==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=14-JUN-2013 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER IMMUNE SYSTEM 18-OCT-10 3P9L . COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR R.WESSELINGH,S.GRAS,C.GUILLONNEAU,S.J.TURNER,J.ROSSJOHN . 770 6 6 6 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 38859.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 490 63.6 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 . 269 34.9 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 8 1.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 10 1.3 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 . 43 5.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 55 7.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 115 14.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 8 1.0 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 2 0 1 2 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 2 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 . 5 12 5 4 0 8 0 6 3 3 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 4 4 0 0 2 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 G 0 0 59 0, 0.0 2,-0.2 0, 0.0 104,-0.1 0.000 360.0 360.0 360.0-179.1 3.5 -6.0 42.0 2 2 A P + 0 0 99 0, 0.0 2,-0.3 0, 0.0 102,-0.2 0.578 360.0 163.6 -77.4 161.7 3.8 -3.6 40.6 3 3 A H E -A 103 0A 27 100,-2.6 100,-3.2 -2,-0.2 2,-0.3 -0.935 19.1-156.3-137.2 165.8 0.8 -4.0 38.2 4 4 A S E -A 102 0A 5 -2,-0.3 25,-2.2 98,-0.2 2,-0.5 -0.995 11.4-161.8-144.1 143.8 -1.2 -1.8 36.0 5 5 A L E +AB 101 28A 0 96,-2.3 96,-2.0 -2,-0.3 2,-0.4 -0.972 27.5 176.7-125.2 112.7 -4.6 -1.7 34.5 6 6 A R E -AB 100 27A 40 21,-2.6 21,-3.2 -2,-0.5 2,-0.4 -0.925 17.6-165.5-123.7 143.1 -4.8 0.7 31.5 7 7 A Y E -AB 99 26A 0 92,-2.5 92,-2.1 -2,-0.4 2,-0.5 -0.995 3.0-164.1-127.3 135.1 -7.4 1.7 29.0 8 8 A F E -AB 98 25A 38 17,-2.8 17,-2.4 -2,-0.4 2,-0.4 -0.980 13.2-169.1-116.4 123.2 -6.8 3.5 25.8 9 9 A V E -AB 97 24A 1 88,-2.8 88,-2.2 -2,-0.5 2,-0.4 -0.936 6.7-176.6-119.9 136.7 -9.9 5.0 24.2 10 10 A T E -AB 96 23A 23 13,-2.0 13,-2.5 -2,-0.4 2,-0.4 -0.999 5.7-177.4-133.1 136.2 -10.3 6.5 20.7 11 11 A A E -AB 95 22A 1 84,-2.2 84,-2.4 -2,-0.4 2,-0.5 -0.981 9.2-178.3-133.9 117.6 -13.3 8.2 19.1 12 