==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=8-APR-2012 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER BIOSYNTHETIC PROTEIN 07-SEP-09 3JQJ . COMPND 2 MOLECULE: MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN C; . SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; . AUTHOR S.P.KANAUJIA,J.JEYAKANTHAN,N.NAKAGAWA,K.SEKAR,S.BABA,A.EBIHA . 1768 12 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 56549.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 1287 72.8 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 . 512 29.0 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 12 0.7 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 . 93 5.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 143 8.1 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 473 26.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 24 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 2 0 0 0 12 0 0 0 0 0 2 0 0 1 0 21 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 . 10 13 4 2 1 0 0 8 8 7 0 12 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 0 0 0 0 0 0 0 0 0 2 3 1 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 9 A G 0 0 82 0, 0.0 784,-1.6 0, 0.0 782,-0.1 0.000 360.0 360.0 360.0 3.7 5.4 40.5 69.5 2 10 A R - 0 0 52 782,-0.2 521,-0.0 1,-0.1 490,-0.0 -0.661 360.0-108.8 -82.3 132.9 6.4 44.1 69.4 3 11 A P + 0 0 18 0, 0.0 519,-0.5 0, 0.0 2,-0.3 -0.226 49.8 157.0 -60.1 149.2 10.0 44.8 70.4 4 12 A R - 0 0 52 779,-1.4 2,-1.1 517,-0.1 517,-0.2 -0.969 50.3-112.4-167.4 154.3 10.7 46.4 73.7 5 13 A M B -A 520 0A 0 515,-2.4 515,-1.6 -2,-0.3 3,-0.1 -0.843 55.4-113.9 -94.2 99.3 13.4 46.8 76.4 6 14 A V - 0 0 57 -2,-1.1 2,-0.6 513,-0.2 777,-0.1 0.040 28.8-107.6 -36.3 134.1 11.6 44.9 79.1 7 15 A D + 0 0 69 1,-0.2 512,-0.2 512,-0.1 -1,-0.2 -0.590 50.2 158.7 -73.3 112.0 10.6 47.1 82.1 8 16 A V > + 0 0 6 510,-3.1 3,-2.2 -2,-0.6 -1,-0.2 0.290 33.2 118.5-116.9 5.9 12.9 46.3 84.9 9 17 A T T 3 S+ 0 0 3 509,-0.5 -1,-0.1 1,-0.3 510,-0.1 0.710 75.9 45.5 -46.3 -34.1 12.4 49.6 86.8 10 18 A E T 3 S+ 0 0 108 508,-0.1 -1,-0.3 -3,-0.1 -2,-0.1 0.450 90.8 101.0 -97.3 2.8 11.0 48.0 90.0 11 19 A K S < S- 0 0 89 -3,-2.2 2,-0.1 1187,-0.1 87,-0.1 -0.532 75.1-110.5 -84.9 153.0 13.5 45.2 90.3 12 20 A P - 0 0 12 0, 0.0 2,-0.7 0, 0.0 85,-0.1 -0.465 27.6-109.1 -82.1 154.7 16.4 45.4 92.8 13 21 A E + 0 0 70 -2,-0.1 2,-0.3 83,-0.1 85,-0.2 -0.752 48.2 170.6 -85.4 112.3 20.1 45.8 91.9 14 22 A T E -L 97 0B 30 