2 -171.3 24 ALA -70.1 -30.5 -177.3 25 GLN -77.7 -28.6 171.9 174.0 171.1 103.0 26 LEU -62.9 -40.8 176.2 -88.3 163.7 27 VAL -64.4 -49.5 172.6 166.4 28 ASP -53.5 -42.1 -174.9 -50.4 -40.2 29 MET -71.3 -39.0 176.9 -82.3 -63.5 -60.4 30 LYS -63.6 -42.4 177.3 170.2 145.0 162.0 -171.6 31 ARG -64.6 -32.1 178.2 -77.8 176.1 179.9 162.7 32 LEU -76.1 -38.9 172.2 -178.4 49.9 33 GLU -60.8 -42.4 178.5 -166.9 72.8 62.8 34 VAL -71.9 -47.9 173.9 164.7 35 ASP -56.1 -42.9 176.4 -179.3 74.8 36 ILE -68.2 -37.3 175.9 -73.5 176.7 37 ASP -61.4 -45.1 177.5 -167.7 67.3 38 ILE -65.3 -42.7 178.5 -73.4 172.0 39 LYS -69.8 -35.2 174.1 -62.0 -74.1 -157.6 -20.1 40 ILE -65.8 -44.4 178.5 -69.2 -172.9 41 ARG -59.9 -41.7 177.1 -163.3 169.7 -69.9 107.6 42 SER -66.5 -1.5 173.0 96.1 43 CYS -93.3 -11.9 -179.3 -62.3 44 ARG -55.1 -32.9 -178.5 -117.5 -159.0 134.2 -131.4 45 GLY -84.2 -6.6 175.5 46 SER -117.4 -35.8 -172.4 -7.1 47 CYS -94.1 157.5 177.3 -51.1 48 SER -50.7 -40.8 177.4 58.3 49 ARG -159.8 163.0 178.5 59.9 172.2 -47.9 -96.4 50 ALA -119.0 141.9 180.0 51 LEU -57.2 125.2 177.6 -142.2 -158.0 52 ALA -79.0 126.2 -175.0 53 ARG -142.6 169.1 -179.5 22.4 -167.4 -10.6 -90.8 54 GLU -140.5 123.2 178.5 -61.0 69.6 28.7 55 VAL -107.3 149.0 175.9 177.0 56 ASP -157.7 116.6 -176.1 -167.6 -7.5 57 LEU -79.3 16.7 -176.0 -64.8 -37.0 58 LYS -76.1 -45.2 173.8 -178.2 73.9 41.9 -82.9 59 ASP -59.3 -32.6 -178.6 -172.9 75.8 60 TYR -74.4 -36.5 -178.2 -73.1 -82.6 61 GLU -74.9 -34.7 175.6 -82.4 159.4 16.2 62 ASP -64.0 -51.1 178.0 -67.6 -17.4 63 GLN -60.5 -35.2 178.6 -65.4 -170.7 105.6 64 GLN -71.7 -38.0 -179.5 -71.4 170.1 -75.5 65 LYS -72.0 -42.9 176.1 -112.6 92.3 143.5 -110.6 66 GLN -47.7 -51.4 178.7 -159.8 161.8 -73.2 67 LEU -65.7 -38.2 -179.8 -173.7 -91.9 68 GLU -64.4 -32.3 179.6 -81.2 -4.2 -81.9 69 GLN -65.4 -49.2 178.8 -82.7 178.5 171.3 70 VAL -61.1 -48.8 -179.4 172.4 71 ILE -61.0 -40.9 -175.5 -66.1 179.7 72 ALA -71.6 -53.1 -176.9 73 LYS -75.6 35.2 178.9 -71.9 157.1 165.4 72.9 74 ASP -105.0 43.3 0.0 -82.8 -11.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ILE 23.890 10.761 3.754 2 GLU 25.468 9.996 7.156 3 VAL 25.057 13.703 8.003 4 LEU 21.435 13.296 6.889 5 LYS 19.095 10.289 6.716 6 ARG 21.603 8.616 9.044 7 LYS 21.642 11.454 11.525 8 VAL 17.853 11.525 11.401 9 ILE 17.615 7.838 12.222 10 GLU 20.168 8.347 15.014 11 LYS 17.880 10.952 16.621 12 VAL 14.621 9.030 16.120 13 GLN 16.085 6.240 18.265 14 HIS 16.775 8.743 21.042 15 ILE 13.218 10.117 20.923 16 GLN 11.910 6.541 21.028 17 LEU 14.023 5.900 24.152 18 LEU 12.619 9.039 25.785 19 GLN 9.097 7.984 24.810 20 LYS 9.311 4.637 26.593 21 ASN 11.056 6.340 29.491 22 VAL 8.315 8.900 30.052 23 ARG 5.703 6.167 29.669 24 ALA 7.252 4.491 32.725 25 GLN 7.600 7.813 34.663 26 LEU 3.885 8.669 34.257 27 VAL 3.143 5.242 35.855 28 ASP 5.602 5.930 38.736 29 MET 3.982 9.395 39.217 30 LYS 0.410 8.050 39.306 31 ARG 1.535 5.457 41.841 32 LEU 3.277 8.058 44.058 33 GLU 0.222 10.399 44.120 34 VAL -2.105 7.516 45.246 35 ASP 0.506 6.304 47.754 36 ILE 0.811 9.847 49.210 37 ASP -2.995 10.298 49.390 