==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=8-JAN-2010 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER IMMUNE SYSTEM 31-MAR-08 3CPL . COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR K.KEDZIERSKA,C.GUILLONNEAU,L.A.HATTON,D.STOCKWELL,S.GRAS, . 766 6 6 6 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 36881.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 481 62.8 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 . 269 35.1 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 . 1 0.1 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 . 41 5.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 48 6.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 114 14.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 6 0.8 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 2 0 0 0 0 0 2 0 2 2 0 0 0 0 0 0 0 0 0 0 0 0 0 0 2 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 . 6 12 4 4 1 7 0 5 3 4 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 1 3 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 86 0, 0.0 102,-0.0 0, 0.0 0, 0.0 0.000 360.0 360.0 360.0 -56.9 31.3 5.5 -35.0 2 2 A P - 0 0 80 0, 0.0 2,-0.3 0, 0.0 102,-0.2 0.203 360.0-163.4 -57.2-178.8 31.3 3.2 -31.8 3 3 A H E -A 103 0A 24 100,-1.5 100,-3.1 2,-0.0 2,-0.3 -0.937 8.0-170.8-159.4 156.6 30.3 -0.4 -31.7 4 4 A S E -A 102 0A 16 -2,-0.3 25,-2.0 98,-0.2 2,-0.4 -0.997 20.1-150.2-154.4 154.1 29.4 -2.6 -28.7 5 5 A M E +AB 101 28A 0 96,-2.3 96,-0.7 -2,-0.3 2,-0.3 -0.969 26.9 171.9-118.6 145.7 28.7 -6.1 -27.5 6 6 A R E -AB 100 27A 35 21,-2.2 21,-3.0 -2,-0.4 2,-0.4 -0.992 22.8-149.1-150.3 145.5 26.4 -6.6 -24.6 7 7 A Y E -AB 99 26A 0 92,-3.3 92,-1.8 -2,-0.3 2,-0.6 -0.987 8.0-162.2-116.0 127.9 24.7 -9.5 -22.8 8 8 A F E -AB 98 25A 18 17,-2.9 17,-2.0 -2,-0.4 2,-0.4 -0.929 15.7-179.4-106.8 117.6 21.4 -9.1 -21.1 9 9 A E E -AB 97 24A 2 88,-2.3 88,-3.0 -2,-0.6 2,-0.4 -0.960 6.4-174.4-122.4 134.1 20.6 -11.9 -18.6 10 10 A T E -AB 96 23A 5 13,-2.9 13,-3.6 -2,-0.4 2,-0.4 -0.972 7.3-170.2-123.7 142.1 17.6 -12.4 -16.4 11 11 A A E -AB 95 22A 0 84,-3.0 84,-2.6 -2,-0.4 2,-0.5 -0.997 8.8-165.1-126.4 131.6 16.7 -14.9 -13.7 12 12 A V E -AB 94 21A 22 9,-2.9 9,-1.4 -2,-0.4 82,-0.2 -0.964 