* HUMAN PHOSPHOLIPID SCRAMBLASE 1 FROM HUMAN_PLSCR1_B99990001.PDB MODIF 2 * DATE: 6/18/14 12:14:47 CREATED BY USER: annesc * 168 1 1 ALA HT1 -3.73270 -1.89339 -0.57210 PROT 1 0.00000 2 1 ALA HT2 -5.33906 -1.45342 -0.18326 PROT 1 0.00000 3 1 ALA N -4.72799 -1.95544 -0.85893 PROT 1 0.00000 4 1 ALA HT3 -4.81204 -1.55126 -1.81423 PROT 1 0.00000 5 1 ALA CA -5.09998 -3.35083 -0.97719 PROT 1 0.00000 6 1 ALA CB -6.57640 -3.47549 -1.32090 PROT 1 0.00000 7 1 ALA C -4.31126 -3.92914 -2.13894 PROT 1 0.00000 8 1 ALA O -4.00544 -3.19938 -3.08702 PROT 1 0.00000 9 2 LEU N -4.00743 -5.22811 -2.09210 PROT 2 0.00000 10 2 LEU H -4.38871 -5.75825 -1.36534 PROT 2 0.00000 11 2 LEU CA -3.16112 -5.88721 -3.08363 PROT 2 0.00000 12 2 LEU CB -3.01258 -7.36886 -2.75001 PROT 2 0.00000 13 2 LEU CG -2.33422 -7.76335 -1.44161 PROT 2 0.00000 14 2 LEU CD1 -2.44060 -9.26388 -1.23425 PROT 2 0.00000 15 2 LEU CD2 -0.87851 -7.31981 -1.41666 PROT 2 0.00000 16 2 LEU C -3.65027 -5.73762 -4.51809 PROT 2 0.00000 17 2 LEU O -2.86433 -5.56234 -5.44907 PROT 2 0.00000 18 3 GLN N -4.97528 -5.75027 -4.67566 PROT 3 0.00000 19 3 GLN H -5.51831 -5.89047 -3.87484 PROT 3 0.00000 20 3 GLN CA -5.63542 -5.54792 -5.95722 PROT 3 0.00000 21 3 GLN CB -7.14888 -5.75524 -5.83024 PROT 3 0.00000 22 3 GLN CG -7.64036 -7.16016 -5.45685 PROT 3 0.00000 23 3 GLN CD -7.44481 -7.60075 -4.00722 PROT 3 0.00000 24 3 GLN OE1 -6.97380 -6.86322 -3.14014 PROT 3 0.00000 25 3 GLN NE2 -7.79973 -8.83703 -3.68806 PROT 3 0.00000 26 3 GLN HE21 -8.16877 -9.41528 -4.38594 PROT 3 0.00000 27 3 GLN HE22 -7.67469 -9.11037 -2.75670 PROT 3 0.00000 28 3 GLN C -5.36767 -4.14431 -6.48911 PROT 3 0.00000 29 3 GLN O -5.03925 -3.96040 -7.66336 PROT 3 0.00000 30 4 ALA N -5.44717 -3.15060 -5.59528 PROT 4 0.00000 31 4 ALA H -5.57391 -3.37454 -4.64929 PROT 4 0.00000 32 4 ALA CA -5.22110 -1.75971 -5.95740 PROT 4 0.00000 33 4 ALA CB -5.58051 -0.84912 -4.79200 PROT 4 0.00000 34 4 ALA C -3.75734 -1.52833 -6.30578 PROT 4 0.00000 35 4 ALA O -3.44461 -0.82070 -7.26463 PROT 4 0.00000 36 5 PHE N -2.85099 -2.16460 -5.55394 PROT 5 0.00000 37 5 PHE H -3.16191 -2.66022 -4.76317 PROT 5 0.00000 38 5 PHE CA -1.42649 -2.11876 -5.85435 PROT 5 0.00000 39 5 PHE CB -0.60060 -2.82041 -4.77180 PROT 5 0.00000 40 5 PHE CG -0.74218 -2.26402 -3.35691 PROT 5 0.00000 41 5 PHE CD1 -0.62065 -3.13019 -2.28726 PROT 5 0.00000 42 5 PHE