==== 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 PEPTIDE BINDING/SIGNALING PROTEIN 26-FEB-02 1L2Z . COMPND 2 MOLECULE: CD2 ANTIGEN (CYTOPLASMIC TAIL)-BINDING PROTEIN 2; . SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; . AUTHOR C.FREUND,R.KUHNE,H.YANG,S.PARK,E.L.REINHERZ,G.WAGNER . 73 2 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 5228.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 32 43.8 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 . 11 15.1 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 . 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-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 . 6 8.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 6.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 9 12.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 1 1.4 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 1 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 . 2 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 ANTIPARALLEL BRIDGES PER LADDER . 0 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 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 D 0 0 166 0, 0.0 2,-0.3 0, 0.0 20,-0.0 0.000 360.0 360.0 360.0-177.9 -4.8 13.9 -0.7 2 2 A V - 0 0 51 2,-0.0 20,-1.4 41,-0.0 2,-0.1 -0.812 360.0-153.7-154.8 108.2 -5.6 10.3 -0.0 3 3 A M B -A 21 0A 77 -2,-0.3 40,-0.5 18,-0.3 2,-0.4 -0.356 8.1-154.4 -78.1 160.8 -3.4 7.8 1.8 4 4 A W - 0 0 6 16,-1.7 16,-0.4 14,-0.5 38,-0.3 -0.925 6.3-141.9-144.2 116.6 -3.5 4.1 1.2 5 5 A E E -B 41 0B 38 36,-3.0 36,-1.6 -2,-0.4 13,-0.4 -0.182 17.2-159.8 -68.2 165.3 -2.5 1.3 3.7 6 6 A Y E -BC 40 17B 0 11,-3.3 11,-1.7 34,-0.2 2,-0.5 -0.960 10.1-167.0-154.1 132.8 -0.8 -1.8 2.5 7 7 A K E -B 39 0B 17 32,-0.6 32,-3.4 -2,-0.3 9,-0.1 -0.981 16.5-150.0-124.7 125.8 -0.3 -5.3 4.0 8 8 A W S S+ 0 0 59 -2,-0.5 -1,-0.1 7,-0.3 2,-0.1 0.919 86.9 34.1 -56.5 -46.6 2.2 -7.8 2.7 9 9 A E S S- 0 0 94 6,-0.2 30,-0.3 2,-0.1 -2,-0.1 -0.362 81.1-122.7-100.8-177.2 -0.0 -10.8 3.7 10 10 A N S S+ 0 0 113 -2,-0.1 2,-0.2 28,-0.1 -2,-0.0 -0.185 70.9 111.4-120.4 38.8 -3.8 -11.2 3.9 11 11 A T S S- 0 0 61 4,-0.1 -2,-0.1 1,-0.1 