==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=13-NOV-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER SUGAR BINDING PROTEIN 22-NOV-99 1DFV . COMPND 2 MOLECULE: HUMAN NEUTROPHIL GELATINASE; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR D.H.GOETZ,S.T.WILLIE,R.S.ARMEN,T.BRATT,N.BORREGAARD,R.K.STRO . 347 2 2 2 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 18321.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 237 68.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 4 1.2 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 129 37.2 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 4 1.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 6 1.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 1 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . 1 0.3 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 . 40 11.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 29 8.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 25 7.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 0.6 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 2 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 2 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 3 4 2 0 4 0 2 2 2 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 0 0 0 0 0 0 0 1 1 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 5 A S 0 0 75 0, 0.0 248,-0.8 0, 0.0 2,-0.3 0.000 360.0 360.0 360.0 99.4 95.2 28.0 51.2 2 6 A D E -A 248 0A 99 246,-0.2 2,-0.3 244,-0.0 246,-0.2 -0.692 360.0-172.7 -91.5 136.5 95.7 27.8 55.0 3 7 A L E -A 247 0A 16 244,-2.6 244,-3.7 -2,-0.3 33,-0.1 -0.942 30.8-114.5-132.5 150.0 92.9 27.2 57.5 4 8 A I - 0 0 16 -2,-0.3 242,-0.2 31,-0.3 31,-0.1 -0.684 53.9-103.1 -78.1 125.0 92.3 27.1 61.3 5 9 A P - 0 0 41 0, 0.0 -1,-0.1 0, 0.0 123,-0.1 -0.254 35.1-104.3 -55.2 125.7 91.4 23.5 62.1 6 10 A A - 0 0 18 121,-0.1 340,-0.1 1,-0.1 114,-0.1 -0.204 44.7-108.8 -49.3 135.9 87.7 22.7 62.7 7 11 A P - 0 0 7 0, 0.0 2,-0.6 0, 0.0 -1,-0.1 -0.302 37.1 -95.6 -67.5 154.5 87.2 22.3 66.4 8 12 A P > - 0 0 76 0, 0.0 3,-3.9 0, 0.0 4,-0.2 -0.651 32.1-122.9 -79.7 119.8 86.4 18.8 67.7 9 13 A L G > S+ 0 0 57 -2,-0.6 3,-3.6 1,-0.3 -3,-0.0 0.684 108.0 72.3 -24.6 -44.8 82.7 18.3 68.1 10 14 A S G 3 S+ 0 0 119 1,-0.3 -1,-0.3 3,-0.0 0, 0.0 0.662 95.5 56.3 -53.4 -15.1 83.1 17.4 71.8 11 15 A K G < S+ 0 0 114 -3,-3.9 -1,-0.3 1,-0.1 -2,-0.2 