18.4-127.2-119.2 125.4 13.2 -15.2 -12.3 13 13 A S - 0 0 19 80,-2.9 80,-0.1 -2,-0.5 4,-0.1 -0.348 18.2-156.6 -58.4 142.8 12.3 -17.0 -9.1 14 14 A R - 0 0 82 3,-0.4 76,-0.1 78,-0.1 78,-0.1 -0.981 28.9-107.0-128.7 118.2 9.5 -19.6 -9.3 15 15 A P S S- 0 0 78 0, 0.0 2,-2.3 0, 0.0 3,-0.1 -0.123 95.9 -16.5 -51.4 122.0 7.6 -20.4 -6.1 16 16 A G S S+ 0 0 76 1,-0.2 -2,-0.1 75,-0.1 75,-0.0 -0.504 101.7 127.7 76.5 -67.0 8.6 -23.8 -4.7 17 17 A L - 0 0 111 -2,-2.3 -3,-0.4 1,-0.2 -1,-0.2 0.144 61.5-141.8 -26.2 91.5 10.1 -24.7 -8.2 18 18 A E S S+ 0 0 158 -3,-0.1 -1,-0.2 2,-0.0 -2,-0.1 0.642 84.6 49.3 -34.0 -26.6 13.6 -25.8 -7.1 19 19 A E S S- 0 0 64 -5,-0.0 2,-0.3 -6,-0.0 53,-0.0 -0.953 76.6-141.1-123.5 142.6 14.9 -24.0 -10.3 20 20 A P - 0 0 10 0, 0.0 -7,-0.2 0, 0.0 2,-0.2 -0.701 30.8 -97.4 -96.2 154.6 14.3 -20.4 -11.6 21 21 A R E -B 12 0A 73 -9,-1.4 -9,-2.9 -2,-0.3 2,-0.4 -0.468 41.4-165.9 -64.9 132.9 13.8 -19.3 -15.2 22 22 A Y E -B 11 0A 2 -11,-0.2 16,-2.6 -2,-0.2 2,-0.4 -0.995 7.2-176.1-127.4 129.8 17.1 -18.0 -16.7 23 23 A I E -BC 10 37A 20 -13,-3.6 -13,-2.9 -2,-0.4 2,-0.4 -0.992 6.0-177.1-127.9 138.8 17.4 -16.0 -19.9 24 24 A S E +BC 9 36A 0 12,-2.5 12,-3.6 -2,-0.4 2,-0.4 -0.995 4.5 178.0-130.2 136.5 20.4 -14.7 -21.7 25 25 A V E -BC 8 35A 6 -17,-2.0 -17,-2.9 -2,-0.4 2,-0.3 -0.985 14.6-148.9-141.0 122.6 20.3 -12.5 -24.9 26 26 A G E -BC 7 34A 0 8,-2.4 7,-2.6 -2,-0.4 8,-1.1 -0.737 10.0-164.7 -99.9 145.5 23.3 -11.1 -26.7 27 27 A Y E -BC 6 32A 21 -21,-3.0 -21,-2.2 -2,-0.3 2,-0.5 -0.975 12.6-168.8-127.9 133.4 23.4 -7.8 -28.7 28 28 A V E > S-BC 5 31A 0 3,-2.4 3,-1.4 -2,-0.4 -23,-0.2 -0.976 89.6 -14.5-116.0 115.5 25.9 -6.5 -31.2 29 29 A D T 3 S- 0 0 40 -25,-2.0 -1,-0.2 -2,-0.5 -24,-0.1 0.991 129.0 -55.7 54.0 59.6 25.1 -2.9 -31.9 30 30 A N T 3 S+ 0 0 136 -3,-0.2 2,-0.5 1,-0.2 -1,-0.3 0.527 113.1 123.8 52.4 9.2 21.7 -3.2 -30.2 31 31 A K E < -C 28 0A 47 -3,-1.4 -3,-2.4 18,-0.0 2,-0.4 -0.851 66.2-123.6 -97.8 131.8 20.9 -6.0 -32.6 32 32 A E E +C 27 0A 34 -2,-0.5 -5,-0.2 -5,-0.2 3,-0.1 -0.624 42.6 157.4 -74.8 125.7 19.9 -9.4 -31.0 33 33 A F E + 0 0 0 -7,-2.6 15,-1.9 -2,-0.4 16,-0.7 0.528 59.2 25.9-130.1 -14.4 22.3 -12.2 -32.3 34 34 A V E -CD 26 47A 0 -8,-1.1 -8,-2.4 13,-0.2 -1,-0.4 -0.987 