==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=5-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE INHIBITOR 30-MAY-07 2V1V . COMPND 2 MOLECULE: TRYPSIN INHIBITOR 1; . SOURCE 2 SYNTHETIC: YES; . AUTHOR P.SLEDZ,K.BOLEWSKA,A.BIERZYNSKI,I.ZHUKOV . 29 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2779.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 11 37.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 2 6.9 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 3 10.3 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, 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 3.4 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-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 . 3 10.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 4 13.8 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+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 . 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 PARALLEL BRIDGES PER LADDER . 0 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 . 0 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 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 R 0 0 239 0, 0.0 2,-0.4 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 142.3 -12.1 4.0 1.4 2 2 A V - 0 0 140 16,-0.1 18,-0.1 18,-0.0 17,-0.0 -0.812 360.0-141.3-101.5 138.1 -10.6 0.7 2.4 3 3 A a - 0 0 25 -2,-0.4 3,-0.1 26,-0.2 15,-0.1 -0.840 31.7 -99.7-100.4 130.3 -8.0 -1.2 0.3 4 4 A P - 0 0 83 0, 0.0 2,-2.2 0, 0.0 13,-0.1 0.017 43.0 -97.7 -42.7 148.2 -8.2 -5.0 0.0 5 5 A R S S+ 0 0 250 2,-0.0 2,-0.4 0, 0.0 24,-0.1 -0.485 75.1 136.7 -73.9 79.6 -5.8 -6.9 2.2 6 6 A I - 0 0 105 -2,-2.2 22,-0.3 22,-0.2 -3,-0.0 -0.981 55.9-118.8-133.7 122.6 -3.2 -7.5 -0.5 7 7 A L + 0 0 129 -2,-0.4 2,-0.3 20,-0.1 20,-0.1 -0.247 38.1 171.2 -56.6 140.1 0.6 -7.2 -0.0 8 8 A L - 0 0 57 18,-0.1 15,-0.5 2,-0.1 2,-0.5 -0.847 19.3-157.4-159.1 117.1 2.1 -4.5 -2.2 9 9 A E B +a 23 0A 158 17,-0.3 2,-0.3 -2,-0.3 15,-0.1 -0.841 30.8 141.7-100.2 127.9 5.7 -3.1 -2.2 10 10 A b - 0 0 13 13,-1.1 16,-0.3 -2,-0.5 17,-0.3 -0.972 46.6-134.3-156.0 166.8 6.3 0.3 -3.7 11 11 A K S S+ 0 0 191 -2,-0.3 2,-0.4 1,-0.2 -1,-0.2 0.928 90.0 52.6 -89.5 -67.2 8.3 3.5 -3.3 12 12 A K S > S- 0 0 154 1,-0.2 3,-1.9 11,-0.1 4,-0.4 -0.591 76.4-140.1 -76.0 125.9 5.9 6.4 -3.8 13 13 A D G > S+ 0 0 85 -2,-0.4 3,-1.9 1,-0.3 -1,-0.2 0.840 101.0 68.8 -53.2 -34.9 2.8 6.0 -1.6 14 14 A S G 3 S+ 0 0 101 1,-0.3 -1,-0.3 7,-0.1 6,-0.1 0.822 84.8 70.9 -53.4 -33.9 0.7 7.2 -4.6 15 15 A D G < S+ 0 0 113 -3,-1.9 -1,-0.3 7,-0.1 -2,-0.2 0.816 79.4 101.8 -53.6 -34.3 1.6 3.9 -6.3 16 16 A c S < S- 0 0 14 -3,-1.9 2,-0.2 -4,-0.4 6,-0.1 0.143 76.9-109.1 -45.9 169.7 -0.7 2.1 -3.8 17 17 A L S > S- 0 0 58 4,-0.2 3,-0.9 -13,-0.1 -1,-0.1 -0.672 71.9 -10.9-105.0 160.2 -4.2 1.0 -4.8 18 18 A A T 3 S- 0 0 70 -2,-0.2 2,-0.9 1,-0.2 -15,-0.1 -0.117 125.3 -27.5 50.1-147.8 -7.6 2.4 -3.8 19 19 A E T 3 S+ 0 0 138 -17,-0.0 -1,-0.2 2,-0.0 2,-0.2 -0.416 114.6 96.6 -95.5 58.8 -7.4 4.8 -0.9 20 20 A a < - 0 0 26 -2,-0.9 2,-0.3 -3,-0.9 -4,-0.1 -0.651 64.5-116.4-130.9-172.8 -4.2 3.4 0.7 21 21 A V - 0 0 64 -2,-0.2 8,-1.8 -6,-0.1 2,-0.4 -0.918 16.3-120.2-132.4 159.4 -0.5 4.0 0.7 22 22 A b E - B 0 28A 2 -2,-0.3 2,-0.3 6,-0.2 6,-0.2 -0.808 25.9-141.0 -99.4 134.9 2.7 2.3 -0.3 23 23 A L E >> -aB 9 27A 53 4,-2.5 -13,-1.1 -15,-0.5 3,-1.0 -0.760 12.1-132.8 -99.7 143.2 5.4 1.5 2.3 24 24 A E T 34 S+ 0 0 176 -2,-0.3 -1,-0.1 1,-0.3 -12,-0.0 0.905 107.5 58.5 -56.7 -46.2 9.1 1.8 1.7 25 25 A H T 34 S- 0 0 126 1,-0.1 -1,-0.3 2,-0.1 -16,-0.1 0.763 131.9 -90.3 -57.7 -22.5 9.8 -1.6 3.2 26 26 A G T <4 S+ 0 0 7 -3,-1.0 -17,-0.3 1,-0.3 2,-0.3 0.792 85.9 105.8 110.9 64.8 7.5 -3.0 0.5 27 27 A Y E < -B 23 0A 113 -4,-0.8 -4,-2.5 -17,-0.3 2,-0.6 -0.930 57.4-127.3-168.2 142.5 3.8 -3.1 1.6 28 28 A c E B 22 0A 22 -22,-0.3 -6,-0.2 -2,-0.3 -22,-0.2 -0.849 360.0 360.0 -99.1 120.0 0.6 -1.3 1.0 29 29 A G 0 0 67 -8,-1.8 -26,-0.2 -2,-0.6 -1,-0.2 0.827 360.0 360.0-102.0 360.0 -1.2 -0.1 4.2