3GEN
  Discovery Studio  3D                             0

  0  0  0  0  0  0  0  0  0  0999 V3000
M  V30 BEGIN CTAB
M  V30 COUNTS 4350 4402 0 0 0
M  V30 BEGIN ATOM
M  V30 1 N     -25.4060   -11.1600     0.0440 0 CHG=1 CFG=0
M  V30 2 H     -25.4617   -11.0013     1.0672 0 CHG=0 CFG=0
M  V30 3 H     -24.6329   -11.7955    -0.2337 0 CHG=0 CFG=0
M  V30 4 H     -26.3149   -11.5820    -0.2544 0 CHG=0 CFG=0
M  V30 5 C     -25.3580    -9.8760    -0.7160 0 CHG=0 CFG=1
M  V30 6 H     -24.4755    -9.3304    -0.3799 0 CHG=0 CFG=0
M  V30 7 C     -25.2330   -10.1410    -2.2200 0 CHG=0 CFG=0
M  V30 8 H     -25.3071    -9.1965    -2.7680 0 CHG=0 CFG=0
M  V30 9 H     -26.0726   -10.7395    -2.5794 0 CHG=0 CFG=0
M  V30 10 C     -23.9370   -10.8010    -2.6350 0 CHG=0 CFG=0
M  V30 11 C     -22.8180   -10.0350    -2.9630 0 CHG=0 CFG=0
M  V30 12 H     -22.8651    -8.9556    -2.9587 0 CHG=0 CFG=0
M  V30 13 C     -21.6230   -10.6350    -3.3460 0 CHG=0 CFG=0
M  V30 14 H     -20.7692   -10.0284    -3.6163 0 CHG=0 CFG=0
M  V30 15 C     -23.8300   -12.1900    -2.7110 0 CHG=0 CFG=0
M  V30 16 H     -24.6806   -12.8255    -2.5129 0 CHG=0 CFG=0
M  V30 17 C     -22.6410   -12.8000    -3.0940 0 CHG=0 CFG=0
M  V30 18 H     -22.5659   -13.8757    -3.1778 0 CHG=0 CFG=0
M  V30 19 C     -21.5420   -12.0160    -3.4110 0 CHG=0 CFG=0
M  V30 20 O     -20.3620   -12.6150    -3.7900 0 CHG=0 CFG=0
M  V30 21 H     -20.4047   -12.8151    -4.7343 0 CHG=0 CFG=0
M  V30 22 C     -26.5880    -9.0140    -0.4490 0 CHG=0 CFG=0
M  V30 23 O     -27.7240    -9.4870    -0.5580 0 CHG=0 CFG=0
M  V30 24 N     -26.3500    -7.7480    -0.0970 0 CHG=0 CFG=0
M  V30 25 H     -25.4345    -7.3532    -0.1748 0 CHG=0 CFG=0
M  V30 26 C     -27.4290    -6.7710     0.0470 0 CHG=0 CFG=0
M  V30 27 H     -27.0357    -5.9491     0.6444 0 CHG=0 CFG=0
M  V30 28 H     -28.2626    -7.2357     0.5768 0 CHG=0 CFG=0
M  V30 29 C     -27.8820    -6.2480    -1.3070 0 CHG=0 CFG=0
M  V30 30 O     -27.2920    -6.5840    -2.3410 0 CHG=0 CFG=0
M  V30 31 N     -28.9270    -5.4210    -1.3000 0 CHG=0 CFG=0
M  V30 32 H     -29.3664    -5.1301    -0.4512 0 CHG=0 CFG=0
M  V30 33 C     -29.5040    -4.8710    -2.5320 0 CHG=0 CFG=1
M  V30 34 H     -29.7268    -5.7254    -3.1744 0 CHG=0 CFG=0
M  V30 35 C     -30.7990    -4.1090    -2.2290 0 CHG=0 CFG=0
M  V30 36 H     -31.5107    -4.7734    -1.7362 0 CHG=0 CFG=0
M  V30 37 H     -31.2919    -3.8027    -3.1646 0 CHG=0 CFG=0
M  V30 38 O     -30.5600    -3.0170    -1.3570 0 CHG=0 CFG=0
M  V30 39 H     -30.3862    -2.2117    -1.8484 0 CHG=0 CFG=0
M  V30 40 C     -28.5280    -3.9700    -3.2890 0 CHG=0 CFG=0
M  V30 41 O     -28.5940    -3.8600    -4.5150 0 CHG=0 CFG=0
M  V30 42 N     -27.6220    -3.3370    -2.5470 0 CHG=0 CFG=0
M  V30 43 H     -27.6326    -3.5021    -1.5669 0 CHG=0 CFG=0
M  V30 44 C     -26.6150    -2.4460    -3.1170 0 CHG=0 CFG=1
M  V30 45 H     -27.0450    -1.9861    -4.0074 0 CHG=0 CFG=0
M  V30 46 C     -26.2530    -1.3450    -2.1110 0 CHG=0 CFG=0
M  V30 47 H     -27.1518    -0.8136    -1.7965 0 CHG=0 CFG=0
M  V30 48 H     -25.6240    -0.5986    -2.6002 0 CHG=0 CFG=0
M  V30 49 C     -25.5200    -1.8540    -0.8930 0 CHG=0 CFG=0
M  V30 50 C     -26.0990    -2.4620     0.2700 0 CHG=0 CFG=0
M  V30 51 C     -25.0360    -2.7830     1.1450 0 CHG=0 CFG=0
M  V30 52 C     -27.4120    -2.7640     0.6600 0 CHG=0 CFG=0
M  V30 53 H     -28.2493    -2.5115     0.0250 0 CHG=0 CFG=0
M  V30 54 C     -24.1700    -1.8350    -0.6820 0 CHG=0 CFG=0
M  V30 55 H     -23.4440    -1.4323    -1.3664 0 CHG=0 CFG=0
M  V30 56 N     -23.8710    -2.3910     0.5380 0 CHG=0 CFG=0
M  V30 57 H     -22.9583    -2.4942     0.8893 0 CHG=0 CFG=0
M  V30 58 C     -25.2440    -3.3950     2.3870 0 CHG=0 CFG=0
M  V30 59 H     -24.4064    -3.6346     3.0276 0 CHG=0 CFG=0
M  V30 60 C     -27.6190    -3.3720     1.8970 0 CHG=0 CFG=0
M  V30 61 H     -28.6294    -3.6007     2.2079 0 CHG=0 CFG=0
M  V30 62 C     -26.5380    -3.6800     2.7440 0 CHG=0 CFG=0
M  V30 63 H     -26.7326    -4.1525     3.6967 0 CHG=0 CFG=0
M  V30 64 C     -25.3540    -3.1990    -3.5450 0 CHG=0 CFG=0
M  V30 65 O     -24.4090    -2.5910    -4.0600 0 CHG=0 CFG=0
M  V30 66 N     -25.3440    -4.5180    -3.3410 0 CHG=0 CFG=0
M  V30 67 H     -26.1854    -5.0216    -3.1476 0 CHG=0 CFG=0
M  V30 68 C     -24.1430    -5.3150    -3.5880 0 CHG=0 CFG=1
M  V30 69 H     -23.3319    -4.6240    -3.8149 0 CHG=0 CFG=0
M  V30 70 C     -23.7150    -6.0770    -2.3290 0 CHG=0 CFG=0
M  V30 71 H     -22.9806    -6.8230    -2.6347 0 CHG=0 CFG=0
M  V30 72 H     -24.5568    -6.6400    -1.9307 0 CHG=0 CFG=0
M  V30 73 C     -23.1010    -5.1800    -1.2650 0 CHG=0 CFG=0
M  V30 74 H     -23.7859    -5.0518    -0.4268 0 CHG=0 CFG=0
M  V30 75 H     -22.9224    -4.1806    -1.6634 0 CHG=0 CFG=0
M  V30 76 C     -21.7570    -5.6870    -0.7750 0 CHG=0 CFG=0
M  V30 77 O     -20.8560    -5.9080    -1.6190 0 CHG=0 CFG=0
M  V30 78 O     -21.6000    -5.8550     0.4550 0 CHG=-1 CFG=0
M  V30 79 C     -24.2320    -6.2590    -4.7830 0 CHG=0 CFG=0
M  V30 80 O     -25.1190    -7.1130    -4.8610 0 CHG=0 CFG=0
M  V30 81 N     -23.2910    -6.0870    -5.7050 0 CHG=0 CFG=0
M  V30 82 H     -22.5472    -5.4480    -5.4980 0 CHG=0 CFG=0
M  V30 83 C     -23.1580    -6.9400    -6.8800 0 CHG=0 CFG=1
M  V30 84 H     -24.1114    -7.4480    -7.0410 0 CHG=0 CFG=0
M  V30 85 C     -22.8110    -6.0900    -8.1410 0 CHG=0 CFG=1
M  V30 86 H     -22.1026    -5.3149    -7.8420 0 CHG=0 CFG=0
M  V30 87 C     -22.1360    -6.9360    -9.2390 0 CHG=0 CFG=0
M  V30 88 H     -22.7473    -7.7912    -9.5282 0 CHG=0 CFG=0
M  V30 89 H     -21.1578    -7.3075    -8.9316 0 CHG=0 CFG=0
M  V30 90 H     -21.9558    -6.3478   -10.1378 0 CHG=0 CFG=0
M  V30 91 C     -24.0850    -5.4240    -8.6750 0 CHG=0 CFG=0
M  V30 92 H     -24.6355    -4.9851    -7.8412 0 CHG=0 CFG=0
M  V30 93 H     -24.7466    -6.1808    -9.0990 0 CHG=0 CFG=0
M  V30 94 C     -23.8550    -4.3390    -9.6870 0 CHG=0 CFG=0
M  V30 95 H     -23.3794    -4.7158   -10.5912 0 CHG=0 CFG=0
M  V30 96 H     -23.2262    -3.5587    -9.2621 0 CHG=0 CFG=0
M  V30 97 H     -24.8006    -3.8827    -9.9765 0 CHG=0 CFG=0
M  V30 98 C     -22.1060    -8.0120    -6.6050 0 CHG=0 CFG=0
M  V30 99 O     -21.0960    -7.7460    -5.9540 0 CHG=0 CFG=0
M  V30 100 N     -22.3680    -9.2280    -7.0740 0 CHG=0 CFG=0
M  V30 101 H     -23.1703    -9.3778    -7.6479 0 CHG=0 CFG=0
M  V30 102 C     -21.3900   -10.3080    -7.0090 0 CHG=0 CFG=1
M  V30 103 H     -20.9675   -10.2689    -6.0108 0 CHG=0 CFG=0
M  V30 104 C     -22.0800   -11.6600    -7.2140 0 CHG=0 CFG=0
M  V30 105 H     -22.4746   -11.7491    -8.2289 0 CHG=0 CFG=0
M  V30 106 H     -22.9299   -11.7454    -6.5377 0 CHG=0 CFG=0
M  V30 107 C     -21.1560   -12.8440    -6.9600 0 CHG=0 CFG=0
M  V30 108 O     -19.9170   -12.6770    -6.9510 0 CHG=0 CFG=0
M  V30 109 O     -21.6820   -13.9580    -6.7650 0 CHG=-1 CFG=0
M  V30 110 C     -20.3480   -10.0730    -8.0950 0 CHG=0 CFG=0
M  V30 111 O     -20.6810   -10.1070    -9.2840 0 CHG=0 CFG=0
M  V30 112 N     -19.0830    -9.8240    -7.6960 0 CHG=0 CFG=0
M  V30 113 C     -18.5620    -9.7680    -6.3170 0 CHG=0 CFG=0
M  V30 114 H     -18.9623   -10.5607    -5.6854 0 CHG=0 CFG=0
M  V30 115 H     -18.7949    -8.7981    -5.8762 0 CHG=0 CFG=0
M  V30 116 C     -18.0340    -9.5520    -8.6800 0 CHG=0 CFG=1
M  V30 117 H     -18.2867    -8.6640    -9.2602 0 CHG=0 CFG=0
M  V30 118 C     -16.7860    -9.3240    -7.8180 0 CHG=0 CFG=0
M  V30 119 H     -16.6563    -8.2508    -7.6714 0 CHG=0 CFG=0
M  V30 120 H     -15.8672    -9.6997    -8.2715 0 CHG=0 CFG=0
M  V30 121 C     -17.0930    -9.9640    -6.5110 0 CHG=0 CFG=0
M  V30 122 H     -16.8759   -11.0316    -6.5676 0 CHG=0 CFG=0
M  V30 123 H     -16.5329    -9.5526    -5.6717 0 CHG=0 CFG=0
M  V30 124 C     -17.8090   -10.7120    -9.6520 0 CHG=0 CFG=0
M  V30 125 O     -17.2840   -10.4990   -10.7390 0 CHG=0 CFG=0
M  V30 126 N     -18.2170   -11.9200    -9.2660 0 CHG=0 CFG=0
M  V30 127 H     -18.7493   -12.0298    -8.4234 0 CHG=0 CFG=0
M  V30 128 C     -18.0860   -13.0840   -10.1440 0 CHG=0 CFG=1
M  V30 129 H     -17.0679   -13.0663   -10.5357 0 CHG=0 CFG=0
M  V30 130 C     -18.3030   -14.3860    -9.3690 0 CHG=0 CFG=0
M  V30 131 H     -18.2341   -15.2293   -10.0584 0 CHG=0 CFG=0
M  V30 132 H     -19.3270   -14.3962    -8.9874 0 CHG=0 CFG=0
M  V30 133 C     -17.3240   -14.5930    -8.2160 0 CHG=0 CFG=0
M  V30 134 H     -17.4025   -13.7373    -7.5431 0 CHG=0 CFG=0
M  V30 135 H     -16.3014   -14.6087    -8.5922 0 CHG=0 CFG=0
M  V30 136 C     -17.6470   -15.8670    -7.4520 0 CHG=0 CFG=0
M  V30 137 H     -17.4632   -16.7533    -8.0607 0 CHG=0 CFG=0
M  V30 138 H     -18.7209   -15.8640    -7.2470 0 CHG=0 CFG=0
M  V30 139 C     -16.9200   -15.9210    -6.1120 0 CHG=0 CFG=0
M  V30 140 H     -17.4542   -16.5977    -5.4414 0 CHG=0 CFG=0
M  V30 141 H     -16.9039   -14.9412    -5.6278 0 CHG=0 CFG=0
M  V30 142 N     -15.5210   -16.4330    -6.2520 0 CHG=1 CFG=0
M  V30 143 H     -14.9900   -15.7882    -6.8733 0 CHG=0 CFG=0
M  V30 144 H     -15.5456   -17.3781    -6.6863 0 CHG=0 CFG=0
M  V30 145 H     -15.0571   -16.4830    -5.3232 0 CHG=0 CFG=0
M  V30 146 C     -19.0310   -13.0030   -11.3480 0 CHG=0 CFG=0
M  V30 147 O     -18.8510   -13.7300   -12.3300 0 CHG=0 CFG=0
M  V30 148 N     -20.0240   -12.1170   -11.2730 0 CHG=0 CFG=0
M  V30 149 H     -20.2318   -11.6532   -10.4122 0 CHG=0 CFG=0
M  V30 150 C     -20.9340   -11.8730   -12.3980 0 CHG=0 CFG=1
M  V30 151 H     -21.1010   -12.8294   -12.8981 0 CHG=0 CFG=0
M  V30 152 C     -22.2630   -11.2890   -11.9100 0 CHG=0 CFG=0
M  V30 153 H     -22.8228   -10.8639   -12.7437 0 CHG=0 CFG=0
M  V30 154 H     -22.0999   -10.4754   -11.2050 0 CHG=0 CFG=0
M  V30 155 C     -23.1710   -12.3310   -11.2830 0 CHG=0 CFG=0
M  V30 156 O     -22.8460   -13.5440   -11.3380 0 CHG=0 CFG=0
M  V30 157 O     -24.2220   -11.9260   -10.7350 0 CHG=-1 CFG=0
M  V30 158 C     -20.3360   -10.9460   -13.4550 0 CHG=0 CFG=0
M  V30 159 O     -20.9530   -10.7100   -14.5020 0 CHG=0 CFG=0
M  V30 160 N     -19.1440   -10.4210   -13.1770 0 CHG=0 CFG=0
M  V30 161 H     -18.6648   -10.7054   -12.3465 0 CHG=0 CFG=0
M  V30 162 C     -18.4700    -9.4790   -14.0710 0 CHG=0 CFG=1
M  V30 163 H     -19.2413    -8.9990   -14.6744 0 CHG=0 CFG=0
M  V30 164 C     -17.7380    -8.4010   -13.2640 0 CHG=0 CFG=0
M  V30 165 H     -17.1906    -7.7435   -13.9417 0 CHG=0 CFG=0
M  V30 166 H     -16.9750    -8.8954   -12.6601 0 CHG=0 CFG=0
M  V30 167 C     -18.6110    -7.5340   -12.3460 0 CHG=0 CFG=0
M  V30 168 H     -19.2218    -8.1977   -11.7307 0 CHG=0 CFG=0
M  V30 169 C     -17.7480    -6.7160   -11.3930 0 CHG=0 CFG=0
M  V30 170 H     -17.1145    -6.0120   -11.9307 0 CHG=0 CFG=0
M  V30 171 H     -17.0975    -7.3619   -10.8026 0 CHG=0 CFG=0
M  V30 172 H     -18.3680    -6.1504   -10.6964 0 CHG=0 CFG=0
M  V30 173 C     -19.5560    -6.6310   -13.1430 0 CHG=0 CFG=0
M  V30 174 H     -20.2334    -7.2125   -13.7685 0 CHG=0 CFG=0
M  V30 175 H     -19.0020    -5.9515   -13.7907 0 CHG=0 CFG=0
M  V30 176 H     -20.1719    -6.0261   -12.4763 0 CHG=0 CFG=0
M  V30 177 C     -17.4870   -10.1550   -15.0170 0 CHG=0 CFG=0
M  V30 178 O     -16.7680   -11.0870   -14.6360 0 CHG=0 CFG=0
M  V30 179 N     -17.4720    -9.6840   -16.2590 0 CHG=0 CFG=0
M  V30 180 H     -18.1657    -9.0054   -16.5057 0 CHG=0 CFG=0
M  V30 181 C     -16.4420   -10.0610   -17.2140 0 CHG=0 CFG=1
M  V30 182 H     -15.7022   -10.6925   -16.7158 0 CHG=0 CFG=0
M  V30 183 C     -17.0360   -10.8000   -18.4250 0 CHG=0 CFG=2
M  V30 184 H     -17.7502   -10.1542   -18.9435 0 CHG=0 CFG=0
M  V30 185 O     -17.7340   -11.9710   -17.9770 0 CHG=0 CFG=0
M  V30 186 H     -18.1994   -11.7931   -17.1611 0 CHG=0 CFG=0
M  V30 187 C     -15.9400   -11.2060   -19.4030 0 CHG=0 CFG=0
M  V30 188 H     -15.1885   -11.8282   -18.9161 0 CHG=0 CFG=0
M  V30 189 H     -15.4367   -10.3452   -19.8442 0 CHG=0 CFG=0
M  V30 190 H     -16.3614   -11.7881   -20.2228 0 CHG=0 CFG=0
M  V30 191 C     -15.7660    -8.7750   -17.6700 0 CHG=0 CFG=0
M  V30 192 O     -16.4350    -7.8600   -18.1520 0 CHG=0 CFG=0
M  V30 193 N     -14.4490    -8.7010   -17.5060 0 CHG=0 CFG=0
M  V30 194 H     -13.9650    -9.5115   -17.1807 0 CHG=0 CFG=0
M  V30 195 C     -13.7040    -7.4890   -17.8490 0 CHG=0 CFG=1
M  V30 196 H     -14.3950    -6.6455   -17.7741 0 CHG=0 CFG=0
M  V30 197 C     -12.5730    -7.2590   -16.8460 0 CHG=0 CFG=0
M  V30 198 H     -12.0378    -6.3439   -17.1012 0 CHG=0 CFG=0
M  V30 199 H     -11.8443    -8.0682   -16.9179 0 CHG=0 CFG=0
M  V30 200 C     -13.0510    -7.1470   -15.4300 0 CHG=0 CFG=0
M  V30 201 C     -13.5970    -5.9600   -14.9610 0 CHG=0 CFG=0
M  V30 202 H     -13.6640    -5.1038   -15.6150 0 CHG=0 CFG=0
M  V30 203 C     -12.9800    -8.2370   -14.5720 0 CHG=0 CFG=0
M  V30 204 H     -12.5763    -9.1789   -14.9155 0 CHG=0 CFG=0
M  V30 205 C     -14.0580    -5.8580   -13.6520 0 CHG=0 CFG=0
M  V30 206 H     -14.4850    -4.9303   -13.3213 0 CHG=0 CFG=0
M  V30 207 C     -13.4330    -8.1410   -13.2650 0 CHG=0 CFG=0
M  V30 208 H     -13.3820    -8.9995   -12.6093 0 CHG=0 CFG=0
M  V30 209 C     -13.9710    -6.9510   -12.8040 0 CHG=0 CFG=0
M  V30 210 H     -14.3392    -6.8767   -11.7921 0 CHG=0 CFG=0
M  V30 211 C     -13.1820    -7.5460   -19.2790 0 CHG=0 CFG=0
M  V30 212 O     -12.5190    -8.5150   -19.6660 0 CHG=0 CFG=0
M  V30 213 N     -13.4870    -6.5080   -20.0570 0 CHG=0 CFG=0
M  V30 214 H     -13.9933    -5.7415   -19.6621 0 CHG=0 CFG=0
M  V30 215 C     -13.2210    -6.5290   -21.5020 0 CHG=0 CFG=1
M  V30 216 H     -12.7731    -7.4924   -21.7435 0 CHG=0 CFG=0
M  V30 217 C     -14.5250    -6.4030   -22.3030 0 CHG=0 CFG=0
M  V30 218 H     -14.2924    -6.1916   -23.3485 0 CHG=0 CFG=0
M  V30 219 H     -15.0756    -5.5386   -21.9336 0 CHG=0 CFG=0
M  V30 220 C     -15.4390    -7.6420   -22.2670 0 CHG=0 CFG=0
M  V30 221 H     -15.7021    -7.8456   -21.2273 0 CHG=0 CFG=0
M  V30 222 C     -16.7330    -7.3850   -23.0230 0 CHG=0 CFG=0
M  V30 223 H     -16.5451    -7.1745   -24.0761 0 CHG=0 CFG=0
M  V30 224 H     -17.2728    -6.5367   -22.6011 0 CHG=0 CFG=0
M  V30 225 H     -17.3955    -8.2497   -22.9704 0 CHG=0 CFG=0
M  V30 226 C     -14.7390    -8.8770   -22.8230 0 CHG=0 CFG=0
M  V30 227 H     -13.9248    -9.2115   -22.1801 0 CHG=0 CFG=0
M  V30 228 H     -14.3331    -8.6950   -23.8185 0 CHG=0 CFG=0
M  V30 229 H     -15.4320    -9.7158   -22.8979 0 CHG=0 CFG=0
M  V30 230 C     -12.1680    -5.5400   -21.9970 0 CHG=0 CFG=0
M  V30 231 O     -11.3500    -5.8850   -22.8490 0 CHG=0 CFG=0
M  V30 232 N     -12.1890    -4.3140   -21.4780 0 CHG=0 CFG=0
M  V30 233 H     -12.8797    -4.0671   -20.7935 0 CHG=0 CFG=0
M  V30 234 C     -11.1580    -3.3280   -21.8240 0 CHG=0 CFG=1
M  V30 235 H     -10.2153    -3.8786   -21.8696 0 CHG=0 CFG=0
M  V30 236 C     -11.4270    -2.6930   -23.1990 0 CHG=0 CFG=0
M  V30 237 H     -11.4609    -3.4985   -23.9339 0 CHG=0 CFG=0
M  V30 238 H     -10.5720    -2.0785   -23.4877 0 CHG=0 CFG=0
M  V30 239 C     -12.6930    -1.8530   -23.3050 0 CHG=0 CFG=0
M  V30 240 H     -12.5890    -0.9226   -22.7433 0 CHG=0 CFG=0
M  V30 241 H     -13.4703    -2.4249   -22.8369 0 CHG=0 CFG=0
M  V30 242 C     -13.0380    -1.5800   -24.7670 0 CHG=0 CFG=0
M  V30 243 H     -13.0885    -2.5384   -25.2865 0 CHG=0 CFG=0
M  V30 244 H     -12.2379    -1.0116   -25.2453 0 CHG=0 CFG=0
M  V30 245 C     -14.3710    -0.8460   -24.9040 0 CHG=0 CFG=0
M  V30 246 H     -14.2254     0.2356   -24.8432 0 CHG=0 CFG=0
M  V30 247 H     -15.0673    -1.1015   -24.1074 0 CHG=0 CFG=0
M  V30 248 N     -15.0370    -1.1680   -26.2070 0 CHG=1 CFG=0
M  V30 249 H     -15.2619    -2.1802   -26.2756 0 CHG=0 CFG=0
M  V30 250 H     -14.4372    -0.8855   -27.0085 0 CHG=0 CFG=0
M  V30 251 H     -15.9313    -0.6300   -26.2547 0 CHG=0 CFG=0
M  V30 252 C     -10.9830    -2.2500   -20.7610 0 CHG=0 CFG=0
M  V30 253 O     -11.9250    -1.9200   -20.0400 0 CHG=0 CFG=0
M  V30 254 N      -9.7700    -1.7130   -20.6690 0 CHG=0 CFG=0
M  V30 255 H      -9.0601    -1.9389   -21.3344 0 CHG=0 CFG=0
M  V30 256 C      -9.4940    -0.5880   -19.7850 0 CHG=0 CFG=1
M  V30 257 H     -10.0931    -0.7250   -18.8834 0 CHG=0 CFG=0
M  V30 258 C      -8.0160    -0.5340   -19.3910 0 CHG=0 CFG=0
M  V30 259 H      -7.3880    -0.4167   -20.2758 0 CHG=0 CFG=0
M  V30 260 H      -7.7429    -1.4937   -18.9528 0 CHG=0 CFG=0
M  V30 261 C      -7.6900     0.5830   -18.3990 0 CHG=0 CFG=0
M  V30 262 H      -8.4088     0.5798   -17.5804 0 CHG=0 CFG=0
M  V30 263 H      -7.7738     1.5554   -18.8860 0 CHG=0 CFG=0
M  V30 264 C      -6.3070     0.4640   -17.7860 0 CHG=0 CFG=0
M  V30 265 O      -5.9300    -0.6510   -17.3650 0 CHG=0 CFG=0
M  V30 266 O      -5.6030     1.4950   -17.7090 0 CHG=-1 CFG=0
M  V30 267 C      -9.9170     0.7090   -20.4640 0 CHG=0 CFG=0
M  V30 268 O      -9.6070     0.9400   -21.6350 0 CHG=0 CFG=0
M  V30 269 N     -10.6270     1.5470   -19.7160 0 CHG=0 CFG=0
M  V30 270 H     -10.7593     1.3165   -18.7539 0 CHG=0 CFG=0
M  V30 271 C     -11.1360     2.8090   -20.2430 0 CHG=0 CFG=1
M  V30 272 H     -11.0846     2.7810   -21.3324 0 CHG=0 CFG=0
M  V30 273 C     -12.5910     3.0080   -19.8180 0 CHG=0 CFG=0
M  V30 274 H     -12.9163     3.9975   -20.1480 0 CHG=0 CFG=0
M  V30 275 H     -12.6199     3.0500   -18.7273 0 CHG=0 CFG=0
M  V30 276 C     -13.6280     1.9880   -20.2940 0 CHG=0 CFG=0
M  V30 277 H     -13.3193     1.0024   -19.9444 0 CHG=0 CFG=0
M  V30 278 C     -14.9810     2.3010   -19.6760 0 CHG=0 CFG=0
M  V30 279 H     -15.3580     3.2446   -20.0610 0 CHG=0 CFG=0
M  V30 280 H     -14.9262     2.3845   -18.5955 0 CHG=0 CFG=0
M  V30 281 H     -15.7169     1.5303   -19.8990 0 CHG=0 CFG=0
M  V30 282 C     -13.7190     1.9470   -21.8150 0 CHG=0 CFG=0
M  V30 283 H     -12.7762     1.6262   -22.2590 0 CHG=0 CFG=0
M  V30 284 H     -13.9611     2.9304   -22.2200 0 CHG=0 CFG=0
M  V30 285 H     -14.4879     1.2520   -22.1495 0 CHG=0 CFG=0
M  V30 286 C     -10.2900     4.0000   -19.8050 0 CHG=0 CFG=0
M  V30 287 O     -10.3130     5.0550   -20.4370 0 CHG=0 CFG=0
M  V30 288 N      -9.5440     3.8250   -18.7210 0 CHG=0 CFG=0
M  V30 289 H      -9.5490     2.9575   -18.2233 0 CHG=0 CFG=0
M  V30 290 C      -8.7050     4.8950   -18.1870 0 CHG=0 CFG=0
M  V30 291 H      -8.9496     5.8468   -18.6627 0 CHG=0 CFG=0
M  V30 292 H      -7.6725     4.6340   -18.4212 0 CHG=0 CFG=0
M  V30 293 C      -8.8770     5.0080   -16.6900 0 CHG=0 CFG=0
M  V30 294 O      -9.0350     4.0030   -16.0050 0 CHG=0 CFG=0
M  V30 295 N      -8.5843     6.2111   -16.1282 0 CHG=0 CFG=0
M  V30 296 H      -8.5776     7.0829   -16.6177 0 CHG=0 CFG=0
M  V30 297 C      -7.9297     6.1378   -14.7997 0 CHG=0 CFG=1
M  V30 298 H      -8.5915     5.5406   -14.1721 0 CHG=0 CFG=0
M  V30 299 C      -6.5319     5.4552   -14.9601 0 CHG=0 CFG=2
M  V30 300 H      -6.6574     4.4499   -15.3854 0 CHG=0 CFG=0
M  V30 301 O      -5.7907     5.3319   -13.7575 0 CHG=0 CFG=0
M  V30 302 H      -6.3001     4.8185   -13.1365 0 CHG=0 CFG=0
M  V30 303 C      -5.6270     6.2091   -15.9434 0 CHG=0 CFG=0
M  V30 304 H      -5.4331     7.2286   -15.6110 0 CHG=0 CFG=0
M  V30 305 H      -6.0619     6.2578   -16.9416 0 CHG=0 CFG=0
M  V30 306 H      -4.6647     5.7054   -16.0411 0 CHG=0 CFG=0
M  V30 307 C      -7.8170     7.5236   -14.1098 0 CHG=0 CFG=0
M  V30 308 O      -8.2436     8.5385   -14.6459 0 CHG=0 CFG=0
M  V30 309 N      -7.2240     7.4735   -12.8859 0 CHG=0 CFG=0
M  V30 310 H      -6.8839     6.5746   -12.6005 0 CHG=0 CFG=0
M  V30 311 C      -6.9405     8.6079   -12.0107 0 CHG=0 CFG=0
M  V30 312 H      -7.8885     9.0978   -11.7868 0 CHG=0 CFG=0
M  V30 313 H      -6.2888     9.2908   -12.5568 0 CHG=0 CFG=0
M  V30 314 C      -6.2510     8.1120   -10.7111 0 CHG=0 CFG=0
M  V30 315 O      -5.8896     6.9469   -10.5861 0 CHG=0 CFG=0
M  V30 316 N      -6.1123     9.0440    -9.7347 0 CHG=0 CFG=0
M  V30 317 H      -6.4187     9.9766    -9.9228 0 CHG=0 CFG=0
M  V30 318 C      -5.5042     8.7258    -8.4255 0 CHG=0 CFG=1
M  V30 319 H      -4.5101     8.3193    -8.6169 0 CHG=0 CFG=0
M  V30 320 C      -5.4211    10.0099    -7.5732 0 CHG=0 CFG=0
M  V30 321 H      -5.1155     9.7558    -6.5556 0 CHG=0 CFG=0
M  V30 322 H      -6.4135    10.4556    -7.4807 0 CHG=0 CFG=0
M  V30 323 C      -4.4399    11.0547    -8.1329 0 CHG=0 CFG=0
M  V30 324 H      -4.6145    11.2195    -9.1955 0 CHG=0 CFG=0
M  V30 325 H      -3.4105    10.7119    -8.0275 0 CHG=0 CFG=0
M  V30 326 C      -4.5778    12.4200    -7.4330 0 CHG=0 CFG=0
M  V30 327 O      -4.7995    13.4324    -8.0844 0 CHG=0 CFG=0
M  V30 328 N      -4.4307    12.3888    -6.0983 0 CHG=0 CFG=0
M  V30 329 H      -4.4881    13.1923    -5.4837 0 CHG=0 CFG=0
M  V30 330 H      -4.2375    11.5820    -5.5372 0 CHG=0 CFG=0
M  V30 331 C      -6.3373     7.6611    -7.6697 0 CHG=0 CFG=0
M  V30 332 O      -5.8462     6.6860    -7.1270 0 CHG=0 CFG=0
M  V30 333 N      -7.6350     7.9660    -7.7610 0 CHG=0 CFG=0
M  V30 334 H      -7.8005     8.9065    -8.0456 0 CHG=0 CFG=0
M  V30 335 C      -8.8580     7.1820    -7.5800 0 CHG=0 CFG=1
M  V30 336 H      -8.9543     7.2078    -6.4999 0 CHG=0 CFG=0
M  V30 337 C     -10.0110     7.8380    -8.3620 0 CHG=0 CFG=0
M  V30 338 H     -10.0129     7.5269    -9.4080 0 CHG=0 CFG=0
M  V30 339 H      -9.8633     8.9182    -8.3706 0 CHG=0 CFG=0
M  V30 340 C     -11.3940     7.6170    -7.7530 0 CHG=0 CFG=0
M  V30 341 C     -11.5510     7.2490    -6.4190 0 CHG=0 CFG=0
M  V30 342 H     -10.7455     7.0848    -5.7215 0 CHG=0 CFG=0
M  V30 343 C     -12.5200     7.8070    -8.5460 0 CHG=0 CFG=0
M  V30 344 H     -12.3616     8.1813    -9.5473 0 CHG=0 CFG=0
M  V30 345 C     -12.8220     7.0650    -5.8850 0 CHG=0 CFG=0
M  V30 346 H     -12.9069     6.7753    -4.8487 0 CHG=0 CFG=0
M  V30 347 C     -13.7910     7.6240    -8.0140 0 CHG=0 CFG=0
M  V30 348 H     -14.7534     8.0204    -8.2268 0 CHG=0 CFG=0
M  V30 349 C     -13.9440     7.2520    -6.6820 0 CHG=0 CFG=0
M  V30 350 H     -14.8813     7.1080    -6.1760 0 CHG=0 CFG=0
M  V30 351 C      -8.6650     5.7270    -8.0040 0 CHG=0 CFG=0
M  V30 352 O      -8.9580     4.8050    -7.2370 0 CHG=0 CFG=0
M  V30 353 N      -8.1740     5.5280    -9.2250 0 CHG=0 CFG=0
M  V30 354 H      -7.9337     6.2924    -9.8199 0 CHG=0 CFG=0
M  V30 355 C      -7.8660     4.1910    -9.7140 0 CHG=0 CFG=0
M  V30 356 H      -8.4724     3.4608    -9.1718 0 CHG=0 CFG=0
M  V30 357 H      -6.8218     4.0191    -9.4822 0 CHG=0 CFG=0
M  V30 358 C      -8.0670     4.0170   -11.2030 0 CHG=0 CFG=0
M  V30 359 O      -7.6800     4.8720   -12.0020 0 CHG=0 CFG=0
M  V30 360 N      -8.6820     2.8990   -11.5690 0 CHG=0 CFG=0
M  V30 361 H      -9.1471     2.3341   -10.8817 0 CHG=0 CFG=0
M  V30 362 C      -8.8780     2.5350   -12.9670 0 CHG=0 CFG=1
M  V30 363 H      -8.5848     3.3745   -13.5973 0 CHG=0 CFG=0
M  V30 364 C      -8.0280     1.2830   -13.3480 0 CHG=0 CFG=0
M  V30 365 H      -8.3786     0.4342   -12.7583 0 CHG=0 CFG=0
M  V30 366 C      -8.1950     0.9300   -14.8200 0 CHG=0 CFG=0
M  V30 367 H      -7.9579     1.7766   -15.4660 0 CHG=0 CFG=0
M  V30 368 H      -9.1978     0.5834   -15.0654 0 CHG=0 CFG=0
M  V30 369 H      -7.5157     0.1255   -15.1055 0 CHG=0 CFG=0
M  V30 370 C      -6.5480     1.4900   -13.0220 0 CHG=0 CFG=0
M  V30 371 H      -6.3811     1.7084   -11.9685 0 CHG=0 CFG=0
M  V30 372 H      -6.1272     2.3002   -13.6172 0 CHG=0 CFG=0
M  V30 373 H      -5.9745     0.5936   -13.2611 0 CHG=0 CFG=0
M  V30 374 C     -10.3620     2.2600   -13.2230 0 CHG=0 CFG=0
M  V30 375 O     -11.0930     1.8570   -12.3160 0 CHG=0 CFG=0
M  V30 376 N     -10.8020     2.5060   -14.4560 0 CHG=0 CFG=0
M  V30 377 H     -10.1583     2.7891   -15.1685 0 CHG=0 CFG=0
M  V30 378 C     -12.1610     2.1960   -14.8750 0 CHG=0 CFG=1
M  V30 379 H     -12.6815     1.7133   -14.0486 0 CHG=0 CFG=0
M  V30 380 C     -12.9320     3.4670   -15.3070 0 CHG=0 CFG=0
M  V30 381 H     -12.3872     3.9373   -16.1282 0 CHG=0 CFG=0
M  V30 382 C     -14.3330     3.1170   -15.8110 0 CHG=0 CFG=0
M  V30 383 H     -14.9440     2.6971   -15.0106 0 CHG=0 CFG=0
M  V30 384 H     -14.3172     2.3920   -16.6187 0 CHG=0 CFG=0
M  V30 385 H     -14.8427     3.9997   -16.1889 0 CHG=0 CFG=0
M  V30 386 C     -13.0040     4.4670   -14.1550 0 CHG=0 CFG=0
M  V30 387 H     -12.0109     4.7809   -13.8331 0 CHG=0 CFG=0
M  V30 388 H     -13.5178     4.0397   -13.2943 0 CHG=0 CFG=0
M  V30 389 H     -13.5459     5.3637   -14.4541 0 CHG=0 CFG=0
M  V30 390 C     -12.0920     1.2250   -16.0400 0 CHG=0 CFG=0
M  V30 391 O     -11.3120     1.4230   -16.9770 0 CHG=0 CFG=0
M  V30 392 N     -12.9010     0.1720   -15.9710 0 CHG=0 CFG=0
M  V30 393 H     -13.5352     0.0915   -15.2016 0 CHG=0 CFG=0
M  V30 394 C     -12.9450    -0.8140   -17.0440 0 CHG=0 CFG=1
M  V30 395 H     -12.2827    -0.4926   -17.8507 0 CHG=0 CFG=0
M  V30 396 C     -12.4740    -2.1810   -16.5390 0 CHG=0 CFG=0
M  V30 397 H     -12.5987    -2.9027   -17.3489 0 CHG=0 CFG=0
M  V30 398 H     -13.1176    -2.5229   -15.7262 0 CHG=0 CFG=0
M  V30 399 C     -11.0180    -2.1950   -16.0870 0 CHG=0 CFG=0
M  V30 400 H     -10.9092    -1.6711   -15.1356 0 CHG=0 CFG=0
M  V30 401 H     -10.4275    -1.6315   -16.8112 0 CHG=0 CFG=0
M  V30 402 C     -10.4800    -3.6120   -15.9860 0 CHG=0 CFG=0
M  V30 403 H     -10.7689    -4.1516   -16.8892 0 CHG=0 CFG=0
M  V30 404 H     -10.9401    -4.1390   -15.1487 0 CHG=0 CFG=0
M  V30 405 C      -8.9670    -3.6130   -15.8740 0 CHG=0 CFG=0
M  V30 406 H      -8.6465    -3.3756   -14.8571 0 CHG=0 CFG=0
M  V30 407 H      -8.5194    -2.8580   -16.5290 0 CHG=0 CFG=0
M  V30 408 N      -8.4020    -4.9350   -16.2690 0 CHG=1 CFG=0
M  V30 409 H      -8.6492    -5.1497   -17.2554 0 CHG=0 CFG=0
M  V30 410 H      -8.7552    -5.6850   -15.6420 0 CHG=0 CFG=0
M  V30 411 H      -7.3630    -4.8831   -16.1956 0 CHG=0 CFG=0
M  V30 412 C     -14.3340    -0.9280   -17.6510 0 CHG=0 CFG=0
M  V30 413 O     -15.3350    -0.6170   -16.9960 0 CHG=0 CFG=0
M  V30 414 N     -14.3730    -1.3490   -18.9150 0 CHG=0 CFG=0
M  V30 415 H     -13.5115    -1.5462   -19.3637 0 CHG=0 CFG=0
M  V30 416 C     -15.6060    -1.7650   -19.5680 0 CHG=0 CFG=1
M  V30 417 H     -16.4499    -1.2840   -19.0666 0 CHG=0 CFG=0
M  V30 418 C     -15.5920    -1.3730   -21.0520 0 CHG=0 CFG=0
M  V30 419 H     -14.5908    -1.5130   -21.4383 0 CHG=0 CFG=0
M  V30 420 H     -15.7980    -0.3084   -21.1445 0 CHG=0 CFG=0
M  V30 421 C     -16.5970    -2.1230   -21.9000 0 CHG=0 CFG=0
M  V30 422 C     -17.9620    -1.8610   -21.7920 0 CHG=0 CFG=0
M  V30 423 H     -18.3247    -1.1256   -21.0875 0 CHG=0 CFG=0
M  V30 424 C     -18.8870    -2.5470   -22.5650 0 CHG=0 CFG=0
M  V30 425 H     -19.9268    -2.2866   -22.4124 0 CHG=0 CFG=0
M  V30 426 C     -16.1820    -3.0960   -22.8080 0 CHG=0 CFG=0
M  V30 427 H     -15.1563    -3.3892   -22.9032 0 CHG=0 CFG=0
M  V30 428 C     -17.1020    -3.7920   -23.5850 0 CHG=0 CFG=0
M  V30 429 H     -16.7845    -4.5628   -24.2711 0 CHG=0 CFG=0
M  V30 430 C     -18.4510    -3.5110   -23.4610 0 CHG=0 CFG=0
M  V30 431 O     -19.3700    -4.1970   -24.2260 0 CHG=0 CFG=0
M  V30 432 H     -20.2621    -3.8821   -24.0608 0 CHG=0 CFG=0
M  V30 433 C     -15.7460    -3.2710   -19.4270 0 CHG=0 CFG=0
M  V30 434 O     -14.7680    -4.0050   -19.5620 0 CHG=0 CFG=0
M  V30 435 N     -16.9640    -3.7310   -19.1690 0 CHG=0 CFG=0
M  V30 436 H     -17.7571    -3.1201   -19.0626 0 CHG=0 CFG=0
M  V30 437 C     -17.2120    -5.1610   -19.0920 0 CHG=0 CFG=0
M  V30 438 H     -16.8722    -5.4781   -18.1061 0 CHG=0 CFG=0
M  V30 439 H     -16.6224    -5.6688   -19.8577 0 CHG=0 CFG=0
M  V30 440 C     -18.6630    -5.5290   -19.2670 0 CHG=0 CFG=0
M  V30 441 O     -19.4970    -4.6810   -19.5940 0 CHG=0 CFG=0
M  V30 442 N     -18.9530    -6.8060   -19.0390 0 CHG=0 CFG=0
M  V30 443 H     -18.2320    -7.3968   -18.6766 0 CHG=0 CFG=0
M  V30 444 C     -20.3060    -7.3400   -19.1060 0 CHG=0 CFG=1
M  V30 445 H     -20.9808    -6.5382   -19.4060 0 CHG=0 CFG=0
M  V30 446 C     -20.3780    -8.4890   -20.1190 0 CHG=0 CFG=0
M  V30 447 H     -21.3340    -9.0093   -20.0333 0 CHG=0 CFG=0
M  V30 448 H     -19.6251    -9.2306   -19.8507 0 CHG=0 CFG=0
M  V30 449 C     -20.1590    -8.0740   -21.5650 0 CHG=0 CFG=0
M  V30 450 H     -19.8802    -8.9590   -22.1388 0 CHG=0 CFG=0
M  V30 451 H     -19.3279    -7.3736   -21.6511 0 CHG=0 CFG=0
M  V30 452 C     -21.4310    -7.4790   -22.1540 0 CHG=0 CFG=0
M  V30 453 H     -21.6623    -6.5341   -21.6577 0 CHG=0 CFG=0
M  V30 454 H     -22.2571    -8.1577   -21.9568 0 CHG=0 CFG=0
M  V30 455 C     -21.3070    -7.2730   -23.6440 0 CHG=0 CFG=0
M  V30 456 H     -21.1559    -8.2247   -24.1558 0 CHG=0 CFG=0
M  V30 457 H     -20.4644    -6.6186   -23.8806 0 CHG=0 CFG=0
M  V30 458 N     -22.5430    -6.6400   -24.1880 0 CHG=1 CFG=0
M  V30 459 H     -22.5517    -5.6498   -23.8333 0 CHG=0 CFG=0
M  V30 460 H     -23.4092    -7.1015   -23.8257 0 CHG=0 CFG=0
M  V30 461 H     -22.5501    -6.5858   -25.2232 0 CHG=0 CFG=0
M  V30 462 C     -20.7360    -7.8430   -17.7390 0 CHG=0 CFG=0
M  V30 463 O     -19.9220    -8.3840   -16.9890 0 CHG=0 CFG=0
M  V30 464 N     -22.0120    -7.6410   -17.4170 0 CHG=0 CFG=0
M  V30 465 H     -22.5915    -7.1119   -18.0305 0 CHG=0 CFG=0
M  V30 466 C     -22.6220    -8.2420   -16.2350 0 CHG=0 CFG=1
M  V30 467 H     -21.8289    -8.5768   -15.5623 0 CHG=0 CFG=0
M  V30 468 C     -23.5100    -7.2310   -15.5010 0 CHG=0 CFG=0
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M  V30 471 C     -24.1180    -7.7410   -14.2120 0 CHG=0 CFG=0
M  V30 472 C     -25.4740    -8.1580   -14.0060 0 CHG=0 CFG=0
M  V30 473 C     -25.5930    -8.5380   -12.6500 0 CHG=0 CFG=0
M  V30 474 C     -26.6000    -8.2470   -14.8350 0 CHG=0 CFG=0
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M  V30 476 C     -23.4910    -7.8750   -13.0050 0 CHG=0 CFG=0
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M  V30 483 H     -28.6707    -8.7757   -14.9240 0 CHG=0 CFG=0
M  V30 484 C     -27.8830    -9.0790   -12.9380 0 CHG=0 CFG=0
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M  V30 486 C     -23.4390    -9.4430   -16.6940 0 CHG=0 CFG=0
M  V30 487 O     -24.2490    -9.3370   -17.6200 0 CHG=0 CFG=0
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M  V30 490 C     -23.8580   -11.8490   -16.4030 0 CHG=0 CFG=1
M  V30 491 H     -23.2394   -12.6140   -15.9318 0 CHG=0 CFG=0
M  V30 492 C     -25.2780   -11.9340   -15.8170 0 CHG=0 CFG=0
M  V30 493 H     -25.7786   -12.8169   -16.2177 0 CHG=0 CFG=0
M  V30 494 H     -25.8713   -11.0750   -16.1318 0 CHG=0 CFG=0
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M  V30 497 H     -24.5671   -12.8398   -13.9988 0 CHG=0 CFG=0
M  V30 498 C     -26.6200   -12.3420   -13.6700 0 CHG=0 CFG=0
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M  V30 504 N     -28.7580   -12.4700   -11.7690 0 CHG=1 CFG=0
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M  V30 510 C     -23.8100   -12.1370   -17.9100 0 CHG=0 CFG=0
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M  V30 514 C     -22.3250   -12.1920   -19.8730 0 CHG=0 CFG=0
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M  V30 524 H     -26.6120   -10.1213   -20.4123 0 CHG=0 CFG=0
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M  V30 529 C     -28.4470   -10.8720   -22.4340 0 CHG=0 CFG=0
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M  V30 556 O     -23.1930    -5.7250   -19.0230 0 CHG=0 CFG=0
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M  V30 601 C     -15.4640    -2.7810   -11.9920 0 CHG=0 CFG=0
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M  V30 608 C     -16.6490    -3.8120   -15.3790 0 CHG=0 CFG=0
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M  V30 618 C     -15.4660     3.1530   -11.0020 0 CHG=0 CFG=0
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M  V30 624 C     -15.3030     5.5020   -10.1670 0 CHG=0 CFG=0
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M  V30 639 H     -12.8753    -0.3195    -8.5747 0 CHG=0 CFG=0
M  V30 640 C     -11.1760    -0.7780    -9.8000 0 CHG=0 CFG=0
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M  V30 643 C     -11.8530    -1.7300   -10.7820 0 CHG=0 CFG=0
M  V30 644 H     -12.3582    -1.1778   -11.5752 0 CHG=0 CFG=0
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M  V30 646 S     -10.7150    -2.8710   -11.5710 0 CHG=0 CFG=0
M  V30 647 C     -11.8570    -3.9770   -12.3730 0 CHG=0 CFG=0
M  V30 648 H     -12.3920    -3.4534   -13.1657 0 CHG=0 CFG=0
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M  V30 650 H     -11.3374    -4.8443   -12.7790 0 CHG=0 CFG=0
M  V30 651 C     -11.4160     1.2120    -8.2670 0 CHG=0 CFG=0
M  V30 652 O     -10.5780     1.9900    -8.7240 0 CHG=0 CFG=0
M  V30 653 N     -11.7490     1.1720    -6.9810 0 CHG=0 CFG=0
M  V30 654 H     -12.3554     0.4635    -6.6293 0 CHG=0 CFG=0
M  V30 655 C     -11.2750     2.1690    -6.0220 0 CHG=0 CFG=1
M  V30 656 H     -11.0350     3.0751    -6.5825 0 CHG=0 CFG=0
M  V30 657 C     -12.3760     2.5190    -4.9830 0 CHG=0 CFG=1
M  V30 658 H     -12.5828     1.6041    -4.4502 0 CHG=0 CFG=0
M  V30 659 C     -11.8720     3.5540    -3.9680 0 CHG=0 CFG=0
M  V30 660 H     -11.4058     4.4186    -4.4396 0 CHG=0 CFG=0
M  V30 661 H     -11.1413     3.1083    -3.2917 0 CHG=0 CFG=0
M  V30 662 H     -12.6894     3.9098    -3.3421 0 CHG=0 CFG=0
M  V30 663 C     -13.6770     2.9730    -5.6720 0 CHG=0 CFG=0
M  V30 664 H     -14.4203     3.1277    -4.8879 0 CHG=0 CFG=0
M  V30 665 H     -14.0875     2.1720    -6.2894 0 CHG=0 CFG=0
M  V30 666 C     -13.5700     4.2560    -6.4910 0 CHG=0 CFG=0
M  V30 667 H     -13.3924     4.0212    -7.5340 0 CHG=0 CFG=0
M  V30 668 H     -12.6719     4.7503    -6.1658 0 CHG=0 CFG=0
M  V30 669 H     -14.4826     4.8358    -6.3959 0 CHG=0 CFG=0
M  V30 670 C     -10.0040     1.6990    -5.3130 0 CHG=0 CFG=0
M  V30 671 O     -10.0300     0.7290    -4.5540 0 CHG=0 CFG=0
M  V30 672 N      -8.9040     2.4090    -5.5640 0 CHG=0 CFG=0
M  V30 673 H      -9.0193     3.2305    -6.1216 0 CHG=0 CFG=0
M  V30 674 C      -7.5830     2.0670    -5.0280 0 CHG=0 CFG=1
M  V30 675 H      -7.3778     1.0466    -5.3578 0 CHG=0 CFG=0
M  V30 676 C      -6.5380     3.0400    -5.5750 0 CHG=0 CFG=0
M  V30 677 H      -5.6739     3.0814    -4.9078 0 CHG=0 CFG=0
M  V30 678 H      -6.9466     4.0522    -5.5932 0 CHG=0 CFG=0
M  V30 679 C      -6.0340     2.6250    -6.9610 0 CHG=0 CFG=0
M  V30 680 H      -6.8795     2.5478    -7.6445 0 CHG=0 CFG=0
M  V30 681 H      -5.6073     1.6236    -6.8871 0 CHG=0 CFG=0
M  V30 682 C      -4.9810     3.5930    -7.5140 0 CHG=0 CFG=0
M  V30 683 H      -4.2321     3.8015    -6.7482 0 CHG=0 CFG=0
M  V30 684 H      -5.4760     4.5330    -7.7349 0 CHG=0 CFG=0
M  V30 685 C      -4.3070     3.0550    -8.7820 0 CHG=0 CFG=0
M  V30 686 H      -5.0472     2.7393    -9.5184 0 CHG=0 CFG=0
M  V30 687 H      -3.7105     2.1731    -8.5387 0 CHG=0 CFG=0
M  V30 688 N      -3.4320     4.0390    -9.4120 0 CHG=1 CFG=0
M  V30 689 H      -2.7021     4.3493    -8.7391 0 CHG=0 CFG=0
M  V30 690 H      -4.0005     4.8655    -9.6989 0 CHG=0 CFG=0
M  V30 691 H      -2.9787     3.6365   -10.2579 0 CHG=0 CFG=0
M  V30 692 C      -7.5350     2.0720    -3.5030 0 CHG=0 CFG=0
M  V30 693 O      -8.2400     2.8500    -2.8540 0 CHG=0 CFG=0
M  V30 694 N      -6.6910     1.1980    -2.9480 0 CHG=0 CFG=0
M  V30 695 H      -6.2965     0.4658    -3.4967 0 CHG=0 CFG=0
M  V30 696 C      -6.4800     1.1020    -1.5010 0 CHG=0 CFG=1
M  V30 697 H      -7.4519     0.8389    -1.0765 0 CHG=0 CFG=0
M  V30 698 C      -5.4270     0.0350    -1.1670 0 CHG=0 CFG=0
M  V30 699 H      -5.3333    -0.0227    -0.0810 0 CHG=0 CFG=0
M  V30 700 H      -4.4476     0.3383    -1.5381 0 CHG=0 CFG=0
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M  V30 704 C      -7.1740    -1.7520    -1.4290 0 CHG=0 CFG=0
M  V30 705 O      -7.6180    -1.7000    -0.2610 0 CHG=0 CFG=0
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M  V30 767 O     -11.1010     0.8670     0.3140 0 CHG=-1 CFG=0
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M  V30 772 C     -17.3700     2.6070     5.2280 0 CHG=0 CFG=1
M  V30 773 H     -17.8172     1.6935     4.8303 0 CHG=0 CFG=0
M  V30 774 C     -17.0610     2.4310     6.7200 0 CHG=0 CFG=0
M  V30 775 H     -17.9861     2.4347     7.2977 0 CHG=0 CFG=0
M  V30 776 H     -16.4547     3.2585     7.0896 0 CHG=0 CFG=0
M  V30 777 C     -16.3610     1.1090     7.0210 0 CHG=0 CFG=0
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M  V30 785 H     -19.6633     6.0319     5.3854 0 CHG=0 CFG=0
M  V30 786 C     -18.0910     7.4100     4.8630 0 CHG=0 CFG=0
M  V30 787 H     -18.6688     8.2116     4.4033 0 CHG=0 CFG=0
M  V30 788 H     -17.1368     7.3803     4.3347 0 CHG=0 CFG=0
M  V30 789 C     -17.8850     7.7900     6.3040 0 CHG=0 CFG=0
M  V30 790 H     -17.3168     7.0156     6.8215 0 CHG=0 CFG=0
M  V30 791 H     -18.8431     7.8691     6.8180 0 CHG=0 CFG=0
M  V30 792 C     -17.1650     9.1060     6.4410 0 CHG=0 CFG=0
M  V30 793 O     -17.7720    10.1450     6.1200 0 CHG=0 CFG=0
M  V30 794 O     -16.0000     9.1010     6.8820 0 CHG=-1 CFG=0
M  V30 795 C     -19.4090     6.0220     3.2770 0 CHG=0 CFG=0
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M  V30 797 N     -18.5680     5.6870     2.3020 0 CHG=0 CFG=0
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M  V30 799 C     -19.0490     5.5840     0.9340 0 CHG=0 CFG=1
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M  V30 804 C     -18.4330     4.8790    -1.4150 0 CHG=0 CFG=0
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M  V30 806 H     -19.2900     6.7781    -1.9009 0 CHG=0 CFG=0
M  V30 807 C     -18.2620     3.5660    -1.8400 0 CHG=0 CFG=0
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M  V30 811 C     -18.7510     3.1460    -3.0740 0 CHG=0 CFG=0
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M  V30 813 C     -19.4330     4.0410    -3.8860 0 CHG=0 CFG=0
M  V30 814 H     -19.8239     3.7141    -4.8387 0 CHG=0 CFG=0
M  V30 815 C     -20.1150     4.5020     0.8060 0 CHG=0 CFG=0
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M  V30 817 N     -19.8990     3.3750     1.4820 0 CHG=0 CFG=0
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M  V30 821 C     -20.2440     0.9830     2.0860 0 CHG=0 CFG=1
M  V30 822 H     -19.9143     1.2838     3.0833 0 CHG=0 CFG=0
M  V30 823 C     -21.3250    -0.0880     2.2320 0 CHG=0 CFG=0
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M  V30 827 C     -19.0450     0.4280     1.3140 0 CHG=0 CFG=0
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M  V30 830 C     -18.2110    -0.5660     2.0990 0 CHG=0 CFG=0
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M  V30 838 C     -23.5350     3.7500     3.5180 0 CHG=0 CFG=1
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M  V30 840 C     -23.3660     4.3740     4.9080 0 CHG=0 CFG=0
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M  V30 842 H     -22.8182     3.6773     5.5438 0 CHG=0 CFG=0
M  V30 843 C     -24.6770     4.7530     5.6060 0 CHG=0 CFG=0
M  V30 844 H     -25.2071     5.5092     5.0252 0 CHG=0 CFG=0
M  V30 845 H     -24.4581     5.2062     6.5726 0 CHG=0 CFG=0
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M  V30 849 C     -24.1990     4.7300     2.5490 0 CHG=0 CFG=0
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M  V30 851 N     -23.4090     5.6230     1.9610 0 CHG=0 CFG=0
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M  V30 853 C     -23.9560     6.6060     1.0300 0 CHG=0 CFG=1
M  V30 854 H     -24.8449     7.0186     1.5113 0 CHG=0 CFG=0
M  V30 855 C     -22.9570     7.7340     0.7660 0 CHG=0 CFG=0
M  V30 856 H     -22.0501     7.3126     0.3309 0 CHG=0 CFG=0
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M  V30 858 C     -23.4800     8.8570    -0.1460 0 CHG=0 CFG=0
M  V30 859 H     -23.8622     8.4521    -1.0813 0 CHG=0 CFG=0
M  V30 860 H     -22.6492     9.4992    -0.4165 0 CHG=0 CFG=0
M  V30 861 C     -24.5700     9.7260     0.4920 0 CHG=0 CFG=0
M  V30 862 O     -24.9190     9.5270     1.6790 0 CHG=0 CFG=0
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M  V30 870 C     -23.2030     2.8880    -2.0060 0 CHG=0 CFG=0
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M  V30 874 C     -25.5680     3.7200    -1.8260 0 CHG=0 CFG=0
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M  V30 880 C     -27.7200     2.5460     0.9980 0 CHG=0 CFG=0
M  V30 881 H     -28.7773     2.3086     1.1268 0 CHG=0 CFG=0
M  V30 882 H     -27.5147     3.3783     1.6751 0 CHG=0 CFG=0
M  V30 883 C     -26.8890     1.3470     1.4140 0 CHG=0 CFG=0
M  V30 884 H     -25.8364     1.5495     1.2072 0 CHG=0 CFG=0
M  V30 885 H     -27.1611     0.4769     0.8160 0 CHG=0 CFG=0
M  V30 886 C     -27.0470     1.0550     2.8970 0 CHG=0 CFG=0
M  V30 887 H     -28.0765     0.7728     3.1191 0 CHG=0 CFG=0
M  V30 888 H     -26.8433     1.9703     3.4603 0 CHG=0 CFG=0
M  V30 889 C     -26.0760    -0.0260     3.3380 0 CHG=0 CFG=0
M  V30 890 H     -25.0591     0.2372     3.0323 0 CHG=0 CFG=0
M  V30 891 H     -26.3346    -0.9686     2.8701 0 CHG=0 CFG=0
M  V30 892 N     -26.0700    -0.2030     4.8200 0 CHG=1 CFG=0
M  V30 893 H     -27.0084    -0.4219     5.2000 0 CHG=0 CFG=0
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M  V30 895 H     -25.3470    -0.8714     5.1419 0 CHG=0 CFG=0
M  V30 896 C     -28.4250     4.1520    -0.8050 0 CHG=0 CFG=0
M  V30 897 O     -29.5040     3.9140    -1.3510 0 CHG=0 CFG=0
M  V30 898 N     -28.0180     5.3830    -0.5030 0 CHG=0 CFG=0
M  V30 899 H     -27.1276     5.5162    -0.0623 0 CHG=0 CFG=0
M  V30 900 C     -28.7750     6.5800    -0.8840 0 CHG=0 CFG=1
M  V30 901 H     -29.8199     6.3916    -0.6315 0 CHG=0 CFG=0
M  V30 902 C     -28.2600     7.8380    -0.1260 0 CHG=0 CFG=0
M  V30 903 H     -27.2024     7.9887    -0.3517 0 CHG=0 CFG=0
M  V30 904 C     -29.0080     9.0950    -0.5630 0 CHG=0 CFG=0
M  V30 905 H     -30.0827     8.9895    -0.4138 0 CHG=0 CFG=0
M  V30 906 H     -28.8344     9.3321    -1.6127 0 CHG=0 CFG=0
M  V30 907 H     -28.6729     9.9581     0.0137 0 CHG=0 CFG=0
M  V30 908 C     -28.3860     7.6470     1.3780 0 CHG=0 CFG=0
M  V30 909 H     -27.7884     6.8033     1.7259 0 CHG=0 CFG=0
M  V30 910 H     -29.4196     7.4762     1.6780 0 CHG=0 CFG=0
M  V30 911 H     -28.0206     8.5261     1.9105 0 CHG=0 CFG=0
M  V30 912 C     -28.6790     6.7970    -2.3980 0 CHG=0 CFG=0
M  V30 913 O     -29.6750     7.1030    -3.0600 0 CHG=0 CFG=0
M  V30 914 N     -27.4760     6.6140    -2.9370 0 CHG=0 CFG=0
M  V30 915 H     -26.7303     6.3897    -2.3056 0 CHG=0 CFG=0
M  V30 916 C     -27.2090     6.8370    -4.3580 0 CHG=0 CFG=1
M  V30 917 H     -27.5964     7.8300    -4.5886 0 CHG=0 CFG=0
M  V30 918 C     -25.7060     6.7990    -4.6230 0 CHG=0 CFG=0
M  V30 919 H     -25.5290     6.8439    -5.6978 0 CHG=0 CFG=0
M  V30 920 H     -25.3189     5.8372    -4.2866 0 CHG=0 CFG=0
M  V30 921 C     -24.9380     7.9180    -3.9340 0 CHG=0 CFG=0
M  V30 922 H     -25.2763     8.0606    -2.9067 0 CHG=0 CFG=0
M  V30 923 H     -25.1223     8.8587    -4.4532 0 CHG=0 CFG=0
M  V30 924 S     -23.1690     7.6020    -3.8920 0 CHG=0 CFG=0
M  V30 925 C     -22.7730     7.7080    -5.6350 0 CHG=0 CFG=0
M  V30 926 H     -22.8308     8.7408    -5.9807 0 CHG=0 CFG=0
M  V30 927 H     -23.4590     7.1085    -6.2311 0 CHG=0 CFG=0
M  V30 928 H     -21.7726     7.3109    -5.7937 0 CHG=0 CFG=0
M  V30 929 C     -27.9330     5.8440    -5.2660 0 CHG=0 CFG=0
M  V30 930 O     -28.3020     6.1840    -6.3940 0 CHG=0 CFG=0
M  V30 931 N     -28.1300     4.6240    -4.7650 0 CHG=0 CFG=0
M  V30 932 H     -27.7208     4.4193    -3.8755 0 CHG=0 CFG=0
M  V30 933 C     -28.8750     3.5780    -5.4760 0 CHG=0 CFG=1
M  V30 934 H     -28.3724     3.4246    -6.4330 0 CHG=0 CFG=0
M  V30 935 C     -28.8860     2.2800    -4.6640 0 CHG=0 CFG=0
M  V30 936 H     -29.6362     1.5942    -5.0614 0 CHG=0 CFG=0
M  V30 937 H     -29.2064     2.5082    -3.6459 0 CHG=0 CFG=0
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M  V30 940 H     -26.7212     2.1990    -4.3904 0 CHG=0 CFG=0
M  V30 941 S     -27.1560     0.6750    -6.1440 0 CHG=0 CFG=0
M  V30 942 C     -28.3170    -0.6930    -6.0760 0 CHG=0 CFG=0
M  V30 943 H     -29.0943    -0.5572    -6.8276 0 CHG=0 CFG=0
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M  V30 945 H     -27.7977    -1.6236    -6.3083 0 CHG=0 CFG=0
M  V30 946 C     -30.3140     3.9880    -5.7690 0 CHG=0 CFG=0
M  V30 947 O     -30.8830     3.5930    -6.7900 0 CHG=0 CFG=0
M  V30 948 N     -30.8950     4.7770    -4.8670 0 CHG=0 CFG=0
M  V30 949 H     -30.3516     5.0722    -4.0813 0 CHG=0 CFG=0
M  V30 950 C     -32.2880     5.2030    -4.9880 0 CHG=0 CFG=1
M  V30 951 H     -32.8249     4.3983    -5.4929 0 CHG=0 CFG=0
M  V30 952 C     -32.9080     5.4250    -3.6050 0 CHG=0 CFG=0
M  V30 953 H     -33.8481     5.9709    -3.6925 0 CHG=0 CFG=0
M  V30 954 H     -32.2438     6.0283    -2.9845 0 CHG=0 CFG=0
M  V30 955 C     -33.2280     4.1210    -2.8840 0 CHG=0 CFG=0
M  V30 956 O     -33.0896     3.0408    -3.4543 0 CHG=0 CFG=0
M  V30 957 N     -33.6529     4.2163    -1.6271 0 CHG=0 CFG=0
M  V30 958 H     -33.7530     5.0946    -1.1676 0 CHG=0 CFG=0
M  V30 959 H     -33.8365     3.3579    -1.1521 0 CHG=0 CFG=0
M  V30 960 C     -32.4890     6.4370    -5.8660 0 CHG=0 CFG=0
M  V30 961 O     -33.6230     6.8180    -6.1530 0 CHG=0 CFG=0
M  V30 962 N     -31.3900     7.0640    -6.2790 0 CHG=0 CFG=0
M  V30 963 H     -30.4950     6.6618    -6.0841 0 CHG=0 CFG=0
M  V30 964 C     -31.4560     8.1470    -7.2470 0 CHG=0 CFG=1
M  V30 965 H     -32.3236     8.7621    -7.0048 0 CHG=0 CFG=0
M  V30 966 C     -30.1790     8.9860    -7.2150 0 CHG=0 CFG=0
M  V30 967 H     -30.1879     9.6922    -8.0459 0 CHG=0 CFG=0
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M  V30 974 H     -28.2126    10.8502    -5.0691 0 CHG=0 CFG=0
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M  V30 979 C     -31.6360     7.5290    -8.6220 0 CHG=0 CFG=0
M  V30 980 O     -30.9630     6.5510    -8.9550 0 CHG=0 CFG=0
M  V30 981 N     -32.5600     8.0900    -9.4000 0 CHG=0 CFG=0
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M  V30 985 C     -33.8700     6.4510   -10.7000 0 CHG=0 CFG=0
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M  V30 987 H     -33.5763     5.6919    -9.9634 0 CHG=0 CFG=0
M  V30 988 O     -34.0370     5.8760   -11.9860 0 CHG=0 CFG=0
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M  V30 990 C     -33.3620     8.7150   -11.6340 0 CHG=0 CFG=0
M  V30 991 O     -34.4140     9.3050   -11.3700 0 CHG=0 CFG=0
M  V30 992 N     -32.5970     9.0120   -12.6760 0 CHG=0 CFG=0
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M  V30 994 C     -32.9700    10.0020   -13.6660 0 CHG=0 CFG=1
M  V30 995 H     -34.0436     9.9012   -13.8416 0 CHG=0 CFG=0
M  V30 996 C     -32.6210    11.4110   -13.1860 0 CHG=0 CFG=0
M  V30 997 H     -31.5413    11.5425   -13.1035 0 CHG=0 CFG=0
M  V30 998 H     -33.0270    11.5557   -12.1864 0 CHG=0 CFG=0
M  V30 999 C     -33.1800    12.4890   -14.0560 0 CHG=0 CFG=0
M  V30 1000 N     -32.5400    12.9320   -15.1930 0 CHG=0 CFG=0
M  V30 1001 C     -33.2690    13.8720   -15.7670 0 CHG=0 CFG=0
M  V30 1002 H     -33.0213    14.3984   -16.6780 0 CHG=0 CFG=0
M  V30 1003 N     -34.3630    14.0470   -15.0480 0 CHG=0 CFG=0
M  V30 1004 H     -35.0644    14.7005   -15.2631 0 CHG=0 CFG=0
M  V30 1005 C     -34.3310    13.1950   -13.9710 0 CHG=0 CFG=0
M  V30 1006 H     -35.0809    13.1027   -13.1990 0 CHG=0 CFG=0
M  V30 1007 C     -32.2230     9.6800   -14.9490 0 CHG=0 CFG=0
M  V30 1008 O     -31.0680     9.2350   -14.9030 0 CHG=0 CFG=0
M  V30 1009 N     -32.8740     9.8990   -16.0900 0 CHG=0 CFG=0
M  V30 1010 H     -33.7551    10.3697   -16.0896 0 CHG=0 CFG=0
M  V30 1011 C     -32.2880     9.5320   -17.3850 0 CHG=0 CFG=1
M  V30 1012 H     -32.0395     8.4728   -17.2997 0 CHG=0 CFG=0
M  V30 1013 C     -33.2950     9.6980   -18.5320 0 CHG=0 CFG=0
M  V30 1014 H     -34.1637     9.0658   -18.3456 0 CHG=0 CFG=0
M  V30 1015 H     -32.8395     9.3052   -19.4431 0 CHG=0 CFG=0
M  V30 1016 C     -33.7670    11.1160   -18.7820 0 CHG=0 CFG=0
M  V30 1017 H     -32.9117    11.7568   -18.9530 0 CHG=0 CFG=0
M  V30 1018 H     -34.3031    11.5116   -17.9184 0 CHG=0 CFG=0
M  V30 1019 C     -34.6450    11.2290   -20.0180 0 CHG=0 CFG=0
M  V30 1020 O     -34.3750    10.5240   -21.0150 0 CHG=0 CFG=0
M  V30 1021 O     -35.6090    12.0220   -19.9940 0 CHG=-1 CFG=0
M  V30 1022 C     -30.9850    10.2700   -17.6920 0 CHG=0 CFG=0
M  V30 1023 O     -30.1870     9.8020   -18.5010 0 CHG=0 CFG=0
M  V30 1024 N     -30.7680    11.4070   -17.0310 0 CHG=0 CFG=0
M  V30 1025 H     -31.4649    11.7207   -16.3849 0 CHG=0 CFG=0
M  V30 1026 C     -29.5810    12.2250   -17.2780 0 CHG=0 CFG=1
M  V30 1027 H     -29.0868    11.8502   -18.1698 0 CHG=0 CFG=0
M  V30 1028 C     -29.9710    13.6910   -17.5360 0 CHG=0 CFG=0
M  V30 1029 H     -29.0706    14.2679   -17.7592 0 CHG=0 CFG=0
M  V30 1030 H     -30.3858    14.1282   -16.6274 0 CHG=0 CFG=0
M  V30 1031 C     -30.9720    13.8940   -18.6840 0 CHG=0 CFG=0
M  V30 1032 H     -31.1403    14.9651   -18.7927 0 CHG=0 CFG=0
M  V30 1033 H     -31.9364    13.4704   -18.4220 0 CHG=0 CFG=0
M  V30 1034 C     -30.4530    13.3320   -20.0120 0 CHG=0 CFG=0
M  V30 1035 H     -30.1944    12.2799   -19.9070 0 CHG=0 CFG=0
M  V30 1036 H     -29.5380    13.8486   -20.3110 0 CHG=0 CFG=0
M  V30 1037 C     -31.5060    13.4230   -21.1210 0 CHG=0 CFG=0
M  V30 1038 H     -32.4221    12.8996   -20.8375 0 CHG=0 CFG=0
M  V30 1039 H     -31.1372    12.9522   -22.0330 0 CHG=0 CFG=0
M  V30 1040 N     -31.8730    14.8260   -21.4650 0 CHG=1 CFG=0
M  V30 1041 H     -31.0447    15.3280   -21.8680 0 CHG=0 CFG=0
M  V30 1042 H     -32.1935    15.3352   -20.6114 0 CHG=0 CFG=0
M  V30 1043 H     -32.6431    14.8444   -22.1545 0 CHG=0 CFG=0
M  V30 1044 C     -28.5350    12.1170   -16.1620 0 CHG=0 CFG=0
M  V30 1045 O     -27.5590    12.8650   -16.1490 0 CHG=0 CFG=0
M  V30 1046 N     -28.7580    11.1740   -15.2450 0 CHG=0 CFG=0
M  V30 1047 H     -29.5520    10.5667   -15.3270 0 CHG=0 CFG=0
M  V30 1048 C     -27.8010    10.8010   -14.2110 0 CHG=0 CFG=1
M  V30 1049 H     -26.9939    11.5350   -14.1711 0 CHG=0 CFG=0
M  V30 1050 C     -28.5090    10.6740   -12.8660 0 CHG=0 CFG=0
M  V30 1051 H     -28.0487     9.8208   -12.3563 0 CHG=0 CFG=0
M  V30 1052 H     -29.5186    10.3097   -13.0633 0 CHG=0 CFG=0
M  V30 1053 C     -28.5900    11.7030   -11.7510 0 CHG=0 CFG=0
M  V30 1054 H     -29.3552    12.4400   -12.0017 0 CHG=0 CFG=0
M  V30 1055 C     -29.0180    10.9260   -10.5110 0 CHG=0 CFG=0
M  V30 1056 H     -28.2518    10.2217   -10.1817 0 CHG=0 CFG=0
M  V30 1057 H     -29.9372    10.3652   -10.6863 0 CHG=0 CFG=0
M  V30 1058 H     -29.2117    11.6026    -9.6792 0 CHG=0 CFG=0
M  V30 1059 C     -27.2770    12.4330   -11.5040 0 CHG=0 CFG=0
M  V30 1060 H     -27.0360    13.0828   -12.3418 0 CHG=0 CFG=0
M  V30 1061 H     -26.4594    11.7300   -11.3893 0 CHG=0 CFG=0
M  V30 1062 H     -27.3339    13.0487   -10.6095 0 CHG=0 CFG=0
M  V30 1063 C     -27.2310     9.4310   -14.5250 0 CHG=0 CFG=0
M  V30 1064 O     -27.9820     8.4870   -14.8040 0 CHG=0 CFG=0
M  V30 1065 N     -25.9110     9.3050   -14.4530 0 CHG=0 CFG=0
M  V30 1066 H     -25.3557    10.0922   -14.1886 0 CHG=0 CFG=0
