==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=8-MAY-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-APR-11 3RNS . COMPND 2 MOLECULE: CUPIN 2 CONSERVED BARREL DOMAIN PROTEIN; . SOURCE 2 ORGANISM_SCIENTIFIC: LEPTOTRICHIA BUCCALIS; . AUTHOR J.OSIPIUK,C.TESAR,J.BEARDEN,A.JOACHIMIAK,MIDWEST CENTER FOR . 208 2 0 0 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 9745.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 148 71.2 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 . 107 51.4 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 0 0.0 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 . 4 1.9 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 . 20 9.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 12 5.8 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 2 1.0 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+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 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 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 . 1 2 1 4 2 2 1 4 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 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 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 0 A A 0 0 117 0, 0.0 3,-0.2 0, 0.0 29,-0.0 0.000 360.0 360.0 360.0 -53.0 44.2 -2.0 31.0 2 1 A X + 0 0 103 1,-0.3 29,-2.3 28,-0.1 2,-0.4 0.682 360.0 33.2 -97.7 -36.1 41.5 -2.7 33.6 3 2 A V B S-A 30 0A 37 27,-0.2 -1,-0.3 1,-0.1 27,-0.2 -0.992 70.1-177.8-116.7 118.9 41.3 0.8 35.0 4 3 A K + 0 0 119 25,-2.7 2,-0.3 -2,-0.4 26,-0.1 0.360 63.0 57.1-105.8 4.3 42.0 3.2 32.1 5 4 A I S S- 0 0 22 24,-0.5 2,-0.1 6,-0.0 6,-0.0 -0.855 99.7 -81.3-122.0 164.2 41.9 6.5 34.1 6 5 A E - 0 0 125 -2,-0.3 179,-0.4 1,-0.1 3,-0.4 -0.412 46.9-132.8 -62.4 137.4 43.9 7.6 37.2 7 6 A V S S+ 0 0 59 1,-0.2 179,-0.2 177,-0.1 -1,-0.1 -0.469 78.1 23.2 -87.5 159.5 42.7 6.2 40.6 8 7 A A S S+ 0 0 8 177,-2.8 -1,-0.2 1,-0.2 163,-0.1 0.819 99.9 105.9 59.5 39.2 42.2 8.1 43.8 9 8 A K S S- 0 0 77 -3,-0.4 176,-0.4 176,-0.2 2,-0.2 -0.991 74.6-112.7-149.7 134.7 41.7 11.4 42.0 10 9 A P - 0 0 49 0, 0.0 2,-0.4 0, 0.0 174,-0.2 -0.553 36.8-175.0 -71.9 135.1 38.7 13.6 41.2 11 10 A I E -G 183 0B 27 172,-2.4 172,-2.8 -2,-0.2 2,-0.9 -0.999 23.1-140.8-133.1 