REM -------------------------------------------------------------------- 1TVQ REM 1TVQ REM STRIDE: Knowledge-based secondary structure assignment 1TVQ REM Please cite: D.Frishman & P.Argos, Proteins XX, XXX-XXX, 1995 1TVQ REM 1TVQ REM Residue accessible surface area calculation 1TVQ REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 1TVQ REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 1TVQ REM 1TVQ REM ------------------------ General information ----------------------- 1TVQ REM 1TVQ HDR LIPID BINDING PROTEIN 30-JUN-04 1TVQ 1TVQ CMP MOL_ID: 1; 1TVQ CMP MOLECULE: FATTY ACID-BINDING PROTEIN; 1TVQ CMP CHAIN: A; 1TVQ CMP SYNONYM: L-FABP, LIVER BASIC FABP, LB- FABP, BILE ACID- 1TVQ CMP BINDING PROTEIN 1TVQ SRC MOL_ID: 1; 1TVQ SRC ORGANISM_SCIENTIFIC: GALLUS GALLUS; 1TVQ SRC ORGANISM_COMMON: CHICKEN; 1TVQ SRC TISSUE: LIVER 1TVQ AUT D.NICHESOLA,M.PERDUCA,S.CAPALDI,M.E.CARRIZO,P.G.RIGHETTI, 1TVQ AUT H.L.MONACO 1TVQ REM 1TVQ REM -------------------- Secondary structure summary ------------------- 1TVQ REM 1TVQ CHN /webclu/data/stride/pdb/pdb1tvq.ent A 1TVQ REM 1TVQ REM . . . . . 1TVQ SEQ 1 AFSGTWQVYAQENYEEFLKALALPEDLIKMARDIKPIVEIQQKGDDFVVT 50 1TVQ STR EEEEEEEEETHHHHHHHH HHHHHHHH EEEEEEETTEEEEE 1TVQ REM 1TVQ REM . . . . . 1TVQ SEQ 51 SKTPRQTVTNSFTLGKEADITTMDGKKLKCTVHLANGKLVTKSEKFSHEQ 100 1TVQ STR EEETTEEEEEEEETTB EEEETTTT EEEEEEEEETTEEEEEETTEEEEE 1TVQ REM 1TVQ REM . . 1TVQ SEQ 101 EVKGNEMVETITFGGVTLIRRSKRV 125 1TVQ STR EEETTEEEEEEEETTEEEEEEEEE 1TVQ REM 1TVQ REM 1TVQ REM 1TVQ LOC AlphaHelix TYR 14 A LEU 21 A 1TVQ LOC AlphaHelix GLU 25 A ARG 32 A 1TVQ LOC Strand GLY 4 A GLU 12 A 1TVQ LOC Strand ILE 37 A LYS 43 A 1TVQ LOC Strand ASP 46 A THR 53 A 1TVQ LOC Strand GLN 56 A THR 63 A 1TVQ LOC Strand ALA 68 A THR 71 A 1TVQ LOC Strand LYS 77 A ALA 85 A 1TVQ LOC Strand LYS 88 A SER 93 A 1TVQ LOC Strand PHE 96 A LYS 103 A 1TVQ LOC Strand GLU 106 A PHE 113 A 1TVQ LOC Strand VAL 116 A ARG 124 A 1TVQ LOC TurnIV GLN 11 A TYR 14 A 1TVQ LOC TurnII' LYS 43 A ASP 46 A 1TVQ LOC TurnI THR 53 A GLN 56 A 1TVQ LOC TurnII THR 63 A LYS 66 A 1TVQ LOC TurnI THR 72 A GLY 75 A 1TVQ LOC TurnIV LEU 84 A GLY 87 A 1TVQ LOC TurnI' ALA 85 A LYS 88 A 1TVQ LOC TurnI SER 93 A PHE 96 A 1TVQ LOC TurnII' LYS 103 A GLU 106 A 1TVQ LOC TurnIV THR 112 A GLY 115 A 1TVQ LOC TurnI' PHE 113 A VAL 116 A 1TVQ REM 1TVQ REM --------------- Detailed secondary structure assignment------------- 1TVQ REM 1TVQ REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 1TVQ ASG ALA A 1 1 C Coil 360.00 -26.36 94.2 1TVQ ASG PHE A 2 2 C Coil -92.48 -19.66 5.8 1TVQ ASG SER A 3 3 C Coil -57.77 137.77 53.6 1TVQ ASG GLY A 4 4 E Strand 136.52 -169.68 20.5 1TVQ ASG THR A 5 5 E Strand -111.10 123.70 35.4 1TVQ ASG TRP A 6 6 E Strand -119.40 121.89 0.0 1TVQ ASG GLN A 7 7 E Strand -98.24 115.68 67.3 1TVQ ASG VAL A 8 8 E Strand -66.61 129.47 1.4 1TVQ ASG TYR A 9 9 E Strand -115.93 -15.43 95.1 1TVQ ASG ALA