==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=6-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE 28-NOV-01 1KGM . COMPND 2 MOLECULE: SERINE PROTEASE INHIBITOR I; . SOURCE 2 SYNTHETIC: YES; . AUTHOR Z.GASPARI,A.PATTHY,L.GRAF,A.PERCZEL . 35 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2897.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 14 40.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 5 14.3 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . 4 11.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . 1 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA 1 1 A E 0 0 237 0, 0.0 2,-0.2 0, 0.0 24,-0.1 0.000 360.0 360.0 360.0 83.0 6.2 0.9 10.3 2 2 A V - 0 0 38 22,-1.1 2,-0.3 2,-0.1 24,-0.0 -0.700 360.0-156.0-105.1 159.9 2.8 0.9 8.5 3 3 A T + 0 0 133 -2,-0.2 2,-0.3 2,-0.1 21,-0.1 -0.656 53.5 86.6-134.5 79.6 -0.6 2.0 9.8 4 4 A a S S- 0 0 28 19,-0.8 21,-0.1 -2,-0.3 -2,-0.1 -0.987 70.5 -95.7-163.0 170.0 -3.4 0.3 7.9 5 5 A E > - 0 0 143 -2,-0.3 2,-0.6 4,-0.1 4,-0.5 -0.643 47.6 -95.7 -95.5 155.9 -5.6 -2.8 7.7 6 6 A P T 4 S+ 0 0 63 0, 0.0 14,-0.1 0, 0.0 15,-0.1 -0.556 110.8 29.4 -71.4 114.1 -4.9 -5.8 5.5 7 7 A G T 4 S+ 0 0 57 12,-0.7 13,-0.1 -2,-0.6 14,-0.1 0.817 103.1 75.8 103.9 47.7 -6.9 -5.3 2.3 8 8 A T T 4 + 0 0 87 -3,-0.4 10,-0.1 11,-0.2 -4,-0.0 0.417 57.8 178.3-154.1 -33.3 -7.2 -1.5 1.9 9 9 A T < - 0 0 50 -4,-0.5 2,-0.3 11,-0.1 9,-0.2 0.162 12.2-168.5 42.7-172.6 -3.8 -0.0 0.7 10 10 A F - 0 0 60 7,-0.4 7,-1.3 -6,-0.1 2,-0.5 -0.986 29.6 -58.8 176.5-173.3 -3.7 3.7 0.1 11 11 A K E +A 16 0A 190 -2,-0.3 2,-0.4 5,-0.2 5,-0.2 -0.803 50.8 179.7 -95.8 126.0 -1.7 6.6 -1.3 12 12 A D E > -A 15 0A 68 3,-3.3 3,-3.9 -2,-0.5 -2,-0.0 -0.962 50.8 -55.0-127.8 145.0 1.8 7.1 0.0 13 13 A K T 3 S- 0 0 109 -2,-0.4 20,-0.1 1,-0.3 3,-0.0 0.110 122.5 -22.0 26.7-105.3 4.6 9.6 -0.8 14 14 A b T 3 S+ 0 0 53 21,-0.1 -1,-0.3 19,-0.1 2,-0.3 0.130 134.7 41.0-114.3 20.7 4.9 9.1 -4.6 15 15 A N E < S-A 12 0A 21 -3,-3.9 -3,-3.3 16,-0.1 2,-0.4 -0.929 84.5 -94.6-153.2 177.7 3.4 5.6 -4.8 16 16 A T E -A 11 0A 60 -2,-0.3 13,-2.2 -5,-0.2 2,-0.7 -0.858 28.2-152.1-104.8 134.0 0.6 3.3 -3.4 17 17 A c - 0 0 6 -7,-1.3 2,-0.8 -2,-0.4 -7,-0.4 -0.881 7.2-147.7-108.4 112.1 1.3 1.0 -0.4 18 18 A R - 0 0 138 -2,-0.7 9,-1.2 -9,-0.2 -14,-0.0 -0.635 26.3-120.7 -78.5 112.2 -0.8 -2.1 -0.3 19 19 A a B -B 26 0B 0 -2,-0.8 -12,-0.7 7,-0.2 7,-0.3 -0.274 30.5-131.8 -52.7 125.2 -1.4 -2.9 3.4 20 20 A G - 0 0 20 5,-4.9 -13,-0.3 -14,-0.1 -11,-0.1 0.327 29.1 -92.6 -61.0-156.3 0.1 -6.4 4.0 21 21 A S S S+ 0 0 117 -15,-0.1 -1,-0.1 1,-0.1 -2,-0.1 0.488 118.2 66.7-102.8 -5.0 -1.9 -9.1 5.8 22 22 A D S S- 0 0 103 -17,-0.1 -1,-0.1 3,-0.0 -3,-0.0 0.466 103.9-123.0 -93.8 -0.2 -0.4 -8.3 9.3 23 23 A G S S+ 0 0 26 2,-0.2 -19,-0.8 -3,-0.1 -2,-0.1 0.660 103.2 66.4 69.9 11.3 -2.1 -4.9 9.4 24 24 A K S S+ 0 0 124 -21,-0.1 -22,-1.1 -23,-0.0 2,-0.3 0.245 85.3 74.1-145.1 11.9 1.4 -3.4 9.9 25 25 A S - 0 0 62 -21,-0.1 -5,-4.9 -24,-0.1 2,-0.3 -0.908 52.7-170.9-127.8 157.0 3.2 -4.1 6.6 26 26 A A B -B 19 0B 35 -2,-0.3 -7,-0.2 -7,-0.3 -9,-0.1 -0.998 21.2-152.0-147.1 150.1 3.0 -2.6 3.1 27 27 A A - 0 0 67 -9,-1.2 -10,-0.1 -2,-0.3 -1,-0.1 0.909 26.0-165.8 -87.9 -48.7 4.4 -3.3 -0.4 28 28 A c - 0 0 17 1,-0.1 -11,-0.3 -13,-0.0 -2,-0.0 0.839 31.3-118.0 61.9 107.0 4.4 0.2 -1.9 29 29 A T - 0 0 65 -13,-2.2 -1,-0.1 1,-0.0 -12,-0.1 0.894 42.1-161.1 -42.1 -43.3 4.9 0.0 -5.7 30 30 A L + 0 0 112 -14,-0.1 3,-0.1 2,-0.1 -15,-0.1 0.956 35.9 141.8 57.9 90.3 8.1 1.9 -5.1 31 31 A K - 0 0 159 1,-0.3 2,-0.2 -17,-0.1 -16,-0.1 0.591 67.7 -35.9-128.4 -33.9 9.1 3.5 -8.5 32 32 A A + 0 0 73 -18,-0.1 -1,-0.3 1,-0.0 -2,-0.1 -0.859 50.1 169.6 174.0 150.5 10.5 6.9 -7.7 33 33 A b - 0 0 45 -2,-0.2 -19,-0.1 -3,-0.1 -18,-0.0 -0.435 11.2-177.5-178.6 97.1 10.0 9.8 -5.2 34 34 A P 0 0 122 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 0.746 360.0 360.0 -72.3 -23.9 12.3 12.8 -4.8 35 35 A Q 0 0 209 0, 0.0 -21,-0.1 0, 0.0 -22,-0.0 0.161 360.0 360.0-166.1 360.0 10.1 14.2 -2.0