131.9 37.9 13.7 37.5 12 11 A N E >> -G 182 0B 71 -2,-0.4 4,-2.0 170,-0.2 3,-1.2 -0.823 11.7-167.0 -92.4 104.6 35.3 15.8 35.8 13 12 A F H 3> S+ 0 0 4 -2,-0.9 4,-2.3 168,-0.5 -1,-0.2 0.838 86.4 65.3 -63.9 -31.1 33.7 13.6 33.0 14 13 A N H 34 S+ 0 0 50 167,-0.4 -1,-0.3 1,-0.2 168,-0.1 0.865 112.4 33.9 -57.0 -32.8 32.1 16.6 31.5 15 14 A R H <4 S+ 0 0 177 -3,-1.2 -2,-0.2 1,-0.1 -1,-0.2 0.772 113.7 61.0 -88.6 -32.3 35.6 17.9 30.7 16 15 A L H < S+ 0 0 72 -4,-2.0 2,-0.5 1,-0.2 -2,-0.2 0.888 110.1 36.8 -66.5 -37.6 37.2 14.5 30.1 17 16 A I < + 0 0 4 -4,-2.3 2,-0.3 -5,-0.1 -1,-0.2 -0.962 68.4 155.3-127.7 127.6 34.9 13.5 27.2 18 17 A T - 0 0 76 -2,-0.5 2,-0.3 23,-0.1 23,-0.1 -0.927 22.3-151.3-143.2 156.7 33.7 15.9 24.5 19 18 A S - 0 0 21 -2,-0.3 2,-0.2 23,-0.1 3,-0.1 -0.987 8.2-143.3-131.4 144.8 32.4 15.7 20.9 20 19 A K > - 0 0 153 -2,-0.3 3,-1.9 1,-0.2 23,-0.2 -0.471 57.7 -48.3 -90.1 178.8 32.5 18.1 17.9 21 20 A E T 3 S+ 0 0 188 1,-0.3 -1,-0.2 -2,-0.2 3,-0.1 -0.151 126.5 2.7 -51.2 136.4 29.7 18.4 15.4 22 21 A A T 3 S+ 0 0 56 22,-0.4 2,-0.3 1,-0.2 -1,-0.3 0.547 103.8 121.5 64.9 13.4 28.5 15.1 13.9 23 22 A E < - 0 0 64 -3,-1.9 20,-2.2 23,-0.1 2,-0.5 -0.781 47.5-159.1-105.0 149.3 30.9 13.0 16.1 24 23 A V E - B 0 42A 58 -2,-0.3 2,-0.4 18,-0.2 18,-0.2 -1.000 19.0-168.4-118.2 126.1 30.2 10.2 18.7 25 24 A V E + B 0 41A 47 16,-2.8 16,-2.7 -2,-0.5 2,-0.3 -0.935 6.6 179.9-117.0 138.3 33.1 9.8 21.0 26 25 A S E - B 0 40A 80 -2,-0.4 2,-0.3 14,-0.2 14,-0.2 -0.975 10.1-176.3-138.6 159.1 33.6 6.9 23.4 27 26 A X E - B 0 39A 57 12,-2.2 12,-3.0 -2,-0.3 2,-0.5 -0.971 22.3-136.3-154.0 128.0 36.0 5.7 26.0 28 27 A R E + B 0 38A 77 -2,-0.3 10,-0.3 10,-0.2 3,-0.1 -0.718 24.4 174.1 -82.3 131.3 36.2 2.6 28.2 29 28 A I E + 0 0 0 8,-2.7 -25,-2.7 -2,-0.5 -24,-0.5 0.782 66.8 19.7-109.5 -34.2 37.1 3.6 31.7 30 29 A L E -AB 3 37A 0 7,-1.9 7,-2.6 -27,-0.2 -1,-0.4 -0.997 67.2-176.8-131.9 139.0 36.8 0.2 33.7 31 30 A N E + B 0 36A 46 -29,-2.3 5,-0.2 -2,-0.4 177,-0.0 -0.985 7.9 164.4-141.9 123.6 36.9 -3.2 32.1 32 31 A Q - 0 0 26 3,-2.7 3,-0.4 -2,-0.4 177,-0.0 -0.832 53.6 -92.8-128.8 169.4 36.5 -6.6 33.6 33 32 A P S S+ 0 0 113 0, 0.0 3,-0.1 0, 0.0 102,-0.0 0.860 121.6 15.6 -56.4 -33.8 35.8 -10.0 32.1 34 33 A N S S+ 0 0 36 175,-0.3 