38 ILE -3.251 6.973 51.327 39 LYS -0.336 7.731 53.773 40 ILE -1.579 11.284 54.615 41 ARG -5.097 9.892 55.291 42 SER -3.516 7.212 57.468 43 CYS -2.245 10.005 59.798 44 ARG -5.824 11.043 60.675 45 GLY -5.794 8.327 63.378 46 SER -2.581 9.524 65.117 47 CYS -2.062 13.290 64.461 48 SER -4.048 16.388 65.475 49 ARG -5.327 16.746 61.871 50 ALA -4.752 15.539 58.300 51 LEU -4.358 17.767 55.189 52 ALA -7.588 18.049 53.097 53 ARG -6.639 17.198 49.524 54 GLU -8.261 16.014 46.283 55 VAL -6.745 13.546 43.838 56 ASP -7.961 12.914 40.272 57 LEU -5.998 10.683 37.987 58 LYS -7.547 12.453 34.953 59 ASP -4.702 14.819 34.193 60 TYR -2.556 11.644 34.399 61 GLU -4.971 9.772 32.167 62 ASP -5.175 12.535 29.579 63 GLN -1.396 12.612 29.458 64 GLN -1.075 8.821 29.155 65 LYS -3.380 8.478 26.096 66 GLN -1.805 11.573 24.571 67 LEU 1.650 10.008 24.864 68 GLU 0.253 6.678 23.590 69 GLN -1.051 8.403 20.438 70 VAL 2.400 9.787 19.711 71 ILE 4.199 6.493 20.473 72 ALA 1.661 4.551 18.420 73 LYS 1.250 6.935 15.534 74 ASP 4.979 6.703 14.896 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H H H H 40 H H H/T T T T C C S S 50 S S S S S S S/H H H H 60 H H H H H H H H H H 70 H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T h H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H H H H 40 H h T T T T t S 50 t h H H H 60 H H H H H H H H H H 70 H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ILE 63.6 44.3 67.0 2 GLU 31.0 22.4 65.8 3 VAL 15.5 13.0 76.9 4 LEU 37.0 25.0 70.4 5 LYS 46.1 26.6 69.7 6 ARG 110.5 52.9 55.2 7 LYS 86.0 49.6 68.5 8 VAL 33.1 27.8 65.4 9 ILE 43.3 30.2 79.0 10 GLU 84.8 61.2 73.0 11 LYS 69.9 40.3 76.6 12 VAL 50.7 42.7 65.2 13 GLN 63.6 42.8 72.8 14 HIS 65.8 43.8 79.0 15 ILE 55.1 38.4 67.6 16 GLN 70.1 47.2 69.6 17 LEU 44.4 30.0 80.7 18 LEU 39.7 26.9 71.0 19 GLN 133.4 89.7 45.5 20 LYS 86.6 50.0 74.0 21 ASN 48.7 40.3 61.8 22 VAL 65.0 54.7 55.4 23 ARG 113.8 54.5 61.5 24 ALA 15.1 20.9 79.4 25 GLN 30.3 20.4 78.6 26 LEU 120.2 81.3 55.6 27 VAL 67.8 57.1 76.7 28 ASP 29.5 26.7 71.9 29 MET 73.1 45.9 66.0 30 LYS 119.0 68.6 60.4 31 ARG 41.8 20.0 79.6 32 LEU 57.9 39.2 69.1 33 GLU 91.0 65.7 61.7 34 VAL 58.4 49.1 55.0 35 ASP 53.1 48.1 67.8 36 ILE 70.3 49.0 66.1 37 ASP 92.6 83.8 63.4 38 ILE 48.2 33.6 73.0 39 LYS 53.9 31.1 83.9 40 ILE 96.4 67.2 57.3 41 ARG 72.8 34.9 77.6 42 SER 26.8 32.1 76.1 43 CYS 46.5 46.9 74.7 44 ARG 39.2 18.8 83.4 45 GLY 0.0 0.0 85.1 46 SER 18.7 22.3 78.5 47 CYS 39.7 40.0 77.4 48 SER 0.0 0.0 81.1 49 ARG 47.7 22.8 84.6 50 ALA 61.5 84.7 58.0 51 LEU 52.9 35.8 74.8 52 ALA 8.0 11.0 85.6 53 ARG 154.2 73.8 60.7 54 GLU 10.4 7.5 84.2 55 VAL 103.5 87.1 61.7 56 ASP 28.7 26.0 71.2 57 LEU 99.1 67.0 53.3 58 LYS 68.5 39.5 85.8 59 ASP 17.1 15.5 81.4 60 TYR 153.7 84.9 51.6 61 GLU 75.4 54.4 77.7 62 ASP 36.9 33.4 70.3 63 GLN 82.6 55.6 68.4 64 GLN 109.6 73.7 54.9 65 LYS 21.4 12.3 83.3 66 GLN 41.6 28.0 77.2 67 LEU 120.4 81.5 47.3 68 GLU 82.2 59.3 60.7 69 GLN 52.8 35.5 70.3 70 VAL 37.1 31.2 77.2 71 ILE 127.0 88.5 57.9 72 ALA 20.7 28.5 78.1 73 LYS 39.4 22.7 77.3 74 ASP 67.6 61.2 82.6