12 A V E -AB 94 21A 16 9,-2.7 9,-3.0 -2,-0.4 82,-0.2 -0.971 12.5-150.7-125.6 122.1 -13.0 9.3 15.5 13 13 A S - 0 0 17 80,-2.3 6,-0.1 -2,-0.5 -2,-0.0 -0.449 13.1-179.2 -85.3 161.4 -15.7 11.1 13.6 14 14 A R > - 0 0 47 4,-0.4 3,-2.4 78,-0.1 4,-0.3 -0.458 21.8-148.2-158.5 72.2 -16.1 10.9 9.8 15 15 A P T 3 S+ 0 0 53 0, 0.0 4,-0.1 0, 0.0 77,-0.1 -0.151 81.5 10.4 -55.8 138.9 -19.1 13.0 8.8 16 16 A G T 3 S+ 0 0 84 2,-0.1 3,-0.1 1,-0.1 74,-0.0 0.293 119.1 75.6 78.1 -8.7 -21.0 11.7 5.8 17 17 A L S < S- 0 0 133 -3,-2.4 2,-0.2 1,-0.4 -1,-0.1 0.317 107.7 -69.8-118.3 7.5 -19.1 8.5 5.9 18 18 A G S S- 0 0 41 -4,-0.3 -1,-0.4 3,-0.0 -4,-0.4 -0.748 70.3 -39.7 132.2 179.0 -20.7 6.6 8.8 19 19 A E S S- 0 0 95 -2,-0.2 -7,-0.0 1,-0.2 3,-0.0 -0.321 78.8 -78.2 -70.2 161.2 -20.9 6.8 12.6 20 20 A P - 0 0 25 0, 0.0 2,-0.6 0, 0.0 -7,-0.3 -0.316 46.9-117.5 -57.2 146.9 -17.8 7.8 14.6 21 21 A R E -B 12 0A 104 -9,-3.0 -9,-2.7 -3,-0.1 2,-0.4 -0.813 36.7-169.1 -89.1 122.6 -15.4 4.9 15.0 22 22 A Y E +B 11 0A 3 -2,-0.6 16,-2.9 -11,-0.2 2,-0.4 -0.932 8.2 178.9-121.2 139.7 -15.0 4.1 18.7 23 23 A M E -BC 10 37A 46 -13,-2.5 -13,-2.0 -2,-0.4 2,-0.4 -0.999 15.8-169.5-144.4 133.5 -12.5 1.8 20.4 24 24 A E E -BC 9 36A 0 12,-2.2 12,-2.6 -2,-0.4 2,-0.5 -0.997 13.7-176.6-117.9 127.3 -11.7 0.7 23.9 25 25 A V E -BC 8 35A 9 -17,-2.4 -17,-2.8 -2,-0.4 2,-0.4 -0.986 6.8-160.8-126.8 124.5 -8.4 -1.1 24.4 26 26 A G E -BC 7 34A 0 8,-2.1 7,-2.4 -2,-0.5 8,-1.1 -0.863 3.9-166.2-109.9 140.7 -7.4 -2.5 27.7 27 27 A Y E -BC 6 32A 29 -21,-3.2 -21,-2.6 -2,-0.4 2,-0.7 -0.982 11.5-161.0-124.4 125.2 -3.9 -3.6 28.9 28 28 A V E > S-BC 5 31A 0 3,-2.2 3,-1.0 -2,-0.4 -23,-0.2 -0.936 92.1 -16.0 -97.7 115.7 -3.0 -5.6 32.0 29 29 A D T 3 S- 0 0 22 -25,-2.2 -1,-0.2 -2,-0.7 -24,-0.1 0.918 129.8 -53.0 51.6 51.5 0.7 -4.8 32.6 30 30 A D T 3 S+ 0 0 104 -3,-0.3 2,-0.5 1,-0.2 -1,-0.2 0.606 116.0 112.7 68.2 13.5 1.1 -3.3 29.1 31 31 A T E < S-C 28 0A 34 -3,-1.0 -3,-2.2 18,-0.0 -1,-0.2 -0.977 72.9-118.7-118.9 121.7 -0.3 -6.4 27.4 32 32 A E E +C 27 0A 40 -2,-0.5 -5,-0.3 -5,-0.2 3,-0.1 -0.326 41.6 161.1 -61.0 128.7 -3.6 -6.1 25.6 33 33 A F E + 0 0 0 -7,-2.4 15,-2.8 1,-0.3 16,-0.9 0.553 60.9 23.9-125.4 -15.7 -6.3 -8.3 27.2 34 34 A V E -CD 26 47A 0 -8,-1.1 -8,-2.1 