M  V30 1067 C     -25.2730     7.9990   -14.6030 0 CHG=0 CFG=1
M  V30 1068 H     -25.5736     7.6167   -15.5812 0 CHG=0 CFG=0
M  V30 1069 C     -23.7390     8.1200   -14.5290 0 CHG=0 CFG=0
M  V30 1070 H     -23.4785     8.6891   -13.6351 0 CHG=0 CFG=0
M  V30 1071 C     -23.0700     6.7480   -14.4260 0 CHG=0 CFG=0
M  V30 1072 H     -23.3560     6.1036   -15.2581 0 CHG=0 CFG=0
M  V30 1073 H     -23.3234     6.2350   -13.4977 0 CHG=0 CFG=0
M  V30 1074 H     -21.9833     6.8432   -14.4471 0 CHG=0 CFG=0
M  V30 1075 C     -23.2230     8.8680   -15.7520 0 CHG=0 CFG=0
M  V30 1076 H     -23.6949     9.8452   -15.8491 0 CHG=0 CFG=0
M  V30 1077 H     -23.4039     8.3113   -16.6727 0 CHG=0 CFG=0
M  V30 1078 H     -22.1685     9.0442   -15.6617 0 CHG=0 CFG=0
M  V30 1079 C     -25.8310     7.0670   -13.5200 0 CHG=0 CFG=0
M  V30 1080 O     -25.8140     7.4000   -12.3370 0 CHG=0 CFG=0
M  V30 1081 N     -26.3450     5.9170   -13.9440 0 CHG=0 CFG=0
M  V30 1082 H     -26.3706     5.7525   -14.9346 0 CHG=0 CFG=0
M  V30 1083 C     -27.0180     4.9880   -13.0400 0 CHG=0 CFG=1
M  V30 1084 H     -27.5582     5.5977   -12.3119 0 CHG=0 CFG=0
M  V30 1085 C     -28.0240     4.1390   -13.8170 0 CHG=0 CFG=0
M  V30 1086 H     -27.4920     3.4444   -14.4699 0 CHG=0 CFG=0
M  V30 1087 H     -28.5918     4.7895   -14.4847 0 CHG=0 CFG=0
M  V30 1088 C     -29.0030     3.3770   -12.9360 0 CHG=0 CFG=0
M  V30 1089 H     -29.6093     4.0771   -12.3609 0 CHG=0 CFG=0
M  V30 1090 H     -28.4602     2.7605   -12.2186 0 CHG=0 CFG=0
M  V30 1091 C     -29.9360     2.4680   -13.7170 0 CHG=0 CFG=0
M  V30 1092 O     -30.0970     2.6100   -14.9320 0 CHG=0 CFG=0
M  V30 1093 N     -30.5610     1.5260   -13.0170 0 CHG=0 CFG=0
M  V30 1094 H     -30.4114     1.4383   -12.0335 0 CHG=0 CFG=0
M  V30 1095 H     -31.1867     0.9137   -13.4949 0 CHG=0 CFG=0
M  V30 1096 C     -26.0190     4.0970   -12.3100 0 CHG=0 CFG=0
M  V30 1097 O     -25.1710     3.4620   -12.9440 0 CHG=0 CFG=0
M  V30 1098 N     -26.1250     4.0690   -10.9800 0 CHG=0 CFG=0
M  V30 1099 H     -26.8484     4.6081   -10.5506 0 CHG=0 CFG=0
M  V30 1100 C     -25.2920     3.2250   -10.1200 0 CHG=0 CFG=1
M  V30 1101 H     -24.3261     3.0892   -10.6106 0 CHG=0 CFG=0
M  V30 1102 C     -25.0920     3.8880    -8.7470 0 CHG=0 CFG=0
M  V30 1103 H     -26.0920     4.1004    -8.3619 0 CHG=0 CFG=0
M  V30 1104 H     -24.6374     4.8705    -8.8798 0 CHG=0 CFG=0
M  V30 1105 C     -24.3360     3.0990    -7.6640 0 CHG=0 CFG=0
M  V30 1106 H     -24.4853     2.0280    -7.8037 0 CHG=0 CFG=0
M  V30 1107 C     -22.8530     3.4060    -7.7540 0 CHG=0 CFG=0
M  V30 1108 H     -22.6481     4.4703    -7.6298 0 CHG=0 CFG=0
M  V30 1109 H     -22.4493     3.0909    -8.7164 0 CHG=0 CFG=0
M  V30 1110 H     -22.3233     2.8691    -6.9674 0 CHG=0 CFG=0
M  V30 1111 C     -24.8330     3.4330    -6.2640 0 CHG=0 CFG=0
M  V30 1112 H     -25.9078     3.2742    -6.1876 0 CHG=0 CFG=0
M  V30 1113 H     -24.6399     4.4759    -6.0153 0 CHG=0 CFG=0
M  V30 1114 H     -24.3530     2.8129    -5.5062 0 CHG=0 CFG=0
M  V30 1115 C     -25.9690     1.8710    -9.9430 0 CHG=0 CFG=0
M  V30 1116 O     -27.0170     1.7840    -9.3010 0 CHG=0 CFG=0
M  V30 1117 N     -25.3820     0.8230   -10.5200 0 CHG=0 CFG=0
M  V30 1118 H     -24.5158     0.9671   -10.9921 0 CHG=0 CFG=0
M  V30 1119 C     -25.9740    -0.5160   -10.4710 0 CHG=0 CFG=1
M  V30 1120 H     -27.0535    -0.3933   -10.5476 0 CHG=0 CFG=0
M  V30 1121 C     -25.4340    -1.3970   -11.5980 0 CHG=0 CFG=0
M  V30 1122 H     -25.7610    -2.4266   -11.4459 0 CHG=0 CFG=0
M  V30 1123 H     -24.3443    -1.4188   -11.5585 0 CHG=0 CFG=0
M  V30 1124 C     -25.8890    -1.0190   -12.9890 0 CHG=0 CFG=0
M  V30 1125 C     -27.2010    -0.6090   -13.2400 0 CHG=0 CFG=0
M  V30 1126 H     -27.9292    -0.5565   -12.4463 0 CHG=0 CFG=0
M  V30 1127 C     -27.6120    -0.2700   -14.5270 0 CHG=0 CFG=0
M  V30 1128 H     -28.6299     0.0446   -14.7062 0 CHG=0 CFG=0
M  V30 1129 C     -25.0060    -1.0900   -14.0630 0 CHG=0 CFG=0
M  V30 1130 H     -23.9865    -1.4045   -13.9131 0 CHG=0 CFG=0
M  V30 1131 C     -25.4050    -0.7620   -15.3470 0 CHG=0 CFG=0
M  V30 1132 H     -24.7120    -0.8149   -16.1745 0 CHG=0 CFG=0
M  V30 1133 C     -26.7080    -0.3520   -15.5740 0 CHG=0 CFG=0
M  V30 1134 O     -27.0890    -0.0230   -16.8560 0 CHG=0 CFG=0
M  V30 1135 H     -27.4457     0.8585   -16.8734 0 CHG=0 CFG=0
M  V30 1136 C     -25.7480    -1.2150    -9.1400 0 CHG=0 CFG=0
M  V30 1137 O     -26.5770    -2.0200    -8.7060 0 CHG=0 CFG=0
M  V30 1138 N     -24.6190    -0.9150    -8.5100 0 CHG=0 CFG=0
M  V30 1139 H     -23.9675    -0.2822    -8.9324 0 CHG=0 CFG=0
M  V30 1140 C     -24.2520    -1.5190    -7.2380 0 CHG=0 CFG=0
M  V30 1141 H     -24.5292    -2.5745    -7.2591 0 CHG=0 CFG=0
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M  V30 1143 C     -22.7710    -1.3880    -6.9720 0 CHG=0 CFG=0
M  V30 1144 O     -22.0380    -0.7870    -7.7580 0 CHG=0 CFG=0
M  V30 1145 N     -22.3300    -1.9440    -5.8530 0 CHG=0 CFG=0
M  V30 1146 H     -22.9555    -2.4419    -5.2508 0 CHG=0 CFG=0
M  V30 1147 C     -20.9270    -1.8940    -5.4680 0 CHG=0 CFG=1
M  V30 1148 H     -20.3448    -1.5770    -6.3344 0 CHG=0 CFG=0
M  V30 1149 C     -20.6720    -0.9150    -4.2800 0 CHG=0 CFG=0
M  V30 1150 H     -19.6147    -0.9736    -4.0124 0 CHG=0 CFG=0
M  V30 1151 C     -20.9460     0.5280    -4.6930 0 CHG=0 CFG=0
M  V30 1152 H     -21.9809     0.6663    -5.0066 0 CHG=0 CFG=0
M  V30 1153 H     -20.3033     0.8293    -5.5206 0 CHG=0 CFG=0
M  V30 1154 H     -20.7663     1.2122    -3.8643 0 CHG=0 CFG=0
M  V30 1155 C     -21.4880    -1.3010    -3.0460 0 CHG=0 CFG=0
M  V30 1156 H     -21.3077    -2.3292    -2.7291 0 CHG=0 CFG=0
M  V30 1157 H     -22.5491    -1.1953    -3.2630 0 CHG=0 CFG=0
M  V30 1158 H     -21.2550    -0.6498    -2.2027 0 CHG=0 CFG=0
M  V30 1159 C     -20.4500    -3.2980    -5.1120 0 CHG=0 CFG=0
M  V30 1160 O     -21.2610    -4.1710    -4.8170 0 CHG=0 CFG=0
M  V30 1161 N     -19.1380    -3.5080    -5.1680 0 CHG=0 CFG=0
M  V30 1162 H     -18.5507    -2.7391    -5.4300 0 CHG=0 CFG=0
M  V30 1163 C     -18.5240    -4.7600    -4.7250 0 CHG=0 CFG=1
M  V30 1164 H     -19.2907    -5.3988    -4.2796 0 CHG=0 CFG=0
M  V30 1165 C     -17.8470    -5.4800    -5.8920 0 CHG=0 CFG=0
M  V30 1166 H     -17.4929    -6.4532    -5.5508 0 CHG=0 CFG=0
M  V30 1167 H     -16.9542    -4.9410    -6.2060 0 CHG=0 CFG=0
M  V30 1168 S     -18.8990    -5.7480    -7.3400 0 CHG=0 CFG=0
M  V30 1169 H     -19.9884    -6.4266    -6.9702 0 CHG=0 CFG=0
M  V30 1170 C     -17.4930    -4.3930    -3.6730 0 CHG=0 CFG=0
M  V30 1171 O     -16.5050    -3.7360    -3.9810 0 CHG=0 CFG=0
M  V30 1172 N     -17.7140    -4.8150    -2.4310 0 CHG=0 CFG=0
M  V30 1173 H     -18.5935    -5.2553    -2.2269 0 CHG=0 CFG=0
M  V30 1174 C     -16.8950    -4.3050    -1.3300 0 CHG=0 CFG=1
M  V30 1175 H     -15.9964    -3.8605    -1.7594 0 CHG=0 CFG=0
M  V30 1176 C     -17.6410    -3.1990    -0.5530 0 CHG=0 CFG=2
M  V30 1177 H     -18.0153    -2.4466    -1.2490 0 CHG=0 CFG=0
M  V30 1178 O     -16.7130    -2.5320     0.3190 0 CHG=0 CFG=0
M  V30 1179 H     -16.1866    -3.1651     0.8097 0 CHG=0 CFG=0
M  V30 1180 C     -18.8030    -3.7880     0.2650 0 CHG=0 CFG=0
M  V30 1181 H     -18.4762    -4.4732     1.0464 0 CHG=0 CFG=0
M  V30 1182 H     -19.4921    -4.3176    -0.3829 0 CHG=0 CFG=0
M  V30 1183 H     -19.3746    -2.9940     0.7420 0 CHG=0 CFG=0
M  V30 1184 C     -16.3620    -5.3540    -0.3510 0 CHG=0 CFG=0
M  V30 1185 O     -15.6390    -5.0200     0.5930 0 CHG=0 CFG=0
M  V30 1186 N     -16.7130    -6.6150    -0.5870 0 CHG=0 CFG=0
M  V30 1187 H     -17.3227    -6.7663    -1.3599 0 CHG=0 CFG=0
M  V30 1188 C     -16.2650    -7.7180     0.2600 0 CHG=0 CFG=1
M  V30 1189 H     -16.3626    -7.3855     1.2957 0 CHG=0 CFG=0
M  V30 1190 C     -17.1410    -8.9510     0.0300 0 CHG=0 CFG=0
M  V30 1191 H     -16.7128    -9.8160     0.5400 0 CHG=0 CFG=0
M  V30 1192 H     -17.1191    -9.1896    -1.0346 0 CHG=0 CFG=0
M  V30 1193 C     -18.5750    -8.7520     0.5050 0 CHG=0 CFG=0
M  V30 1194 H     -18.8655    -7.7132     0.3305 0 CHG=0 CFG=0
M  V30 1195 H     -18.6308    -8.9007     1.5835 0 CHG=0 CFG=0
M  V30 1196 C     -19.5560    -9.6440    -0.2370 0 CHG=0 CFG=0
M  V30 1197 H     -19.4082   -10.6926     0.0248 0 CHG=0 CFG=0
M  V30 1198 H     -19.3614    -9.5690    -1.3093 0 CHG=0 CFG=0
M  V30 1199 C     -20.9910    -9.1960     0.0060 0 CHG=0 CFG=0
M  V30 1200 H     -21.6616    -9.7046    -0.6781 0 CHG=0 CFG=0
M  V30 1201 H     -21.0856    -8.1296    -0.1926 0 CHG=0 CFG=0
M  V30 1202 N     -21.4580    -9.4810     1.3960 0 CHG=1 CFG=0
M  V30 1203 H     -20.7471    -9.0208     2.0062 0 CHG=0 CFG=0
M  V30 1204 H     -21.4835   -10.4957     1.6119 0 CHG=0 CFG=0
M  V30 1205 H     -22.3538    -8.9871     1.5703 0 CHG=0 CFG=0
M  V30 1206 C     -14.7860    -8.0320     0.0270 0 CHG=0 CFG=0
M  V30 1207 O     -14.1190    -8.6150     0.8880 0 CHG=0 CFG=0
M  V30 1208 N     -14.2890    -7.6370    -1.1420 0 CHG=0 CFG=0
M  V30 1209 H     -14.8054    -7.0084    -1.7197 0 CHG=0 CFG=0
M  V30 1210 C     -12.8700    -7.7100    -1.4660 0 CHG=0 CFG=1
M  V30 1211 H     -12.3225    -8.0635    -0.5898 0 CHG=0 CFG=0
M  V30 1212 C     -12.6550    -8.6470    -2.6290 0 CHG=0 CFG=0
M  V30 1213 H     -13.0093    -9.6399    -2.3506 0 CHG=0 CFG=0
M  V30 1214 H     -11.5872    -8.7615    -2.8232 0 CHG=0 CFG=0
M  V30 1215 C     -13.3580    -8.2020    -3.9330 0 CHG=0 CFG=0
M  V30 1216 H     -12.9430    -7.2550    -4.2817 0 CHG=0 CFG=0
M  V30 1217 H     -14.4176    -8.0287    -3.7487 0 CHG=0 CFG=0
M  V30 1218 C     -13.2400    -9.2080    -5.0950 0 CHG=0 CFG=0
M  V30 1219 O     -12.3911   -10.0897    -5.0766 0 CHG=0 CFG=0
M  V30 1220 N     -14.1216    -9.0405    -6.0954 0 CHG=0 CFG=0
M  V30 1221 H     -14.7423    -8.2601    -6.1085 0 CHG=0 CFG=0
M  V30 1222 H     -14.1196    -9.6976    -6.8460 0 CHG=0 CFG=0
M  V30 1223 C     -12.3500    -6.3180    -1.8150 0 CHG=0 CFG=0
M  V30 1224 O     -13.1350    -5.3840    -2.0150 0 CHG=0 CFG=0
M  V30 1225 N     -11.0290    -6.1820    -1.8800 0 CHG=0 CFG=0
M  V30 1226 H     -10.4100    -6.9618    -1.8044 0 CHG=0 CFG=0
M  V30 1227 C     -10.4030    -4.9160    -2.2590 0 CHG=0 CFG=1
M  V30 1228 H     -11.1969    -4.2346    -2.5401 0 CHG=0 CFG=0
M  V30 1229 C      -9.6810    -4.2870    -1.0630 0 CHG=0 CFG=0
M  V30 1230 H      -9.2930    -3.3646    -1.4270 0 CHG=0 CFG=0
M  V30 1231 H      -8.8366    -4.8791    -0.7107 0 CHG=0 CFG=0
M  V30 1232 C     -10.6100    -3.8550     0.0660 0 CHG=0 CFG=0
M  V30 1233 H     -10.7386    -4.6773     0.7684 0 CHG=0 CFG=0
M  V30 1234 H     -11.6024    -3.6314    -0.3302 0 CHG=0 CFG=0
M  V30 1235 C     -10.1010    -2.6050     0.7680 0 CHG=0 CFG=0
M  V30 1236 H     -10.1637    -1.7206     0.1294 0 CHG=0 CFG=0
M  V30 1237 H      -9.0689    -2.7527     1.0597 0 CHG=0 CFG=0
M  V30 1238 N     -10.8460    -2.3010     1.9890 0 CHG=0 CFG=0
M  V30 1239 H     -11.6854    -1.8130     1.7681 0 CHG=0 CFG=0
M  V30 1240 C     -10.4910    -2.6980     3.2100 0 CHG=0 CFG=0
M  V30 1241 N      -9.3940    -3.4280     3.3930 0 CHG=1 CFG=0
M  V30 1242 H      -8.8428    -3.6156     2.5749 0 CHG=0 CFG=0
M  V30 1243 H      -9.0981    -3.7718     4.2789 0 CHG=0 CFG=0
M  V30 1244 N     -11.2400    -2.3660     4.2540 0 CHG=0 CFG=0
M  V30 1245 H     -12.0280    -1.7661     4.0625 0 CHG=0 CFG=0
M  V30 1246 H     -11.0691    -2.6526     5.1921 0 CHG=0 CFG=0
M  V30 1247 C      -9.4510    -5.1040    -3.4480 0 CHG=0 CFG=0
M  V30 1248 O      -8.7660    -6.1260    -3.5310 0 CHG=0 CFG=0
M  V30 1249 N      -9.4060    -4.1270    -4.3800 0 CHG=0 CFG=0
M  V30 1250 C      -8.5340    -4.2900    -5.5580 0 CHG=0 CFG=0
M  V30 1251 H      -8.5981    -5.2970    -5.9732 0 CHG=0 CFG=0
M  V30 1252 H      -7.5018    -4.0955    -5.2627 0 CHG=0 CFG=0
M  V30 1253 C     -10.1230    -2.8450    -4.4180 0 CHG=0 CFG=1
M  V30 1254 H      -9.9466    -2.2693    -3.5109 0 CHG=0 CFG=0
M  V30 1255 C      -9.5160    -2.1470    -5.6410 0 CHG=0 CFG=0
M  V30 1256 H      -8.6655    -1.5493    -5.3088 0 CHG=0 CFG=0
M  V30 1257 H     -10.2058    -1.4683    -6.1457 0 CHG=0 CFG=0
M  V30 1258 C      -9.0410    -3.2510    -6.5100 0 CHG=0 CFG=0
M  V30 1259 H      -9.8810    -3.6551    -7.0735 0 CHG=0 CFG=0
M  V30 1260 H      -8.2815    -2.9292    -7.2221 0 CHG=0 CFG=0
M  V30 1261 C     -11.6330    -2.9860    -4.5960 0 CHG=0 CFG=0
M  V30 1262 O     -12.0890    -3.9000    -5.2860 0 CHG=0 CFG=0
M  V30 1263 N     -12.3920    -2.0850    -3.9720 0 CHG=0 CFG=0
M  V30 1264 H     -11.9402    -1.3754    -3.4295 0 CHG=0 CFG=0
M  V30 1265 C     -13.8500    -2.0770    -4.1130 0 CHG=0 CFG=1
M  V30 1266 H     -14.1519    -3.1217    -4.0161 0 CHG=0 CFG=0
M  V30 1267 C     -14.5690    -1.2530    -3.0020 0 CHG=0 CFG=1
M  V30 1268 H     -15.6360    -1.4674    -3.0769 0 CHG=0 CFG=0
M  V30 1269 C     -14.1080    -1.7090    -1.6200 0 CHG=0 CFG=0
M  V30 1270 H     -13.0929    -1.3708    -1.4045 0 CHG=0 CFG=0
M  V30 1271 H     -14.1096    -2.7941    -1.5268 0 CHG=0 CFG=0
M  V30 1272 H     -14.7472    -1.3093    -0.8329 0 CHG=0 CFG=0
M  V30 1273 C     -14.3850     0.2560    -3.2040 0 CHG=0 CFG=0
M  V30 1274 H     -14.6494     0.5746    -4.2110 0 CHG=0 CFG=0
M  V30 1275 H     -13.3251     0.4422    -3.0496 0 CHG=0 CFG=0
M  V30 1276 C     -15.1310     1.1450    -2.2040 0 CHG=0 CFG=0
M  V30 1277 H     -14.8023     0.9545    -1.1812 0 CHG=0 CFG=0
M  V30 1278 H     -16.2059     0.9726    -2.2477 0 CHG=0 CFG=0
M  V30 1279 H     -14.9488     2.1983    -2.4122 0 CHG=0 CFG=0
M  V30 1280 C     -14.2470    -1.5930    -5.5100 0 CHG=0 CFG=0
M  V30 1281 O     -13.5370    -0.7880    -6.1160 0 CHG=0 CFG=0
M  V30 1282 N     -15.3620    -2.1130    -6.0200 0 CHG=0 CFG=0
M  V30 1283 H     -15.8905    -2.7072    -5.4168 0 CHG=0 CFG=0
M  V30 1284 C     -15.8500    -1.7400    -7.3480 0 CHG=0 CFG=1
M  V30 1285 H     -15.0951    -1.1341    -7.8478 0 CHG=0 CFG=0
M  V30 1286 C     -16.1890    -2.9710    -8.2020 0 CHG=0 CFG=0
M  V30 1287 H     -16.5415    -2.6356    -9.1741 0 CHG=0 CFG=0
M  V30 1288 H     -17.0250    -3.5155    -7.7653 0 CHG=0 CFG=0
M  V30 1289 C     -15.0430    -3.9180    -8.4410 0 CHG=0 CFG=0
M  V30 1290 C     -13.7200    -3.5240    -8.2780 0 CHG=0 CFG=0
M  V30 1291 H     -13.4494    -2.5320    -7.9530 0 CHG=0 CFG=0
M  V30 1292 C     -15.3030    -5.2140    -8.8790 0 CHG=0 CFG=0
M  V30 1293 H     -16.3260    -5.5327    -9.0269 0 CHG=0 CFG=0
M  V30 1294 C     -12.6760    -4.4170    -8.5090 0 CHG=0 CFG=0
M  V30 1295 H     -11.6576    -4.0987    -8.3452 0 CHG=0 CFG=0
M  V30 1296 C     -14.2680    -6.1110    -9.1200 0 CHG=0 CFG=0
M  V30 1297 H     -14.4928    -7.1175    -9.4418 0 CHG=0 CFG=0
M  V30 1298 C     -12.9520    -5.7100    -8.9350 0 CHG=0 CFG=0
M  V30 1299 H     -12.1383    -6.3995    -9.1057 0 CHG=0 CFG=0
M  V30 1300 C     -17.1150    -0.9110    -7.2530 0 CHG=0 CFG=0
M  V30 1301 O     -17.9700    -1.1710    -6.4060 0 CHG=0 CFG=0
M  V30 1302 N     -17.2290     0.0790    -8.1340 0 CHG=0 CFG=0
M  V30 1303 H     -16.4902     0.2358    -8.7782 0 CHG=0 CFG=0
M  V30 1304 C     -18.4870     0.7770    -8.3660 0 CHG=0 CFG=1
M  V30 1305 H     -19.2223     0.4337    -7.6343 0 CHG=0 CFG=0
M  V30 1306 C     -18.3310     2.3140    -8.2610 0 CHG=0 CFG=1
M  V30 1307 H     -17.6875     2.6590    -9.0524 0 CHG=0 CFG=0
M  V30 1308 C     -19.6780     2.9920    -8.4450 0 CHG=0 CFG=0
M  V30 1309 H     -20.3341     2.7032    -7.6288 0 CHG=0 CFG=0
M  V30 1310 H     -20.1619     2.7238    -9.3830 0 CHG=0 CFG=0
M  V30 1311 H     -19.5911     4.0771    -8.4377 0 CHG=0 CFG=0
M  V30 1312 C     -17.6900     2.7080    -6.9250 0 CHG=0 CFG=0
M  V30 1313 H     -16.7703     2.1423    -6.7709 0 CHG=0 CFG=0
M  V30 1314 H     -18.3460     2.4268    -6.1013 0 CHG=0 CFG=0
M  V30 1315 C     -17.3160     4.1890    -6.8290 0 CHG=0 CFG=0
M  V30 1316 H     -18.1931     4.8323    -6.8833 0 CHG=0 CFG=0
M  V30 1317 H     -16.6299     4.4719    -7.6259 0 CHG=0 CFG=0
M  V30 1318 H     -16.8241     4.3952    -5.8774 0 CHG=0 CFG=0
M  V30 1319 C     -18.9720     0.4050    -9.7660 0 CHG=0 CFG=0
M  V30 1320 O     -18.2910     0.6700   -10.7600 0 CHG=0 CFG=0
M  V30 1321 N     -20.1490    -0.2020    -9.8420 0 CHG=0 CFG=0
M  V30 1322 H     -20.7185    -0.3118    -9.0253 0 CHG=0 CFG=0
M  V30 1323 C     -20.6620    -0.7170   -11.1100 0 CHG=0 CFG=1
M  V30 1324 H     -19.8404    -0.7531   -11.8275 0 CHG=0 CFG=0
M  V30 1325 C     -21.2390    -2.1460   -10.9440 0 CHG=0 CFG=1
M  V30 1326 H     -22.1644    -2.0695   -10.3730 0 CHG=0 CFG=0
M  V30 1327 C     -21.5550    -2.7830   -12.2940 0 CHG=0 CFG=0
M  V30 1328 H     -20.6801    -2.8063   -12.9444 0 CHG=0 CFG=0
M  V30 1329 H     -22.3302    -2.2303   -12.8185 0 CHG=0 CFG=0
M  V30 1330 H     -21.9096    -3.8071   -12.1775 0 CHG=0 CFG=0
M  V30 1331 C     -20.2730    -3.0410   -10.1540 0 CHG=0 CFG=0
M  V30 1332 H     -20.7211    -4.0295   -10.0397 0 CHG=0 CFG=0
M  V30 1333 H     -20.1679    -2.6677    -9.1341 0 CHG=0 CFG=0
M  V30 1334 C     -18.8970    -3.2030   -10.7700 0 CHG=0 CFG=0
M  V30 1335 H     -18.3895    -2.2456   -10.8718 0 CHG=0 CFG=0
M  V30 1336 H     -18.9511    -3.6673   -11.7541 0 CHG=0 CFG=0
M  V30 1337 H     -18.2760    -3.8448   -10.1455 0 CHG=0 CFG=0
M  V30 1338 C     -21.7230     0.2330   -11.6420 0 CHG=0 CFG=0
M  V30 1339 O     -22.7130     0.5110   -10.9660 0 CHG=0 CFG=0
M  V30 1340 N     -21.5050     0.7450   -12.8500 0 CHG=0 CFG=0
M  V30 1341 H     -20.7034     0.4802   -13.3893 0 CHG=0 CFG=0
M  V30 1342 C     -22.4080     1.7400   -13.4130 0 CHG=0 CFG=1
M  V30 1343 H     -23.3464     1.7030   -12.8560 0 CHG=0 CFG=0
M  V30 1344 C     -21.8230     3.1850   -13.3210 0 CHG=0 CFG=2
M  V30 1345 H     -22.6358     3.9040   -13.4911 0 CHG=0 CFG=0
M  V30 1346 O     -20.8070     3.3670   -14.3180 0 CHG=0 CFG=0
M  V30 1347 H     -21.2015     3.3404   -15.1967 0 CHG=0 CFG=0
M  V30 1348 C     -21.2670     3.4930   -11.9250 0 CHG=0 CFG=0
M  V30 1349 H     -20.4230     2.8494   -11.6799 0 CHG=0 CFG=0
M  V30 1350 H     -22.0287     3.3607   -11.1569 0 CHG=0 CFG=0
M  V30 1351 H     -20.9164     4.5164   -11.8787 0 CHG=0 CFG=0
M  V30 1352 C     -22.7690     1.4740   -14.8720 0 CHG=0 CFG=0
M  V30 1353 O     -22.1550     0.6530   -15.5600 0 CHG=0 CFG=0
M  V30 1354 N     -23.7930     2.1910   -15.3150 0 CHG=0 CFG=0
M  V30 1355 H     -24.3313     2.6941   -14.6352 0 CHG=0 CFG=0
M  V30 1356 C     -24.1010     2.3980   -16.7130 0 CHG=0 CFG=1
M  V30 1357 H     -24.5889     1.4958   -17.0831 0 CHG=0 CFG=0
M  V30 1358 C     -25.0260     3.6120   -16.7660 0 CHG=0 CFG=0
M  V30 1359 H     -24.5906     4.4210   -16.1782 0 CHG=0 CFG=0
M  V30 1360 H     -25.9468     3.3370   -16.2492 0 CHG=0 CFG=0
M  V30 1361 C     -25.3660     4.1500   -18.1170 0 CHG=0 CFG=0
M  V30 1362 H     -25.6764     3.3341   -18.7716 0 CHG=0 CFG=0
M  V30 1363 H     -24.5006     4.6234   -18.5816 0 CHG=0 CFG=0
M  V30 1364 C     -26.4910     5.1610   -18.0490 0 CHG=0 CFG=0
M  V30 1365 O     -26.7630     5.7080   -16.9530 0 CHG=0 CFG=0
M  V30 1366 O     -27.1100     5.3920   -19.0970 0 CHG=-1 CFG=0
M  V30 1367 C     -22.8190     2.6760   -17.5070 0 CHG=0 CFG=0
M  V30 1368 O     -21.9540     3.4190   -17.0460 0 CHG=0 CFG=0
M  V30 1369 N     -22.7010     2.0560   -18.6810 0 CHG=0 CFG=0
M  V30 1370 H     -23.4837     1.5301   -19.0131 0 CHG=0 CFG=0
M  V30 1371 C     -21.5560     2.2580   -19.5700 0 CHG=0 CFG=1
M  V30 1372 H     -20.6970     2.5002   -18.9412 0 CHG=0 CFG=0
M  V30 1373 C     -21.2470     0.9840   -20.3690 0 CHG=0 CFG=0
M  V30 1374 H     -22.1683     0.6332   -20.8374 0 CHG=0 CFG=0
M  V30 1375 H     -20.9278     0.1882   -19.6972 0 CHG=0 CFG=0
M  V30 1376 C     -20.1960     1.1660   -21.4480 0 CHG=0 CFG=0
M  V30 1377 C     -18.9170     1.6360   -21.1340 0 CHG=0 CFG=0
M  V30 1378 H     -18.6764     1.8671   -20.1055 0 CHG=0 CFG=0
M  V30 1379 C     -17.9470     1.8070   -22.1150 0 CHG=0 CFG=0
M  V30 1380 H     -16.9690     2.1650   -21.8305 0 CHG=0 CFG=0
M  V30 1381 C     -20.4770     0.8790   -22.7830 0 CHG=0 CFG=0
M  V30 1382 H     -21.4580     0.5146   -23.0656 0 CHG=0 CFG=0
M  V30 1383 C     -19.5090     1.0490   -23.7770 0 CHG=0 CFG=0
M  V30 1384 H     -19.7555     0.8205   -24.8037 0 CHG=0 CFG=0
M  V30 1385 C     -18.2470     1.5130   -23.4310 0 CHG=0 CFG=0
M  V30 1386 O     -17.2810     1.6880   -24.3960 0 CHG=0 CFG=0
M  V30 1387 H     -16.9277     2.5709   -24.3452 0 CHG=0 CFG=0
M  V30 1388 C     -21.8120     3.4230   -20.5160 0 CHG=0 CFG=0
M  V30 1389 O     -22.8290     3.4530   -21.2040 0 CHG=0 CFG=0
M  V30 1390 N     -20.8740     4.3690   -20.5550 0 CHG=0 CFG=0
M  V30 1391 H     -20.0977     4.2592   -19.9444 0 CHG=0 CFG=0
M  V30 1392 C     -21.0290     5.5830   -21.3540 0 CHG=0 CFG=1
M  V30 1393 H     -22.0196     5.5821   -21.8145 0 CHG=0 CFG=0
M  V30 1394 C     -20.9190     6.8170   -20.4530 0 CHG=0 CFG=0
M  V30 1395 H     -20.9947     7.7210   -21.0563 0 CHG=0 CFG=0
M  V30 1396 H     -19.9238     6.8424   -20.0074 0 CHG=0 CFG=0
M  V30 1397 C     -21.9570     6.8530   -19.3220 0 CHG=0 CFG=0
M  V30 1398 H     -21.7107     7.6630   -18.6384 0 CHG=0 CFG=0
M  V30 1399 H     -21.9244     5.9486   -18.7129 0 CHG=0 CFG=0
M  V30 1400 S     -23.6530     7.1250   -19.8760 0 CHG=0 CFG=0
M  V30 1401 C     -23.5640     8.8730   -20.2610 0 CHG=0 CFG=0
M  V30 1402 H     -22.7672     9.0523   -20.9750 0 CHG=0 CFG=0
M  V30 1403 H     -23.3107     9.4456   -19.3738 0 CHG=0 CFG=0
M  V30 1404 H     -24.4971     9.2230   -20.6969 0 CHG=0 CFG=0
M  V30 1405 C     -19.9830     5.6060   -22.4750 0 CHG=0 CFG=0
M  V30 1406 O     -18.8470     6.0530   -22.2800 0 CHG=0 CFG=0
M  V30 1407 N     -20.3870     5.1250   -23.6490 0 CHG=0 CFG=0
M  V30 1408 H     -21.3406     4.8308   -23.7109 0 CHG=0 CFG=0
M  V30 1409 C     -19.4570     4.7700   -24.7280 0 CHG=0 CFG=1
M  V30 1410 H     -18.8274     4.0061   -24.2929 0 CHG=0 CFG=0
M  V30 1411 C     -20.2130     4.1760   -25.9100 0 CHG=0 CFG=0
M  V30 1412 H     -20.8657     4.9183   -26.3713 0 CHG=0 CFG=0
M  V30 1413 H     -20.8330     3.3337   -25.6018 0 CHG=0 CFG=0
M  V30 1414 H     -19.5276     3.8171   -26.6787 0 CHG=0 CFG=0
M  V30 1415 C     -18.5340     5.8930   -25.1980 0 CHG=0 CFG=0
M  V30 1416 O     -17.3960     5.6340   -25.6070 0 CHG=0 CFG=0
M  V30 1417 N     -19.0170     7.1320   -25.1360 0 CHG=0 CFG=0
M  V30 1418 H     -19.8889     7.3177   -24.6833 0 CHG=0 CFG=0
M  V30 1419 C     -18.2330     8.2650   -25.6180 0 CHG=0 CFG=1
M  V30 1420 H     -17.4847     7.8804   -26.3124 0 CHG=0 CFG=0
M  V30 1421 C     -19.1110     9.2470   -26.3990 0 CHG=0 CFG=0
M  V30 1422 H     -18.6149    10.2136   -26.4937 0 CHG=0 CFG=0
M  V30 1423 H     -20.0504     9.4284   -25.8786 0 CHG=0 CFG=0
M  V30 1424 C     -19.3840     8.7720   -27.8170 0 CHG=0 CFG=0
M  V30 1425 O     -18.4643     8.4316   -28.5704 0 CHG=0 CFG=0
M  V30 1426 N     -20.6557     8.7722   -28.1980 0 CHG=0 CFG=0
M  V30 1427 H     -21.3965     9.0306   -27.5765 0 CHG=0 CFG=0
M  V30 1428 H     -20.8950     8.5022   -29.1292 0 CHG=0 CFG=0
M  V30 1429 C     -17.3990     8.9580   -24.5380 0 CHG=0 CFG=0
M  V30 1430 O     -16.7820     9.9930   -24.7870 0 CHG=0 CFG=0
M  V30 1431 N     -17.3800     8.3680   -23.3460 0 CHG=0 CFG=0
M  V30 1432 H     -18.0051     7.6060   -23.1818 0 CHG=0 CFG=0
M  V30 1433 C     -16.4400     8.7620   -22.3020 0 CHG=0 CFG=0
M  V30 1434 H     -15.4408     8.7276   -22.7392 0 CHG=0 CFG=0
M  V30 1435 H     -16.5023     7.9945   -21.5304 0 CHG=0 CFG=0
M  V30 1436 C     -16.6910    10.1120   -21.6740 0 CHG=0 CFG=0
M  V30 1437 O     -17.8270    10.6050   -21.6440 0 CHG=0 CFG=0
M  V30 1438 N     -15.6050    10.7250   -21.2170 0 CHG=0 CFG=0
M  V30 1439 H     -14.7288    10.3100   -21.4472 0 CHG=0 CFG=0
M  V30 1440 C     -15.6460    11.9800   -20.4750 0 CHG=0 CFG=1
M  V30 1441 H     -16.3733    11.8665   -19.6752 0 CHG=0 CFG=0
M  V30 1442 C     -14.2670    12.2370   -19.8870 0 CHG=0 CFG=0
M  V30 1443 H     -13.5309    12.3286   -20.6872 0 CHG=0 CFG=0
M  V30 1444 H     -13.9593    11.3919   -19.2711 0 CHG=0 CFG=0
M  V30 1445 S     -14.2070    13.7000   -18.8980 0 CHG=0 CFG=0
M  V30 1446 H     -14.7288    13.4358   -17.6943 0 CHG=0 CFG=0
M  V30 1447 C     -16.0720    13.1660   -21.3470 0 CHG=0 CFG=0
M  V30 1448 O     -15.5700    13.3220   -22.4640 0 CHG=0 CFG=0
M  V30 1449 N     -16.9890    13.9970   -20.8430 0 CHG=0 CFG=0
M  V30 1450 H     -17.3120    13.8334   -19.9151 0 CHG=0 CFG=0
M  V30 1451 C     -17.4590    15.1520   -21.6190 0 CHG=0 CFG=1
M  V30 1452 H     -17.9054    14.7409   -22.5252 0 CHG=0 CFG=0
M  V30 1453 C     -18.5100    15.9530   -20.8350 0 CHG=0 CFG=0
M  V30 1454 H     -18.0898    16.2308   -19.8737 0 CHG=0 CFG=0
M  V30 1455 H     -19.3533    15.2971   -20.6155 0 CHG=0 CFG=0
M  V30 1456 C     -19.0250    17.2240   -21.5260 0 CHG=0 CFG=0
M  V30 1457 H     -18.1882    17.8786   -21.7272 0 CHG=0 CFG=0
M  V30 1458 C     -19.7280    16.9010   -22.8410 0 CHG=0 CFG=0
M  V30 1459 H     -20.5580    16.2110   -22.6899 0 CHG=0 CFG=0
M  V30 1460 H     -19.0449    16.4480   -23.5596 0 CHG=0 CFG=0
M  V30 1461 H     -20.1280    17.8031   -23.3060 0 CHG=0 CFG=0
M  V30 1462 C     -19.9680    17.9940   -20.5930 0 CHG=0 CFG=0
M  V30 1463 H     -19.4650    18.2657   -19.6664 0 CHG=0 CFG=0
M  V30 1464 H     -20.8397    17.3969   -20.3340 0 CHG=0 CFG=0
M  V30 1465 H     -20.3207    18.9129   -21.0623 0 CHG=0 CFG=0
M  V30 1466 C     -16.3210    16.0790   -22.0410 0 CHG=0 CFG=0
M  V30 1467 O     -16.3150    16.5970   -23.1640 0 CHG=0 CFG=0
M  V30 1468 N     -15.3670    16.2930   -21.1430 0 CHG=0 CFG=0
M  V30 1469 H     -15.4682    15.8125   -20.2706 0 CHG=0 CFG=0
M  V30 1470 C     -14.2660    17.2190   -21.4230 0 CHG=0 CFG=1
M  V30 1471 H     -14.7377    18.1791   -21.6368 0 CHG=0 CFG=0
M  V30 1472 C     -13.3280    17.3280   -20.2170 0 CHG=0 CFG=0
M  V30 1473 H     -12.9020    16.3436   -20.0131 0 CHG=0 CFG=0
M  V30 1474 H     -13.9327    17.5655   -19.3416 0 CHG=0 CFG=0
M  V30 1475 C     -12.1910    18.3500   -20.3150 0 CHG=0 CFG=0
M  V30 1476 H     -11.5470    18.0803   -21.1542 0 CHG=0 CFG=0
M  V30 1477 C     -12.7500    19.7510   -20.5680 0 CHG=0 CFG=0
M  V30 1478 H     -13.4571    20.0463   -19.7936 0 CHG=0 CFG=0
M  V30 1479 H     -13.2587    19.8106   -21.5308 0 CHG=0 CFG=0
M  V30 1480 H     -11.9528    20.4934   -20.5907 0 CHG=0 CFG=0
M  V30 1481 C     -11.3560    18.3120   -19.0490 0 CHG=0 CFG=0
M  V30 1482 H     -10.9477    17.3142   -18.8805 0 CHG=0 CFG=0
M  V30 1483 H     -11.9508    18.5799   -18.1754 0 CHG=0 CFG=0
M  V30 1484 H     -10.5173    19.0047   -19.1092 0 CHG=0 CFG=0
M  V30 1485 C     -13.4860    16.7840   -22.6580 0 CHG=0 CFG=0
M  V30 1486 O     -13.2210    17.5900   -23.5500 0 CHG=0 CFG=0
M  V30 1487 N     -13.1180    15.5060   -22.7020 0 CHG=0 CFG=0
M  V30 1488 H     -13.4394    14.8991   -21.9792 0 CHG=0 CFG=0
M  V30 1489 C     -12.4100    14.9550   -23.8490 0 CHG=0 CFG=1
M  V30 1490 H     -11.5246    15.5748   -24.0044 0 CHG=0 CFG=0
M  V30 1491 C     -12.0040    13.5080   -23.5780 0 CHG=0 CFG=0
M  V30 1492 H     -11.6130    13.0560   -24.4919 0 CHG=0 CFG=0
M  V30 1493 H     -12.8711    12.9164   -23.2804 0 CHG=0 CFG=0
M  V30 1494 C     -10.9190    13.3930   -22.5200 0 CHG=0 CFG=0
M  V30 1495 O     -10.2720    14.3810   -22.1540 0 CHG=0 CFG=0
M  V30 1496 N     -10.7120    12.1760   -22.0230 0 CHG=0 CFG=0
M  V30 1497 H     -11.2262    11.3896   -22.3693 0 CHG=0 CFG=0
M  V30 1498 H     -10.0075    12.0490   -21.3245 0 CHG=0 CFG=0
M  V30 1499 C     -13.2480    15.0460   -25.1160 0 CHG=0 CFG=0
M  V30 1500 O     -12.7420    15.3870   -26.1740 0 CHG=0 CFG=0
M  V30 1501 N     -14.5390    14.7450   -24.9880 0 CHG=0 CFG=0
M  V30 1502 H     -14.8790    14.4292   -24.1027 0 CHG=0 CFG=0
M  V30 1503 C     -15.4830    14.7770   -26.1060 0 CHG=0 CFG=1
M  V30 1504 H     -15.0955    14.0934   -26.8629 0 CHG=0 CFG=0
M  V30 1505 C     -16.8390    14.2990   -25.5850 0 CHG=0 CFG=0
M  V30 1506 H     -17.1992    14.9822   -24.8171 0 CHG=0 CFG=0
M  V30 1507 H     -16.6902    13.3488   -25.0695 0 CHG=0 CFG=0
M  V30 1508 C     -17.9560    14.0740   -26.5860 0 CHG=0 CFG=0
M  V30 1509 C     -17.9530    12.9660   -27.4370 0 CHG=0 CFG=0
M  V30 1510 H     -17.1182    12.2776   -27.4123 0 CHG=0 CFG=0
M  V30 1511 C     -19.0160    12.7450   -28.3310 0 CHG=0 CFG=0
M  V30 1512 H     -19.0013    11.8950   -28.9953 0 CHG=0 CFG=0
M  V30 1513 C     -19.0600    14.9260   -26.6190 0 CHG=0 CFG=0
M  V30 1514 H     -19.0979    15.7781   -25.9561 0 CHG=0 CFG=0
M  V30 1515 C     -20.1180    14.7160   -27.4980 0 CHG=0 CFG=0
M  V30 1516 H     -20.9398    15.4163   -27.4969 0 CHG=0 CFG=0
M  V30 1517 C     -20.0910    13.6310   -28.3490 0 CHG=0 CFG=0
M  V30 1518 O     -21.1480    13.4300   -29.2140 0 CHG=0 CFG=0
M  V30 1519 H     -21.9715    13.5274   -28.7540 0 CHG=0 CFG=0
M  V30 1520 C     -15.5690    16.1850   -26.7080 0 CHG=0 CFG=0
M  V30 1521 O     -15.5130    16.3560   -27.9260 0 CHG=0 CFG=0
M  V30 1522 N     -15.6750    17.1930   -25.8440 0 CHG=0 CFG=0
M  V30 1523 H     -15.7395    16.9540   -24.8789 0 CHG=0 CFG=0
M  V30 1524 C     -15.7050    18.5980   -26.2770 0 CHG=0 CFG=1
M  V30 1525 H     -16.5745    18.7161   -26.9220 0 CHG=0 CFG=0
M  V30 1526 C     -15.7900    19.4950   -25.0470 0 CHG=0 CFG=0
M  V30 1527 H     -15.0187    20.2653   -25.0988 0 CHG=0 CFG=0
M  V30 1528 H     -15.4217    18.8969   -24.2128 0 CHG=0 CFG=0
M  V30 1529 C     -17.0470    20.2410   -24.5650 0 CHG=0 CFG=0
M  V30 1530 H     -16.8537    21.2963   -24.7661 0 CHG=0 CFG=0
M  V30 1531 C     -18.3560    20.0080   -25.3400 0 CHG=0 CFG=0
M  V30 1532 H     -18.6831    18.9715   -25.2495 0 CHG=0 CFG=0
M  V30 1533 H     -18.2364    20.2265   -26.4020 0 CHG=0 CFG=0
M  V30 1534 H     -19.1592    20.6432   -24.9679 0 CHG=0 CFG=0
M  V30 1535 C     -17.2350    20.1780   -23.0310 0 CHG=0 CFG=0
M  V30 1536 H     -16.5600    20.8713   -22.5293 0 CHG=0 CFG=0
M  V30 1537 H     -16.9905    19.1847   -22.6695 0 CHG=0 CFG=0
M  V30 1538 H     -18.2511    20.4165   -22.7243 0 CHG=0 CFG=0
M  V30 1539 C     -14.4550    18.9920   -27.0690 0 CHG=0 CFG=0
M  V30 1540 O     -14.5270    19.7740   -28.0190 0 CHG=0 CFG=0
M  V30 1541 N     -13.3120    18.4430   -26.6640 0 CHG=0 CFG=0
M  V30 1542 H     -13.3517    17.7347   -25.9586 0 CHG=0 CFG=0
M  V30 1543 C     -12.0210    18.8230   -27.2320 0 CHG=0 CFG=1
M  V30 1544 H     -12.0647    19.8954   -27.4363 0 CHG=0 CFG=0
M  V30 1545 C     -10.9000    18.5530   -26.2250 0 CHG=0 CFG=0
M  V30 1546 H      -9.9324    18.6920   -26.7107 0 CHG=0 CFG=0
M  V30 1547 H     -10.9406    17.5065   -25.9172 0 CHG=0 CFG=0
M  V30 1548 C     -10.9630    19.4650   -24.9990 0 CHG=0 CFG=0
M  V30 1549 H     -11.9454    19.3961   -24.5338 0 CHG=0 CFG=0
M  V30 1550 H     -10.8597    20.4991   -25.3321 0 CHG=0 CFG=0
M  V30 1551 C      -9.8930    19.1410   -23.9770 0 CHG=0 CFG=0
M  V30 1552 H      -8.9092    19.1035   -24.4485 0 CHG=0 CFG=0
M  V30 1553 H     -10.0970    18.1803   -23.4993 0 CHG=0 CFG=0
M  V30 1554 N      -9.8390    20.1660   -22.9390 0 CHG=0 CFG=0
M  V30 1555 H     -10.4843    20.9181   -23.0908 0 CHG=0 CFG=0
M  V30 1556 C      -9.0150    20.1480   -21.8930 0 CHG=0 CFG=0
M  V30 1557 N      -8.1520    19.1490   -21.7230 0 CHG=1 CFG=0
M  V30 1558 H      -8.1592    18.4052   -22.3965 0 CHG=0 CFG=0
M  V30 1559 H      -7.4989    19.0969   -20.9699 0 CHG=0 CFG=0
M  V30 1560 N      -9.0550    21.1400   -21.0100 0 CHG=0 CFG=0
M  V30 1561 H      -9.7293    21.8702   -21.1786 0 CHG=0 CFG=0
M  V30 1562 H      -8.4521    21.1982   -20.2170 0 CHG=0 CFG=0
M  V30 1563 C     -11.7310    18.1300   -28.5620 0 CHG=0 CFG=0
M  V30 1564 O     -10.7650    18.4770   -29.2450 0 CHG=0 CFG=0
M  V30 1565 N     -12.5590    17.1480   -28.9130 0 CHG=0 CFG=0
M  V30 1566 H     -13.3263    16.8771   -28.3287 0 CHG=0 CFG=0
M  V30 1567 C     -12.4270    16.4450   -30.1910 0 CHG=0 CFG=1
M  V30 1568 H     -11.3614    16.3040   -30.3803 0 CHG=0 CFG=0
M  V30 1569 C     -13.1140    15.0670   -30.1240 0 CHG=0 CFG=0
M  V30 1570 H     -13.2702    14.6413   -31.1143 0 CHG=0 CFG=0
M  V30 1571 H     -14.0946    15.2197   -29.6858 0 CHG=0 CFG=0
M  V30 1572 C     -12.3760    14.0500   -29.2270 0 CHG=0 CFG=0
M  V30 1573 H     -12.0536    14.5376   -28.3090 0 CHG=0 CFG=0
M  V30 1574 H     -11.4663    13.7109   -29.7210 0 CHG=0 CFG=0
M  V30 1575 C     -13.1990    12.8160   -28.8040 0 CHG=0 CFG=0
M  V30 1576 O     -14.4450    12.7650   -28.9760 0 CHG=0 CFG=0
M  V30 1577 O     -12.5730    11.8710   -28.2760 0 CHG=-1 CFG=0
M  V30 1578 C     -13.0170    17.3260   -31.2960 0 CHG=0 CFG=0
M  V30 1579 O     -14.2290    17.3560   -31.4940 0 CHG=0 CFG=0
M  V30 1580 N     -12.1620    18.0620   -32.0010 0 CHG=0 CFG=0
M  V30 1581 H     -11.2281    18.0832   -31.6431 0 CHG=0 CFG=0
M  V30 1582 C     -12.6550    19.0460   -32.9740 0 CHG=0 CFG=1
M  V30 1583 H     -13.3960    19.6430   -32.4374 0 CHG=0 CFG=0
M  V30 1584 C     -11.5330    19.9890   -33.4450 0 CHG=0 CFG=0
M  V30 1585 H     -11.9097    20.6094   -34.2597 0 CHG=0 CFG=0
M  V30 1586 H     -10.7128    19.4063   -33.8649 0 CHG=0 CFG=0
M  V30 1587 C     -10.9940    20.9330   -32.3510 0 CHG=0 CFG=0
M  V30 1588 H     -10.2198    21.5662   -32.7845 0 CHG=0 CFG=0
M  V30 1589 H     -10.4950    20.3599   -31.5680 0 CHG=0 CFG=0
M  V30 1590 S     -12.2190    22.0210   -31.5500 0 CHG=0 CFG=0
M  V30 1591 C     -12.4980    23.2300   -32.8510 0 CHG=0 CFG=0
M  V30 1592 H     -12.9272    22.7447   -33.7272 0 CHG=0 CFG=0
M  V30 1593 H     -11.5533    23.6843   -33.1494 0 CHG=0 CFG=0
M  V30 1594 H     -13.1739    24.0121   -32.5054 0 CHG=0 CFG=0
M  V30 1595 C     -13.4030    18.4130   -34.1580 0 CHG=0 CFG=0
M  V30 1596 O     -14.2250    19.0660   -34.8000 0 CHG=0 CFG=0
M  V30 1597 N     -13.1460    17.1340   -34.4190 0 CHG=0 CFG=0
M  V30 1598 H     -12.5253    16.6684   -33.7918 0 CHG=0 CFG=0
M  V30 1599 C     -13.8130    16.4320   -35.5240 0 CHG=0 CFG=1
M  V30 1600 H     -13.5212    16.9704   -36.4258 0 CHG=0 CFG=0
M  V30 1601 C     -13.3310    14.9820   -35.6250 0 CHG=0 CFG=0
M  V30 1602 H     -12.2607    14.9947   -35.8340 0 CHG=0 CFG=0
M  V30 1603 H     -13.7987    14.5005   -36.4856 0 CHG=0 CFG=0
M  V30 1604 C     -13.5830    14.1480   -34.3810 0 CHG=0 CFG=0
M  V30 1605 H     -14.6526    14.0403   -34.1950 0 CHG=0 CFG=0
M  V30 1606 H     -13.1719    14.6524   -33.5053 0 CHG=0 CFG=0
M  V30 1607 C     -12.9310    12.7870   -34.5140 0 CHG=0 CFG=0
M  V30 1608 H     -11.8773    12.8914   -34.7774 0 CHG=0 CFG=0
M  V30 1609 H     -13.3950    12.1731   -35.2881 0 CHG=0 CFG=0
M  V30 1610 N     -12.9340    12.0510   -33.2520 0 CHG=0 CFG=0
M  V30 1611 H     -12.1144    12.1347   -32.6776 0 CHG=0 CFG=0
M  V30 1612 C     -13.9550    11.3310   -32.7980 0 CHG=0 CFG=0
M  V30 1613 N     -15.0820    11.2470   -33.4970 0 CHG=1 CFG=0
M  V30 1614 H     -15.1684    11.7511   -34.3542 0 CHG=0 CFG=0
M  V30 1615 H     -15.8604    10.7056   -33.1770 0 CHG=0 CFG=0
M  V30 1616 N     -13.8490    10.7010   -31.6350 0 CHG=0 CFG=0
M  V30 1617 H     -13.0652    10.8493   -31.0198 0 CHG=0 CFG=0
M  V30 1618 H     -14.5626    10.1020   -31.2709 0 CHG=0 CFG=0
M  V30 1619 C     -15.3470    16.4860   -35.4440 0 CHG=0 CFG=0
M  V30 1620 O     -16.0170    16.4680   -36.4760 0 CHG=0 CFG=0
M  V30 1621 N     -15.8980    16.5580   -34.2290 0 CHG=0 CFG=0
M  V30 1622 H     -15.3362    16.6398   -33.4028 0 CHG=0 CFG=0
M  V30 1623 C     -17.3590    16.5390   -34.0610 0 CHG=0 CFG=1
M  V30 1624 H     -17.7208    15.6335   -34.5501 0 CHG=0 CFG=0
M  V30 1625 C     -17.7560    16.5150   -32.5910 0 CHG=0 CFG=0
M  V30 1626 H     -18.8413    16.5748   -32.4983 0 CHG=0 CFG=0
M  V30 1627 H     -17.3508    17.3869   -32.0762 0 CHG=0 CFG=0
M  V30 1628 C     -17.3130    15.2810   -31.8680 0 CHG=0 CFG=0
M  V30 1629 N     -17.7740    14.0220   -32.1880 0 CHG=0 CFG=0
M  V30 1630 C     -17.2100    13.1340   -31.3900 0 CHG=0 CFG=0
M  V30 1631 H     -17.4048    12.0726   -31.3796 0 CHG=0 CFG=0
M  V30 1632 N     -16.4030    13.7720   -30.5610 0 CHG=0 CFG=0
M  V30 1633 H     -15.9197    13.3940   -29.8033 0 CHG=0 CFG=0
M  V30 1634 C     -16.4530    15.1170   -30.8370 0 CHG=0 CFG=0
M  V30 1635 H     -15.9471    15.9200   -30.3217 0 CHG=0 CFG=0
M  V30 1636 C     -18.0200    17.7270   -34.7390 0 CHG=0 CFG=0
M  V30 1637 O     -19.1870    17.6480   -35.1200 0 CHG=0 CFG=0
M  V30 1638 N     -17.2770    18.8270   -34.8750 0 CHG=0 CFG=0
M  V30 1639 H     -16.3423    18.8263   -34.5187 0 CHG=0 CFG=0
M  V30 1640 C     -17.7750    20.0120   -35.5710 0 CHG=0 CFG=1
M  V30 1641 H     -17.0947    20.8256   -35.3199 0 CHG=0 CFG=0
M  V30 1642 C     -17.7900    19.7620   -37.0820 0 CHG=0 CFG=0
M  V30 1643 H     -18.3072    20.5892   -37.5719 0 CHG=0 CFG=0
M  V30 1644 H     -18.3908    18.8757   -37.2943 0 CHG=0 CFG=0
M  V30 1645 C     -16.4030    19.6230   -37.7110 0 CHG=0 CFG=0
M  V30 1646 H     -15.8187    18.8670   -37.1885 0 CHG=0 CFG=0
M  V30 1647 H     -15.8650    20.5654   -37.6023 0 CHG=0 CFG=0
M  V30 1648 C     -16.5620    19.2690   -39.1760 0 CHG=0 CFG=0
M  V30 1649 H     -17.2862    19.9385   -39.6434 0 CHG=0 CFG=0
M  V30 1650 H     -16.9508    18.2561   -39.2996 0 CHG=0 CFG=0
M  V30 1651 N     -15.3540    19.3970   -39.9920 0 CHG=0 CFG=0
M  V30 1652 H     -15.3815    20.2049   -40.5851 0 CHG=0 CFG=0
M  V30 1653 C     -14.3260    18.5500   -39.9920 0 CHG=0 CFG=0
M  V30 1654 N     -14.3010    17.5020   -39.1700 0 CHG=1 CFG=0
M  V30 1655 H     -15.0766    17.3685   -38.5389 0 CHG=0 CFG=0
M  V30 1656 H     -13.5568    16.8383   -39.1449 0 CHG=0 CFG=0
M  V30 1657 N     -13.3010    18.7720   -40.8090 0 CHG=0 CFG=0
M  V30 1658 H     -13.3105    19.5638   -41.4225 0 CHG=0 CFG=0
M  V30 1659 H     -12.5038    18.1689   -40.8404 0 CHG=0 CFG=0
M  V30 1660 C     -19.1700    20.3720   -35.0510 0 CHG=0 CFG=0
M  V30 1661 O     -20.1290    20.4740   -35.8160 0 CHG=0 CFG=0
M  V30 1662 N     -19.2690    20.5490   -33.7340 0 CHG=0 CFG=0
M  V30 1663 H     -18.4445    20.4831   -33.1800 0 CHG=0 CFG=0
M  V30 1664 C     -20.5650    20.7360   -33.0780 0 CHG=0 CFG=1
M  V30 1665 H     -21.1509    19.8466   -33.3176 0 CHG=0 CFG=0
M  V30 1666 C     -20.4040    20.8710   -31.5650 0 CHG=0 CFG=0
M  V30 1667 H     -21.3678    21.1119   -31.1105 0 CHG=0 CFG=0
M  V30 1668 H     -19.7532    21.7158   -31.3329 0 CHG=0 CFG=0
M  V30 1669 C     -19.8990    19.6300   -30.8740 0 CHG=0 CFG=0
M  V30 1670 C     -20.6810    18.4820   -30.7960 0 CHG=0 CFG=0
M  V30 1671 H     -21.6583    18.4641   -31.2537 0 CHG=0 CFG=0
M  V30 1672 C     -18.6540    19.6380   -30.2590 0 CHG=0 CFG=0
M  V30 1673 H     -18.0340    20.5210   -30.2930 0 CHG=0 CFG=0
M  V30 1674 C     -20.2130    17.3410   -30.1270 0 CHG=0 CFG=0
M  V30 1675 H     -20.8177    16.4457   -30.0794 0 CHG=0 CFG=0
M  V30 1676 C     -18.1770    18.5080   -29.5880 0 CHG=0 CFG=0
M  V30 1677 H     -17.1967    18.5133   -29.1291 0 CHG=0 CFG=0
M  V30 1678 C     -18.9620    17.3610   -29.5230 0 CHG=0 CFG=0
M  V30 1679 H     -18.5788    16.4865   -29.0155 0 CHG=0 CFG=0
M  V30 1680 C     -21.3210    21.9620   -33.5800 0 CHG=0 CFG=0
M  V30 1681 O     -20.7260    23.0150   -33.8260 0 CHG=0 CFG=0
M  V30 1682 N     -22.6330    21.8110   -33.7260 0 CHG=0 CFG=0
M  V30 1683 H     -23.0035    20.8913   -33.5967 0 CHG=0 CFG=0
M  V30 1684 C     -23.5140    22.9550   -33.9020 0 CHG=0 CFG=1
M  V30 1685 H     -22.9958    23.7067   -34.5014 0 CHG=0 CFG=0
M  V30 1686 C     -24.8330    22.5480   -34.5470 0 CHG=0 CFG=0
M  V30 1687 H     -25.4291    23.4480   -34.7061 0 CHG=0 CFG=0
M  V30 1688 H     -25.3816    21.9241   -33.8388 0 CHG=0 CFG=0
M  V30 1689 C     -24.7680    21.7800   -35.8450 0 CHG=0 CFG=0
M  V30 1690 H     -24.2291    20.8400   -35.7151 0 CHG=0 CFG=0
M  V30 1691 H     -24.2298    22.3563   -36.5974 0 CHG=0 CFG=0
M  V30 1692 C     -26.1660    21.5060   -36.3700 0 CHG=0 CFG=0
M  V30 1693 O     -26.9033    22.4235   -36.7406 0 CHG=0 CFG=0
M  V30 1694 N     -26.5248    20.2301   -36.4380 0 CHG=0 CFG=0
M  V30 1695 H     -25.8977    19.4921   -36.1956 0 CHG=0 CFG=0
M  V30 1696 H     -27.4610    20.0208   -36.7145 0 CHG=0 CFG=0
M  V30 1697 C     -23.8310    23.4960   -32.5200 0 CHG=0 CFG=0
M  V30 1698 O     -23.7770    22.7560   -31.5330 0 CHG=0 CFG=0
M  V30 1699 N     -24.2040    24.7670   -32.4320 0 CHG=0 CFG=0
M  V30 1700 H     -24.2866    25.3666   -33.2281 0 CHG=0 CFG=0
M  V30 1701 C     -24.5420    25.3240   -31.1160 0 CHG=0 CFG=1
M  V30 1702 H     -23.7200    25.0595   -30.4472 0 CHG=0 CFG=0
M  V30 1703 C     -24.6740    26.8480   -31.1550 0 CHG=0 CFG=2
M  V30 1704 H     -24.9805    27.1918   -30.1578 0 CHG=0 CFG=0
M  V30 1705 O     -25.6500    27.2120   -32.1320 0 CHG=0 CFG=0
M  V30 1706 H     -25.8821    28.1377   -32.0724 0 CHG=0 CFG=0
M  V30 1707 C     -23.3300    27.4760   -31.5260 0 CHG=0 CFG=0
M  V30 1708 H     -23.0139    27.1967   -32.5312 0 CHG=0 CFG=0
M  V30 1709 H     -22.5476    27.1609   -30.8349 0 CHG=0 CFG=0
M  V30 1710 H     -23.3691    28.5650   -31.4840 0 CHG=0 CFG=0
M  V30 1711 C     -25.8080    24.6830   -30.5280 0 CHG=0 CFG=0
M  V30 1712 O     -25.9430    24.5840   -29.3050 0 CHG=0 CFG=0
M  V30 1713 N     -26.7170    24.2240   -31.3890 0 CHG=0 CFG=0
M  V30 1714 H     -26.6289    24.5035   -32.3435 0 CHG=0 CFG=0
M  V30 1715 C     -27.8920    23.4740   -30.9220 0 CHG=0 CFG=1
M  V30 1716 H     -28.4615    24.1406   -30.2708 0 CHG=0 CFG=0
M  V30 1717 C     -28.7320    23.0360   -32.0960 0 CHG=0 CFG=0
M  V30 1718 H     -29.2287    23.9188   -32.5013 0 CHG=0 CFG=0
M  V30 1719 H     -29.5460    22.4081   -31.7238 0 CHG=0 CFG=0
M  V30 1720 C     -28.0140    22.3110   -33.2430 0 CHG=0 CFG=0
M  V30 1721 H     -27.4261    21.4682   -32.8855 0 CHG=0 CFG=0
M  V30 1722 H     -27.3549    22.9961   -33.7680 0 CHG=0 CFG=0
M  V30 1723 C     -29.0280    21.7530   -34.2510 0 CHG=0 CFG=0
M  V30 1724 O     -29.2280    20.5510   -34.3610 0 CHG=0 CFG=0
M  V30 1725 N     -29.6510    22.7000   -34.9720 0 CHG=0 CFG=0
M  V30 1726 H     -29.4770    23.6752   -34.8427 0 CHG=0 CFG=0
M  V30 1727 H     -30.3259    22.4171   -35.6486 0 CHG=0 CFG=0
M  V30 1728 C     -27.4730    22.2490   -30.1050 0 CHG=0 CFG=0
M  V30 1729 O     -28.1040    21.9210   -29.0930 0 CHG=0 CFG=0
M  V30 1730 N     -26.4030    21.5820   -30.5450 0 CHG=0 CFG=0
M  V30 1731 H     -25.8886    21.9447   -31.3189 0 CHG=0 CFG=0
M  V30 1732 C     -25.8840    20.4080   -29.8420 0 CHG=0 CFG=1
M  V30 1733 H     -26.7268    19.7352   -29.6678 0 CHG=0 CFG=0
M  V30 1734 C     -24.8090    19.7110   -30.6700 0 CHG=0 CFG=0
M  V30 1735 H     -24.2713    19.0043   -30.0328 0 CHG=0 CFG=0
M  V30 1736 H     -24.0598    20.4360   -30.9880 0 CHG=0 CFG=0
M  V30 1737 C     -25.3260    18.9300   -31.8700 0 CHG=0 CFG=0
M  V30 1738 H     -25.9255    19.5765   -32.5108 0 CHG=0 CFG=0
M  V30 1739 H     -25.9736    18.1126   -31.5513 0 CHG=0 CFG=0
M  V30 1740 C     -24.1910    18.3880   -32.7020 0 CHG=0 CFG=0
M  V30 1741 O     -23.6250    19.1000   -33.5310 0 CHG=0 CFG=0
M  V30 1742 N     -23.8300    17.1300   -32.4710 0 CHG=0 CFG=0
M  V30 1743 H     -23.0776    16.7483   -33.0031 0 CHG=0 CFG=0
M  V30 1744 H     -24.2846    16.5632   -31.7826 0 CHG=0 CFG=0
M  V30 1745 C     -25.3090    20.7920   -28.4830 0 CHG=0 CFG=0
M  V30 1746 O     -25.5150    20.0960   -27.5020 0 CHG=0 CFG=0
M  V30 1747 N     -24.5840    21.9040   -28.4430 0 CHG=0 CFG=0
M  V30 1748 H     -24.4336    22.3934   -29.3020 0 CHG=0 CFG=0
M  V30 1749 C     -24.0080    22.3950   -27.2000 0 CHG=0 CFG=1
M  V30 1750 H     -23.4474    21.5635   -26.7696 0 CHG=0 CFG=0
M  V30 1751 C     -23.0650    23.5710   -27.4720 0 CHG=0 CFG=0
M  V30 1752 H     -22.6213    23.9119   -26.5397 0 CHG=0 CFG=0
M  V30 1753 H     -23.6611    24.4125   -27.8288 0 CHG=0 CFG=0
M  V30 1754 C     -21.9580    23.2930   -28.4990 0 CHG=0 CFG=0
M  V30 1755 H     -22.4188    22.9713   -29.4328 0 CHG=0 CFG=0
M  V30 1756 C     -21.1390    24.5520   -28.8270 0 CHG=0 CFG=0
M  V30 1757 H     -20.5948    24.9039   -27.9507 0 CHG=0 CFG=0
M  V30 1758 H     -21.7751    25.3653   -29.1753 0 CHG=0 CFG=0
M  V30 1759 H     -20.4074    24.3428   -29.6079 0 CHG=0 CFG=0
M  V30 1760 C     -21.0640    22.1560   -28.0110 0 CHG=0 CFG=0
M  V30 1761 H     -21.6070    21.2159   -27.9191 0 CHG=0 CFG=0
M  V30 1762 H     -20.6180    22.3871   -27.0431 0 CHG=0 CFG=0
M  V30 1763 H     -20.2463    21.9781   -28.7102 0 CHG=0 CFG=0
M  V30 1764 C     -25.0940    22.7580   -26.1920 0 CHG=0 CFG=0
M  V30 1765 O     -24.9840    22.4160   -25.0100 0 CHG=0 CFG=0
M  V30 1766 N     -26.1520    23.4210   -26.6570 0 CHG=0 CFG=0
M  V30 1767 H     -26.1900    23.6822   -27.6214 0 CHG=0 CFG=0
M  V30 1768 C     -27.2520    23.7860   -25.7680 0 CHG=0 CFG=1
M  V30 1769 H     -26.7736    24.3118   -24.9421 0 CHG=0 CFG=0
M  V30 1770 C     -28.2560    24.6990   -26.4700 0 CHG=0 CFG=0
M  V30 1771 H     -28.8371    24.1157   -27.1879 0 CHG=0 CFG=0
M  V30 1772 H     -27.7269    25.4161   -27.0851 0 CHG=0 CFG=0
M  V30 1773 C     -29.2200    25.4430   -25.5350 0 CHG=0 CFG=0
M  V30 1774 H     -29.9350    24.7255   -25.1341 0 CHG=0 CFG=0
M  V30 1775 C     -28.5060    26.1030   -24.3380 0 CHG=0 CFG=0
M  V30 1776 H     -27.6721    26.7246   -24.6613 0 CHG=0 CFG=0
M  V30 1777 H     -28.1338    25.3627   -23.6316 0 CHG=0 CFG=0
M  V30 1778 H     -29.1954    26.7443   -23.7878 0 CHG=0 CFG=0
M  V30 1779 C     -30.0000    26.4600   -26.3440 0 CHG=0 CFG=0
M  V30 1780 H     -30.4720    26.0082   -27.2169 0 CHG=0 CFG=0
M  V30 1781 H     -29.3571    27.2646   -26.7008 0 CHG=0 CFG=0
M  V30 1782 H     -30.7959    26.9092   -25.7475 0 CHG=0 CFG=0
M  V30 1783 C     -27.9490    22.5440   -25.2130 0 CHG=0 CFG=0
M  V30 1784 O     -28.3050    22.5090   -24.0330 0 CHG=0 CFG=0
M  V30 1785 N     -28.1130    21.5220   -26.0530 0 CHG=0 CFG=0
M  V30 1786 H     -27.8999    21.6248   -27.0262 0 CHG=0 CFG=0
M  V30 1787 C     -28.6780    20.2460   -25.6040 0 CHG=0 CFG=1
M  V30 1788 H     -29.6363    20.4632   -25.1476 0 CHG=0 CFG=0
M  V30 1789 C     -28.8730    19.2870   -26.7810 0 CHG=0 CFG=0
M  V30 1790 H     -27.8907    19.0439   -27.1866 0 CHG=0 CFG=0
M  V30 1791 H     -29.3967    19.7897   -27.5954 0 CHG=0 CFG=0
M  V30 1792 C     -29.5680    17.9780   -26.4170 0 CHG=0 CFG=0
M  V30 1793 H     -29.2262    17.5686   -25.4652 0 CHG=0 CFG=0
M  V30 1794 H     -29.3218    17.2268   -27.1674 0 CHG=0 CFG=0
M  V30 1795 C     -31.0870    18.0820   -26.3980 0 CHG=0 CFG=0
M  V30 1796 O     -31.6350    19.1370   -26.7800 0 CHG=0 CFG=0
M  V30 1797 O     -31.7400    17.0890   -26.0070 0 CHG=-1 CFG=0
M  V30 1798 C     -27.8200    19.5930   -24.5130 0 CHG=0 CFG=0
M  V30 1799 O     -28.3610    19.0220   -23.5600 0 CHG=0 CFG=0
M  V30 1800 N     -26.4910    19.6710   -24.6420 0 CHG=0 CFG=0
M  V30 1801 H     -26.1330    20.0398   -25.5007 0 CHG=0 CFG=0
M  V30 1802 C     -25.6000    19.1610   -23.5770 0 CHG=0 CFG=1
M  V30 1803 H     -25.8566    18.1076   -23.4372 0 CHG=0 CFG=0
M  V30 1804 C     -24.1200    19.3080   -23.9380 0 CHG=0 CFG=0
M  V30 1805 H     -23.5068    18.9300   -23.1190 0 CHG=0 CFG=0
M  V30 1806 H     -23.8723    20.3653   -24.0361 0 CHG=0 CFG=0
M  V30 1807 C     -23.7160    18.6030   -25.2230 0 CHG=0 CFG=0
M  V30 1808 H     -24.3076    18.9407   -26.0601 0 CHG=0 CFG=0
M  V30 1809 H     -23.8823    17.5276   -25.1546 0 CHG=0 CFG=0
M  V30 1810 S     -21.9800    18.9200   -25.5740 0 CHG=0 CFG=0
M  V30 1811 C     -21.8940    18.3250   -27.2550 0 CHG=0 CFG=0
M  V30 1812 H     -22.5142    18.9412   -27.9062 0 CHG=0 CFG=0
M  V30 1813 H     -22.2705    17.3043   -27.3110 0 CHG=0 CFG=0
M  V30 1814 H     -20.8626    18.3475   -27.6028 0 CHG=0 CFG=0
M  V30 1815 C     -25.8530    19.8940   -22.2670 0 CHG=0 CFG=0
M  V30 1816 O     -25.9280    19.2780   -21.2030 0 CHG=0 CFG=0
M  V30 1817 N     -25.9740    21.2170   -22.3530 0 CHG=0 CFG=0
M  V30 1818 H     -25.8754    21.6242   -23.2636 0 CHG=0 CFG=0
M  V30 1819 C     -26.3400    22.0270   -21.1910 0 CHG=0 CFG=1
M  V30 1820 H     -25.5609    21.8714   -20.4432 0 CHG=0 CFG=0
M  V30 1821 C     -26.4190    23.4990   -21.5710 0 CHG=0 CFG=0
M  V30 1822 H     -26.8160    24.0762   -20.7341 0 CHG=0 CFG=0
M  V30 1823 H     -27.0994    23.6637   -22.4024 0 CHG=0 CFG=0
M  V30 1824 S     -24.8140    24.1790   -21.9820 0 CHG=0 CFG=0
M  V30 1825 H     -24.3778    23.5947   -23.1041 0 CHG=0 CFG=0
M  V30 1826 C     -27.6700    21.5820   -20.5880 0 CHG=0 CFG=0
M  V30 1827 O     -27.7980    21.4820   -19.3680 0 CHG=0 CFG=0
M  V30 1828 N     -28.6560    21.3230   -21.4420 0 CHG=0 CFG=0
M  V30 1829 H     -28.4834    21.3519   -22.4289 0 CHG=0 CFG=0
M  V30 1830 C     -29.9750    20.9140   -20.9700 0 CHG=0 CFG=1
M  V30 1831 H     -30.2653    21.6411   -20.2092 0 CHG=0 CFG=0
M  V30 1832 C     -31.0070    20.9450   -22.1000 0 CHG=0 CFG=0
M  V30 1833 H     -30.6979    20.2715   -22.9023 0 CHG=0 CFG=0
M  V30 1834 H     -31.0127    21.9433   -22.5359 0 CHG=0 CFG=0
M  V30 1835 C     -32.4140    20.5690   -21.6390 0 CHG=0 CFG=0
M  V30 1836 H     -32.6093    21.1175   -20.7162 0 CHG=0 CFG=0
M  V30 1837 H     -32.4691    19.5183   -21.3556 0 CHG=0 CFG=0
M  V30 1838 C     -33.4720    20.9770   -22.6400 0 CHG=0 CFG=0
M  V30 1839 H     -33.1883    21.8825   -23.1783 0 CHG=0 CFG=0
M  V30 1840 H     -34.3741    21.2322   -22.0878 0 CHG=0 CFG=0
M  V30 1841 C     -33.7880    19.8510   -23.5940 0 CHG=0 CFG=0
M  V30 1842 H     -32.8984    19.6008   -24.1817 0 CHG=0 CFG=0
M  V30 1843 H     -34.5616    20.1367   -24.3089 0 CHG=0 CFG=0
M  V30 1844 N     -34.2250    18.6070   -22.8820 0 CHG=1 CFG=0
M  V30 1845 H     -35.2096    18.6521   -22.5569 0 CHG=0 CFG=0
M  V30 1846 H     -33.6814    18.4332   -22.0052 0 CHG=0 CFG=0
M  V30 1847 H     -34.0894    17.7943   -23.5156 0 CHG=0 CFG=0
M  V30 1848 C     -29.9220    19.5410   -20.2970 0 CHG=0 CFG=0
M  V30 1849 O     -30.5420    19.3390   -19.2500 0 CHG=0 CFG=0
M  V30 1850 N     -29.1640    18.6130   -20.8830 0 CHG=0 CFG=0
M  V30 1851 H     -28.7559    18.7632   -21.7830 0 CHG=0 CFG=0
M  V30 1852 C     -28.9710    17.2910   -20.2800 0 CHG=0 CFG=1
M  V30 1853 H     -29.9426    16.7956   -20.2550 0 CHG=0 CFG=0
M  V30 1854 C     -27.9260    16.4780   -21.0480 0 CHG=0 CFG=0
M  V30 1855 H     -27.6845    15.5973   -20.4677 0 CHG=0 CFG=0
M  V30 1856 H     -27.0050    17.0440   -21.1825 0 CHG=0 CFG=0
M  V30 1857 C     -28.4090    15.9830   -22.4020 0 CHG=0 CFG=0
M  V30 1858 O     -29.6320    15.9590   -22.6910 0 CHG=0 CFG=0
M  V30 1859 O     -27.5170    15.5910   -23.1880 0 CHG=-1 CFG=0
M  V30 1860 C     -28.4740    17.4500   -18.8520 0 CHG=0 CFG=0
M  V30 1861 O     -29.0200    16.8660   -17.9180 0 CHG=0 CFG=0
M  V30 1862 N     -27.4210    18.2400   -18.6820 0 CHG=0 CFG=0
M  V30 1863 H     -27.0315    18.6490   -19.5117 0 CHG=0 CFG=0
M  V30 1864 C     -26.8300    18.3900   -17.3600 0 CHG=0 CFG=1
M  V30 1865 H     -26.6812    17.3812   -16.9689 0 CHG=0 CFG=0
M  V30 1866 C     -25.4800    19.1100   -17.4450 0 CHG=0 CFG=0
M  V30 1867 H     -25.6268    20.0456   -17.9880 0 CHG=0 CFG=0
M  V30 1868 C     -24.9550    19.4460   -16.0490 0 CHG=0 CFG=0
M  V30 1869 H     -24.7918    18.5490   -15.4546 0 CHG=0 CFG=0
M  V30 1870 H     -25.6245    20.0962   -15.4864 0 CHG=0 CFG=0
M  V30 1871 H     -24.0159    19.9761   -16.1223 0 CHG=0 CFG=0
M  V30 1872 C     -24.4870    18.2610   -18.2310 0 CHG=0 CFG=0
M  V30 1873 H     -24.8479    18.0448   -19.2378 0 CHG=0 CFG=0