73,-1.6 73,-0.1 2,-0.3 0.249 127.3 34.7-129.8 18.9 32.0 -9.7 32.6 35 34 A S E + C 0 106A 0 -3,-0.4 -3,-2.7 71,-0.3 2,-0.3 -0.986 56.7 174.4-158.7 162.1 31.3 -6.0 33.3 36 35 A Y E -BC 31 105A 10 69,-2.0 69,-2.1 -2,-0.3 2,-0.4 -0.983 23.2-135.5-158.1 167.5 32.6 -2.6 32.2 37 36 A I E +BC 30 104A 0 -7,-2.6 -8,-2.7 -2,-0.3 -7,-1.9 -0.998 27.6 174.4-132.4 128.5 32.0 1.1 32.5 38 37 A S E -BC 28 103A 7 65,-2.8 65,-3.6 -2,-0.4 2,-0.4 -0.917 21.6-136.6-128.9 157.0 32.3 3.4 29.4 39 38 A L E -BC 27 102A 0 -12,-3.0 -12,-2.2 -2,-0.3 2,-0.4 -0.903 17.7-168.8-110.2 143.2 31.7 7.0 28.7 40 39 A F E -BC 26 101A 29 61,-2.7 61,-2.5 -2,-0.4 2,-0.4 -0.987 11.1-171.0-127.0 139.3 29.9 8.4 25.6 41 40 A S E -BC 25 100A 0 -16,-2.7 -16,-2.8 -2,-0.4 2,-0.5 -0.984 12.5-169.3-126.2 120.4 29.5 11.9 24.2 42 41 A L E -BC 24 99A 0 57,-3.1 57,-1.6 -2,-0.4 -18,-0.2 -0.942 16.6-133.8-110.2 127.8 27.1 12.3 21.3 43 42 A A > - 0 0 7 -20,-2.2 3,-2.4 -2,-0.5 52,-0.3 -0.375 51.3 -66.2 -72.6 157.6 26.9 15.5 19.2 44 43 A K T 3 S+ 0 0 135 1,-0.3 -22,-0.4 52,-0.1 52,-0.2 -0.150 121.5 8.2 -46.3 132.7 23.5 16.8 18.5 45 44 A D T 3 S+ 0 0 99 50,-3.0 -1,-0.3 1,-0.3 51,-0.1 0.366 99.1 122.0 72.5 1.3 21.4 14.6 16.2 46 45 A E < - 0 0 62 -3,-2.4 49,-2.5 51,-0.2 2,-0.3 -0.440 43.5-158.4 -82.5 166.6 23.9 11.7 16.3 47 46 A E E -L 94 0C 91 47,-0.2 2,-0.4 -2,-0.1 47,-0.2 -0.989 19.5-148.1-142.9 155.9 22.9 8.3 17.5 48 47 A I E -L 93 0C 23 45,-2.1 45,-3.0 -2,-0.3 2,-0.4 -0.957 20.3-159.6-113.0 139.6 24.2 5.0 18.9 49 48 A T E -L 92 0C 90 -2,-0.4 2,-0.4 43,-0.2 43,-0.2 -0.970 4.2-166.5-118.6 137.7 22.3 1.8 18.0 50 49 A A E -L 91 0C 17 41,-3.1 41,-2.5 -2,-0.4 3,-0.1 -0.993 11.1-142.4-127.6 130.0 22.6 -1.4 19.9 51 50 A E - 0 0 133 -2,-0.4 2,-0.9 39,-0.2 38,-0.2 -0.241 59.4 -52.4 -78.5 174.5 21.4 -4.8 18.8 52 51 A A S S- 0 0 55 36,-0.2 38,-0.2 35,-0.1 -1,-0.2 -0.290 72.3-142.6 -58.9 94.6 19.7 -7.4 21.2 53 52 A X - 0 0 47 -2,-0.9 35,-2.7 36,-0.8 36,-0.2 -0.184 13.3-135.0 -68.6 145.6 22.5 -7.4 23.9 54 53 A L S S+ 0 0 123 53,-0.2 2,-0.3 33,-0.2 33,-0.1 0.720 89.5 28.6 -73.0 -23.5 23.6 -10.5 25.8 55 54 A G S S- 0 0 3 51,-0.2 33,-0.2 53,-0.2 -2,-0.1 -0.868 95.6 -81.1-130.6 171.8 23.6 -8.6 29.1 56 55 A N - 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