CD2 -0.99608 -0.92150 -3.12891 PROT 5 0.00000 43 5 PHE CE1 -0.76631 -2.65896 -0.99890 PROT 5 0.00000 44 5 PHE CE2 -1.14123 -0.45959 -1.83689 PROT 5 0.00000 45 5 PHE CZ -1.02895 -1.32594 -0.77210 PROT 5 0.00000 46 5 PHE C -1.12812 -2.74824 -7.20896 PROT 5 0.00000 47 5 PHE O -0.39228 -2.17112 -8.00887 PROT 5 0.00000 48 6 ALA N -1.72915 -3.90830 -7.50044 PROT 6 0.00000 49 6 ALA H -2.27970 -4.33965 -6.80963 PROT 6 0.00000 50 6 ALA CA -1.57177 -4.57380 -8.78641 PROT 6 0.00000 51 6 ALA CB -2.35046 -5.88193 -8.79292 PROT 6 0.00000 52 6 ALA C -2.05407 -3.73816 -9.96651 PROT 6 0.00000 53 6 ALA O -1.33225 -3.60731 -10.96060 PROT 6 0.00000 54 7 ILE N -3.24906 -3.13462 -9.88322 PROT 7 0.00000 55 7 ILE H -3.81531 -3.29926 -9.09613 PROT 7 0.00000 56 7 ILE CA -3.73021 -2.27257 -10.95854 PROT 7 0.00000 57 7 ILE CB -5.25339 -1.98113 -10.90411 PROT 7 0.00000 58 7 ILE CG2 -6.00575 -3.29227 -11.10548 PROT 7 0.00000 59 7 ILE CG1 -5.70921 -1.24331 -9.64929 PROT 7 0.00000 60 7 ILE CD -7.19445 -0.82852 -9.62985 PROT 7 0.00000 61 7 ILE C -2.91714 -0.98720 -11.09273 PROT 7 0.00000 62 7 ILE O -2.70063 -0.51073 -12.21107 PROT 7 0.00000 63 8 ALA N -2.42125 -0.43018 -9.97804 PROT 8 0.00000 64 8 ALA H -2.70415 -0.77812 -9.10354 PROT 8 0.00000 65 8 ALA CA -1.50603 0.70444 -10.01704 PROT 8 0.00000 66 8 ALA CB -1.16286 1.16343 -8.60613 PROT 8 0.00000 67 8 ALA C -0.20161 0.35944 -10.72701 PROT 8 0.00000 68 8 ALA O 0.21637 1.08755 -11.62897 PROT 8 0.00000 69 9 LEU N 0.42590 -0.77299 -10.38251 PROT 9 0.00000 70 9 LEU H 0.06175 -1.30159 -9.63764 PROT 9 0.00000 71 9 LEU CA 1.63373 -1.24122 -11.05514 PROT 9 0.00000 72 9 LEU CB 2.19846 -2.48376 -10.36929 PROT 9 0.00000 73 9 LEU CG 2.76617 -2.35236 -8.95898 PROT 9 0.00000 74 9 LEU CD1 3.07634 -3.72648 -8.39167 PROT 9 0.00000 75 9 LEU CD2 3.99952 -1.46199 -8.93691 PROT 9 0.00000 76 9 LEU C 1.41768 -1.52350 -12.53673 PROT 9 0.00000 77 9 LEU O 2.27246 -1.20042 -13.36553 PROT 9 0.00000 78 10 SER N 0.25857 -2.09397 -12.88946 PROT 10 0.00000 79 10 SER H -0.33655 -2.42395 -12.17585 PROT 10 0.00000 80 10 SER CA -0.13038 -2.27355 -14.28318 PROT 10 0.00000 81 10 SER CB -1.43915 -3.05175 -14.37570 PROT 10 0.00000 82 10 SER OG -1.34328 -4.32614 -13.75194 PROT 10 0.00000 83 10 SER HG -1.26503 -4.22001 -12.79708 PROT 10 0.00000 84 10 SER C -0.26185 -0.94276 -15.02147 PROT 10 0.00000 85 10 SER O 0.19837 -0.81234 -16.16025 PROT 10 0.00000 86 11 SER N -0.84633 0.07351 -14.37182 PROT 11 0.00000 87 11 SER H -1.22827 -0.09009 -13.47803 PROT 11 0.00000 88 11 SER CA -0.93947 1.41459 -14.93652 PROT 11 0.00000 89 11 SER CB -1.81562 2.30571 -14.06117 PROT 11 0.00000 90 11 SER OG -3.12713 1.77532 -13.91502 PROT 11 0.00000 91 11 SER HG -3.09551 0.96592 -13.39285 PROT 11 0.00000 92 11 SER C 0.43214 2.05648 -15.13013 PROT 11 0.00000 93 11 SER O 0.69767 2.63421 -16.18755 PROT 11 0.00000 94 12 PHE N 1.33641 1.92151 -14.14824 PROT 12 0.00000 95 12 PHE H 1.06004 1.48512 -13.31206 PROT 12 0.00000 96 12 PHE CA 2.70575 2.41755 -14.26355 PROT 12 0.00000 97 12 PHE CB 3.49960 2.21313 -12.96673 PROT 12 0.00000 98 12 PHE CG 2.97025 2.92505 -11.72456 PROT 12 0.00000 99 12 PHE CD1 2.32959 4.15006 -11.81084 PROT 12 0.00000 100 12 PHE CD2 3.13904 2.32425 -10.49133 PROT 12 0.00000 101 12 PHE CE1 1.85293 4.75715 -10.66694 PROT 12 0.00000 102 12 PHE CE2 2.65969 2.93931 -9.35331 PROT 12 0.00000 103 12 PHE CZ 2.01491 4.15357 -9.43928 PROT 12 0.00000 104 12 PHE C 3.45641 1.75254 -15.41155 PROT 12 0.00000 105 12 PHE O 4.11268 2.43255 -16.20240 PROT 12 0.00000 106 13 ASP N 3.33512 0.42408 -15.54065 PROT 13 0.00000 107 13 ASP H 2.85731 -0.06975 -14.83903 PROT 13 0.00000 108 13 ASP CA 3.91487 -0.31297 -16.65981 PROT 13 0.00000 109 13 ASP CB 3.71787 -1.81792 -16.46877 PROT 13 0.00000 110 13 ASP CG 4.35421 -2.67991 -17.55523 PROT 13 0.00000 111 13 ASP OD1 3.62117 -3.21679 -18.38332 PROT 13 0.00000 112 13 ASP OD2 5.57624 -2.82773 -17.55607 PROT 13 0.00000 113 13 ASP C 3.34607 0.12487 -18.00731 PROT 13 0.00000 114 13 ASP O 4.09282 0.23801 -18.98027 PROT 13 0.00000 115 14 SER N 2.03630 0.39570 -18.07380 PROT 14 0.00000 116 14 SER H 1.47407 0.21500 -17.28880 PROT 14 0.00000 117 14 SER CA 1.41256 0.93657 -19.27627 PROT 14 0.00000 118 14 SER CB -0.10273 1.00989 -19.11200 PROT 14 0.00000 119 14 SER OG -0.67352 -0.26678 -18.85103 PROT 14 0.00000 120 14 SER HG -0.37989 -0.58956 -17.99230 PROT 14 0.00000 121 14 SER C 1.96567 2.31129 -19.64500 PROT 14 0.00000 122 14 SER O 2.24403 2.56707 -20.81787 PROT 14 0.00000 123 15 LYS N 2.17489 3.20145 -18.66414 PROT 15 0.00000 124 15 LYS H 1.87373 2.98426 -17.75329 PROT 15 0.00000 125 15 LYS CA 2.81577 4.49091 -18.90881 PROT 15 0.00000 126 15 LYS CB 2.77847 5.37450 -17.65925 PROT 15 0.00000 127 15 LYS