M  V30 1874 H     -24.3020    17.3065   -17.7375 0 CHG=0 CFG=0
M  V30 1875 H     -23.5318    18.7739   -18.3392 0 CHG=0 CFG=0
M  V30 1876 C     -27.7950    19.1030   -16.4110 0 CHG=0 CFG=0
M  V30 1877 O     -27.9350    18.7160   -15.2400 0 CHG=0 CFG=0
M  V30 1878 N     -28.4810    20.1220   -16.9210 0 CHG=0 CFG=0
M  V30 1879 H     -28.3621    20.3326   -17.8926 0 CHG=0 CFG=0
M  V30 1880 C     -29.3880    20.9090   -16.0940 0 CHG=0 CFG=1
M  V30 1881 H     -28.8102    21.2382   -15.2288 0 CHG=0 CFG=0
M  V30 1882 C     -29.8900    22.1250   -16.8630 0 CHG=0 CFG=0
M  V30 1883 H     -30.6234    21.8314   -17.6163 0 CHG=0 CFG=0
M  V30 1884 H     -29.0668    22.5781   -17.4098 0 CHG=0 CFG=0
M  V30 1885 S     -30.6070    23.3850   -15.7990 0 CHG=0 CFG=0
M  V30 1886 H     -31.6836    22.8864   -15.1805 0 CHG=0 CFG=0
M  V30 1887 C     -30.5630    20.0580   -15.6020 0 CHG=0 CFG=0
M  V30 1888 O     -31.0000    20.1940   -14.4530 0 CHG=0 CFG=0
M  V30 1889 N     -31.0620    19.1670   -16.4600 0 CHG=0 CFG=0
M  V30 1890 H     -30.7180    19.0904   -17.3964 0 CHG=0 CFG=0
M  V30 1891 C     -32.1080    18.2350   -16.0330 0 CHG=0 CFG=1
M  V30 1892 H     -32.9376    18.8416   -15.6621 0 CHG=0 CFG=0
M  V30 1893 C     -32.5800    17.3810   -17.2010 0 CHG=0 CFG=0
M  V30 1894 H     -33.1791    16.5508   -16.8298 0 CHG=0 CFG=0
M  V30 1895 H     -31.7061    16.9473   -17.6902 0 CHG=0 CFG=0
M  V30 1896 C     -33.4380    18.1360   -18.1970 0 CHG=0 CFG=0
M  V30 1897 H     -32.9324    19.0462   -18.5174 0 CHG=0 CFG=0
M  V30 1898 H     -34.3790    18.4400   -17.7363 0 CHG=0 CFG=0
M  V30 1899 C     -33.7350    17.3160   -19.4300 0 CHG=0 CFG=0
M  V30 1900 O     -33.2150    16.1820   -19.5280 0 CHG=0 CFG=0
M  V30 1901 O     -34.4850    17.8010   -20.3010 0 CHG=-1 CFG=0
M  V30 1902 C     -31.6510    17.3350   -14.8790 0 CHG=0 CFG=0
M  V30 1903 O     -32.3920    17.1330   -13.9030 0 CHG=0 CFG=0
M  V30 1904 N     -30.4370    16.7900   -14.9940 0 CHG=0 CFG=0
M  V30 1905 H     -29.9317    16.9684   -15.8421 0 CHG=0 CFG=0
M  V30 1906 C     -29.9040    15.9340   -13.9310 0 CHG=0 CFG=1
M  V30 1907 H     -30.6222    15.1240   -13.7885 0 CHG=0 CFG=0
M  V30 1908 C     -28.5600    15.3820   -14.3260 0 CHG=0 CFG=0
M  V30 1909 H     -27.8167    16.1734   -14.4292 0 CHG=0 CFG=0
M  V30 1910 H     -28.6242    14.8790   -15.2878 0 CHG=0 CFG=0
M  V30 1911 H     -28.1941    14.6621   -13.5944 0 CHG=0 CFG=0
M  V30 1912 C     -29.7740    16.7110   -12.6330 0 CHG=0 CFG=0
M  V30 1913 O     -30.0730    16.1980   -11.5460 0 CHG=0 CFG=0
M  V30 1914 N     -29.3100    17.9520   -12.7530 0 CHG=0 CFG=0
M  V30 1915 H     -29.1187    18.3070   -13.6705 0 CHG=0 CFG=0
M  V30 1916 C     -29.0690    18.7840   -11.5870 0 CHG=0 CFG=1
M  V30 1917 H     -28.5573    18.1633   -10.8498 0 CHG=0 CFG=0
M  V30 1918 C     -28.1890    19.9750   -11.9540 0 CHG=0 CFG=0
M  V30 1919 H     -28.1715    20.6536   -11.1064 0 CHG=0 CFG=0
M  V30 1920 H     -28.6359    20.5316   -12.7793 0 CHG=0 CFG=0
M  V30 1921 C     -26.7460    19.6070   -12.2860 0 CHG=0 CFG=0
M  V30 1922 H     -26.1848    20.5320   -12.4194 0 CHG=0 CFG=0
M  V30 1923 H     -26.6975    19.0843   -13.2388 0 CHG=0 CFG=0
M  V30 1924 S     -25.8860    18.5920   -11.0540 0 CHG=0 CFG=0
M  V30 1925 C     -25.9110    19.6840    -9.6320 0 CHG=0 CFG=0
M  V30 1926 H     -26.9387    19.9305    -9.3635 0 CHG=0 CFG=0
M  V30 1927 H     -25.4014    20.6196    -9.8619 0 CHG=0 CFG=0
M  V30 1928 H     -25.4399    19.2227    -8.7670 0 CHG=0 CFG=0
M  V30 1929 C     -30.3720    19.2490   -10.9440 0 CHG=0 CFG=0
M  V30 1930 O     -30.4580    19.3380    -9.7210 0 CHG=0 CFG=0
M  V30 1931 N     -31.3860    19.5370   -11.7620 0 CHG=0 CFG=0
M  V30 1932 H     -31.2567    19.4837   -12.7507 0 CHG=0 CFG=0
M  V30 1933 C     -32.7080    19.8630   -11.2290 0 CHG=0 CFG=1
M  V30 1934 H     -32.5766    20.7001   -10.5449 0 CHG=0 CFG=0
M  V30 1935 C     -33.6860    20.2440   -12.3480 0 CHG=0 CFG=0
M  V30 1936 H     -33.7287    19.4011   -13.0410 0 CHG=0 CFG=0
M  V30 1937 H     -33.2963    21.0796   -12.9299 0 CHG=0 CFG=0
M  V30 1938 C     -35.0800    20.5800   -11.8370 0 CHG=0 CFG=0
M  V30 1939 H     -35.0812    21.5815   -11.4068 0 CHG=0 CFG=0
M  V30 1940 H     -35.3959    19.9042   -11.0448 0 CHG=0 CFG=0
M  V30 1941 C     -36.1570    20.4880   -12.8980 0 CHG=0 CFG=0
M  V30 1942 O     -35.9620    19.7920   -13.9150 0 CHG=0 CFG=0
M  V30 1943 O     -37.2220    21.1050   -12.6960 0 CHG=-1 CFG=0
M  V30 1944 C     -33.2440    18.6830   -10.4190 0 CHG=0 CFG=0
M  V30 1945 O     -33.8100    18.8660    -9.3360 0 CHG=0 CFG=0
M  V30 1946 N     -33.0430    17.4740   -10.9430 0 CHG=0 CFG=0
M  V30 1947 H     -32.6607    17.4295   -11.8698 0 CHG=0 CFG=0
M  V30 1948 C     -33.4260    16.2670   -10.2210 0 CHG=0 CFG=1
M  V30 1949 H     -34.4873    16.3771    -9.9962 0 CHG=0 CFG=0
M  V30 1950 C     -33.2240    15.0190   -11.0870 0 CHG=0 CFG=0
M  V30 1951 H     -32.2193    15.0071   -11.5090 0 CHG=0 CFG=0
M  V30 1952 H     -33.9023    15.0608   -11.9387 0 CHG=0 CFG=0
M  V30 1953 C     -33.4510    13.7380   -10.3200 0 CHG=0 CFG=0
M  V30 1954 C     -34.7430    13.2610   -10.0870 0 CHG=0 CFG=0
M  V30 1955 H     -35.5848    13.8199   -10.4710 0 CHG=0 CFG=0
M  V30 1956 C     -34.9580    12.0900    -9.3740 0 CHG=0 CFG=0
M  V30 1957 H     -35.9705    11.7488    -9.2273 0 CHG=0 CFG=0
M  V30 1958 C     -32.3770    13.0100    -9.8210 0 CHG=0 CFG=0
M  V30 1959 H     -31.3678    13.3617    -9.9894 0 CHG=0 CFG=0
M  V30 1960 C     -32.5850    11.8360    -9.1000 0 CHG=0 CFG=0
M  V30 1961 H     -31.7422    11.2856    -8.7114 0 CHG=0 CFG=0
M  V30 1962 C     -33.8740    11.3850    -8.8880 0 CHG=0 CFG=0
M  V30 1963 O     -34.0780    10.2270    -8.1780 0 CHG=0 CFG=0
M  V30 1964 H     -34.6087     9.6444    -8.7167 0 CHG=0 CFG=0
M  V30 1965 C     -32.6550    16.1480    -8.9050 0 CHG=0 CFG=0
M  V30 1966 O     -33.2500    15.9680    -7.8420 0 CHG=0 CFG=0
M  V30 1967 N     -31.3310    16.2570    -8.9650 0 CHG=0 CFG=0
M  V30 1968 H     -30.9019    16.4404    -9.8506 0 CHG=0 CFG=0
M  V30 1969 C     -30.5460    16.1960    -7.7270 0 CHG=0 CFG=1
M  V30 1970 H     -30.7658    15.2310    -7.2706 0 CHG=0 CFG=0
M  V30 1971 C     -29.0530    16.3140    -8.0120 0 CHG=0 CFG=0
M  V30 1972 H     -28.5355    16.4859    -7.0693 0 CHG=0 CFG=0
M  V30 1973 H     -28.8808    17.2155    -8.6034 0 CHG=0 CFG=0
M  V30 1974 C     -28.3720    15.1180    -8.6840 0 CHG=0 CFG=0
M  V30 1975 H     -28.8338    14.9708    -9.6616 0 CHG=0 CFG=0
M  V30 1976 C     -26.9040    15.4170    -8.9100 0 CHG=0 CFG=0
M  V30 1977 H     -26.3966    15.6181    -7.9655 0 CHG=0 CFG=0
M  V30 1978 H     -26.7839    16.2955    -9.5450 0 CHG=0 CFG=0
M  V30 1979 H     -26.3878    14.5883    -9.3923 0 CHG=0 CFG=0
M  V30 1980 C     -28.5390    13.8150    -7.8870 0 CHG=0 CFG=0
M  V30 1981 H     -29.5775    13.4854    -7.8654 0 CHG=0 CFG=0
M  V30 1982 H     -28.2040    13.9340    -6.8577 0 CHG=0 CFG=0
M  V30 1983 H     -27.9560    13.0055    -8.3259 0 CHG=0 CFG=0
M  V30 1984 C     -30.9980    17.2620    -6.7160 0 CHG=0 CFG=0
M  V30 1985 O     -31.1370    16.9700    -5.5210 0 CHG=0 CFG=0
M  V30 1986 N     -31.2590    18.4780    -7.1980 0 CHG=0 CFG=0
M  V30 1987 H     -31.1036    18.6571    -8.1657 0 CHG=0 CFG=0
M  V30 1988 C     -31.7380    19.5620    -6.3310 0 CHG=0 CFG=1
M  V30 1989 H     -30.9839    19.6735    -5.5504 0 CHG=0 CFG=0
M  V30 1990 C     -31.8570    20.8720    -7.1160 0 CHG=0 CFG=0
M  V30 1991 H     -32.6147    20.7967    -7.8972 0 CHG=0 CFG=0
M  V30 1992 H     -30.9121    20.9955    -7.6477 0 CHG=0 CFG=0
M  V30 1993 C     -32.1070    22.1020    -6.2640 0 CHG=0 CFG=0
M  V30 1994 H     -31.6420    21.9768    -5.2852 0 CHG=0 CFG=0
M  V30 1995 H     -33.1733    22.2379    -6.0844 0 CHG=0 CFG=0
M  V30 1996 C     -31.5340    23.3550    -6.8960 0 CHG=0 CFG=0
M  V30 1997 O     -32.1560    23.8870    -7.8360 0 CHG=0 CFG=0
M  V30 1998 O     -30.4430    23.7960    -6.4640 0 CHG=-1 CFG=0
M  V30 1999 C     -33.0670    19.1950    -5.6630 0 CHG=0 CFG=0
M  V30 2000 O     -33.2790    19.4710    -4.4760 0 CHG=0 CFG=0
M  V30 2001 N     -33.9420    18.5420    -6.4260 0 CHG=0 CFG=0
M  V30 2002 H     -33.6912    18.4049    -7.3872 0 CHG=0 CFG=0
M  V30 2003 C     -35.2600    18.1410    -5.9290 0 CHG=0 CFG=1
M  V30 2004 H     -35.7140    19.0441    -5.5184 0 CHG=0 CFG=0
M  V30 2005 C     -36.1200    17.6010    -7.0730 0 CHG=0 CFG=0
M  V30 2006 H     -36.0132    18.2045    -7.9830 0 CHG=0 CFG=0
M  V30 2007 H     -37.1702    17.6605    -6.7838 0 CHG=0 CFG=0
M  V30 2008 O     -35.8380    16.2350    -7.3360 0 CHG=0 CFG=0
M  V30 2009 H     -34.9111    16.1572    -7.5295 0 CHG=0 CFG=0
M  V30 2010 C     -35.1460    17.1010    -4.8110 0 CHG=0 CFG=0
M  V30 2011 O     -36.0630    16.9510    -3.9980 0 CHG=0 CFG=0
M  V30 2012 N     -34.0250    16.3790    -4.8030 0 CHG=0 CFG=0
M  V30 2013 H     -33.3352    16.5545    -5.5077 0 CHG=0 CFG=0
M  V30 2014 C     -33.7150    15.3800    -3.7790 0 CHG=0 CFG=1
M  V30 2015 H     -34.6446    15.1027    -3.2818 0 CHG=0 CFG=0
M  V30 2016 C     -33.0720    14.1430    -4.4250 0 CHG=0 CFG=0
M  V30 2017 H     -32.7882    13.4310    -3.6476 0 CHG=0 CFG=0
M  V30 2018 H     -32.1367    14.4444    -4.9015 0 CHG=0 CFG=0
M  V30 2019 C     -33.9370    13.4220    -5.4610 0 CHG=0 CFG=0
M  V30 2020 H     -33.3472    12.6192    -5.9062 0 CHG=0 CFG=0
M  V30 2021 H     -34.1860    14.0956    -6.2789 0 CHG=0 CFG=0
M  V30 2022 C     -35.1970    12.8440    -4.8390 0 CHG=0 CFG=0
M  V30 2023 H     -35.8100    13.6680    -4.4713 0 CHG=0 CFG=0
M  V30 2024 H     -34.9377    12.2307    -3.9742 0 CHG=0 CFG=0
M  V30 2025 C     -35.9900    12.0300    -5.8450 0 CHG=0 CFG=0
M  V30 2026 H     -35.4903    11.0820    -6.0620 0 CHG=0 CFG=0
M  V30 2027 H     -36.0698    12.5820    -6.7839 0 CHG=0 CFG=0
M  V30 2028 N     -37.3720    11.7640    -5.3610 0 CHG=1 CFG=0
M  V30 2029 H     -37.8510    12.6753    -5.2040 0 CHG=0 CFG=0
M  V30 2030 H     -37.3259    11.2414    -4.4632 0 CHG=0 CFG=0
M  V30 2031 H     -37.8966    11.2083    -6.0656 0 CHG=0 CFG=0
M  V30 2032 C     -32.7920    15.9300    -2.6820 0 CHG=0 CFG=0
M  V30 2033 O     -32.3670    15.1830    -1.7840 0 CHG=0 CFG=0
M  V30 2034 N     -32.4940    17.2300    -2.7590 0 CHG=0 CFG=0
M  V30 2035 H     -32.8793    17.7762    -3.5026 0 CHG=0 CFG=0
M  V30 2036 C     -31.5770    17.9080    -1.8260 0 CHG=0 CFG=1
M  V30 2037 H     -31.4423    18.9054    -2.2445 0 CHG=0 CFG=0
M  V30 2038 C     -32.1830    18.0190    -0.4140 0 CHG=0 CFG=0
M  V30 2039 H     -31.4574    18.5095     0.2355 0 CHG=0 CFG=0
M  V30 2040 H     -32.3321    17.0262     0.0148 0 CHG=0 CFG=0
M  V30 2041 C     -33.4790    18.8230    -0.3460 0 CHG=0 CFG=0
M  V30 2042 H     -33.3688    19.7692    -0.8760 0 CHG=0 CFG=0
M  V30 2043 H     -33.7008    19.0646     0.6932 0 CHG=0 CFG=0
M  V30 2044 C     -34.6780    18.0600    -0.8900 0 CHG=0 CFG=0
M  V30 2045 O     -34.9590    16.9340    -0.4710 0 CHG=0 CFG=0
M  V30 2046 N     -35.3880    18.6700    -1.8320 0 CHG=0 CFG=0
M  V30 2047 H     -35.1660    19.5837    -2.1663 0 CHG=0 CFG=0
M  V30 2048 H     -36.1266    18.1390    -2.2554 0 CHG=0 CFG=0
M  V30 2049 C     -30.1950    17.2430    -1.7870 0 CHG=0 CFG=0
M  V30 2050 O     -29.5570    17.1640    -0.7360 0 CHG=0 CFG=0
M  V30 2051 N     -29.7480    16.7780    -2.9520 0 CHG=0 CFG=0
M  V30 2052 H     -30.3047    16.9162    -3.7736 0 CHG=0 CFG=0
M  V30 2053 C     -28.4750    16.0770    -3.0940 0 CHG=0 CFG=1
M  V30 2054 H     -28.0889    15.8436    -2.0999 0 CHG=0 CFG=0
M  V30 2055 C     -28.6780    14.7780    -3.8940 0 CHG=0 CFG=0
M  V30 2056 H     -28.9304    15.0048    -4.9313 0 CHG=0 CFG=0
M  V30 2057 H     -29.5469    14.2515    -3.4962 0 CHG=0 CFG=0
M  V30 2058 C     -27.4990    13.8500    -3.8570 0 CHG=0 CFG=0
M  V30 2059 C     -26.3560    14.1200    -4.6100 0 CHG=0 CFG=0
M  V30 2060 H     -26.3205    14.9963    -5.2418 0 CHG=0 CFG=0
M  V30 2061 C     -27.5310    12.6990    -3.0750 0 CHG=0 CFG=0
M  V30 2062 H     -28.4060    12.4601    -2.4854 0 CHG=0 CFG=0
M  V30 2063 C     -25.2530    13.2700    -4.5680 0 CHG=0 CFG=0
M  V30 2064 H     -24.3738    13.5069    -5.1442 0 CHG=0 CFG=0
M  V30 2065 C     -26.4330    11.8290    -3.0350 0 CHG=0 CFG=0
M  V30 2066 H     -26.4741    10.9387    -2.4174 0 CHG=0 CFG=0
M  V30 2067 C     -25.2920    12.1190    -3.7800 0 CHG=0 CFG=0
M  V30 2068 H     -24.4506    11.4404    -3.7573 0 CHG=0 CFG=0
M  V30 2069 C     -27.5050    16.9900    -3.8350 0 CHG=0 CFG=0
M  V30 2070 O     -27.7310    17.3060    -5.0020 0 CHG=0 CFG=0
M  V30 2071 N     -26.4410    17.4200    -3.1590 0 CHG=0 CFG=0
M  V30 2072 H     -26.3670    17.0997    -2.2201 0 CHG=0 CFG=0
M  V30 2073 C     -25.4350    18.2710    -3.7910 0 CHG=0 CFG=1
M  V30 2074 H     -25.9511    18.9418    -4.4820 0 CHG=0 CFG=0
M  V30 2075 C     -24.6590    19.0820    -2.7500 0 CHG=0 CFG=0
M  V30 2076 H     -23.8661    19.5982    -3.2977 0 CHG=0 CFG=0
M  V30 2077 H     -24.1481    18.4002    -2.0721 0 CHG=0 CFG=0
M  V30 2078 C     -25.3820    20.1550    -1.9410 0 CHG=0 CFG=0
M  V30 2079 H     -26.0163    19.6704    -1.1975 0 CHG=0 CFG=0
M  V30 2080 C     -24.3360    21.0110    -1.2380 0 CHG=0 CFG=0
M  V30 2081 H     -23.7242    21.5569    -1.9593 0 CHG=0 CFG=0
M  V30 2082 H     -23.6683    20.4089    -0.6247 0 CHG=0 CFG=0
M  V30 2083 H     -24.8085    21.7495    -0.5900 0 CHG=0 CFG=0
M  V30 2084 C     -26.2650    21.0190    -2.8190 0 CHG=0 CFG=0
M  V30 2085 H     -27.0690    20.4409    -3.2766 0 CHG=0 CFG=0
M  V30 2086 H     -25.6949    21.4841    -3.6262 0 CHG=0 CFG=0
M  V30 2087 H     -26.7391    21.8103    -2.2403 0 CHG=0 CFG=0
M  V30 2088 C     -24.4490    17.4410    -4.5870 0 CHG=0 CFG=0
M  V30 2089 O     -24.0420    16.3610    -4.1580 0 CHG=0 CFG=0
M  V30 2090 N     -24.0400    17.9510    -5.7400 0 CHG=0 CFG=0
M  V30 2091 H     -24.4803    18.7813    -6.0624 0 CHG=0 CFG=0
M  V30 2092 C     -23.0010    17.2610    -6.4850 0 CHG=0 CFG=1
M  V30 2093 H     -23.2442    16.1959    -6.4709 0 CHG=0 CFG=0
M  V30 2094 C     -22.9330    17.7390    -7.9280 0 CHG=0 CFG=0
M  V30 2095 H     -22.6485    18.7918    -7.9858 0 CHG=0 CFG=0
M  V30 2096 H     -23.9294    17.6747    -8.3646 0 CHG=0 CFG=0
M  V30 2097 C     -22.0190    16.9160    -8.7680 0 CHG=0 CFG=0
M  V30 2098 C     -22.2680    16.0810    -9.8040 0 CHG=0 CFG=0
M  V30 2099 H     -23.2477    15.8757   -10.2033 0 CHG=0 CFG=0
M  V30 2100 N     -20.6570    16.8760    -8.5580 0 CHG=0 CFG=0
M  V30 2101 H     -20.1373    17.2604    -7.8297 0 CHG=0 CFG=0
M  V30 2102 C     -20.1050    16.0550    -9.4360 0 CHG=0 CFG=0
M  V30 2103 H     -19.0491    15.8027    -9.4990 0 CHG=0 CFG=0
M  V30 2104 N     -21.0600    15.5580   -10.2010 0 CHG=1 CFG=0
M  V30 2105 H     -20.9159    14.8736   -10.9034 0 CHG=0 CFG=0
M  V30 2106 C     -21.6500    17.4650    -5.8050 0 CHG=0 CFG=0
M  V30 2107 O     -20.9150    16.4990    -5.5700 0 CHG=0 CFG=0
M  V30 2108 N     -21.3480    18.7320    -5.5080 0 CHG=0 CFG=0
M  V30 2109 H     -22.0150    19.4522    -5.7442 0 CHG=0 CFG=0
M  V30 2110 C     -20.1190    19.1880    -4.8360 0 CHG=0 CFG=1
M  V30 2111 H     -20.3396    20.2280    -4.5918 0 CHG=0 CFG=0
M  V30 2112 C     -19.8560    18.4420    -3.5070 0 CHG=0 CFG=0
M  V30 2113 H     -18.8199    18.6098    -3.2111 0 CHG=0 CFG=0
M  V30 2114 H     -19.9408    17.3634    -3.6281 0 CHG=0 CFG=0
M  V30 2115 C     -20.7100    18.9290    -2.3310 0 CHG=0 CFG=0
M  V30 2116 H     -21.7569    18.9730    -2.6292 0 CHG=0 CFG=0
M  V30 2117 H     -20.4172    19.9496    -2.0787 0 CHG=0 CFG=0
M  V30 2118 C     -20.5640    18.0140    -1.1100 0 CHG=0 CFG=0
M  V30 2119 H     -19.5057    17.8281    -0.9155 0 CHG=0 CFG=0
M  V30 2120 H     -21.0221    17.0377    -1.2741 0 CHG=0 CFG=0
M  V30 2121 N     -21.0710    18.6250     0.1240 0 CHG=0 CFG=0
M  V30 2122 H     -20.4368    19.3134     0.4886 0 CHG=0 CFG=0
M  V30 2123 C     -22.2250    18.3240     0.7220 0 CHG=0 CFG=0
M  V30 2124 N     -23.0460    17.4040     0.2260 0 CHG=1 CFG=0
M  V30 2125 H     -22.7982    16.9426    -0.6302 0 CHG=0 CFG=0
M  V30 2126 H     -23.9135    17.1578     0.6629 0 CHG=0 CFG=0
M  V30 2127 N     -22.5640    18.9540     1.8360 0 CHG=0 CFG=0
M  V30 2128 H     -21.9538    19.6413     2.2342 0 CHG=0 CFG=0
M  V30 2129 H     -23.4209    18.7650     2.3180 0 CHG=0 CFG=0
M  V30 2130 C     -18.8550    19.2720    -5.7140 0 CHG=0 CFG=0
M  V30 2131 O     -17.8860    19.9150    -5.3180 0 CHG=0 CFG=0
M  V30 2132 N     -18.8710    18.6720    -6.9060 0 CHG=0 CFG=0
M  V30 2133 H     -19.8061    18.5062    -7.1784 0 CHG=0 CFG=0
M  V30 2134 C     -17.7580    18.8640    -7.8430 0 CHG=0 CFG=1
M  V30 2135 H     -17.3985    19.8858    -7.6915 0 CHG=0 CFG=0
M  V30 2136 C     -16.6110    17.8780    -7.5550 0 CHG=0 CFG=0
M  V30 2137 H     -16.8947    16.8562    -7.8087 0 CHG=0 CFG=0
M  V30 2138 H     -16.3960    17.8906    -6.4867 0 CHG=0 CFG=0
M  V30 2139 C     -15.3200    18.2390    -8.2930 0 CHG=0 CFG=0
M  V30 2140 O     -15.1880    19.3860    -8.7590 0 CHG=0 CFG=0
M  V30 2141 O     -14.4350    17.3680    -8.4170 0 CHG=-1 CFG=0
M  V30 2142 C     -18.2130    18.7930    -9.3040 0 CHG=0 CFG=0
M  V30 2143 O     -17.6550    18.0410   -10.1030 0 CHG=0 CFG=0
M  V30 2144 N     -19.2360    19.5730    -9.6510 0 CHG=0 CFG=0
M  V30 2145 H     -19.4960    20.3127    -9.0305 0 CHG=0 CFG=0
M  V30 2146 C     -19.7390    19.5620   -11.0190 0 CHG=0 CFG=1
M  V30 2147 H     -19.8301    18.5117   -11.2993 0 CHG=0 CFG=0
M  V30 2148 C     -21.1290    20.2280   -11.1080 0 CHG=0 CFG=0
M  V30 2149 H     -21.0390    21.2626   -10.7726 0 CHG=0 CFG=0
M  V30 2150 H     -21.8038    19.7509   -10.3968 0 CHG=0 CFG=0
M  V30 2151 C     -21.7860    20.2240   -12.4980 0 CHG=0 CFG=0
M  V30 2152 H     -21.1064    20.7070   -13.2011 0 CHG=0 CFG=0
M  V30 2153 C     -22.0300    18.8000   -12.9860 0 CHG=0 CFG=0
M  V30 2154 H     -22.6776    18.2523   -12.3006 0 CHG=0 CFG=0
M  V30 2155 H     -21.1038    18.2390   -13.1033 0 CHG=0 CFG=0
M  V30 2156 H     -22.5204    18.8045   -13.9607 0 CHG=0 CFG=0
M  V30 2157 C     -23.0850    21.0470   -12.5240 0 CHG=0 CFG=0
M  V30 2158 H     -22.9014    22.0799   -12.2271 0 CHG=0 CFG=0
M  V30 2159 H     -23.8252    20.6397   -11.8352 0 CHG=0 CFG=0
M  V30 2160 H     -23.5270    21.0542   -13.5189 0 CHG=0 CFG=0
M  V30 2161 C     -18.7350    20.2350   -11.9600 0 CHG=0 CFG=0
M  V30 2162 O     -18.2640    21.3370   -11.6820 0 CHG=0 CFG=0
M  V30 2163 N     -18.4160    19.5520   -13.0640 0 CHG=0 CFG=0
M  V30 2164 H     -18.8490    18.6727   -13.2626 0 CHG=0 CFG=0
M  V30 2165 C     -17.4470    20.0340   -14.0600 0 CHG=0 CFG=1
M  V30 2166 H     -17.7627    21.0376   -14.3526 0 CHG=0 CFG=0
M  V30 2167 C     -16.0510    20.0510   -13.4790 0 CHG=0 CFG=0
M  V30 2168 H     -15.7507    19.0600   -13.1364 0 CHG=0 CFG=0
M  V30 2169 H     -15.9914    20.7248   -12.6235 0 CHG=0 CFG=0
M  V30 2170 H     -15.3179    20.3988   -14.2074 0 CHG=0 CFG=0
M  V30 2171 C     -17.4790    19.1240   -15.2800 0 CHG=0 CFG=0
M  V30 2172 O     -17.9220    17.9830   -15.1790 0 CHG=0 CFG=0
M  V30 2173 N     -16.9960    19.6060   -16.4260 0 CHG=0 CFG=0
M  V30 2174 H     -16.7439    20.5755   -16.4468 0 CHG=0 CFG=0
M  V30 2175 C     -17.0320    18.7910   -17.6440 0 CHG=0 CFG=1
M  V30 2176 H     -18.0854    18.5536   -17.8052 0 CHG=0 CFG=0
M  V30 2177 C     -16.5130    19.5670   -18.8680 0 CHG=0 CFG=0
M  V30 2178 H     -15.4630    19.8326   -18.7520 0 CHG=0 CFG=0
M  V30 2179 H     -17.0823    20.4842   -19.0195 0 CHG=0 CFG=0
M  V30 2180 H     -16.6089    18.9700   -19.7773 0 CHG=0 CFG=0
M  V30 2181 C     -16.3040    17.4600   -17.4750 0 CHG=0 CFG=0
M  V30 2182 O     -16.7220    16.4350   -18.0270 0 CHG=0 CFG=0
M  V30 2183 N     -15.2550    17.4640   -16.6580 0 CHG=0 CFG=0
M  V30 2184 H     -15.0125    18.3226   -16.2167 0 CHG=0 CFG=0
M  V30 2185 C     -14.4500    16.2570   -16.4330 0 CHG=0 CFG=1
M  V30 2186 H     -14.1911    15.8661   -17.4176 0 CHG=0 CFG=0
M  V30 2187 C     -13.1700    16.5890   -15.6650 0 CHG=0 CFG=0
M  V30 2188 H     -12.5512    17.2550   -16.2658 0 CHG=0 CFG=0
M  V30 2189 H     -12.5870    15.6738   -15.5393 0 CHG=0 CFG=0
M  V30 2190 C     -13.4200    17.2120   -14.3060 0 CHG=0 CFG=0
M  V30 2191 H     -14.1013    16.5981   -13.7154 0 CHG=0 CFG=0
M  V30 2192 H     -13.9272    18.1651   -14.4562 0 CHG=0 CFG=0
M  V30 2193 C     -12.1450    17.4350   -13.4990 0 CHG=0 CFG=0
M  V30 2194 H     -11.2957    17.6632   -14.1437 0 CHG=0 CFG=0
M  V30 2195 H     -11.8779    16.5832   -12.8700 0 CHG=0 CFG=0
M  V30 2196 N     -12.3460    18.6240   -12.6700 0 CHG=0 CFG=0
M  V30 2197 H     -11.9390    19.4675   -13.0195 0 CHG=0 CFG=0
M  V30 2198 C     -13.0250    18.6540   -11.5270 0 CHG=0 CFG=0
M  V30 2199 N     -13.5510    17.5470   -11.0210 0 CHG=1 CFG=0
M  V30 2200 H     -13.5380    16.6715   -11.5040 0 CHG=0 CFG=0
M  V30 2201 H     -13.9828    17.5691   -10.1050 0 CHG=0 CFG=0
M  V30 2202 N     -13.1780    19.8040   -10.8890 0 CHG=0 CFG=0
M  V30 2203 H     -12.7974    20.6726   -11.1943 0 CHG=0 CFG=0
M  V30 2204 H     -13.7419    19.7950   -10.0418 0 CHG=0 CFG=0
M  V30 2205 C     -15.2290    15.1750   -15.6880 0 CHG=0 CFG=0
M  V30 2206 O     -14.8390    14.0030   -15.7230 0 CHG=0 CFG=0
M  V30 2207 N     -16.3110    15.5940   -15.0260 0 CHG=0 CFG=0
M  V30 2208 H     -16.6142    16.5389   -15.1215 0 CHG=0 CFG=0
M  V30 2209 C     -17.1930    14.7280   -14.2290 0 CHG=0 CFG=1
M  V30 2210 H     -16.7032    13.7569   -14.1226 0 CHG=0 CFG=0
M  V30 2211 C     -17.4440    15.3440   -12.8390 0 CHG=0 CFG=0
M  V30 2212 H     -18.2444    14.8174   -12.3166 0 CHG=0 CFG=0
M  V30 2213 H     -17.7499    16.3865   -12.9288 0 CHG=0 CFG=0
M  V30 2214 C     -16.2360    15.2380   -11.9380 0 CHG=0 CFG=0
M  V30 2215 O     -15.3760    14.3770   -12.1400 0 CHG=0 CFG=0
M  V30 2216 N     -16.1490    16.1160   -10.9490 0 CHG=0 CFG=0
M  V30 2217 H     -16.7709    16.8730   -11.0215 0 CHG=0 CFG=0
M  V30 2218 H     -15.5323    16.0640   -10.1615 0 CHG=0 CFG=0
M  V30 2219 C     -18.5340    14.4510   -14.8920 0 CHG=0 CFG=0
M  V30 2220 O     -19.4830    14.0430   -14.2150 0 CHG=0 CFG=0
M  V30 2221 N     -18.6300    14.7010   -16.1970 0 CHG=0 CFG=0
M  V30 2222 H     -17.8298    14.9954   -16.7215 0 CHG=0 CFG=0
M  V30 2223 C     -19.8080    14.2990   -16.9610 0 CHG=0 CFG=1
M  V30 2224 H     -20.5329    13.8174   -16.3013 0 CHG=0 CFG=0
M  V30 2225 C     -20.4580    15.4870   -17.6580 0 CHG=0 CFG=0
M  V30 2226 H     -21.2845    15.1389   -18.2791 0 CHG=0 CFG=0
M  V30 2227 H     -19.7458    15.9670   -18.3283 0 CHG=0 CFG=0
M  V30 2228 S     -21.1060    16.7400   -16.5390 0 CHG=0 CFG=0
M  V30 2229 H     -21.8384    17.6189   -17.2284 0 CHG=0 CFG=0
M  V30 2230 C     -19.3660    13.2910   -18.0010 0 CHG=0 CFG=0
M  V30 2231 O     -18.2200    13.3090   -18.4330 0 CHG=0 CFG=0
M  V30 2232 N     -20.2910    12.4240   -18.4000 0 CHG=0 CFG=0
M  V30 2233 H     -21.2394    12.5151   -18.0879 0 CHG=0 CFG=0
M  V30 2234 C     -20.0080    11.3640   -19.3650 0 CHG=0 CFG=1
M  V30 2235 H     -19.0034    11.5127   -19.7596 0 CHG=0 CFG=0
M  V30 2236 C     -20.1120     9.9980   -18.6930 0 CHG=0 CFG=0
M  V30 2237 H     -20.0254     9.2143   -19.4464 0 CHG=0 CFG=0
M  V30 2238 H     -21.1187     9.9024   -18.2820 0 CHG=0 CFG=0
M  V30 2239 C     -19.0960     9.7060   -17.5800 0 CHG=0 CFG=0
M  V30 2240 H     -19.0414    10.5685   -16.9145 0 CHG=0 CFG=0
M  V30 2241 C     -19.5330     8.5130   -16.7200 0 CHG=0 CFG=0
M  V30 2242 H     -19.8872     7.6738   -17.3180 0 CHG=0 CFG=0
M  V30 2243 H     -20.2871     8.7874   -16.0030 0 CHG=0 CFG=0
M  V30 2244 H     -18.6993     8.1590   -16.1210 0 CHG=0 CFG=0
M  V30 2245 C     -17.7020     9.4860   -18.1570 0 CHG=0 CFG=0
M  V30 2246 H     -17.3678    10.3612   -18.7010 0 CHG=0 CFG=0
M  V30 2247 H     -17.6833     8.6392   -18.8444 0 CHG=0 CFG=0
M  V30 2248 H     -16.9731     9.2927   -17.3698 0 CHG=0 CFG=0
M  V30 2249 C     -20.9670    11.4370   -20.5450 0 CHG=0 CFG=0
M  V30 2250 O     -22.0450    12.0100   -20.4390 0 CHG=0 CFG=0
M  V30 2251 N     -20.5840    10.8280   -21.6640 0 CHG=0 CFG=0
M  V30 2252 H     -19.6972    10.3676   -21.7179 0 CHG=0 CFG=0
M  V30 2253 C     -21.3830    10.9030   -22.8840 0 CHG=0 CFG=1
M  V30 2254 H     -22.3318    11.3890   -22.6583 0 CHG=0 CFG=0
M  V30 2255 C     -20.6410    11.6980   -23.9880 0 CHG=0 CFG=0
M  V30 2256 H     -19.7873    11.1164   -24.3401 0 CHG=0 CFG=0
M  V30 2257 C     -21.5710    11.9750   -25.1760 0 CHG=0 CFG=0
M  V30 2258 H     -22.4422    12.5565   -24.8698 0 CHG=0 CFG=0
M  V30 2259 H     -21.9287    11.0525   -25.6334 0 CHG=0 CFG=0
M  V30 2260 H     -21.0527    12.5361   -25.9496 0 CHG=0 CFG=0
M  V30 2261 C     -20.0810    13.0120   -23.4340 0 CHG=0 CFG=0
M  V30 2262 H     -19.2891    12.8290   -22.7071 0 CHG=0 CFG=0
M  V30 2263 H     -20.8565    13.5997   -22.9447 0 CHG=0 CFG=0
M  V30 2264 H     -19.6474    13.6215   -24.2245 0 CHG=0 CFG=0
M  V30 2265 C     -21.6630     9.4880   -23.3850 0 CHG=0 CFG=0
M  V30 2266 O     -20.7390     8.6820   -23.5100 0 CHG=0 CFG=0
M  V30 2267 N     -22.9320     9.1730   -23.6520 0 CHG=0 CFG=0
M  V30 2268 H     -23.6269     9.8961   -23.6135 0 CHG=0 CFG=0
M  V30 2269 C     -23.2560     7.8320   -24.1420 0 CHG=0 CFG=1
M  V30 2270 H     -22.5022     7.1546   -23.7385 0 CHG=0 CFG=0
M  V30 2271 C     -24.6020     7.3170   -23.5900 0 CHG=0 CFG=0
M  V30 2272 H     -24.6494     7.4727   -22.5135 0 CHG=0 CFG=0
M  V30 2273 H     -24.6882     6.2412   -23.7523 0 CHG=0 CFG=0
M  V30 2274 C     -25.8120     7.9790   -24.2350 0 CHG=0 CFG=0
M  V30 2275 O     -25.6980     8.7230   -25.2160 0 CHG=0 CFG=0
M  V30 2276 N     -26.9890     7.6910   -23.6880 0 CHG=0 CFG=0
M  V30 2277 H     -27.8146     8.1045   -24.0707 0 CHG=0 CFG=0
M  V30 2278 H     -27.0341     7.0294   -22.9421 0 CHG=0 CFG=0
M  V30 2279 C     -23.1570     7.7160   -25.6650 0 CHG=0 CFG=0
M  V30 2280 O     -22.8010     8.6860   -26.3460 0 CHG=0 CFG=0
M  V30 2281 N     -23.4760     6.5360   -26.1920 0 CHG=0 CFG=0
M  V30 2282 H     -23.9429     5.8125   -25.6784 0 CHG=0 CFG=0
M  V30 2283 C     -23.3780     6.2710   -27.6290 0 CHG=0 CFG=1
M  V30 2284 H     -22.3636     6.5524   -27.9152 0 CHG=0 CFG=0
M  V30 2285 C     -23.5580     4.7760   -27.9290 0 CHG=0 CFG=0
M  V30 2286 H     -22.7560     4.2004   -27.4704 0 CHG=0 CFG=0
M  V30 2287 H     -23.4938     4.5941   -29.0032 0 CHG=0 CFG=0
M  V30 2288 C     -24.8860     4.2060   -27.4160 0 CHG=0 CFG=0
M  V30 2289 O     -25.6030     4.8630   -26.6290 0 CHG=0 CFG=0
M  V30 2290 O     -25.2010     3.0600   -27.7980 0 CHG=-1 CFG=0
M  V30 2291 C     -24.3270     7.1140   -28.4920 0 CHG=0 CFG=0
M  V30 2292 O     -24.1570     7.1970   -29.7140 0 CHG=0 CFG=0
M  V30 2293 N     -25.3190     7.7240   -27.8510 0 CHG=0 CFG=0
M  V30 2294 H     -25.4314     7.5263   -26.8781 0 CHG=0 CFG=0
M  V30 2295 C     -26.3060     8.5510   -28.5400 0 CHG=0 CFG=1
M  V30 2296 H     -26.2712     8.3140   -29.6048 0 CHG=0 CFG=0
M  V30 2297 C     -27.7110     8.2600   -28.0020 0 CHG=0 CFG=0
M  V30 2298 H     -28.4260     8.9167   -28.5018 0 CHG=0 CFG=0
M  V30 2299 H     -27.7603     8.5083   -26.9419 0 CHG=0 CFG=0
M  V30 2300 C     -28.1660     6.8100   -28.2050 0 CHG=0 CFG=0
M  V30 2301 H     -29.2029     6.6966   -27.8913 0 CHG=0 CFG=0
M  V30 2302 H     -27.5759     6.1420   -27.5782 0 CHG=0 CFG=0
M  V30 2303 C     -28.0600     6.3600   -29.6480 0 CHG=0 CFG=0
M  V30 2304 O     -28.5800     7.0140   -30.5560 0 CHG=0 CFG=0
M  V30 2305 N     -27.3800     5.2390   -29.8690 0 CHG=0 CFG=0
M  V30 2306 H     -26.9299     4.7524   -29.1071 0 CHG=0 CFG=0
M  V30 2307 H     -27.2760     4.8808   -30.7928 0 CHG=0 CFG=0
M  V30 2308 C     -25.9860    10.0370   -28.4300 0 CHG=0 CFG=0
M  V30 2309 O     -26.7220    10.8820   -28.9590 0 CHG=0 CFG=0
M  V30 2310 N     -24.8900    10.3520   -27.7400 0 CHG=0 CFG=0
M  V30 2311 H     -24.3813     9.6221   -27.2831 0 CHG=0 CFG=0
M  V30 2312 C     -24.4540    11.7350   -27.5680 0 CHG=0 CFG=0
M  V30 2313 H     -24.6366    12.2792   -28.4958 0 CHG=0 CFG=0
M  V30 2314 H     -23.3808    11.6991   -27.3901 0 CHG=0 CFG=0
M  V30 2315 C     -25.1290    12.4460   -26.4110 0 CHG=0 CFG=0
M  V30 2316 O     -24.9670    13.6590   -26.2450 0 CHG=0 CFG=0
M  V30 2317 N     -25.8890    11.6890   -25.6160 0 CHG=0 CFG=0
M  V30 2318 H     -25.9429    10.7052   -25.7816 0 CHG=0 CFG=0
M  V30 2319 C     -26.5300    12.2240   -24.4200 0 CHG=0 CFG=1
M  V30 2320 H     -26.9412    13.2010   -24.6895 0 CHG=0 CFG=0
M  V30 2321 C     -27.6710    11.2980   -23.8960 0 CHG=0 CFG=0
M  V30 2322 H     -27.2382    10.3438   -23.6011 0 CHG=0 CFG=0
M  V30 2323 C     -28.3440    11.9130   -22.6740 0 CHG=0 CFG=0
M  V30 2324 H     -28.7111    12.9181   -22.8925 0 CHG=0 CFG=0
M  V30 2325 H     -27.6647    11.9960   -21.8250 0 CHG=0 CFG=0
M  V30 2326 H     -29.1941    11.3158   -22.3448 0 CHG=0 CFG=0
M  V30 2327 C     -28.7010    11.0470   -24.9750 0 CHG=0 CFG=0
M  V30 2328 H     -28.2631    10.5563   -25.8445 0 CHG=0 CFG=0
M  V30 2329 H     -29.1428    11.9841   -25.3176 0 CHG=0 CFG=0
M  V30 2330 H     -29.5104    10.4121   -24.6150 0 CHG=0 CFG=0
M  V30 2331 C     -25.4790    12.4090   -23.3330 0 CHG=0 CFG=0
M  V30 2332 O     -24.6610    11.5160   -23.0980 0 CHG=0 CFG=0
M  V30 2333 N     -25.4870    13.5780   -22.6950 0 CHG=0 CFG=0
M  V30 2334 H     -26.1839    14.2591   -22.9300 0 CHG=0 CFG=0
M  V30 2335 C     -24.5870    13.8470   -21.5710 0 CHG=0 CFG=1
M  V30 2336 H     -23.7133    13.2070   -21.6948 0 CHG=0 CFG=0
M  V30 2337 C     -24.1100    15.3240   -21.5420 0 CHG=0 CFG=0
M  V30 2338 H     -24.9847    15.9694   -21.4383 0 CHG=0 CFG=0
M  V30 2339 C     -23.1840    15.5700   -20.3550 0 CHG=0 CFG=0
M  V30 2340 H     -22.3027    14.9290   -20.4012 0 CHG=0 CFG=0
M  V30 2341 H     -23.6810    15.4057   -19.3991 0 CHG=0 CFG=0
M  V30 2342 H     -22.8549    16.6077   -20.3527 0 CHG=0 CFG=0
M  V30 2343 C     -23.4080    15.6890   -22.8490 0 CHG=0 CFG=0
M  V30 2344 H     -24.0982    15.6271   -23.6922 0 CHG=0 CFG=0
M  V30 2345 H     -22.5767    15.0180   -23.0588 0 CHG=0 CFG=0
M  V30 2346 H     -23.0216    16.7070   -22.8223 0 CHG=0 CFG=0
M  V30 2347 C     -25.2760    13.4900   -20.2540 0 CHG=0 CFG=0
M  V30 2348 O     -26.4510    13.8080   -20.0450 0 CHG=0 CFG=0
M  V30 2349 N     -24.5520    12.8110   -19.3730 0 CHG=0 CFG=0
M  V30 2350 H     -23.6046    12.5869   -19.5947 0 CHG=0 CFG=0
M  V30 2351 C     -25.0780    12.5020   -18.0480 0 CHG=0 CFG=1
M  V30 2352 H     -25.9922    13.0788   -17.9036 0 CHG=0 CFG=0
M  V30 2353 C     -25.3950    11.0080   -17.9210 0 CHG=0 CFG=0
M  V30 2354 H     -25.7990    10.8250   -16.9238 0 CHG=0 CFG=0
M  V30 2355 H     -24.4843    10.4190   -17.9801 0 CHG=0 CFG=0
M  V30 2356 C     -26.4150    10.5340   -18.9430 0 CHG=0 CFG=0
M  V30 2357 H     -25.9716    10.5821   -19.9370 0 CHG=0 CFG=0
M  V30 2358 H     -27.2505    11.2303   -18.9766 0 CHG=0 CFG=0
M  V30 2359 C     -26.9190     9.1420   -18.6590 0 CHG=0 CFG=0
M  V30 2360 H     -27.5443     9.1703   -17.7640 0 CHG=0 CFG=0
M  V30 2361 H     -26.0943     8.4616   -18.4363 0 CHG=0 CFG=0
M  V30 2362 C     -27.7030     8.6250   -19.8420 0 CHG=0 CFG=0
M  V30 2363 H     -27.0272     8.2417   -20.6077 0 CHG=0 CFG=0
M  V30 2364 H     -28.3129     9.4146   -20.2876 0 CHG=0 CFG=0
M  V30 2365 N     -28.6350     7.5240   -19.4400 0 CHG=1 CFG=0
M  V30 2366 H     -29.3689     7.9433   -18.8293 0 CHG=0 CFG=0
M  V30 2367 H     -28.1002     6.8054   -18.8890 0 CHG=0 CFG=0
M  V30 2368 H     -29.0652     7.0386   -20.2461 0 CHG=0 CFG=0
M  V30 2369 C     -24.1100    12.9380   -16.9630 0 CHG=0 CFG=0
M  V30 2370 O     -22.8970    12.9610   -17.1690 0 CHG=0 CFG=0
M  V30 2371 N     -24.6610    13.2930   -15.8090 0 CHG=0 CFG=0
M  V30 2372 H     -25.6614    13.2403   -15.7429 0 CHG=0 CFG=0
M  V30 2373 C     -23.8700    13.7170   -14.6610 0 CHG=0 CFG=1
M  V30 2374 H     -23.0010    14.2535   -15.0509 0 CHG=0 CFG=0
M  V30 2375 C     -24.6930    14.6810   -13.7730 0 CHG=0 CFG=0
M  V30 2376 H     -25.6666    14.2261   -13.5918 0 CHG=0 CFG=0
M  V30 2377 C     -24.0390    14.9290   -12.4270 0 CHG=0 CFG=0
M  V30 2378 H     -23.0313    15.3264   -12.5512 0 CHG=0 CFG=0
M  V30 2379 H     -23.9883    14.0249   -11.8201 0 CHG=0 CFG=0
M  V30 2380 H     -24.6290    15.6580   -11.8699 0 CHG=0 CFG=0
M  V30 2381 C     -24.9250    16.0050   -14.5210 0 CHG=0 CFG=0
M  V30 2382 H     -25.4690    15.8480   -15.4536 0 CHG=0 CFG=0
M  V30 2383 H     -23.9800    16.4908   -14.7663 0 CHG=0 CFG=0
M  V30 2384 H     -25.5126    16.7013   -13.9203 0 CHG=0 CFG=0
M  V30 2385 C     -23.3590    12.4890   -13.9010 0 CHG=0 CFG=0
M  V30 2386 O     -24.0860    11.5060   -13.7100 0 CHG=0 CFG=0
M  V30 2387 N     -22.0970    12.5490   -13.4910 0 CHG=0 CFG=0
M  V30 2388 H     -21.5355    13.3669   -13.6361 0 CHG=0 CFG=0
M  V30 2389 C     -21.4160    11.4100   -12.8830 0 CHG=0 CFG=1
M  V30 2390 H     -22.1625    10.6750   -12.5745 0 CHG=0 CFG=0
M  V30 2391 C     -20.4570    10.7870   -13.9000 0 CHG=0 CFG=0
M  V30 2392 H     -19.6685    11.4951   -14.1914 0 CHG=0 CFG=0
M  V30 2393 H     -21.0055    10.5911   -14.8189 0 CHG=0 CFG=0
M  V30 2394 O     -19.9160     9.5540   -13.4540 0 CHG=0 CFG=0
M  V30 2395 H     -19.2181     9.7257   -12.8269 0 CHG=0 CFG=0
M  V30 2396 C     -20.6470    11.8530   -11.6410 0 CHG=0 CFG=0
M  V30 2397 O     -20.5050    13.0530   -11.3870 0 CHG=0 CFG=0
M  V30 2398 N     -20.1610    10.8720   -10.8750 0 CHG=0 CFG=0
M  V30 2399 H     -20.3421     9.9211   -11.1313 0 CHG=0 CFG=0
M  V30 2400 C     -19.3520    11.1080    -9.6710 0 CHG=0 CFG=1
M  V30 2401 H     -19.2461    10.1382    -9.1875 0 CHG=0 CFG=0
M  V30 2402 C     -17.9820    11.6970   -10.0480 0 CHG=0 CFG=0
M  V30 2403 H     -17.5321    12.2284    -9.2082 0 CHG=0 CFG=0
M  V30 2404 H     -18.0596    12.4258   -10.8551 0 CHG=0 CFG=0
M  V30 2405 C     -16.9600    10.6330   -10.4280 0 CHG=0 CFG=0
M  V30 2406 O     -17.2580     9.4230   -10.3440 0 CHG=0 CFG=0
M  V30 2407 O     -15.8350    11.0220   -10.8010 0 CHG=-1 CFG=0
M  V30 2408 C     -20.0470    11.9990    -8.6410 0 CHG=0 CFG=0
M  V30 2409 O     -19.3820    12.6540    -7.8190 0 CHG=0 CFG=0
M  V30 2410 N     -21.3790    12.0140    -8.6700 0 CHG=0 CFG=0
M  V30 2411 H     -21.8331    11.3223    -9.2286 0 CHG=0 CFG=0
M  V30 2412 C     -22.1320    12.9410    -7.8280 0 CHG=0 CFG=1
M  V30 2413 H     -21.7049    13.9250    -8.0188 0 CHG=0 CFG=0
M  V30 2414 C     -23.6240    12.9860    -8.1960 0 CHG=0 CFG=0
M  V30 2415 H     -23.7592    13.6718    -9.0318 0 CHG=0 CFG=0
M  V30 2416 H     -24.2280    13.4067    -7.3915 0 CHG=0 CFG=0
M  V30 2417 C     -24.2000    11.6630    -8.6200 0 CHG=0 CFG=0
M  V30 2418 C     -24.1740    11.2770    -9.9600 0 CHG=0 CFG=0
M  V30 2419 H     -23.7366    11.9189   -10.7103 0 CHG=0 CFG=0
M  V30 2420 C     -24.7980    10.8170    -7.6950 0 CHG=0 CFG=0
M  V30 2421 H     -24.8412    11.0923    -6.6504 0 CHG=0 CFG=0
M  V30 2422 C     -24.7160    10.0560   -10.3660 0 CHG=0 CFG=0
M  V30 2423 H     -24.6957     9.7594   -11.4072 0 CHG=0 CFG=0
M  V30 2424 C     -25.3480     9.5950    -8.0920 0 CHG=0 CFG=0
M  V30 2425 H     -25.8053     8.9403    -7.3623 0 CHG=0 CFG=0
M  V30 2426 C     -25.3060     9.2140    -9.4300 0 CHG=0 CFG=0
M  V30 2427 H     -25.7320     8.2696    -9.7456 0 CHG=0 CFG=0
M  V30 2428 C     -21.9390    12.6490    -6.3500 0 CHG=0 CFG=0
M  V30 2429 O     -22.1960    11.5370    -5.8930 0 CHG=0 CFG=0
M  V30 2430 N     -21.4700    13.6580    -5.6190 0 CHG=0 CFG=0
M  V30 2431 H     -21.2060    14.5217    -6.0470 0 CHG=0 CFG=0
M  V30 2432 C     -21.2410    13.5580    -4.1760 0 CHG=0 CFG=0
M  V30 2433 H     -22.1115    13.0700    -3.7377 0 CHG=0 CFG=0
M  V30 2434 H     -21.2063    14.5804    -3.8004 0 CHG=0 CFG=0
M  V30 2435 C     -19.9740    12.8310    -3.7490 0 CHG=0 CFG=0
M  V30 2436 O     -19.6430    12.8070    -2.5550 0 CHG=0 CFG=0
M  V30 2437 N     -19.2610    12.2510    -4.7140 0 CHG=0 CFG=0
M  V30 2438 H     -19.5122    12.3819    -5.6747 0 CHG=0 CFG=0
M  V30 2439 C     -18.1370    11.3510    -4.4210 0 CHG=0 CFG=1
M  V30 2440 H     -18.5453    10.6243    -3.7187 0 CHG=0 CFG=0
M  V30 2441 C     -17.6820    10.6230    -5.7010 0 CHG=0 CFG=0
M  V30 2442 H     -17.0808    11.3021    -6.3093 0 CHG=0 CFG=0
M  V30 2443 H     -18.5806    10.4492    -6.2951 0 CHG=0 CFG=0
M  V30 2444 C     -16.9630     9.2750    -5.5830 0 CHG=0 CFG=0
M  V30 2445 H     -15.9937     9.4275    -5.1046 0 CHG=0 CFG=0
M  V30 2446 C     -17.7470     8.2830    -4.7280 0 CHG=0 CFG=0
M  V30 2447 H     -18.7829     8.2015    -5.0581 0 CHG=0 CFG=0
M  V30 2448 H     -17.7474     8.5692    -3.6767 0 CHG=0 CFG=0
M  V30 2449 H     -17.3130     7.2842    -4.7828 0 CHG=0 CFG=0
M  V30 2450 C     -16.7270     8.7060    -6.9740 0 CHG=0 CFG=0
M  V30 2451 H     -15.9889     9.3226    -7.4809 0 CHG=0 CFG=0
M  V30 2452 H     -17.6343     8.8264    -7.5681 0 CHG=0 CFG=0
M  V30 2453 H     -16.5523     7.6374    -7.0192 0 CHG=0 CFG=0
M  V30 2454 C     -16.9600    12.0330    -3.7290 0 CHG=0 CFG=0
M  V30 2455 O     -16.2160    11.3780    -2.9890 0 CHG=0 CFG=0
M  V30 2456 N     -16.8080    13.3450    -3.9420 0 CHG=0 CFG=0
M  V30 2457 H     -17.4485    13.8404    -4.5237 0 CHG=0 CFG=0
M  V30 2458 C     -15.7050    14.1010    -3.3310 0 CHG=0 CFG=1
M  V30 2459 H     -14.7934    13.6121    -3.6751 0 CHG=0 CFG=0
M  V30 2460 C     -15.7060    15.5690    -3.7840 0 CHG=0 CFG=0
M  V30 2461 H     -15.6619    15.6083    -4.8774 0 CHG=0 CFG=0
M  V30 2462 H     -14.7813    16.0339    -3.4097 0 CHG=0 CFG=0
M  V30 2463 O     -16.8470    16.2720    -3.3190 0 CHG=0 CFG=0
M  V30 2464 H     -16.7374    17.2079    -3.4905 0 CHG=0 CFG=0
M  V30 2465 C     -15.7080    14.0220    -1.8050 0 CHG=0 CFG=0
M  V30 2466 O     -14.6670    14.1850    -1.1730 0 CHG=0 CFG=0
M  V30 2467 N     -16.8780    13.7620    -1.2260 0 CHG=0 CFG=0
M  V30 2468 H     -17.6724    13.6345    -1.8159 0 CHG=0 CFG=0
M  V30 2469 C     -17.0280    13.6530     0.2320 0 CHG=0 CFG=1
M  V30 2470 H     -16.6633    14.5932     0.6493 0 CHG=0 CFG=0
M  V30 2471 C     -18.4980    13.4530     0.6000 0 CHG=0 CFG=0
M  V30 2472 H     -18.5778    13.1528     1.6480 0 CHG=0 CFG=0
M  V30 2473 H     -18.8753    12.6087     0.0250 0 CHG=0 CFG=0
M  V30 2474 C     -19.3700    14.6780     0.3970 0 CHG=0 CFG=0
M  V30 2475 H     -19.2179    15.0798    -0.6058 0 CHG=0 CFG=0
M  V30 2476 H     -19.0658    15.4593     1.0948 0 CHG=0 CFG=0
M  V30 2477 C     -20.8440    14.3390     0.5910 0 CHG=0 CFG=0
M  V30 2478 H     -21.4625    15.2293     0.5019 0 CHG=0 CFG=0
M  V30 2479 H     -20.9985    13.8998     1.5796 0 CHG=0 CFG=0
M  V30 2480 N     -21.3190    13.3780    -0.4050 0 CHG=0 CFG=0
M  V30 2481 H     -20.6385    13.0887    -1.0782 0 CHG=0 CFG=0
M  V30 2482 C     -22.5020    12.7770    -0.3510 0 CHG=0 CFG=0
M  V30 2483 N     -23.3440    13.0500     0.6430 0 CHG=1 CFG=0
M  V30 2484 H     -23.1259    13.6804     1.3796 0 CHG=0 CFG=0
M  V30 2485 H     -24.2064    12.5198     0.6873 0 CHG=0 CFG=0
M  V30 2486 N     -22.8550    11.9210    -1.3030 0 CHG=0 CFG=0
M  V30 2487 H     -23.7259    11.4094    -1.1925 0 CHG=0 CFG=0
M  V30 2488 H     -22.2826    11.7139    -2.0911 0 CHG=0 CFG=0
M  V30 2489 C     -16.1890    12.5370     0.8600 0 CHG=0 CFG=0
M  V30 2490 O     -15.9260    12.5530     2.0680 0 CHG=0 CFG=0
M  V30 2491 N     -15.7770    11.5750     0.0390 0 CHG=0 CFG=0
M  V30 2492 H     -15.9381    11.6484    -0.9445 0 CHG=0 CFG=0
M  V30 2493 C     -15.1520    10.3470     0.5470 0 CHG=0 CFG=1
M  V30 2494 H     -15.1108    10.4125     1.6364 0 CHG=0 CFG=0
M  V30 2495 C     -16.0250     9.1240     0.1930 0 CHG=0 CFG=0
M  V30 2496 H     -15.7059     8.2482     0.7617 0 CHG=0 CFG=0
M  V30 2497 H     -15.9186     8.8695    -0.8624 0 CHG=0 CFG=0
M  V30 2498 C     -17.4750     9.4180     0.4990 0 CHG=0 CFG=0
M  V30 2499 C     -17.8960     9.5710     1.8190 0 CHG=0 CFG=0
M  V30 2500 H     -17.1953     9.4413     2.6345 0 CHG=0 CFG=0
M  V30 2501 C     -19.2060     9.8890     2.1250 0 CHG=0 CFG=0
M  V30 2502 H     -19.4430     9.9891     3.1777 0 CHG=0 CFG=0
M  V30 2503 C     -18.4060     9.6210    -0.5210 0 CHG=0 CFG=0
M  V30 2504 H     -18.0907     9.5252    -1.5484 0 CHG=0 CFG=0
M  V30 2505 C     -19.7340     9.9430    -0.2220 0 CHG=0 CFG=0
M  V30 2506 H     -20.4580    10.0792    -1.0078 0 CHG=0 CFG=0
M  V30 2507 C     -20.1180    10.0730     1.1090 0 CHG=0 CFG=0
M  V30 2508 O     -21.4080    10.3970     1.4480 0 CHG=0 CFG=0
M  V30 2509 H     -21.6345    10.0920     2.3215 0 CHG=0 CFG=0
M  V30 2510 C     -13.7050    10.1850     0.1070 0 CHG=0 CFG=0
M  V30 2511 O     -13.0940     9.1540     0.3750 0 CHG=0 CFG=0
M  V30 2512 N     -13.1510    11.2190    -0.5280 0 CHG=0 CFG=0
M  V30 2513 H     -13.6393    12.0913    -0.5747 0 CHG=0 CFG=0
M  V30 2514 C     -11.7380    11.2210    -0.9440 0 CHG=0 CFG=1
M  V30 2515 H     -11.4955    10.1964    -1.2359 0 CHG=0 CFG=0
M  V30 2516 C     -11.5110    12.1500    -2.1630 0 CHG=0 CFG=0
M  V30 2517 H     -11.9324    13.1313    -1.9351 0 CHG=0 CFG=0
M  V30 2518 C     -10.0200    12.3330    -2.4460 0 CHG=0 CFG=0
M  V30 2519 H      -9.4917    11.3793    -2.4301 0 CHG=0 CFG=0
M  V30 2520 H      -9.5488    12.9911    -1.7124 0 CHG=0 CFG=0
M  V30 2521 H      -9.8399    12.7738    -3.4253 0 CHG=0 CFG=0
M  V30 2522 C     -12.2150    11.5910    -3.3830 0 CHG=0 CFG=0
M  V30 2523 H     -13.2903    11.5126    -3.2183 0 CHG=0 CFG=0
M  V30 2524 H     -11.8435    10.5966    -3.6319 0 CHG=0 CFG=0
M  V30 2525 H     -12.0644    12.2318    -4.2517 0 CHG=0 CFG=0
M  V30 2526 C     -10.8020    11.6060     0.2130 0 CHG=0 CFG=0
M  V30 2527 O     -10.9760    12.6520     0.8410 0 CHG=0 CFG=0
M  V30 2528 N      -9.8050    10.7570     0.4760 0 CHG=0 CFG=0
M  V30 2529 H      -9.7179     9.9268    -0.0758 0 CHG=0 CFG=0
M  V30 2530 C      -8.9070    10.9330     1.6250 0 CHG=0 CFG=1
M  V30 2531 H      -9.4821    11.4237     2.4113 0 CHG=0 CFG=0
M  V30 2532 C      -8.4080     9.5750     2.1420 0 CHG=0 CFG=0
M  V30 2533 H      -7.5757     9.7519     2.8271 0 CHG=0 CFG=0
M  V30 2534 H      -7.9702     9.0298     1.3040 0 CHG=0 CFG=0
M  V30 2535 C      -9.3900     8.6520     2.8810 0 CHG=0 CFG=0
M  V30 2536 H     -10.2200     8.4412     2.2052 0 CHG=0 CFG=0
M  V30 2537 C      -8.7300     7.3270     3.2280 0 CHG=0 CFG=0
M  V30 2538 H      -7.8420     7.4695     3.8440 0 CHG=0 CFG=0
M  V30 2539 H      -8.4354     6.7968     2.3247 0 CHG=0 CFG=0
M  V30 2540 H      -9.4180     6.6748     3.7674 0 CHG=0 CFG=0
M  V30 2541 C      -9.9690     9.2990     4.1350 0 CHG=0 CFG=0
M  V30 2542 H     -10.5472    10.1910     3.8942 0 CHG=0 CFG=0
M  V30 2543 H      -9.1821     9.5889     4.8318 0 CHG=0 CFG=0
M  V30 2544 H     -10.6424     8.6156     4.6539 0 CHG=0 CFG=0
M  V30 2545 C      -7.7170    11.8500     1.3550 0 CHG=0 CFG=0
M  V30 2546 O      -7.0800    12.3310     2.2970 0 CHG=0 CFG=0
M  V30 2547 N      -7.4140    12.0830     0.0800 0 CHG=0 CFG=0
M  V30 2548 H      -8.0382    11.7499    -0.6166 0 CHG=0 CFG=0
M  V30 2549 C      -6.3190    12.9710    -0.3040 0 CHG=0 CFG=1
M  V30 2550 H      -5.4619    12.6906     0.3129 0 CHG=0 CFG=0
M  V30 2551 C      -5.9660    12.7810    -1.7870 0 CHG=0 CFG=0
M  V30 2552 H      -6.7638    13.1609    -2.4259 0 CHG=0 CFG=0
M  V30 2553 H      -5.8580    11.7184    -2.0006 0 CHG=0 CFG=0
M  V30 2554 C      -4.6590    13.4720    -2.1780 0 CHG=0 CFG=0
M  V30 2555 O      -4.1550    14.3310    -1.4190 0 CHG=0 CFG=0
M  V30 2556 O      -4.1320    13.1480    -3.2610 0 CHG=-1 CFG=0
M  V30 2557 C      -6.6910    14.4260    -0.0130 0 CHG=0 CFG=0
M  V30 2558 O      -7.5280    15.0130    -0.7070 0 CHG=0 CFG=0
M  V30 2559 N      -6.0510    14.9930     1.0120 0 CHG=0 CFG=0
M  V30 2560 H      -5.4960    14.4010     1.5941 0 CHG=0 CFG=0
M  V30 2561 C      -6.3350    16.3550     1.4860 0 CHG=0 CFG=1
M  V30 2562 H      -7.3903    16.3884     1.7173 0 CHG=0 CFG=0
M  V30 2563 C      -5.5300    16.6660     2.7540 0 CHG=0 CFG=0
M  V30 2564 H      -5.5625    17.7348     2.9708 0 CHG=0 CFG=0
M  V30 2565 H      -4.4806    16.4046     2.6176 0 CHG=0 CFG=0
M  V30 2566 C      -6.0650    15.9500     3.9870 0 CHG=0 CFG=0
M  V30 2567 O      -6.9480    15.0750     3.8500 0 CHG=0 CFG=0
M  V30 2568 O      -5.5960    16.2670     5.1010 0 CHG=-1 CFG=0
M  V30 2569 C      -6.0940    17.4450     0.4410 0 CHG=0 CFG=0
M  V30 2570 O      -6.7070    18.5150     0.5060 0 CHG=0 CFG=0
M  V30 2571 N      -5.2080    17.1680    -0.5160 0 CHG=0 CFG=0
M  V30 2572 H      -4.7405    16.2782    -0.5095 0 CHG=0 CFG=0
M  V30 2573 C      -4.9210    18.0970    -1.6150 0 CHG=0 CFG=1
M  V30 2574 H      -4.5975    19.0255    -1.1450 0 CHG=0 CFG=0
M  V30 2575 C      -3.8130    17.5440    -2.5200 0 CHG=0 CFG=0
M  V30 2576 H      -3.6997    18.1664    -3.4061 0 CHG=0 CFG=0
M  V30 2577 H      -4.1457    16.5753    -2.8959 0 CHG=0 CFG=0
M  V30 2578 C      -2.4600    17.3300    -1.8300 0 CHG=0 CFG=0
M  V30 2579 H      -1.8659    16.6371    -2.4264 0 CHG=0 CFG=0
M  V30 2580 H      -2.5850    16.8568    -0.8561 0 CHG=0 CFG=0
M  V30 2581 C      -1.6510    18.6120    -1.6550 0 CHG=0 CFG=0
M  V30 2582 O      -2.2450    19.7110    -1.5630 0 CHG=0 CFG=0
M  V30 2583 O      -0.4060    18.5170    -1.6070 0 CHG=-1 CFG=0
M  V30 2584 C      -6.1680    18.4130    -2.4440 0 CHG=0 CFG=0
M  V30 2585 O      -6.2140    19.4160    -3.1550 0 CHG=0 CFG=0
M  V30 2586 N      -7.1780    17.5550    -2.3340 0 CHG=0 CFG=0
M  V30 2587 H      -7.0595    16.7498    -1.7449 0 CHG=0 CFG=0
M  V30 2588 C      -8.4290    17.7190    -3.0640 0 CHG=0 CFG=1
M  V30 2589 H      -8.3076    18.5206    -3.7935 0 CHG=0 CFG=0
M  V30 2590 C      -8.7530    16.4170    -3.8090 0 CHG=0 CFG=0
M  V30 2591 H      -8.6850    15.5880    -3.1013 0 CHG=0 CFG=0
M  V30 2592 H      -7.9884    16.2257    -4.5611 0 CHG=0 CFG=0
M  V30 2593 C     -10.1080    16.3710    -4.4780 0 CHG=0 CFG=0
M  V30 2594 C     -10.4530    17.2830    -5.4780 0 CHG=0 CFG=0
M  V30 2595 H      -9.7476    18.0407    -5.7552 0 CHG=0 CFG=0
M  V30 2596 C     -11.6980    17.2380    -6.0880 0 CHG=0 CFG=0
M  V30 2597 H     -11.9062    17.9640    -6.8592 0 CHG=0 CFG=0
M  V30 2598 C     -11.0410    15.4020    -4.1180 0 CHG=0 CFG=0
M  V30 2599 H     -10.8024    14.7049    -3.3313 0 CHG=0 CFG=0
M  V30 2600 C     -12.2830    15.3460    -4.7220 0 CHG=0 CFG=0
M  V30 2601 H     -12.9850    14.5867    -4.4251 0 CHG=0 CFG=0
M  V30 2602 C     -12.6060    16.2650    -5.7050 0 CHG=0 CFG=0
M  V30 2603 O     -13.8390    16.2070    -6.3040 0 CHG=0 CFG=0
M  V30 2604 H     -14.0477    17.0389    -6.7048 0 CHG=0 CFG=0
M  V30 2605 C      -9.5800    18.1430    -2.1380 0 CHG=0 CFG=0
M  V30 2606 O     -10.6200    18.6160    -2.6010 0 CHG=0 CFG=0
M  V30 2607 N      -9.3650    18.0040    -0.8300 0 CHG=0 CFG=0
M  V30 2608 H      -8.5201    17.5849    -0.4959 0 CHG=0 CFG=0
M  V30 2609 C     -10.4160    18.2030     0.1730 0 CHG=0 CFG=1
M  V30 2610 H     -11.3021    17.7035    -0.2235 0 CHG=0 CFG=0
M  V30 2611 C     -10.0150    17.5110     1.4590 0 CHG=0 CFG=2
M  V30 2612 H      -9.0850    17.9552     1.8321 0 CHG=0 CFG=0
M  V30 2613 O      -9.7650    16.1630     1.0930 0 CHG=0 CFG=0
M  V30 2614 H      -9.6039    15.6009     1.8505 0 CHG=0 CFG=0
M  V30 2615 C     -11.1000    17.5860     2.5550 0 CHG=0 CFG=0
M  V30 2616 H     -12.0281    17.1268     2.2133 0 CHG=0 CFG=0
M  V30 2617 H     -11.3207    18.6149     2.8368 0 CHG=0 CFG=0
M  V30 2618 H     -10.7891    17.0740     3.4666 0 CHG=0 CFG=0
M  V30 2619 C     -10.8080    19.6630     0.4420 0 CHG=0 CFG=0
M  V30 2620 O     -11.9970    19.9670     0.5770 0 CHG=0 CFG=0
M  V30 2621 N      -9.8210    20.5560     0.5260 0 CHG=0 CFG=0
M  V30 2622 H      -8.8946    20.2475     0.2959 0 CHG=0 CFG=0
M  V30 2623 C     -10.0790    21.9710     0.8350 0 CHG=0 CFG=1
M  V30 2624 H     -11.1577    22.1283     0.7831 0 CHG=0 CFG=0
M  V30 2625 C      -9.5920    22.3140     2.2460 0 CHG=0 CFG=0
M  V30 2626 H      -8.5000    22.2892     2.2736 0 CHG=0 CFG=0
M  V30 2627 H      -9.9158    21.5534     2.9682 0 CHG=0 CFG=0
M  V30 2628 O     -10.0090    23.6140     2.6270 0 CHG=0 CFG=0
M  V30 2629 H     -10.9084    23.6093     2.9548 0 CHG=0 CFG=0
M  V30 2630 C      -9.4640    22.9270    -0.1920 0 CHG=0 CFG=0
M  V30 2631 O      -8.5710    22.5380    -0.9500 0 CHG=0 CFG=0
M  V30 2632 N      -9.9400    24.1750    -0.1980 0 CHG=0 CFG=0
M  V30 2633 H     -10.5023    24.4504     0.5808 0 CHG=0 CFG=0
M  V30 2634 C      -9.5730    25.1620    -1.2300 0 CHG=0 CFG=1
M  V30 2635 H      -9.7211    24.6658    -2.1737 0 CHG=0 CFG=0
M  V30 2636 C     -10.4780    26.4040    -1.1650 0 CHG=0 CFG=0
M  V30 2637 H     -11.5259    26.0991    -1.0780 0 CHG=0 CFG=0
M  V30 2638 H     -10.3682    26.9434    -2.1124 0 CHG=0 CFG=0
M  V30 2639 O     -10.1130    27.2650    -0.0920 0 CHG=0 CFG=0
M  V30 2640 H     -10.6460    28.0640    -0.0610 0 CHG=0 CFG=0
M  V30 2641 C      -8.0970    25.5670    -1.2360 0 CHG=0 CFG=0
M  V30 2642 O      -7.6120    26.1420    -2.2170 0 CHG=0 CFG=0
M  V30 2643 N      -7.3970    25.2750    -0.1410 0 CHG=0 CFG=0
M  V30 2644 H      -7.8889    24.8933     0.6374 0 CHG=0 CFG=0
M  V30 2645 C      -5.9530    25.4820    -0.0630 0 CHG=0 CFG=1
M  V30 2646 H      -5.7267    26.4348    -0.5455 0 CHG=0 CFG=0
M  V30 2647 C      -5.4780    25.4910     1.3930 0 CHG=0 CFG=0
M  V30 2648 H      -4.3892    25.5781     1.3909 0 CHG=0 CFG=0
M  V30 2649 C      -6.0260    26.7250     2.1240 0 CHG=0 CFG=0
M  V30 2650 H      -7.1146    26.7001     2.1893 0 CHG=0 CFG=0
M  V30 2651 H      -5.7469    27.6436     1.6069 0 CHG=0 CFG=0
M  V30 2652 H      -5.6342    26.7858     3.1395 0 CHG=0 CFG=0
M  V30 2653 C      -5.8420    24.2140     2.1750 0 CHG=0 CFG=0
M  V30 2654 H      -5.3867    23.3234     1.7411 0 CHG=0 CFG=0
M  V30 2655 H      -6.9195    24.0560     2.2174 0 CHG=0 CFG=0
M  V30 2656 H      -5.4836    24.2767     3.2026 0 CHG=0 CFG=0
M  V30 2657 C      -5.2190    24.3820    -0.8210 0 CHG=0 CFG=0
M  V30 2658 O      -4.1340    24.6080    -1.3640 0 CHG=0 CFG=0
M  V30 2659 N      -5.8300    23.1960    -0.8570 0 CHG=0 CFG=0
M  V30 2660 H      -6.7584    23.0978    -0.5078 0 CHG=0 CFG=0
M  V30 2661 C      -5.2610    22.0270    -1.5250 0 CHG=0 CFG=0
M  V30 2662 H      -6.0026    21.2336    -1.4427 0 CHG=0 CFG=0
M  V30 2663 H      -4.3718    21.7305    -0.9657 0 CHG=0 CFG=0
M  V30 2664 C      -4.9140    22.2560    -2.9850 0 CHG=0 CFG=0
M  V30 2665 O      -5.5330    23.0810    -3.6620 0 CHG=0 CFG=0
M  V30 2666 N      -3.9230    21.5080    -3.4640 0 CHG=0 CFG=0
M  V30 2667 H      -3.4899    20.8400    -2.8466 0 CHG=0 CFG=0
M  V30 2668 C      -3.3910    21.6730    -4.8150 0 CHG=0 CFG=1
M  V30 2669 H      -3.3931    22.7442    -5.0225 0 CHG=0 CFG=0
M  V30 2670 C      -1.9460    21.1650    -4.8670 0 CHG=0 CFG=0
M  V30 2671 H      -1.2995    21.7642    -4.2112 0 CHG=0 CFG=0
M  V30 2672 H      -1.5461    21.2896    -5.8742 0 CHG=0 CFG=0
M  V30 2673 O      -1.8790    19.7850    -4.5540 0 CHG=0 CFG=0
M  V30 2674 H      -1.7658    19.6454    -3.5990 0 CHG=0 CFG=0
M  V30 2675 C      -4.2330    20.9920    -5.9010 0 CHG=0 CFG=0
M  V30 2676 O      -3.9590    21.1510    -7.0900 0 CHG=0 CFG=0
M  V30 2677 N      -5.2470    20.2340    -5.4870 0 CHG=0 CFG=0
M  V30 2678 H      -5.3239    20.1402    -4.4992 0 CHG=0 CFG=0
M  V30 2679 C      -6.1030    19.4900    -6.4160 0 CHG=0 CFG=1