58.1-176.1-143.8 157.4 22.2 -15.0 -29.7 35 35 A R E -CD 25 46A 14 11,-1.2 11,-1.3 -2,-0.3 2,-0.4 -0.969 7.3-169.0-152.4 132.3 19.7 -16.2 -27.1 36 36 A F E -C 24 0A 0 -12,-3.6 -12,-2.5 -2,-0.3 2,-0.4 -0.989 10.9-173.6-122.4 133.9 19.6 -18.9 -24.3 37 37 A D E > -C 23 0A 27 7,-0.4 3,-1.8 -2,-0.4 -14,-0.2 -0.942 23.5-155.1-135.9 114.3 16.4 -19.9 -22.5 38 38 A S T 3 S+ 0 0 25 -16,-2.6 -1,-0.1 -2,-0.4 -15,-0.1 0.830 95.5 60.2 -41.9 -43.4 15.9 -22.2 -19.5 39 39 A D T 3 S+ 0 0 75 -17,-0.2 -1,-0.3 3,-0.1 -16,-0.1 0.615 78.5 111.8 -75.7 -12.8 12.3 -23.0 -20.5 40 40 A A S < S- 0 0 33 -3,-1.8 -4,-0.0 1,-0.1 0, 0.0 -0.225 78.9-119.7 -57.4 150.1 13.2 -24.4 -23.8 41 41 A E S S+ 0 0 166 1,-0.3 -1,-0.1 2,-0.0 -3,-0.0 0.906 113.5 14.4 -55.1 -48.0 12.6 -28.2 -24.3 42 42 A N S S- 0 0 112 2,-0.1 -1,-0.3 0, 0.0 2,-0.1 -0.781 97.3-149.8-130.0 85.8 16.3 -28.6 -25.0 43 43 A P + 0 0 24 0, 0.0 2,-0.3 0, 0.0 -5,-0.1 -0.361 35.1 130.1 -70.9 128.5 17.8 -25.3 -23.8 44 44 A R - 0 0 78 -9,-0.2 -7,-0.4 -2,-0.1 17,-0.1 -0.963 63.6 -72.5-161.2 167.2 20.9 -23.9 -25.4 45 45 A Y - 0 0 1 15,-0.5 -9,-0.2 -2,-0.3 19,-0.1 -0.423 54.0-163.4 -63.2 144.3 22.3 -20.8 -27.0 46 46 A E E -D 35 0A 88 -11,-1.3 -11,-1.2 -2,-0.1 -1,-0.0 -0.997 21.4-106.9-141.8 132.3 20.6 -20.3 -30.3 47 47 A P E +D 34 0A 26 0, 0.0 -13,-0.2 0, 0.0 -14,-0.1 -0.273 33.9 171.7 -60.9 146.3 21.5 -18.1 -33.3 48 48 A R + 0 0 93 -15,-1.9 -14,-0.2 1,-0.2 -16,-0.1 0.214 62.6 55.0-143.5 10.8 19.3 -15.0 -33.8 49 49 A A S > S- 0 0 6 -16,-0.7 3,-1.4 1,-0.1 -1,-0.2 -0.944 86.4-118.8-128.7 154.9 21.1 -13.0 -36.5 50 50 A P G > S+ 0 0 87 0, 0.0 3,-2.2 0, 0.0 4,-0.2 0.913 108.6 61.7 -52.3 -47.3 22.0 -14.6 -39.9 51 51 A W G 3 S+ 0 0 14 1,-0.3 3,-0.4 2,-0.2 4,-0.3 0.465 90.8 66.2 -70.2 -0.9 25.7 -14.1 -39.5 52 52 A M G < S+ 0 0 0 -3,-1.4 -1,-0.3 1,-0.2 123,-0.0 0.434 78.1 86.6 -92.2 -1.9 25.9 -16.4 -36.4 53 53 A E S < S+ 0 0 140 -3,-2.2 -1,-0.2 1,-0.2 -2,-0.2 0.689 79.4 63.5 -74.4 -18.0 25.0 -19.4 -38.5 54 54 A Q S S+ 0 0 113 -3,-0.4 -1,-0.2 -4,-0.2 -2,-0.1 0.995 73.2 99.2 -65.2 -63.2 28.6 -19.9 -39.4 55 55 A E S S- 0 0 16 -4,-0.3 5,-0.1 2,-0.1 -3,-0.0 0.122 75.4-130.1 -30.0 120.2 30.0 -20.6 -35.9 56 56 A G >> - 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