==== 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 IMMUNE SYSTEM 17-JAN-02 1KTR . COMPND 2 MOLECULE: ANTI-HIS TAG ANTIBODY 3D5 VARIABLE LIGHT CHAIN; . SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; . AUTHOR M.KAUFMANN,P.LINDNER,A.HONEGGER,K.BLANK,M.TSCHOPP, . 233 4 2 2 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 11066.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 161 69.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 9 3.9 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 91 39.1 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 3 1.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 3 1.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 1 0.4 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 . 30 12.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 19 8.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 6 2.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 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 0 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 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 PARALLEL BRIDGES PER LADDER . 2 3 4 2 0 6 1 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 2 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 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 L D 0 0 127 0, 0.0 2,-0.4 0, 0.0 100,-0.1 0.000 360.0 360.0 360.0 124.4 21.4 71.3 10.9 2 2 L I - 0 0 10 98,-0.4 2,-0.5 96,-0.2 93,-0.1 -0.661 360.0-154.4 -86.2 127.5 19.3 72.8 8.2 3 3 L L - 0 0 99 -2,-0.4 23,-1.7 99,-0.0 2,-0.6 -0.875 6.2-149.9-102.6 125.1 18.9 76.6 8.1 4 4 L M E -A 25 0A 6 -2,-0.5 2,-0.7 99,-0.5 101,-0.4 -0.866 9.1-161.1 -99.1 117.6 15.7 77.9 6.5 5 5 L T E -A 24 0A 70 19,-3.4 19,-1.7 -2,-0.6 2,-0.3 -0.876 5.9-161.9-103.9 112.7 16.2 81.4 4.9 6 6 L Q E -A 23 0A 9 -2,-0.7 17,-0.2 17,-0.2 3,-0.1 -0.724 12.4-131.3 -96.5 140.6 13.0 83.3 4.2 7 7 L T E S+A 22 0A 79 15,-2.6 15,-3.3 -2,-0.3 2,-0.1 -0.983 75.8 16.2-145.0 128.7 12.8 86.3 1.8 8 8 L P - 0 0 47 0, 0.0 -1,-0.2 0, 0.0 3,-0.1 0.633 58.2-161.6 -92.3 171.3 11.6 88.9 2.2 9 9 L S S S+ 0 0 87 1,-0.2 99,-3.1 98,-0.2 2,-0.4 0.814 86.2 36.8 -78.9 -30.0 11.1 89.5 5.9 10 10 L S E +d 108 0B 57 97,-0.2 -1,-0.2 99,-0.0 99,-0.2 -0.983 64.7 178.6-125.7 132.7 8.6 92.3 5.2 11 11 L L E -d 109 0B 29 97,-2.9 99,-1.2 -2,-0.4 2,-0.2 -0.787 9.6-163.8-138.3 93.8 6.1 92.3 2.3 12 12 L P E +d 110 