M  V30 2680 H      -5.7764    19.6919    -7.4362 0 CHG=0 CFG=0
M  V30 2681 C      -6.0000    17.9830    -6.1470 0 CHG=0 CFG=0
M  V30 2682 H      -6.7749    17.4398    -6.6909 0 CHG=0 CFG=0
M  V30 2683 H      -6.2278    17.8090    -5.0967 0 CHG=0 CFG=0
M  V30 2684 C      -4.6420    17.3590    -6.4520 0 CHG=0 CFG=0
M  V30 2685 H      -4.5468    16.4502    -5.8534 0 CHG=0 CFG=0
M  V30 2686 H      -3.8320    18.0131    -6.1229 0 CHG=0 CFG=0
M  V30 2687 C      -4.5090    16.9930    -7.9230 0 CHG=0 CFG=0
M  V30 2688 H      -4.5349    17.9126    -8.5085 0 CHG=0 CFG=0
M  V30 2689 H      -5.3644    16.3907    -8.2348 0 CHG=0 CFG=0
M  V30 2690 C      -3.2230    16.2270    -8.1870 0 CHG=0 CFG=0
M  V30 2691 H      -3.2793    15.2095    -7.7967 0 CHG=0 CFG=0
M  V30 2692 H      -2.3914    16.7132    -7.6694 0 CHG=0 CFG=0
M  V30 2693 N      -2.8900    16.1890    -9.6430 0 CHG=1 CFG=0
M  V30 2694 H      -2.7994    17.1628    -9.9923 0 CHG=0 CFG=0
M  V30 2695 H      -3.6590    15.6864   -10.1300 0 CHG=0 CFG=0
M  V30 2696 H      -1.9924    15.6793    -9.7669 0 CHG=0 CFG=0
M  V30 2697 C      -7.5700    19.9310    -6.3440 0 CHG=0 CFG=0
M  V30 2698 O      -8.4360    19.3360    -6.9910 0 CHG=0 CFG=0
M  V30 2699 N      -7.8350    20.9750    -5.5620 0 CHG=0 CFG=0
M  V30 2700 H      -7.0901    21.3883    -5.0368 0 CHG=0 CFG=0
M  V30 2701 C      -9.1940    21.4830    -5.3500 0 CHG=0 CFG=1
M  V30 2702 H      -9.7966    20.6048    -5.1128 0 CHG=0 CFG=0
M  V30 2703 C      -9.2000    22.4420    -4.1540 0 CHG=0 CFG=0
M  V30 2704 H      -8.6300    23.3450    -4.3788 0 CHG=0 CFG=0
M  V30 2705 H      -8.6722    21.9657    -3.3268 0 CHG=0 CFG=0
M  V30 2706 C     -10.5760    22.8140    -3.6710 0 CHG=0 CFG=0
M  V30 2707 C     -11.2640    21.9910    -2.7790 0 CHG=0 CFG=0
M  V30 2708 H     -10.8061    21.0745    -2.4303 0 CHG=0 CFG=0
M  V30 2709 C     -11.1820    23.9920    -4.1030 0 CHG=0 CFG=0
M  V30 2710 H     -10.6613    24.6459    -4.7864 0 CHG=0 CFG=0
M  V30 2711 C     -12.5390    22.3340    -2.3290 0 CHG=0 CFG=0
M  V30 2712 H     -13.0487    21.6763    -1.6377 0 CHG=0 CFG=0
M  V30 2713 C     -12.4560    24.3460    -3.6620 0 CHG=0 CFG=0
M  V30 2714 H     -12.9246    25.2537    -4.0171 0 CHG=0 CFG=0
M  V30 2715 C     -13.1370    23.5160    -2.7720 0 CHG=0 CFG=0
M  V30 2716 H     -14.1248    23.7978    -2.4447 0 CHG=0 CFG=0
M  V30 2717 C      -9.7300    22.1800    -6.6140 0 CHG=0 CFG=0
M  V30 2718 O      -8.9650    22.8580    -7.3060 0 CHG=0 CFG=0
M  V30 2719 N     -11.0350    21.9960    -6.9310 0 CHG=0 CFG=0
M  V30 2720 C     -12.0100    21.1350    -6.2310 0 CHG=0 CFG=0
M  V30 2721 H     -12.0698    21.3222    -5.1663 0 CHG=0 CFG=0
M  V30 2722 H     -11.7348    20.0930    -6.3772 0 CHG=0 CFG=0
M  V30 2723 C     -11.6380    22.6460    -8.1050 0 CHG=0 CFG=1
M  V30 2724 H     -11.0036    22.5152    -8.9822 0 CHG=0 CFG=0
M  V30 2725 C     -12.9610    21.8950    -8.2810 0 CHG=0 CFG=0
M  V30 2726 H     -12.7617    20.9948    -8.8467 0 CHG=0 CFG=0
M  V30 2727 H     -13.7565    22.4447    -8.7853 0 CHG=0 CFG=0
M  V30 2728 C     -13.3200    21.4560    -6.9080 0 CHG=0 CFG=0
M  V30 2729 H     -13.8060    22.2795    -6.3814 0 CHG=0 CFG=0
M  V30 2730 H     -14.0114    20.6129    -6.8897 0 CHG=0 CFG=0
M  V30 2731 C     -11.8870    24.1460    -7.9060 0 CHG=0 CFG=0
M  V30 2732 O     -13.0340    24.6100    -7.9500 0 CHG=0 CFG=0
M  V30 2733 N     -10.8040    24.8900    -7.7010 0 CHG=0 CFG=0
M  V30 2734 H      -9.9190    24.4363    -7.5966 0 CHG=0 CFG=0
M  V30 2735 C     -10.8630    26.3400    -7.5530 0 CHG=0 CFG=1
M  V30 2736 H     -11.4170    26.5258    -6.6316 0 CHG=0 CFG=0
M  V30 2737 C      -9.4430    26.9280    -7.4640 0 CHG=0 CFG=0
M  V30 2738 H      -8.8472    26.5404    -8.2914 0 CHG=0 CFG=0
M  V30 2739 C      -9.4640    28.4480    -7.5940 0 CHG=0 CFG=0
M  V30 2740 H     -10.1543    28.9079    -6.8870 0 CHG=0 CFG=0
M  V30 2741 H      -9.7325    28.7858    -8.5954 0 CHG=0 CFG=0
M  V30 2742 H      -8.4779    28.8643    -7.3875 0 CHG=0 CFG=0
M  V30 2743 C      -8.7610    26.5060    -6.1470 0 CHG=0 CFG=0
M  V30 2744 H      -8.6547    25.4228    -6.0741 0 CHG=0 CFG=0
M  V30 2745 H      -9.3326    26.8408    -5.2800 0 CHG=0 CFG=0
M  V30 2746 H      -7.7627    26.9345    -6.0596 0 CHG=0 CFG=0
M  V30 2747 C     -11.6230    27.0230    -8.6970 0 CHG=0 CFG=0
M  V30 2748 O     -12.4280    27.9250    -8.4660 0 CHG=0 CFG=0
M  V30 2749 N     -11.3820    26.5840    -9.9290 0 CHG=0 CFG=0
M  V30 2750 H     -10.7128    25.8517   -10.0242 0 CHG=0 CFG=0
M  V30 2751 C     -11.9810    27.2410   -11.1010 0 CHG=0 CFG=1
M  V30 2752 H     -11.8254    28.3126   -10.9579 0 CHG=0 CFG=0
M  V30 2753 C     -11.2610    26.8140   -12.3890 0 CHG=0 CFG=0
M  V30 2754 H     -11.7072    27.3354   -13.2276 0 CHG=0 CFG=0
M  V30 2755 H     -11.4357    25.7611   -12.5683 0 CHG=0 CFG=0
M  V30 2756 C      -9.7770    27.0870   -12.3570 0 CHG=0 CFG=0
M  V30 2757 H      -9.3666    26.8408   -11.3775 0 CHG=0 CFG=0
M  V30 2758 H      -9.5929    28.1548   -12.4885 0 CHG=0 CFG=0
M  V30 2759 C      -8.9990    26.2860   -13.3890 0 CHG=0 CFG=0
M  V30 2760 H      -9.2036    26.5940   -14.4143 0 CHG=0 CFG=0
M  V30 2761 H      -9.2355    25.2245   -13.3150 0 CHG=0 CFG=0
M  V30 2762 N      -7.5720    26.3910   -13.1000 0 CHG=0 CFG=0
M  V30 2763 H      -7.2368    25.7997   -12.3623 0 CHG=0 CFG=0
M  V30 2764 C      -6.7680    27.3300   -13.5890 0 CHG=0 CFG=0
M  V30 2765 N      -7.2330    28.2480   -14.4420 0 CHG=1 CFG=0
M  V30 2766 H      -8.1849    28.2314   -14.7681 0 CHG=0 CFG=0
M  V30 2767 H      -6.6560    28.9958   -14.7987 0 CHG=0 CFG=0
M  V30 2768 N      -5.4910    27.3390   -13.2400 0 CHG=0 CFG=0
M  V30 2769 H      -5.1155    26.6833   -12.5915 0 CHG=0 CFG=0
M  V30 2770 H      -4.8913    28.0428   -13.6507 0 CHG=0 CFG=0
M  V30 2771 C     -13.4980    27.0360   -11.2580 0 CHG=0 CFG=0
M  V30 2772 O     -14.1220    27.6780   -12.1190 0 CHG=0 CFG=0
M  V30 2773 N     -14.0700    26.1340   -10.4560 0 CHG=0 CFG=0
M  V30 2774 H     -13.5458    25.7068    -9.7185 0 CHG=0 CFG=0
M  V30 2775 C     -15.5140    25.8460   -10.4790 0 CHG=0 CFG=1
M  V30 2776 H     -15.9759    26.4218   -11.2815 0 CHG=0 CFG=0
M  V30 2777 C     -15.7750    24.3490   -10.7300 0 CHG=0 CFG=0
M  V30 2778 H     -16.8349    24.1230   -10.5932 0 CHG=0 CFG=0
M  V30 2779 H     -15.2450    23.7402    -9.9969 0 CHG=0 CFG=0
M  V30 2780 C     -15.4100    23.9170   -12.1090 0 CHG=0 CFG=0
M  V30 2781 C     -14.0920    23.6030   -12.5870 0 CHG=0 CFG=0
M  V30 2782 C     -14.2130    23.2720   -13.9560 0 CHG=0 CFG=0
M  V30 2783 C     -12.8240    23.5590   -11.9880 0 CHG=0 CFG=0
M  V30 2784 H     -12.7162    23.7997   -10.9406 0 CHG=0 CFG=0
M  V30 2785 C     -16.2510    23.7740   -13.1760 0 CHG=0 CFG=0
M  V30 2786 H     -17.3209    23.9339   -13.1391 0 CHG=0 CFG=0
M  V30 2787 N     -15.5390    23.3820   -14.2900 0 CHG=0 CFG=0
M  V30 2788 H     -15.9573    23.2056   -15.1635 0 CHG=0 CFG=0
M  V30 2789 C     -13.1100    22.9080   -14.7390 0 CHG=0 CFG=0
M  V30 2790 H     -13.2190    22.6621   -15.7834 0 CHG=0 CFG=0
M  V30 2791 C     -11.7240    23.1980   -12.7670 0 CHG=0 CFG=0
M  V30 2792 H     -10.7416    23.1688   -12.3172 0 CHG=0 CFG=0
M  V30 2793 C     -11.8770    22.8820   -14.1300 0 CHG=0 CFG=0
M  V30 2794 H     -11.0072    22.6165   -14.7141 0 CHG=0 CFG=0
M  V30 2795 C     -16.1910    26.2850    -9.1770 0 CHG=0 CFG=0
M  V30 2796 O     -17.3490    25.9320    -8.9290 0 CHG=0 CFG=0
M  V30 2797 N     -15.4770    27.0800    -8.3760 0 CHG=0 CFG=0
M  V30 2798 H     -14.6073    27.4762    -8.6708 0 CHG=0 CFG=0
M  V30 2799 C     -15.9130    27.4130    -7.0220 0 CHG=0 CFG=1
M  V30 2800 H     -16.7668    26.7760    -6.7952 0 CHG=0 CFG=0
M  V30 2801 C     -14.8090    27.0640    -6.0230 0 CHG=0 CFG=0
M  V30 2802 H     -15.0907    27.3989    -5.0226 0 CHG=0 CFG=0
M  V30 2803 H     -13.8787    27.5811    -6.2797 0 CHG=0 CFG=0
M  V30 2804 O     -14.6030    25.6690    -5.9480 0 CHG=0 CFG=0
M  V30 2805 H     -14.3583    25.3160    -6.8047 0 CHG=0 CFG=0
M  V30 2806 C     -16.3170    28.8790    -6.8520 0 CHG=0 CFG=0
M  V30 2807 O     -15.5750    29.7850    -7.2650 0 CHG=0 CFG=0
M  V30 2808 N     -17.4700    29.1260    -6.2000 0 CHG=0 CFG=0
M  V30 2809 C     -18.3990    28.1440    -5.6050 0 CHG=0 CFG=0
M  V30 2810 H     -17.8873    27.4473    -4.9430 0 CHG=0 CFG=0
M  V30 2811 H     -18.8792    27.5756    -6.4037 0 CHG=0 CFG=0
M  V30 2812 C     -17.9220    30.5020    -5.9900 0 CHG=0 CFG=1
M  V30 2813 H     -17.8311    31.0824    -6.9058 0 CHG=0 CFG=0
M  V30 2814 C     -19.3800    30.3260    -5.5590 0 CHG=0 CFG=0
M  V30 2815 H     -20.0285    30.2828    -6.4282 0 CHG=0 CFG=0
M  V30 2816 H     -19.7503    31.1293    -4.9286 0 CHG=0 CFG=0
M  V30 2817 C     -19.4140    29.0060    -4.8810 0 CHG=0 CFG=0
M  V30 2818 H     -19.0944    29.1421    -3.8465 0 CHG=0 CFG=0
M  V30 2819 H     -20.4128    28.5890    -4.8422 0 CHG=0 CFG=0
M  V30 2820 C     -17.1070    31.1880    -4.8900 0 CHG=0 CFG=0
M  V30 2821 O     -16.4210    30.5040    -4.1270 0 CHG=0 CFG=0
M  V30 2822 N     -17.1900    32.5270    -4.7880 0 CHG=0 CFG=0
M  V30 2823 C     -18.0070    33.4310    -5.6170 0 CHG=0 CFG=0
M  V30 2824 H     -19.0575    33.1442    -5.5874 0 CHG=0 CFG=0
M  V30 2825 H     -17.6516    33.4016    -6.6449 0 CHG=0 CFG=0
M  V30 2826 C     -16.4120    33.2370    -3.7630 0 CHG=0 CFG=1
M  V30 2827 H     -15.3541    33.2134    -4.0284 0 CHG=0 CFG=0
M  V30 2828 C     -16.9590    34.6690    -3.8050 0 CHG=0 CFG=0
M  V30 2829 H     -16.1590    35.4110    -3.7925 0 CHG=0 CFG=0
M  V30 2830 H     -17.6003    34.8920    -2.9512 0 CHG=0 CFG=0
M  V30 2831 C     -17.7920    34.7730    -5.0160 0 CHG=0 CFG=0
M  V30 2832 H     -18.7398    35.2702    -4.7963 0 CHG=0 CFG=0
M  V30 2833 H     -17.2880    35.4199    -5.7368 0 CHG=0 CFG=0
M  V30 2834 C     -16.5950    32.6530    -2.3620 0 CHG=0 CFG=0
M  V30 2835 O     -15.6190    32.4760    -1.6460 0 CHG=0 CFG=0
M  V30 2836 N     -17.8310    32.3410    -1.9810 0 CHG=0 CFG=0
M  V30 2837 H     -18.6024    32.5059    -2.5964 0 CHG=0 CFG=0
M  V30 2838 C     -18.1010    31.8850    -0.6080 0 CHG=0 CFG=1
M  V30 2839 H     -17.6138    32.6036     0.0501 0 CHG=0 CFG=0
M  V30 2840 C     -19.6030    31.9090    -0.2860 0 CHG=0 CFG=0
M  V30 2841 H     -20.0169    32.8973    -0.4914 0 CHG=0 CFG=0
M  V30 2842 H     -19.6969    31.7871     0.7936 0 CHG=0 CFG=0
M  V30 2843 C     -20.4410    30.8160    -0.9390 0 CHG=0 CFG=0
M  V30 2844 H     -21.3366    30.6578    -0.3383 0 CHG=0 CFG=0
M  V30 2845 H     -19.9343    29.8520    -0.9675 0 CHG=0 CFG=0
M  V30 2846 C     -20.9190    31.1720    -2.3440 0 CHG=0 CFG=0
M  V30 2847 O     -20.5140    32.2320    -2.8900 0 CHG=0 CFG=0
M  V30 2848 O     -21.7180    30.3810    -2.8990 0 CHG=-1 CFG=0
M  V30 2849 C     -17.4880    30.5200    -0.2940 0 CHG=0 CFG=0
M  V30 2850 O     -17.2600    30.2030     0.8700 0 CHG=0 CFG=0
M  V30 2851 N     -17.2380    29.7100    -1.3270 0 CHG=0 CFG=0
M  V30 2852 H     -17.4466    30.0388    -2.2484 0 CHG=0 CFG=0
M  V30 2853 C     -16.5060    28.4540    -1.1260 0 CHG=0 CFG=1
M  V30 2854 H     -16.8614    28.0175    -0.1917 0 CHG=0 CFG=0
M  V30 2855 C     -16.7430    27.4170    -2.2700 0 CHG=0 CFG=0
M  V30 2856 H     -16.6684    27.9525    -3.2161 0 CHG=0 CFG=0
M  V30 2857 C     -15.6550    26.3290    -2.2790 0 CHG=0 CFG=0
M  V30 2858 H     -15.5778    25.8338    -1.3103 0 CHG=0 CFG=0
M  V30 2859 H     -14.6711    26.7222    -2.5372 0 CHG=0 CFG=0
M  V30 2860 H     -15.8819    25.5638    -3.0229 0 CHG=0 CFG=0
M  V30 2861 C     -18.1350    26.7990    -2.1680 0 CHG=0 CFG=0
M  V30 2862 H     -18.9119    27.5642    -2.1667 0 CHG=0 CFG=0
M  V30 2863 H     -18.2441    26.2231    -1.2484 0 CHG=0 CFG=0
M  V30 2864 H     -18.3302    26.1246    -3.0016 0 CHG=0 CFG=0
M  V30 2865 C     -15.0140    28.7590    -0.9360 0 CHG=0 CFG=0
M  V30 2866 O     -14.4170    28.3100     0.0370 0 CHG=0 CFG=0
M  V30 2867 N     -14.4290    29.5410    -1.8450 0 CHG=0 CFG=0
M  V30 2868 H     -14.9844    29.9123    -2.5920 0 CHG=0 CFG=0
M  V30 2869 C     -12.9950    29.8700    -1.7750 0 CHG=0 CFG=1
M  V30 2870 H     -12.4612    28.9211    -1.8026 0 CHG=0 CFG=0
M  V30 2871 C     -12.5770    30.7500    -2.9610 0 CHG=0 CFG=0
M  V30 2872 H     -11.8960    31.5351    -2.6222 0 CHG=0 CFG=0
M  V30 2873 H     -13.4662    31.3151    -3.2470 0 CHG=0 CFG=0
M  V30 2874 C     -11.9290    30.1840    -4.2450 0 CHG=0 CFG=0
M  V30 2875 H     -10.8514    30.3229    -4.1390 0 CHG=0 CFG=0
M  V30 2876 C     -12.1140    28.6900    -4.4640 0 CHG=0 CFG=0
M  V30 2877 H     -13.1623    28.4212    -4.3509 0 CHG=0 CFG=0
M  V30 2878 H     -11.5445    28.1083    -3.7403 0 CHG=0 CFG=0
M  V30 2879 H     -11.7887    28.3911    -5.4581 0 CHG=0 CFG=0
M  V30 2880 C     -12.3480    31.0180    -5.4720 0 CHG=0 CFG=0
M  V30 2881 H     -12.1385    32.0782    -5.3224 0 CHG=0 CFG=0
M  V30 2882 H     -13.4159    30.9157    -5.6716 0 CHG=0 CFG=0
M  V30 2883 H     -11.8168    30.6997    -6.3695 0 CHG=0 CFG=0
M  V30 2884 C     -12.6120    30.5600    -0.4690 0 CHG=0 CFG=0
M  V30 2885 O     -11.5470    30.2950     0.0940 0 CHG=0 CFG=0
M  V30 2886 N     -13.4920    31.4360     0.0070 0 CHG=0 CFG=0
M  V30 2887 H     -14.3089    31.6175    -0.5400 0 CHG=0 CFG=0
M  V30 2888 C     -13.2310    32.2300     1.2050 0 CHG=0 CFG=1
M  V30 2889 H     -12.1567    32.4246     1.2340 0 CHG=0 CFG=0
M  V30 2890 C     -13.9650    33.5710     1.1350 0 CHG=0 CFG=0
M  V30 2891 H     -13.7644    34.1424     2.0430 0 CHG=0 CFG=0
M  V30 2892 H     -15.0354    33.3756     1.1445 0 CHG=0 CFG=0
M  V30 2893 C     -13.5880    34.4330    -0.0590 0 CHG=0 CFG=0
M  V30 2894 H     -13.7192    33.8667    -0.9800 0 CHG=0 CFG=0
M  V30 2895 H     -12.5331    34.7039    -0.0079 0 CHG=0 CFG=0
M  V30 2896 S     -14.5700    35.9450    -0.2110 0 CHG=0 CFG=0
M  V30 2897 C     -16.2490    35.3190    -0.2750 0 CHG=0 CFG=0
M  V30 2898 H     -16.8103    35.6895     0.5805 0 CHG=0 CFG=0
M  V30 2899 H     -16.2855    34.2411    -0.2820 0 CHG=0 CFG=0
M  V30 2900 H     -16.7422    35.7071    -1.1636 0 CHG=0 CFG=0
M  V30 2901 C     -13.5960    31.5240     2.5040 0 CHG=0 CFG=0
M  V30 2902 O     -12.8510    31.6210     3.4800 0 CHG=0 CFG=0
M  V30 2903 N     -14.7310    30.8220     2.5150 0 CHG=0 CFG=0
M  V30 2904 H     -15.2592    30.7488     1.6693 0 CHG=0 CFG=0
M  V30 2905 C     -15.3170    30.3190     3.7690 0 CHG=0 CFG=1
M  V30 2906 H     -14.5772    30.4396     4.5622 0 CHG=0 CFG=0
M  V30 2907 C     -16.5760    31.1310     4.1330 0 CHG=0 CFG=0
M  V30 2908 H     -16.9196    30.8499     5.1299 0 CHG=0 CFG=0
M  V30 2909 H     -17.3840    30.8576     3.4524 0 CHG=0 CFG=0
M  V30 2910 C     -16.4230    32.6330     4.1060 0 CHG=0 CFG=0
M  V30 2911 C     -15.4190    33.2670     4.8390 0 CHG=0 CFG=0
M  V30 2912 H     -14.7217    32.6783     5.4182 0 CHG=0 CFG=0
M  V30 2913 C     -15.2830    34.6490     4.8350 0 CHG=0 CFG=0
M  V30 2914 H     -14.4985    35.1232     5.4057 0 CHG=0 CFG=0
M  V30 2915 C     -17.3010    33.4280     3.3660 0 CHG=0 CFG=0
M  V30 2916 H     -18.0905    32.9688     2.7898 0 CHG=0 CFG=0
M  V30 2917 C     -17.1710    34.8180     3.3480 0 CHG=0 CFG=0
M  V30 2918 H     -17.8570    35.4200     2.7704 0 CHG=0 CFG=0
M  V30 2919 C     -16.1580    35.4190     4.0880 0 CHG=0 CFG=0
M  V30 2920 O     -16.0060    36.7870     4.0910 0 CHG=0 CFG=0
M  V30 2921 H     -15.7650    37.0786     3.2199 0 CHG=0 CFG=0
M  V30 2922 C     -15.7000    28.8380     3.7830 0 CHG=0 CFG=0
M  V30 2923 O     -16.1650    28.3290     4.8150 0 CHG=0 CFG=0
M  V30 2924 N     -15.5270    28.1540     2.6500 0 CHG=0 CFG=0
M  V30 2925 H     -15.0630    28.5894     1.8771 0 CHG=0 CFG=0
M  V30 2926 C     -15.9740    26.7600     2.4890 0 CHG=0 CFG=1
M  V30 2927 H     -15.7549    26.5088     1.4509 0 CHG=0 CFG=0
M  V30 2928 C     -15.2040    25.8070     3.4180 0 CHG=0 CFG=0
M  V30 2929 H     -15.3738    24.7718     3.1197 0 CHG=0 CFG=0
M  V30 2930 H     -15.5628    25.8847     4.4514 0 CHG=0 CFG=0
M  V30 2931 O     -13.8070    26.0540     3.3850 0 CHG=0 CFG=0
M  V30 2932 H     -13.6392    26.9799     3.5402 0 CHG=0 CFG=0
M  V30 2933 C     -17.4860    26.6110     2.7070 0 CHG=0 CFG=0
M  V30 2934 O     -17.9490    25.6280     3.3020 0 CHG=0 CFG=0
M  V30 2935 N     -18.2490    27.5930     2.2300 0 CHG=0 CFG=0
M  V30 2936 H     -17.8083    28.3611     1.7591 0 CHG=0 CFG=0
M  V30 2937 C     -19.7020    27.5460     2.3310 0 CHG=0 CFG=1
M  V30 2938 H     -19.9476    26.9590     3.2186 0 CHG=0 CFG=0
M  V30 2939 C     -20.2890    28.9470     2.5140 0 CHG=0 CFG=0
M  V30 2940 H     -20.1431    29.5329     1.6043 0 CHG=0 CFG=0
M  V30 2941 H     -19.7134    29.4569     3.2879 0 CHG=0 CFG=0
M  V30 2942 C     -21.7540    28.9440     2.9170 0 CHG=0 CFG=0
M  V30 2943 H     -21.9077    28.2774     3.7666 0 CHG=0 CFG=0
M  V30 2944 H     -22.3282    28.5389     2.0819 0 CHG=0 CFG=0
M  V30 2945 C     -22.2420    30.3390     3.2520 0 CHG=0 CFG=0
M  V30 2946 H     -21.8010    31.0661     2.5657 0 CHG=0 CFG=0
M  V30 2947 H     -21.8917    30.6178     4.2475 0 CHG=0 CFG=0
M  V30 2948 C     -23.7620    30.4500     3.1630 0 CHG=0 CFG=0
M  V30 2949 H     -24.0553    30.5183     2.1124 0 CHG=0 CFG=0
M  V30 2950 H     -24.0982    31.3758     3.6362 0 CHG=0 CFG=0
M  V30 2951 N     -24.5200    29.3110     3.7610 0 CHG=1 CFG=0
M  V30 2952 H     -24.2937    29.2368     4.7739 0 CHG=0 CFG=0
M  V30 2953 H     -24.2574    28.4264     3.2817 0 CHG=0 CFG=0
M  V30 2954 H     -25.5431    29.4758     3.6523 0 CHG=0 CFG=0
M  V30 2955 C     -20.2940    26.8540     1.1040 0 CHG=0 CFG=0
M  V30 2956 O     -20.4830    27.4790     0.0630 0 CHG=0 CFG=0
M  V30 2957 N     -20.5640    25.5560     1.2380 0 CHG=0 CFG=0
M  V30 2958 H     -20.3111    25.1268     2.1031 0 CHG=0 CFG=0
M  V30 2959 C     -21.1920    24.7760     0.1750 0 CHG=0 CFG=1
M  V30 2960 H     -20.9206    25.2350    -0.7801 0 CHG=0 CFG=0
M  V30 2961 C     -20.6930    23.3290     0.1860 0 CHG=0 CFG=0
M  V30 2962 H     -21.2577    22.7369    -0.5368 0 CHG=0 CFG=0
M  V30 2963 H     -20.8770    22.8776     1.1612 0 CHG=0 CFG=0
M  V30 2964 C     -19.2370    23.2040    -0.1470 0 CHG=0 CFG=0
M  V30 2965 C     -18.2740    23.3490     0.8450 0 CHG=0 CFG=0
M  V30 2966 H     -18.5625    23.5429     1.8687 0 CHG=0 CFG=0
M  V30 2967 C     -18.8290    22.9810    -1.4610 0 CHG=0 CFG=0
M  V30 2968 H     -19.5544    22.8911    -2.2577 0 CHG=0 CFG=0
M  V30 2969 C     -16.9170    23.2560     0.5470 0 CHG=0 CFG=0
M  V30 2970 H     -16.1741    23.3620     1.3252 0 CHG=0 CFG=0
M  V30 2971 C     -17.4710    22.8840    -1.7670 0 CHG=0 CFG=0
M  V30 2972 H     -17.1534    22.7045    -2.7858 0 CHG=0 CFG=0
M  V30 2973 C     -16.5180    23.0250    -0.7640 0 CHG=0 CFG=0
M  V30 2974 H     -15.4663    22.9390    -0.9900 0 CHG=0 CFG=0
M  V30 2975 C     -22.7020    24.8220     0.3170 0 CHG=0 CFG=0
M  V30 2976 O     -23.2190    24.8630     1.4290 0 CHG=0 CFG=0
M  V30 2977 N     -23.3920    24.8100    -0.8220 0 CHG=0 CFG=0
M  V30 2978 H     -22.9083    24.7625    -1.7039 0 CHG=0 CFG=0
M  V30 2979 C     -24.8580    24.9140    -0.8750 0 CHG=0 CFG=1
M  V30 2980 H     -25.2595    24.1850    -0.1690 0 CHG=0 CFG=0
M  V30 2981 C     -25.3210    26.3370    -0.5470 0 CHG=0 CFG=0
M  V30 2982 H     -24.9007    26.6881     0.4007 0 CHG=0 CFG=0
M  V30 2983 H     -26.4055    26.3553    -0.4160 0 CHG=0 CFG=0
M  V30 2984 O     -25.0180    27.2310    -1.5980 0 CHG=0 CFG=0
M  V30 2985 H     -24.0683    27.3123    -1.7028 0 CHG=0 CFG=0
M  V30 2986 C     -25.3370    24.5750    -2.2760 0 CHG=0 CFG=0
M  V30 2987 O     -24.5260    24.4110    -3.1930 0 CHG=0 CFG=0
M  V30 2988 N     -26.6590    24.5270    -2.4540 0 CHG=0 CFG=0
M  V30 2989 H     -27.3014    24.6854    -1.7087 0 CHG=0 CFG=0
M  V30 2990 C     -27.2210    24.4150    -3.7980 0 CHG=0 CFG=1
M  V30 2991 H     -26.9763    23.4188    -4.1701 0 CHG=0 CFG=0
M  V30 2992 C     -28.7390    24.6290    -3.7890 0 CHG=0 CFG=0
M  V30 2993 H     -29.2294    23.8792    -3.1585 0 CHG=0 CFG=0
M  V30 2994 H     -29.0675    24.4527    -4.8133 0 CHG=0 CFG=0
M  V30 2995 O     -29.0770    25.9510    -3.3920 0 CHG=0 CFG=0
M  V30 2996 H     -30.0256    26.0632    -3.4516 0 CHG=0 CFG=0
M  V30 2997 C     -26.5750    25.4460    -4.7150 0 CHG=0 CFG=0
M  V30 2998 O     -26.3320    25.1780    -5.8950 0 CHG=0 CFG=0
M  V30 2999 N     -26.2880    26.6180    -4.1570 0 CHG=0 CFG=0
M  V30 3000 H     -26.4833    26.7520    -3.1859 0 CHG=0 CFG=0
M  V30 3001 C     -25.8030    27.7400    -4.9510 0 CHG=0 CFG=1
M  V30 3002 H     -26.3751    27.7237    -5.8785 0 CHG=0 CFG=0
M  V30 3003 C     -26.0590    29.0730    -4.2410 0 CHG=0 CFG=0
M  V30 3004 H     -25.6987    29.8900    -4.8665 0 CHG=0 CFG=0
M  V30 3005 H     -25.4731    29.1159    -3.3228 0 CHG=0 CFG=0
M  V30 3006 C     -27.5360    29.3370    -3.9140 0 CHG=0 CFG=0
M  V30 3007 H     -27.6330    30.3443    -3.5084 0 CHG=0 CFG=0
M  V30 3008 H     -27.8609    28.6618    -3.1210 0 CHG=0 CFG=0
M  V30 3009 C     -28.4500    29.1630    -5.1300 0 CHG=0 CFG=0
M  V30 3010 H     -28.4933    28.1098    -5.4127 0 CHG=0 CFG=0
M  V30 3011 H     -28.0500    29.7033    -5.9863 0 CHG=0 CFG=0
M  V30 3012 C     -29.8580    29.6620    -4.8050 0 CHG=0 CFG=0
M  V30 3013 H     -29.8496    30.7338    -4.5855 0 CHG=0 CFG=0
M  V30 3014 H     -30.2415    29.1469    -3.9223 0 CHG=0 CFG=0
M  V30 3015 N     -30.8130    29.4250    -5.9280 0 CHG=1 CFG=0
M  V30 3016 H     -30.6683    28.4860    -6.3532 0 CHG=0 CFG=0
M  V30 3017 H     -30.5930    30.1438    -6.6613 0 CHG=0 CFG=0
M  V30 3018 H     -31.7944    29.5641    -5.6227 0 CHG=0 CFG=0
M  V30 3019 C     -24.3370    27.6080    -5.3700 0 CHG=0 CFG=0
M  V30 3020 O     -23.9090    28.2940    -6.3040 0 CHG=0 CFG=0
M  V30 3021 N     -23.5710    26.7320    -4.7120 0 CHG=0 CFG=0
M  V30 3022 H     -23.9498    26.1673    -3.9782 0 CHG=0 CFG=0
M  V30 3023 C     -22.2230    26.4340    -5.2050 0 CHG=0 CFG=1
M  V30 3024 H     -21.8333    27.3538    -5.6369 0 CHG=0 CFG=0
M  V30 3025 C     -21.2480    25.9820    -4.1060 0 CHG=0 CFG=0
M  V30 3026 H     -21.0441    26.8155    -3.4298 0 CHG=0 CFG=0
M  V30 3027 H     -20.2789    25.6986    -4.5335 0 CHG=0 CFG=0
M  V30 3028 O     -21.7610    24.9260    -3.3240 0 CHG=0 CFG=0
M  V30 3029 H     -22.0843    24.2310    -3.8999 0 CHG=0 CFG=0
M  V30 3030 C     -22.2830    25.4520    -6.3800 0 CHG=0 CFG=0
M  V30 3031 O     -21.4620    25.5350    -7.2950 0 CHG=0 CFG=0
M  V30 3032 N     -23.2740    24.5560    -6.3650 0 CHG=0 CFG=0
M  V30 3033 H     -23.9108    24.4896    -5.5968 0 CHG=0 CFG=0
M  V30 3034 C     -23.5520    23.7220    -7.5370 0 CHG=0 CFG=1
M  V30 3035 H     -22.6136    23.2486    -7.8330 0 CHG=0 CFG=0
M  V30 3036 C     -24.6450    22.6740    -7.2600 0 CHG=0 CFG=0
M  V30 3037 H     -25.1271    22.3772    -8.1927 0 CHG=0 CFG=0
M  V30 3038 H     -25.4323    23.0750    -6.6243 0 CHG=0 CFG=0
M  V30 3039 C     -24.1110    21.3820    -6.6380 0 CHG=0 CFG=0
M  V30 3040 O     -22.8980    21.2430    -6.3510 0 CHG=0 CFG=0
M  V30 3041 O     -24.9470    20.4730    -6.4490 0 CHG=-1 CFG=0
M  V30 3042 C     -23.9930    24.6070    -8.7000 0 CHG=0 CFG=0
M  V30 3043 O     -23.6190    24.3690    -9.8410 0 CHG=0 CFG=0
M  V30 3044 N     -24.8030    25.6240    -8.4070 0 CHG=0 CFG=0
M  V30 3045 H     -25.1957    25.6261    -7.4864 0 CHG=0 CFG=0
M  V30 3046 C     -25.2860    26.5240    -9.4540 0 CHG=0 CFG=1
M  V30 3047 H     -25.7529    25.8950   -10.2130 0 CHG=0 CFG=0
M  V30 3048 C     -26.3100    27.5580    -8.9050 0 CHG=0 CFG=1
M  V30 3049 H     -25.8774    28.0317    -8.0248 0 CHG=0 CFG=0
M  V30 3050 C     -26.5730    28.6610    -9.9280 0 CHG=0 CFG=0
M  V30 3051 H     -26.7657    28.2450   -10.9171 0 CHG=0 CFG=0
M  V30 3052 H     -25.7325    29.3508   -10.0128 0 CHG=0 CFG=0
M  V30 3053 H     -27.4511    29.2447    -9.6531 0 CHG=0 CFG=0
M  V30 3054 C     -27.6230    26.8710    -8.4820 0 CHG=0 CFG=0
M  V30 3055 H     -28.2038    27.5578    -7.8671 0 CHG=0 CFG=0
M  V30 3056 H     -27.4069    26.0161    -7.8441 0 CHG=0 CFG=0
M  V30 3057 C     -28.5030    26.3960    -9.6280 0 CHG=0 CFG=0
M  V30 3058 H     -27.9561    25.7721   -10.3291 0 CHG=0 CFG=0
M  V30 3059 H     -28.9129    27.2336   -10.1913 0 CHG=0 CFG=0
M  V30 3060 H     -29.3414    25.8101    -9.2512 0 CHG=0 CFG=0
M  V30 3061 C     -24.1090    27.2270   -10.1180 0 CHG=0 CFG=0
M  V30 3062 O     -24.0010    27.2650   -11.3520 0 CHG=0 CFG=0
M  V30 3063 N     -23.2020    27.7390    -9.2960 0 CHG=0 CFG=0
M  V30 3064 H     -23.3641    27.6482    -8.3131 0 CHG=0 CFG=0
M  V30 3065 C     -22.0080    28.4010    -9.8080 0 CHG=0 CFG=1
M  V30 3066 H     -22.3465    29.2591   -10.3887 0 CHG=0 CFG=0
M  V30 3067 C     -21.1200    28.8560    -8.6530 0 CHG=0 CFG=0
M  V30 3068 H     -20.8184    28.0033    -8.0431 0 CHG=0 CFG=0
M  V30 3069 H     -21.6875    29.5152    -7.9960 0 CHG=0 CFG=0
M  V30 3070 C     -19.8840    29.5560    -9.1260 0 CHG=0 CFG=0
M  V30 3071 C     -19.5990    30.9580    -9.0470 0 CHG=0 CFG=0
M  V30 3072 C     -18.3230    31.1580    -9.6180 0 CHG=0 CFG=0
M  V30 3073 C     -20.2950    32.0640    -8.5450 0 CHG=0 CFG=0
M  V30 3074 H     -21.2758    31.9328    -8.1185 0 CHG=0 CFG=0
M  V30 3075 C     -18.7960    28.9770    -9.7180 0 CHG=0 CFG=0
M  V30 3076 H     -18.6752    27.9213    -9.9162 0 CHG=0 CFG=0
M  V30 3077 N     -17.8530    29.9370   -10.0170 0 CHG=0 CFG=0
M  V30 3078 H     -16.9819    29.7715   -10.4345 0 CHG=0 CFG=0
M  V30 3079 C     -17.7260    32.4230    -9.6980 0 CHG=0 CFG=0
M  V30 3080 H     -16.7425    32.5527   -10.1274 0 CHG=0 CFG=0
M  V30 3081 C     -19.7060    33.3260    -8.6410 0 CHG=0 CFG=0
M  V30 3082 H     -20.2350    34.1918    -8.2679 0 CHG=0 CFG=0
M  V30 3083 C     -18.4350    33.4880    -9.2090 0 CHG=0 CFG=0
M  V30 3084 H     -17.9895    34.4669    -9.2566 0 CHG=0 CFG=0
M  V30 3085 C     -21.2330    27.4600   -10.7400 0 CHG=0 CFG=0
M  V30 3086 O     -20.8950    27.8260   -11.8830 0 CHG=0 CFG=0
M  V30 3087 N     -20.9760    26.2480   -10.2510 0 CHG=0 CFG=0
M  V30 3088 H     -21.2799    26.0232    -9.3218 0 CHG=0 CFG=0
M  V30 3089 C     -20.2260    25.2420   -11.0100 0 CHG=0 CFG=1
M  V30 3090 H     -19.2464    25.6774   -11.2150 0 CHG=0 CFG=0
M  V30 3091 C     -20.0640    23.9700   -10.2100 0 CHG=0 CFG=0
M  V30 3092 H     -21.0306    23.5278    -9.9646 0 CHG=0 CFG=0
M  V30 3093 H     -19.5454    24.1722    -9.2719 0 CHG=0 CFG=0
M  V30 3094 H     -19.4777    23.2333   -10.7569 0 CHG=0 CFG=0
M  V30 3095 C     -20.9070    24.9510   -12.3320 0 CHG=0 CFG=0
M  V30 3096 O     -20.2440    24.8100   -13.3570 0 CHG=0 CFG=0
M  V30 3097 N     -22.2370    24.8770   -12.3150 0 CHG=0 CFG=0
M  V30 3098 H     -22.7205    24.9898   -11.4450 0 CHG=0 CFG=0
M  V30 3099 C     -22.9810    24.6500   -13.5550 0 CHG=0 CFG=1
M  V30 3100 H     -22.6139    23.7076   -13.9634 0 CHG=0 CFG=0
M  V30 3101 C     -24.4820    24.5390   -13.2890 0 CHG=0 CFG=0
M  V30 3102 H     -24.8380    25.4132   -12.7436 0 CHG=0 CFG=0
M  V30 3103 H     -24.6625    23.6856   -12.6360 0 CHG=0 CFG=0
M  V30 3104 C     -25.2900    24.3810   -14.5380 0 CHG=0 CFG=0
M  V30 3105 C     -25.3100    23.1630   -15.2150 0 CHG=0 CFG=0
M  V30 3106 H     -24.7555    22.3232   -14.8297 0 CHG=0 CFG=0
M  V30 3107 C     -26.0110    25.4540   -15.0590 0 CHG=0 CFG=0
M  V30 3108 H     -26.0015    26.4089   -14.5513 0 CHG=0 CFG=0
M  V30 3109 C     -26.0320    23.0140   -16.3850 0 CHG=0 CFG=0
M  V30 3110 H     -26.0477    22.0696   -16.9086 0 CHG=0 CFG=0
M  V30 3111 C     -26.7430    25.3160   -16.2320 0 CHG=0 CFG=0
M  V30 3112 H     -27.3043    26.1545   -16.6191 0 CHG=0 CFG=0
M  V30 3113 C     -26.7580    24.0960   -16.8930 0 CHG=0 CFG=0
M  V30 3114 H     -27.3270    23.9794   -17.8036 0 CHG=0 CFG=0
M  V30 3115 C     -22.7220    25.7390   -14.6010 0 CHG=0 CFG=0
M  V30 3116 O     -22.5860    25.4500   -15.8030 0 CHG=0 CFG=0
M  V30 3117 N     -22.6730    26.9960   -14.1540 0 CHG=0 CFG=0
M  V30 3118 H     -22.8576    27.1622   -13.1809 0 CHG=0 CFG=0
M  V30 3119 C     -22.3820    28.1040   -15.0710 0 CHG=0 CFG=0
M  V30 3120 H     -22.4099    29.0244   -14.4932 0 CHG=0 CFG=0
M  V30 3121 H     -23.1556    28.1296   -15.8402 0 CHG=0 CFG=0
M  V30 3122 C     -21.0050    27.9340   -15.6950 0 CHG=0 CFG=0
M  V30 3123 O     -20.8210    28.1280   -16.9160 0 CHG=0 CFG=0
M  V30 3124 N     -20.0310    27.5460   -14.8740 0 CHG=0 CFG=0
M  V30 3125 H     -20.2586    27.3756   -13.9119 0 CHG=0 CFG=0
M  V30 3126 C     -18.6820    27.2660   -15.3920 0 CHG=0 CFG=1
M  V30 3127 H     -18.3781    28.1570   -15.9433 0 CHG=0 CFG=0
M  V30 3128 C     -17.6520    27.0070   -14.2570 0 CHG=0 CFG=0
M  V30 3129 H     -17.9661    26.1268   -13.6955 0 CHG=0 CFG=0
M  V30 3130 C     -16.2530    26.7460   -14.8240 0 CHG=0 CFG=0
M  V30 3131 H     -15.9080    27.5860   -15.4276 0 CHG=0 CFG=0
M  V30 3132 H     -16.2244    25.8531   -15.4473 0 CHG=0 CFG=0
M  V30 3133 H     -15.5295    26.5995   -14.0211 0 CHG=0 CFG=0
M  V30 3134 C     -17.6190    28.1920   -13.2880 0 CHG=0 CFG=0
M  V30 3135 H     -18.5712    28.3184   -12.7729 0 CHG=0 CFG=0
M  V30 3136 H     -17.3982    29.1245   -13.8086 0 CHG=0 CFG=0
M  V30 3137 H     -16.8561    28.0581   -12.5220 0 CHG=0 CFG=0
M  V30 3138 C     -18.7240    26.1050   -16.4010 0 CHG=0 CFG=0
M  V30 3139 O     -18.0830    26.1650   -17.4480 0 CHG=0 CFG=0
M  V30 3140 N     -19.5240    25.0810   -16.1100 0 CHG=0 CFG=0
M  V30 3141 H     -20.0274    25.1080   -15.2455 0 CHG=0 CFG=0
M  V30 3142 C     -19.6830    23.9580   -17.0290 0 CHG=0 CFG=1
M  V30 3143 H     -18.6830    23.5855   -17.2309 0 CHG=0 CFG=0
M  V30 3144 C     -20.5070    22.8490   -16.3680 0 CHG=0 CFG=0
M  V30 3145 H     -21.4028    23.2997   -15.9406 0 CHG=0 CFG=0
M  V30 3146 H     -19.9336    22.4967   -15.5090 0 CHG=0 CFG=0
M  V30 3147 C     -20.9610    21.6400   -17.1940 0 CHG=0 CFG=0
M  V30 3148 H     -21.7540    21.9573   -17.8744 0 CHG=0 CFG=0
M  V30 3149 C     -19.8370    21.0410   -18.0190 0 CHG=0 CFG=0
M  V30 3150 H     -18.9871    20.8053   -17.3879 0 CHG=0 CFG=0
M  V30 3151 H     -19.4895    21.7159   -18.7977 0 CHG=0 CFG=0
M  V30 3152 H     -20.1614    20.1262   -18.5144 0 CHG=0 CFG=0
M  V30 3153 C     -21.5200    20.5990   -16.2540 0 CHG=0 CFG=0
M  V30 3154 H     -22.2782    21.0342   -15.6035 0 CHG=0 CFG=0
M  V30 3155 H     -20.7426    20.1851   -15.6107 0 CHG=0 CFG=0
M  V30 3156 H     -21.9601    19.7685   -16.8056 0 CHG=0 CFG=0
M  V30 3157 C     -20.2860    24.4110   -18.3800 0 CHG=0 CFG=0
M  V30 3158 O     -19.8300    23.9850   -19.4380 0 CHG=0 CFG=0
M  V30 3159 N     -21.3020    25.2720   -18.3550 0 CHG=0 CFG=0
M  V30 3160 H     -21.6996    25.5312   -17.4727 0 CHG=0 CFG=0
M  V30 3161 C     -21.8350    25.8460   -19.6180 0 CHG=0 CFG=1
M  V30 3162 H     -22.2313    25.0219   -20.2143 0 CHG=0 CFG=0
M  V30 3163 C     -22.9130    26.9110   -19.3280 0 CHG=0 CFG=0
M  V30 3164 H     -23.1795    27.4012   -20.2648 0 CHG=0 CFG=0
M  V30 3165 H     -22.5293    27.6946   -18.6740 0 CHG=0 CFG=0
M  V30 3166 C     -24.1880    26.3160   -18.7150 0 CHG=0 CFG=0
M  V30 3167 H     -24.0184    25.9977   -17.6874 0 CHG=0 CFG=0
M  V30 3168 H     -24.4627    25.4223   -19.2763 0 CHG=0 CFG=0
M  V30 3169 S     -25.5880    27.4190   -18.7590 0 CHG=0 CFG=0
M  V30 3170 C     -25.7840    27.7710   -20.5170 0 CHG=0 CFG=0
M  V30 3171 H     -25.4400    26.9278   -21.1165 0 CHG=0 CFG=0
M  V30 3172 H     -25.2302    28.6685   -20.7938 0 CHG=0 CFG=0
M  V30 3173 H     -26.8392    27.9252   -20.7443 0 CHG=0 CFG=0
M  V30 3174 C     -20.7260    26.5280   -20.3840 0 CHG=0 CFG=0
M  V30 3175 O     -20.6170    26.3860   -21.6250 0 CHG=0 CFG=0
M  V30 3176 N     -19.9000    27.2710   -19.6450 0 CHG=0 CFG=0
M  V30 3177 H     -20.1018    27.3649   -18.6666 0 CHG=0 CFG=0
M  V30 3178 C     -18.7700    27.9730   -20.2510 0 CHG=0 CFG=1
M  V30 3179 H     -19.1870    28.5869   -21.0515 0 CHG=0 CFG=0
M  V30 3180 C     -18.0800    28.8830   -19.2220 0 CHG=0 CFG=0
M  V30 3181 H     -17.6795    28.2980   -18.3962 0 CHG=0 CFG=0
M  V30 3182 H     -18.8166    29.5543   -18.7796 0 CHG=0 CFG=0
M  V30 3183 C     -16.9640    29.7120   -19.7950 0 CHG=0 CFG=0
M  V30 3184 C     -15.6120    29.2890   -20.0240 0 CHG=0 CFG=0
M  V30 3185 C     -14.9170    30.3920   -20.5780 0 CHG=0 CFG=0
M  V30 3186 C     -14.9260    28.0790   -19.8370 0 CHG=0 CFG=0
M  V30 3187 H     -15.4230    27.2230   -19.4101 0 CHG=0 CFG=0
M  V30 3188 C     -17.0290    31.0200   -20.1940 0 CHG=0 CFG=0
M  V30 3189 H     -17.9143    31.6381   -20.1503 0 CHG=0 CFG=0
M  V30 3190 N     -15.8030    31.4360   -20.6650 0 CHG=0 CFG=0
M  V30 3191 H     -15.6366    32.3379   -21.0236 0 CHG=0 CFG=0
M  V30 3192 C     -13.5670    30.3250   -20.9310 0 CHG=0 CFG=0
M  V30 3193 H     -13.0594    31.1821   -21.3475 0 CHG=0 CFG=0
M  V30 3194 C     -13.5760    28.0170   -20.1880 0 CHG=0 CFG=0
M  V30 3195 H     -13.0340    27.0974   -20.0345 0 CHG=0 CFG=0
M  V30 3196 C     -12.9160    29.1350   -20.7280 0 CHG=0 CFG=0
M  V30 3197 H     -11.8642    29.0498   -20.9566 0 CHG=0 CFG=0
M  V30 3198 C     -17.7930    26.9650   -20.8870 0 CHG=0 CFG=0
M  V30 3199 O     -17.3130    27.1960   -21.9980 0 CHG=0 CFG=0
M  V30 3200 N     -17.5240    25.8420   -20.2100 0 CHG=0 CFG=0
M  V30 3201 H     -17.9585    25.7438   -19.3128 0 CHG=0 CFG=0
M  V30 3202 C     -16.6310    24.8070   -20.7690 0 CHG=0 CFG=1
M  V30 3203 H     -15.6864    25.2973   -21.0106 0 CHG=0 CFG=0
M  V30 3204 C     -16.4000    23.6310   -19.8080 0 CHG=0 CFG=0
M  V30 3205 H     -15.7907    22.8795   -20.3164 0 CHG=0 CFG=0
M  V30 3206 H     -17.3574    23.1457   -19.6040 0 CHG=0 CFG=0
M  V30 3207 C     -15.7460    23.9680   -18.4790 0 CHG=0 CFG=0
M  V30 3208 H     -16.3654    24.6547   -17.9090 0 CHG=0 CFG=0
M  V30 3209 H     -14.7853    24.4613   -18.6293 0 CHG=0 CFG=0
M  V30 3210 C     -15.5450    22.7250   -17.6370 0 CHG=0 CFG=0
M  V30 3211 O     -16.4381    22.4004   -16.8193 0 CHG=0 CFG=0
M  V30 3212 O     -14.4915    22.0762   -17.7854 0 CHG=0 CFG=0
M  V30 3213 H     -13.9521    22.4472   -18.4676 0 CHG=0 CFG=0
M  V30 3214 C     -17.2250    24.2460   -22.0490 0 CHG=0 CFG=0
M  V30 3215 O     -16.5140    24.0240   -23.0360 0 CHG=0 CFG=0
M  V30 3216 N     -18.5320    23.9920   -22.0170 0 CHG=0 CFG=0
M  V30 3217 H     -19.0613    24.1845   -21.1879 0 CHG=0 CFG=0
M  V30 3218 C     -19.2170    23.4460   -23.1840 0 CHG=0 CFG=1
M  V30 3219 H     -18.6690    22.5467   -23.4673 0 CHG=0 CFG=0
M  V30 3220 C     -20.6840    23.0580   -22.8560 0 CHG=0 CFG=1
M  V30 3221 H     -21.1550    23.8925   -22.3335 0 CHG=0 CFG=0
M  V30 3222 C     -21.4770    22.7850   -24.1240 0 CHG=0 CFG=0
M  V30 3223 H     -21.0211    22.0000   -24.7274 0 CHG=0 CFG=0
M  V30 3224 H     -21.5634    23.6800   -24.7353 0 CHG=0 CFG=0
M  V30 3225 H     -22.4974    22.4737   -23.9007 0 CHG=0 CFG=0
M  V30 3226 C     -20.6890    21.8280   -21.9390 0 CHG=0 CFG=0
M  V30 3227 H     -19.9616    21.9599   -21.1380 0 CHG=0 CFG=0
M  V30 3228 H     -20.3666    20.9527   -22.5034 0 CHG=0 CFG=0
M  V30 3229 C     -22.0210    21.5270   -21.3010 0 CHG=0 CFG=0
M  V30 3230 H     -22.7846    21.2912   -22.0418 0 CHG=0 CFG=0
M  V30 3231 H     -22.3749    22.3774   -20.7174 0 CHG=0 CFG=0
M  V30 3232 H     -21.9471    20.6738   -20.6265 0 CHG=0 CFG=0
M  V30 3233 C     -19.1090    24.4000   -24.3740 0 CHG=0 CFG=0
M  V30 3234 O     -18.6680    24.0000   -25.4510 0 CHG=0 CFG=0
M  V30 3235 N     -19.4800    25.6660   -24.1710 0 CHG=0 CFG=0
M  V30 3236 H     -19.8327    25.9168   -23.2690 0 CHG=0 CFG=0
M  V30 3237 C     -19.4500    26.6260   -25.2710 0 CHG=0 CFG=1
M  V30 3238 H     -19.8773    26.1115   -26.1343 0 CHG=0 CFG=0
M  V30 3239 C     -20.3270    27.8400   -24.9540 0 CHG=0 CFG=0
M  V30 3240 H     -20.0278    28.6979   -25.5567 0 CHG=0 CFG=0
M  V30 3241 H     -20.2191    28.1385   -23.9102 0 CHG=0 CFG=0
M  V30 3242 C     -21.7690    27.5420   -25.2730 0 CHG=0 CFG=0
M  V30 3243 C     -22.6170    26.9750   -24.3120 0 CHG=0 CFG=0
M  V30 3244 H     -22.2525    26.7592   -23.3193 0 CHG=0 CFG=0
M  V30 3245 C     -23.9490    26.6820   -24.6170 0 CHG=0 CFG=0
M  V30 3246 H     -24.6030    26.2520   -23.8719 0 CHG=0 CFG=0
M  V30 3247 C     -22.2820    27.7860   -26.5510 0 CHG=0 CFG=0
M  V30 3248 H     -21.6403    28.1972   -27.3148 0 CHG=0 CFG=0
M  V30 3249 C     -23.6080    27.4970   -26.8690 0 CHG=0 CFG=0
M  V30 3250 H     -23.9224    27.7192   -27.8791 0 CHG=0 CFG=0
M  V30 3251 C     -24.4320    26.9380   -25.9050 0 CHG=0 CFG=0
M  V30 3252 O     -25.7410    26.6700   -26.2100 0 CHG=0 CFG=0
M  V30 3253 H     -25.9950    27.0036   -27.0586 0 CHG=0 CFG=0
M  V30 3254 C     -18.0410    27.0080   -25.7020 0 CHG=0 CFG=0
M  V30 3255 O     -17.8500    27.5330   -26.8050 0 CHG=0 CFG=0
M  V30 3256 N     -17.0640    26.7030   -24.8470 0 CHG=0 CFG=0
M  V30 3257 H     -17.3105    26.3541   -23.9428 0 CHG=0 CFG=0
M  V30 3258 C     -15.6500    26.9380   -25.1450 0 CHG=0 CFG=1
M  V30 3259 H     -15.5971    27.7234   -25.9010 0 CHG=0 CFG=0
M  V30 3260 C     -14.9150    27.4190   -23.8870 0 CHG=0 CFG=0
M  V30 3261 H     -13.8824    27.6540   -24.1371 0 CHG=0 CFG=0
M  V30 3262 H     -14.8734    26.6409   -23.1124 0 CHG=0 CFG=0
M  V30 3263 O     -15.5080    28.6150   -23.4000 0 CHG=0 CFG=0
M  V30 3264 H     -16.3200    28.3980   -22.9378 0 CHG=0 CFG=0
M  V30 3265 C     -14.9680    25.6950   -25.7270 0 CHG=0 CFG=0
M  V30 3266 O     -13.7440    25.6790   -25.9230 0 CHG=0 CFG=0
M  V30 3267 N     -15.7620    24.6550   -26.0060 0 CHG=0 CFG=0
M  V30 3268 H     -16.7524    24.7011   -25.8606 0 CHG=0 CFG=0
M  V30 3269 C     -15.2380    23.3840   -26.5400 0 CHG=0 CFG=1
M  V30 3270 H     -16.0675    22.6817   -26.4658 0 CHG=0 CFG=0
M  V30 3271 C     -14.8230    23.5230   -28.0190 0 CHG=0 CFG=0
M  V30 3272 H     -14.4984    22.5417   -28.3732 0 CHG=0 CFG=0
M  V30 3273 H     -13.9350    24.1536   -28.0769 0 CHG=0 CFG=0
M  V30 3274 C     -15.8710    24.0620   -28.9950 0 CHG=0 CFG=0
M  V30 3275 H     -16.1460    25.0714   -28.6874 0 CHG=0 CFG=0
M  V30 3276 C     -15.3130    24.1450   -30.4140 0 CHG=0 CFG=0
M  V30 3277 H     -15.0118    23.1603   -30.7736 0 CHG=0 CFG=0
M  V30 3278 H     -14.4390    24.7949   -30.4550 0 CHG=0 CFG=0
M  V30 3279 H     -16.0544    24.5393   -31.1087 0 CHG=0 CFG=0
M  V30 3280 C     -17.1280    23.1990   -28.9580 0 CHG=0 CFG=0
M  V30 3281 H     -17.6296    23.2560   -27.9913 0 CHG=0 CFG=0
M  V30 3282 H     -16.8899    22.1522   -29.1485 0 CHG=0 CFG=0
M  V30 3283 H     -17.8502    23.5211   -29.7089 0 CHG=0 CFG=0
M  V30 3284 C     -14.1020    22.8170   -25.6800 0 CHG=0 CFG=0
M  V30 3285 O     -13.0740    22.3290   -26.1880 0 CHG=0 CFG=0
M  V30 3286 N     -14.2750    22.9240   -24.3650 0 CHG=0 CFG=0
M  V30 3287 H     -15.1347    23.3364   -24.0661 0 CHG=0 CFG=0
M  V30 3288 C     -13.3720    22.2650   -23.4210 0 CHG=0 CFG=0
M  V30 3289 H     -13.0690    21.3073   -23.8484 0 CHG=0 CFG=0
M  V30 3290 H     -13.9705    22.0517   -22.5360 0 CHG=0 CFG=0
M  V30 3291 C     -12.1400    23.0480   -23.0000 0 CHG=0 CFG=0
M  V30 3292 O     -11.2060    22.4870   -22.4190 0 CHG=0 CFG=0
M  V30 3293 N     -12.1240    24.3420   -23.2890 0 CHG=0 CFG=0
M  V30 3294 H     -12.8666    24.6902   -23.8607 0 CHG=0 CFG=0
M  V30 3295 C     -11.0720    25.2130   -22.7720 0 CHG=0 CFG=1
M  V30 3296 H     -10.1293    24.8354   -23.1731 0 CHG=0 CFG=0
M  V30 3297 C     -11.3260    26.6450   -23.2440 0 CHG=0 CFG=0
M  V30 3298 H     -12.2267    27.0079   -22.7464 0 CHG=0 CFG=0
M  V30 3299 H     -11.5654    26.6101   -24.3051 0 CHG=0 CFG=0
M  V30 3300 C     -10.1940    27.6320   -23.0100 0 CHG=0 CFG=0
M  V30 3301 H      -9.2914    27.3588   -23.5607 0 CHG=0 CFG=0
M  V30 3302 H      -9.9098    27.6127   -21.9571 0 CHG=0 CFG=0
M  V30 3303 C     -10.6490    29.0580   -23.3400 0 CHG=0 CFG=0
M  V30 3304 H     -10.1183    29.7485   -22.6808 0 CHG=0 CFG=0
M  V30 3305 H     -11.7100    29.2001   -23.1400 0 CHG=0 CFG=0
M  V30 3306 C     -10.3490    29.4660   -24.7780 0 CHG=0 CFG=0
M  V30 3307 H      -9.2664    29.4391   -24.9384 0 CHG=0 CFG=0
M  V30 3308 H     -10.6696    30.4944   -24.9537 0 CHG=0 CFG=0
M  V30 3309 N     -10.9910    28.5880   -25.8030 0 CHG=1 CFG=0
M  V30 3310 H     -12.0256    28.5878   -25.6990 0 CHG=0 CFG=0
M  V30 3311 H     -10.6370    27.6161   -25.6792 0 CHG=0 CFG=0
M  V30 3312 H     -10.7370    28.9037   -26.7607 0 CHG=0 CFG=0
M  V30 3313 C     -11.0530    25.1430   -21.2390 0 CHG=0 CFG=0
M  V30 3314 O     -12.0940    24.9680   -20.6030 0 CHG=0 CFG=0
M  V30 3315 N      -9.8660    25.2600   -20.6520 0 CHG=0 CFG=0
M  V30 3316 H      -9.0787    25.4990   -21.2233 0 CHG=0 CFG=0
M  V30 3317 C      -9.7380    25.3660   -19.2040 0 CHG=0 CFG=1
M  V30 3318 H     -10.3253    24.5590   -18.7705 0 CHG=0 CFG=0
M  V30 3319 C      -8.2720    25.2080   -18.7970 0 CHG=0 CFG=0
M  V30 3320 H      -7.6793    25.8994   -19.3995 0 CHG=0 CFG=0
M  V30 3321 H      -7.9067    24.2119   -19.0441 0 CHG=0 CFG=0
M  V30 3322 C      -8.0020    25.5320   -17.3370 0 CHG=0 CFG=0
M  V30 3323 H      -8.4648    26.4503   -16.9875 0 CHG=0 CFG=0
M  V30 3324 H      -6.9333    25.7000   -17.1965 0 CHG=0 CFG=0
M  V30 3325 S      -8.4920    24.1560   -16.2970 0 CHG=0 CFG=0
M  V30 3326 C      -7.0010    23.1630   -16.3380 0 CHG=0 CFG=0
M  V30 3327 H      -6.1388    23.7706   -16.0616 0 CHG=0 CFG=0
M  V30 3328 H      -6.8240    22.7854   -17.3449 0 CHG=0 CFG=0
M  V30 3329 H      -7.0750    22.3285   -15.6408 0 CHG=0 CFG=0
M  V30 3330 C     -10.2590    26.7570   -18.7550 0 CHG=0 CFG=0
M  V30 3331 O      -9.8430    27.7670   -19.3130 0 CHG=0 CFG=0
M  V30 3332 N     -11.1850    26.7950   -17.7710 0 CHG=0 CFG=0
M  V30 3333 C     -11.8760    25.6790   -17.0900 0 CHG=0 CFG=0
M  V30 3334 H     -11.2303    25.2627   -16.3159 0 CHG=0 CFG=0
M  V30 3335 H     -12.1686    24.8916   -17.7854 0 CHG=0 CFG=0
M  V30 3336 C     -11.6310    28.0930   -17.2670 0 CHG=0 CFG=1
M  V30 3337 H     -12.1419    28.6528   -18.0472 0 CHG=0 CFG=0
M  V30 3338 C     -12.5880    27.7110   -16.1320 0 CHG=0 CFG=0
M  V30 3339 H     -13.3910    28.4366   -15.9979 0 CHG=0 CFG=0
M  V30 3340 H     -12.0531    27.6368   -15.1921 0 CHG=0 CFG=0
M  V30 3341 C     -13.0940    26.3460   -16.5040 0 CHG=0 CFG=0
M  V30 3342 H     -13.5082    25.8055   -15.6516 0 CHG=0 CFG=0
M  V30 3343 H     -13.8789    26.4370   -17.2566 0 CHG=0 CFG=0
M  V30 3344 C     -10.4530    28.9010   -16.7230 0 CHG=0 CFG=0
M  V30 3345 O      -9.5650    28.3380   -16.0630 0 CHG=0 CFG=0
M  V30 3346 N     -10.4310    30.2030   -17.0110 0 CHG=0 CFG=0
M  V30 3347 H     -11.1902    30.5820   -17.5387 0 CHG=0 CFG=0
M  V30 3348 C      -9.3410    31.0860   -16.5410 0 CHG=0 CFG=1
M  V30 3349 H      -9.5114    32.0476   -17.0247 0 CHG=0 CFG=0
M  V30 3350 C      -9.3810    31.2540   -15.0020 0 CHG=0 CFG=0
M  V30 3351 H      -8.7358    32.0680   -14.6981 0 CHG=0 CFG=0
M  V30 3352 H      -8.9618    30.3741   -14.5140 0 CHG=0 CFG=0
M  V30 3353 C     -10.7780    31.4650   -14.4280 0 CHG=0 CFG=0
M  V30 3354 C     -11.3500    32.7420   -14.3670 0 CHG=0 CFG=0
M  V30 3355 H     -10.7938    33.6017   -14.7133 0 CHG=0 CFG=0
M  V30 3356 C     -12.6270    32.9350   -13.8500 0 CHG=0 CFG=0
M  V30 3357 H     -13.0491    33.9281   -13.8007 0 CHG=0 CFG=0
M  V30 3358 C     -11.5270    30.3840   -13.9530 0 CHG=0 CFG=0
M  V30 3359 H     -11.0982    29.3955   -13.9803 0 CHG=0 CFG=0
M  V30 3360 C     -12.8100    30.5610   -13.4260 0 CHG=0 CFG=0
M  V30 3361 H     -13.3280    29.6828   -13.0736 0 CHG=0 CFG=0
M  V30 3362 C     -13.3540    31.8360   -13.3770 0 CHG=0 CFG=0
M  V30 3363 O     -14.6230    32.0090   -12.8700 0 CHG=0 CFG=0
M  V30 3364 H     -15.0986    31.1970   -12.7792 0 CHG=0 CFG=0
M  V30 3365 C      -7.9940    30.5220   -17.0200 0 CHG=0 CFG=0
M  V30 3366 O      -7.0340    30.4390   -16.2600 0 CHG=0 CFG=0
M  V30 3367 N      -7.9540    30.1510   -18.3040 0 CHG=0 CFG=0
M  V30 3368 H      -8.7888    30.2398   -18.8428 0 CHG=0 CFG=0
M  V30 3369 C      -6.8620    29.3910   -18.9300 0 CHG=0 CFG=1
M  V30 3370 H      -6.9449    28.3785   -18.5333 0 CHG=0 CFG=0
M  V30 3371 C      -7.0800    29.3810   -20.4500 0 CHG=0 CFG=0
M  V30 3372 H      -6.8820    30.3733   -20.8591 0 CHG=0 CFG=0
M  V30 3373 H      -8.1380    29.1944   -20.6393 0 CHG=0 CFG=0
M  V30 3374 C      -6.2970    28.3460   -21.2300 0 CHG=0 CFG=0
M  V30 3375 H      -6.4855    27.3519   -20.8256 0 CHG=0 CFG=0
M  V30 3376 H      -5.2257    28.5265   -21.1396 0 CHG=0 CFG=0
M  V30 3377 C      -6.6530    28.3390   -22.7140 0 CHG=0 CFG=0
M  V30 3378 O      -7.2020    29.3460   -23.2120 0 CHG=0 CFG=0
M  V30 3379 O      -6.3780    27.3270   -23.3930 0 CHG=-1 CFG=0
M  V30 3380 C      -5.4620    29.9170   -18.6240 0 CHG=0 CFG=0
M  V30 3381 O      -4.5310    29.1360   -18.4040 0 CHG=0 CFG=0
M  V30 3382 N      -5.3310    31.2400   -18.6210 0 CHG=0 CFG=0
M  V30 3383 H      -6.1613    31.7789   -18.7291 0 CHG=0 CFG=0
M  V30 3384 C      -4.0360    31.9100   -18.5030 0 CHG=0 CFG=1
M  V30 3385 H      -3.2862    31.2499   -18.9445 0 CHG=0 CFG=0
M  V30 3386 C      -4.0700    33.2250   -19.2830 0 CHG=0 CFG=0
M  V30 3387 H      -3.1350    33.7620   -19.1080 0 CHG=0 CFG=0
M  V30 3388 H      -4.8612    33.8697   -18.8972 0 CHG=0 CFG=0
M  V30 3389 C      -4.2360    33.0160   -20.7760 0 CHG=0 CFG=0
M  V30 3390 H      -5.2080    32.5663   -20.9848 0 CHG=0 CFG=0
M  V30 3391 H      -3.4929    32.2912   -21.1102 0 CHG=0 CFG=0
M  V30 3392 C      -4.0870    34.3060   -21.5610 0 CHG=0 CFG=0
M  V30 3393 H      -3.1633    34.8351   -21.3182 0 CHG=0 CFG=0
M  V30 3394 H      -4.9114    34.9856   -21.3399 0 CHG=0 CFG=0
M  V30 3395 N      -4.1250    34.0650   -23.0040 0 CHG=0 CFG=0
M  V30 3396 H      -5.0294    34.2131   -23.4113 0 CHG=0 CFG=0
M  V30 3397 C      -3.0860    33.6470   -23.7240 0 CHG=0 CFG=0
M  V30 3398 N      -1.9170    33.4130   -23.1420 0 CHG=1 CFG=0
M  V30 3399 H      -1.8342    33.5572   -22.1528 0 CHG=0 CFG=0
M  V30 3400 H      -1.1095    33.0896   -23.6355 0 CHG=0 CFG=0
M  V30 3401 N      -3.2170    33.4530   -25.0290 0 CHG=0 CFG=0
M  V30 3402 H      -4.0934    33.6154   -25.4834 0 CHG=0 CFG=0
M  V30 3403 H      -2.4532    33.1334   -25.5915 0 CHG=0 CFG=0
M  V30 3404 C      -3.6000    32.1600   -17.0600 0 CHG=0 CFG=0
M  V30 3405 O      -2.4970    32.6790   -16.8230 0 CHG=0 CFG=0
M  V30 3406 N      -4.4620    31.7820   -16.1150 0 CHG=0 CFG=0
M  V30 3407 H      -5.2733    31.2556   -16.3570 0 CHG=0 CFG=0
M  V30 3408 C      -4.2350    32.0160   -14.6900 0 CHG=0 CFG=1
M  V30 3409 H      -3.3568    32.6493   -14.5775 0 CHG=0 CFG=0
M  V30 3410 C      -5.4830    32.6140   -14.0300 0 CHG=0 CFG=0
M  V30 3411 H      -5.3456    32.6466   -12.9499 0 CHG=0 CFG=0
M  V30 3412 H      -6.3518    31.9884   -14.2347 0 CHG=0 CFG=0
M  V30 3413 C      -5.7800    34.0310   -14.4260 0 CHG=0 CFG=0
M  V30 3414 C      -4.7570    34.9290   -14.7170 0 CHG=0 CFG=0
M  V30 3415 H      -3.7132    34.6541   -14.6504 0 CHG=0 CFG=0
M  V30 3416 C      -7.0950    34.4810   -14.4690 0 CHG=0 CFG=0
M  V30 3417 H      -7.9049    33.8332   -14.1897 0 CHG=0 CFG=0
M  V30 3418 C      -5.0430    36.2460   -15.0740 0 CHG=0 CFG=0
M  V30 3419 H      -4.2304    36.9264   -15.2863 0 CHG=0 CFG=0
M  V30 3420 C      -7.3900    35.7990   -14.8220 0 CHG=0 CFG=0
M  V30 3421 H      -8.4170    36.1337   -14.8419 0 CHG=0 CFG=0
M  V30 3422 C      -6.3610    36.6800   -15.1240 0 CHG=0 CFG=0
M  V30 3423 H      -6.5792    37.7058   -15.3834 0 CHG=0 CFG=0
M  V30 3424 C      -3.9140    30.7280   -13.9550 0 CHG=0 CFG=0
M  V30 3425 O      -4.3610    29.6440   -14.3470 0 CHG=0 CFG=0
M  V30 3426 N      -3.1690    30.8650   -12.8620 0 CHG=0 CFG=0
M  V30 3427 H      -2.8042    31.7812   -12.6692 0 CHG=0 CFG=0
M  V30 3428 C      -3.0370    29.8000   -11.8770 0 CHG=0 CFG=1
M  V30 3429 H      -2.9097    28.8622   -12.4195 0 CHG=0 CFG=0
M  V30 3430 C      -1.8350    30.0490   -10.9460 0 CHG=0 CFG=2
M  V30 3431 H      -1.7354    29.2518   -10.2085 0 CHG=0 CFG=0
M  V30 3432 O      -2.0320    31.2720   -10.2220 0 CHG=0 CFG=0
M  V30 3433 H      -1.7960    32.0185   -10.7832 0 CHG=0 CFG=0
M  V30 3434 C      -0.5420    30.1340   -11.7360 0 CHG=0 CFG=0
M  V30 3435 H      -0.5594    30.8833   -12.5312 0 CHG=0 CFG=0
M  V30 3436 H      -0.3171    29.1792   -12.2105 0 CHG=0 CFG=0
M  V30 3437 H       0.2987    30.3742   -11.0834 0 CHG=0 CFG=0
M  V30 3438 C      -4.3080    29.7350   -11.0220 0 CHG=0 CFG=0
M  V30 3439 O      -5.1590    30.6360   -11.0850 0 CHG=0 CFG=0
M  V30 3440 N      -4.4270    28.6810   -10.2160 0 CHG=0 CFG=0
M  V30 3441 H      -3.6736    28.0291   -10.1993 0 CHG=0 CFG=0
M  V30 3442 C      -5.5110    28.5700    -9.2370 0 CHG=0 CFG=1
M  V30 3443 H      -6.4487    28.6562    -9.7904 0 CHG=0 CFG=0
M  V30 3444 C      -5.4330    27.2360    -8.4810 0 CHG=0 CFG=0
M  V30 3445 H      -5.9788    27.3095    -7.5383 0 CHG=0 CFG=0
M  V30 3446 H      -4.4027    26.9924    -8.2205 0 CHG=0 CFG=0
M  V30 3447 C      -6.0730    26.0740    -9.2440 0 CHG=0 CFG=0
M  V30 3448 O      -6.8730    26.2630   -10.1640 0 CHG=0 CFG=0
M  V30 3449 N      -5.7260    24.8590    -8.8410 0 CHG=0 CFG=0
M  V30 3450 H      -5.0898    24.7375    -8.0767 0 CHG=0 CFG=0
M  V30 3451 H      -6.1185    24.0264    -9.2262 0 CHG=0 CFG=0
M  V30 3452 C      -5.4790    29.7410    -8.2510 0 CHG=0 CFG=0
M  V30 3453 O      -6.5140    30.3350    -7.9450 0 CHG=0 CFG=0
M  V30 3454 N      -4.2780    30.0710    -7.7700 0 CHG=0 CFG=0
M  V30 3455 H      -3.4653    29.5946    -8.0899 0 CHG=0 CFG=0
M  V30 3456 C      -4.0790    31.1970    -6.8590 0 CHG=0 CFG=1
M  V30 3457 H      -4.6616    30.9900    -5.9599 0 CHG=0 CFG=0
M  V30 3458 C      -2.5900    31.3350    -6.5170 0 CHG=0 CFG=0
M  V30 3459 H      -1.9798    31.4503    -7.4210 0 CHG=0 CFG=0
M  V30 3460 H      -2.2307    30.4461    -5.9991 0 CHG=0 CFG=0
M  V30 3461 O      -2.3580    32.4380    -5.6630 0 CHG=0 CFG=0
M  V30 3462 H      -2.6440    33.2804    -6.0529 0 CHG=0 CFG=0
M  V30 3463 C      -4.5970    32.4950    -7.4790 0 CHG=0 CFG=0
M  V30 3464 O      -5.3360    33.2520    -6.8490 0 CHG=0 CFG=0
M  V30 3465 N      -4.2030    32.7390    -8.7280 0 CHG=0 CFG=0
M  V30 3466 H      -3.4856    32.1861    -9.1494 0 CHG=0 CFG=0
M  V30 3467 C      -4.6140    33.9360    -9.4530 0 CHG=0 CFG=1
M  V30 3468 H      -4.3810    34.7901    -8.8123 0 CHG=0 CFG=0
M  V30 3469 C      -3.8440    34.0560   -10.7680 0 CHG=0 CFG=0
M  V30 3470 H      -4.3316    34.7774   -11.4269 0 CHG=0 CFG=0
M  V30 3471 H      -3.9126    33.1033   -11.2878 0 CHG=0 CFG=0
M  V30 3472 C      -2.4090    34.5230   -10.5760 0 CHG=0 CFG=0
M  V30 3473 H      -1.9544    34.1063    -9.6765 0 CHG=0 CFG=0
M  V30 3474 H      -2.4162    35.5991   -10.3947 0 CHG=0 CFG=0
M  V30 3475 C      -1.5120    34.2620   -11.7780 0 CHG=0 CFG=0
M  V30 3476 O      -1.9420    33.5250   -12.7010 0 CHG=0 CFG=0
M  V30 3477 O      -0.3730    34.7960   -11.7850 0 CHG=-1 CFG=0
M  V30 3478 C      -6.1200    33.9500    -9.7020 0 CHG=0 CFG=0
M  V30 3479 O      -6.7630    34.9950    -9.5910 0 CHG=0 CFG=0
M  V30 3480 N      -6.6710    32.7870   -10.0350 0 CHG=0 CFG=0
M  V30 3481 H      -6.0372    32.0195   -10.0946 0 CHG=0 CFG=0
M  V30 3482 C      -8.1070    32.6590   -10.2430 0 CHG=0 CFG=1
M  V30 3483 H      -8.3669    33.3809   -11.0201 0 CHG=0 CFG=0
M  V30 3484 C      -8.4700    31.2380   -10.7170 0 CHG=0 CFG=2
M  V30 3485 H      -8.0983    30.4969    -9.9980 0 CHG=0 CFG=0
M  V30 3486 O      -7.8910    31.0100   -12.0090 0 CHG=0 CFG=0