0, 0.0 -0.673 74.6-121.4-109.4 166.0 -4.2 -12.1 7.5 12 12 A G S S+ 0 0 79 -2,-0.2 -1,-0.1 1,-0.2 -2,-0.0 0.502 115.1 43.5 -82.8 -3.8 -5.7 -10.2 10.5 13 13 A D S S+ 0 0 159 2,-0.1 -1,-0.2 0, 0.0 3,-0.1 0.637 87.0 113.3-110.3 -25.5 -2.4 -10.3 12.3 14 14 A A S S- 0 0 25 1,-0.1 2,-0.1 -7,-0.0 -7,-0.0 0.120 83.9 -73.7 -43.0 163.7 -0.0 -9.4 9.4 15 15 A E - 0 0 86 1,-0.1 2,-0.7 55,-0.0 -7,-0.3 -0.410 44.2-144.8 -67.1 136.9 1.8 -6.1 9.5 16 16 A L + 0 0 75 -3,-0.1 2,-0.2 -9,-0.1 -9,-0.2 -0.899 39.4 135.4-109.9 107.8 -0.3 -3.1 8.8 17 17 A Y B +C 6 0B 74 -11,-1.7 -11,-3.3 -2,-0.7 0, 0.0 -0.552 18.2 100.4-130.8-163.8 1.5 -0.3 6.9 18 18 A G + 0 0 0 -13,-0.4 -14,-0.5 -2,-0.2 25,-0.2 0.761 32.9 147.7 89.4 28.7 0.8 2.1 4.1 19 19 A P + 0 0 68 0, 0.0 2,-0.2 0, 0.0 -14,-0.1 0.103 45.4 108.1 -82.2 25.8 -0.0 5.3 6.1 20 20 A F S S- 0 0 49 -16,-0.4 -16,-1.7 1,-0.1 2,-0.0 -0.549 80.5 -85.0 -99.3 166.3 1.6 7.3 3.2 21 21 A T B >> -A 3 0A 45 -18,-0.2 4,-2.4 -2,-0.2 3,-0.9 -0.349 40.6-108.4 -69.2 150.0 -0.0 9.5 0.6 22 22 A S H 3> S+ 0 0 5 -20,-1.4 4,-2.9 1,-0.3 5,-0.2 0.808 122.7 60.9 -46.7 -30.3 -1.4 7.9 -2.6 23 23 A A H 3> S+ 0 0 61 2,-0.2 4,-1.6 1,-0.2 -1,-0.3 0.942 106.4 41.7 -63.1 -50.1 1.6 9.6 -4.2 24 24 A Q H <> S+ 0 0 59 -3,-0.9 4,-1.9 1,-0.2 -2,-0.2 0.864 115.9 51.1 -66.0 -36.6 4.1 7.8 -2.0 25 25 A M H X S+ 0 0 0 -4,-2.4 4,-3.5 1,-0.2 5,-0.3 0.916 106.0 53.9 -67.1 -44.3 2.2 4.5 -2.5 26 26 A Q H X S+ 0 0 72 -4,-2.9 4,-2.7 -5,-0.3 5,-0.3 0.876 107.2 53.6 -57.8 -38.6 2.1 4.9 -6.2 27 27 A T H X S+ 0 0 47 -4,-1.6 4,-4.4 2,-0.2 6,-0.2 0.974 115.6 36.3 -60.7 -57.8 5.9 5.2 -6.2 28 28 A W H X>S+ 0 0 4 -4,-1.9 5,-1.4 2,-0.2 4,-1.1 0.916 121.6 47.1 -62.2 -45.3 6.5 2.0 -4.3 29 29 A V H <5S+ 0 0 21 -4,-3.5 -1,-0.2 -5,-0.2 -2,-0.2 0.843 123.4 34.6 -65.7 -34.8 3.6 0.2 -6.0 30 30 A S H <5S+ 0 0 70 -4,-2.7 -2,-0.2 -5,-0.3 -3,-0.2 0.811 106.8 67.1 -88.6 -35.1 4.8 1.5 -9.4 31 31 A E H <5S- 0 0 107 -4,-4.4 -3,-0.2 -5,-0.3 -2,-0.2 0.805 116.3-109.0 -55.7 -30.1 8.6 1.4 -8.7 32 32 A G T <5S+ 0 0 44 -4,-1.1 -3,-0.2 -5,-0.2 -1,-0.1 0.424 80.9 130.4 113.3 2.6 8.2 -2.4 -8.5 33 33 A Y S -D 39 0B 53 -2,-0.3 3,-2.8 -13,-0.3 4,-0.3 -0.276 