13,-0.3 -1,-0.3 -0.982 57.9-177.8-147.6 158.4 -9.6 -6.9 26.0 35 35 A R E -CD 25 46A 12 11,-1.4 11,-1.8 -2,-0.3 2,-0.5 -0.944 13.5-163.4-160.5 135.1 -10.9 -4.7 23.1 36 36 A F E -C 24 0A 0 -12,-2.6 -12,-2.2 -2,-0.3 2,-0.5 -0.993 11.7-176.3-118.2 125.8 -14.1 -3.2 22.0 37 37 A D E -C 23 0A 65 -2,-0.5 7,-0.2 7,-0.4 -14,-0.2 -0.978 13.2-162.6-123.5 114.7 -14.2 -2.1 18.3 38 38 A S + 0 0 14 -16,-2.9 2,-2.6 -2,-0.5 -15,-0.1 0.642 68.6 97.5 -70.8 -13.9 -17.5 -0.3 17.3 39 39 A D S S+ 0 0 88 -17,-0.3 2,-0.3 3,-0.1 -1,-0.2 -0.323 71.1 80.5 -80.6 61.9 -16.7 -0.8 13.6 40 40 A A S S- 0 0 59 -2,-2.6 0, 0.0 1,-0.1 0, 0.0 -0.978 84.4-111.5-158.8 162.5 -18.9 -3.9 13.3 41 41 A E S S+ 0 0 206 1,-0.3 -1,-0.1 -2,-0.3 -3,-0.0 0.859 116.6 16.0 -69.1 -39.4 -22.6 -5.0 12.9 42 42 A N S S- 0 0 118 -3,-0.0 -1,-0.3 2,-0.0 -3,-0.1 -0.600 89.0-162.3-132.9 71.0 -22.8 -6.6 16.4 43 43 A P + 0 0 21 0, 0.0 2,-0.3 0, 0.0 -5,-0.1 -0.286 13.4 176.5 -65.7 139.8 -19.9 -5.1 18.2 44 44 A R - 0 0 71 -7,-0.2 -7,-0.4 -9,-0.1 2,-0.2 -0.991 38.7-105.2-141.4 143.5 -18.8 -6.9 21.4 45 45 A Y - 0 0 5 15,-0.4 -9,-0.2 -2,-0.3 19,-0.1 -0.562 48.5-165.8 -61.1 135.8 -16.1 -6.7 24.0 46 46 A E E -D 35 0A 100 -11,-1.8 -11,-1.4 -2,-0.2 2,-0.3 -0.969 24.0-108.9-130.1 144.9 -13.8 -9.6 23.2 47 47 A P E -D 34 0A 33 0, 0.0 -13,-0.3 0, 0.0 3,-0.1 -0.571 26.0-173.8 -70.3 134.6 -11.0 -11.3 25.1 48 48 A R S S+ 0 0 99 -15,-2.8 2,-0.4 -2,-0.3 -14,-0.2 0.330 73.0 53.2-112.3 0.2 -7.6 -10.5 23.5 49 49 A A S > S- 0 0 14 -16,-0.9 3,-1.7 1,-0.1 4,-0.3 -0.995 83.5-131.6-132.8 134.5 -5.6 -12.8 25.7 50 50 A R G > S+ 0 0 199 -2,-0.4 3,-1.7 1,-0.3 4,-0.2 0.795 105.2 64.1 -60.7 -29.3 -6.7 -16.5 26.0 51 51 A W G > S+ 0 0 41 1,-0.3 3,-1.8 2,-0.2 -1,-0.3 0.845 91.9 65.2 -60.3 -32.3 -6.5 -16.4 29.8 52 52 A M G X S+ 0 0 0 -3,-1.7 3,-1.5 1,-0.3 -1,-0.3 0.582 78.6 82.7 -66.9 -9.0 -9.3 -13.8 29.7 53 53 A E G < S+ 0 0 94 -3,-1.7 -1,-0.3 -4,-0.3 -2,-0.2 0.701 72.3 79.3 -68.1 -17.1 -11.6 -16.6 28.3 54 54 A Q G < S+ 0 0 135 -3,-1.8 -1,-0.3 -4,-0.2 -2,-0.2 0.811 73.5 94.9 -56.2 -31.8 -12.0 -17.6 32.0 55 55 A E S < S- 0 0 18 -3,-1.5 5,-0.0 -4,-0.2 -3,-0.0 -0.428 78.2-126.0 -68.7 137.5 -14.4 -14.7 32.3 56 56 A G >> - 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