0.397 91.7 81.5 -96.9 -0.4 83.8 21.2 72.1 12 16 A V S < S- 0 0 2 -3,-3.6 -1,-0.1 -4,-0.2 106,-0.0 -0.896 75.4-142.7-113.7 103.9 80.5 22.2 70.5 13 17 A P - 0 0 67 0, 0.0 2,-0.4 0, 0.0 -2,-0.1 -0.058 7.5-136.9 -58.3 160.3 77.5 22.1 72.9 14 18 A L - 0 0 49 73,-0.0 2,-0.3 4,-0.0 93,-0.2 -0.987 29.3-102.6-123.3 131.4 74.0 20.9 71.8 15 19 A Q > - 0 0 38 91,-3.0 3,-0.6 -2,-0.4 93,-0.1 -0.378 40.6-123.7 -56.8 113.4 70.9 22.8 72.8 16 20 A Q T 3 S+ 0 0 150 -2,-0.3 -1,-0.1 1,-0.2 70,-0.0 -0.329 89.0 5.2 -56.2 134.2 69.3 20.8 75.6 17 21 A N T 3 S- 0 0 119 1,-0.1 -1,-0.2 68,-0.1 2,-0.2 0.952 87.0-153.9 57.2 56.2 65.7 19.8 74.8 18 22 A F < - 0 0 17 -3,-0.6 2,-0.7 67,-0.3 -1,-0.1 -0.441 7.3-157.6 -69.5 132.5 65.6 21.2 71.2 19 23 A Q > - 0 0 83 -2,-0.2 4,-1.4 1,-0.1 3,-0.4 -0.867 4.5-168.2-110.7 97.4 62.1 22.2 69.9 20 24 A D T 4 S+ 0 0 44 -2,-0.7 -1,-0.1 1,-0.2 34,-0.1 0.724 86.0 54.8 -59.0 -22.3 62.1 22.3 66.1 21 25 A N T >4 S+ 0 0 83 1,-0.2 3,-1.0 2,-0.1 -1,-0.2 0.903 107.8 47.2 -78.7 -40.1 58.7 24.0 66.0 22 26 A Q T 34 S+ 0 0 92 -3,-0.4 -2,-0.2 1,-0.2 -1,-0.2 0.721 103.2 63.0 -71.4 -25.1 59.8 27.0 68.2 23 27 A F T 3< S+ 0 0 1 -4,-1.4 -1,-0.2 86,-0.0 29,-0.2 0.473 84.1 112.2 -80.9 0.2 63.0 27.5 66.2 24 28 A Q < + 0 0 70 -3,-1.0 29,-0.2 27,-0.1 2,-0.2 -0.183 51.1 44.9 -69.3 163.9 60.9 28.3 63.2 25 29 A G E S-K 52 0B 28 27,-2.6 27,-2.5 2,-0.0 2,-0.4 -0.509 92.5 -22.5 105.3-171.1 60.7 31.7 61.6 26 30 A K E -K 51 0B 61 25,-0.2 2,-0.4 -2,-0.2 25,-0.2 -0.671 52.0-170.6 -86.5 132.6 63.0 34.6 60.5 27 31 A W E -K 50 0B 0 23,-2.3 23,-2.3 -2,-0.4 2,-0.5 -0.978 15.4-139.1-125.8 131.8 66.4 34.9 62.1 28 32 A Y E -KL 49 135B 25 107,-4.1 107,-2.6 -2,-0.4 2,-1.5 -0.756 15.5-133.8 -91.2 131.1 68.8 37.9 61.8 29 33 A V E + L 0 134B 0 19,-2.1 19,-0.4 -2,-0.5 105,-0.2 -0.660 41.5 156.9 -83.3 90.5 72.4 37.0 61.4 30 34 A V E + 0 0 7 103,-1.7 2,-0.4 -2,-1.5 -1,-0.2 0.650 62.9 39.1 -90.3 -14.9 73.9 39.5 63.8 31 35 A G E + L 0 133B 0 102,-1.6 102,-3.1 -3,-0.2 2,-0.4 -0.984 60.8 179.5-141.6 130.8 77.1 37.6 64.4 32 36 A L E +ML 163 132B 4 131,-3.3 131,-3.7 -2,-0.4 2,-0.3 -0.990 8.5 159.6-133.2 132.4 79.4 35.6 62.1 33 37 A A E +ML 162 131B 0 98,-1.7 98,-3.2 -2,-0.4 2,-0.3 -0.983 11.9 136.4-150.4 135.6 82.7 33.8 62.8 34 38 A G E > - L 0 130B 0 127,-1.4 3,-1.7 3,-0.3 96,-0.2 -0.983 62.3-100.9-169.5 165.1 84.5 31.0 61.0 35 39 A N T 3 S+ 0 0 6 94,-1.6 -31,-0.3 -2,-0.3 