CG 1.38637 5.82999 -17.22536 PROT 15 0.00000 128 15 LYS CD 0.73502 6.73335 -18.26576 PROT 15 0.00000 129 15 LYS CE -0.64947 7.15438 -17.79933 PROT 15 0.00000 130 15 LYS NZ -1.28221 8.00872 -18.78586 PROT 15 0.00000 131 15 LYS HZ1 -0.70351 8.86066 -18.93006 PROT 15 0.00000 132 15 LYS HZ2 -2.22792 8.28317 -18.45213 PROT 15 0.00000 133 15 LYS HZ3 -1.36774 7.49286 -19.68474 PROT 15 0.00000 134 15 LYS C 4.25237 4.34651 -19.40349 PROT 15 0.00000 135 15 LYS O 4.63996 4.98888 -20.38330 PROT 15 0.00000 136 16 LEU N 5.03991 3.46793 -18.76915 PROT 16 0.00000 137 16 LEU H 4.68774 3.01838 -17.96935 PROT 16 0.00000 138 16 LEU CA 6.40307 3.17535 -19.20359 PROT 16 0.00000 139 16 LEU CB 7.10057 2.23596 -18.22086 PROT 16 0.00000 140 16 LEU CG 7.41968 2.73461 -16.81404 PROT 16 0.00000 141 16 LEU CD1 7.90723 1.58354 -15.95162 PROT 16 0.00000 142 16 LEU CD2 8.44045 3.86204 -16.84226 PROT 16 0.00000 143 16 LEU C 6.49490 2.59715 -20.61301 PROT 16 0.00000 144 16 LEU O 7.44381 2.88942 -21.34286 PROT 16 0.00000 145 17 ALA N 5.52038 1.77582 -21.01716 PROT 17 0.00000 146 17 ALA H 4.86974 1.45376 -20.35537 PROT 17 0.00000 147 17 ALA CA 5.43647 1.29456 -22.38979 PROT 17 0.00000 148 17 ALA CB 4.46253 0.12617 -22.46255 PROT 17 0.00000 149 17 ALA C 4.97221 2.35529 -23.38769 PROT 17 0.00000 150 17 ALA O 5.52260 2.46076 -24.48337 PROT 17 0.00000 151 18 CYS N 3.97133 3.16632 -23.02934 PROT 18 0.00000 152 18 CYS H 3.58037 3.07444 -22.13170 PROT 18 0.00000 153 18 CYS CA 3.40469 4.15111 -23.94284 PROT 18 0.00000 154 18 CYS CB 1.89659 4.24139 -23.72533 PROT 18 0.00000 155 18 CYS SG 1.02905 2.70080 -24.11948 PROT 18 0.00000 156 18 CYS C 4.02628 5.54801 -23.90626 PROT 18 0.00000 157 18 CYS O 3.55098 6.45211 -24.59543 PROT 18 0.00000 158 19 GLU N 5.07423 5.77609 -23.10565 PROT 19 0.00000 159 19 GLU H 5.31631 5.08615 -22.45109 PROT 19 0.00000 160 19 GLU CA 5.78322 7.05684 -23.08988 PROT 19 0.00000 161 19 GLU CB 6.90581 7.05504 -22.03735 PROT 19 0.00000 162 19 GLU CG 7.98219 5.97626 -22.18572 PROT 19 0.00000 163 19 GLU CD 9.10001 6.05232 -21.15588 PROT 19 0.00000 164 19 GLU OE1 8.86162 5.76266 -19.98253 PROT 19 0.00000 165 19 GLU OE2 10.21654 6.41233 -21.52910 PROT 19 0.00000 166 19 GLU C 6.31386 7.57496 -24.43232 PROT 19 0.00000 167 19 GLU OT1 6.81119 6.78144 -25.23383 PROT 19 0.00000 168 19 GLU OT2 6.24403 8.78321 -24.64961 PROT 19 0.00000