M  V30 3487 H      -6.9401    31.0996   -11.9212 0 CHG=0 CFG=0
M  V30 3488 C      -9.9710    31.0720   -10.8080 0 CHG=0 CFG=0
M  V30 3489 H     -10.4170    31.8553   -11.4220 0 CHG=0 CFG=0
M  V30 3490 H     -10.4528    31.1004    -9.8299 0 CHG=0 CFG=0
M  V30 3491 H     -10.2235    30.1135   -11.2586 0 CHG=0 CFG=0
M  V30 3492 C      -8.8940    33.0490    -8.9810 0 CHG=0 CFG=0
M  V30 3493 O      -9.8440    33.8390    -9.0480 0 CHG=0 CFG=0
M  V30 3494 N      -8.4820    32.5170    -7.8340 0 CHG=0 CFG=0
M  V30 3495 H      -7.6449    31.9666    -7.8266 0 CHG=0 CFG=0
M  V30 3496 C      -9.1370    32.8490    -6.5650 0 CHG=0 CFG=1
M  V30 3497 H     -10.1798    32.5519    -6.6816 0 CHG=0 CFG=0
M  V30 3498 C      -8.5160    32.0720    -5.4080 0 CHG=0 CFG=0
M  V30 3499 H      -7.4662    32.3393    -5.2730 0 CHG=0 CFG=0
M  V30 3500 H      -8.5655    30.9981    -5.5871 0 CHG=0 CFG=0
M  V30 3501 H      -9.0366    32.2785    -4.4721 0 CHG=0 CFG=0
M  V30 3502 C      -9.1180    34.3520    -6.2920 0 CHG=0 CFG=0
M  V30 3503 O     -10.1280    34.9130    -5.8640 0 CHG=0 CFG=0
M  V30 3504 N      -7.9790    34.9940    -6.5690 0 CHG=0 CFG=0
M  V30 3505 H      -7.1535    34.4847    -6.8282 0 CHG=0 CFG=0
M  V30 3506 C      -7.8380    36.4570    -6.4580 0 CHG=0 CFG=1
M  V30 3507 H      -8.0894    36.7222    -5.4305 0 CHG=0 CFG=0
M  V30 3508 C      -6.4060    36.8960    -6.7860 0 CHG=0 CFG=0
M  V30 3509 H      -6.3378    37.9852    -6.7730 0 CHG=0 CFG=0
M  V30 3510 H      -6.1815    36.6095    -7.8145 0 CHG=0 CFG=0
M  V30 3511 C      -5.3010    36.3410    -5.8920 0 CHG=0 CFG=0
M  V30 3512 H      -5.4673    35.2883    -5.6760 0 CHG=0 CFG=0
M  V30 3513 H      -5.3017    36.8520    -4.9301 0 CHG=0 CFG=0
M  V30 3514 C      -3.9130    36.4990    -6.5180 0 CHG=0 CFG=0
M  V30 3515 O      -3.5860    37.6100    -6.9880 0 CHG=0 CFG=0
M  V30 3516 O      -3.1480    35.5070    -6.5430 0 CHG=-1 CFG=0
M  V30 3517 C      -8.8070    37.1790    -7.4010 0 CHG=0 CFG=0
M  V30 3518 O      -9.5340    38.0870    -6.9860 0 CHG=0 CFG=0
M  V30 3519 N      -8.7910    36.7650    -8.6690 0 CHG=0 CFG=0
M  V30 3520 H      -8.0977    36.0752    -8.8752 0 CHG=0 CFG=0
M  V30 3521 C      -9.6770    37.2790    -9.7210 0 CHG=0 CFG=1
M  V30 3522 H      -9.3587    38.3032    -9.9221 0 CHG=0 CFG=0
M  V30 3523 C      -9.5430    36.3750   -10.9580 0 CHG=0 CFG=0
M  V30 3524 H     -10.0418    35.4170   -10.8208 0 CHG=0 CFG=0
M  V30 3525 H      -8.4887    36.1392   -11.1070 0 CHG=0 CFG=0
M  V30 3526 C     -10.0240    36.9900   -12.2370 0 CHG=0 CFG=0
M  V30 3527 N     -11.1080    36.4990   -12.9350 0 CHG=0 CFG=0
M  V30 3528 C     -11.2870    37.2190   -14.0290 0 CHG=0 CFG=0
M  V30 3529 H     -12.0664    37.0651   -14.7627 0 CHG=0 CFG=0
M  V30 3530 N     -10.3550    38.1560   -14.0690 0 CHG=0 CFG=0
M  V30 3531 H     -10.2538    38.8369   -14.7641 0 CHG=0 CFG=0
M  V30 3532 C      -9.5450    38.0270   -12.9660 0 CHG=0 CFG=0
M  V30 3533 H      -8.6863    38.6322   -12.7096 0 CHG=0 CFG=0
M  V30 3534 C     -11.1180    37.2720    -9.2220 0 CHG=0 CFG=0
M  V30 3535 O     -11.8210    38.2870    -9.2690 0 CHG=0 CFG=0
M  V30 3536 N     -11.5310    36.1140    -8.7200 0 CHG=0 CFG=0
M  V30 3537 H     -10.8596    35.3743    -8.7031 0 CHG=0 CFG=0
M  V30 3538 C     -12.8830    35.8900    -8.2200 0 CHG=0 CFG=1
M  V30 3539 H     -13.5585    36.2184    -9.0071 0 CHG=0 CFG=0
M  V30 3540 C     -13.0740    34.3880    -7.8580 0 CHG=0 CFG=1
M  V30 3541 H     -12.1712    34.0384    -7.3537 0 CHG=0 CFG=0
M  V30 3542 C     -14.2300    34.1650    -6.8650 0 CHG=0 CFG=0
M  V30 3543 H     -15.1625    34.5953    -7.2306 0 CHG=0 CFG=0
M  V30 3544 H     -14.0225    34.5960    -5.8849 0 CHG=0 CFG=0
M  V30 3545 H     -14.4014    33.1002    -6.7030 0 CHG=0 CFG=0
M  V30 3546 C     -13.2550    33.5560    -9.1300 0 CHG=0 CFG=0
M  V30 3547 H     -13.5575    32.5440    -8.8571 0 CHG=0 CFG=0
M  V30 3548 H     -12.2910    33.4470    -9.6284 0 CHG=0 CFG=0
M  V30 3549 C     -14.2480    34.1310   -10.1410 0 CHG=0 CFG=0
M  V30 3550 H     -15.1761    34.4406    -9.6629 0 CHG=0 CFG=0
M  V30 3551 H     -14.4982    33.3824   -10.8883 0 CHG=0 CFG=0
M  V30 3552 H     -13.8335    34.9797   -10.6843 0 CHG=0 CFG=0
M  V30 3553 C     -13.2040    36.7990    -7.0360 0 CHG=0 CFG=0
M  V30 3554 O     -14.2720    37.4230    -6.9950 0 CHG=0 CFG=0
M  V30 3555 N     -12.2680    36.8940    -6.0940 0 CHG=0 CFG=0
M  V30 3556 H     -11.4145    36.3789    -6.1997 0 CHG=0 CFG=0
M  V30 3557 C     -12.4510    37.7320    -4.9050 0 CHG=0 CFG=1
M  V30 3558 H     -13.3957    37.4218    -4.4548 0 CHG=0 CFG=0
M  V30 3559 C     -11.3220    37.5030    -3.9110 0 CHG=0 CFG=0
M  V30 3560 H     -10.3601    37.7970    -4.3339 0 CHG=0 CFG=0
M  V30 3561 H     -11.2540    36.4504    -3.6367 0 CHG=0 CFG=0
M  V30 3562 H     -11.4795    38.0777    -2.9976 0 CHG=0 CFG=0
M  V30 3563 C     -12.5740    39.2180    -5.2560 0 CHG=0 CFG=0
M  V30 3564 O     -13.1130    40.0090    -4.4760 0 CHG=0 CFG=0
M  V30 3565 N     -12.0780    39.5850    -6.4360 0 CHG=0 CFG=0
M  V30 3566 H     -11.5617    38.9180    -6.9773 0 CHG=0 CFG=0
M  V30 3567 C     -12.1650    40.9570    -6.9320 0 CHG=0 CFG=1
M  V30 3568 H     -12.2493    41.6228    -6.0711 0 CHG=0 CFG=0
M  V30 3569 C     -10.9050    41.3240    -7.7150 0 CHG=0 CFG=0
M  V30 3570 H     -11.0569    42.2619    -8.2530 0 CHG=0 CFG=0
M  V30 3571 H     -10.7331    40.5670    -8.4831 0 CHG=0 CFG=0
M  V30 3572 C      -9.6610    41.4750    -6.8520 0 CHG=0 CFG=0
M  V30 3573 H      -9.5068    40.5701    -6.2636 0 CHG=0 CFG=0
M  V30 3574 H      -9.7895    42.2985    -6.1501 0 CHG=0 CFG=0
M  V30 3575 C      -8.4010    41.7120    -7.6640 0 CHG=0 CFG=0
M  V30 3576 O      -8.4130    41.6480    -8.8960 0 CHG=0 CFG=0
M  V30 3577 N      -7.3020    41.9830    -6.9730 0 CHG=0 CFG=0
M  V30 3578 H      -7.3034    42.0326    -5.9789 0 CHG=0 CFG=0
M  V30 3579 H      -6.4557    42.0838    -7.4915 0 CHG=0 CFG=0
M  V30 3580 C     -13.4070    41.1910    -7.7920 0 CHG=0 CFG=0
M  V30 3581 O     -13.5990    42.2840    -8.3330 0 CHG=0 CFG=0
M  V30 3582 N     -14.2380    40.1600    -7.9260 0 CHG=0 CFG=0
M  V30 3583 H     -14.0063    39.2962    -7.4784 0 CHG=0 CFG=0
M  V30 3584 C     -15.5070    40.2760    -8.6360 0 CHG=0 CFG=0
M  V30 3585 H     -15.9464    41.2477    -8.4041 0 CHG=0 CFG=0
M  V30 3586 H     -16.1601    39.5064    -8.2266 0 CHG=0 CFG=0
M  V30 3587 C     -15.4010    40.1080   -10.1390 0 CHG=0 CFG=0
M  V30 3588 O     -16.3500    40.3790   -10.8750 0 CHG=0 CFG=0
M  V30 3589 N     -14.2490    39.6500   -10.6060 0 CHG=0 CFG=0
M  V30 3590 H     -13.5135    39.3786    -9.9797 0 CHG=0 CFG=0
M  V30 3591 C     -14.0750    39.4370   -12.0320 0 CHG=0 CFG=1
M  V30 3592 H     -14.6891    40.1718   -12.5555 0 CHG=0 CFG=0
M  V30 3593 C     -12.6230    39.6740   -12.4330 0 CHG=0 CFG=0
M  V30 3594 H     -12.5094    39.5472   -13.5083 0 CHG=0 CFG=0
M  V30 3595 H     -12.0092    38.9250   -11.9358 0 CHG=0 CFG=0
M  V30 3596 C     -12.1140    41.0730   -12.0320 0 CHG=0 CFG=0
M  V30 3597 H     -12.2822    41.2105   -10.9623 0 CHG=0 CFG=0
M  V30 3598 C     -10.6090    41.2350   -12.2280 0 CHG=0 CFG=0
M  V30 3599 H     -10.3196    41.0846   -13.2680 0 CHG=0 CFG=0
M  V30 3600 H     -10.0615    40.5179   -11.6151 0 CHG=0 CFG=0
M  V30 3601 H     -10.2752    42.2277   -11.9240 0 CHG=0 CFG=0
M  V30 3602 C     -12.8670    42.1950   -12.7580 0 CHG=0 CFG=0
M  V30 3603 H     -13.9232    42.2103   -12.4901 0 CHG=0 CFG=0
M  V30 3604 H     -12.7907    42.0904   -13.8402 0 CHG=0 CFG=0
M  V30 3605 H     -12.4629    43.1710   -12.4875 0 CHG=0 CFG=0
M  V30 3606 C     -14.6170    38.0650   -12.4360 0 CHG=0 CFG=0
M  V30 3607 O     -14.8570    37.2070   -11.5800 0 CHG=0 CFG=0
M  V30 3608 N     -14.8520    37.8780   -13.7320 0 CHG=0 CFG=0
M  V30 3609 H     -14.5421    38.5367   -14.4163 0 CHG=0 CFG=0
M  V30 3610 C     -15.6320    36.7370   -14.2080 0 CHG=0 CFG=1
M  V30 3611 H     -15.5475    35.9314   -13.4766 0 CHG=0 CFG=0
M  V30 3612 C     -17.1040    37.1420   -14.4230 0 CHG=0 CFG=0
M  V30 3613 H     -17.6577    36.3186   -14.8791 0 CHG=0 CFG=0
M  V30 3614 H     -17.1398    37.9505   -15.1558 0 CHG=0 CFG=0
M  V30 3615 C     -17.8600    37.5960   -13.1680 0 CHG=0 CFG=0
M  V30 3616 H     -18.8348    37.9878   -13.4612 0 CHG=0 CFG=0
M  V30 3617 H     -17.3411    38.4181   -12.6736 0 CHG=0 CFG=0
M  V30 3618 C     -18.0520    36.4340   -12.2180 0 CHG=0 CFG=0
M  V30 3619 H     -17.1073    35.9861   -11.9091 0 CHG=0 CFG=0
M  V30 3620 H     -18.6100    35.6433   -12.7194 0 CHG=0 CFG=0
M  V30 3621 N     -18.8360    36.7700   -11.0280 0 CHG=0 CFG=0
M  V30 3622 H     -19.8367    36.7299   -11.1058 0 CHG=0 CFG=0
M  V30 3623 C     -18.3200    37.0510    -9.8360 0 CHG=0 CFG=0
M  V30 3624 N     -16.9990    37.0840    -9.6580 0 CHG=1 CFG=0
M  V30 3625 H     -16.3610    36.9550   -10.4290 0 CHG=0 CFG=0
M  V30 3626 H     -16.5986    37.2574    -8.7531 0 CHG=0 CFG=0
M  V30 3627 N     -19.1300    37.3120    -8.8150 0 CHG=0 CFG=0
M  V30 3628 H     -20.1174    37.1756    -8.9244 0 CHG=0 CFG=0
M  V30 3629 H     -18.7921    37.6397    -7.9134 0 CHG=0 CFG=0
M  V30 3630 C     -15.0830    36.1960   -15.5140 0 CHG=0 CFG=0
M  V30 3631 O     -14.3210    36.8730   -16.2130 0 CHG=0 CFG=0
M  V30 3632 N     -15.4830    34.9710   -15.8420 0 CHG=0 CFG=0
M  V30 3633 H     -16.0763    34.4822   -15.2061 0 CHG=0 CFG=0
M  V30 3634 C     -15.2800    34.4440   -17.1820 0 CHG=0 CFG=1
M  V30 3635 H     -14.2145    34.5158   -17.4043 0 CHG=0 CFG=0
M  V30 3636 C     -15.7810    33.0050   -17.2700 0 CHG=0 CFG=0
M  V30 3637 H     -15.7935    32.6807   -18.3103 0 CHG=0 CFG=0
M  V30 3638 H     -16.8210    32.9968   -16.9486 0 CHG=0 CFG=0
M  V30 3639 C     -14.9970    31.9790   -16.4460 0 CHG=0 CFG=0
M  V30 3640 H     -14.8519    32.3940   -15.4530 0 CHG=0 CFG=0
M  V30 3641 C     -15.8010    30.6930   -16.2920 0 CHG=0 CFG=0
M  V30 3642 H     -15.9970    30.2236   -17.2538 0 CHG=0 CFG=0
M  V30 3643 H     -16.7594    30.8829   -15.8092 0 CHG=0 CFG=0
M  V30 3644 H     -15.2682    29.9715   -15.6726 0 CHG=0 CFG=0
M  V30 3645 C     -13.6510    31.7030   -17.0900 0 CHG=0 CFG=0
M  V30 3646 H     -13.0362    32.6012   -17.1388 0 CHG=0 CFG=0
M  V30 3647 H     -13.7668    31.3142   -18.1012 0 CHG=0 CFG=0
M  V30 3648 H     -13.0984    30.9630   -16.5125 0 CHG=0 CFG=0
M  V30 3649 C     -16.0540    35.3240   -18.1500 0 CHG=0 CFG=0
M  V30 3650 O     -17.0280    35.9890   -17.7650 0 CHG=0 CFG=0
M  V30 3651 N     -15.6140    35.3700   -19.3960 0 CHG=0 CFG=0
M  V30 3652 H     -14.8527    34.8044   -19.7018 0 CHG=0 CFG=0
M  V30 3653 C     -16.3730    36.1420   -20.3670 0 CHG=0 CFG=1
M  V30 3654 H     -17.2776    36.5281   -19.9012 0 CHG=0 CFG=0
M  V30 3655 C     -15.6040    37.3760   -20.8600 0 CHG=0 CFG=0
M  V30 3656 H     -15.3914    38.0068   -19.9957 0 CHG=0 CFG=0
M  V30 3657 H     -16.2381    37.9908   -21.5000 0 CHG=0 CFG=0
M  V30 3658 C     -14.2960    37.1140   -21.5660 0 CHG=0 CFG=0
M  V30 3659 C     -13.1320    36.8600   -20.8450 0 CHG=0 CFG=0
M  V30 3660 H     -13.1686    36.8391   -19.7642 0 CHG=0 CFG=0
M  V30 3661 C     -11.9220    36.6410   -21.4790 0 CHG=0 CFG=0
M  V30 3662 H     -11.0298    36.4441   -20.9032 0 CHG=0 CFG=0
M  V30 3663 C     -14.2100    37.1650   -22.9580 0 CHG=0 CFG=0
M  V30 3664 H     -15.0909    37.3706   -23.5491 0 CHG=0 CFG=0
M  V30 3665 C     -13.0020    36.9440   -23.6090 0 CHG=0 CFG=0
M  V30 3666 H     -12.9782    36.9746   -24.6889 0 CHG=0 CFG=0
M  V30 3667 C     -11.8620    36.6850   -22.8610 0 CHG=0 CFG=0
M  V30 3668 O     -10.6580    36.4720   -23.4910 0 CHG=0 CFG=0
M  V30 3669 H     -10.5214    37.1379   -24.1525 0 CHG=0 CFG=0
M  V30 3670 C     -16.8980    35.2660   -21.4930 0 CHG=0 CFG=0
M  V30 3671 O     -16.6760    34.0520   -21.5040 0 CHG=0 CFG=0
M  V30 3672 N     -17.6100    35.8910   -22.4230 0 CHG=0 CFG=0
M  V30 3673 H     -17.6795    36.8838   -22.3492 0 CHG=0 CFG=0
M  V30 3674 C     -18.4400    35.1690   -23.3810 0 CHG=0 CFG=1
M  V30 3675 H     -19.0926    34.5348   -22.7862 0 CHG=0 CFG=0
M  V30 3676 C     -19.3140    36.1870   -24.1180 0 CHG=0 CFG=0
M  V30 3677 H     -18.6683    36.8637   -24.6806 0 CHG=0 CFG=0
M  V30 3678 H     -19.8236    36.8064   -23.3816 0 CHG=0 CFG=0
M  V30 3679 C     -20.3380    35.5880   -25.0480 0 CHG=0 CFG=0
M  V30 3680 H     -20.9447    34.8405   -24.5394 0 CHG=0 CFG=0
M  V30 3681 H     -19.8259    35.0717   -25.8608 0 CHG=0 CFG=0
M  V30 3682 C     -21.1990    36.7010   -25.6200 0 CHG=0 CFG=0
M  V30 3683 H     -20.5710    37.5602   -25.8631 0 CHG=0 CFG=0
M  V30 3684 H     -21.9687    37.0195   -24.9148 0 CHG=0 CFG=0
M  V30 3685 N     -21.8660    36.2780   -26.8450 0 CHG=0 CFG=0
M  V30 3686 H     -21.9043    35.2857   -26.9327 0 CHG=0 CFG=0
M  V30 3687 C     -22.3180    37.1090   -27.7770 0 CHG=0 CFG=0
M  V30 3688 N     -22.1780    38.4280   -27.6360 0 CHG=1 CFG=0
M  V30 3689 H     -21.6900    38.7957   -26.8442 0 CHG=0 CFG=0
M  V30 3690 H     -22.5672    39.0872   -28.2855 0 CHG=0 CFG=0
M  V30 3691 N     -22.9080    36.6200   -28.8580 0 CHG=0 CFG=0
M  V30 3692 H     -22.9254    35.6206   -28.9638 0 CHG=0 CFG=0
M  V30 3693 H     -23.3086    37.2065   -29.5649 0 CHG=0 CFG=0
M  V30 3694 C     -17.6450    34.3110   -24.3780 0 CHG=0 CFG=0
M  V30 3695 O     -16.8350    34.8470   -25.1370 0 CHG=0 CFG=0
M  V30 3696 N     -17.8640    32.9750   -24.3670 0 CHG=0 CFG=0
M  V30 3697 C     -18.6100    32.1640   -23.3890 0 CHG=0 CFG=0
M  V30 3698 H     -19.6760    32.2010   -23.6161 0 CHG=0 CFG=0
M  V30 3699 H     -18.4510    32.5046   -22.3659 0 CHG=0 CFG=0
M  V30 3700 C     -17.2680    32.1440   -25.4170 0 CHG=0 CFG=1
M  V30 3701 H     -16.1804    32.2249   -25.3793 0 CHG=0 CFG=0
M  V30 3702 C     -17.7490    30.7290   -25.0720 0 CHG=0 CFG=0
M  V30 3703 H     -17.0143    29.9644   -25.3281 0 CHG=0 CFG=0
M  V30 3704 H     -18.6733    30.4835   -25.5975 0 CHG=0 CFG=0
M  V30 3705 C     -18.0340    30.7760   -23.5980 0 CHG=0 CFG=0
M  V30 3706 H     -18.6930    29.9786   -23.2530 0 CHG=0 CFG=0
M  V30 3707 H     -17.0982    30.7128   -23.0437 0 CHG=0 CFG=0
M  V30 3708 C     -17.8030    32.5520   -26.7830 0 CHG=0 CFG=0
M  V30 3709 O     -18.9630    32.9440   -26.9020 0 CHG=0 CFG=0
M  V30 3710 N     -16.9600    32.4460   -27.8020 0 CHG=0 CFG=0
M  V30 3711 H     -16.0180    32.1924   -27.5981 0 CHG=0 CFG=0
M  V30 3712 C     -17.3270    32.8370   -29.1530 0 CHG=0 CFG=1
M  V30 3713 H     -17.5232    33.9099   -29.1191 0 CHG=0 CFG=0
M  V30 3714 C     -16.1680    32.5470   -30.1000 0 CHG=0 CFG=0
M  V30 3715 H     -16.4848    32.7200   -31.1303 0 CHG=0 CFG=0
M  V30 3716 H     -15.8778    31.4973   -30.0411 0 CHG=0 CFG=0
M  V30 3717 C     -14.9630    33.4100   -29.8700 0 CHG=0 CFG=0
M  V30 3718 N     -15.0510    34.7210   -29.4540 0 CHG=0 CFG=0
M  V30 3719 C     -13.8360    35.2340   -29.3570 0 CHG=0 CFG=0
M  V30 3720 H     -13.6054    36.2470   -29.0581 0 CHG=0 CFG=0
M  V30 3721 N     -12.9630    34.3010   -29.6940 0 CHG=0 CFG=0
M  V30 3722 H     -11.9916    34.4250   -29.7260 0 CHG=0 CFG=0
M  V30 3723 C     -13.6420    33.1540   -30.0230 0 CHG=0 CFG=0
M  V30 3724 H     -13.2089    32.2216   -30.3554 0 CHG=0 CFG=0
M  V30 3725 C     -18.6100    32.1580   -29.6580 0 CHG=0 CFG=0
M  V30 3726 O     -19.3890    32.7590   -30.4090 0 CHG=0 CFG=0
M  V30 3727 N     -18.8360    30.9180   -29.2260 0 CHG=0 CFG=0
M  V30 3728 H     -18.1845    30.5007   -28.5959 0 CHG=0 CFG=0
M  V30 3729 C     -19.9910    30.1440   -29.6920 0 CHG=0 CFG=1
M  V30 3730 H     -20.1843    30.4511   -30.7203 0 CHG=0 CFG=0
M  V30 3731 C     -19.6770    28.6430   -29.6800 0 CHG=0 CFG=0
M  V30 3732 H     -20.5999    28.0672   -29.7755 0 CHG=0 CFG=0
M  V30 3733 H     -19.2828    28.3815   -28.6973 0 CHG=0 CFG=0
M  V30 3734 C     -18.7170    28.1550   -30.7660 0 CHG=0 CFG=0
M  V30 3735 H     -17.8410    28.8044   -30.7775 0 CHG=0 CFG=0
M  V30 3736 C     -18.2340    26.7370   -30.4770 0 CHG=0 CFG=0
M  V30 3737 H     -19.0606    26.0267   -30.4828 0 CHG=0 CFG=0
M  V30 3738 H     -17.7518    26.6741   -29.5005 0 CHG=0 CFG=0
M  V30 3739 H     -17.5114    26.4077   -31.2236 0 CHG=0 CFG=0
M  V30 3740 C     -19.3810    28.2140   -32.1260 0 CHG=0 CFG=0
M  V30 3741 H     -19.6425    29.2310   -32.4149 0 CHG=0 CFG=0
M  V30 3742 H     -20.2920    27.6147   -32.1517 0 CHG=0 CFG=0
M  V30 3743 H     -18.7163    27.8275   -32.8994 0 CHG=0 CFG=0
M  V30 3744 C     -21.2950    30.4200   -28.9410 0 CHG=0 CFG=0
M  V30 3745 O     -22.3640    29.9630   -29.3760 0 CHG=0 CFG=0
M  V30 3746 N     -21.2120    31.1470   -27.8220 0 CHG=0 CFG=0
M  V30 3747 H     -20.3561    31.6239   -27.6146 0 CHG=0 CFG=0
M  V30 3748 C     -22.3990    31.4900   -27.0290 0 CHG=0 CFG=1
M  V30 3749 H     -23.0963    30.6541   -27.1167 0 CHG=0 CFG=0
M  V30 3750 C     -22.0310    31.6500   -25.5450 0 CHG=0 CFG=0
M  V30 3751 H     -21.3160    32.4621   -25.4053 0 CHG=0 CFG=0
M  V30 3752 H     -21.5813    30.7380   -25.1528 0 CHG=0 CFG=0
M  V30 3753 H     -22.9114    31.8723   -24.9396 0 CHG=0 CFG=0
M  V30 3754 C     -23.0880    32.7530   -27.5440 0 CHG=0 CFG=0
M  V30 3755 O     -22.4640    33.8070   -27.6660 0 CHG=0 CFG=0
M  V30 3756 N     -24.3750    32.6390   -27.8520 0 CHG=0 CFG=0
M  V30 3757 H     -24.8378    31.7628   -27.7239 0 CHG=0 CFG=0
M  V30 3758 C     -25.2070    33.8090   -28.1510 0 CHG=0 CFG=1
M  V30 3759 H     -24.7140    34.3667   -28.9478 0 CHG=0 CFG=0
M  V30 3760 C     -26.5890    33.3530   -28.5760 0 CHG=0 CFG=0
M  V30 3761 H     -26.4976    32.6786   -29.4386 0 CHG=0 CFG=0
M  V30 3762 H     -27.1861    34.2115   -28.9078 0 CHG=0 CFG=0
M  V30 3763 O     -27.2350    32.7080   -27.4970 0 CHG=0 CFG=0
M  V30 3764 H     -28.0732    32.3274   -27.7943 0 CHG=0 CFG=0
M  V30 3765 C     -25.3440    34.6730   -26.9050 0 CHG=0 CFG=0
M  V30 3766 O     -25.0760    34.2020   -25.8040 0 CHG=0 CFG=0
M  V30 3767 N     -25.7960    35.9170   -27.0650 0 CHG=0 CFG=0
M  V30 3768 H     -26.0338    36.2855   -27.9622 0 CHG=0 CFG=0
M  V30 3769 C     -26.0440    36.7680   -25.8990 0 CHG=0 CFG=1
M  V30 3770 H     -25.0858    36.8777   -25.3877 0 CHG=0 CFG=0
M  V30 3771 C     -26.5570    38.1500   -26.3180 0 CHG=0 CFG=0
M  V30 3772 H     -26.9565    38.6773   -25.4482 0 CHG=0 CFG=0
M  V30 3773 H     -27.3963    38.0428   -27.0070 0 CHG=0 CFG=0
M  V30 3774 C     -25.4850    39.0310   -26.9340 0 CHG=0 CFG=0
M  V30 3775 H     -24.9961    38.4999   -27.7489 0 CHG=0 CFG=0
M  V30 3776 H     -24.7187    39.2656   -26.1953 0 CHG=0 CFG=0
M  V30 3777 C     -26.0300    40.3370   -27.4740 0 CHG=0 CFG=0
M  V30 3778 O     -26.6200    41.1110   -26.6890 0 CHG=0 CFG=0
M  V30 3779 O     -25.8610    40.5940   -28.6850 0 CHG=-1 CFG=0
M  V30 3780 C     -27.0040    36.1020   -24.9080 0 CHG=0 CFG=0
M  V30 3781 O     -26.7750    36.1430   -23.6970 0 CHG=0 CFG=0
M  V30 3782 N     -28.0540    35.4650   -25.4230 0 CHG=0 CFG=0
M  V30 3783 H     -28.1818    35.4674   -26.4116 0 CHG=0 CFG=0
M  V30 3784 C     -29.0320    34.7820   -24.5660 0 CHG=0 CFG=1
M  V30 3785 H     -29.3856    35.5287   -23.8519 0 CHG=0 CFG=0
M  V30 3786 C     -30.2160    34.2760   -25.3880 0 CHG=0 CFG=0
M  V30 3787 H     -30.8653    33.6826   -24.7424 0 CHG=0 CFG=0
M  V30 3788 H     -29.8726    33.5973   -26.1697 0 CHG=0 CFG=0
M  V30 3789 C     -31.0540    35.3930   -25.9880 0 CHG=0 CFG=0
M  V30 3790 H     -30.4275    36.0283   -26.6145 0 CHG=0 CFG=0
M  V30 3791 H     -31.4432    36.0262   -25.1889 0 CHG=0 CFG=0
M  V30 3792 C     -32.2050    34.8450   -26.8140 0 CHG=0 CFG=0
M  V30 3793 H     -32.8565    34.2343   -26.1834 0 CHG=0 CFG=0
M  V30 3794 H     -31.8228    34.1783   -27.5896 0 CHG=0 CFG=0
M  V30 3795 C     -33.0020    35.9750   -27.4430 0 CHG=0 CFG=0
M  V30 3796 H     -32.3638    36.5917   -28.0760 0 CHG=0 CFG=0
M  V30 3797 H     -33.4512    36.6100   -26.6771 0 CHG=0 CFG=0
M  V30 3798 N     -34.1030    35.4390   -28.2870 0 CHG=1 CFG=0
M  V30 3799 H     -34.8078    34.9872   -27.6591 0 CHG=0 CFG=0
M  V30 3800 H     -33.7901    34.6541   -28.8991 0 CHG=0 CFG=0
M  V30 3801 H     -34.6183    36.1420   -28.8433 0 CHG=0 CFG=0
M  V30 3802 C     -28.4100    33.6460   -23.7500 0 CHG=0 CFG=0
M  V30 3803 O     -28.6960    33.5030   -22.5590 0 CHG=0 CFG=0
M  V30 3804 N     -27.5490    32.8510   -24.3850 0 CHG=0 CFG=0
M  V30 3805 H     -27.3746    32.9978   -25.3605 0 CHG=0 CFG=0
M  V30 3806 C     -26.8520    31.7670   -23.6850 0 CHG=0 CFG=1
M  V30 3807 H     -27.6159    31.2046   -23.1434 0 CHG=0 CFG=0
M  V30 3808 C     -26.1330    30.8270   -24.6810 0 CHG=0 CFG=0
M  V30 3809 H     -25.5392    31.4412   -25.3598 0 CHG=0 CFG=0
M  V30 3810 C     -25.1880    29.8770   -23.9560 0 CHG=0 CFG=0
M  V30 3811 H     -25.7192    29.2232   -23.2627 0 CHG=0 CFG=0
M  V30 3812 H     -24.3970    30.3879   -23.4096 0 CHG=0 CFG=0
M  V30 3813 H     -24.6790    29.2576   -24.6854 0 CHG=0 CFG=0
M  V30 3814 C     -27.1490    30.0400   -25.5020 0 CHG=0 CFG=0
M  V30 3815 H     -27.8729    30.6936   -25.9790 0 CHG=0 CFG=0
M  V30 3816 H     -27.7109    29.3426   -24.8780 0 CHG=0 CFG=0
M  V30 3817 H     -26.6609    29.4619   -26.2857 0 CHG=0 CFG=0
M  V30 3818 C     -25.8660    32.3130   -22.6360 0 CHG=0 CFG=0
M  V30 3819 O     -25.7810    31.8060   -21.5000 0 CHG=0 CFG=0
M  V30 3820 N     -25.1210    33.3480   -23.0160 0 CHG=0 CFG=0
M  V30 3821 H     -25.2406    33.6929   -23.9474 0 CHG=0 CFG=0
M  V30 3822 C     -24.2040    33.9970   -22.0900 0 CHG=0 CFG=1
M  V30 3823 H     -23.5255    33.2108   -21.7658 0 CHG=0 CFG=0
M  V30 3824 C     -23.4140    35.0980   -22.7950 0 CHG=0 CFG=0
M  V30 3825 H     -24.1033    35.8629   -23.1567 0 CHG=0 CFG=0
M  V30 3826 H     -22.9414    34.6821   -23.6830 0 CHG=0 CFG=0
M  V30 3827 C     -22.3420    35.7550   -21.9410 0 CHG=0 CFG=0
M  V30 3828 C     -21.3930    34.9910   -21.2560 0 CHG=0 CFG=0
M  V30 3829 H     -21.4161    33.9125   -21.3097 0 CHG=0 CFG=0
M  V30 3830 C     -20.3920    35.6040   -20.4820 0 CHG=0 CFG=0
M  V30 3831 H     -19.6656    35.0054   -19.9511 0 CHG=0 CFG=0
M  V30 3832 C     -22.2590    37.1470   -21.8430 0 CHG=0 CFG=0
M  V30 3833 H     -22.9752    37.7681   -22.3621 0 CHG=0 CFG=0
M  V30 3834 C     -21.2660    37.7660   -21.0710 0 CHG=0 CFG=0
M  V30 3835 H     -21.2379    38.8455   -21.0212 0 CHG=0 CFG=0
M  V30 3836 C     -20.3410    36.9890   -20.3960 0 CHG=0 CFG=0
M  V30 3837 O     -19.3590    37.5960   -19.6450 0 CHG=0 CFG=0
M  V30 3838 H     -19.7362    38.2582   -19.0784 0 CHG=0 CFG=0
M  V30 3839 C     -24.9340    34.5490   -20.8680 0 CHG=0 CFG=0
M  V30 3840 O     -24.4540    34.4150   -19.7480 0 CHG=0 CFG=0
M  V30 3841 N     -26.1060    35.1450   -21.0840 0 CHG=0 CFG=0
M  V30 3842 H     -26.4433    35.2361   -22.0203 0 CHG=0 CFG=0
M  V30 3843 C     -26.9330    35.6320   -19.9750 0 CHG=0 CFG=1
M  V30 3844 H     -26.3349    36.3903   -19.4668 0 CHG=0 CFG=0
M  V30 3845 C     -28.2310    36.2800   -20.5030 0 CHG=0 CFG=2
M  V30 3846 H     -28.7833    35.5702   -21.1316 0 CHG=0 CFG=0
M  V30 3847 O     -27.8930    37.4490   -21.2610 0 CHG=0 CFG=0
M  V30 3848 H     -27.3904    37.2005   -22.0380 0 CHG=0 CFG=0
M  V30 3849 C     -29.1570    36.6720   -19.3590 0 CHG=0 CFG=0
M  V30 3850 H     -28.6456    37.3126   -18.6397 0 CHG=0 CFG=0
M  V30 3851 H     -29.5492    35.8064   -18.8239 0 CHG=0 CFG=0
M  V30 3852 H     -30.0154    37.2267   -19.7386 0 CHG=0 CFG=0
M  V30 3853 C     -27.2360    34.5370   -18.9420 0 CHG=0 CFG=0
M  V30 3854 O     -27.1600    34.7740   -17.7220 0 CHG=0 CFG=0
M  V30 3855 N     -27.5480    33.3410   -19.4370 0 CHG=0 CFG=0
M  V30 3856 H     -27.6206    33.2243   -20.4282 0 CHG=0 CFG=0
M  V30 3857 C     -27.8360    32.1960   -18.5720 0 CHG=0 CFG=1
M  V30 3858 H     -28.5807    32.5420   -17.8528 0 CHG=0 CFG=0
M  V30 3859 C     -28.4350    31.0000   -19.3700 0 CHG=0 CFG=1
M  V30 3860 H     -27.7469    30.7536   -20.1799 0 CHG=0 CFG=0
M  V30 3861 C     -28.5860    29.7530   -18.4760 0 CHG=0 CFG=0
M  V30 3862 H     -29.2592    29.9527   -17.6423 0 CHG=0 CFG=0
M  V30 3863 H     -27.6364    29.4143   -18.0629 0 CHG=0 CFG=0
M  V30 3864 H     -28.9943    28.9087   -19.0304 0 CHG=0 CFG=0
M  V30 3865 C     -29.7890    31.3790   -19.9790 0 CHG=0 CFG=0
M  V30 3866 H     -29.7187    32.3488   -20.4719 0 CHG=0 CFG=0
M  V30 3867 H     -30.5235    31.5039   -19.1839 0 CHG=0 CFG=0
M  V30 3868 C     -30.2930    30.3810   -21.0110 0 CHG=0 CFG=0
M  V30 3869 H     -30.4744    29.3981   -20.5777 0 CHG=0 CFG=0
M  V30 3870 H     -29.5877    30.2657   -21.8339 0 CHG=0 CFG=0
M  V30 3871 H     -31.2400    30.7180   -21.4335 0 CHG=0 CFG=0
M  V30 3872 C     -26.5920    31.7700   -17.7770 0 CHG=0 CFG=0
M  V30 3873 O     -26.6550    31.6430   -16.5520 0 CHG=0 CFG=0
M  V30 3874 N     -25.4520    31.5670   -18.4330 0 CHG=0 CFG=0
M  V30 3875 H     -25.4358    31.6768   -19.4283 0 CHG=0 CFG=0
M  V30 3876 C     -24.2890    31.1370   -17.6490 0 CHG=0 CFG=1
M  V30 3877 H     -24.6204    30.2745   -17.0653 0 CHG=0 CFG=0
M  V30 3878 C     -23.1120    30.6750   -18.5180 0 CHG=0 CFG=0
M  V30 3879 H     -23.4693    29.9133   -19.2106 0 CHG=0 CFG=0
M  V30 3880 H     -22.3843    30.1737   -17.8765 0 CHG=0 CFG=0
M  V30 3881 C     -22.3990    31.7670   -19.2820 0 CHG=0 CFG=0
M  V30 3882 H     -21.9786    32.5235   -18.6193 0 CHG=0 CFG=0
M  V30 3883 H     -23.1135    32.2731   -19.9243 0 CHG=0 CFG=0
M  V30 3884 S     -21.0600    31.0930   -20.2940 0 CHG=0 CFG=0
M  V30 3885 C     -21.9680    30.2040   -21.5610 0 CHG=0 CFG=0
M  V30 3886 H     -23.0084    30.5276   -21.5933 0 CHG=0 CFG=0
M  V30 3887 H     -21.9219    29.1304   -21.3787 0 CHG=0 CFG=0
M  V30 3888 H     -21.5250    30.3978   -22.5377 0 CHG=0 CFG=0
M  V30 3889 C     -23.8820    32.2220   -16.6540 0 CHG=0 CFG=0
M  V30 3890 O     -23.5530    31.9330   -15.4940 0 CHG=0 CFG=0
M  V30 3891 N     -23.9530    33.4760   -17.0900 0 CHG=0 CFG=0
M  V30 3892 H     -24.2758    33.6410   -18.0213 0 CHG=0 CFG=0
M  V30 3893 C     -23.5430    34.5960   -16.2490 0 CHG=0 CFG=1
M  V30 3894 H     -22.5329    34.3621   -15.9203 0 CHG=0 CFG=0
M  V30 3895 C     -23.5360    35.8990   -17.0520 0 CHG=0 CFG=0
M  V30 3896 H     -24.5515    36.2732   -17.1962 0 CHG=0 CFG=0
M  V30 3897 H     -23.1585    35.6920   -18.0537 0 CHG=0 CFG=0
M  V30 3898 C     -22.6560    36.9890   -16.4690 0 CHG=0 CFG=0
M  V30 3899 C     -21.2940    37.0560   -16.7740 0 CHG=0 CFG=0
M  V30 3900 H     -20.8519    36.3191   -17.4292 0 CHG=0 CFG=0
M  V30 3901 C     -20.4830    38.0600   -16.2340 0 CHG=0 CFG=0
M  V30 3902 H     -19.4275    38.0952   -16.4648 0 CHG=0 CFG=0
M  V30 3903 C     -23.1850    37.9510   -15.6160 0 CHG=0 CFG=0
M  V30 3904 H     -24.2350    37.9179   -15.3601 0 CHG=0 CFG=0
M  V30 3905 C     -22.3860    38.9620   -15.0790 0 CHG=0 CFG=0
M  V30 3906 H     -22.8666    39.6845   -14.4343 0 CHG=0 CFG=0
M  V30 3907 C     -21.0370    39.0070   -15.3870 0 CHG=0 CFG=0
M  V30 3908 O     -20.2500    40.0080   -14.8520 0 CHG=0 CFG=0
M  V30 3909 H     -20.6168    40.3691   -14.0563 0 CHG=0 CFG=0
M  V30 3910 C     -24.4260    34.7260   -15.0060 0 CHG=0 CFG=0
M  V30 3911 O     -23.9480    35.1360   -13.9490 0 CHG=0 CFG=0
M  V30 3912 N     -25.7060    34.3600   -15.1310 0 CHG=0 CFG=0
M  V30 3913 H     -26.0526    34.0888   -16.0310 0 CHG=0 CFG=0
M  V30 3914 C     -26.6360    34.4280   -13.9940 0 CHG=0 CFG=1
M  V30 3915 H     -26.5809    35.4521   -13.6193 0 CHG=0 CFG=0
M  V30 3916 C     -28.0730    34.1350   -14.4340 0 CHG=0 CFG=0
M  V30 3917 H     -28.3594    34.7276   -15.3094 0 CHG=0 CFG=0
M  V30 3918 H     -28.7580    34.4227   -13.6328 0 CHG=0 CFG=0
M  V30 3919 O     -28.2780    32.7560   -14.6780 0 CHG=0 CFG=0
M  V30 3920 H     -27.6931    32.4397   -15.3660 0 CHG=0 CFG=0
M  V30 3921 C     -26.2390    33.4890   -12.8560 0 CHG=0 CFG=0
M  V30 3922 O     -26.6310    33.6980   -11.7040 0 CHG=0 CFG=0
M  V30 3923 N     -25.4550    32.4620   -13.1830 0 CHG=0 CFG=0
M  V30 3924 H     -25.2095    32.3090   -14.1429 0 CHG=0 CFG=0
M  V30 3925 C     -24.9340    31.5350   -12.1730 0 CHG=0 CFG=1
M  V30 3926 H     -25.7673    31.2738   -11.5190 0 CHG=0 CFG=0
M  V30 3927 C     -24.4120    30.2780   -12.8520 0 CHG=0 CFG=0
M  V30 3928 H     -23.9714    29.6087   -12.1133 0 CHG=0 CFG=0
M  V30 3929 H     -23.6040    30.5470   -13.5293 0 CHG=0 CFG=0
M  V30 3930 S     -25.6470    29.3490   -13.7650 0 CHG=0 CFG=0
M  V30 3931 H     -26.4638    28.7367   -12.9055 0 CHG=0 CFG=0
M  V30 3932 C     -23.8100    32.1210   -11.3010 0 CHG=0 CFG=0
M  V30 3933 O     -23.4020    31.4970   -10.3160 0 CHG=0 CFG=0
M  V30 3934 N     -23.3190    33.3090   -11.6540 0 CHG=0 CFG=0
M  V30 3935 H     -23.7057    33.8040   -12.4362 0 CHG=0 CFG=0
M  V30 3936 C     -22.1170    33.8570   -11.0200 0 CHG=0 CFG=1
M  V30 3937 H     -21.7570    33.1156   -10.3198 0 CHG=0 CFG=0
M  V30 3938 C     -21.0050    34.1130   -12.0570 0 CHG=0 CFG=0
M  V30 3939 H     -20.0966    34.4255   -11.5447 0 CHG=0 CFG=0
M  V30 3940 H     -21.2989    34.9297   -12.7190 0 CHG=0 CFG=0
M  V30 3941 C     -20.6560    32.9070   -12.8840 0 CHG=0 CFG=0
M  V30 3942 C     -20.2410    32.8950   -14.2570 0 CHG=0 CFG=0
M  V30 3943 C     -20.0310    31.5430   -14.6180 0 CHG=0 CFG=0
M  V30 3944 C     -20.0200    33.8960   -15.2150 0 CHG=0 CFG=0
M  V30 3945 H     -20.1682    34.9348   -14.9605 0 CHG=0 CFG=0
M  V30 3946 C     -20.6780    31.5970   -12.4800 0 CHG=0 CFG=0
M  V30 3947 H     -20.9510    31.2458   -11.4961 0 CHG=0 CFG=0
M  V30 3948 N     -20.2990    30.7760   -13.5140 0 CHG=0 CFG=0
M  V30 3949 H     -20.2339    29.7980   -13.4421 0 CHG=0 CFG=0
M  V30 3950 C     -19.6130    31.1650   -15.9010 0 CHG=0 CFG=0
M  V30 3951 H     -19.4511    30.1352   -16.1737 0 CHG=0 CFG=0
M  V30 3952 C     -19.6180    33.5240   -16.4930 0 CHG=0 CFG=0
M  V30 3953 H     -19.4483    34.2880   -17.2392 0 CHG=0 CFG=0
M  V30 3954 C     -19.4100    32.1660   -16.8210 0 CHG=0 CFG=0
M  V30 3955 H     -19.0884    31.9020   -17.8178 0 CHG=0 CFG=0
M  V30 3956 C     -22.3650    35.1170   -10.1950 0 CHG=0 CFG=0
M  V30 3957 O     -21.4220    35.8480    -9.8820 0 CHG=0 CFG=0
M  V30 3958 N     -23.6220    35.3790    -9.8410 0 CHG=0 CFG=0
M  V30 3959 H     -24.3609    34.7918   -10.1726 0 CHG=0 CFG=0
M  V30 3960 C     -23.9200    36.4880    -8.9310 0 CHG=0 CFG=1
M  V30 3961 H     -23.6589    37.4072    -9.4584 0 CHG=0 CFG=0
M  V30 3962 C     -25.3960    36.5040    -8.5190 0 CHG=0 CFG=0
M  V30 3963 H     -25.5362    37.1303    -7.6351 0 CHG=0 CFG=0
M  V30 3964 H     -25.7293    35.5089    -8.2258 0 CHG=0 CFG=0
M  V30 3965 C     -26.3170    37.0400    -9.5700 0 CHG=0 CFG=0
M  V30 3966 C     -27.1410    36.4100   -10.4420 0 CHG=0 CFG=0
M  V30 3967 H     -27.3329    35.3559   -10.4802 0 CHG=0 CFG=0
M  V30 3968 N     -26.4790    38.3900    -9.7970 0 CHG=0 CFG=0
M  V30 3969 H     -26.0818    39.1155    -9.2712 0 CHG=0 CFG=0
M  V30 3970 C     -27.3550    38.5690   -10.7700 0 CHG=0 CFG=0
M  V30 3971 H     -27.6941    39.5220   -11.1509 0 CHG=0 CFG=0
M  V30 3972 N     -27.7730    37.3840   -11.1780 0 CHG=0 CFG=0
M  V30 3973 C     -23.0500    36.3560    -7.6880 0 CHG=0 CFG=0
M  V30 3974 O     -22.9130    35.2630    -7.1340 0 CHG=0 CFG=0
M  V30 3975 N     -22.4470    37.4640    -7.2670 0 CHG=0 CFG=0
M  V30 3976 H     -22.6137    38.3163    -7.7588 0 CHG=0 CFG=0
M  V30 3977 C     -21.6690    37.4930    -6.0380 0 CHG=0 CFG=1
M  V30 3978 H     -20.8107    36.8399    -6.2034 0 CHG=0 CFG=0
M  V30 3979 C     -21.2050    38.9200    -5.7250 0 CHG=0 CFG=0
M  V30 3980 H     -22.0688    39.5504    -5.5114 0 CHG=0 CFG=0
M  V30 3981 H     -20.7389    39.3594    -6.6076 0 CHG=0 CFG=0
M  V30 3982 C     -20.2430    39.0070    -4.5560 0 CHG=0 CFG=0
M  V30 3983 H     -20.6604    38.5468    -3.6597 0 CHG=0 CFG=0
M  V30 3984 H     -20.0595    40.0523    -4.3078 0 CHG=0 CFG=0
M  V30 3985 C     -18.8960    38.3780    -4.8570 0 CHG=0 CFG=0
M  V30 3986 O     -18.5240    38.2900    -6.0500 0 CHG=0 CFG=0
M  V30 3987 O     -18.2050    37.9770    -3.9000 0 CHG=-1 CFG=0
M  V30 3988 C     -22.4720    36.9400    -4.8630 0 CHG=0 CFG=0
M  V30 3989 O     -21.9920    36.0690    -4.1320 0 CHG=0 CFG=0
M  V30 3990 N     -23.6880    37.4530    -4.6930 0 CHG=0 CFG=0
M  V30 3991 H     -24.0078    38.1510    -5.3302 0 CHG=0 CFG=0
M  V30 3992 C     -24.5880    36.9960    -3.6330 0 CHG=0 CFG=1
M  V30 3993 H     -23.9890    36.8813    -2.7270 0 CHG=0 CFG=0
M  V30 3994 C     -25.6830    38.0280    -3.4050 0 CHG=0 CFG=0
M  V30 3995 H     -26.1864    38.2505    -4.3493 0 CHG=0 CFG=0
M  V30 3996 H     -25.2126    38.9615    -3.0942 0 CHG=0 CFG=0
M  V30 3997 C     -26.7400    37.6210    -2.3650 0 CHG=0 CFG=0
M  V30 3998 H     -26.2589    37.2053    -1.4789 0 CHG=0 CFG=0
M  V30 3999 H     -27.3668    36.8324    -2.7836 0 CHG=0 CFG=0
M  V30 4000 C     -27.6210    38.8070    -1.9580 0 CHG=0 CFG=0
M  V30 4001 H     -27.9349    39.3444    -2.8535 0 CHG=0 CFG=0
M  V30 4002 H     -27.0193    39.5123    -1.3837 0 CHG=0 CFG=0
M  V30 4003 C     -28.8560    38.3840    -1.1600 0 CHG=0 CFG=0
M  V30 4004 H     -28.5927    37.8144    -0.2655 0 CHG=0 CFG=0
M  V30 4005 H     -29.4838    37.7504    -1.7884 0 CHG=0 CFG=0
M  V30 4006 N     -29.6740    39.5280    -0.7760 0 CHG=1 CFG=0
M  V30 4007 H     -29.9207    40.0337    -1.6568 0 CHG=0 CFG=0
M  V30 4008 H     -29.1374    40.1640    -0.1557 0 CHG=0 CFG=0
M  V30 4009 H     -30.5434    39.2002    -0.3083 0 CHG=0 CFG=0
M  V30 4010 C     -25.2100    35.6580    -4.0120 0 CHG=0 CFG=0
M  V30 4011 O     -25.9020    35.5600    -5.0230 0 CHG=0 CFG=0
M  V30 4012 N     -24.9780    34.6320    -3.1950 0 CHG=0 CFG=0
M  V30 4013 H     -24.3667    34.7968    -2.4225 0 CHG=0 CFG=0
M  V30 4014 C     -25.4580    33.2860    -3.5180 0 CHG=0 CFG=1
M  V30 4015 H     -25.0208    33.0330    -4.4825 0 CHG=0 CFG=0
M  V30 4016 C     -25.0000    32.2780    -2.4660 0 CHG=0 CFG=0
M  V30 4017 H     -25.4036    32.5183    -1.4818 0 CHG=0 CFG=0
M  V30 4018 H     -23.9118    32.2591    -2.3892 0 CHG=0 CFG=0
M  V30 4019 H     -25.3260    31.2708    -2.7196 0 CHG=0 CFG=0
M  V30 4020 C     -26.9770    33.2440    -3.6920 0 CHG=0 CFG=0
M  V30 4021 O     -27.4770    32.5690    -4.5910 0 CHG=0 CFG=0
M  V30 4022 N     -27.7000    33.9900    -2.8540 0 CHG=0 CFG=0
M  V30 4023 H     -27.2489    34.4542    -2.0959 0 CHG=0 CFG=0
M  V30 4024 C     -29.1700    33.9940    -2.8870 0 CHG=0 CFG=1
M  V30 4025 H     -29.4822    32.9481    -2.8707 0 CHG=0 CFG=0
M  V30 4026 C     -29.7490    34.7320    -1.6690 0 CHG=0 CFG=0
M  V30 4027 H     -30.8197    34.9050    -1.7911 0 CHG=0 CFG=0
M  V30 4028 H     -29.2679    35.6978    -1.5665 0 CHG=0 CFG=0
M  V30 4029 C     -29.5690    33.9650    -0.3670 0 CHG=0 CFG=0
M  V30 4030 O     -29.3250    32.7390    -0.4030 0 CHG=0 CFG=0
M  V30 4031 O     -29.6840    34.5980     0.7080 0 CHG=-1 CFG=0
M  V30 4032 C     -29.7600    34.5870    -4.1710 0 CHG=0 CFG=0
M  V30 4033 O     -30.9480    34.4090    -4.4460 0 CHG=0 CFG=0
M  V30 4034 N     -28.9330    35.2820    -4.9490 0 CHG=0 CFG=0
M  V30 4035 H     -27.9684    35.3932    -4.7150 0 CHG=0 CFG=0
M  V30 4036 C     -29.3820    35.9000    -6.2010 0 CHG=0 CFG=1
M  V30 4037 H     -30.4536    36.0889    -6.1135 0 CHG=0 CFG=0
M  V30 4038 C     -28.6830    37.2450    -6.4180 0 CHG=0 CFG=0
M  V30 4039 H     -28.9246    37.6277    -7.4123 0 CHG=0 CFG=0
M  V30 4040 H     -27.6006    37.1149    -6.3992 0 CHG=0 CFG=0
M  V30 4041 C     -29.1110    38.2860    -5.3810 0 CHG=0 CFG=0
M  V30 4042 H     -28.8384    37.9483    -4.3839 0 CHG=0 CFG=0
M  V30 4043 H     -30.1964    38.3884    -5.3957 0 CHG=0 CFG=0
M  V30 4044 C     -28.5140    39.6630    -5.6010 0 CHG=0 CFG=0
M  V30 4045 O     -27.6220    39.8200    -6.4610 0 CHG=0 CFG=0
M  V30 4046 O     -28.9520    40.5970    -4.8980 0 CHG=-1 CFG=0
M  V30 4047 C     -29.2120    34.9910    -7.4190 0 CHG=0 CFG=0
M  V30 4048 O     -29.7140    35.2950    -8.5060 0 CHG=0 CFG=0
M  V30 4049 N     -28.5030    33.8800    -7.2320 0 CHG=0 CFG=0
M  V30 4050 H     -28.1621    33.6793    -6.3145 0 CHG=0 CFG=0
M  V30 4051 C     -28.3350    32.8940    -8.2910 0 CHG=0 CFG=1
M  V30 4052 H     -28.1323    33.4511    -9.2078 0 CHG=0 CFG=0
M  V30 4053 C     -27.1630    31.9540    -7.9830 0 CHG=0 CFG=0
M  V30 4054 H     -27.0861    31.1898    -8.7540 0 CHG=0 CFG=0
M  V30 4055 H     -27.3613    31.4368    -7.0460 0 CHG=0 CFG=0
M  V30 4056 C     -25.8310    32.6710    -7.8770 0 CHG=0 CFG=0
M  V30 4057 H     -25.9281    33.4669    -7.1363 0 CHG=0 CFG=0
M  V30 4058 H     -25.5870    33.1581    -8.8223 0 CHG=0 CFG=0
M  V30 4059 C     -24.6870    31.7540    -7.4490 0 CHG=0 CFG=0
M  V30 4060 H     -24.2688    31.1577    -8.2544 0 CHG=0 CFG=0
M  V30 4061 H     -25.0545    31.0648    -6.6889 0 CHG=0 CFG=0
M  V30 4062 N     -23.6310    32.5670    -6.8520 0 CHG=0 CFG=0
M  V30 4063 H     -23.5407    33.5022    -7.2044 0 CHG=0 CFG=0
M  V30 4064 C     -22.8360    32.1800    -5.8590 0 CHG=0 CFG=0
M  V30 4065 N     -22.9140    30.9490    -5.3610 0 CHG=1 CFG=0
M  V30 4066 H     -23.4777    30.2406    -5.7944 0 CHG=0 CFG=0
M  V30 4067 H     -22.3910    30.7071    -4.5289 0 CHG=0 CFG=0
M  V30 4068 N     -21.9440    33.0320    -5.3700 0 CHG=0 CFG=0
M  V30 4069 H     -21.8715    33.9674    -5.7326 0 CHG=0 CFG=0
M  V30 4070 H     -21.3500    32.7821    -4.5874 0 CHG=0 CFG=0
M  V30 4071 C     -29.6210    32.0920    -8.4480 0 CHG=0 CFG=0
M  V30 4072 O     -30.3160    31.8540    -7.4680 0 CHG=0 CFG=0
M  V30 4073 N     -29.9440    31.6780    -9.6840 0 CHG=0 CFG=0
M  V30 4074 C     -29.1880    31.8740   -10.9350 0 CHG=0 CFG=0
M  V30 4075 H     -28.1265    31.6573   -10.8099 0 CHG=0 CFG=0
M  V30 4076 H     -29.2964    32.9059   -11.2742 0 CHG=0 CFG=0
M  V30 4077 C     -31.1890    30.9430    -9.9150 0 CHG=0 CFG=1
M  V30 4078 H     -32.0419    31.4758    -9.4913 0 CHG=0 CFG=0
M  V30 4079 C     -31.2700    30.8860   -11.4470 0 CHG=0 CFG=0
M  V30 4080 H     -31.7760    31.7773   -11.8207 0 CHG=0 CFG=0
M  V30 4081 H     -31.8071    30.0212   -11.8412 0 CHG=0 CFG=0
M  V30 4082 C     -29.8440    30.9130   -11.8760 0 CHG=0 CFG=0
M  V30 4083 H     -29.3997    29.9222   -11.7631 0 CHG=0 CFG=0
M  V30 4084 H     -29.7242    31.2103   -12.9195 0 CHG=0 CFG=0
M  V30 4085 C     -31.1370    29.5250    -9.3440 0 CHG=0 CFG=0
M  V30 4086 O     -30.0840    29.0820    -8.8720 0 CHG=0 CFG=0
M  V30 4087 N     -32.2770    28.8410    -9.3820 0 CHG=0 CFG=0
M  V30 4088 H     -33.0750    29.2105    -9.8572 0 CHG=0 CFG=0
M  V30 4089 C     -32.3630    27.4100    -9.1000 0 CHG=0 CFG=1
M  V30 4090 H     -31.5946    27.1256    -8.3777 0 CHG=0 CFG=0
M  V30 4091 C     -33.7690    27.0340    -8.6400 0 CHG=0 CFG=2
M  V30 4092 H     -33.8049    25.9475    -8.4724 0 CHG=0 CFG=0
M  V30 4093 O     -34.6880    27.3960    -9.6740 0 CHG=0 CFG=0
M  V30 4094 H     -35.5790    27.2886    -9.3544 0 CHG=0 CFG=0
M  V30 4095 C     -34.1520    27.7480    -7.3350 0 CHG=0 CFG=0
M  V30 4096 H     -34.2309    28.8271    -7.4713 0 CHG=0 CFG=0
M  V30 4097 H     -33.3987    27.5603    -6.5697 0 CHG=0 CFG=0
M  V30 4098 H     -35.0983    27.3880    -6.9289 0 CHG=0 CFG=0
M  V30 4099 C     -32.1590    26.6550   -10.4080 0 CHG=0 CFG=0
M  V30 4100 O     -32.2630    27.2430   -11.4920 0 CHG=0 CFG=0
M  V30 4101 N     -31.9160    25.3490   -10.3280 0 CHG=0 CFG=0
M  V30 4102 H     -31.7530    24.8875    -9.4505 0 CHG=0 CFG=0
M  V30 4103 C     -31.8300    24.5530   -11.5590 0 CHG=0 CFG=1
M  V30 4104 H     -31.1344    25.0804   -12.2118 0 CHG=0 CFG=0
M  V30 4105 C     -31.2760    23.1610   -11.2870 0 CHG=0 CFG=0
M  V30 4106 H     -31.4617    22.5044   -12.1401 0 CHG=0 CFG=0
M  V30 4107 H     -31.7968    22.7177   -10.4381 0 CHG=0 CFG=0
M  V30 4108 C     -29.8060    23.1510   -11.0410 0 CHG=0 CFG=0
M  V30 4109 C     -28.9230    23.4310   -12.0770 0 CHG=0 CFG=0
M  V30 4110 H     -29.3027    23.6440   -13.0671 0 CHG=0 CFG=0
M  V30 4111 C     -29.2990    22.8790    -9.7760 0 CHG=0 CFG=0
M  V30 4112 H     -29.9709    22.6680    -8.9559 0 CHG=0 CFG=0
M  V30 4113 C     -27.5470    23.4390   -11.8550 0 CHG=0 CFG=0
M  V30 4114 H     -26.8928    23.6550   -12.6760 0 CHG=0 CFG=0
M  V30 4115 C     -27.9200    22.8710    -9.5480 0 CHG=0 CFG=0
M  V30 4116 H     -27.5466    22.6500    -8.5573 0 CHG=0 CFG=0
M  V30 4117 C     -27.0450    23.1590   -10.5900 0 CHG=0 CFG=0
M  V30 4118 H     -25.9784    23.1596   -10.4154 0 CHG=0 CFG=0
M  V30 4119 C     -33.1540    24.4950   -12.3270 0 CHG=0 CFG=0
M  V30 4120 O     -33.1520    24.4010   -13.5630 0 CHG=0 CFG=0
M  V30 4121 N     -34.2740    24.5740   -11.6090 0 CHG=0 CFG=0
M  V30 4122 H     -34.1591    24.5294   -10.6189 0 CHG=0 CFG=0
M  V30 4123 C     -35.5770    24.6370   -12.2690 0 CHG=0 CFG=1
M  V30 4124 H     -35.6359    23.7561   -12.9144 0 CHG=0 CFG=0
M  V30 4125 C     -36.7240    24.6120   -11.2580 0 CHG=0 CFG=0
M  V30 4126 H     -36.6283    25.4310   -10.5514 0 CHG=0 CFG=0
M  V30 4127 H     -36.6362    23.6913   -10.6781 0 CHG=0 CFG=0
M  V30 4128 C     -38.0930    24.6610   -11.9120 0 CHG=0 CFG=0
M  V30 4129 H     -38.1211    23.8679   -12.6614 0 CHG=0 CFG=0
M  V30 4130 H     -38.2288    25.6005   -12.4502 0 CHG=0 CFG=0
M  V30 4131 C     -39.2080    24.4780   -10.9100 0 CHG=0 CFG=0
M  V30 4132 H     -39.2388    25.3345   -10.2346 0 CHG=0 CFG=0
M  V30 4133 H     -39.0143    23.6013   -10.2888 0 CHG=0 CFG=0
M  V30 4134 C     -40.5420    24.3250   -11.6210 0 CHG=0 CFG=0
M  V30 4135 H     -40.7334    25.1854   -12.2665 0 CHG=0 CFG=0
M  V30 4136 H     -41.3560    24.2729   -10.8954 0 CHG=0 CFG=0
M  V30 4137 N     -40.5920    23.0900   -12.4610 0 CHG=1 CFG=0
M  V30 4138 H     -40.4667    22.2392   -11.8721 0 CHG=0 CFG=0
M  V30 4139 H     -39.7793    23.0804   -13.1193 0 CHG=0 CFG=0
M  V30 4140 H     -41.4714    23.0117   -13.0088 0 CHG=0 CFG=0
M  V30 4141 C     -35.6550    25.8810   -13.1500 0 CHG=0 CFG=0
M  V30 4142 O     -36.0670    25.8060   -14.3110 0 CHG=0 CFG=0
M  V30 4143 N     -35.2280    27.0190   -12.6020 0 CHG=0 CFG=0
M  V30 4144 H     -34.7980    27.0010   -11.6980 0 CHG=0 CFG=0
M  V30 4145 C     -35.2590    28.2770   -13.3510 0 CHG=0 CFG=1
M  V30 4146 H     -36.2578    28.3555   -13.7857 0 CHG=0 CFG=0
M  V30 4147 C     -35.0090    29.4940   -12.4340 0 CHG=0 CFG=1
M  V30 4148 H     -34.1255    29.2881   -11.8279 0 CHG=0 CFG=0
M  V30 4149 C     -34.7470    30.7510   -13.2660 0 CHG=0 CFG=0
M  V30 4150 H     -35.5457    30.9291   -13.9881 0 CHG=0 CFG=0
M  V30 4151 H     -33.8098    30.6948   -13.8212 0 CHG=0 CFG=0
M  V30 4152 H     -34.6702    31.6360   -12.6353 0 CHG=0 CFG=0
M  V30 4153 C     -36.2200    29.6970   -11.5130 0 CHG=0 CFG=0
M  V30 4154 H     -36.5943    28.7332   -11.1729 0 CHG=0 CFG=0
M  V30 4155 H     -37.0397    30.1337   -12.0854 0 CHG=0 CFG=0
M  V30 4156 C     -35.9490    30.5510   -10.2890 0 CHG=0 CFG=0
M  V30 4157 H     -35.6524    31.5622   -10.5679 0 CHG=0 CFG=0
M  V30 4158 H     -35.1498    30.1245    -9.6828 0 CHG=0 CFG=0
M  V30 4159 H     -36.8379    30.6292    -9.6630 0 CHG=0 CFG=0
M  V30 4160 C     -34.2790    28.2350   -14.5270 0 CHG=0 CFG=0
M  V30 4161 O     -34.6260    28.6190   -15.6500 0 CHG=0 CFG=0
M  V30 4162 N     -33.0670    27.7460   -14.2820 0 CHG=0 CFG=0
M  V30 4163 H     -32.8199    27.4843   -13.3489 0 CHG=0 CFG=0
M  V30 4164 C     -32.1070    27.5800   -15.3680 0 CHG=0 CFG=1
M  V30 4165 H     -31.9283    28.5743   -15.7781 0 CHG=0 CFG=0
M  V30 4166 C     -30.8070    26.9620   -14.8540 0 CHG=0 CFG=0
M  V30 4167 H     -30.2169    26.5809   -15.6911 0 CHG=0 CFG=0
M  V30 4168 H     -31.0617    26.0783   -14.2672 0 CHG=0 CFG=0
M  V30 4169 C     -29.9050    27.8810   -14.0260 0 CHG=0 CFG=0
M  V30 4170 H     -30.5144    28.4021   -13.2868 0 CHG=0 CFG=0
M  V30 4171 C     -28.8480    27.0800   -13.2760 0 CHG=0 CFG=0
M  V30 4172 H     -28.2735    26.4568   -13.9567 0 CHG=0 CFG=0
M  V30 4173 H     -29.3046    26.4216   -12.5372 0 CHG=0 CFG=0
M  V30 4174 H     -28.1563    27.7327   -12.7451 0 CHG=0 CFG=0
M  V30 4175 C     -29.2520    28.9110   -14.9400 0 CHG=0 CFG=0
M  V30 4176 H     -29.9890    29.5585   -15.4133 0 CHG=0 CFG=0
M  V30 4177 H     -28.6653    28.4353   -15.7266 0 CHG=0 CFG=0
M  V30 4178 H     -28.5776    29.5610   -14.3811 0 CHG=0 CFG=0
M  V30 4179 C     -32.6580    26.7210   -16.4960 0 CHG=0 CFG=0
M  V30 4180 O     -32.4540    27.0370   -17.6720 0 CHG=0 CFG=0
M  V30 4181 N     -33.3420    25.6330   -16.1390 0 CHG=0 CFG=0
M  V30 4182 H     -33.4271    25.4072   -15.1682 0 CHG=0 CFG=0
M  V30 4183 C     -33.8870    24.7130   -17.1370 0 CHG=0 CFG=1
M  V30 4184 H     -33.0461    24.4088   -17.7622 0 CHG=0 CFG=0
M  V30 4185 C     -34.5160    23.4880   -16.4710 0 CHG=0 CFG=0
M  V30 4186 H     -35.2762    23.8231   -15.7639 0 CHG=0 CFG=0
M  V30 4187 H     -33.7574    22.9938   -15.8619 0 CHG=0 CFG=0
M  V30 4188 C     -35.1400    22.4560   -17.4130 0 CHG=0 CFG=0
M  V30 4189 H     -35.9195    22.9420   -18.0008 0 CHG=0 CFG=0
M  V30 4190 C     -34.1140    21.8720   -18.3950 0 CHG=0 CFG=0
M  V30 4191 H     -33.2808    21.4067   -17.8667 0 CHG=0 CFG=0
M  V30 4192 H     -33.7114    22.6385   -19.0577 0 CHG=0 CFG=0
M  V30 4193 H     -34.5687    21.1070   -19.0260 0 CHG=0 CFG=0
M  V30 4194 C     -35.8170    21.3640   -16.6090 0 CHG=0 CFG=0
M  V30 4195 H     -36.5407    21.7649   -15.8989 0 CHG=0 CFG=0
M  V30 4196 H     -35.0798    20.7950   -16.0408 0 CHG=0 CFG=0
M  V30 4197 H     -36.3387    20.6590   -17.2564 0 CHG=0 CFG=0
M  V30 4198 C     -34.9120    25.4190   -18.0230 0 CHG=0 CFG=0
M  V30 4199 O     -34.9120    25.2420   -19.2590 0 CHG=0 CFG=0
M  V30 4200 N     -35.7880    26.1980   -17.3880 0 CHG=0 CFG=0
M  V30 4201 H     -35.7228    26.2460   -16.3899 0 CHG=0 CFG=0
M  V30 4202 C     -36.7840    26.9850   -18.1080 0 CHG=0 CFG=1
M  V30 4203 H     -37.3643    26.2771   -18.7033 0 CHG=0 CFG=0
M  V30 4204 C     -37.6920    27.7320   -17.1310 0 CHG=0 CFG=0
M  V30 4205 H     -37.1372    28.4953   -16.5778 0 CHG=0 CFG=0
M  V30 4206 H     -38.1121    27.0410   -16.4011 0 CHG=0 CFG=0
M  V30 4207 O     -38.7710    28.3490   -17.8120 0 CHG=0 CFG=0
M  V30 4208 H     -38.5099    28.7161   -18.6665 0 CHG=0 CFG=0
M  V30 4209 C     -36.0990    27.9640   -19.0580 0 CHG=0 CFG=0
M  V30 4210 O     -36.5090    28.1110   -20.2060 0 CHG=0 CFG=0
M  V30 4211 N     -35.0410    28.6190   -18.5800 0 CHG=0 CFG=0
M  V30 4212 H     -34.7666    28.4660   -17.6298 0 CHG=0 CFG=0
M  V30 4213 C     -34.3010    29.5620   -19.4200 0 CHG=0 CFG=1
M  V30 4214 H     -35.0482    30.2156   -19.8788 0 CHG=0 CFG=0
M  V30 4215 C     -33.2940    30.3680   -18.5890 0 CHG=0 CFG=0
M  V30 4216 H     -32.6727    30.9727   -19.2479 0 CHG=0 CFG=0
M  V30 4217 H     -32.6298    29.7087   -18.0303 0 CHG=0 CFG=0
M  V30 4218 C     -33.9810    31.3310   -17.6160 0 CHG=0 CFG=0
M  V30 4219 O     -33.4048    31.7271   -16.5995 0 CHG=0 CFG=0
M  V30 4220 N     -35.2173    31.6954   -17.9189 0 CHG=0 CFG=0
M  V30 4221 H     -35.7191    31.3986   -18.7358 0 CHG=0 CFG=0
M  V30 4222 H     -35.6917    32.3212   -17.3064 0 CHG=0 CFG=0
M  V30 4223 C     -33.6430    28.8980   -20.6340 0 CHG=0 CFG=0
M  V30 4224 O     -33.6900    29.4300   -21.7550 0 CHG=0 CFG=0
M  V30 4225 N     -33.0580    27.7240   -20.4100 0 CHG=0 CFG=0
M  V30 4226 H     -33.0695    27.3581   -19.4795 0 CHG=0 CFG=0
M  V30 4227 C     -32.4510    26.9470   -21.4840 0 CHG=0 CFG=1
M  V30 4228 H     -31.7774    27.6239   -22.0132 0 CHG=0 CFG=0
M  V30 4229 C     -31.6510    25.7500   -20.9260 0 CHG=0 CFG=1
M  V30 4230 H     -32.2920    25.2102   -20.2263 0 CHG=0 CFG=0
M  V30 4231 C     -31.2610    24.7910   -22.0420 0 CHG=0 CFG=0
M  V30 4232 H     -30.7529    25.3111   -22.8530 0 CHG=0 CFG=0
M  V30 4233 H     -32.1278    24.2857   -22.4703 0 CHG=0 CFG=0
M  V30 4234 H     -30.5950    24.0074   -21.6868 0 CHG=0 CFG=0
M  V30 4235 C     -30.4150    26.2570   -20.1660 0 CHG=0 CFG=0
M  V30 4236 H     -30.7100    27.0468   -19.4750 0 CHG=0 CFG=0
M  V30 4237 H     -29.7196    26.7216   -20.8658 0 CHG=0 CFG=0
M  V30 4238 C     -29.6910    25.1870   -19.3590 0 CHG=0 CFG=0
M  V30 4239 H     -29.2691    24.4082   -19.9932 0 CHG=0 CFG=0
M  V30 4240 H     -30.3683    24.7116   -18.6478 0 CHG=0 CFG=0
M  V30 4241 H     -28.8724    25.6259   -18.7887 0 CHG=0 CFG=0
M  V30 4242 C     -33.5100    26.5040   -22.4940 0 CHG=0 CFG=0
M  V30 4243 O     -33.3140    26.6290   -23.6980 0 CHG=0 CFG=0
M  V30 4244 N     -34.6440    26.0100   -22.0040 0 CHG=0 CFG=0
M  V30 4245 H     -34.7873    25.9732   -21.0171 0 CHG=0 CFG=0
M  V30 4246 C     -35.7260    25.6260   -22.9020 0 CHG=0 CFG=1
M  V30 4247 H     -35.3076    24.8953   -23.5951 0 CHG=0 CFG=0
M  V30 4248 C     -36.8910    24.9960   -22.1290 0 CHG=0 CFG=0
M  V30 4249 H     -37.7702    24.9484   -22.7757 0 CHG=0 CFG=0
M  V30 4250 H     -37.1652    25.6799   -21.3236 0 CHG=0 CFG=0
M  V30 4251 C     -36.6180    23.5950   -21.5600 0 CHG=0 CFG=0
M  V30 4252 H     -35.6340    23.6006   -21.0892 0 CHG=0 CFG=0
M  V30 4253 C     -37.6210    23.2280   -20.4890 0 CHG=0 CFG=0
M  V30 4254 H     -38.6346    23.2078   -20.8907 0 CHG=0 CFG=0
M  V30 4255 H     -37.5994    23.9545   -19.6761 0 CHG=0 CFG=0
M  V30 4256 H     -37.4038    22.2492   -20.0607 0 CHG=0 CFG=0
M  V30 4257 C     -36.6130    22.5420   -22.6610 0 CHG=0 CFG=0
M  V30 4258 H     -35.7931    22.7016   -23.3619 0 CHG=0 CFG=0
M  V30 4259 H     -37.5401    22.5783   -23.2349 0 CHG=0 CFG=0
M  V30 4260 H     -36.5232    21.5367   -22.2520 0 CHG=0 CFG=0
M  V30 4261 C     -36.1820    26.8170   -23.7600 0 CHG=0 CFG=0
M  V30 4262 O     -36.3900    26.6730   -24.9730 0 CHG=0 CFG=0
M  V30 4263 N     -36.2920    27.9900   -23.1340 0 CHG=0 CFG=0
M  V30 4264 H     -36.2511    28.0442   -22.1388 0 CHG=0 CFG=0
M  V30 4265 C     -36.7150    29.2080   -23.8290 0 CHG=0 CFG=1
M  V30 4266 H     -37.6853    28.9947   -24.2836 0 CHG=0 CFG=0
M  V30 4267 C     -36.8070    30.3960   -22.8590 0 CHG=0 CFG=0
M  V30 4268 H     -36.8614    31.3270   -23.4274 0 CHG=0 CFG=0
M  V30 4269 H     -35.9206    30.4607   -22.2312 0 CHG=0 CFG=0
M  V30 4270 C     -38.0550    30.3640   -21.9790 0 CHG=0 CFG=0
M  V30 4271 O     -38.9600    29.5340   -22.2070 0 CHG=0 CFG=0
M  V30 4272 O     -38.1290    31.1970   -21.0480 0 CHG=-1 CFG=0
M  V30 4273 C     -35.7590    29.5450   -24.9750 0 CHG=0 CFG=0
M  V30 4274 O     -36.2040    29.8600   -26.0830 0 CHG=0 CFG=0
M  V30 4275 N     -34.4540    29.4680   -24.7070 0 CHG=0 CFG=0
M  V30 4276 H     -34.2353    29.2390   -23.7592 0 CHG=0 CFG=0
M  V30 4277 C     -33.4470    29.7490   -25.7360 0 CHG=0 CFG=1
M  V30 4278 H     -33.7206    30.7149   -26.1666 0 CHG=0 CFG=0
M  V30 4279 C     -32.0120    29.8240   -25.1580 0 CHG=0 CFG=0
M  V30 4280 H     -31.8078    28.9000   -24.6143 0 CHG=0 CFG=0
M  V30 4281 C     -30.9770    29.9670   -26.2780 0 CHG=0 CFG=0
M  V30 4282 H     -31.1996    30.8269   -26.9120 0 CHG=0 CFG=0
M  V30 4283 H     -30.9418    29.0918   -26.9272 0 CHG=0 CFG=0
M  V30 4284 H     -29.9805    30.0973   -25.8651 0 CHG=0 CFG=0
M  V30 4285 C     -31.9000    30.9890   -24.1970 0 CHG=0 CFG=0
M  V30 4286 H     -32.5728    30.8674   -23.3495 0 CHG=0 CFG=0
M  V30 4287 H     -32.1820    31.9180   -24.6915 0 CHG=0 CFG=0
M  V30 4288 H     -30.8879    31.0978   -23.8098 0 CHG=0 CFG=0
M  V30 4289 C     -33.5120    28.7320   -26.8700 0 CHG=0 CFG=0
M  V30 4290 O     -33.3800    29.0940   -28.0390 0 CHG=0 CFG=0
M  V30 4291 N     -33.7370    27.4650   -26.5300 0 CHG=0 CFG=0
M  V30 4292 H     -33.9313    27.2509   -25.5721 0 CHG=0 CFG=0
M  V30 4293 C     -33.9350    26.4360   -27.5500 0 CHG=0 CFG=1