83,-2.3 83,-1.9 -2,-0.7 2,-0.3 -0.853 41.7 -89.0-121.9 158.1 21.8 42.5 92.6 15 23 A F E -L 96 0B 61 -2,-0.3 2,-0.3 81,-0.2 81,-0.2 -0.483 47.9-169.5 -67.4 126.4 25.3 41.1 91.8 16 24 A R E +L 95 0B 27 79,-3.0 79,-1.8 -2,-0.3 2,-0.3 -0.886 10.0 178.9-119.6 151.3 25.2 39.3 88.5 17 25 A T E -LM 94 138B 29 121,-1.6 121,-1.9 -2,-0.3 2,-0.3 -0.989 1.4-179.5-148.6 148.7 27.9 37.1 86.9 18 26 A A E -LM 93 137B 0 75,-2.0 75,-2.5 -2,-0.3 2,-0.4 -0.987 8.0-164.4-152.4 142.5 28.0 35.2 83.6 19 27 A T E +LM 92 136B 17 117,-3.4 116,-3.7 -2,-0.3 117,-2.0 -0.997 14.5 168.4-132.4 130.0 30.6 33.0 81.9 20 28 A A E -LM 91 134B 0 71,-2.5 71,-2.5 -2,-0.4 2,-0.3 -0.829 12.9-158.6-131.6 169.3 30.6 31.9 78.2 21 29 A E E -LM 90 133B 11 112,-2.3 112,-2.5 -2,-0.3 2,-0.3 -0.958 5.8-174.2-146.2 162.2 33.1 30.2 75.9 22 30 A A E -L 89 0B 0 67,-2.3 67,-3.3 -2,-0.3 2,-0.3 -0.975 10.7-146.2-154.1 156.6 33.7 30.0 72.2 23 31 A F E -LM 88 130B 6 107,-2.3 107,-2.7 -2,-0.3 2,-0.5 -0.935 5.5-155.8-130.6 154.7 36.1 28.1 69.9 24 32 A V E -LM 87 129B 0 63,-2.1 63,-2.5 -2,-0.3 2,-0.4 -0.960 18.9-143.9-129.7 110.1 37.9 28.7 66.6 25 33 A E E -LM 86 128B 84 103,-2.4 103,-1.2 -2,-0.5 61,-0.2 -0.629 21.7-147.8 -77.5 126.7 38.8 25.5 64.7 26 34 A L - 0 0 16 59,-2.5 2,-0.2 -2,-0.4 -1,-0.0 -0.645 6.2-140.5 -99.7 152.9 42.1 25.9 63.0 27 35 A T > - 0 0 42 -2,-0.2 4,-3.0 1,-0.1 5,-0.2 -0.494 37.4-102.9 -96.5 172.1 43.5 24.5 59.7 28 36 A E H > S+ 0 0 106 2,-0.2 4,-2.9 1,-0.2 5,-0.2 0.942 125.0 51.6 -62.1 -44.8 47.1 23.4 59.4 29 37 A E H > S+ 0 0 115 2,-0.2 4,-2.3 1,-0.2 -1,-0.2 0.915 113.8 43.2 -56.4 -47.1 47.9 26.6 57.6 30 38 A A H > S+ 0 0 0 2,-0.2 4,-2.8 1,-0.2 -2,-0.2 0.940 113.8 50.1 -65.6 -48.8 46.3 28.7 60.4 31 39 A L H X S+ 0 0 10 -4,-3.0 4,-2.1 1,-0.2 -2,-0.2 0.883 112.5 48.3 -57.5 -40.5 47.8 26.7 63.2 32 40 A S H X S+ 0 0 48 -4,-2.9 4,-0.7 -5,-0.2 -1,-0.2 0.933 112.3 47.9 -66.1 -46.0 51.3 27.0 61.6 33 41 A A H ><>S+ 0 0 12 -4,-2.3 5,-2.9 -5,-0.2 3,-0.6 0.885 110.4 54.5 -61.5 -38.6 50.8 30.8 61.1 34 42 A L H ><5S+ 0 0 13 -4,-2.8 3,-2.1 1,-0.2 -2,-0.2 0.935 104.7 50.1 -61.2 -51.4 49.7 31.1 64.7 35 43 A E H 3<5S+ 0 0 106 -4,-2.1 -1,-0.2 1,-0.3 -2,-0.2 0.624 108.9 56.5 -65.8 -10.9 52.7 29.4 66.3 36 44 A K T <<5S- 0 0 161 -4,-0.7 -1,-0.3 -3,-0.6 -2,-0.2 0.358 130.7 -90.3-101.1 4.0 54.8 31.8 64.2 37 45 A G T < 5S- 0 0 43 -3,-2.1 2,-0.3 -4,-0.1 3,-0.3 0.504 71.9 -74.0 102.5 5.4 53.2 34.9 65.6 38 46 A G < - 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