==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=22-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER LIPID BINDING PROTEIN 16-OCT-98 3IFB . COMPND 2 MOLECULE: INTESTINAL FATTY ACID BINDING PROTEIN; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR F.ZHANG,C.LUECKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON . 131 1 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 7479.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 99 75.6 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 . 68 51.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 1 0.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 1 0.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 4 3.1 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 . 10 7.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 10 7.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 12 9.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 1.5 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 1 1 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 0 2 0 3 2 2 1 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 0 0 0 0 0 0 0 0 0 1 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 A 0 0 113 0, 0.0 3,-0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -62.2 14.9 -11.5 -11.0 2 2 A F + 0 0 25 1,-0.1 40,-0.5 39,-0.1 2,-0.2 0.861 360.0 105.5 44.1 49.2 11.7 -9.5 -11.4 3 3 A D E +A 41 0A 89 38,-0.2 2,-0.3 2,-0.1 38,-0.2 -0.778 53.5 107.9-158.2 103.5 11.0 -9.6 -7.6 4 4 A S E S-A 40 0A 12 36,-1.2 36,-2.0 -2,-0.2 2,-0.5 -0.957 72.8 -81.3-164.4 164.0 11.7 -6.3 -6.0 5 5 A T E -A 39 0A 42 -2,-0.3 126,-0.5 34,-0.2 2,-0.3 -0.863 50.3-179.1 -81.2 134.0 10.7 -3.0 -4.4 6 6 A W E -AB 38 130A 0 32,-3.1 32,-1.1 -2,-0.5 2,-0.3 -0.880 4.3-172.3-118.4 165.3 9.8 -0.8 -7.3 7 7 A K E -AB 37 129A 63 122,-1.6 122,-2.1 -2,-0.3 30,-0.2 -0.975 37.0 -76.5-150.9 159.5 8.7 2.8 -6.9 8 8 A V E + B 0 128A 26 28,-2.1 120,-0.3 -2,-0.3 3,-0.1 -0.292 43.4 167.9 -59.9 136.5 7.3 5.5 -9.2 9 9 A D E - 0 0 56 118,-2.8 2,-0.3 1,-0.5 119,-0.2 0.752 66.0 -7.8-104.7 -64.8 9.9 7.1 -11.4 10 10 A R E - B 0 127A 147 117,-1.5 117,-1.9 2,-0.0 -1,-0.5 -0.793 57.2-165.4-126.7 168.6 7.8 9.1 -13.9 11 11 A S E - B 0 126A 54 -2,-0.3 2,-0.3 115,-0.2 115,-0.2 -0.978 1.4-167.2-153.8 154.9 4.1 9.5 -14.8 12 12 A E E S+ B 0 125A 102 113,-2.3 113,-1.8 -2,-0.3 5,-0.1 -0.988 75.3 0.6-147.9 146.0 2.2 11.0 -17.8 13 13 A N S > S+ 0 0 83 -2,-0.3 4,-1.2 111,-0.2 -1,-0.1 0.853 89.4 133.6 33.9 44.0 -1.4 11.9 -18.3 14 14 A Y H > S+ 0 0 50 2,-0.2 4,-1.6 3,-0.2 -1,-0.1 0.810 73.7 34.8 -88.3 -29.5 -1.7 10.6 -14.7 15 15 A D H > S+ 0 0 90 2,-0.2 4,-3.6 3,-0.2 5,-0.2 0.845 117.1 54.5 -87.7 -39.6 -3.8 13.5 -13.4 16 16 A K H > S+ 0 0 81 1,-0.2 4,-1.7 2,-0.2 -2,-0.2 0.959 113.7 44.2 -49.3 -51.9 -5.6 13.8 -16.8 17 17 A F H X S+ 0 0 9 -4,-1.2 4,-0.7 2,-0.2 3,-0.2 0.933 112.9 48.5 -61.5 -48.1 -6.4 10.1 -16.3 18 18 A M H >X>S+ 0 0 26 -4,-1.6 3,-1.7 1,-0.3 5,-1.0 0.943 105.6 58.7 -63.0 -42.8 -7.4 10.4 -12.6 19 19 A E H ><5S+ 0 0 99 -4,-3.6 3,-1.2 1,-0.3 4,-0.5 0.915 109.5 47.3 -45.7 -44.0 -9.6 13.4 -13.5 20 20 A K H 3<5S+ 0 0 95 -4,-1.7 -1,-0.3 1,-0.3 -2,-0.2 0.484 92.8 71.1 -87.1 0.1 -11.3 10.9 -15.7 21 21 A M H <<5S- 0 0 16 -3,-1.7 -1,-0.3 -4,-0.7 -2,-0.2 0.581 117.9-114.0 -67.5 -11.6 -11.6 8.1 -13.2 22 22 A G T <<5 + 0 0 47 -3,-1.2 -2,-0.2 -4,-0.6 -3,-0.2 0.963 68.6 150.9 64.6 54.3 -14.1 10.7 -11.9 23 23 A V < - 0 0 23 -5,-1.0 2,-0.3 -4,-0.5 3,-0.1 0.086 46.9-109.2 -83.6-153.5 -11.9 11.1 -8.9 24 24 A N >> - 0 0 85 1,-0.1 3,-1.6 -2,-0.1 4,-1.4 -0.991 21.9 -98.2-146.8 159.6 -12.4 14.7 -7.6 25 25 A I H 3> S+ 0 0 97 -2,-0.3 4,-1.5 1,-0.3 -1,-0.1 0.753 118.5 48.5 -36.5 -51.7 -10.2 17.8 -7.6 26 26 A V H 3> S+ 0 0 90 1,-0.3 4,-0.9 2,-0.3 -1,-0.3 0.828 104.5 58.1 -75.5 -27.5 -8.9 17.5 -4.1 27 27 A K H X> S+ 0 0 46 -3,-1.6 4,-2.8 1,-0.2 3,-1.9 0.984 110.9 46.5 -52.2 -55.3 -7.9 13.8 -4.5 28 28 A R H 3X S+ 0 0 63 -4,-1.4 4,-3.1 1,-0.3 -2,-0.3 0.784 97.4 68.3 -56.7 -32.8 -5.8 15.1 -7.3 29 29 A K H 3< S+ 0 0 132 -4,-1.5 -1,-0.3 1,-0.2 -2,-0.2 0.749 117.2 28.5 -66.8 -17.8 -4.4 18.0 -5.3 30 30 A L H X< S+ 0 0 63 -3,-1.9 3,-2.8 -4,-0.9 -2,-0.3 0.692 109.6 65.4-101.7 -29.9 -2.7 15.2 -3.4 31 31 A A H >X S+ 0 0 26 -4,-2.8 3,-2.0 1,-0.3 4,-0.8 0.937 93.8 70.2 -54.5 -38.1 -2.4 12.6 -6.2 32 32 A A T 3< S+ 0 0 79 -4,-3.1 -1,-0.3 1,-0.3 -2,-0.1 0.757 117.3 16.8 -23.7 -47.2 -0.2 15.4 -7.4 33 33 A H T <4 S+ 0 0 133 -3,-2.8 -1,-0.3 -5,-0.1 -2,-0.2 -0.105 103.0 92.4-138.5 28.4 2.2 14.5 -4.7 34 34 A D T <4 - 0 0 7 -3,-2.0 20,-0.6 -6,-0.1 -3,-0.1 0.848 64.6-163.8 -94.8 -44.7 1.2 11.0 -3.6 35 35 A N < - 0 0 101 -4,-0.8 19,-0.5 18,-0.1 20,-0.3 -0.159 7.5-126.3 79.2 178.6 3.3 8.8 -5.8 36 36 A L + 0 0 27 17,-0.2 -28,-2.1 18,-0.1 2,-0.3 -0.972 28.5 162.4-163.2 148.1 2.8 5.1 -6.5 37 37 A K E -AC 7 52A 67 15,-1.8 15,-1.5 -2,-0.3 2,-0.3 -0.954 24.3-122.3-156.1-177.1 4.8 1.8 -6.2 38 38 A L E -AC 6 51A 0 -32,-1.1 -32,-3.1 -2,-0.3 2,-0.4 -0.982 9.7-168.7-125.6 150.6 5.2 -1.9 -6.1 39 39 A T E -AC 5 50A 47 11,-2.0 11,-2.3 -2,-0.3 2,-0.3 -0.913 36.3-175.9-109.6 104.6 6.7 -4.4 -3.8 40 40 A I E +AC 4 49A 0 -36,-2.0 -36,-1.2 -2,-0.4 9,-0.2 -0.739 14.5 168.4 -97.2 148.3 6.3 -7.2 -6.4 41 41 A T E -AC 3 48A 59 7,-1.4 7,-1.3 -2,-0.3 -38,-0.2 -0.659 16.2-159.6-160.1 92.2 7.2 -10.7 -5.4 42 42 A Q E + C 0 47A 50 -40,-0.5 5,-0.3 5,-0.2 2,-0.2 -0.352 13.9 177.8 -72.6 162.7 6.3 -13.5 -7.7 43 43 A E E > - C 0 46A 133 3,-1.4 3,-2.5 20,-0.1 2,-0.4 -0.649 57.6 -9.5-144.6-165.7 6.1 -17.0 -6.3 44 44 A G T 3 S- 0 0 45 1,-0.3 3,-0.1 -2,-0.2 -1,-0.0 -0.096 131.8 -43.5 -38.8 89.2 5.1 -20.5 -7.7 45 45 A N T 3 S+ 0 0 102 -2,-0.4 -1,-0.3 1,-0.2 2,-0.2 0.782 123.1 111.5 52.8 32.2 3.7 -19.1 -11.1 46 46 A K E < -C 43 0A 76 -3,-2.5 -3,-1.4 2,-0.0 2,-0.4 -0.781 61.7-132.6-136.6 174.2 2.0 -16.4 -9.0 47 47 A F E -CD 42 62A 3 15,-3.0 15,-2.3 -5,-0.3 2,-0.9 -0.945 8.5-171.3-136.6 108.5 2.1 -12.7 -8.3 48 48 A T E -CD 41 61A 39 -7,-1.3 -7,-1.4 -2,-0.4 2,-1.0 -0.881 20.7-174.5 -94.9 102.6 2.1 -10.9 -5.0 49 49 A V E -CD 40 60A 2 11,-1.4 11,-1.3 -2,-0.9 2,-1.2 -0.773 7.0-170.4-105.3 87.6 1.6 -7.4 -6.3 50 50 A K E -CD 39 59A 96 -11,-2.3 -11,-2.0 -2,-1.0 2,-0.3 -0.647 14.2-177.1 -84.1 98.1 1.9 -5.1 -3.3 51 51 A E E +CD 38 58A 18 7,-1.5 7,-3.2 -2,-1.2 2,-0.3 -0.795 8.1 167.2-107.0 138.9 0.8 -1.9 -4.9 52 52 A S E +C 37 0A 26 -15,-1.5 -15,-1.8 -2,-0.3 2,-0.3 -0.976 19.4 170.5-157.3 160.3 0.8 1.3 -2.8 53 53 A S - 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