A 10 10 E Strand -150.50 144.46 31.2 1TVQ ASG GLN A 11 11 E Strand -140.73 137.21 35.1 1TVQ ASG GLU A 12 12 E Strand -117.94 130.15 78.8 1TVQ ASG ASN A 13 13 T Turn 66.55 28.81 77.7 1TVQ ASG TYR A 14 14 H AlphaHelix -68.60 -39.59 14.7 1TVQ ASG GLU A 15 15 H AlphaHelix -62.48 -42.59 79.9 1TVQ ASG GLU A 16 16 H AlphaHelix -62.38 -41.64 98.7 1TVQ ASG PHE A 17 17 H AlphaHelix -61.81 -46.38 0.6 1TVQ ASG LEU A 18 18 H AlphaHelix -64.69 -36.46 1.0 1TVQ ASG LYS A 19 19 H AlphaHelix -67.85 -40.65 143.9 1TVQ ASG ALA A 20 20 H AlphaHelix -61.04 -29.16 30.9 1TVQ ASG LEU A 21 21 H AlphaHelix -81.30 -4.07 28.0 1TVQ ASG ALA A 22 22 C Coil 60.55 42.34 81.3 1TVQ ASG LEU A 23 23 C Coil -79.30 164.90 38.1 1TVQ ASG PRO A 24 24 C Coil -55.65 138.70 84.8 1TVQ ASG GLU A 25 25 H AlphaHelix -48.89 -44.54 163.5 1TVQ ASG ASP A 26 26 H AlphaHelix -71.40 -31.40 124.2 1TVQ ASG LEU A 27 27 H AlphaHelix -68.43 -44.07 40.6 1TVQ ASG ILE A 28 28 H AlphaHelix -58.73 -49.94 9.4 1TVQ ASG LYS A 29 29 H AlphaHelix -59.57 -39.14 137.2 1TVQ ASG MET A 30 30 H AlphaHelix -80.52 -26.48 93.3 1TVQ ASG ALA A 31 31 H AlphaHelix -99.18 -11.18 8.8 1TVQ ASG ARG A 32 32 H AlphaHelix -58.95 -19.54 99.5 1TVQ ASG ASP A 33 33 C Coil -113.56 5.33 108.3 1TVQ ASG ILE A 34 34 C Coil -75.96 126.26 39.2 1TVQ ASG LYS A 35 35 C Coil -115.35 120.96 88.3 1TVQ ASG PRO A 36 36 C Coil -85.84 170.19 0.6 1TVQ ASG ILE A 37 37 E Strand -109.44 127.00 54.8 1TVQ ASG VAL A 38 38 E Strand -114.85 126.45 4.6 1TVQ ASG GLU A 39 39 E Strand -100.98 130.73 58.5 1TVQ ASG ILE A 40 40 E Strand -124.63 125.31 2.3 1TVQ ASG GLN A 41 41 E Strand -110.94 125.60 96.0 1TVQ ASG GLN A 42 42 E Strand -122.86 119.85 60.2 1TVQ ASG LYS A 43 43 E Strand -134.29 95.93 155.4 1TVQ ASG GLY A 44 44 T Turn 69.69 -124.83 64.1 1TVQ ASG ASP A 45 45 T Turn -97.76 7.08 93.9 1TVQ ASG ASP A 46 46 E Strand -98.78 128.14 86.3 1TVQ ASG PHE A 47 47 E Strand -121.14 143.79 1.6 1TVQ ASG VAL A 48 48 E Strand -131.04 116.93 39.8 1TVQ ASG VAL A 49 49 E Strand -117.60 124.24 22.4 1TVQ ASG THR A 50 50 E Strand -125.49 114.31 18.0 1TVQ ASG SER A 51 51 E Strand -95.15 134.84 14.6 1TVQ ASG LYS A 52 52 E Strand -128.78 134.70 73.9 1TVQ ASG THR A 53 53 E Strand -139.48 163.57 19.6 1TVQ ASG PRO A 54 54 T Turn -56.24 -38.51 140.4 1TVQ ASG ARG A 55 55 T Turn -85.18 -19.06 132.3 1TVQ ASG GLN A 56 56 E Strand -162.21 145.23 75.5 1TVQ ASG THR A 57 57 E Strand -121.79 128.06 81.8 1TVQ ASG VAL A 58 58 E Strand -125.54 120.91 16.6 1TVQ ASG THR A 59 59 E Strand -108.52 143.26 78.1 1TVQ ASG ASN A 60 60 E Strand -142.04 147.21 30.4 1TVQ ASG SER A 61 61 E Strand -132.28 146.48 70.9 1TVQ ASG PHE A 62 62 E Strand -161.64 160.95 19.9 1TVQ ASG THR A 63 63 E Strand -124.34 130.39 35.0 1TVQ ASG LEU A 64 64 T Turn -52.36 131.77 22.4 1TVQ ASG GLY A 65 65 T Turn 84.91 -2.13 56.2 1TVQ ASG LYS A 66 66 B Bridge -121.62 123.16 134.8 1TVQ ASG GLU A 67 67 C Coil -52.05 133.43 124.1 1TVQ ASG ALA A 68 68 E Strand -124.30 153.93 11.0 1TVQ ASG ASP A 69 69 E Strand -95.08 111.77 94.4 1TVQ ASG ILE A 70 70 E Strand -110.67 144.21 17.4 1TVQ ASG THR A 71 71 E Strand -130.34 117.16 50.3 1TVQ ASG THR A 72 72 T Turn -77.05 165.87 18.0 1TVQ ASG MET A 73 73 T Turn -69.20 -17.39 26.8 1TVQ ASG ASP A 74 74 T Turn -91.86 11.43 21.4 1TVQ ASG GLY A 75 75 T Turn 80.04 -0.75 52.6 1TVQ ASG LYS A 76 76 C Coil -77.25 126.30 57.8 1TVQ ASG LYS A 77 77 E Strand -92.98 144.04 115.9 1TVQ ASG LEU A 78 78 E Strand -172.45 166.48 18.8 1TVQ ASG LYS A 79 79 E Strand -121.71 135.53 104.4 1TVQ ASG CYS A 80 80 E Strand -158.26 154.39 3.3 1TVQ ASG THR A 81 81 E Strand -105.93 105.98 58.1 1TVQ ASG VAL A 82 82 E Strand -72.66 137.56 1.0 1TVQ ASG HIS A 83 83 E Strand -143.20 164.04 85.4 1TVQ ASG LEU A 84 84 E Strand -93.24 134.83 82.3 1TVQ ASG ALA A 85 85 E Strand -126.92 99.23 38.6 1TVQ ASG ASN A 86 86 T Turn 50.54 48.97 174.4 1TVQ ASG GLY A 87 87 T Turn 87.98 -12.51 49.2 1TVQ ASG LYS A 88 88 E Strand -97.03 138.64 35.3 1TVQ ASG LEU A 89 89 E Strand -80.84 129.89 2.2 1TVQ ASG VAL A 90 90 E Strand -127.85 129.47 4.2 1TVQ ASG THR A 91 91 E Strand -126.75 109.08 16.4 1TVQ ASG LYS A 92 92 E Strand -126.38 136.62 106.3 1TVQ ASG SER A 93 93 E Strand -129.80 170.36 35.0 1TVQ ASG GLU A 94 94 T Turn -44.28 -49.79 175.5 1TVQ ASG LYS A 95 95 T Turn -118.22 12.26 143.5 1TVQ ASG PHE A 96 96 E Strand -130.93 138.21 8.6 1TVQ ASG SER A 97 97 E Strand -137.91 128.81 20.6 1TVQ ASG HIS A 98 98 E Strand -136.06 104.96 35.3 1TVQ ASG GLU A 99 99 E Strand -109.15 140.22 54.9 1TVQ ASG GLN A 100 100 E Strand -128.25 121.24 14.4 1TVQ ASG GLU A 101 101 E Strand -123.43 134.62 102.7 1TVQ ASG VAL A 102 102 E Strand -120.27 136.90 29.8 1TVQ ASG LYS A 103 103 E Strand -134.12 98.62 181.9 1TVQ ASG GLY A 104 104 T Turn 70.35 -128.15 56.6 1TVQ ASG ASN A 105 105 T Turn -98.82 22.52 88.5 1TVQ ASG GLU A 106 106 E Strand -117.47 140.02 70.1 1TVQ ASG MET A 107 107 E Strand -131.25 144.03 0.2 1TVQ ASG VAL A 108 108 E Strand -131.82 123.04 43.7 1TVQ ASG GLU A 109 109 E Strand -110.04 138.35 5.6 1TVQ ASG THR A 110 110 E Strand -121.94 112.87 50.6 1TVQ ASG ILE A 111 111 E Strand -119.79 121.36 5.0 1TVQ ASG THR A 112 112 E Strand -119.43 142.46 41.6 1TVQ ASG PHE A 113 113 E Strand -166.12 136.36 38.5 1TVQ ASG GLY A 114 114 T Turn 49.50 42.99 58.1 1TVQ ASG GLY A 115 115 T Turn 78.81 -4.56 79.4 1TVQ ASG VAL A 116 116 E Strand -107.99 130.90 28.2 1TVQ ASG THR A 117 117 E Strand -110.57 112.72 54.3 1TVQ ASG LEU A 118 118 E Strand -90.51 135.54 0.0 1TVQ ASG ILE A 119 119 E Strand -118.21 124.51 36.6 1TVQ ASG ARG A 120 120 E Strand -120.90 116.74 12.2 1TVQ ASG ARG A 121 121 E Strand -102.65 133.47 76.2 1TVQ ASG SER A 122 122 E Strand -133.63 156.54 0.0 1TVQ ASG LYS A 123 123 E Strand -129.84 143.69 86.2 1TVQ ASG ARG A 124 124 E Strand -65.66 138.45 104.8 1TVQ ASG VAL A 125 125 C Coil 38.16 360.00 134.7 1TVQ