95,-0.1 0.646 129.0 41.4 -70.6 -11.6 87.9 29.8 59.8 36 40 A A T 3 S+ 0 0 51 93,-0.5 2,-0.5 125,-0.1 -1,-0.3 0.074 96.3 101.6-117.8 19.5 86.9 31.2 56.4 37 41 A I < - 0 0 27 -3,-1.7 2,-0.4 124,-0.1 -3,-0.3 -0.928 52.0-170.1-110.1 120.2 85.4 34.4 57.8 38 42 A L - 0 0 115 -2,-0.5 2,-2.1 -5,-0.1 123,-0.2 -0.940 27.7-126.2-121.4 132.3 87.4 37.6 57.6 39 43 A R - 0 0 117 121,-1.8 122,-0.1 -2,-0.4 2,-0.1 -0.422 36.0-167.4 -68.2 73.1 86.8 41.0 59.3 40 44 A E - 0 0 55 -2,-2.1 5,-0.2 3,-0.2 -1,-0.0 -0.362 13.9-174.8 -65.5 142.7 86.9 43.2 56.1 41 45 A D S S+ 0 0 120 2,-0.1 -1,-0.1 3,-0.1 -2,-0.0 0.670 76.8 59.5-111.7 -24.7 87.2 47.0 56.7 42 46 A K S S+ 0 0 108 1,-0.3 -1,-0.1 0, 0.0 -2,-0.1 0.572 129.2 11.5 -80.6 -9.4 87.0 48.5 53.2 43 47 A D S S- 0 0 125 3,-0.0 -1,-0.3 2,-0.0 -3,-0.2 -0.333 85.0-152.7-167.3 70.7 83.5 46.9 52.8 44 48 A P - 0 0 69 0, 0.0 -3,-0.1 0, 0.0 -5,-0.1 -0.128 33.2 -92.6 -53.3 141.7 82.1 45.4 56.0 45 49 A Q - 0 0 83 -5,-0.2 121,-2.1 1,-0.1 2,-0.2 -0.281 38.8-133.8 -58.4 133.7 79.6 42.5 55.7 46 50 A K B -t 166 0C 87 119,-0.3 2,-0.2 21,-0.1 -1,-0.1 -0.561 28.1 -99.0 -86.8 154.9 76.0 43.5 55.5 47 51 A M - 0 0 3 119,-2.0 20,-0.3 -2,-0.2 2,-0.3 -0.516 42.8-177.5 -75.2 138.2 73.4 41.7 57.6 48 52 A Y - 0 0 21 -19,-0.4 -19,-2.1 -2,-0.2 2,-0.3 -0.788 14.8-131.2-125.8 172.3 71.4 39.0 55.9 49 53 A A E -KN 28 65B 0 16,-2.3 16,-2.4 -2,-0.3 2,-0.4 -0.884 6.9-153.5-129.3 161.8 68.6 36.8 57.2 50 54 A T E -KN 27 64B 3 -23,-2.3 -23,-2.3 -2,-0.3 2,-0.5 -0.995 7.8-155.2-136.6 126.9 67.7 33.2 57.3 51 55 A I E -KN 26 63B 36 12,-3.1 12,-2.0 -2,-0.4 2,-0.5 -0.910 7.1-156.5-107.3 124.2 64.1 31.7 57.5 52 56 A Y E -KN 25 62B 3 -27,-2.5 -27,-2.6 -2,-0.5 2,-0.4 -0.849 12.1-177.8-101.5 128.4 63.6 28.3 58.9 53 57 A E E - N 0 61B 92 8,-0.5 8,-2.2 -2,-0.5 2,-0.1 -0.977 21.5-133.2-131.4 122.7 60.4 26.3 58.0 54 58 A L E - N 0 60B 33 -2,-0.4 2,-0.3 6,-0.2 6,-0.2 -0.448 17.0-154.1 -70.7 140.0 59.4 22.9 59.2 55 59 A K > - 0 0 59 4,-2.3 3,-1.7 -2,-0.1 -1,-0.0 -0.723 32.2-108.0-105.4 162.0 58.2 20.4 56.6 56 60 A E T 3 S+ 0 0 196 1,-0.3 -1,-0.1 -2,-0.3 -2,-0.0 0.792 121.9 62.9 -64.7 -22.7 55.8 17.7 57.6 57 61 A D T 3 S- 0 0 101 2,-0.1 -1,-0.3 1,-0.1 3,-0.1 0.175 122.8-111.3 -84.5 20.2 58.6 15.2 57.3 58 62 A K S < S+ 0 0 108 -3,-1.7 2,-0.2 1,-0.2 -2,-0.2 0.613 77.8 129.1 60.9 18.1 60.2 17.3 60.1 59 63 A S - 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