==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=18-MAR-2012 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER IMMUNE SYSTEM 24-FEB-11 3QUL . COMPND 2 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR E.ALLERBRING,A.D.DURU,H.UCHTENHAGEN,C.MADHURANTAKAM,S.GRIMM, . 1495 24 12 8 4 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 75258.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 910 60.9 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 . 524 35.1 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 4 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 14 0.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 20 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 . 2 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 . 49 3.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 99 6.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 217 14.5 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 14 0.9 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 6 0 2 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 4 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 . 9 28 4 10 2 12 0 9 11 0 4 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 0 3 5 8 0 0 4 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 69 0, 0.0 106,-0.1 0, 0.0 2,-0.0 0.000 360.0 360.0 360.0 156.0 5.5 -17.3 22.2 2 2 A P - 0 0 98 0, 0.0 2,-0.3 0, 0.0 102,-0.2 -0.256 360.0-159.2 -75.6 164.4 2.2 -15.9 21.1 3 3 A H E -A 103 0A 28 100,-1.9 100,-3.2 101,-0.1 2,-0.3 -0.921 8.7-173.7-142.6 162.6 1.8 -12.4 19.4 4 4 A S E -A 102 0A 12 -2,-0.3 25,-2.7 98,-0.2 2,-0.3 -0.990 13.5-156.2-155.6 156.3 -0.8 -9.8 18.8 5 5 A M E +AB 101 28A 0 96,-2.3 96,-1.3 -2,-0.3 2,-0.3 -0.994 18.6 177.0-133.1 141.3 -1.7 -6.5 17.1 6 6 A R E -AB 100 27A 12 21,-2.4 21,-3.0 -2,-0.3 2,-0.5 -0.999 20.9-158.3-140.1 142.4 -4.4 -4.0 18.0 7 7 A Y E -AB 99 26A 0 92,-2.7 92,-1.6 -2,-0.3 2,-0.6 -0.993 13.0-166.6-112.9 122.2 -5.6 -0.7 16.9 8 8 A F E -AB 98 25A 13 17,-3.0 17,-2.8 -2,-0.5 2,-0.4 -0.947 13.4-175.7-105.8 117.9 -7.6 1.2 19.6 9 9 A E E -AB 97 24A 0 88,-2.6 88,-2.3 -2,-0.6 2,-0.4 -0.913 7.4-176.7-122.0 143.7 -9.4 4.1 18.2 10 10 A T E -AB 96 23A 16 13,-2.6 13,-2.7 -2,-0.4 2,-0.4 -1.000 9.6-172.7-140.4 136.5 -11.5 6.8 