29.6-126.7 -57.0 136.9 -4.7 -5.9 -3.7 53 53 A S G > S+ 0 0 3 -15,-3.2 3,-1.1 1,-0.3 5,-0.2 0.812 112.8 60.2 -54.9 -30.8 -2.7 -2.9 -4.9 54 54 A K G 3 S+ 0 0 119 1,-0.2 -1,-0.3 -16,-0.2 -2,-0.1 0.569 103.7 51.6 -74.4 -8.3 -2.7 -4.5 -8.3 55 55 A R G < S+ 0 0 208 -3,-2.8 2,-0.3 -15,-0.0 -1,-0.2 0.349 98.0 83.0-107.8 2.7 -6.5 -4.3 -8.2 56 56 A I < - 0 0 28 -3,-1.1 2,-0.6 -4,-0.3 3,-0.1 -0.783 66.6-144.2-109.1 153.1 -6.6 -0.6 -7.3 57 57 A D > + 0 0 78 -2,-0.3 3,-2.0 1,-0.1 -3,-0.1 -0.783 18.4 175.0-118.5 87.0 -6.4 2.4 -9.7 58 58 A F G >> S+ 0 0 2 -2,-0.6 4,-2.2 1,-0.3 3,-1.5 0.754 77.1 73.6 -60.4 -24.0 -4.5 5.2 -7.9 59 59 A D G 34 S+ 0 0 122 1,-0.3 -1,-0.3 2,-0.2 -2,-0.0 0.730 89.8 59.2 -62.6 -21.8 -4.8 7.1 -11.2 60 60 A L G <4 S+ 0 0 120 -3,-2.0 -1,-0.3 1,-0.1 -2,-0.1 -0.019 113.5 36.1 -97.1 29.3 -8.4 7.7 -10.4 61 61 A Y T <4 0 0 117 -3,-1.5 -2,-0.2 1,-0.3 -1,-0.1 0.466 360.0 360.0-142.8 -46.1 -7.7 9.5 -7.2 62 62 A T < 0 0 129 -4,-2.2 -1,-0.3 -40,-0.1 0, 0.0 -0.553 360.0 360.0 -72.9 360.0 -4.5 11.6 -7.6 63 !* 0 0 0 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 360.0 0.0 0.0 0.0 64 63 B S 0 0 164 0, 0.0 0, 0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -65.4 12.3 11.9 -6.8 65 64 B H - 0 0 173 1,-0.0 0, 0.0 0, 0.0 0, 0.0 0.028 360.0-159.4 -62.4 177.4 14.0 9.1 -4.8 66 65 B R - 0 0 71 -39,-0.0 -1,-0.0 -38,-0.0 -42,-0.0 -0.989 16.8-103.5-160.3 155.5 12.3 7.5 -1.7 67 66 B P - 0 0 79 0, 0.0 0, 0.0 0, 0.0 0, 0.0 -0.259 53.1 -77.0 -77.6 167.4 13.1 5.4 1.4 68 67 B P - 0 0 98 0, 0.0 -40,-0.0 0, 0.0 0, 0.0 -0.441 51.7-115.0 -67.4 132.8 12.5 1.7 1.9 69 68 B P - 0 0 5 0, 0.0 -3,-0.0 0, 0.0 3,-0.0 -0.244 36.7 -95.8 -65.7 155.7 8.8 0.8 2.7 70 69 B P S S+ 0 0 33 0, 0.0 2,-2.0 0, 0.0 -53,-0.1 0.087 99.3 36.8 -61.4-179.4 7.9 -0.7 6.1 71 70 B G S S+ 0 0 7 -55,-0.1 -55,-0.0 -64,-0.0 -64,-0.0 -0.515 74.8 148.7 76.8 -80.1 7.5 -4.4 6.7 72 71 B H - 0 0 118 -2,-2.0 2,-0.1 1,-0.1 -64,-0.1 0.157 39.9-129.4 42.0-163.8 10.3 -5.6 4.5 73 72 B R 0 0 193 0, 0.0 -1,-0.1 0, 0.0 0, 0.0 -0.481 360.0 360.0 176.0 106.6 12.2 -8.8 5.5 74 73 B V 0 0 199 -2,-0.1 -2,-0.0 0, 0.0 0, 0.0 0.437 360.0 360.0-135.5 360.0 15.9 -9.4 5.7