M  V30 4294 H     -33.0309    26.4207   -28.1600 0 CHG=0 CFG=0
M  V30 4295 C     -34.1730    25.0760   -26.9070 0 CHG=0 CFG=0
M  V30 4296 H     -34.5287    24.3837   -27.6731 0 CHG=0 CFG=0
M  V30 4297 H     -34.9709    25.1324   -26.1674 0 CHG=0 CFG=0
M  V30 4298 C     -32.9310    24.4970   -26.3040 0 CHG=0 CFG=0
M  V30 4299 H     -32.5861    25.0675   -25.4428 0 CHG=0 CFG=0
M  V30 4300 H     -32.1305    24.5227   -27.0420 0 CHG=0 CFG=0
M  V30 4301 S     -33.1940    22.7930   -25.8430 0 CHG=0 CFG=0
M  V30 4302 C     -31.4910    22.3080   -25.6240 0 CHG=0 CFG=0
M  V30 4303 H     -31.0398    22.8559   -24.7986 0 CHG=0 CFG=0
M  V30 4304 H     -30.9158    22.4958   -26.5308 0 CHG=0 CFG=0
M  V30 4305 H     -31.4808    21.2447   -25.4048 0 CHG=0 CFG=0
M  V30 4306 C     -35.0950    26.7740   -28.4830 0 CHG=0 CFG=0
M  V30 4307 O     -35.0000    26.5930   -29.7020 0 CHG=0 CFG=0
M  V30 4308 N     -36.1820    27.2750   -27.9020 0 CHG=0 CFG=0
M  V30 4309 H     -36.2695    27.3360   -26.9075 0 CHG=0 CFG=0
M  V30 4310 C     -37.3700    27.6330   -28.6680 0 CHG=0 CFG=1
M  V30 4311 H     -37.5639    26.8115   -29.3610 0 CHG=0 CFG=0
M  V30 4312 C     -38.5540    27.8630   -27.7300 0 CHG=0 CFG=0
M  V30 4313 H     -39.3422    28.4146   -28.2434 0 CHG=0 CFG=0
M  V30 4314 H     -38.2569    28.4652   -26.8703 0 CHG=0 CFG=0
M  V30 4315 C     -39.1800    26.5680   -27.2500 0 CHG=0 CFG=0
M  V30 4316 O     -38.8320    25.4940   -27.7940 0 CHG=0 CFG=0
M  V30 4317 O     -40.0300    26.6330   -26.3330 0 CHG=-1 CFG=0
M  V30 4318 C     -37.1470    28.8540   -29.5500 0 CHG=0 CFG=0
M  V30 4319 O     -37.7160    28.9490   -30.6370 0 CHG=0 CFG=0
M  V30 4320 N     -36.3210    29.7810   -29.0710 0 CHG=0 CFG=0
M  V30 4321 H     -36.0105    29.6421   -28.1301 0 CHG=0 CFG=0
M  V30 4322 C     -35.9960    31.0020   -29.8080 0 CHG=0 CFG=1
M  V30 4323 H     -36.8777    31.2845   -30.3855 0 CHG=0 CFG=0
M  V30 4324 C     -35.6250    32.1260   -28.8330 0 CHG=0 CFG=0
M  V30 4325 H     -35.1068    32.9270   -29.3578 0 CHG=0 CFG=0
M  V30 4326 H     -34.9093    31.7156   -28.1171 0 CHG=0 CFG=0
M  V30 4327 C     -36.8310    32.7090   -28.1020 0 CHG=0 CFG=0
M  V30 4328 H     -37.5743    31.9196   -27.9670 0 CHG=0 CFG=0
M  V30 4329 H     -37.3168    33.4810   -28.6960 0 CHG=0 CFG=0
M  V30 4330 C     -36.5070    33.2520   -26.7190 0 CHG=0 CFG=0
M  V30 4331 O     -35.5030    33.9810   -26.5720 0 CHG=0 CFG=0
M  V30 4332 O     -37.2730    32.9590   -25.7750 0 CHG=-1 CFG=0
M  V30 4333 C     -34.8680    30.7520   -30.8020 0 CHG=0 CFG=0
M  V30 4334 O     -34.7220    31.4870   -31.7870 0 CHG=0 CFG=0
M  V30 4335 N     -34.1020    29.6920   -30.5350 0 CHG=0 CFG=0
M  V30 4336 H     -34.3473    29.1046   -29.7682 0 CHG=0 CFG=0
M  V30 4337 C     -32.9060    29.3010   -31.2940 0 CHG=0 CFG=1
M  V30 4338 H     -32.5043    28.4508   -30.7431 0 CHG=0 CFG=0
M  V30 4339 C     -33.2400    28.8610   -32.7270 0 CHG=0 CFG=0
M  V30 4340 H     -32.3030    28.7419   -33.2697 0 CHG=0 CFG=0
M  V30 4341 H     -33.7672    29.6552   -33.2565 0 CHG=0 CFG=0
M  V30 4342 C     -33.9590    27.5140   -32.8250 0 CHG=0 CFG=0
M  V30 4343 H     -33.8296    26.9365   -31.9094 0 CHG=0 CFG=0
M  V30 4344 H     -33.5284    26.9213   -33.6297 0 CHG=0 CFG=0
M  V30 4345 C     -35.4500    27.6480   -33.1320 0 CHG=0 CFG=0
M  V30 4346 O     -35.8230    28.4940   -33.9810 0 CHG=0 CFG=0
M  V30 4347 O     -36.2510    26.8890   -32.5420 0 CHG=-1 CFG=0
M  V30 4348 C     -31.8330    30.3860   -31.2860 0 CHG=0 CFG=0
M  V30 4349 O     -31.2950    30.7190   -30.2310 0 CHG=0 CFG=0
M  V30 4350 O     -31.4980    30.9350   -32.3340 0 CHG=-1 CFG=0
M  V30 END ATOM
M  V30 BEGIN BOND
M  V30 1 1 1 2 CFG=0
M  V30 2 1 1 3 CFG=0
M  V30 3 1 1 4 CFG=0
M  V30 4 1 1 5 CFG=0
M  V30 5 1 5 6 CFG=0
M  V30 6 1 5 7 CFG=0
M  V30 7 1 5 22 CFG=0
M  V30 8 1 7 8 CFG=0
M  V30 9 1 7 9 CFG=0
M  V30 10 1 7 10 CFG=0
M  V30 11 2 10 11 CFG=0
M  V30 12 1 10 15 CFG=0
M  V30 13 1 11 12 CFG=0
M  V30 14 1 11 13 CFG=0
M  V30 15 1 13 14 CFG=0
M  V30 16 2 13 19 CFG=0
M  V30 17 1 15 16 CFG=0
M  V30 18 2 15 17 CFG=0
M  V30 19 1 17 18 CFG=0
M  V30 20 1 17 19 CFG=0
M  V30 21 1 19 20 CFG=0
M  V30 22 1 20 21 CFG=0
M  V30 23 2 22 23 CFG=0
M  V30 24 1 24 25 CFG=0
M  V30 25 1 24 26 CFG=0
M  V30 26 1 26 27 CFG=0
M  V30 27 1 26 28 CFG=0
M  V30 28 1 26 29 CFG=0
M  V30 29 2 29 30 CFG=0
M  V30 30 1 31 32 CFG=0
M  V30 31 1 31 33 CFG=0
M  V30 32 1 33 34 CFG=0
M  V30 33 1 33 35 CFG=0
M  V30 34 1 33 40 CFG=0
M  V30 35 1 35 36 CFG=0
M  V30 36 1 35 37 CFG=0
M  V30 37 1 35 38 CFG=0
M  V30 38 1 38 39 CFG=0
M  V30 39 2 40 41 CFG=0
M  V30 40 1 42 43 CFG=0
M  V30 41 1 42 44 CFG=0
M  V30 42 1 44 45 CFG=0
M  V30 43 1 44 46 CFG=0
M  V30 44 1 44 64 CFG=0
M  V30 45 1 46 47 CFG=0
M  V30 46 1 46 48 CFG=0
M  V30 47 1 46 49 CFG=0
M  V30 48 1 49 50 CFG=0
M  V30 49 2 49 54 CFG=0
M  V30 50 2 50 51 CFG=0
M  V30 51 1 50 52 CFG=0
M  V30 52 1 51 58 CFG=0
M  V30 53 1 52 53 CFG=0
M  V30 54 2 52 60 CFG=0
M  V30 55 1 54 55 CFG=0
M  V30 56 1 54 56 CFG=0
M  V30 57 1 56 51 CFG=0
M  V30 58 1 56 57 CFG=0
M  V30 59 1 58 59 CFG=0
M  V30 60 2 58 62 CFG=0
M  V30 61 1 60 61 CFG=0
M  V30 62 1 60 62 CFG=0
M  V30 63 1 62 63 CFG=0
M  V30 64 2 64 65 CFG=0
M  V30 65 1 66 67 CFG=0
M  V30 66 1 66 68 CFG=0
M  V30 67 1 68 69 CFG=0
M  V30 68 1 68 70 CFG=0
M  V30 69 1 68 79 CFG=0
M  V30 70 1 70 71 CFG=0
M  V30 71 1 70 72 CFG=0
M  V30 72 1 70 73 CFG=0
M  V30 73 1 73 74 CFG=0
M  V30 74 1 73 75 CFG=0
M  V30 75 1 73 76 CFG=0
M  V30 76 2 76 77 CFG=0
M  V30 77 1 76 78 CFG=0
M  V30 78 2 79 80 CFG=0
M  V30 79 1 81 82 CFG=0
M  V30 80 1 81 83 CFG=0
M  V30 81 1 83 84 CFG=0
M  V30 82 1 83 85 CFG=0
M  V30 83 1 83 98 CFG=0
M  V30 84 1 85 86 CFG=0
M  V30 85 1 85 87 CFG=0
M  V30 86 1 85 91 CFG=0
M  V30 87 1 87 88 CFG=0
M  V30 88 1 87 89 CFG=0
M  V30 89 1 87 90 CFG=0
M  V30 90 1 91 92 CFG=0
M  V30 91 1 91 93 CFG=0
M  V30 92 1 91 94 CFG=0
M  V30 93 1 94 95 CFG=0
M  V30 94 1 94 96 CFG=0
M  V30 95 1 94 97 CFG=0
M  V30 96 2 98 99 CFG=0
M  V30 97 1 100 101 CFG=0
M  V30 98 1 100 102 CFG=0
M  V30 99 1 102 103 CFG=0
M  V30 100 1 102 104 CFG=0
M  V30 101 1 102 110 CFG=0
M  V30 102 1 104 105 CFG=0
M  V30 103 1 104 106 CFG=0
M  V30 104 1 104 107 CFG=0
M  V30 105 2 107 108 CFG=0
M  V30 106 1 107 109 CFG=0
M  V30 107 2 110 111 CFG=0
M  V30 108 1 112 116 CFG=0
M  V30 109 1 113 112 CFG=0
M  V30 110 1 113 114 CFG=0
M  V30 111 1 113 115 CFG=0
M  V30 112 1 116 117 CFG=0
M  V30 113 1 116 118 CFG=0
M  V30 114 1 116 124 CFG=0
M  V30 115 1 118 119 CFG=0
M  V30 116 1 118 120 CFG=0
M  V30 117 1 118 121 CFG=0
M  V30 118 1 121 113 CFG=0
M  V30 119 1 121 122 CFG=0
M  V30 120 1 121 123 CFG=0
M  V30 121 2 124 125 CFG=0
M  V30 122 1 126 127 CFG=0
M  V30 123 1 126 128 CFG=0
M  V30 124 1 128 129 CFG=0
M  V30 125 1 128 130 CFG=0
M  V30 126 1 128 146 CFG=0
M  V30 127 1 130 131 CFG=0
M  V30 128 1 130 132 CFG=0
M  V30 129 1 130 133 CFG=0
M  V30 130 1 133 134 CFG=0
M  V30 131 1 133 135 CFG=0
M  V30 132 1 133 136 CFG=0
M  V30 133 1 136 137 CFG=0
M  V30 134 1 136 138 CFG=0
M  V30 135 1 136 139 CFG=0
M  V30 136 1 139 140 CFG=0
M  V30 137 1 139 141 CFG=0
M  V30 138 1 139 142 CFG=0
M  V30 139 1 142 143 CFG=0
M  V30 140 1 142 144 CFG=0
M  V30 141 1 142 145 CFG=0
M  V30 142 2 146 147 CFG=0
M  V30 143 1 148 149 CFG=0
M  V30 144 1 148 150 CFG=0
M  V30 145 1 150 151 CFG=0
M  V30 146 1 150 152 CFG=0
M  V30 147 1 150 158 CFG=0
M  V30 148 1 152 153 CFG=0
M  V30 149 1 152 154 CFG=0
M  V30 150 1 152 155 CFG=0
M  V30 151 2 155 156 CFG=0
M  V30 152 1 155 157 CFG=0
M  V30 153 2 158 159 CFG=0
M  V30 154 1 160 161 CFG=0
M  V30 155 1 160 162 CFG=0
M  V30 156 1 162 163 CFG=0
M  V30 157 1 162 164 CFG=0
M  V30 158 1 162 177 CFG=0
M  V30 159 1 164 165 CFG=0
M  V30 160 1 164 166 CFG=0
M  V30 161 1 164 167 CFG=0
M  V30 162 1 167 168 CFG=0
M  V30 163 1 167 169 CFG=0
M  V30 164 1 167 173 CFG=0
M  V30 165 1 169 170 CFG=0
M  V30 166 1 169 171 CFG=0
M  V30 167 1 169 172 CFG=0
M  V30 168 1 173 174 CFG=0
M  V30 169 1 173 175 CFG=0
M  V30 170 1 173 176 CFG=0
M  V30 171 2 177 178 CFG=0
M  V30 172 1 179 180 CFG=0
M  V30 173 1 179 181 CFG=0
M  V30 174 1 181 182 CFG=0
M  V30 175 1 181 183 CFG=0
M  V30 176 1 181 191 CFG=0
M  V30 177 1 183 184 CFG=0
M  V30 178 1 183 185 CFG=0
M  V30 179 1 183 187 CFG=0
M  V30 180 1 185 186 CFG=0
M  V30 181 1 187 188 CFG=0
M  V30 182 1 187 189 CFG=0
M  V30 183 1 187 190 CFG=0
M  V30 184 2 191 192 CFG=0
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M  V30 740 2 777 778 CFG=0
M  V30 741 1 777 779 CFG=0
M  V30 742 2 780 781 CFG=0
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M  V30 748 1 786 787 CFG=0
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M  V30 750 1 786 789 CFG=0
M  V30 751 1 789 790 CFG=0
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M  V30 754 2 792 793 CFG=0
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M  V30 756 2 795 796 CFG=0
M  V30 757 1 797 798 CFG=0
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M  V30 759 1 799 800 CFG=0
M  V30 760 1 799 801 CFG=0
M  V30 761 1 799 815 CFG=0
M  V30 762 1 801 802 CFG=0
M  V30 763 1 801 803 CFG=0
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M  V30 765 2 804 805 CFG=0
M  V30 766 1 804 807 CFG=0
M  V30 767 1 805 806 CFG=0
M  V30 768 1 805 809 CFG=0
M  V30 769 1 807 808 CFG=0
M  V30 770 2 807 811 CFG=0
M  V30 771 1 809 810 CFG=0
M  V30 772 2 809 813 CFG=0
M  V30 773 1 811 812 CFG=0
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M  V30 779 1 819 820 CFG=0
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M  V30 823 1 866 867 CFG=0
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M  V30 828 1 870 871 CFG=0
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M  V30 883 2 929 930 CFG=0
M  V30 884 1 931 932 CFG=0
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M  V30 889 1 935 936 CFG=0
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M  V30 891 1 935 938 CFG=0
M  V30 892 1 938 939 CFG=0
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M  V30 895 1 941 942 CFG=0
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M  V30 900 1 948 949 CFG=0
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M  V30 902 1 950 951 CFG=0
M  V30 903 1 950 952 CFG=0
M  V30 904 1 950 960 CFG=0
M  V30 905 1 952 953 CFG=0
M  V30 906 1 952 954 CFG=0
M  V30 907 1 952 955 CFG=0
M  V30 908 2 955 956 CFG=0
M  V30 909 1 955 957 CFG=0
M  V30 910 1 957 958 CFG=0
M  V30 911 1 957 959 CFG=0
M  V30 912 2 960 961 CFG=0
M  V30 913 1 962 963 CFG=0
M  V30 914 1 962 964 CFG=0
M  V30 915 1 964 965 CFG=0
M  V30 916 1 964 966 CFG=0
M  V30 917 1 964 979 CFG=0
M  V30 918 1 966 967 CFG=0
M  V30 919 1 966 968 CFG=0
M  V30 920 1 966 969 CFG=0
M  V30 921 1 969 970 CFG=0
M  V30 922 1 969 971 CFG=0
M  V30 923 1 969 975 CFG=0
M  V30 924 1 971 972 CFG=0
M  V30 925 1 971 973 CFG=0
M  V30 926 1 971 974 CFG=0
M  V30 927 1 975 976 CFG=0
M  V30 928 1 975 977 CFG=0
M  V30 929 1 975 978 CFG=0
M  V30 930 2 979 980 CFG=0
M  V30 931 1 981 982 CFG=0
M  V30 932 1 981 983 CFG=0
M  V30 933 1 983 984 CFG=0
M  V30 934 1 983 985 CFG=0
M  V30 935 1 983 990 CFG=0
M  V30 936 1 985 986 CFG=0
M  V30 937 1 985 987 CFG=0
M  V30 938 1 985 988 CFG=0
M  V30 939 1 988 989 CFG=0
M  V30 940 2 990 991 CFG=0
M  V30 941 1 992 993 CFG=0
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M  V30 943 1 994 995 CFG=0
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M  V30 945 1 994 1007 CFG=0
M  V30 946 1 996 997 CFG=0
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M  V30 948 1 996 999 CFG=0
M  V30 949 1 999 1000 CFG=0
M  V30 950 2 999 1005 CFG=0
M  V30 951 2 1000 1001 CFG=0
M  V30 952 1 1001 1002 CFG=0
M  V30 953 1 1001 1003 CFG=0
M  V30 954 1 1003 1004 CFG=0
M  V30 955 1 1005 1003 CFG=0
M  V30 956 1 1005 1006 CFG=0
M  V30 957 2 1007 1008 CFG=0
M  V30 958 1 1009 1010 CFG=0
M  V30 959 1 1009 1011 CFG=0
M  V30 960 1 1011 1012 CFG=0
M  V30 961 1 1011 1013 CFG=0
M  V30 962 1 1011 1022 CFG=0
M  V30 963 1 1013 1014 CFG=0
M  V30 964 1 1013 1015 CFG=0
M  V30 965 1 1013 1016 CFG=0
M  V30 966 1 1016 1017 CFG=0
M  V30 967 1 1016 1018 CFG=0
M  V30 968 1 1016 1019 CFG=0
M  V30 969 2 1019 1020 CFG=0
M  V30 970 1 1019 1021 CFG=0
M  V30 971 2 1022 1023 CFG=0
M  V30 972 1 1024 1025 CFG=0
M  V30 973 1 1024 1026 CFG=0
M  V30 974 1 1026 1027 CFG=0
M  V30 975 1 1026 1028 CFG=0
M  V30 976 1 1026 1044 CFG=0
M  V30 977 1 1028 1029 CFG=0
M  V30 978 1 1028 1030 CFG=0
M  V30 979 1 1028 1031 CFG=0
M  V30 980 1 1031 1032 CFG=0
M  V30 981 1 1031 1033 CFG=0
M  V30 982 1 1031 1034 CFG=0
M  V30 983 1 1034 1035 CFG=0
M  V30 984 1 1034 1036 CFG=0
M  V30 985 1 1034 1037 CFG=0
M  V30 986 1 1037 1038 CFG=0
M  V30 987 1 1037 1039 CFG=0
M  V30 988 1 1037 1040 CFG=0
M  V30 989 1 1040 1041 CFG=0
M  V30 990 1 1040 1042 CFG=0
M  V30 991 1 1040 1043 CFG=0
M  V30 992 2 1044 1045 CFG=0
M  V30 993 1 1046 1047 CFG=0
M  V30 994 1 1046 1048 CFG=0
M  V30 995 1 1048 1049 CFG=0
M  V30 996 1 1048 1050 CFG=0
M  V30 997 1 1048 1063 CFG=0
M  V30 998 1 1050 1051 CFG=0
M  V30 999 1 1050 1052 CFG=0
M  V30 1000 1 1050 1053 CFG=0
M  V30 1001 1 1053 1054 CFG=0
M  V30 1002 1 1053 1055 CFG=0
M  V30 1003 1 1053 1059 CFG=0
M  V30 1004 1 1055 1056 CFG=0
M  V30 1005 1 1055 1057 CFG=0
M  V30 1006 1 1055 1058 CFG=0
M  V30 1007 1 1059 1060 CFG=0
M  V30 1008 1 1059 1061 CFG=0
M  V30 1009 1 1059 1062 CFG=0
M  V30 1010 2 1063 1064 CFG=0
M  V30 1011 1 1065 1066 CFG=0
M  V30 1012 1 1065 1067 CFG=0
M  V30 1013 1 1067 1068 CFG=0
M  V30 1014 1 1067 1069 CFG=0
M  V30 1015 1 1067 1079 CFG=0
M  V30 1016 1 1069 1070 CFG=0
M  V30 1017 1 1069 1071 CFG=0
M  V30 1018 1 1069 1075 CFG=0
M  V30 1019 1 1071 1072 CFG=0
M  V30 1020 1 1071 1073 CFG=0
M  V30 1021 1 1071 1074 CFG=0
M  V30 1022 1 1075 1076 CFG=0
M  V30 1023 1 1075 1077 CFG=0
M  V30 1024 1 1075 1078 CFG=0
M  V30 1025 2 1079 1080 CFG=0
M  V30 1026 1 1081 1082 CFG=0
M  V30 1027 1 1081 1083 CFG=0
M  V30 1028 1 1083 1084 CFG=0
M  V30 1029 1 1083 1085 CFG=0
M  V30 1030 1 1083 1096 CFG=0
M  V30 1031 1 1085 1086 CFG=0
M  V30 1032 1 1085 1087 CFG=0
M  V30 1033 1 1085 1088 CFG=0
M  V30 1034 1 1088 1089 CFG=0
M  V30 1035 1 1088 1090 CFG=0
M  V30 1036 1 1088 1091 CFG=0
M  V30 1037 2 1091 1092 CFG=0
M  V30 1038 1 1091 1093 CFG=0
M  V30 1039 1 1093 1094 CFG=0
M  V30 1040 1 1093 1095 CFG=0
M  V30 1041 2 1096 1097 CFG=0
M  V30 1042 1 1098 1099 CFG=0
M  V30 1043 1 1098 1100 CFG=0
M  V30 1044 1 1100 1101 CFG=0
M  V30 1045 1 1100 1102 CFG=0
M  V30 1046 1 1100 1115 CFG=0
M  V30 1047 1 1102 1103 CFG=0
M  V30 1048 1 1102 1104 CFG=0
M  V30 1049 1 1102 1105 CFG=0
M  V30 1050 1 1105 1106 CFG=0
M  V30 1051 1 1105 1107 CFG=0
M  V30 1052 1 1105 1111 CFG=0
M  V30 1053 1 1107 1108 CFG=0
M  V30 1054 1 1107 1109 CFG=0
M  V30 1055 1 1107 1110 CFG=0
M  V30 1056 1 1111 1112 CFG=0
M  V30 1057 1 1111 1113 CFG=0
M  V30 1058 1 1111 1114 CFG=0
M  V30 1059 2 1115 1116 CFG=0
M  V30 1060 1 1117 1118 CFG=0
M  V30 1061 1 1117 1119 CFG=0
M  V30 1062 1 1119 1120 CFG=0
M  V30 1063 1 1119 1121 CFG=0
M  V30 1064 1 1119 1136 CFG=0
M  V30 1065 1 1121 1122 CFG=0
M  V30 1066 1 1121 1123 CFG=0
M  V30 1067 1 1121 1124 CFG=0
M  V30 1068 2 1124 1125 CFG=0
M  V30 1069 1 1124 1129 CFG=0
M  V30 1070 1 1125 1126 CFG=0
M  V30 1071 1 1125 1127 CFG=0
M  V30 1072 1 1127 1128 CFG=0
M  V30 1073 2 1127 1133 CFG=0
M  V30 1074 1 1129 1130 CFG=0
M  V30 1075 2 1129 1131 CFG=0
M  V30 1076 1 1131 1132 CFG=0
M  V30 1077 1 1131 1133 CFG=0
M  V30 1078 1 1133 1134 CFG=0
M  V30 1079 1 1134 1135 CFG=0
M  V30 1080 2 1136 1137 CFG=0
M  V30 1081 1 1138 1139 CFG=0
M  V30 1082 1 1138 1140 CFG=0
M  V30 1083 1 1140 1141 CFG=0
M  V30 1084 1 1140 1142 CFG=0
M  V30 1085 1 1140 1143 CFG=0
M  V30 1086 2 1143 1144 CFG=0
M  V30 1087 1 1145 1146 CFG=0
M  V30 1088 1 1145 1147 CFG=0
M  V30 1089 1 1147 1148 CFG=0
M  V30 1090 1 1147 1149 CFG=0
M  V30 1091 1 1147 1159 CFG=0
M  V30 1092 1 1149 1150 CFG=0
M  V30 1093 1 1149 1151 CFG=0
M  V30 1094 1 1149 1155 CFG=0
M  V30 1095 1 1151 1152 CFG=0
M  V30 1096 1 1151 1153 CFG=0
M  V30 1097 1 1151 1154 CFG=0
M  V30 1098 1 1155 1156 CFG=0
M  V30 1099 1 1155 1157 CFG=0
M  V30 1100 1 1155 1158 CFG=0
M  V30 1101 2 1159 1160 CFG=0
M  V30 1102 1 1161 1162 CFG=0
M  V30 1103 1 1161 1163 CFG=0
M  V30 1104 1 1163 1164 CFG=0
M  V30 1105 1 1163 1165 CFG=0
M  V30 1106 1 1163 1170 CFG=0
M  V30 1107 1 1165 1166 CFG=0
M  V30 1108 1 1165 1167 CFG=0
M  V30 1109 1 1165 1168 CFG=0
M  V30 1110 1 1168 1169 CFG=0
M  V30 1111 2 1170 1171 CFG=0
M  V30 1112 1 1172 1173 CFG=0
M  V30 1113 1 1172 1174 CFG=0
M  V30 1114 1 1174 1175 CFG=0
M  V30 1115 1 1174 1176 CFG=0
M  V30 1116 1 1174 1184 CFG=0
M  V30 1117 1 1176 1177 CFG=0
M  V30 1118 1 1176 1178 CFG=0
M  V30 1119 1 1176 1180 CFG=0
M  V30 1120 1 1178 1179 CFG=0
M  V30 1121 1 1180 1181 CFG=0
M  V30 1122 1 1180 1182 CFG=0
M  V30 1123 1 1180 1183 CFG=0
M  V30 1124 2 1184 1185 CFG=0
M  V30 1125 1 1186 1187 CFG=0
M  V30 1126 1 1186 1188 CFG=0
M  V30 1127 1 1188 1189 CFG=0
M  V30 1128 1 1188 1190 CFG=0
M  V30 1129 1 1188 1206 CFG=0
M  V30 1130 1 1190 1191 CFG=0
M  V30 1131 1 1190 1192 CFG=0
M  V30 1132 1 1190 1193 CFG=0
M  V30 1133 1 1193 1194 CFG=0
M  V30 1134 1 1193 1195 CFG=0
M  V30 1135 1 1193 1196 CFG=0
M  V30 1136 1 1196 1197 CFG=0
M  V30 1137 1 1196 1198 CFG=0
M  V30 1138 1 1196 1199 CFG=0
M  V30 1139 1 1199 1200 CFG=0
M  V30 1140 1 1199 1201 CFG=0
M  V30 1141 1 1199 1202 CFG=0
M  V30 1142 1 1202 1203 CFG=0
M  V30 1143 1 1202 1204 CFG=0
M  V30 1144 1 1202 1205 CFG=0
M  V30 1145 2 1206 1207 CFG=0
M  V30 1146 1 1208 1209 CFG=0
M  V30 1147 1 1208 1210 CFG=0
M  V30 1148 1 1210 1211 CFG=0
M  V30 1149 1 1210 1212 CFG=0
M  V30 1150 1 1210 1223 CFG=0
M  V30 1151 1 1212 1213 CFG=0
M  V30 1152 1 1212 1214 CFG=0
M  V30 1153 1 1212 1215 CFG=0
M  V30 1154 1 1215 1216 CFG=0
M  V30 1155 1 1215 1217 CFG=0
M  V30 1156 1 1215 1218 CFG=0
M  V30 1157 2 1218 1219 CFG=0
M  V30 1158 1 1218 1220 CFG=0
M  V30 1159 1 1220 1221 CFG=0
M  V30 1160 1 1220 1222 CFG=0
M  V30 1161 2 1223 1224 CFG=0
M  V30 1162 1 1225 1226 CFG=0
M  V30 1163 1 1225 1227 CFG=0
M  V30 1164 1 1227 1228 CFG=0
M  V30 1165 1 1227 1229 CFG=0
M  V30 1166 1 1227 1247 CFG=0
M  V30 1167 1 1229 1230 CFG=0
M  V30 1168 1 1229 1231 CFG=0
M  V30 1169 1 1229 1232 CFG=0
M  V30 1170 1 1232 1233 CFG=0
M  V30 1171 1 1232 1234 CFG=0
M  V30 1172 1 1232 1235 CFG=0
M  V30 1173 1 1235 1236 CFG=0
M  V30 1174 1 1235 1237 CFG=0
M  V30 1175 1 1235 1238 CFG=0
M  V30 1176 1 1238 1239 CFG=0
M  V30 1177 1 1238 1240 CFG=0
M  V30 1178 2 1240 1241 CFG=0
M  V30 1179 1 1240 1244 CFG=0
M  V30 1180 1 1241 1242 CFG=0
M  V30 1181 1 1241 1243 CFG=0
M  V30 1182 1 1244 1245 CFG=0
M  V30 1183 1 1244 1246 CFG=0
M  V30 1184 2 1247 1248 CFG=0
M  V30 1185 1 1249 1253 CFG=0
M  V30 1186 1 1250 1249 CFG=0
M  V30 1187 1 1250 1251 CFG=0
M  V30 1188 1 1250 1252 CFG=0
M  V30 1189 1 1253 1254 CFG=0
M  V30 1190 1 1253 1255 CFG=0
M  V30 1191 1 1253 1261 CFG=0
M  V30 1192 1 1255 1256 CFG=0
M  V30 1193 1 1255 1257 CFG=0
M  V30 1194 1 1255 1258 CFG=0
M  V30 1195 1 1258 1250 CFG=0
M  V30 1196 1 1258 1259 CFG=0
M  V30 1197 1 1258 1260 CFG=0
M  V30 1198 2 1261 1262 CFG=0
M  V30 1199 1 1263 1264 CFG=0
M  V30 1200 1 1263 1265 CFG=0
M  V30 1201 1 1265 1266 CFG=0
M  V30 1202 1 1265 1267 CFG=0
M  V30 1203 1 1265 1280 CFG=0
M  V30 1204 1 1267 1268 CFG=0
M  V30 1205 1 1267 1269 CFG=0
M  V30 1206 1 1267 1273 CFG=0
M  V30 1207 1 1269 1270 CFG=0
M  V30 1208 1 1269 1271 CFG=0
M  V30 1209 1 1269 1272 CFG=0
M  V30 1210 1 1273 1274 CFG=0
M  V30 1211 1 1273 1275 CFG=0
M  V30 1212 1 1273 1276 CFG=0
M  V30 1213 1 1276 1277 CFG=0
M  V30 1214 1 1276 1278 CFG=0
M  V30 1215 1 1276 1279 CFG=0
M  V30 1216 2 1280 1281 CFG=0
M  V30 1217 1 1282 1283 CFG=0
M  V30 1218 1 1282 1284 CFG=0
M  V30 1219 1 1284 1285 CFG=0
M  V30 1220 1 1284 1286 CFG=0
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M  V30 1701 1 1789 1790 CFG=0
M  V30 1702 1 1789 1791 CFG=0
M  V30 1703 1 1789 1792 CFG=0
M  V30 1704 1 1792 1793 CFG=0
M  V30 1705 1 1792 1794 CFG=0
M  V30 1706 1 1792 1795 CFG=0
M  V30 1707 2 1795 1796 CFG=0
M  V30 1708 1 1795 1797 CFG=0
M  V30 1709 2 1798 1799 CFG=0
M  V30 1710 1 1800 1801 CFG=0
M  V30 1711 1 1800 1802 CFG=0
M  V30 1712 1 1802 1803 CFG=0
M  V30 1713 1 1802 1804 CFG=0
M  V30 1714 1 1802 1815 CFG=0
M  V30 1715 1 1804 1805 CFG=0
M  V30 1716 1 1804 1806 CFG=0
M  V30 1717 1 1804 1807 CFG=0
M  V30 1718 1 1807 1808 CFG=0
M  V30 1719 1 1807 1809 CFG=0
M  V30 1720 1 1807 1810 CFG=0
M  V30 1721 1 1810 1811 CFG=0
M  V30 1722 1 1811 1812 CFG=0
M  V30 1723 1 1811 1813 CFG=0
M  V30 1724 1 1811 1814 CFG=0
M  V30 1725 2 1815 1816 CFG=0
M  V30 1726 1 1817 1818 CFG=0
M  V30 1727 1 1817 1819 CFG=0
M  V30 1728 1 1819 1820 CFG=0
M  V30 1729 1 1819 1821 CFG=0
M  V30 1730 1 1819 1826 CFG=0
M  V30 1731 1 1821 1822 CFG=0
M  V30 1732 1 1821 1823 CFG=0
M  V30 1733 1 1821 1824 CFG=0
M  V30 1734 1 1824 1825 CFG=0
M  V30 1735 2 1826 1827 CFG=0
M  V30 1736 1 1828 1829 CFG=0
M  V30 1737 1 1828 1830 CFG=0
M  V30 1738 1 1830 1831 CFG=0
M  V30 1739 1 1830 1832 CFG=0
M  V30 1740 1 1830 1848 CFG=0
M  V30 1741 1 1832 1833 CFG=0
M  V30 1742 1 1832 1834 CFG=0
M  V30 1743 1 1832 1835 CFG=0
M  V30 1744 1 1835 1836 CFG=0
M  V30 1745 1 1835 1837 CFG=0
M  V30 1746 1 1835 1838 CFG=0
M  V30 1747 1 1838 1839 CFG=0
M  V30 1748 1 1838 1840 CFG=0
M  V30 1749 1 1838 1841 CFG=0
M  V30 1750 1 1841 1842 CFG=0
M  V30 1751 1 1841 1843 CFG=0
M  V30 1752 1 1841 1844 CFG=0
M  V30 1753 1 1844 1845 CFG=0
M  V30 1754 1 1844 1846 CFG=0
M  V30 1755 1 1844 1847 CFG=0
M  V30 1756 2 1848 1849 CFG=0
M  V30 1757 1 1850 1851 CFG=0
M  V30 1758 1 1850 1852 CFG=0
M  V30 1759 1 1852 1853 CFG=0
M  V30 1760 1 1852 1854 CFG=0
M  V30 1761 1 1852 1860 CFG=0
M  V30 1762 1 1854 1855 CFG=0
M  V30 1763 1 1854 1856 CFG=0
M  V30 1764 1 1854 1857 CFG=0
M  V30 1765 2 1857 1858 CFG=0
M  V30 1766 1 1857 1859 CFG=0
M  V30 1767 2 1860 1861 CFG=0
M  V30 1768 1 1862 1863 CFG=0
M  V30 1769 1 1862 1864 CFG=0
M  V30 1770 1 1864 1865 CFG=0
M  V30 1771 1 1864 1866 CFG=0
M  V30 1772 1 1864 1876 CFG=0
M  V30 1773 1 1866 1867 CFG=0
M  V30 1774 1 1866 1868 CFG=0
M  V30 1775 1 1866 1872 CFG=0
M  V30 1776 1 1868 1869 CFG=0
M  V30 1777 1 1868 1870 CFG=0
M  V30 1778 1 1868 1871 CFG=0
M  V30 1779 1 1872 1873 CFG=0
M  V30 1780 1 1872 1874 CFG=0
M  V30 1781 1 1872 1875 CFG=0
M  V30 1782 2 1876 1877 CFG=0
M  V30 1783 1 1878 1879 CFG=0
M  V30 1784 1 1878 1880 CFG=0
M  V30 1785 1 1880 1881 CFG=0
M  V30 1786 1 1880 1882 CFG=0
M  V30 1787 1 1880 1887 CFG=0
M  V30 1788 1 1882 1883 CFG=0
M  V30 1789 1 1882 1884 CFG=0
M  V30 1790 1 1882 1885 CFG=0
M  V30 1791 1 1885 1886 CFG=0
M  V30 1792 2 1887 1888 CFG=0
M  V30 1793 1 1889 1890 CFG=0
M  V30 1794 1 1889 1891 CFG=0
M  V30 1795 1 1891 1892 CFG=0
M  V30 1796 1 1891 1893 CFG=0
M  V30 1797 1 1891 1902 CFG=0
M  V30 1798 1 1893 1894 CFG=0
M  V30 1799 1 1893 1895 CFG=0
M  V30 1800 1 1893 1896 CFG=0
M  V30 1801 1 1896 1897 CFG=0
M  V30 1802 1 1896 1898 CFG=0
M  V30 1803 1 1896 1899 CFG=0
M  V30 1804 2 1899 1900 CFG=0
M  V30 1805 1 1899 1901 CFG=0
M  V30 1806 2 1902 1903 CFG=0
M  V30 1807 1 1904 1905 CFG=0
M  V30 1808 1 1904 1906 CFG=0
M  V30 1809 1 1906 1907 CFG=0
M  V30 1810 1 1906 1908 CFG=0
M  V30 1811 1 1906 1912 CFG=0
M  V30 1812 1 1908 1909 CFG=0
M  V30 1813 1 1908 1910 CFG=0
M  V30 1814 1 1908 1911 CFG=0
M  V30 1815 2 1912 1913 CFG=0
M  V30 1816 1 1914 1915 CFG=0
M  V30 1817 1 1914 1916 CFG=0
M  V30 1818 1 1916 1917 CFG=0
M  V30 1819 1 1916 1918 CFG=0
M  V30 1820 1 1916 1929 CFG=0
M  V30 1821 1 1918 1919 CFG=0
M  V30 1822 1 1918 1920 CFG=0
M  V30 1823 1 1918 1921 CFG=0
M  V30 1824 1 1921 1922 CFG=0
M  V30 1825 1 1921 1923 CFG=0
M  V30 1826 1 1921 1924 CFG=0
M  V30 1827 1 1924 1925 CFG=0
M  V30 1828 1 1925 1926 CFG=0
M  V30 1829 1 1925 1927 CFG=0
M  V30 1830 1 1925 1928 CFG=0
M  V30 1831 2 1929 1930 CFG=0
M  V30 1832 1 1931 1932 CFG=0
M  V30 1833 1 1931 1933 CFG=0
M  V30 1834 1 1933 1934 CFG=0
M  V30 1835 1 1933 1935 CFG=0
M  V30 1836 1 1933 1944 CFG=0
M  V30 1837 1 1935 1936 CFG=0
M  V30 1838 1 1935 1937 CFG=0
M  V30 1839 1 1935 1938 CFG=0
M  V30 1840 1 1938 1939 CFG=0
M  V30 1841 1 1938 1940 CFG=0
M  V30 1842 1 1938 1941 CFG=0
M  V30 1843 2 1941 1942 CFG=0
M  V30 1844 1 1941 1943 CFG=0
M  V30 1845 2 1944 1945 CFG=0
M  V30 1846 1 1946 1947 CFG=0
M  V30 1847 1 1946 1948 CFG=0
M  V30 1848 1 1948 1949 CFG=0
M  V30 1849 1 1948 1950 CFG=0
M  V30 1850 1 1948 1965 CFG=0
M  V30 1851 1 1950 1951 CFG=0
M  V30 1852 1 1950 1952 CFG=0
M  V30 1853 1 1950 1953 CFG=0
M  V30 1854 2 1953 1954 CFG=0
M  V30 1855 1 1953 1958 CFG=0
M  V30 1856 1 1954 1955 CFG=0
M  V30 1857 1 1954 1956 CFG=0
M  V30 1858 1 1956 1957 CFG=0
M  V30 1859 2 1956 1962 CFG=0
M  V30 1860 1 1958 1959 CFG=0
M  V30 1861 2 1958 1960 CFG=0
M  V30 1862 1 1960 1961 CFG=0
M  V30 1863 1 1960 1962 CFG=0
M  V30 1864 1 1962 1963 CFG=0
M  V30 1865 1 1963 1964 CFG=0
M  V30 1866 2 1965 1966 CFG=0
M  V30 1867 1 1967 1968 CFG=0
M  V30 1868 1 1967 1969 CFG=0
M  V30 1869 1 1969 1970 CFG=0
M  V30 1870 1 1969 1971 CFG=0
M  V30 1871 1 1969 1984 CFG=0
M  V30 1872 1 1971 1972 CFG=0
M  V30 1873 1 1971 1973 CFG=0
M  V30 1874 1 1971 1974 CFG=0
M  V30 1875 1 1974 1975 CFG=0
M  V30 1876 1 1974 1976 CFG=0
M  V30 1877 1 1974 1980 CFG=0
M  V30 1878 1 1976 1977 CFG=0
M  V30 1879 1 1976 1978 CFG=0
M  V30 1880 1 1976 1979 CFG=0
M  V30 1881 1 1980 1981 CFG=0
M  V30 1882 1 1980 1982 CFG=0
M  V30 1883 1 1980 1983 CFG=0
M  V30 1884 2 1984 1985 CFG=0
M  V30 1885 1 1986 1987 CFG=0
M  V30 1886 1 1986 1988 CFG=0
M  V30 1887 1 1988 1989 CFG=0
M  V30 1888 1 1988 1990 CFG=0
M  V30 1889 1 1988 1999 CFG=0
M  V30 1890 1 1990 1991 CFG=0
M  V30 1891 1 1990 1992 CFG=0
M  V30 1892 1 1990 1993 CFG=0
M  V30 1893 1 1993 1994 CFG=0
M  V30 1894 1 1993 1995 CFG=0
M  V30 1895 1 1993 1996 CFG=0
M  V30 1896 2 1996 1997 CFG=0
M  V30 1897 1 1996 1998 CFG=0
M  V30 1898 2 1999 2000 CFG=0
M  V30 1899 1 2001 2002 CFG=0
M  V30 1900 1 2001 2003 CFG=0
M  V30 1901 1 2003 2004 CFG=0
M  V30 1902 1 2003 2005 CFG=0
M  V30 1903 1 2003 2010 CFG=0
M  V30 1904 1 2005 2006 CFG=0
M  V30 1905 1 2005 2007 CFG=0
M  V30 1906 1 2005 2008 CFG=0
M  V30 1907 1 2008 2009 CFG=0
M  V30 1908 2 2010 2011 CFG=0
M  V30 1909 1 2012 2013 CFG=0
M  V30 1910 1 2012 2014 CFG=0
M  V30 1911 1 2014 2015 CFG=0
M  V30 1912 1 2014 2016 CFG=0
M  V30 1913 1 2014 2032 CFG=0
M  V30 1914 1 2016 2017 CFG=0
M  V30 1915 1 2016 2018 CFG=0
M  V30 1916 1 2016 2019 CFG=0
M  V30 1917 1 2019 2020 CFG=0
M  V30 1918 1 2019 2021 CFG=0
M  V30 1919 1 2019 2022 CFG=0
M  V30 1920 1 2022 2023 CFG=0
M  V30 1921 1 2022 2024 CFG=0
M  V30 1922 1 2022 2025 CFG=0
M  V30 1923 1 2025 2026 CFG=0
M  V30 1924 1 2025 2027 CFG=0
M  V30 1925 1 2025 2028 CFG=0
M  V30 1926 1 2028 2029 CFG=0
M  V30 1927 1 2028 2030 CFG=0
M  V30 1928 1 2028 2031 CFG=0
M  V30 1929 2 2032 2033 CFG=0
M  V30 1930 1 2034 2035 CFG=0
M  V30 1931 1 2034 2036 CFG=0
M  V30 1932 1 2036 2037 CFG=0
M  V30 1933 1 2036 2038 CFG=0
M  V30 1934 1 2036 2049 CFG=0
M  V30 1935 1 2038 2039 CFG=0
M  V30 1936 1 2038 2040 CFG=0
M  V30 1937 1 2038 2041 CFG=0
M  V30 1938 1 2041 2042 CFG=0
M  V30 1939 1 2041 2043 CFG=0
M  V30 1940 1 2041 2044 CFG=0
M  V30 1941 2 2044 2045 CFG=0
M  V30 1942 1 2044 2046 CFG=0
M  V30 1943 1 2046 2047 CFG=0
M  V30 1944 1 2046 2048 CFG=0
M  V30 1945 2 2049 2050 CFG=0
M  V30 1946 1 2051 2052 CFG=0
M  V30 1947 1 2051 2053 CFG=0
M  V30 1948 1 2053 2054 CFG=0
M  V30 1949 1 2053 2055 CFG=0
M  V30 1950 1 2053 2069 CFG=0
M  V30 1951 1 2055 2056 CFG=0
M  V30 1952 1 2055 2057 CFG=0
M  V30 1953 1 2055 2058 CFG=0
M  V30 1954 2 2058 2059 CFG=0
M  V30 1955 1 2058 2061 CFG=0
M  V30 1956 1 2059 2060 CFG=0
M  V30 1957 1 2059 2063 CFG=0
M  V30 1958 1 2061 2062 CFG=0
M  V30 1959 2 2061 2065 CFG=0
M  V30 1960 1 2063 2064 CFG=0
M  V30 1961 2 2063 2067 CFG=0
M  V30 1962 1 2065 2066 CFG=0
M  V30 1963 1 2065 2067 CFG=0
M  V30 1964 1 2067 2068 CFG=0
M  V30 1965 2 2069 2070 CFG=0
M  V30 1966 1 2071 2072 CFG=0
M  V30 1967 1 2071 2073 CFG=0
M  V30 1968 1 2073 2074 CFG=0
M  V30 1969 1 2073 2075 CFG=0
M  V30 1970 1 2073 2088 CFG=0
M  V30 1971 1 2075 2076 CFG=0
M  V30 1972 1 2075 2077 CFG=0
M  V30 1973 1 2075 2078 CFG=0
M  V30 1974 1 2078 2079 CFG=0
M  V30 1975 1 2078 2080 CFG=0
M  V30 1976 1 2078 2084 CFG=0
M  V30 1977 1 2080 2081 CFG=0
M  V30 1978 1 2080 2082 CFG=0
M  V30 1979 1 2080 2083 CFG=0
M  V30 1980 1 2084 2085 CFG=0
M  V30 1981 1 2084 2086 CFG=0
M  V30 1982 1 2084 2087 CFG=0
M  V30 1983 2 2088 2089 CFG=0
M  V30 1984 1 2090 2091 CFG=0
M  V30 1985 1 2090 2092 CFG=0
M  V30 1986 1 2092 2093 CFG=0
M  V30 1987 1 2092 2094 CFG=0
M  V30 1988 1 2092 2106 CFG=0
M  V30 1989 1 2094 2095 CFG=0
M  V30 1990 1 2094 2096 CFG=0
M  V30 1991 1 2094 2097 CFG=0
M  V30 1992 2 2097 2098 CFG=0
M  V30 1993 1 2097 2100 CFG=0
M  V30 1994 1 2098 2099 CFG=0
M  V30 1995 1 2098 2104 CFG=0
M  V30 1996 1 2100 2101 CFG=0
M  V30 1997 1 2100 2102 CFG=0
M  V30 1998 1 2102 2103 CFG=0
M  V30 1999 2 2102 2104 CFG=0
M  V30 2000 1 2104 2105 CFG=0
M  V30 2001 2 2106 2107 CFG=0
M  V30 2002 1 2108 2109 CFG=0
M  V30 2003 1 2108 2110 CFG=0
M  V30 2004 1 2110 2111 CFG=0
M  V30 2005 1 2110 2112 CFG=0
M  V30 2006 1 2110 2130 CFG=0
M  V30 2007 1 2112 2113 CFG=0
M  V30 2008 1 2112 2114 CFG=0
M  V30 2009 1 2112 2115 CFG=0
M  V30 2010 1 2115 2116 CFG=0
M  V30 2011 1 2115 2117 CFG=0
M  V30 2012 1 2115 2118 CFG=0
M  V30 2013 1 2118 2119 CFG=0
M  V30 2014 1 2118 2120 CFG=0
M  V30 2015 1 2118 2121 CFG=0
M  V30 2016 1 2121 2122 CFG=0
M  V30 2017 1 2121 2123 CFG=0
M  V30 2018 2 2123 2124 CFG=0
M  V30 2019 1 2123 2127 CFG=0
M  V30 2020 1 2124 2125 CFG=0
M  V30 2021 1 2124 2126 CFG=0
M  V30 2022 1 2127 2128 CFG=0
M  V30 2023 1 2127 2129 CFG=0
M  V30 2024 2 2130 2131 CFG=0
M  V30 2025 1 2132 2133 CFG=0
M  V30 2026 1 2132 2134 CFG=0
M  V30 2027 1 2134 2135 CFG=0
M  V30 2028 1 2134 2136 CFG=0
M  V30 2029 1 2134 2142 CFG=0
M  V30 2030 1 2136 2137 CFG=0
M  V30 2031 1 2136 2138 CFG=0
M  V30 2032 1 2136 2139 CFG=0
M  V30 2033 2 2139 2140 CFG=0
M  V30 2034 1 2139 2141 CFG=0
M  V30 2035 2 2142 2143 CFG=0
M  V30 2036 1 2144 2145 CFG=0
M  V30 2037 1 2144 2146 CFG=0
M  V30 2038 1 2146 2147 CFG=0
M  V30 2039 1 2146 2148 CFG=0
M  V30 2040 1 2146 2161 CFG=0
M  V30 2041 1 2148 2149 CFG=0
M  V30 2042 1 2148 2150 CFG=0
M  V30 2043 1 2148 2151 CFG=0
M  V30 2044 1 2151 2152 CFG=0
M  V30 2045 1 2151 2153 CFG=0
M  V30 2046 1 2151 2157 CFG=0
M  V30 2047 1 2153 2154 CFG=0
M  V30 2048 1 2153 2155 CFG=0
M  V30 2049 1 2153 2156 CFG=0
M  V30 2050 1 2157 2158 CFG=0
M  V30 2051 1 2157 2159 CFG=0
M  V30 2052 1 2157 2160 CFG=0
M  V30 2053 2 2161 2162 CFG=0
M  V30 2054 1 2163 2164 CFG=0
M  V30 2055 1 2163 2165 CFG=0
M  V30 2056 1 2165 2166 CFG=0
M  V30 2057 1 2165 2167 CFG=0
M  V30 2058 1 2165 2171 CFG=0
M  V30 2059 1 2167 2168 CFG=0
M  V30 2060 1 2167 2169 CFG=0
M  V30 2061 1 2167 2170 CFG=0
M  V30 2062 2 2171 2172 CFG=0
M  V30 2063 1 2173 2174 CFG=0
M  V30 2064 1 2173 2175 CFG=0
M  V30 2065 1 2175 2176 CFG=0
M  V30 2066 1 2175 2177 CFG=0
M  V30 2067 1 2175 2181 CFG=0
M  V30 2068 1 2177 2178 CFG=0
M  V30 2069 1 2177 2179 CFG=0
M  V30 2070 1 2177 2180 CFG=0
M  V30 2071 2 2181 2182 CFG=0
M  V30 2072 1 2183 2184 CFG=0
M  V30 2073 1 2183 2185 CFG=0
M  V30 2074 1 2185 2186 CFG=0
M  V30 2075 1 2185 2187 CFG=0
M  V30 2076 1 2185 2205 CFG=0
M  V30 2077 1 2187 2188 CFG=0
M  V30 2078 1 2187 2189 CFG=0
M  V30 2079 1 2187 2190 CFG=0
M  V30 2080 1 2190 2191 CFG=0
M  V30 2081 1 2190 2192 CFG=0
M  V30 2082 1 2190 2193 CFG=0
M  V30 2083 1 2193 2194 CFG=0
M  V30 2084 1 2193 2195 CFG=0
M  V30 2085 1 2193 2196 CFG=0
M  V30 2086 1 2196 2197 CFG=0
M  V30 2087 1 2196 2198 CFG=0
M  V30 2088 2 2198 2199 CFG=0
M  V30 2089 1 2198 2202 CFG=0
M  V30 2090 1 2199 2200 CFG=0
M  V30 2091 1 2199 2201 CFG=0
M  V30 2092 1 2202 2203 CFG=0
M  V30 2093 1 2202 2204 CFG=0
M  V30 2094 2 2205 2206 CFG=0
M  V30 2095 1 2207 2208 CFG=0
M  V30 2096 1 2207 2209 CFG=0
M  V30 2097 1 2209 2210 CFG=0
M  V30 2098 1 2209 2211 CFG=0
M  V30 2099 1 2209 2219 CFG=0
M  V30 2100 1 2211 2212 CFG=0
M  V30 2101 1 2211 2213 CFG=0
M  V30 2102 1 2211 2214 CFG=0
M  V30 2103 2 2214 2215 CFG=0
M  V30 2104 1 2214 2216 CFG=0
M  V30 2105 1 2216 2217 CFG=0
M  V30 2106 1 2216 2218 CFG=0
M  V30 2107 2 2219 2220 CFG=0
M  V30 2108 1 2221 2222 CFG=0
M  V30 2109 1 2221 2223 CFG=0
M  V30 2110 1 2223 2224 CFG=0
M  V30 2111 1 2223 2225 CFG=0
M  V30 2112 1 2223 2230 CFG=0
M  V30 2113 1 2225 2226 CFG=0
M  V30 2114 1 2225 2227 CFG=0
M  V30 2115 1 2225 2228 CFG=0
M  V30 2116 1 2228 2229 CFG=0
M  V30 2117 2 2230 2231 CFG=0
M  V30 2118 1 2232 2233 CFG=0
M  V30 2119 1 2232 2234 CFG=0
M  V30 2120 1 2234 2235 CFG=0
M  V30 2121 1 2234 2236 CFG=0
M  V30 2122 1 2234 2249 CFG=0
M  V30 2123 1 2236 2237 CFG=0
M  V30 2124 1 2236 2238 CFG=0
M  V30 2125 1 2236 2239 CFG=0
M  V30 2126 1 2239 2240 CFG=0
M  V30 2127 1 2239 2241 CFG=0
M  V30 2128 1 2239 2245 CFG=0
M  V30 2129 1 2241 2242 CFG=0
M  V30 2130 1 2241 2243 CFG=0
M  V30 2131 1 2241 2244 CFG=0
M  V30 2132 1 2245 2246 CFG=0
M  V30 2133 1 2245 2247 CFG=0
M  V30 2134 1 2245 2248 CFG=0
M  V30 2135 2 2249 2250 CFG=0
M  V30 2136 1 2251 2252 CFG=0
M  V30 2137 1 2251 2253 CFG=0
M  V30 2138 1 2253 2254 CFG=0
M  V30 2139 1 2253 2255 CFG=0
M  V30 2140 1 2253 2265 CFG=0
M  V30 2141 1 2255 2256 CFG=0
M  V30 2142 1 2255 2257 CFG=0
M  V30 2143 1 2255 2261 CFG=0
M  V30 2144 1 2257 2258 CFG=0
M  V30 2145 1 2257 2259 CFG=0
M  V30 2146 1 2257 2260 CFG=0
M  V30 2147 1 2261 2262 CFG=0
M  V30 2148 1 2261 2263 CFG=0
M  V30 2149 1 2261 2264 CFG=0
M  V30 2150 2 2265 2266 CFG=0
M  V30 2151 1 2267 2268 CFG=0
M  V30 2152 1 2267 2269 CFG=0
M  V30 2153 1 2269 2270 CFG=0
M  V30 2154 1 2269 2271 CFG=0
M  V30 2155 1 2269 2279 CFG=0
M  V30 2156 1 2271 2272 CFG=0
M  V30 2157 1 2271 2273 CFG=0
M  V30 2158 1 2271 2274 CFG=0
M  V30 2159 2 2274 2275 CFG=0
M  V30 2160 1 2274 2276 CFG=0
M  V30 2161 1 2276 2277 CFG=0
M  V30 2162 1 2276 2278 CFG=0
M  V30 2163 2 2279 2280 CFG=0
M  V30 2164 1 2281 2282 CFG=0
M  V30 2165 1 2281 2283 CFG=0
M  V30 2166 1 2283 2284 CFG=0
M  V30 2167 1 2283 2285 CFG=0
M  V30 2168 1 2283 2291 CFG=0
M  V30 2169 1 2285 2286 CFG=0
M  V30 2170 1 2285 2287 CFG=0
M  V30 2171 1 2285 2288 CFG=0
M  V30 2172 2 2288 2289 CFG=0
M  V30 2173 1 2288 2290 CFG=0
M  V30 2174 2 2291 2292 CFG=0
M  V30 2175 1 2293 2294 CFG=0
M  V30 2176 1 2293 2295 CFG=0
M  V30 2177 1 2295 2296 CFG=0
M  V30 2178 1 2295 2297 CFG=0
M  V30 2179 1 2295 2308 CFG=0
M  V30 2180 1 2297 2298 CFG=0
M  V30 2181 1 2297 2299 CFG=0
M  V30 2182 1 2297 2300 CFG=0
M  V30 2183 1 2300 2301 CFG=0
M  V30 2184 1 2300 2302 CFG=0
M  V30 2185 1 2300 2303 CFG=0
M  V30 2186 2 2303 2304 CFG=0
M  V30 2187 1 2303 2305 CFG=0
M  V30 2188 1 2305 2306 CFG=0
M  V30 2189 1 2305 2307 CFG=0
M  V30 2190 2 2308 2309 CFG=0
M  V30 2191 1 2310 2311 CFG=0
M  V30 2192 1 2310 2312 CFG=0
M  V30 2193 1 2312 2313 CFG=0
M  V30 2194 1 2312 2314 CFG=0
M  V30 2195 1 2312 2315 CFG=0
M  V30 2196 2 2315 2316 CFG=0
M  V30 2197 1 2317 2318 CFG=0
M  V30 2198 1 2317 2319 CFG=0
M  V30 2199 1 2319 2320 CFG=0
M  V30 2200 1 2319 2321 CFG=0
M  V30 2201 1 2319 2331 CFG=0
M  V30 2202 1 2321 2322 CFG=0
M  V30 2203 1 2321 2323 CFG=0
M  V30 2204 1 2321 2327 CFG=0
M  V30 2205 1 2323 2324 CFG=0
M  V30 2206 1 2323 2325 CFG=0
M  V30 2207 1 2323 2326 CFG=0
M  V30 2208 1 2327 2328 CFG=0
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M  V30 2211 2 2331 2332 CFG=0
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M  V30 2231 1 2351 2369 CFG=0
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M  V30 3167 1 3333 3332 CFG=0
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M  V30 3182 1 3348 3349 CFG=0
M  V30 3183 1 3348 3350 CFG=0
M  V30 3184 1 3348 3365 CFG=0
M  V30 3185 1 3350 3351 CFG=0
M  V30 3186 1 3350 3352 CFG=0
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M  V30 3189 1 3353 3358 CFG=0
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M  V30 3193 2 3356 3362 CFG=0
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M  V30 3196 1 3360 3361 CFG=0
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M  V30 3203 1 3369 3370 CFG=0
M  V30 3204 1 3369 3371 CFG=0
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M  V30 3206 1 3371 3372 CFG=0
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M  V30 3320 2 3492 3493 CFG=0
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M  V30 3325 1 3496 3502 CFG=0
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M  V30 3329 2 3502 3503 CFG=0
M  V30 3330 1 3504 3505 CFG=0
M  V30 3331 1 3504 3506 CFG=0
M  V30 3332 1 3506 3507 CFG=0
M  V30 3333 1 3506 3508 CFG=0
M  V30 3334 1 3506 3517 CFG=0
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M  V30 3336 1 3508 3510 CFG=0
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M  V30 3341 2 3514 3515 CFG=0
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M  V30 3349 1 3523 3524 CFG=0
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M  V30 3355 1 3528 3529 CFG=0
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M  V30 3361 1 3536 3537 CFG=0
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M  V30 3365 1 3538 3553 CFG=0
M  V30 3366 1 3540 3541 CFG=0
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M  V30 3368 1 3540 3546 CFG=0
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M  V30 3378 2 3553 3554 CFG=0
M  V30 3379 1 3555 3556 CFG=0
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M  V30 3381 1 3557 3558 CFG=0
M  V30 3382 1 3557 3559 CFG=0
M  V30 3383 1 3557 3563 CFG=0
M  V30 3384 1 3559 3560 CFG=0
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M  V30 3386 1 3559 3562 CFG=0
M  V30 3387 2 3563 3564 CFG=0
M  V30 3388 1 3565 3566 CFG=0
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M  V30 3392 1 3567 3580 CFG=0
M  V30 3393 1 3569 3570 CFG=0
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M  V30 3396 1 3572 3573 CFG=0
M  V30 3397 1 3572 3574 CFG=0
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M  V30 3399 2 3575 3576 CFG=0
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M  V30 3402 1 3577 3579 CFG=0
M  V30 3403 2 3580 3581 CFG=0
M  V30 3404 1 3582 3583 CFG=0
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M  V30 3410 1 3589 3590 CFG=0
M  V30 3411 1 3589 3591 CFG=0
M  V30 3412 1 3591 3592 CFG=0
M  V30 3413 1 3591 3593 CFG=0
M  V30 3414 1 3591 3606 CFG=0
M  V30 3415 1 3593 3594 CFG=0
M  V30 3416 1 3593 3595 CFG=0
M  V30 3417 1 3593 3596 CFG=0
M  V30 3418 1 3596 3597 CFG=0
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M  V30 3420 1 3596 3602 CFG=0
M  V30 3421 1 3598 3599 CFG=0
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M  V30 3424 1 3602 3603 CFG=0
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M  V30 3427 2 3606 3607 CFG=0
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M  V30 3430 1 3610 3611 CFG=0
M  V30 3431 1 3610 3612 CFG=0
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M  V30 3441 1 3618 3621 CFG=0
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M  V30 3444 2 3623 3624 CFG=0
M  V30 3445 1 3623 3627 CFG=0
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M  V30 3448 1 3627 3628 CFG=0
M  V30 3449 1 3627 3629 CFG=0
M  V30 3450 2 3630 3631 CFG=0
M  V30 3451 1 3632 3633 CFG=0
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M  V30 3455 1 3634 3649 CFG=0
M  V30 3456 1 3636 3637 CFG=0
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M  V30 3462 1 3641 3642 CFG=0
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M  V30 3468 2 3649 3650 CFG=0
M  V30 3469 1 3651 3652 CFG=0
M  V30 3470 1 3651 3653 CFG=0
M  V30 3471 1 3653 3654 CFG=0
M  V30 3472 1 3653 3655 CFG=0
M  V30 3473 1 3653 3670 CFG=0
M  V30 3474 1 3655 3656 CFG=0
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M  V30 3477 2 3658 3659 CFG=0
M  V30 3478 1 3658 3663 CFG=0
M  V30 3479 1 3659 3660 CFG=0
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M  V30 3481 1 3661 3662 CFG=0
M  V30 3482 2 3661 3667 CFG=0
M  V30 3483 1 3663 3664 CFG=0
M  V30 3484 2 3663 3665 CFG=0
M  V30 3485 1 3665 3666 CFG=0
M  V30 3486 1 3665 3667 CFG=0
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M  V30 3489 2 3670 3671 CFG=0
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M  V30 3504 1 3685 3686 CFG=0
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M  V30 3506 2 3687 3688 CFG=0
M  V30 3507 1 3687 3691 CFG=0
M  V30 3508 1 3688 3689 CFG=0
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M  V30 3510 1 3691 3692 CFG=0
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M  V30 3512 2 3694 3695 CFG=0
M  V30 3513 1 3696 3700 CFG=0
M  V30 3514 1 3697 3696 CFG=0
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M  V30 3516 1 3697 3699 CFG=0
M  V30 3517 1 3700 3701 CFG=0
M  V30 3518 1 3700 3702 CFG=0
M  V30 3519 1 3700 3708 CFG=0
M  V30 3520 1 3702 3703 CFG=0
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M  V30 3523 1 3705 3697 CFG=0
M  V30 3524 1 3705 3706 CFG=0
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M  V30 3526 2 3708 3709 CFG=0
M  V30 3527 1 3710 3711 CFG=0
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M  V30 3531 1 3712 3725 CFG=0
M  V30 3532 1 3714 3715 CFG=0
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M  V30 3538 1 3719 3720 CFG=0
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M  V30 3543 2 3725 3726 CFG=0
M  V30 3544 1 3727 3728 CFG=0
M  V30 3545 1 3727 3729 CFG=0
M  V30 3546 1 3729 3730 CFG=0
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M  V30 3549 1 3731 3732 CFG=0
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M  V30 3558 1 3740 3741 CFG=0
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M  V30 3561 2 3744 3745 CFG=0
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M  V30 3570 2 3754 3755 CFG=0
M  V30 3571 1 3756 3757 CFG=0
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M  V30 3576 1 3760 3761 CFG=0
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M  V30 3583 1 3769 3770 CFG=0
M  V30 3584 1 3769 3771 CFG=0
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M  V30 3586 1 3771 3772 CFG=0
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M  V30 3588 1 3771 3774 CFG=0
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M  V30 3599 1 3784 3802 CFG=0
M  V30 3600 1 3786 3787 CFG=0
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M  V30 3602 1 3786 3789 CFG=0
M  V30 3603 1 3789 3790 CFG=0
M  V30 3604 1 3789 3791 CFG=0
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M  V30 3606 1 3792 3793 CFG=0
M  V30 3607 1 3792 3794 CFG=0
M  V30 3608 1 3792 3795 CFG=0
M  V30 3609 1 3795 3796 CFG=0
M  V30 3610 1 3795 3797 CFG=0
M  V30 3611 1 3795 3798 CFG=0
M  V30 3612 1 3798 3799 CFG=0
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M  V30 3615 2 3802 3803 CFG=0
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M  V30 3624 1 3810 3811 CFG=0
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M  V30 3630 2 3818 3819 CFG=0
M  V30 3631 1 3820 3821 CFG=0
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M  V30 3641 1 3828 3829 CFG=0
M  V30 3642 1 3828 3830 CFG=0
M  V30 3643 1 3830 3831 CFG=0
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M  V30 4124 1 4337 4338 CFG=0
M  V30 4125 1 4337 4339 CFG=0
M  V30 4126 1 4337 4348 CFG=0
M  V30 4127 1 4339 4340 CFG=0
M  V30 4128 1 4339 4341 CFG=0
M  V30 4129 1 4339 4342 CFG=0
M  V30 4130 1 4342 4343 CFG=0
M  V30 4131 1 4342 4344 CFG=0
M  V30 4132 1 4342 4345 CFG=0
M  V30 4133 2 4345 4346 CFG=0
M  V30 4134 1 4345 4347 CFG=0
M  V30 4135 2 4348 4349 CFG=0
M  V30 4136 1 4348 4350 CFG=0
M  V30 4137 1 22 24 CFG=0
M  V30 4138 1 29 31 CFG=0
M  V30 4139 1 40 42 CFG=0
M  V30 4140 1 64 66 CFG=0
M  V30 4141 1 79 81 CFG=0
M  V30 4142 1 98 100 CFG=0
M  V30 4143 1 110 112 CFG=0
M  V30 4144 1 124 126 CFG=0
M  V30 4145 1 146 148 CFG=0
M  V30 4146 1 158 160 CFG=0
M  V30 4147 1 177 179 CFG=0
M  V30 4148 1 191 193 CFG=0
M  V30 4149 1 211 213 CFG=0
M  V30 4150 1 230 232 CFG=0
M  V30 4151 1 252 254 CFG=0
M  V30 4152 1 267 269 CFG=0
M  V30 4153 1 286 288 CFG=0
M  V30 4154 1 293 295 CFG=0
M  V30 4155 1 307 309 CFG=0
M  V30 4156 1 314 316 CFG=0
M  V30 4157 1 331 333 CFG=0
M  V30 4158 1 351 353 CFG=0
M  V30 4159 1 358 360 CFG=0
M  V30 4160 1 374 376 CFG=0
M  V30 4161 1 390 392 CFG=0
M  V30 4162 1 412 414 CFG=0
M  V30 4163 1 433 435 CFG=0
M  V30 4164 1 440 442 CFG=0
M  V30 4165 1 462 464 CFG=0
M  V30 4166 1 486 488 CFG=0
M  V30 4167 1 510 512 CFG=0
M  V30 4168 1 517 519 CFG=0
M  V30 4169 1 534 536 CFG=0
M  V30 4170 1 555 557 CFG=0
M  V30 4171 1 567 569 CFG=0
M  V30 4172 1 583 585 CFG=0
M  V30 4173 1 593 595 CFG=0
M  V30 4174 1 612 614 CFG=0
M  V30 4175 1 634 636 CFG=0
M  V30 4176 1 651 653 CFG=0
M  V30 4177 1 670 672 CFG=0
M  V30 4178 1 692 694 CFG=0
M  V30 4179 1 707 709 CFG=0
M  V30 4180 1 714 716 CFG=0
M  V30 4181 1 725 727 CFG=0
M  V30 4182 1 742 744 CFG=0
M  V30 4183 1 753 755 CFG=0
M  V30 4184 1 768 770 CFG=0
M  V30 4185 1 780 782 CFG=0
M  V30 4186 1 795 797 CFG=0
M  V30 4187 1 815 817 CFG=0
M  V30 4188 1 834 836 CFG=0
M  V30 4189 1 849 851 CFG=0
M  V30 4190 1 864 866 CFG=0
M  V30 4191 1 874 876 CFG=0
M  V30 4192 1 896 898 CFG=0
M  V30 4193 1 912 914 CFG=0
M  V30 4194 1 929 931 CFG=0
M  V30 4195 1 946 948 CFG=0
M  V30 4196 1 960 962 CFG=0
M  V30 4197 1 979 981 CFG=0
M  V30 4198 1 990 992 CFG=0
M  V30 4199 1 1007 1009 CFG=0
M  V30 4200 1 1022 1024 CFG=0
M  V30 4201 1 1044 1046 CFG=0
M  V30 4202 1 1063 1065 CFG=0
M  V30 4203 1 1079 1081 CFG=0
M  V30 4204 1 1096 1098 CFG=0
M  V30 4205 1 1115 1117 CFG=0
M  V30 4206 1 1136 1138 CFG=0
M  V30 4207 1 1143 1145 CFG=0
M  V30 4208 1 1159 1161 CFG=0
M  V30 4209 1 1170 1172 CFG=0
M  V30 4210 1 1184 1186 CFG=0
M  V30 4211 1 1206 1208 CFG=0
M  V30 4212 1 1223 1225 CFG=0
M  V30 4213 1 1247 1249 CFG=0
M  V30 4214 1 1261 1263 CFG=0
M  V30 4215 1 1280 1282 CFG=0
M  V30 4216 1 1300 1302 CFG=0
M  V30 4217 1 1319 1321 CFG=0
M  V30 4218 1 1338 1340 CFG=0
M  V30 4219 1 1352 1354 CFG=0
M  V30 4220 1 1367 1369 CFG=0
M  V30 4221 1 1388 1390 CFG=0
M  V30 4222 1 1405 1407 CFG=0
M  V30 4223 1 1415 1417 CFG=0
M  V30 4224 1 1429 1431 CFG=0
M  V30 4225 1 1436 1438 CFG=0
M  V30 4226 1 1447 1449 CFG=0
M  V30 4227 1 1466 1468 CFG=0
M  V30 4228 1 1485 1487 CFG=0
M  V30 4229 1 1499 1501 CFG=0
M  V30 4230 1 1520 1522 CFG=0
M  V30 4231 1 1539 1541 CFG=0
M  V30 4232 1 1563 1565 CFG=0
M  V30 4233 1 1578 1580 CFG=0
M  V30 4234 1 1595 1597 CFG=0
M  V30 4235 1 1619 1621 CFG=0
M  V30 4236 1 1636 1638 CFG=0
M  V30 4237 1 1660 1662 CFG=0
M  V30 4238 1 1680 1682 CFG=0
M  V30 4239 1 1697 1699 CFG=0
M  V30 4240 1 1711 1713 CFG=0
M  V30 4241 1 1728 1730 CFG=0
M  V30 4242 1 1745 1747 CFG=0
M  V30 4243 1 1764 1766 CFG=0
M  V30 4244 1 1783 1785 CFG=0
M  V30 4245 1 1798 1800 CFG=0
M  V30 4246 1 1815 1817 CFG=0
M  V30 4247 1 1826 1828 CFG=0
M  V30 4248 1 1848 1850 CFG=0
M  V30 4249 1 1860 1862 CFG=0
M  V30 4250 1 1876 1878 CFG=0
M  V30 4251 1 1887 1889 CFG=0
M  V30 4252 1 1902 1904 CFG=0
M  V30 4253 1 1912 1914 CFG=0
M  V30 4254 1 1929 1931 CFG=0
M  V30 4255 1 1944 1946 CFG=0
M  V30 4256 1 1965 1967 CFG=0
M  V30 4257 1 1984 1986 CFG=0
M  V30 4258 1 1999 2001 CFG=0
M  V30 4259 1 2010 2012 CFG=0
M  V30 4260 1 2032 2034 CFG=0
M  V30 4261 1 2049 2051 CFG=0
M  V30 4262 1 2069 2071 CFG=0
M  V30 4263 1 2088 2090 CFG=0
M  V30 4264 1 2106 2108 CFG=0
M  V30 4265 1 2130 2132 CFG=0
M  V30 4266 1 2142 2144 CFG=0
M  V30 4267 1 2161 2163 CFG=0
M  V30 4268 1 2171 2173 CFG=0
M  V30 4269 1 2181 2183 CFG=0
M  V30 4270 1 2205 2207 CFG=0
M  V30 4271 1 2219 2221 CFG=0
M  V30 4272 1 2230 2232 CFG=0
M  V30 4273 1 2249 2251 CFG=0
M  V30 4274 1 2265 2267 CFG=0
M  V30 4275 1 2279 2281 CFG=0
M  V30 4276 1 2291 2293 CFG=0
M  V30 4277 1 2308 2310 CFG=0
M  V30 4278 1 2315 2317 CFG=0
M  V30 4279 1 2331 2333 CFG=0
M  V30 4280 1 2347 2349 CFG=0
M  V30 4281 1 2369 2371 CFG=0
M  V30 4282 1 2385 2387 CFG=0
M  V30 4283 1 2396 2398 CFG=0
M  V30 4284 1 2408 2410 CFG=0
M  V30 4285 1 2428 2430 CFG=0
M  V30 4286 1 2435 2437 CFG=0
M  V30 4287 1 2454 2456 CFG=0
M  V30 4288 1 2465 2467 CFG=0
M  V30 4289 1 2489 2491 CFG=0
M  V30 4290 1 2510 2512 CFG=0
M  V30 4291 1 2526 2528 CFG=0
M  V30 4292 1 2545 2547 CFG=0
M  V30 4293 1 2557 2559 CFG=0
M  V30 4294 1 2569 2571 CFG=0
M  V30 4295 1 2584 2586 CFG=0
M  V30 4296 1 2605 2607 CFG=0
M  V30 4297 1 2619 2621 CFG=0
M  V30 4298 1 2630 2632 CFG=0
M  V30 4299 1 2641 2643 CFG=0
M  V30 4300 1 2657 2659 CFG=0
M  V30 4301 1 2664 2666 CFG=0
M  V30 4302 1 2675 2677 CFG=0
M  V30 4303 1 2697 2699 CFG=0
M  V30 4304 1 2717 2719 CFG=0
M  V30 4305 1 2731 2733 CFG=0
M  V30 4306 1 2747 2749 CFG=0
M  V30 4307 1 2771 2773 CFG=0
M  V30 4308 1 2795 2797 CFG=0
M  V30 4309 1 2806 2808 CFG=0
M  V30 4310 1 2820 2822 CFG=0
M  V30 4311 1 2834 2836 CFG=0
M  V30 4312 1 2849 2851 CFG=0
M  V30 4313 1 2865 2867 CFG=0
M  V30 4314 1 2884 2886 CFG=0
M  V30 4315 1 2901 2903 CFG=0
M  V30 4316 1 2922 2924 CFG=0
M  V30 4317 1 2933 2935 CFG=0
M  V30 4318 1 2955 2957 CFG=0
M  V30 4319 1 2975 2977 CFG=0
M  V30 4320 1 2986 2988 CFG=0
M  V30 4321 1 2997 2999 CFG=0
M  V30 4322 1 3019 3021 CFG=0
M  V30 4323 1 3030 3032 CFG=0
M  V30 4324 1 3042 3044 CFG=0
M  V30 4325 1 3061 3063 CFG=0
M  V30 4326 1 3085 3087 CFG=0
M  V30 4327 1 3095 3097 CFG=0
M  V30 4328 1 3115 3117 CFG=0
M  V30 4329 1 3122 3124 CFG=0
M  V30 4330 1 3138 3140 CFG=0
M  V30 4331 1 3157 3159 CFG=0
M  V30 4332 1 3174 3176 CFG=0
M  V30 4333 1 3198 3200 CFG=0
M  V30 4334 1 3214 3216 CFG=0
M  V30 4335 1 3233 3235 CFG=0
M  V30 4336 1 3254 3256 CFG=0
M  V30 4337 1 3265 3267 CFG=0
M  V30 4338 1 3284 3286 CFG=0
M  V30 4339 1 3291 3293 CFG=0
M  V30 4340 1 3313 3315 CFG=0
M  V30 4341 1 3330 3332 CFG=0
M  V30 4342 1 3344 3346 CFG=0
M  V30 4343 1 3365 3367 CFG=0
M  V30 4344 1 3380 3382 CFG=0
M  V30 4345 1 3404 3406 CFG=0
M  V30 4346 1 3424 3426 CFG=0
M  V30 4347 1 3438 3440 CFG=0
M  V30 4348 1 3452 3454 CFG=0
M  V30 4349 1 3463 3465 CFG=0
M  V30 4350 1 3478 3480 CFG=0
M  V30 4351 1 3492 3494 CFG=0
M  V30 4352 1 3502 3504 CFG=0
M  V30 4353 1 3517 3519 CFG=0
M  V30 4354 1 3534 3536 CFG=0
M  V30 4355 1 3553 3555 CFG=0
M  V30 4356 1 3563 3565 CFG=0
M  V30 4357 1 3580 3582 CFG=0
M  V30 4358 1 3587 3589 CFG=0
M  V30 4359 1 3606 3608 CFG=0
M  V30 4360 1 3630 3632 CFG=0
M  V30 4361 1 3649 3651 CFG=0
M  V30 4362 1 3670 3672 CFG=0
M  V30 4363 1 3694 3696 CFG=0
M  V30 4364 1 3708 3710 CFG=0
M  V30 4365 1 3725 3727 CFG=0
M  V30 4366 1 3744 3746 CFG=0
M  V30 4367 1 3754 3756 CFG=0
M  V30 4368 1 3765 3767 CFG=0
M  V30 4369 1 3780 3782 CFG=0
M  V30 4370 1 3802 3804 CFG=0
M  V30 4371 1 3818 3820 CFG=0
M  V30 4372 1 3839 3841 CFG=0
M  V30 4373 1 3853 3855 CFG=0
M  V30 4374 1 3872 3874 CFG=0
M  V30 4375 1 3889 3891 CFG=0
M  V30 4376 1 3910 3912 CFG=0
M  V30 4377 1 3921 3923 CFG=0
M  V30 4378 1 3932 3934 CFG=0
M  V30 4379 1 3956 3958 CFG=0
M  V30 4380 1 3973 3975 CFG=0
M  V30 4381 1 3988 3990 CFG=0
M  V30 4382 1 4010 4012 CFG=0
M  V30 4383 1 4020 4022 CFG=0
M  V30 4384 1 4032 4034 CFG=0
M  V30 4385 1 4047 4049 CFG=0
M  V30 4386 1 4071 4073 CFG=0
M  V30 4387 1 4085 4087 CFG=0
M  V30 4388 1 4099 4101 CFG=0
M  V30 4389 1 4119 4121 CFG=0
M  V30 4390 1 4141 4143 CFG=0
M  V30 4391 1 4160 4162 CFG=0
M  V30 4392 1 4179 4181 CFG=0
M  V30 4393 1 4198 4200 CFG=0
M  V30 4394 1 4209 4211 CFG=0
M  V30 4395 1 4223 4225 CFG=0
M  V30 4396 1 4242 4244 CFG=0
M  V30 4397 1 4261 4263 CFG=0
M  V30 4398 1 4273 4275 CFG=0
M  V30 4399 1 4289 4291 CFG=0
M  V30 4400 1 4306 4308 CFG=0
M  V30 4401 1 4318 4320 CFG=0
M  V30 4402 1 4333 4335 CFG=0
M  V30 END BOND
M  V30 END CTAB
M  END
> <OBJECTID>
9223372036858118160

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Resolution>
1.6

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <PartialChargeMethod>
MomanyRone

> <UseResidueTemplateCharge>
True

> <Refined Residues>
6

> <ChiRotor RMSD>
2.23148

> <ChiRotor E-total>
-21.3158

> <ChiRotor E-elec>
-2.6883

> <ChiRotor E-vdw>
-31.6052

> <Forcefield>
CHARMm

> <ForcefieldBase>
CHARMm

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Initial RMS Gradient>
11.8341

> <CHARMm Energy>
-65.3804

> <Bond Energy>
1.79762

> <Angle Energy>
8.48058

> <Urey-Bradley Energy>
0

> <Dihedral Energy>
10.5161

> <Improper Energy>
3.01515

> <Hydrogen Bond Energy>
0

> <Solvation Free Energy>
0

> <pI>
6.32

> <At pH>
7.4

> <Net Charge>
-4.97

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.3779    4.7472  -16.8097 N   0  0
  -18.3244    5.0182  -17.6159 C   0  0
  -18.4566    4.6354  -18.8981 N   0  0
  -17.4983    4.9628  -19.7820 C   0  0
  -16.3830    5.6205  -19.4753 N   0  0
  -16.2275    5.9581  -18.1883 C   0  0
  -17.1830    5.6534  -17.1922 C   0  0
  -15.1675    6.6395  -17.6009 N   0  0
  -13.9755    7.1175  -18.3294 C   0  0
  -12.6631    6.5469  -17.7856 C   0  0
  -11.5835    7.5564  -18.1966 C   0  0
  -12.3187    8.8451  -18.6010 C   0  0
  -13.7887    8.6289  -18.2361 C   0  0
  -15.4820    6.7376  -16.2951 C   0  0
  -16.6732    6.1193  -15.9606 C   0  0
  -17.2486    5.9866  -14.5983 C   0  0
  -17.3592    7.0910  -13.7792 C   0  0
  -17.8855    6.9741  -12.4993 C   0  0
  -18.3188    5.7477  -12.0140 C   0  0
  -18.1888    4.6353  -12.8318 C   0  0
  -17.6673    4.7608  -14.1151 C   0  0
  -18.7869    5.5963  -10.7150 O   0  0
  -19.6886    6.5505  -10.2489 C   0  0
  -20.7251    7.0638  -11.0301 C   0  0
  -21.6587    7.9289  -10.4743 C   0  0
  -21.5479    8.3094   -9.1431 C   0  0
  -20.4984    7.8276   -8.3720 C   0  0
  -19.5826    6.9405   -8.9212 C   0  0
  -20.1963    4.2955  -17.1751 H   0  0
  -19.3792    4.9818  -15.8368 H   0  0
  -17.6339    4.6644  -20.8112 H   0  0
  -14.0471    6.8518  -19.3866 H   0  0
  -12.4604    5.5443  -18.1626 H   0  0
  -12.6974    6.4835  -16.6976 H   0  0
  -10.8877    7.7331  -17.3758 H   0  0
  -11.0028    7.1766  -19.0383 H   0  0
  -12.2285    8.9897  -19.6782 H   0  0
  -11.9039    9.7294  -18.1164 H   0  0
  -13.9625    8.9719  -17.2157 H   0  0
  -14.4740    9.1689  -18.8895 H   0  0
  -14.8493    7.2421  -15.5791 H   0  0
  -17.0428    8.0669  -14.1217 H   0  0
  -17.9524    7.8406  -11.8712 H   0  0
  -18.4974    3.6658  -12.4709 H   0  0
  -17.5873    3.8705  -14.7217 H   0  0
  -20.8341    6.7740  -12.0655 H   0  0
  -22.4750    8.2954  -11.0798 H   0  0
  -22.2761    8.9784   -8.7067 H   0  0
  -20.3911    8.1422   -7.3447 H   0  0
  -18.7780    6.5496   -8.3184 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372041153085456

> <LigScore1_Dreiding>
4.79

> <LigScore2_Dreiding>
7

> <-PLP1>
122.28

> <-PLP2>
117.05

> <Jain>
8.54

> <-PMF>
117.53

> <-PMF04>
46.31

> <AbsoluteEnergy>
146.471

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
9

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.424

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
1

> <LibDockScore>
119.456

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-21.80,7.92,-10.89,A,54,25
-19.80,7.72,-8.89,A,70,28

> <-In-Situ Starting Energy>
-11.669

> <-In-Situ Final Energy>
43.229

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4107    4.7151  -16.7251 N   0  0  0  1  0  0
  -18.3569    5.0394  -17.5092 C   0  0  0  1  0  0
  -18.4622    4.6935  -18.8063 N   0  0  0  1  0  0
  -17.4900    5.0633  -19.6587 C   0  0  0  1  0  0
  -16.3977    5.7412  -19.3106 N   0  0  0  1  0  0
  -16.2791    6.0623  -18.0129 C   0  0  0  1  0  0
  -17.2437    5.6969  -17.0458 C   0  0  0  1  0  0
  -15.2653    6.7843  -17.3799 N   0  0  0  1  0  0
  -14.0808    7.3737  -18.0332 C   0  0  0  1  0  0
  -13.1971    6.3324  -18.7356 C   0  0  0  1  0  0
  -13.1628    6.7449  -20.2095 C   0  0  0  1  0  0
  -13.4024    8.2505  -20.1906 C   0  0  0  1  0  0
  -14.4427    8.4276  -19.0882 C   0  0  0  1  0  0
  -15.6015    6.8141  -16.0812 C   0  0  0  1  0  0
  -16.7741    6.1465  -15.7919 C   0  0  0  1  0  0
  -17.3587    5.9772  -14.4402 C   0  0  0  1  0  0
  -17.5246    7.0792  -13.6282 C   0  0  0  1  0  0
  -18.0436    6.9453  -12.3489 C   0  0  0  1  0  0
  -18.4134    5.7023  -11.8556 C   0  0  0  1  0  0
  -18.2263    4.5925  -12.6678 C   0  0  0  1  0  0
  -17.7210    4.7349  -13.9564 C   0  0  0  1  0  0
  -18.8891    5.5390  -10.5600 O   0  0  0  1  0  0
  -19.7611    6.5148  -10.0805 C   0  0  0  1  0  0
  -20.8216    7.0193  -10.8347 C   0  0  0  1  0  0
  -21.7115    7.9255  -10.2745 C   0  0  0  1  0  0
  -21.5354    8.3545   -8.9658 C   0  0  0  1  0  0
  -20.4616    7.8816   -8.2231 C   0  0  0  1  0  0
  -19.5884    6.9544   -8.7756 C   0  0  0  1  0  0
  -20.2226    4.2818  -17.1245 H   0  0
  -19.4200    4.8888  -15.7390 H   0  0
  -17.5958    4.7877  -20.6982 H   0  0
  -13.4793    7.8559  -17.2610 H   0  0
  -13.5713    5.3196  -18.5957 H   0  0
  -12.1882    6.3592  -18.3215 H   0  0
  -12.2318    6.4779  -20.7068 H   0  0
  -13.9764    6.2530  -20.7442 H   0  0
  -13.7274    8.6284  -21.1577 H   0  0
  -12.4809    8.7664  -19.9186 H   0  0
  -14.4621    9.4287  -18.6652 H   0  0
  -15.4306    8.2375  -19.5035 H   0  0
  -14.9989    7.3113  -15.3347 H   0  0
  -17.2564    8.0676  -13.9762 H   0  0
  -18.1562    7.8128  -11.7286 H   0  0
  -18.4779    3.6101  -12.2987 H   0  0
  -17.6006    3.8482  -14.5621 H   0  0
  -20.9772    6.7006  -11.8551 H   0  0
  -22.5445    8.2860  -10.8599 H   0  0
  -22.2314    9.0548   -8.5258 H   0  0
  -20.3020    8.2354   -7.2153 H   0  0
  -18.7622    6.5760   -8.1950 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372045448052752

> <LigScore1_Dreiding>
4.73

> <LigScore2_Dreiding>
6.83

> <-PLP1>
121.72

> <-PLP2>
118.01

> <Jain>
9.15

> <-PMF>
111.29

> <-PMF04>
39.46

> <AbsoluteEnergy>
164.152

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
51

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.105

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
7

> <LibDockScore>
118.453

> <HotSpots>
-17.60,6.32,-19.49,A,8,4
-17.40,4.12,-13.89,A,32,21
-21.60,7.92,-9.29,A,66,26

> <-In-Situ Starting Energy>
-30.688

> <-In-Situ Final Energy>
41.659

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.4901    6.7435  -17.4207 N   0  0  0  1  0  0
  -15.5710    6.3989  -18.7239 C   0  0  0  1  0  0
  -16.7033    5.7674  -19.0710 N   0  0  0  1  0  0
  -16.8417    5.3331  -20.3312 C   0  0  0  1  0  0
  -15.9058    5.4513  -21.2702 N   0  0  0  1  0  0
  -14.7865    6.1112  -20.9416 C   0  0  0  1  0  0
  -14.5845    6.6497  -19.6486 C   0  0  0  1  0  0
  -13.6730    6.4040  -21.7302 N   0  0  0  1  0  0
  -13.4593    6.0436  -23.1504 C   0  0  0  1  0  0
  -14.5822    5.3414  -23.9214 C   0  0  0  1  0  0
  -13.8696    4.7769  -25.1453 C   0  0  0  1  0  0
  -12.4957    4.3344  -24.6267 C   0  0  0  1  0  0
  -12.2454    5.1266  -23.3336 C   0  0  0  1  0  0
  -12.8430    7.0921  -20.9241 C   0  0  0  1  0  0
  -13.3524    7.3423  -19.6634 C   0  0  0  1  0  0
  -12.7211    8.1760  -18.6045 C   0  0  0  1  0  0
  -13.4796    9.0467  -17.8409 C   0  0  0  1  0  0
  -12.8956    9.8471  -16.8660 C   0  0  0  1  0  0
  -11.5258    9.7990  -16.6569 C   0  0  0  1  0  0
  -10.7559    8.9358  -17.4240 C   0  0  0  1  0  0
  -11.3561    8.1244  -18.3845 C   0  0  0  1  0  0
  -10.9347   10.6433  -15.7371 O   0  0  0  1  0  0
  -10.9556   10.2317  -14.4070 C   0  0  0  1  0  0
  -10.6764   11.2091  -13.4619 C   0  0  0  1  0  0
  -10.6421   10.8987  -12.1100 C   0  0  0  1  0  0
  -10.8691    9.5954  -11.6951 C   0  0  0  1  0  0
  -11.1502    8.6069  -12.6291 C   0  0  0  1  0  0
  -11.2030    8.9228  -13.9818 C   0  0  0  1  0  0
  -16.2943    6.6185  -16.8405 H   0  0
  -14.6464    7.1076  -17.0279 H   0  0
  -17.7630    4.8372  -20.5962 H   0  0
  -13.2589    6.9761  -23.6811 H   0  0
  -15.3982    6.0167  -24.1782 H   0  0
  -14.9985    4.5096  -23.3580 H   0  0
  -14.4265    3.9680  -25.6183 H   0  0
  -13.7468    5.5695  -25.8845 H   0  0
  -12.5015    3.2664  -24.4079 H   0  0
  -11.7147    4.5137  -25.3667 H   0  0
  -11.3138    5.6926  -23.3690 H   0  0
  -12.1661    4.4394  -22.4922 H   0  0
  -11.8687    7.4281  -21.2513 H   0  0
  -14.5456    9.1336  -17.9948 H   0  0
  -13.4981   10.5321  -16.2855 H   0  0
   -9.6883    8.9087  -17.2662 H   0  0
  -10.7319    7.4608  -18.9691 H   0  0
  -10.4874   12.2189  -13.7924 H   0  0
  -10.4354   11.6725  -11.3851 H   0  0
  -10.8170    9.3618  -10.6446 H   0  0
  -11.3101    7.5879  -12.3113 H   0  0
  -11.3996    8.1274  -14.6844 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372049743020048

> <LigScore1_Dreiding>
1.67

> <LigScore2_Dreiding>
4.65

> <-PLP1>
70.89

> <-PLP2>
63.18

> <Jain>
1.27

> <-PMF>
42.83

> <-PMF04>
-2.51

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
38

> <LibDockScore>
104.021

> <HotSpots>
-19.20,4.92,-17.69,A,16,4
-16.20,4.32,-22.89,A,1,11
-12.40,7.52,-12.49,A,43,28

> <-In-Situ Starting Energy>
-307.738

> <-In-Situ Final Energy>
9.608

> <In-Situ Gradient>
0.169

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4365    4.5262  -17.3423 N   0  0  0  1  0  0
  -18.3183    4.8977  -18.0045 C   0  0  0  1  0  0
  -18.3003    4.6678  -19.3254 N   0  0  0  1  0  0
  -17.2429    5.0667  -20.0506 C   0  0  0  1  0  0
  -16.1592    5.6475  -19.5416 N   0  0  0  1  0  0
  -16.1542    5.8297  -18.2148 C   0  0  0  1  0  0
  -17.2416    5.4702  -17.3864 C   0  0  0  1  0  0
  -15.1413    6.3584  -17.4242 N   0  0  0  1  0  0
  -13.8204    6.7669  -17.9460 C   0  0  0  1  0  0
  -12.8115    7.2107  -16.8871 C   0  0  0  1  0  0
  -11.7308    7.9218  -17.6993 C   0  0  0  1  0  0
  -12.4660    8.5706  -18.8812 C   0  0  0  1  0  0
  -13.8728    7.9531  -18.9137 C   0  0  0  1  0  0
  -15.6411    6.3733  -16.1727 C   0  0  0  1  0  0
  -16.9062    5.8205  -16.0655 C   0  0  0  1  0  0
  -17.6917    5.6950  -14.8127 C   0  0  0  1  0  0
  -18.9659    6.1956  -14.7341 C   0  0  0  1  0  0
  -19.4807    6.5931  -13.5203 C   0  0  0  1  0  0
  -18.8450    6.2541  -12.3477 C   0  0  0  1  0  0
  -17.7895    5.3710  -12.4437 C   0  0  0  1  0  0
  -17.1528    5.1601  -13.6670 C   0  0  0  1  0  0
  -19.0427    6.8745  -11.1260 O   0  0  0  1  0  0
  -20.2939    6.9204  -10.5398 C   0  0  0  1  0  0
  -20.2777    6.5964   -9.1987 C   0  0  0  1  0  0
  -21.4519    6.5578   -8.4770 C   0  0  0  1  0  0
  -22.6593    6.8758   -9.0806 C   0  0  0  1  0  0
  -22.6828    7.2357  -10.4172 C   0  0  0  1  0  0
  -21.5007    7.2912  -11.1371 C   0  0  0  1  0  0
  -20.2931    4.2817  -17.8001 H   0  0
  -19.4490    4.4637  -16.3441 H   0  0
  -17.2551    4.8872  -21.1153 H   0  0
  -13.3879    5.9104  -18.4680 H   0  0
  -12.4131    6.3782  -16.3076 H   0  0
  -13.2669    7.9204  -16.1960 H   0  0
  -11.1700    8.6430  -17.1038 H   0  0
  -11.0207    7.1845  -18.0766 H   0  0
  -12.5251    9.6514  -18.7556 H   0  0
  -11.9306    8.3783  -19.8118 H   0  0
  -14.1697    7.6497  -19.9182 H   0  0
  -14.6026    8.6849  -18.5645 H   0  0
  -15.1048    6.7749  -15.3261 H   0  0
  -19.5769    6.3561  -15.6025 H   0  0
  -20.2886    7.2835  -13.5528 H   0  0
  -17.4367    4.9476  -11.5242 H   0  0
  -16.2113    4.6344  -13.7155 H   0  0
  -19.3382    6.3500   -8.7280 H   0  0
  -21.4087    6.2311   -7.4541 H   0  0
  -23.5798    6.8429   -8.5165 H   0  0
  -23.6189    7.4747  -10.9017 H   0  0
  -21.5829    7.6470  -12.1448 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372054037987344

> <LigScore1_Dreiding>
3.62

> <LigScore2_Dreiding>
5.81

> <-PLP1>
108.97

> <-PLP2>
105.52

> <Jain>
8.4

> <-PMF>
108.44

> <-PMF04>
38.63

> <AbsoluteEnergy>
150.049

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
31

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.002

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
39

> <LibDockScore>
102.832

> <HotSpots>
-18.00,4.72,-19.09,A,9,4
-16.20,6.52,-15.49,A,24,14
-20.80,8.12,-10.89,P,69,22

> <-In-Situ Starting Energy>
-1171.203

> <-In-Situ Final Energy>
3.909

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.2891    8.1022  -13.4713 N   0  0  0  1  0  0
  -15.3315    7.4900  -14.6749 C   0  0  0  1  0  0
  -14.4249    7.9259  -15.5633 N   0  0  0  1  0  0
  -14.4355    7.4171  -16.8062 C   0  0  0  1  0  0
  -15.3197    6.5227  -17.2440 N   0  0  0  1  0  0
  -16.2126    6.0727  -16.3472 C   0  0  0  1  0  0
  -16.2326    6.5077  -15.0094 C   0  0  0  1  0  0
  -17.2886    5.1938  -16.5144 N   0  0  0  1  0  0
  -17.8926    4.7641  -17.7634 C   0  0  0  1  0  0
  -18.3222    6.0425  -18.4168 C   0  0  0  1  0  0
  -17.5123    6.1743  -19.6951 C   0  0  0  1  0  0
  -17.3185    4.7390  -20.1103 C   0  0  0  1  0  0
  -17.0208    4.0700  -18.7598 C   0  0  0  1  0  0
  -17.7690    4.9360  -15.3144 C   0  0  0  1  0  0
  -17.2542    5.7699  -14.3726 C   0  0  0  1  0  0
  -17.7809    5.8231  -13.0153 C   0  0  0  1  0  0
  -18.0417    4.6657  -12.3284 C   0  0  0  1  0  0
  -18.4663    4.7278  -11.0200 C   0  0  0  1  0  0
  -18.7369    5.9488  -10.4339 C   0  0  0  1  0  0
  -18.6246    7.0953  -11.1981 C   0  0  0  1  0  0
  -18.0746    7.0321  -12.4584 C   0  0  0  1  0  0
  -19.0573    6.0200   -9.1013 O   0  0  0  1  0  0
  -20.1276    6.8362   -8.8435 C   0  0  0  1  0  0
  -21.2607    6.8654   -9.6488 C   0  0  0  1  0  0
  -22.1750    7.8829   -9.4844 C   0  0  0  1  0  0
  -21.9462    8.8482   -8.5166 C   0  0  0  1  0  0
  -20.8570    8.7729   -7.6681 C   0  0  0  1  0  0
  -19.9828    7.7159   -7.7962 C   0  0  0  1  0  0
  -14.5810    8.7972  -13.3371 H   0  0
  -15.9727    7.8853  -12.7796 H   0  0
  -13.6803    7.7599  -17.4990 H   0  0
  -18.7783    4.1668  -17.5488 H   0  0
  -18.1175    6.9123  -17.8179 H   0  0
  -19.3943    5.9192  -18.4903 H   0  0
  -17.9494    6.8376  -20.4278 H   0  0
  -16.5362    6.6036  -19.4731 H   0  0
  -16.5438    4.6560  -20.8702 H   0  0
  -18.2347    4.3404  -20.5367 H   0  0
  -17.1969    2.9967  -18.7607 H   0  0
  -15.9949    4.2751  -18.4577 H   0  0
  -18.5240    4.1905  -15.1146 H   0  0
  -17.9114    3.6934  -12.7844 H   0  0
  -18.6015    3.8076  -10.4937 H   0  0
  -18.9495    8.0390  -10.8003 H   0  0
  -17.8994    7.9177  -13.0396 H   0  0
  -21.4145    6.1383  -10.4308 H   0  0
  -23.0398    7.9190  -10.1276 H   0  0
  -22.6348    9.6481   -8.3710 H   0  0
  -20.7238    9.5053   -6.8840 H   0  0
  -19.1583    7.5813   -7.1207 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372058332954640

> <LigScore1_Dreiding>
1.49

> <LigScore2_Dreiding>
3.57

> <-PLP1>
95.8

> <-PLP2>
98.5

> <Jain>
8.24

> <-PMF>
109.36

> <-PMF04>
34.06

> <AbsoluteEnergy>
157.761

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
48

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
11.714

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
40

> <LibDockScore>
100.696

> <HotSpots>
-17.20,4.12,-18.29,A,12,13
-18.80,5.32,-15.29,A,26,14
-20.00,7.52,-7.09,A,89,28

> <-In-Situ Starting Energy>
-1409.454

> <-In-Situ Final Energy>
-22.409

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -17.5917    3.0908  -13.8959 N   0  0  0  1  0  0
  -18.1133    3.9297  -12.9794 C   0  0  0  1  0  0
  -18.1239    3.5013  -11.7151 N   0  0  0  1  0  0
  -18.3075    4.4193  -10.7585 C   0  0  0  1  0  0
  -18.8138    5.5942  -10.9155 N   0  0  0  1  0  0
  -19.1012    5.8951  -12.1544 C   0  0  0  1  0  0
  -18.6228    5.1591  -13.2533 C   0  0  0  1  0  0
  -19.9882    6.8420  -12.5644 N   0  0  0  1  0  0
  -20.9592    7.5386  -11.6479 C   0  0  0  1  0  0
  -20.4125    7.8878  -10.2503 C   0  0  0  1  0  0
  -21.6341    8.2584   -9.4272 C   0  0  0  1  0  0
  -22.5446    7.0876   -9.7899 C   0  0  0  1  0  0
  -22.3181    6.8823  -11.2938 C   0  0  0  1  0  0
  -19.7002    6.8950  -13.8882 C   0  0  0  1  0  0
  -18.8156    5.9427  -14.3733 C   0  0  0  1  0  0
  -18.1835    5.7582  -15.7051 C   0  0  0  1  0  0
  -16.8345    6.0283  -15.8320 C   0  0  0  1  0  0
  -16.1967    5.9687  -17.0648 C   0  0  0  1  0  0
  -16.9143    5.6586  -18.2148 C   0  0  0  1  0  0
  -18.2502    5.3095  -18.0664 C   0  0  0  1  0  0
  -18.8799    5.3473  -16.8231 C   0  0  0  1  0  0
  -16.3806    5.5872  -19.5010 O   0  0  0  1  0  0
  -15.2667    6.3331  -19.8948 C   0  0  0  1  0  0
  -14.8455    7.5358  -19.3224 C   0  0  0  1  0  0
  -13.7167    8.1886  -19.8026 C   0  0  0  1  0  0
  -13.0232    7.6751  -20.8892 C   0  0  0  1  0  0
  -13.4763    6.5206  -21.5094 C   0  0  0  1  0  0
  -14.5997    5.8668  -21.0206 C   0  0  0  1  0  0
  -17.3419    2.1681  -13.6089 H   0  0
  -17.4770    3.3837  -14.8439 H   0  0
  -18.0177    4.3213   -9.7453 H   0  0
  -21.2749    8.4548  -12.1319 H   0  0
  -19.5761    8.5606  -10.2971 H   0  0
  -20.0336    7.0404   -9.6933 H   0  0
  -21.4300    8.3208   -8.3578 H   0  0
  -22.0599    9.2047   -9.7562 H   0  0
  -23.5886    7.2430   -9.5329 H   0  0
  -22.2190    6.1963   -9.2519 H   0  0
  -22.4096    5.8360  -11.5596 H   0  0
  -23.1221    7.4129  -11.8015 H   0  0
  -20.1512    7.6294  -14.5019 H   0  0
  -16.2484    6.3016  -14.9660 H   0  0
  -15.1344    6.1561  -17.1019 H   0  0
  -18.7976    5.0262  -18.9460 H   0  0
  -19.9301    5.0973  -16.7540 H   0  0
  -15.3804    7.9886  -18.5046 H   0  0
  -13.3752    9.0940  -19.3242 H   0  0
  -12.1324    8.1671  -21.2538 H   0  0
  -12.9455    6.1224  -22.3624 H   0  0
  -14.9564    4.9743  -21.5105 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372062627921936

> <LigScore1_Dreiding>
1.97

> <LigScore2_Dreiding>
3.79

> <-PLP1>
94.08

> <-PLP2>
93

> <Jain>
7.2

> <-PMF>
64.37

> <-PMF04>
4.61

> <AbsoluteEnergy>
146.833

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
13

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.786

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
41

> <LibDockScore>
100.518

> <HotSpots>
-22.60,6.72,-9.09,A,69,12
-17.80,5.12,-16.89,A,19,20
-14.40,5.92,-18.29,A,15,24

> <-In-Situ Starting Energy>
-21891142

> <-In-Situ Final Energy>
-39.53

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.5492    8.8031  -14.0805 N   0  0  0  1  0  0
  -14.3705    8.5894  -15.4007 C   0  0  0  1  0  0
  -13.4437    9.3794  -15.9643 N   0  0  0  1  0  0
  -13.1563    9.2251  -17.2611 C   0  0  0  1  0  0
  -13.7288    8.3221  -18.0490 N   0  0  0  1  0  0
  -14.6564    7.5254  -17.4928 C   0  0  0  1  0  0
  -15.0517    7.6436  -16.1371 C   0  0  0  1  0  0
  -15.3538    6.4647  -18.0684 N   0  0  0  1  0  0
  -15.1252    5.8995  -19.4139 C   0  0  0  1  0  0
  -14.2127    6.6485  -20.3884 C   0  0  0  1  0  0
  -14.4671    5.9822  -21.7408 C   0  0  0  1  0  0
  -15.8878    5.4044  -21.6701 C   0  0  0  1  0  0
  -16.3913    5.6299  -20.2313 C   0  0  0  1  0  0
  -16.2137    6.0463  -17.1207 C   0  0  0  1  0  0
  -16.0851    6.6953  -15.9054 C   0  0  0  1  0  0
  -16.8707    6.4086  -14.6674 C   0  0  0  1  0  0
  -17.2582    5.1154  -14.3513 C   0  0  0  1  0  0
  -17.9453    4.8298  -13.1700 C   0  0  0  1  0  0
  -18.2346    5.8391  -12.2623 C   0  0  0  1  0  0
  -17.8632    7.1321  -12.5936 C   0  0  0  1  0  0
  -17.2397    7.4165  -13.7996 C   0  0  0  1  0  0
  -18.7918    5.5349  -11.0228 O   0  0  0  1  0  0
  -19.6625    6.4709  -10.4637 C   0  0  0  1  0  0
  -20.7088    7.0440  -11.1872 C   0  0  0  1  0  0
  -21.6145    7.8905  -10.5611 C   0  0  0  1  0  0
  -21.4667    8.1916   -9.2132 C   0  0  0  1  0  0
  -20.4079    7.6488   -8.4961 C   0  0  0  1  0  0
  -19.5164    6.7848   -9.1193 C   0  0  0  1  0  0
  -14.0977    9.5940  -13.6660 H   0  0
  -15.1198    8.1947  -13.5390 H   0  0
  -12.4093    9.8757  -17.6929 H   0  0
  -14.6439    4.9493  -19.2072 H   0  0
  -13.1614    6.6044  -20.1001 H   0  0
  -14.5013    7.6978  -20.4428 H   0  0
  -14.3449    6.6810  -22.5682 H   0  0
  -13.7472    5.1797  -21.8973 H   0  0
  -16.5319    5.8762  -22.4081 H   0  0
  -15.8730    4.3437  -21.9158 H   0  0
  -16.9618    4.7796  -19.8575 H   0  0
  -17.0592    6.4889  -20.1834 H   0  0
  -16.9338    5.2597  -17.2974 H   0  0
  -17.0328    4.2929  -15.0143 H   0  0
  -18.2460    3.8162  -12.9450 H   0  0
  -18.0523    7.9190  -11.8929 H   0  0
  -17.0518    8.4532  -14.0387 H   0  0
  -20.8412    6.8092  -12.2340 H   0  0
  -22.4383    8.3040  -11.1249 H   0  0
  -22.1748    8.8456   -8.7231 H   0  0
  -20.2770    7.8951   -7.4528 H   0  0
  -18.7029    6.3492   -8.5609 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372066922889232

> <LigScore1_Dreiding>
2.51

> <LigScore2_Dreiding>
5.8

> <-PLP1>
100.25

> <-PLP2>
93.13

> <Jain>
4.96

> <-PMF>
114.73

> <-PMF04>
42.33

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
42

> <LibDockScore>
99.859

> <HotSpots>
-14.40,7.72,-18.49,A,11,13
-17.20,7.52,-13.09,A,39,21
-21.60,6.52,-10.49,A,59,24

> <-In-Situ Starting Energy>
-304.276

> <-In-Situ Final Energy>
19.637

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.1634    7.8379  -13.5214 N   0  0  0  1  0  0
  -14.0742    7.9824  -14.8620 C   0  0  0  1  0  0
  -13.0290    8.7068  -15.2898 N   0  0  0  1  0  0
  -12.8342    8.8444  -16.6098 C   0  0  0  1  0  0
  -13.6136    8.3049  -17.5459 N   0  0  0  1  0  0
  -14.6557    7.5751  -17.1148 C   0  0  0  1  0  0
  -14.9565    7.4113  -15.7476 C   0  0  0  1  0  0
  -15.5942    6.8684  -17.8636 N   0  0  0  1  0  0
  -15.5662    6.8110  -19.3369 C   0  0  0  1  0  0
  -16.6219    5.9078  -19.9966 C   0  0  0  1  0  0
  -16.0312    5.4855  -21.3572 C   0  0  0  1  0  0
  -14.5504    5.8752  -21.3218 C   0  0  0  1  0  0
  -14.2521    6.2653  -19.8733 C   0  0  0  1  0  0
  -16.4464    6.3257  -16.9676 C   0  0  0  1  0  0
  -16.1507    6.6590  -15.6577 C   0  0  0  1  0  0
  -16.9305    6.3229  -14.4377 C   0  0  0  1  0  0
  -17.3757    5.0408  -14.1682 C   0  0  0  1  0  0
  -18.0769    4.7581  -12.9936 C   0  0  0  1  0  0
  -18.3501    5.7644  -12.0740 C   0  0  0  1  0  0
  -17.9315    7.0501  -12.3759 C   0  0  0  1  0  0
  -17.2364    7.3248  -13.5411 C   0  0  0  1  0  0
  -18.9448    5.4673  -10.8504 O   0  0  0  1  0  0
  -19.7773    6.4415  -10.2995 C   0  0  0  1  0  0
  -20.8248    7.0156  -11.0196 C   0  0  0  1  0  0
  -21.6869    7.9150  -10.4069 C   0  0  0  1  0  0
  -21.4928    8.2685   -9.0778 C   0  0  0  1  0  0
  -20.4278    7.7285   -8.3680 C   0  0  0  1  0  0
  -19.5806    6.8114   -8.9762 C   0  0  0  1  0  0
  -13.5291    8.3881  -12.9792 H   0  0
  -14.8308    7.1961  -13.1475 H   0  0
  -11.9874    9.4324  -16.9347 H   0  0
  -15.6704    7.8364  -19.6857 H   0  0
  -17.5854    6.4070  -20.0963 H   0  0
  -16.7823    5.0117  -19.3975 H   0  0
  -16.1756    4.4243  -21.5449 H   0  0
  -16.5146    5.9815  -22.1950 H   0  0
  -13.8969    5.0918  -21.6985 H   0  0
  -14.3903    6.7426  -21.9622 H   0  0
  -13.4283    6.9760  -19.8057 H   0  0
  -13.9978    5.4049  -19.2608 H   0  0
  -17.2890    5.7053  -17.2383 H   0  0
  -17.1844    4.2352  -14.8625 H   0  0
  -18.4133    3.7509  -12.7918 H   0  0
  -18.1426    7.8448  -11.6915 H   0  0
  -16.9470    8.3494  -13.7343 H   0  0
  -20.9885    6.7474  -12.0537 H   0  0
  -22.5124    8.3285  -10.9673 H   0  0
  -22.1682    8.9627   -8.5974 H   0  0
  -20.2560    8.0203   -7.3425 H   0  0
  -18.7599    6.3821   -8.4242 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372071217856528