19.9 11 11 A A E -AB 95 22A 0 84,-2.6 84,-2.3 -2,-0.4 2,-0.4 -0.998 10.9-170.1-125.6 131.5 -13.6 9.8 18.7 12 12 A V E -AB 94 21A 28 9,-2.5 9,-2.4 -2,-0.4 2,-0.3 -0.976 5.4-162.3-122.3 129.7 -15.0 12.2 21.1 13 13 A S E -A 93 0A 28 80,-2.6 80,-1.5 -2,-0.4 5,-0.1 -0.826 9.2-170.1-102.2 147.7 -17.6 15.0 20.4 14 14 A R - 0 0 109 -2,-0.3 78,-0.2 3,-0.3 77,-0.1 -0.975 37.3-105.1-136.6 151.8 -18.1 17.9 22.8 15 15 A P S S+ 0 0 86 0, 0.0 75,-0.1 0, 0.0 76,-0.1 0.836 117.6 33.6 -45.3 -42.8 -20.8 20.7 22.9 16 16 A G S S+ 0 0 71 74,-0.1 -3,-0.0 -3,-0.0 74,-0.0 0.968 92.0 98.9 -77.0 -53.9 -18.4 23.3 21.5 17 17 A L - 0 0 98 1,-0.1 -3,-0.3 2,-0.0 4,-0.0 -0.006 58.1-151.7 -51.7 128.2 -16.1 21.5 19.1 18 18 A E S S+ 0 0 175 1,-0.1 -1,-0.1 -5,-0.1 -5,-0.0 0.946 85.7 24.7 -58.5 -51.0 -16.9 21.8 15.4 19 19 A E S S- 0 0 95 1,-0.0 -1,-0.1 -6,-0.0 -5,-0.1 -0.871 92.1-105.3-118.7 147.6 -15.3 18.4 14.7 20 20 A P - 0 0 21 0, 0.0 2,-0.5 0, 0.0 -7,-0.2 -0.307 33.9-113.5 -65.7 154.8 -14.8 15.4 17.0 21 21 A R E -B 12 0A 99 -9,-2.4 -9,-2.5 -4,-0.0 2,-0.5 -0.822 33.8-160.7 -86.4 129.3 -11.3 14.7 18.3 22 22 A Y E +B 11 0A 2 -2,-0.5 16,-2.8 -11,-0.2 2,-0.4 -0.952 11.8 178.9-117.4 128.3 -10.0 11.4 16.9 23 23 A I E -BC 10 37A 27 -13,-2.7 -13,-2.6 -2,-0.5 2,-0.4 -0.998 4.3-172.7-130.4 133.3 -7.1 9.4 18.4 24 24 A S E -BC 9 36A 0 12,-2.5 12,-2.5 -2,-0.4 2,-0.4 -0.989 0.6-171.9-127.0 132.3 -5.7 6.1 17.2 25 25 A V E -BC 8 35A 6 -17,-2.8 -17,-3.0 -2,-0.4 2,-0.4 -0.989 8.0-155.7-127.7 125.8 -3.2 3.9 18.9 26 26 A G E -BC 7 34A 0 8,-2.2 7,-2.7 -2,-0.4 8,-1.1 -0.807 11.4-169.3 -97.4 140.0 -1.5 0.9 17.5 27 27 A Y E -BC 6 32A 21 -21,-3.0 -21,-2.4 -2,-0.4 2,-0.4 -0.983 12.8-166.4-128.4 139.7 -0.1 -1.9 19.6 28 28 A V E > S-BC 5 31A 10 3,-2.4 3,-2.0 -2,-0.4 -23,-0.2 -0.998 87.2 -8.8-120.8 130.8 2.2 -4.9 18.9 29 29 A D T 3 S- 0 0 32 -25,-2.7 -1,-0.1 -2,-0.4 -24,-0.1 0.882 131.1 -58.1 46.2 46.6 2.4 -7.5 21.7 30 30 A N T 3 S+ 0 0 109 1,-0.2 2,-0.5 -26,-0.1 -1,-0.3 0.565 114.5 117.1 63.2 15.4 0.5 -5.0 23.9 31 31 A K E < S-C 28 0A 85 -3,-2.0 -3,-2.4 18,-0.0 -1,-0.2 -0.957 72.3-112.9-116.1 129.1 3.2 -2.3 23.4 32 32 A E E +C 27 0A 48 -2,-0.5 -5,-0.3 -5,-0.2 3,-0.1 -0.322 43.2 161.6 -60.9 128.4 2.4 1.0 21.7 33 33 A F E + 0 0 1 -7,-2.7 15,-2.4 1,-0.4 16,-0.6 0.606 