0B 64 0, 0.0 2,-0.3 0, 0.0 99,-0.2 -0.541 21.0 173.8 -74.5 138.9 3.7 95.3 1.9 13 13 L V E -d 111 0B 6 97,-2.6 99,-2.0 -2,-0.2 2,-0.3 -0.995 30.7-132.1-149.9 153.3 0.8 94.6 -0.4 14 14 L S > - 0 0 45 -2,-0.3 3,-1.9 97,-0.2 69,-0.3 -0.775 47.8 -89.3-100.8 148.6 -2.5 96.1 -1.6 15 15 L L T 3 S+ 0 0 98 -2,-0.3 69,-0.2 1,-0.2 3,-0.1 -0.252 113.6 25.1 -56.9 143.5 -5.6 94.0 -1.6 16 16 L G T 3 S+ 0 0 47 67,-2.9 66,-0.5 1,-0.3 -1,-0.2 0.275 99.0 117.6 86.0 -12.0 -6.1 92.0 -4.8 17 17 L D < - 0 0 75 -3,-1.9 66,-3.0 65,-0.2 2,-0.5 -0.205 68.3-105.9 -81.0 176.1 -2.4 91.9 -5.5 18 18 L Q - 0 0 128 64,-0.2 2,-0.3 63,-0.2 63,-0.2 -0.916 28.4-162.9-111.0 127.5 -0.1 89.0 -5.7 19 19 L A E - B 0 80A 2 61,-2.7 61,-2.8 -2,-0.5 2,-0.4 -0.809 2.3-167.5-106.5 147.6 2.4 88.2 -3.0 20 20 L S E - B 0 79A 53 -2,-0.3 2,-0.4 59,-0.2 59,-0.2 -0.957 2.5-170.6-139.8 117.5 5.4 85.8 -3.4 21 21 L I E - B 0 78A 0 57,-3.0 57,-2.7 -2,-0.4 2,-0.3 -0.885 8.4-152.3-111.2 138.5 7.4 84.5 -0.5 22 22 L S E -AB 7 77A 43 -15,-3.3 -15,-2.6 -2,-0.4 2,-0.4 -0.816 10.8-176.2-111.8 151.2 10.7 82.6 -0.9 23 23 L a E -AB 6 76A 2 53,-2.3 53,-2.5 -2,-0.3 2,-0.4 -0.995 3.0-171.8-144.5 136.1 12.3 80.1 1.3 24 24 L R E -AB 5 75A 139 -19,-1.7 -19,-3.4 -2,-0.4 2,-0.3 -0.997 13.6-142.4-134.6 134.5 15.7 78.4 0.9 25 25 L S E -A 4 0A 6 49,-1.5 -21,-0.2 -2,-0.4 4,-0.1 -0.752 20.1-128.8 -97.5 143.0 17.3 75.5 2.9 26 26 L S S S+ 0 0 67 -23,-1.7 2,-0.3 -2,-0.3 -1,-0.1 0.717 95.5 5.3 -58.9 -21.3 21.0 75.4 3.7 27 27 L Q S S- 0 0 97 -24,-0.2 -1,-0.1 46,-0.1 -25,-0.0 -0.981 104.4 -59.1-158.3 161.9 20.9 71.9 2.3 28 30 L S - 0 0 59 -2,-0.3 46,-0.2 1,-0.1 -2,-0.1 -0.077 33.1-165.9 -46.2 134.6 18.5 69.5 0.4 29 31 L I + 0 0 0 44,-1.8 2,-0.6 -4,-0.1 8,-0.6 0.008 43.9 130.5-112.7 27.1 15.3 68.7 2.3 30 32 L V B -Q 36 0C 64 6,-0.2 6,-0.2 43,-0.1 2,-0.1 -0.723 54.1-139.8 -79.2 119.9 14.5 65.8 0.1 31 33 L H > - 0 0 11 4,-3.0 3,-1.8 -2,-0.6 67,-0.1 -0.441 18.7-112.4 -79.4 157.7 13.7 62.9 2.5 32 34 L S T 3 S+ 0 0 110 1,-0.3 -1,-0.1 65,-0.2 4,-0.1 0.728 113.6 64.3 -64.3 -19.9 15.0 59.4 1.7 33 35 L N T 3 S- 0 0 77 2,-0.1 -1,-0.3 200,-0.1 3,-0.1 0.490 121.3-102.4 -82.4 -0.8 11.4 58.2 1.3 34 37 L G S < S+ 0 0 57 -3,-1.8 2,-0.1 1,-0.4 -2,-0.1 0.163 86.6 112.6 103.9 -19.5 10.9 60.5 -1.7 35 38 L N - 0 0 61 -5,-0.1 -4,-3.0 62,-0.0 2,-0.5 -0.432 57.2-144.5 -85.0 162.1 8.9 63.2 -0.0 36 39 L T B -Q 30 0C 24 -6,-0.2 2,-2.3 -2,-0.1 -6,-0.2 -0.929 12.5-152.2-127.2 101.1 10.0 66.8 0.6 37 40 L Y + 0 0 12 -8,-0.6 59,-2.4 -2,-0.5 2,-0.5 -0.329 38.2 148.5 -75.1 58.7 8.5 67.8 3.9 38 41 L L E -E 95 0B 0 -2,-2.3 18,-2.7 57,-0.2 2,-0.3 -0.846 23.2-174.5 -97.3 126.6 8.3 71.5 3.3 39 42 L E E -E 94 0B 4 55,-3.2 55,-1.9 -2,-0.5 2,-0.5 -0.892 17.8-148.2-124.5 150.4 5.4 73.3 5.0 40 43 L W E -EF 93 53B 0 13,-2.6 12,-2.9 -2,-0.3 13,-1.4 -0.970 17.3-171.7-119.0 129.2 3.9 76.8 4.9 41 44 L Y E -EF 92 51B 1 51,-3.2 51,-2.7 -2,-0.5 2,-0.5 -0.893 12.2-155.0-120.9 148.8 2.3 78.4 8.0 42 45 L L E -EF 91 50B 11 8,-2.3 8,-1.8 -2,-0.3 2,-0.5 -0.987 10.9-168.9-122.9 125.4 0.3 81.6 8.5 43 46 L Q E -E 90 0B 20 47,-2.9 47,-2.7 -2,-0.5 3,-0.1 -0.955 5.5-159.5-122.0 119.3 0.1 83.2 11.9 44 47 L K > - 0 0 45 -2,-0.5 3,-2.3 4,-0.5 45,-0.1 -0.658 45.1 -80.1 -88.6 147.7 -2.3 86.0 12.8 45 48 L P T 3 S+ 0 0 117 0, 0.0 -1,-0.1 0, 0.0 3,-0.1 -0.162 116.0 10.4 -50.6 134.0 -1.4 88.1 15.8 46 49 L G T 3 S+ 0 0 95 1,-0.3 2,-0.2 -3,-0.1 -2,-0.0 0.400 114.2 97.2 78.2 -3.7 -2.4 86.6 19.1 47 50 L Q S < S- 0 0 81 -3,-2.3 -1,-0.3 1,-0.1 3,-0.1 -0.579 77.1-100.4-112.5 175.4 -3.1 83.2 17.4 48 51 L S - 0 0 23 -2,-0.2 -4,-0.5 1,-0.1 -1,-0.1 -0.496 50.6 -88.1 -88.6 161.6 -1.3 79.9 16.8 49 52 L P - 0 0 2 0, 0.0 2,-0.4 0, 0.0 -6,-0.2 -0.413 42.2-148.3 -69.2 148.6 0.3 79.1 13.5 50 53 L K E -F 42 0B 92 -8,-1.8 -8,-2.3 -2,-0.1 2,-0.2 -0.974 15.4-116.0-123.1 136.6 -2.0 77.5 10.9 51 54 L L E +F 41 0B 12 167,-0.5 -10,-0.2 -2,-0.4 3,-0.1 -0.471 39.6 159.8 -71.0 133.1 -1.0 75.0 8.3 52 55 L L E + 0 0 12 -12,-2.9 8,-2.4 1,-0.4 2,-0.4 0.719 65.1 15.3-116.8 -50.4 -1.5 76.2 4.7 53 56 L I E -FG 40 59B 0 -13,-1.4 -13,-2.6 6,-0.2 -1,-0.4 -0.984 61.1-178.2-132.2 140.0 0.8 74.0 2.5 54 57 L Y E > + G 0 58B 75 4,-2.2 4,-2.4 -2,-0.4 3,-0.4 -0.947 66.8 23.0-135.3 157.3 2.5 70.7 3.2 55 58 L K T 4 S- 0 0 84 -2,-0.3 2,-2.2 1,-0.3 -18,-0.2 0.908 125.9 -70.4 52.9 45.0 4.9 68.4 1.2 56 67 L V T 4 S+ 0 0 19 -18,-2.7 -1,-0.3 1,-0.2 21,-0.1 -0.252 128.5 19.8 73.5 -50.4 5.8 71.5 -0.9 57 68 L S T 4 S+ 0 0 64 -2,-2.2 2,-0.4 -3,-0.4 12,-0.3 0.438 83.3 116.7-133.7 1.3 2.5 71.8 -2.7 58 69 L N E < -G 54 0B 67 -4,-2.4 -4,-2.2 10,-0.1 2,-0.5 -0.603 55.7-139.1 -76.5 131.9 -0.4 70.1 -0.9 59 70 L R E -G 53 0B 103 -2,-0.4 -6,-0.2 -6,-0.2 3,-0.1 -0.770 21.5-118.1 -90.8 130.4 -3.1 72.5 0.2 60 71 L F > - 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