60.1 21.2-124.7 -21.8 4.1 1.3 18.3 34 34 A V E -CD 26 47A 1 -8,-1.1 -8,-2.2 13,-0.3 -1,-0.4 -0.981 58.9-169.6-143.6 159.0 2.2 4.1 16.4 35 35 A R E -CD 25 46A 11 11,-1.7 11,-2.3 -2,-0.3 2,-0.4 -0.989 7.2-172.0-152.5 135.9 -0.1 7.0 17.3 36 36 A F E +C 24 0A 0 -12,-2.5 -12,-2.5 -2,-0.3 2,-0.4 -0.998 8.1 179.2-124.6 134.7 -2.4 9.4 15.4 37 37 A D E > -C 23 0A 27 7,-0.4 3,-1.7 -2,-0.4 -14,-0.2 -0.968 23.4-152.3-138.9 118.9 -4.0 12.4 17.1 38 38 A S T 3 S+ 0 0 20 -16,-2.8 -15,-0.1 -2,-0.4 -1,-0.1 0.673 94.9 65.7 -65.0 -17.2 -6.3 14.9 15.2 39 39 A D T 3 S+ 0 0 98 -17,-0.2 -1,-0.3 3,-0.1 -16,-0.1 0.599 78.3 109.1 -78.6 -12.2 -5.3 17.6 17.7 40 40 A A S < S- 0 0 52 -3,-1.7 -4,-0.0 1,-0.1 0, 0.0 -0.147 85.2-110.1 -59.7 160.5 -1.7 17.6 16.5 41 41 A E S S+ 0 0 210 1,-0.3 -1,-0.1 2,-0.0 -3,-0.0 0.938 113.9 9.9 -63.1 -47.9 -0.4 20.6 14.5 42 42 A N S S- 0 0 108 2,-0.1 -1,-0.3 0, 0.0 -3,-0.1 -0.734 97.4-135.2-127.8 85.2 -0.2 18.6 11.3 43 43 A P + 0 0 25 0, 0.0 2,-0.3 0, 0.0 -5,-0.1 -0.109 42.6 145.1 -56.5 123.7 -1.9 15.3 12.3 44 44 A R - 0 0 70 -7,-0.2 -7,-0.4 -9,-0.1 2,-0.3 -0.961 56.8 -91.8-146.7 156.9 0.0 12.2 11.1 45 45 A Y - 0 0 4 15,-0.4 -9,-0.2 -2,-0.3 19,-0.1 -0.623 49.5-164.7 -67.5 133.0 0.7 8.7 12.3 46 46 A E E -D 35 0A 105 -11,-2.3 -11,-1.7 -2,-0.3 2,-0.0 -0.968 22.3-107.0-124.5 141.1 4.0 8.9 14.3 47 47 A P E -D 34 0A 42 0, 0.0 -13,-0.3 0, 0.0 -14,-0.1 -0.344 25.5-171.6 -63.0 145.9 6.3 6.1 15.4 48 48 A R + 0 0 114 -15,-2.4 -14,-0.2 1,-0.2 -16,-0.1 0.296 69.2 42.9-123.5 2.7 6.1 5.3 19.2 49 49 A A S > S- 0 0 22 -16,-0.6 3,-1.6 1,-0.1 4,-0.4 -0.974 84.9-115.9-145.5 152.5 9.1 2.9 19.5 50 50 A P G > S+ 0 0 105 0, 0.0 3,-1.7 0, 0.0 4,-0.2 0.840 107.6 64.9 -62.0 -36.4 12.5 3.1 17.9 51 51 A W G > S+ 0 0 54 1,-0.3 3,-0.7 2,-0.2 4,-0.1 0.643 93.0 63.9 -63.3 -15.7 12.2 0.0 15.7 52 52 A M G X S+ 0 0 0 -3,-1.6 3,-1.7 1,-0.2 -1,-0.3 0.621 79.2 81.0 -83.4 -14.8 9.4 1.7 13.6 53 53 A E G < S+ 0 0 148 -3,-1.7 -1,-0.2 -4,-0.4 -2,-0.2 0.699 76.6 75.5 -62.2 -17.4 11.8 4.4 12.4 54 54 A Q G < S+ 0 0 117 -3,-0.7 -1,-0.3 -4,-0.2 2,-0.2 0.778 74.3 96.7 -61.0 -28.2 12.9 1.8 9.8 55 55 A E S < S- 0 0 15 -3,-1.7 5,-0.1 -4,-0.1 -3,-0.0 -0.487 75.5-130.6 -70.1 131.5 9.7 2.4 7.9 56 56 A G >> - 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