> <LigScore1_Dreiding>
2.59

> <LigScore2_Dreiding>
5.65

> <-PLP1>
98.55

> <-PLP2>
92.85

> <Jain>
5.83

> <-PMF>
116.02

> <-PMF04>
42.86

> <AbsoluteEnergy>
150.049

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
31

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.002

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
43

> <LibDockScore>
99.229

> <HotSpots>
-15.60,6.12,-19.69,A,6,13
-18.60,7.12,-11.89,A,46,20
-22.60,6.72,-9.09,A,69,26

> <-In-Situ Starting Energy>
-435.791

> <-In-Situ Final Energy>
20.08

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.7512    5.2545  -15.5537 N   0  0  0  1  0  0
  -17.2284    4.7841  -14.3828 C   0  0  0  1  0  0
  -17.3866    3.4548  -14.2671 N   0  0  0  1  0  0
  -18.0212    2.9785  -13.1818 C   0  0  0  1  0  0
  -18.3906    3.7317  -12.1494 N   0  0  0  1  0  0
  -18.2793    5.0503  -12.2907 C   0  0  0  1  0  0
  -17.5762    5.6213  -13.3649 C   0  0  0  1  0  0
  -18.7961    6.0782  -11.5056 N   0  0  0  1  0  0
  -19.7258    5.9305  -10.3578 C   0  0  0  1  0  0
  -19.1887    6.6421   -9.1050 C   0  0  0  1  0  0
  -20.0931    7.8473   -8.9874 C   0  0  0  1  0  0
  -21.4699    7.3596   -9.3588 C   0  0  0  1  0  0
  -21.1485    6.5254  -10.5893 C   0  0  0  1  0  0
  -18.2513    7.1866  -12.0200 C   0  0  0  1  0  0
  -17.3845    6.9806  -13.0786 C   0  0  0  1  0  0
  -16.4033    7.8892  -13.7398 C   0  0  0  1  0  0
  -15.0694    7.5258  -13.6844 C   0  0  0  1  0  0
  -14.0820    8.2758  -14.3105 C   0  0  0  1  0  0
  -14.4191    9.4249  -15.0130 C   0  0  0  1  0  0
  -15.7445    9.8329  -15.0208 C   0  0  0  1  0  0
  -16.7275    9.0529  -14.4133 C   0  0  0  1  0  0
  -13.4662   10.1392  -15.7227 O   0  0  0  1  0  0
  -12.7583    9.3891  -16.6561 C   0  0  0  1  0  0
  -11.3869    9.5819  -16.7553 C   0  0  0  1  0  0
  -10.6404    8.8627  -17.6809 C   0  0  0  1  0  0
  -11.2659    7.9485  -18.5194 C   0  0  0  1  0  0
  -12.6382    7.7580  -18.4328 C   0  0  0  1  0  0
  -13.3844    8.4795  -17.5091 C   0  0  0  1  0  0
  -16.6103    4.6187  -16.3099 H   0  0
  -16.5464    6.2242  -15.6823 H   0  0
  -18.2424    1.9229  -13.1252 H   0  0
  -19.8297    4.8718  -10.1799 H   0  0
  -18.1350    6.9140   -9.1707 H   0  0
  -19.3248    6.0573   -8.2026 H   0  0
  -20.0348    8.3734   -8.0341 H   0  0
  -19.8089    8.4781   -9.8149 H   0  0
  -22.1690    8.1702   -9.5684 H   0  0
  -21.8851    6.7412   -8.5616 H   0  0
  -21.9378    5.7846  -10.7065 H   0  0
  -21.1566    7.1553  -11.4804 H   0  0
  -18.5149    8.0900  -11.5343 H   0  0
  -14.7677    6.6324  -13.1567 H   0  0
  -13.0508    7.9549  -14.2745 H   0  0
  -16.0105   10.7376  -15.5489 H   0  0
  -17.7463    9.3614  -14.5519 H   0  0
  -10.9019   10.2880  -16.0978 H   0  0
   -9.5738    9.0196  -17.7472 H   0  0
  -10.6913    7.3884  -19.2455 H   0  0
  -13.1240    7.0506  -19.0894 H   0  0
  -14.4529    8.3306  -17.4670 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372075512823824

> <LigScore1_Dreiding>
1.6

> <LigScore2_Dreiding>
4.32

> <-PLP1>
88.08

> <-PLP2>
80.91

> <Jain>
5.17

> <-PMF>
102.19

> <-PMF04>
28.5

> <AbsoluteEnergy>
155.445

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
46

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
9.398

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
50

> <LibDockScore>
96.102

> <HotSpots>
-18.40,2.92,-12.29,P,54,3
-21.60,7.92,-9.29,A,66,11
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-718.586

> <-In-Situ Final Energy>
-6.263

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.6000    7.7023  -13.5374 N   0  0  0  1  0  0
  -14.7758    7.5938  -14.8717 C   0  0  0  1  0  0
  -13.8383    8.1687  -15.6390 N   0  0  0  1  0  0
  -13.9281    8.0339  -16.9713 C   0  0  0  1  0  0
  -14.9232    7.4096  -17.6013 N   0  0  0  1  0  0
  -15.8796    6.8586  -16.8358 C   0  0  0  1  0  0
  -15.8289    6.9168  -15.4267 C   0  0  0  1  0  0
  -17.0599    6.1904  -17.1833 N   0  0  0  1  0  0
  -17.6807    5.9939  -18.4896 C   0  0  0  1  0  0
  -17.0277    6.5606  -19.7450 C   0  0  0  1  0  0
  -16.5370    5.3856  -20.5404 C   0  0  0  1  0  0
  -17.5522    4.3154  -20.1543 C   0  0  0  1  0  0
  -17.8655    4.5055  -18.6988 C   0  0  0  1  0  0
  -17.5917    5.7501  -16.0445 C   0  0  0  1  0  0
  -16.9546    6.2262  -14.9398 C   0  0  0  1  0  0
  -17.4590    6.0516  -13.5755 C   0  0  0  1  0  0
  -17.7413    4.8056  -13.0619 C   0  0  0  1  0  0
  -18.2734    4.6841  -11.7856 C   0  0  0  1  0  0
  -18.6291    5.8182  -11.0761 C   0  0  0  1  0  0
  -18.3842    7.0603  -11.6317 C   0  0  0  1  0  0
  -17.7270    7.1741  -12.8382 C   0  0  0  1  0  0
  -19.1504    5.6882   -9.8106 O   0  0  0  1  0  0
  -20.0600    6.6511   -9.4186 C   0  0  0  1  0  0
  -21.1743    6.9615  -10.1894 C   0  0  0  1  0  0
  -22.0321    7.9669   -9.7865 C   0  0  0  1  0  0
  -21.7714    8.6741   -8.6216 C   0  0  0  1  0  0
  -20.6601    8.3633   -7.8517 C   0  0  0  1  0  0
  -19.8261    7.3250   -8.2325 C   0  0  0  1  0  0
  -13.8730    8.3175  -13.2313 H   0  0
  -15.1943    7.1635  -12.9439 H   0  0
  -13.1423    8.4654  -17.5750 H   0  0
  -18.6657    6.4372  -18.4103 H   0  0
  -16.2393    7.2862  -19.5772 H   0  0
  -17.8123    7.0542  -20.3152 H   0  0
  -16.5032    5.5730  -21.6139 H   0  0
  -15.5226    5.1880  -20.2028 H   0  0
  -17.2181    3.3164  -20.2629 H   0  0
  -18.4371    4.4088  -20.7585 H   0  0
  -18.8649    4.1650  -18.4284 H   0  0
  -17.1469    3.9312  -18.1107 H   0  0
  -18.4646    5.1118  -16.0027 H   0  0
  -17.5542    3.9105  -13.6394 H   0  0
  -18.4427    3.7087  -11.3547 H   0  0
  -18.7148    7.9435  -11.1234 H   0  0
  -17.4918    8.1503  -13.2354 H   0  0
  -21.3783    6.4379  -11.1094 H   0  0
  -22.8948    8.1814  -10.3946 H   0  0
  -22.4398    9.4543   -8.2956 H   0  0
  -20.4591    8.9148   -6.9443 H   0  0
  -18.9747    7.0539   -7.6282 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372079807791120

> <LigScore1_Dreiding>
1.86

> <LigScore2_Dreiding>
4.32

> <-PLP1>
97.68

> <-PLP2>
98.05

> <Jain>
8

> <-PMF>
114.5

> <-PMF04>
36.8

> <AbsoluteEnergy>
164.245

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
52

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.198

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
52

> <LibDockScore>
95.987

> <HotSpots>
-14.40,7.72,-18.49,A,11,4
-17.80,5.12,-16.89,A,19,14
-19.80,7.72,-8.89,A,70,28

> <-In-Situ Starting Energy>
-413.447

> <-In-Situ Final Energy>
-7.645

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.1483    7.9424  -11.7676 N   0  0  0  1  0  0
  -10.9305    8.0891  -12.8497 C   0  0  0  1  0  0
  -10.7735    7.1444  -13.7883 N   0  0  0  1  0  0
  -11.4839    7.2303  -14.9224 C   0  0  0  1  0  0
  -12.4309    8.1333  -15.1386 N   0  0  0  1  0  0
  -12.6295    9.0319  -14.1648 C   0  0  0  1  0  0
  -11.8515    9.0937  -12.9936 C   0  0  0  1  0  0
  -13.6281    9.9858  -14.0866 N   0  0  0  1  0  0
  -14.7127   10.0436  -15.0879 C   0  0  0  1  0  0
  -15.5592    8.7721  -14.9049 C   0  0  0  1  0  0
  -16.6534    9.1776  -13.9320 C   0  0  0  1  0  0
  -16.9620   10.6372  -14.2728 C   0  0  0  1  0  0
  -15.6943   11.2111  -14.9100 C   0  0  0  1  0  0
  -13.3609   10.7035  -12.9720 C   0  0  0  1  0  0
  -12.2807   10.2185  -12.2493 C   0  0  0  1  0  0
  -11.7421   10.7526  -10.9664 C   0  0  0  1  0  0
  -12.6100   11.0639   -9.9398 C   0  0  0  1  0  0
  -12.1494   11.4628   -8.6941 C   0  0  0  1  0  0
  -10.7937   11.5974   -8.4591 C   0  0  0  1  0  0
   -9.9079   11.3614   -9.5109 C   0  0  0  1  0  0
  -10.3876   10.9423  -10.7530 C   0  0  0  1  0  0
  -10.4058   11.8607   -7.1544 O   0  0  0  1  0  0
   -9.3353   12.7135   -6.9386 C   0  0  0  1  0  0
   -9.1123   13.8625   -7.6946 C   0  0  0  1  0  0
   -8.0403   14.6924   -7.3955 C   0  0  0  1  0  0
   -7.2052   14.3874   -6.3296 C   0  0  0  1  0  0
   -7.4493   13.2659   -5.5507 C   0  0  0  1  0  0
   -8.5104   12.4289   -5.8602 C   0  0  0  1  0  0
   -9.4969    7.1836  -11.7613 H   0  0
  -10.2126    8.5680  -10.9930 H   0  0
  -11.2910    6.5079  -15.7021 H   0  0
  -14.2627   10.0863  -16.0815 H   0  0
  -15.0080    7.9064  -14.5395 H   0  0
  -15.9921    8.4563  -15.8465 H   0  0
  -17.5103    8.5112  -14.0198 H   0  0
  -16.2772    9.1170  -12.9107 H   0  0
  -17.2567   11.2163  -13.3966 H   0  0
  -17.7729   10.6779  -14.9984 H   0  0
  -15.9400   11.6448  -15.8804 H   0  0
  -15.2772   12.0207  -14.3145 H   0  0
  -13.9351   11.5651  -12.6569 H   0  0
  -13.6738   10.9971  -10.0734 H   0  0
  -12.8477   11.6564   -7.8928 H   0  0
   -8.8452   11.4720   -9.3563 H   0  0
   -9.6837   10.7598  -11.5533 H   0  0
   -9.7760   14.1296   -8.5029 H   0  0
   -7.8646   15.5826   -7.9808 H   0  0
   -6.3699   15.0280   -6.0918 H   0  0
   -6.8113   13.0498   -4.7050 H   0  0
   -8.7104   11.5589   -5.2532 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372084102758416

> <LigScore1_Dreiding>
2.76

> <LigScore2_Dreiding>
5.13

> <-PLP1>
84.08

> <-PLP2>
80.06

> <Jain>
4.03

> <-PMF>
108.98

> <-PMF04>
40.86

> <AbsoluteEnergy>
152.006

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
37

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.959

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
53

> <LibDockScore>
95.601

> <HotSpots>
-11.40,6.12,-12.49,P,51,3
-16.80,9.32,-14.09,A,31,11
-12.00,11.32,-8.69,A,74,18

> <-In-Situ Starting Energy>
-210.905

> <-In-Situ Final Energy>
13.188

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.6642   11.3160  -12.7936 N   0  0  0  1  0  0
   -9.0033   11.5348  -11.5027 C   0  0  0  1  0  0
   -7.9670   11.7066  -10.6537 N   0  0  0  1  0  0
   -8.2295   12.0922   -9.3924 C   0  0  0  1  0  0
   -9.4490   12.1713   -8.8699 N   0  0  0  1  0  0
  -10.4783   11.9477   -9.6997 C   0  0  0  1  0  0
  -10.3036   11.5938  -11.0599 C   0  0  0  1  0  0
  -11.8394   12.0327   -9.4318 N   0  0  0  1  0  0
  -12.4322   12.4237   -8.1362 C   0  0  0  1  0  0
  -13.2115   13.7307   -8.3128 C   0  0  0  1  0  0
  -14.6753   13.3397   -8.4770 C   0  0  0  1  0  0
  -14.8205   12.0915   -7.6117 C   0  0  0  1  0  0
  -13.4568   11.3884   -7.6367 C   0  0  0  1  0  0
  -12.4512   11.7175  -10.5849 C   0  0  0  1  0  0
  -11.5919   11.3986  -11.6179 C   0  0  0  1  0  0
  -12.0175   10.9562  -12.9753 C   0  0  0  1  0  0
  -13.1185   11.5439  -13.5733 C   0  0  0  1  0  0
  -13.5759   11.1161  -14.8145 C   0  0  0  1  0  0
  -12.9323   10.0902  -15.4931 C   0  0  0  1  0  0
  -11.8149    9.5050  -14.8969 C   0  0  0  1  0  0
  -11.3673    9.9412  -13.6533 C   0  0  0  1  0  0
  -13.4798    9.6633  -16.7000 O   0  0  0  1  0  0
  -12.6062    9.1192  -17.6298 C   0  0  0  1  0  0
  -11.4848    9.8176  -18.0684 C   0  0  0  1  0  0
  -10.6362    9.2530  -19.0127 C   0  0  0  1  0  0
  -10.9192    7.9977  -19.5349 C   0  0  0  1  0  0
  -12.0485    7.3077  -19.1134 C   0  0  0  1  0  0
  -12.8933    7.8710  -18.1661 C   0  0  0  1  0  0
   -7.7036   11.2196  -13.0482 H   0  0
   -9.3533   11.2482  -13.5161 H   0  0
   -7.3960   12.3535   -8.7533 H   0  0
  -11.6422   12.5675   -7.3965 H   0  0
  -12.8447   14.3565   -9.1268 H   0  0
  -13.1077   14.2998   -7.3978 H   0  0
  -15.3541   14.1399   -8.1787 H   0  0
  -14.8884   13.1025   -9.5192 H   0  0
  -15.6219   11.4516   -7.9737 H   0  0
  -15.0591   12.3873   -6.5900 H   0  0
  -13.1930   11.0172   -6.6455 H   0  0
  -13.4974   10.5233   -8.2959 H   0  0
  -13.5258   11.7126  -10.6878 H   0  0
  -13.6558   12.3501  -13.0879 H   0  0
  -14.4441   11.5840  -15.2584 H   0  0
  -11.2892    8.6898  -15.3744 H   0  0
  -10.5152    9.4377  -13.2181 H   0  0
  -11.2737   10.8002  -17.6730 H   0  0
   -9.7579    9.7873  -19.3448 H   0  0
  -10.2635    7.5499  -20.2709 H   0  0
  -12.2635    6.3332  -19.5280 H   0  0
  -13.7714    7.3366  -17.8364 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372088397725712

> <LigScore1_Dreiding>
2.43

> <LigScore2_Dreiding>
4.77

> <-PLP1>
65.68

> <-PLP2>
58.94

> <Jain>
0.86

> <-PMF>
72.92

> <-PMF04>
27.51

> <AbsoluteEnergy>
151.939

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
36

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.892

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
59

> <LibDockScore>
93.559

> <HotSpots>
-14.00,11.52,-7.09,A,94,13
-11.00,6.92,-12.09,A,44,20
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-1334.716

> <-In-Situ Final Energy>
20.35

> <In-Situ Gradient>
0.397

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.0639    7.7496  -13.1724 N   0  0  0  1  0  0
  -14.1653    7.9284  -14.5064 C   0  0  0  1  0  0
  -13.1690    8.6119  -15.0900 N   0  0  0  1  0  0
  -13.1448    8.6994  -16.4310 C   0  0  0  1  0  0
  -14.0542    8.1559  -17.2427 N   0  0  0  1  0  0
  -15.0614    7.4964  -16.6482 C   0  0  0  1  0  0
  -15.1846    7.3911  -15.2453 C   0  0  0  1  0  0
  -16.1150    6.7898  -17.2233 N   0  0  0  1  0  0
  -16.2830    6.5213  -18.6531 C   0  0  0  1  0  0
  -15.7516    5.1325  -18.8573 C   0  0  0  1  0  0
  -16.9267    4.2042  -18.4532 C   0  0  0  1  0  0
  -18.1250    4.8803  -19.0570 C   0  0  0  1  0  0
  -17.7446    6.3499  -19.0930 C   0  0  0  1  0  0
  -16.8802    6.3802  -16.2097 C   0  0  0  1  0  0
  -16.3877    6.7031  -14.9780 C   0  0  0  1  0  0
  -17.0763    6.3660  -13.7196 C   0  0  0  1  0  0
  -17.4354    5.0620  -13.4437 C   0  0  0  1  0  0
  -18.1627    4.7539  -12.2994 C   0  0  0  1  0  0
  -18.5878    5.7628  -11.4498 C   0  0  0  1  0  0
  -18.2436    7.0695  -11.7607 C   0  0  0  1  0  0
  -17.4361    7.3623  -12.8473 C   0  0  0  1  0  0
  -19.2986    5.4308  -10.3063 O   0  0  0  1  0  0
  -20.0960    6.4333   -9.7748 C   0  0  0  1  0  0
  -21.2094    6.9002  -10.4639 C   0  0  0  1  0  0
  -21.9837    7.9125   -9.9259 C   0  0  0  1  0  0
  -21.6408    8.4807   -8.7071 C   0  0  0  1  0  0
  -20.5150    8.0328   -8.0285 C   0  0  0  1  0  0
  -19.7530    6.9992   -8.5548 C   0  0  0  1  0  0
  -13.3977    8.3260  -12.6976 H   0  0
  -14.6296    7.0379  -12.7575 H   0  0
  -12.3299    9.2472  -16.8831 H   0  0
  -15.7429    7.2592  -19.2503 H   0  0
  -14.8219    4.9274  -18.3244 H   0  0
  -15.5390    5.1274  -19.9261 H   0  0
  -16.9369    3.1732  -18.7777 H   0  0
  -17.0088    4.1376  -17.3733 H   0  0
  -18.2639    4.5194  -20.0764 H   0  0
  -19.0297    4.6899  -18.4779 H   0  0
  -18.4298    6.8675  -18.4404 H   0  0
  -17.8549    6.7423  -20.1033 H   0  0
  -17.8104    5.8447  -16.3387 H   0  0
  -17.1630    4.2581  -14.1138 H   0  0
  -18.4175    3.7273  -12.0819 H   0  0
  -18.6179    7.8727  -11.1586 H   0  0
  -17.1560    8.3884  -13.0416 H   0  0
  -21.4791    6.4908  -11.4248 H   0  0
  -22.8510    8.2421  -10.4722 H   0  0
  -22.2511    9.2656   -8.2840 H   0  0
  -20.2342    8.4863   -7.0889 H   0  0
  -18.8770    6.6493   -8.0321 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372092692693008

> <LigScore1_Dreiding>
2.08

> <LigScore2_Dreiding>
4.57

> <-PLP1>
88.98

> <-PLP2>
88.32

> <Jain>
6.71

> <-PMF>
113.51

> <-PMF04>
40.98

> <AbsoluteEnergy>
149.96

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
29

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.913

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
60

> <LibDockScore>
93.299

> <HotSpots>
-18.60,3.92,-18.69,A,10,11
-18.60,7.12,-11.89,A,46,20
-20.40,8.32,-7.89,A,83,27

> <-In-Situ Starting Energy>
-377.287

> <-In-Situ Final Energy>
-2.619

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.5480    8.8027  -14.0813 N   0  0  0  1  0  0
  -14.3696    8.5892  -15.4016 C   0  0  0  1  0  0
  -13.4429    9.3792  -15.9653 N   0  0  0  1  0  0
  -13.1557    9.2250  -17.2621 C   0  0  0  1  0  0
  -13.7284    8.3221  -18.0500 N   0  0  0  1  0  0
  -14.6560    7.5254  -17.4937 C   0  0  0  1  0  0
  -15.0510    7.6435  -16.1380 C   0  0  0  1  0  0
  -15.3534    6.4648  -18.0692 N   0  0  0  1  0  0
  -15.1250    5.8995  -19.4148 C   0  0  0  1  0  0
  -14.2125    6.6485  -20.3894 C   0  0  0  1  0  0
  -14.4671    5.9821  -21.7417 C   0  0  0  1  0  0
  -15.8877    5.4042  -21.6708 C   0  0  0  1  0  0
  -16.3912    5.6298  -20.2320 C   0  0  0  1  0  0
  -16.2133    6.0464  -17.1215 C   0  0  0  1  0  0
  -16.0845    6.6953  -15.9062 C   0  0  0  1  0  0
  -16.8700    6.4087  -14.6681 C   0  0  0  1  0  0
  -17.2577    5.1156  -14.3521 C   0  0  0  1  0  0
  -17.9448    4.8300  -13.1708 C   0  0  0  1  0  0
  -18.2339    5.8393  -12.2630 C   0  0  0  1  0  0
  -17.8623    7.1322  -12.5942 C   0  0  0  1  0  0
  -17.2388    7.4165  -13.8002 C   0  0  0  1  0  0
  -18.7910    5.5350  -11.0235 O   0  0  0  1  0  0
  -19.6624    6.4705  -10.4645 C   0  0  0  1  0  0
  -19.5166    6.7848   -9.1202 C   0  0  0  1  0  0
  -20.4085    7.6488   -8.4975 C   0  0  0  1  0  0
  -21.4669    8.1916   -9.2150 C   0  0  0  1  0  0
  -21.6140    7.8906  -10.5631 C   0  0  0  1  0  0
  -20.7080    7.0440  -11.1887 C   0  0  0  1  0  0
  -14.0965    9.5934  -13.6668 H   0  0
  -15.1184    8.1941  -13.5398 H   0  0
  -12.4087    9.8756  -17.6940 H   0  0
  -14.6436    4.9493  -19.2080 H   0  0
  -13.1613    6.6045  -20.1011 H   0  0
  -14.5011    7.6978  -20.4438 H   0  0
  -14.3450    6.6809  -22.5692 H   0  0
  -13.7471    5.1797  -21.8982 H   0  0
  -15.8728    4.3434  -21.9164 H   0  0
  -16.5319    5.8758  -22.4089 H   0  0
  -17.0591    6.4887  -20.1841 H   0  0
  -16.9615    4.7795  -19.8581 H   0  0
  -16.9335    5.2598  -17.2982 H   0  0
  -17.0325    4.2930  -15.0152 H   0  0
  -18.2455    3.8164  -12.9458 H   0  0
  -18.0513    7.9190  -11.8935 H   0  0
  -17.0507    8.4533  -14.0392 H   0  0
  -18.7034    6.3494   -8.5614 H   0  0
  -20.2780    7.8952   -7.4541 H   0  0
  -22.1752    8.8456   -8.7253 H   0  0
  -22.4373    8.3042  -11.1273 H   0  0
  -20.8395    6.8093  -12.2356 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372096987660304

> <LigScore1_Dreiding>
2.51

> <LigScore2_Dreiding>
5.8

> <-PLP1>
100.25

> <-PLP2>
93.12

> <Jain>
4.96

> <-PMF>
114.62

> <-PMF04>
42.32

> <AbsoluteEnergy>
150.942

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
33

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
4.895

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
63

> <LibDockScore>
91.951

> <HotSpots>
-18.60,3.92,-18.69,A,10,13
-18.60,7.12,-11.89,A,46,20
-22.60,6.72,-9.09,A,69,26

> <-In-Situ Starting Energy>
-1045.633

> <-In-Situ Final Energy>
19.635

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.3386    9.5249  -14.4201 N   0  0  0  1  0  0
  -14.7535    8.9767  -15.5087 C   0  0  0  1  0  0
  -13.7021    9.6693  -15.9740 N   0  0  0  1  0  0
  -13.1403    9.3071  -17.1330 C   0  0  0  1  0  0
  -13.5572    8.2894  -17.8782 N   0  0  0  1  0  0
  -14.5729    7.5566  -17.3938 C   0  0  0  1  0  0
  -15.1924    7.8343  -16.1469 C   0  0  0  1  0  0
  -15.2138    6.4639  -17.9768 N   0  0  0  1  0  0
  -14.9518    5.8770  -19.3064 C   0  0  0  1  0  0
  -14.0469    6.6377  -20.2806 C   0  0  0  1  0  0
  -14.3436    6.0270  -21.6536 C   0  0  0  1  0  0
  -15.7655    5.4528  -21.5700 C   0  0  0  1  0  0
  -16.2343    5.6608  -20.1195 C   0  0  0  1  0  0
  -16.1068    6.0521  -17.0654 C   0  0  0  1  0  0
  -16.1636    6.8207  -15.9184 C   0  0  0  1  0  0
  -17.0985    6.5958  -14.7755 C   0  0  0  1  0  0
  -16.8590    7.0503  -13.4931 C   0  0  0  1  0  0
  -17.8705    7.0641  -12.5337 C   0  0  0  1  0  0
  -19.1397    6.5781  -12.8355 C   0  0  0  1  0  0
  -19.3109    5.9730  -14.0641 C   0  0  0  1  0  0
  -18.2956    5.9440  -15.0056 C   0  0  0  1  0  0
  -20.2992    6.7180  -12.0739 O   0  0  0  1  0  0
  -20.2799    7.0790  -10.7368 C   0  0  0  1  0  0
  -21.3226    7.8868  -10.3026 C   0  0  0  1  0  0
  -21.3820    8.3121   -8.9828 C   0  0  0  1  0  0
  -20.3936    7.9192   -8.0920 C   0  0  0  1  0  0
  -19.4019    7.0392   -8.4998 C   0  0  0  1  0  0
  -19.3555    6.5995   -9.8147 C   0  0  0  1  0  0
  -14.8773   10.2769  -13.9478 H   0  0
  -16.2304    9.2237  -14.0861 H   0  0
  -12.2966    9.8828  -17.4862 H   0  0
  -14.5026    4.9108  -19.1011 H   0  0
  -12.9908    6.5724  -20.0146 H   0  0
  -14.3240    7.6920  -20.2993 H   0  0
  -14.2418    6.7611  -22.4525 H   0  0
  -13.6330    5.2293  -21.8683 H   0  0
  -15.7573    4.3963  -21.8323 H   0  0
  -16.4343    5.9280  -22.2850 H   0  0
  -16.8683    6.5436  -20.0485 H   0  0
  -16.8353    4.8278  -19.7551 H   0  0
  -16.7256    5.1835  -17.2385 H   0  0
  -15.8855    7.4205  -13.2205 H   0  0
  -17.6700    7.5086  -11.5791 H   0  0
  -20.2782    5.5737  -14.3056 H   0  0
  -18.5333    5.5017  -15.9620 H   0  0
  -22.0805    8.1923  -11.0091 H   0  0
  -22.1842    8.9583   -8.6554 H   0  0
  -20.3907    8.3002   -7.0821 H   0  0
  -18.6554    6.7155   -7.7933 H   0  0
  -18.5992    5.8920  -10.1166 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372101282627600

> <LigScore1_Dreiding>
2.15

> <LigScore2_Dreiding>
5.32

> <-PLP1>
96.49

> <-PLP2>
90.04

> <Jain>
4.26

> <-PMF>
114.88

> <-PMF04>
41.17

> <AbsoluteEnergy>
151.199

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
34

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.152

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
64

> <LibDockScore>
91.827

> <HotSpots>
-16.80,8.92,-13.09,P,46,1
-17.20,4.12,-18.29,A,12,13
-19.80,7.72,-8.89,A,70,24

> <-In-Situ Starting Energy>
-2477.059

> <-In-Situ Final Energy>
8.083

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -17.5839   10.1172  -14.8992 N   0  0  0  1  0  0
  -16.2496   10.1008  -15.0456 C   0  0  0  1  0  0
  -15.7379   11.1064  -15.7666 N   0  0  0  1  0  0
  -14.4016   11.2246  -15.8525 C   0  0  0  1  0  0
  -13.5327   10.4072  -15.2613 N   0  0  0  1  0  0
  -14.0600    9.3793  -14.5843 C   0  0  0  1  0  0
  -15.4471    9.1395  -14.5042 C   0  0  0  1  0  0
  -13.4116    8.4130  -13.8281 N   0  0  0  1  0  0
  -11.9684    8.4579  -13.5133 C   0  0  0  1  0  0
  -11.8382    8.3043  -12.0005 C   0  0  0  1  0  0
  -11.5315    6.8172  -11.8022 C   0  0  0  1  0  0
  -10.5417    6.5745  -12.8981 C   0  0  0  1  0  0
  -11.1493    7.3086  -14.1096 C   0  0  0  1  0  0
  -14.3749    7.5415  -13.4580 C   0  0  0  1  0  0
  -15.6458    7.9185  -13.8305 C   0  0  0  1  0  0
  -16.9213    7.2201  -13.5294 C   0  0  0  1  0  0
  -17.3133    7.1066  -12.2278 C   0  0  0  1  0  0
  -18.5262    6.5962  -11.8519 C   0  0  0  1  0  0
  -19.5141    6.5258  -12.8067 C   0  0  0  1  0  0
  -19.0964    6.4149  -14.1304 C   0  0  0  1  0  0
  -17.7669    6.6882  -14.4744 C   0  0  0  1  0  0
  -20.8662    6.5867  -12.4954 O   0  0  0  1  0  0
  -21.3451    6.9943  -11.2470 C   0  0  0  1  0  0
  -20.7175    7.8696  -10.3559 C   0  0  0  1  0  0
  -21.3214    8.2303   -9.1647 C   0  0  0  1  0  0
  -22.5941    7.7848   -8.8964 C   0  0  0  1  0  0
  -23.2344    6.9349   -9.7732 C   0  0  0  1  0  0
  -22.5975    6.5044  -10.9146 C   0  0  0  1  0  0
  -18.0778   10.9134  -15.2403 H   0  0
  -18.1028    9.3688  -14.4802 H   0  0
  -13.9894   12.0248  -16.4466 H   0  0
  -11.5411    9.4120  -13.8302 H   0  0
  -12.7258    8.6653  -11.4894 H   0  0
  -10.9970    8.8997  -11.6421 H   0  0
  -11.1428    6.5513  -10.8239 H   0  0
  -12.3817    6.1770  -12.0095 H   0  0
   -9.6389    7.0538  -12.5474 H   0  0
  -10.3170    5.5206  -13.0426 H   0  0
  -11.7826    6.6680  -14.7151 H   0  0
  -10.4007    7.6865  -14.7973 H   0  0
  -14.2016    6.6328  -12.9061 H   0  0
  -16.7026    7.4297  -11.4337 H   0  0
  -18.7104    6.4385  -10.8015 H   0  0
  -19.8210    6.1792  -14.8949 H   0  0
  -17.4480    6.6077  -15.5039 H   0  0
  -19.7522    8.3013  -10.5528 H   0  0
  -20.8328    8.8822   -8.4578 H   0  0
  -23.1160    8.1473   -8.0348 H   0  0
  -24.2565    6.6555   -9.5982 H   0  0
  -23.1027    5.7956  -11.5479 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372105577594896

> <LigScore1_Dreiding>
1.47

> <LigScore2_Dreiding>
3.18

> <-PLP1>
88.57

> <-PLP2>
84.5

> <Jain>
7.46

> <-PMF>
81.4

> <-PMF04>
16.91

> <AbsoluteEnergy>
149.872

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
27

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.825

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
65

> <LibDockScore>
91.616

> <HotSpots>
-10.60,5.72,-12.49,A,42,12
-18.00,6.32,-14.09,A,30,20
-21.80,7.92,-10.89,A,54,25

> <-In-Situ Starting Energy>
-29473.715

> <-In-Situ Final Energy>
-26.225

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.9356    9.9091  -13.5202 N   0  0  0  1  0  0
  -15.1374    9.5822  -14.5613 C   0  0  0  1  0  0
  -14.1858   10.4873  -14.8289 N   0  0  0  1  0  0
  -13.4343   10.3392  -15.9259 C   0  0  0  1  0  0
  -13.5217    9.3047  -16.7605 N   0  0  0  1  0  0
  -14.4273    8.3590  -16.4613 C   0  0  0  1  0  0
  -15.2697    8.4395  -15.3256 C   0  0  0  1  0  0
  -14.7381    7.1956  -17.1661 N   0  0  0  1  0  0
  -14.1282    6.7704  -18.4434 C   0  0  0  1  0  0
  -14.4224    7.7657  -19.5798 C   0  0  0  1  0  0
  -13.0789    8.3794  -19.9650 C   0  0  0  1  0  0
  -12.0865    7.2606  -19.6780 C   0  0  0  1  0  0
  -12.5984    6.6083  -18.3924 C   0  0  0  1  0  0
  -15.7022    6.5880  -16.4526 C   0  0  0  1  0  0
  -16.0730    7.2671  -15.3086 C   0  0  0  1  0  0
  -17.1150    6.8530  -14.3277 C   0  0  0  1  0  0
  -17.0177    7.1967  -13.0015 C   0  0  0  1  0  0
  -18.0992    7.0770  -12.1446 C   0  0  0  1  0  0
  -19.3194    6.5994  -12.6035 C   0  0  0  1  0  0
  -19.3418    6.0604  -13.8810 C   0  0  0  1  0  0
  -18.2369    6.1497  -14.7213 C   0  0  0  1  0  0
  -20.5327    6.6921  -11.9157 O   0  0  0  1  0  0
  -20.5744    7.1026  -10.5900 C   0  0  0  1  0  0
  -21.5473    8.0296  -10.2468 C   0  0  0  1  0  0
  -21.5908    8.5527   -8.9620 C   0  0  0  1  0  0
  -20.6535    8.1519   -8.0217 C   0  0  0  1  0  0
  -19.7589    7.1369   -8.3231 C   0  0  0  1  0  0
  -19.7422    6.5894   -9.5980 C   0  0  0  1  0  0
  -15.6675   10.6330  -12.8753 H   0  0
  -16.8139    9.4625  -13.3614 H   0  0
  -12.7120   11.1129  -16.1450 H   0  0
  -14.5694    5.8095  -18.7136 H   0  0
  -15.1620    8.5222  -19.3161 H   0  0
  -14.8088    7.2090  -20.4324 H   0  0
  -13.0488    8.7118  -21.0024 H   0  0
  -12.8603    9.2371  -19.3295 H   0  0
  -11.0563    7.6080  -19.5969 H   0  0
  -12.1363    6.5435  -20.4970 H   0  0
  -12.2948    5.5649  -18.3106 H   0  0
  -12.1748    7.1283  -17.5335 H   0  0
  -16.1498    5.6536  -16.7574 H   0  0
  -16.0970    7.5914  -12.6151 H   0  0
  -17.9789    7.4275  -11.1414 H   0  0
  -20.2528    5.6183  -14.2429 H   0  0
  -18.3354    5.7698  -15.7282 H   0  0
  -22.2504    8.3589  -10.9977 H   0  0
  -22.3360    9.2869   -8.6972 H   0  0
  -20.6292    8.6234   -7.0503 H   0  0
  -19.0663    6.7923   -7.5703 H   0  0
  -19.0481    5.7971   -9.8333 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372109872562192

> <LigScore1_Dreiding>
3.57

> <LigScore2_Dreiding>
5.75

> <-PLP1>
87.61

> <-PLP2>
80.11

> <Jain>
3.85

> <-PMF>
113.24

> <-PMF04>
38.69

> <AbsoluteEnergy>
162.605

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
49

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
16.558

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
68

> <LibDockScore>
89.909

> <HotSpots>
-12.60,6.32,-17.69,A,17,13
-19.80,7.72,-8.89,A,70,25
-21.60,6.32,-8.29,A,80,27

> <-In-Situ Starting Energy>
-577.008

> <-In-Situ Final Energy>
8.846

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -19.4108    4.7151  -16.7249 N   0  0  0  1  0  0
  -18.3570    5.0394  -17.5090 C   0  0  0  1  0  0
  -18.4623    4.6935  -18.8061 N   0  0  0  1  0  0
  -17.4901    5.0632  -19.6585 C   0  0  0  1  0  0
  -16.3978    5.7412  -19.3104 N   0  0  0  1  0  0
  -16.2792    6.0624  -18.0127 C   0  0  0  1  0  0
  -17.2439    5.6970  -17.0455 C   0  0  0  1  0  0
  -15.2656    6.7844  -17.3797 N   0  0  0  1  0  0
  -14.0812    7.3741  -18.0330 C   0  0  0  1  0  0
  -13.1971    6.3329  -18.7353 C   0  0  0  1  0  0
  -13.1624    6.7457  -20.2092 C   0  0  0  1  0  0
  -13.4025    8.2511  -20.1902 C   0  0  0  1  0  0
  -14.4432    8.4278  -19.0881 C   0  0  0  1  0  0
  -15.6018    6.8142  -16.0810 C   0  0  0  1  0  0
  -16.7743    6.1466  -15.7917 C   0  0  0  1  0  0
  -17.3589    5.9772  -14.4400 C   0  0  0  1  0  0
  -17.5250    7.0792  -13.6280 C   0  0  0  1  0  0
  -18.0439    6.9453  -12.3487 C   0  0  0  1  0  0
  -18.4136    5.7023  -11.8554 C   0  0  0  1  0  0
  -18.2263    4.5924  -12.6676 C   0  0  0  1  0  0
  -17.7210    4.7349  -13.9561 C   0  0  0  1  0  0
  -18.8892    5.5389  -10.5598 O   0  0  0  1  0  0
  -19.7616    6.5143  -10.0800 C   0  0  0  1  0  0
  -19.5886    6.9544   -8.7754 C   0  0  0  1  0  0
  -20.4616    7.8818   -8.2231 C   0  0  0  1  0  0
  -21.5354    8.3546   -8.9658 C   0  0  0  1  0  0
  -21.7115    7.9255  -10.2745 C   0  0  0  1  0  0
  -20.8217    7.0191  -10.8345 C   0  0  0  1  0  0
  -20.2228    4.2819  -17.1243 H   0  0
  -19.4202    4.8888  -15.7388 H   0  0
  -17.5959    4.7876  -20.6979 H   0  0
  -13.4798    7.8564  -17.2608 H   0  0
  -13.5713    5.3201  -18.5957 H   0  0
  -12.1884    6.3597  -18.3208 H   0  0
  -12.2310    6.4791  -20.7060 H   0  0
  -13.9756    6.2535  -20.7442 H   0  0
  -13.7274    8.6290  -21.1574 H   0  0
  -12.4813    8.7673  -19.9179 H   0  0
  -14.4632    9.4289  -18.6651 H   0  0
  -15.4309    8.2373  -19.5037 H   0  0
  -14.9992    7.3114  -15.3345 H   0  0
  -17.2568    8.0676  -13.9760 H   0  0
  -18.1567    7.8127  -11.7284 H   0  0
  -18.4778    3.6100  -12.2984 H   0  0
  -17.6005    3.8481  -14.5619 H   0  0
  -18.7623    6.5762   -8.1948 H   0  0
  -20.3020    8.2358   -7.2153 H   0  0
  -22.2313    9.0551   -8.5259 H   0  0
  -22.5443    8.2862  -10.8601 H   0  0
  -20.9771    6.7005  -11.8550 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372114167529488

> <LigScore1_Dreiding>
4.73

> <LigScore2_Dreiding>
6.83

> <-PLP1>
121.71

> <-PLP2>
118.01

> <Jain>
9.15

> <-PMF>
111.23

> <-PMF04>
39.5

> <AbsoluteEnergy>
157.761

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
48

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
11.714

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
69

> <LibDockScore>
89.897

> <HotSpots>
-16.80,5.32,-18.29,A,13,4
-12.60,6.32,-17.69,A,17,11
-20.60,5.92,-7.09,A,88,27

> <-In-Situ Starting Energy>
-306153.469

> <-In-Situ Final Energy>
41.657

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -11.4920    8.4386  -15.6215 N   0  0  0  1  0  0
  -12.7311    7.9248  -15.7973 C   0  0  0  1  0  0
  -12.9118    7.2394  -16.9367 N   0  0  0  1  0  0
  -14.1233    6.7276  -17.1946 C   0  0  0  1  0  0
  -15.1816    6.8530  -16.3939 N   0  0  0  1  0  0
  -15.0121    7.5251  -15.2439 C   0  0  0  1  0  0
  -13.7588    8.0863  -14.8970 C   0  0  0  1  0  0
  -15.9256    7.8056  -14.2120 N   0  0  0  1  0  0
  -17.3373    7.3473  -14.0795 C   0  0  0  1  0  0
  -17.7801    6.1337  -14.9242 C   0  0  0  1  0  0
  -17.4713    4.9279  -14.0470 C   0  0  0  1  0  0
  -17.9705    5.3962  -12.6854 C   0  0  0  1  0  0
  -17.6882    6.9037  -12.6406 C   0  0  0  1  0  0
  -15.2519    8.6190  -13.3744 C   0  0  0  1  0  0
  -13.8986    8.6965  -13.6343 C   0  0  0  1  0  0
  -12.8336    9.2603  -12.7648 C   0  0  0  1  0  0
  -11.7143    8.4946  -12.5088 C   0  0  0  1  0  0
  -10.6913    8.9671  -11.7040 C   0  0  0  1  0  0
  -10.7593   10.2253  -11.1249 C   0  0  0  1  0  0
  -11.8888   11.0050  -11.3843 C   0  0  0  1  0  0
  -12.9213   10.5125  -12.1858 C   0  0  0  1  0  0
   -9.6492   10.6233  -10.3812 O   0  0  0  1  0  0
   -9.7878   11.5319   -9.3345 C   0  0  0  1  0  0
  -10.8808   11.5589   -8.4675 C   0  0  0  1  0  0
  -10.9034   12.4467   -7.3983 C   0  0  0  1  0  0
   -9.8259   13.2932   -7.1732 C   0  0  0  1  0  0
   -8.7228   13.2495   -8.0144 C   0  0  0  1  0  0
   -8.7068   12.3694   -9.0886 C   0  0  0  1  0  0
  -10.7731    8.2227  -16.2799 H   0  0
  -11.2614    9.0360  -14.8534 H   0  0
  -14.2486    6.1749  -18.1149 H   0  0
  -17.9321    8.2266  -14.2967 H   0  0
  -17.3696    6.0625  -15.9259 H   0  0
  -18.8626    6.1757  -15.0579 H   0  0
  -17.9724    4.0199  -14.3851 H   0  0
  -16.3967    4.7429  -14.0251 H   0  0
  -17.5572    4.8483  -11.8433 H   0  0
  -19.0477    5.2425  -12.6549 H   0  0
  -18.5883    7.4044  -12.2879 H   0  0
  -16.9168    7.1580  -11.9225 H   0  0
  -15.7407    9.1343  -12.5599 H   0  0
  -11.6088    7.5046  -12.9327 H   0  0
   -9.8362    8.3354  -11.5296 H   0  0
  -11.9765   12.0042  -10.9833 H   0  0
  -13.7874   11.1399  -12.3593 H   0  0
  -11.7139   10.8856   -8.6008 H   0  0
  -11.7559   12.4749   -6.7345 H   0  0
   -9.8412   13.9818   -6.3402 H   0  0
   -7.8770   13.8978   -7.8301 H   0  0
   -7.8477   12.3350   -9.7405 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372118462496784

> <LigScore1_Dreiding>
2.29

> <LigScore2_Dreiding>
5.01

> <-PLP1>
82.78

> <-PLP2>
76.2

> <Jain>
2.26

> <-PMF>
136.64

> <-PMF04>
58.89

> <AbsoluteEnergy>
154.674

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
44

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
8.627

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
74

> <LibDockScore>
87.768

> <HotSpots>
-16.60,5.52,-13.89,A,33,11
-11.00,8.32,-11.89,A,47,17
-10.40,11.52,-8.49,A,77,24

> <-In-Situ Starting Energy>
-160.618

> <-In-Situ Final Energy>
12.244

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.1583   12.2033  -13.7305 N   0  0  0  1  0  0
  -15.0005   11.1776  -13.9681 C   0  0  0  1  0  0
  -16.1625   11.4903  -14.5583 N   0  0  0  1  0  0
  -17.0516   10.5308  -14.7929 C   0  0  0  1  0  0
  -16.8649    9.2482  -14.5256 N   0  0  0  1  0  0
  -15.6946    8.9228  -13.9698 C   0  0  0  1  0  0
  -14.7116    9.8787  -13.6528 C   0  0  0  1  0  0
  -15.2268    7.6622  -13.6107 N   0  0  0  1  0  0
  -16.0220    6.4215  -13.7814 C   0  0  0  1  0  0
  -16.3603    6.1316  -15.2436 C   0  0  0  1  0  0
  -17.4170    5.0275  -15.1671 C   0  0  0  1  0  0
  -18.1856    5.2867  -13.8631 C   0  0  0  1  0  0
  -17.4141    6.3887  -13.1213 C   0  0  0  1  0  0
  -13.9697    7.8678  -13.1411 C   0  0  0  1  0  0
  -13.6268    9.2114  -13.0611 C   0  0  0  1  0  0
  -12.4181    9.8555  -12.4842 C   0  0  0  1  0  0
  -11.1649    9.6714  -13.0245 C   0  0  0  1  0  0
  -10.0637   10.3342  -12.4903 C   0  0  0  1  0  0
  -10.1719   11.1392  -11.3594 C   0  0  0  1  0  0
  -11.4507   11.3643  -10.8567 C   0  0  0  1  0  0
  -12.5453   10.7075  -11.4027 C   0  0  0  1  0  0
   -8.9959   11.7086  -10.8604 O   0  0  0  1  0  0
   -8.9185   12.2525   -9.5730 C   0  0  0  1  0  0
   -9.5942   11.7623   -8.4532 C   0  0  0  1  0  0
   -9.4158   12.3428   -7.2032 C   0  0  0  1  0  0
   -8.5425   13.4094   -7.0516 C   0  0  0  1  0  0
   -7.8456   13.8870   -8.1517 C   0  0  0  1  0  0
   -8.0281   13.3052   -9.4008 C   0  0  0  1  0  0
  -14.4470   13.1169  -14.0262 H   0  0
  -13.2791   12.0901  -13.2734 H   0  0
  -17.9814   10.8298  -15.2317 H   0  0
  -15.4450    5.5822  -13.3955 H   0  0
  -15.4861    5.8868  -15.8389 H   0  0
  -16.8099    7.0025  -15.7165 H   0  0
  -18.0713    5.0192  -16.0394 H   0  0
  -16.9335    4.0533  -15.1089 H   0  0
  -18.2389    4.3735  -13.2686 H   0  0
  -19.2127    5.5981  -14.0601 H   0  0
  -17.9370    7.3304  -13.2808 H   0  0
  -17.4079    6.2252  -12.0468 H   0  0
  -13.3059    7.0691  -12.8404 H   0  0
  -11.0175    9.0250  -13.8796 H   0  0
   -9.1112   10.2305  -12.9852 H   0  0
  -11.6312   12.0595  -10.0507 H   0  0
  -13.5121   10.9212  -10.9755 H   0  0
  -10.2820   10.9393   -8.5312 H   0  0
   -9.9595   11.9688   -6.3469 H   0  0
   -8.4031   13.8655   -6.0804 H   0  0
   -7.1489   14.7039   -8.0299 H   0  0
   -7.4763   13.6756  -10.2510 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372122757464080

> <LigScore1_Dreiding>
3.12

> <LigScore2_Dreiding>
4.98

> <-PLP1>
85.06

> <-PLP2>
81.27

> <Jain>
3.15

> <-PMF>
119.95

> <-PMF04>
47.84

> <AbsoluteEnergy>
146.57

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
11

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.523

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
76

> <LibDockScore>
86.946

> <HotSpots>
-16.20,11.72,-14.69,P,28,3
-18.00,6.32,-14.09,A,30,12
-9.00,11.12,-7.09,A,92,25

> <-In-Situ Starting Energy>
-842.635

> <-In-Situ Final Energy>
14.231

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.3949   11.3977  -12.7322 N   0  0  0  1  0  0
   -8.9055   11.6821  -11.5123 C   0  0  0  1  0  0
   -7.9993   11.7923  -10.5188 N   0  0  0  1  0  0
   -8.4168   12.2382   -9.3191 C   0  0  0  1  0  0
   -9.6874   12.4735   -9.0040 N   0  0  0  1  0  0
  -10.5961   12.2965   -9.9750 C   0  0  0  1  0  0
  -10.2487   11.8644  -11.2760 C   0  0  0  1  0  0
  -11.9720   12.4994   -9.9256 N   0  0  0  1  0  0
  -12.7086   13.0094   -8.7507 C   0  0  0  1  0  0
  -13.5284   14.2660   -9.1021 C   0  0  0  1  0  0
  -14.9821   13.9464   -8.7479 C   0  0  0  1  0  0
  -14.8966   12.8218   -7.7247 C   0  0  0  1  0  0
  -13.7086   11.9877   -8.1926 C   0  0  0  1  0  0
  -12.4354   12.1516  -11.1415 C   0  0  0  1  0  0
  -11.4480   11.7444  -12.0213 C   0  0  0  1  0  0
  -11.6529   11.2960  -13.4259 C   0  0  0  1  0  0
  -12.4957   12.0051  -14.2627 C   0  0  0  1  0  0
  -12.6867   11.6160  -15.5847 C   0  0  0  1  0  0
  -12.0566   10.4876  -16.0857 C   0  0  0  1  0  0
  -11.2153    9.7660  -15.2462 C   0  0  0  1  0  0
  -11.0246   10.1692  -13.9276 C   0  0  0  1  0  0
  -12.2596   10.1258  -17.4088 O   0  0  0  1  0  0
  -12.7255    8.8327  -17.6116 C   0  0  0  1  0  0
  -13.6745    8.2355  -16.7821 C   0  0  0  1  0  0
  -14.1263    6.9495  -17.0506 C   0  0  0  1  0  0
  -13.6399    6.2564  -18.1508 C   0  0  0  1  0  0
  -12.7090    6.8553  -18.9892 C   0  0  0  1  0  0
  -12.2587    8.1412  -18.7208 C   0  0  0  1  0  0
   -7.4070   11.3102  -12.8491 H   0  0
   -8.9775   11.2720  -13.5356 H   0  0
   -7.6722   12.4161   -8.5545 H   0  0
  -12.0105   13.2692   -7.9521 H   0  0
  -13.4420   14.5597  -10.1483 H   0  0
  -13.1723   15.1059   -8.5065 H   0  0
  -15.5259   14.8137   -8.3728 H   0  0
  -15.4998   13.5774   -9.6348 H   0  0
  -15.8136   12.2407   -7.6856 H   0  0
  -14.7019   13.2358   -6.7343 H   0  0
  -13.2843   11.3792   -7.3938 H   0  0
  -14.0413   11.3087   -8.9776 H   0  0
  -13.4880   12.1946  -11.3946 H   0  0
  -13.0247   12.8813  -13.9093 H   0  0
  -13.3396   12.1871  -16.2276 H   0  0
  -10.6962    8.8937  -15.6164 H   0  0
  -10.3683    9.5742  -13.3074 H   0  0
  -14.0775    8.7656  -15.9317 H   0  0
  -14.8592    6.4899  -16.4042 H   0  0
  -13.9898    5.2551  -18.3552 H   0  0
  -12.3306    6.3268  -19.8532 H   0  0
  -11.5332    8.6061  -19.3715 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372127052431376

> <LigScore1_Dreiding>
2.58

> <LigScore2_Dreiding>
4.73

> <-PLP1>
60.35

> <-PLP2>
53.15

> <Jain>
1.82

> <-PMF>
74.59

> <-PMF04>
23.32

> <AbsoluteEnergy>
152.006

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
37

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
5.959

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
77

> <LibDockScore>
86.371

> <HotSpots>
-9.00,11.32,-8.89,A,71,4
-13.00,12.72,-7.09,A,96,10
-16.00,6.12,-17.09,A,18,26

> <-In-Situ Starting Energy>
-251.125

> <-In-Situ Final Energy>
22.018

> <In-Situ Gradient>
0.131

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -8.4038   11.3910  -12.8136 N   0  0  0  1  0  0
   -8.8912   11.6868  -11.5868 C   0  0  0  1  0  0
   -7.9661   11.8069  -10.6117 N   0  0  0  1  0  0
   -8.3606   12.2608   -9.4076 C   0  0  0  1  0  0
   -9.6259   12.4912   -9.0680 N   0  0  0  1  0  0
  -10.5533   12.3063  -10.0198 C   0  0  0  1  0  0
  -10.2301   11.8694  -11.3258 C   0  0  0  1  0  0
  -11.9289   12.5023   -9.9429 N   0  0  0  1  0  0
  -12.6455   13.0037   -8.7515 C   0  0  0  1  0  0
  -13.6487   11.9823   -8.1975 C   0  0  0  1  0  0
  -14.8194   12.8186   -7.6906 C   0  0  0  1  0  0
  -14.9074   13.9710   -8.6835 C   0  0  0  1  0  0
  -13.4575   14.2738   -9.0698 C   0  0  0  1  0  0
  -12.4140   12.1554  -11.1509 C   0  0  0  1  0  0
  -11.4436   11.7442  -12.0477 C   0  0  0  1  0  0
  -11.6765   11.2855  -13.4452 C   0  0  0  1  0  0
  -12.5401   11.9837  -14.2701 C   0  0  0  1  0  0
  -12.7571   11.5827  -15.5849 C   0  0  0  1  0  0
  -12.1318   10.4543  -16.0909 C   0  0  0  1  0  0
  -11.2716    9.7416  -15.2625 C   0  0  0  1  0  0
  -11.0547   10.1571  -13.9516 C   0  0  0  1  0  0
  -12.3525   10.0920  -17.4111 O   0  0  0  1  0  0
  -12.8022    8.7931  -17.6100 C   0  0  0  1  0  0
  -13.7596    8.1965  -16.7902 C   0  0  0  1  0  0
  -14.1975    6.9048  -17.0544 C   0  0  0  1  0  0
  -13.6886    6.2062  -18.1411 C   0  0  0  1  0  0
  -12.7483    6.8047  -18.9694 C   0  0  0  1  0  0
  -12.3115    8.0958  -18.7051 C   0  0  0  1  0  0
   -7.4219   11.2636  -12.9423 H   0  0
   -8.9995   11.2954  -13.6116 H   0  0
   -7.6006   12.4496   -8.6610 H   0  0
  -11.9344   13.2436   -7.9580 H   0  0
  -13.2176   11.3522   -7.4190 H   0  0
  -14.0038   11.3242   -8.9902 H   0  0
  -15.7436   12.2478   -7.6494 H   0  0
  -14.6039   13.2038   -6.6928 H   0  0
  -15.4568   13.6372   -9.5654 H   0  0
  -15.4227   14.8391   -8.2716 H   0  0
  -13.0760   15.1039   -8.4761 H   0  0
  -13.3906   14.5760  -10.1150 H   0  0
  -13.4709   12.1990  -11.3846 H   0  0
  -13.0662   12.8605  -13.9136 H   0  0
  -13.4247   12.1453  -16.2197 H   0  0
  -10.7545    8.8695  -15.6368 H   0  0
  -10.3841    9.5696  -13.3402 H   0  0
  -14.1788    8.7326  -15.9519 H   0  0
  -14.9366    6.4446  -16.4152 H   0  0
  -14.0276    5.2005  -18.3430 H   0  0
  -12.3523    6.2723  -19.8223 H   0  0
  -11.5790    8.5604  -19.3479 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372131347398672

> <LigScore1_Dreiding>
2.55

> <LigScore2_Dreiding>
4.75

> <-PLP1>
60.56

> <-PLP2>
53.32

> <Jain>
1.8

> <-PMF>
74.44

> <-PMF04>
23.58

> <AbsoluteEnergy>
146.3

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
4

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.253

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
79

> <LibDockScore>
85.273

> <HotSpots>
-10.20,11.32,-7.09,A,93,4
-15.40,12.12,-7.69,A,86,10
-12.60,6.32,-17.69,A,17,27

> <-In-Situ Starting Energy>
-1422.036

> <-In-Situ Final Energy>
22.151

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -14.9512    9.3335  -12.8978 N   0  0  0  1  0  0
  -14.3435    9.0375  -14.0705 C   0  0  0  1  0  0
  -13.2362    9.7631  -14.2849 N   0  0  0  1  0  0
  -12.6321    9.6943  -15.4768 C   0  0  0  1  0  0
  -13.0350    8.9139  -16.4745 N   0  0  0  1  0  0
  -14.0892    8.1173  -16.2347 C   0  0  0  1  0  0
  -14.7894    8.1178  -15.0035 C   0  0  0  1  0  0
  -14.6881    7.1983  -17.0937 N   0  0  0  1  0  0
  -14.2916    6.9573  -18.4954 C   0  0  0  1  0  0
  -14.4545    8.1880  -19.3848 C   0  0  0  1  0  0
  -13.6419    7.8539  -20.6334 C   0  0  0  1  0  0
  -12.5133    6.9319  -20.1597 C   0  0  0  1  0  0
  -12.8353    6.5354  -18.7104 C   0  0  0  1  0  0
  -15.6713    6.6217  -16.3795 C   0  0  0  1  0  0
  -15.7982    7.1169  -15.0957 C   0  0  0  1  0  0
  -16.7787    6.6635  -14.0698 C   0  0  0  1  0  0
  -17.0749    5.3268  -13.8606 C   0  0  0  1  0  0
  -17.9097    4.9306  -12.8101 C   0  0  0  1  0  0
  -18.4211    5.8683  -11.9210 C   0  0  0  1  0  0
  -18.1816    7.2045  -12.1948 C   0  0  0  1  0  0
  -17.4178    7.5885  -13.2854 C   0  0  0  1  0  0
  -19.0724    5.4562  -10.7577 O   0  0  0  1  0  0
  -19.8894    6.3944  -10.1284 C   0  0  0  1  0  0
  -21.0129    6.9250  -10.7600 C   0  0  0  1  0  0
  -21.8155    7.8465  -10.1042 C   0  0  0  1  0  0
  -21.4908    8.2622   -8.8203 C   0  0  0  1  0  0
  -20.3573    7.7562   -8.1967 C   0  0  0  1  0  0
  -19.5640    6.8205   -8.8479 C   0  0  0  1  0  0
  -14.5767   10.0615  -12.3147 H   0  0
  -15.8128    8.9454  -12.5859 H   0  0
  -11.7599   10.3124  -15.6371 H   0  0
  -14.9315    6.1694  -18.8962 H   0  0
  -14.0264    9.0675  -18.9058 H   0  0
  -15.4984    8.4067  -19.5954 H   0  0
  -14.2648    7.3067  -21.3406 H   0  0
  -13.2673    8.7441  -21.1382 H   0  0
  -11.5426    7.4262  -20.2143 H   0  0
  -12.4651    6.0602  -20.8105 H   0  0
  -12.6774    5.4776  -18.5089 H   0  0
  -12.1679    7.0803  -18.0443 H   0  0
  -16.3068    5.8436  -16.7785 H   0  0
  -16.6559    4.5638  -14.5009 H   0  0
  -18.1289    3.8843  -12.6508 H   0  0
  -18.5671    7.9490  -11.5279 H   0  0
  -17.2899    8.6328  -13.5151 H   0  0
  -21.2674    6.6274  -11.7666 H   0  0
  -22.6935    8.2309  -10.5996 H   0  0
  -22.1192    8.9784   -8.3095 H   0  0
  -20.0885    8.0930   -7.2062 H   0  0
  -18.6800    6.4307   -8.3693 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372135642365968

> <LigScore1_Dreiding>
3.81

> <LigScore2_Dreiding>
6.03

> <-PLP1>
86.01

> <-PLP2>
80.98

> <Jain>
5.2

> <-PMF>
112.47

> <-PMF04>
40.29

> <AbsoluteEnergy>
164.245

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
52

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
18.198

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
80

> <LibDockScore>
85.13

> <HotSpots>
-15.60,6.12,-19.69,A,6,13
-17.20,7.52,-13.09,A,39,21
-21.80,7.92,-10.89,A,54,25

> <-In-Situ Starting Energy>
-6890.141

> <-In-Situ Final Energy>
15.795

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.4290   10.3082  -13.7167 N   0  0  0  1  0  0
  -15.5319    9.9621  -14.6631 C   0  0  0  1  0  0
  -14.6806   10.9382  -14.9945 N   0  0  0  1  0  0
  -13.8712   10.7763  -16.0463 C   0  0  0  1  0  0
  -13.8163    9.6656  -16.7832 N   0  0  0  1  0  0
  -14.6222    8.6564  -16.4113 C   0  0  0  1  0  0
  -15.4852    8.7337  -15.2877 C   0  0  0  1  0  0
  -14.8144    7.4240  -17.0341 N   0  0  0  1  0  0
  -14.1480    6.9826  -18.2792 C   0  0  0  1  0  0
  -14.7874    5.7334  -18.9240 C   0  0  0  1  0  0
  -14.7406    5.9544  -20.4449 C   0  0  0  1  0  0
  -13.8341    7.1649  -20.6425 C   0  0  0  1  0  0
  -14.1122    8.0164  -19.4088 C   0  0  0  1  0  0
  -15.6951    6.7686  -16.2565 C   0  0  0  1  0  0
  -16.0938    7.4578  -15.1289 C   0  0  0  1  0  0
  -16.9454    6.9051  -14.0325 C   0  0  0  1  0  0
  -16.9222    7.4617  -12.7741 C   0  0  0  1  0  0
  -17.6921    6.9491  -11.7483 C   0  0  0  1  0  0
  -18.4832    5.8472  -11.9166 C   0  0  0  1  0  0
  -18.4788    5.2341  -13.1601 C   0  0  0  1  0  0
  -17.7462    5.7846  -14.2156 C   0  0  0  1  0  0
  -19.1699    5.3933  -10.8002 O   0  0  0  1  0  0
  -19.9679    6.3798  -10.2184 C   0  0  0  1  0  0
  -19.7269    6.7687   -8.9071 C   0  0  0  1  0  0
  -20.5078    7.7494   -8.3108 C   0  0  0  1  0  0
  -21.5549    8.3284   -9.0160 C   0  0  0  1  0  0
  -21.7894    7.9557  -10.3330 C   0  0  0  1  0  0
  -20.9879    6.9987  -10.9375 C   0  0  0  1  0  0
  -16.2142   11.0498  -13.0734 H   0  0
  -17.3011    9.8296  -13.6420 H   0  0
  -13.2283   11.6046  -16.3098 H   0  0
  -13.1107    6.7530  -18.0280 H   0  0
  -15.8305    5.5981  -18.6409 H   0  0
  -14.2537    4.8382  -18.6105 H   0  0
  -14.4120    5.0928  -21.0204 H   0  0
  -15.7467    6.1761  -20.7962 H   0  0
  -14.0033    7.6850  -21.5809 H   0  0
  -12.7909    6.8429  -20.6357 H   0  0
  -13.3499    8.7808  -19.2577 H   0  0
  -15.0789    8.5130  -19.4978 H   0  0
  -16.0489    5.7762  -16.4856 H   0  0
  -16.2981    8.2983  -12.5291 H   0  0
  -17.6365    7.3158  -10.7462 H   0  0
  -19.0443    4.3305  -13.3058 H   0  0
  -17.8114    5.2900  -15.1738 H   0  0
  -18.9142    6.3177   -8.3615 H   0  0
  -20.2965    8.0628   -7.2993 H   0  0
  -22.1827    9.0698   -8.5420 H   0  0
  -22.5954    8.4012  -10.8953 H   0  0
  -21.1725    6.7267  -11.9669 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372139937333264

> <LigScore1_Dreiding>
3.05

> <LigScore2_Dreiding>
5.52

> <-PLP1>
93.11

> <-PLP2>
84.23

> <Jain>
5.04

> <-PMF>
111.77

> <-PMF04>
40.17

> <AbsoluteEnergy>
155.445

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
46

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
9.398

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
85

> <LibDockScore>
83.536

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-19.80,6.72,-7.69,A,85,25
-20.40,7.32,-10.49,A,60,28

> <-In-Situ Starting Energy>
-417.618

> <-In-Situ Final Energy>
8.728

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.6541    5.8274  -20.0260 N   0  0  0  1  0  0
  -17.2198    5.6061  -18.8190 C   0  0  0  1  0  0
  -18.3700    4.9087  -18.8638 N   0  0  0  1  0  0
  -19.0655    4.7440  -17.7292 C   0  0  0  1  0  0
  -18.6822    5.1700  -16.5391 N   0  0  0  1  0  0
  -17.5286    5.8381  -16.4903 C   0  0  0  1  0  0
  -16.7175    6.0742  -17.6220 C   0  0  0  1  0  0
  -16.9686    6.4588  -15.3861 N   0  0  0  1  0  0
  -17.6520    6.5140  -14.0803 C   0  0  0  1  0  0
  -16.9606    7.3278  -12.9935 C   0  0  0  1  0  0
  -17.7611    6.9320  -11.7511 C   0  0  0  1  0  0
  -18.1574    5.4715  -11.9579 C   0  0  0  1  0  0
  -17.8817    5.1513  -13.4295 C   0  0  0  1  0  0
  -15.8009    6.9718  -15.8144 C   0  0  0  1  0  0
  -15.5780    6.7904  -17.1711 C   0  0  0  1  0  0
  -14.4000    7.2860  -17.9345 C   0  0  0  1  0  0
  -13.7860    6.5169  -18.9037 C   0  0  0  1  0  0
  -12.7252    7.0186  -19.6524 C   0  0  0  1  0  0
  -12.2301    8.2911  -19.4086 C   0  0  0  1  0  0
  -12.8186    9.0527  -18.4071 C   0  0  0  1  0  0
  -13.8921    8.5479  -17.6791 C   0  0  0  1  0  0
  -11.2433    8.8047  -20.2354 O   0  0  0  1  0  0
   -9.9615    8.9984  -19.7219 C   0  0  0  1  0  0
   -9.5993    8.9029  -18.3750 C   0  0  0  1  0  0
   -8.2877    9.1507  -17.9845 C   0  0  0  1  0  0
   -7.3217    9.4611  -18.9307 C   0  0  0  1  0  0
   -7.6712    9.5407  -20.2708 C   0  0  0  1  0  0
   -8.9855    9.3154  -20.6582 C   0  0  0  1  0  0
  -17.1643    5.5535  -20.8461 H   0  0
  -15.7655    6.2688  -20.1309 H   0  0
  -20.0065    4.2304  -17.7837 H   0  0
  -18.6318    6.9694  -14.2424 H   0  0
  -16.9824    8.4003  -13.1877 H   0  0
  -15.9194    7.0223  -12.9045 H   0  0
  -17.2487    7.0858  -10.8096 H   0  0
  -18.6684    7.5337  -11.7020 H   0  0
  -17.6485    4.7772  -11.2955 H   0  0
  -19.2057    5.3968  -11.7222 H   0  0
  -18.7025    4.6010  -13.8889 H   0  0
  -16.9837    4.5430  -13.5297 H   0  0
  -15.1096    7.4862  -15.1630 H   0  0
  -14.1260    5.5098  -19.0933 H   0  0
  -12.2779    6.4246  -20.4359 H   0  0
  -12.4480   10.0467  -18.2059 H   0  0
  -14.3354    9.1790  -16.9210 H   0  0
  -10.3124    8.6512  -17.6062 H   0  0
   -8.0160    9.1105  -16.9402 H   0  0
   -6.3000    9.6402  -18.6264 H   0  0
   -6.9224    9.7771  -21.0132 H   0  0
   -9.2575    9.3723  -21.7015 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372144232300560

> <LigScore1_Dreiding>
3.12

> <LigScore2_Dreiding>
4.9

> <-PLP1>
82.86

> <-PLP2>
78.13

> <Jain>
4.61

> <-PMF>
79.23

> <-PMF04>
19.6

> <AbsoluteEnergy>
146.3

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
4

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
0.253

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
91

> <LibDockScore>
81.76

> <HotSpots>
-19.40,4.52,-16.69,P,20,5
-18.40,4.72,-11.29,A,50,12
-12.60,6.32,-17.69,A,17,18

> <-In-Situ Starting Energy>
-206.126

> <-In-Situ Final Energy>
14.897

> <In-Situ Gradient>
0.062

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.4232   10.3086  -13.7170 N   0  0  0  1  0  0
  -15.5271    9.9613  -14.6641 C   0  0  0  1  0  0
  -14.6746   10.9363  -14.9956 N   0  0  0  1  0  0
  -13.8660   10.7736  -16.0479 C   0  0  0  1  0  0
  -13.8131    9.6631  -16.7851 N   0  0  0  1  0  0
  -14.6202    8.6549  -16.4131 C   0  0  0  1  0  0
  -15.4825    8.7331  -15.2890 C   0  0  0  1  0  0
  -14.8141    7.4230  -17.0360 N   0  0  0  1  0  0
  -14.1485    6.9810  -18.2814 C   0  0  0  1  0  0
  -14.1122    8.0147  -19.4111 C   0  0  0  1  0  0
  -13.8346    7.1628  -20.6447 C   0  0  0  1  0  0
  -14.7416    5.9527  -20.4469 C   0  0  0  1  0  0
  -14.7891    5.7323  -18.9259 C   0  0  0  1  0  0
  -15.6953    6.7685  -16.2584 C   0  0  0  1  0  0
  -16.0928    7.4578  -15.1304 C   0  0  0  1  0  0
  -16.9447    6.9058  -14.0340 C   0  0  0  1  0  0
  -16.9211    7.4620  -12.7754 C   0  0  0  1  0  0
  -17.6912    6.9495  -11.7496 C   0  0  0  1  0  0
  -18.4828    5.8481  -11.9181 C   0  0  0  1  0  0
  -18.4791    5.2354  -13.1618 C   0  0  0  1  0  0
  -17.7463    5.7859  -14.2173 C   0  0  0  1  0  0
  -19.1693    5.3941  -10.8016 O   0  0  0  1  0  0
  -19.9675    6.3806  -10.2199 C   0  0  0  1  0  0
  -19.7274    6.7689   -8.9084 C   0  0  0  1  0  0
  -20.5087    7.7494   -8.3122 C   0  0  0  1  0  0
  -21.5553    8.3286   -9.0179 C   0  0  0  1  0  0
  -21.7889    7.9566  -10.3352 C   0  0  0  1  0  0
  -20.9870    6.9997  -10.9396 C   0  0  0  1  0  0
  -16.2074   11.0503  -13.0742 H   0  0
  -17.2956    9.8307  -13.6409 H   0  0
  -13.2220   11.6010  -16.3114 H   0  0
  -13.1113    6.7505  -18.0305 H   0  0
  -13.3496    8.7786  -19.2600 H   0  0
  -15.0787    8.5117  -19.5001 H   0  0
  -14.0036    7.6827  -21.5832 H   0  0
  -12.7915    6.8404  -20.6378 H   0  0
  -15.7475    6.1744  -20.7988 H   0  0
  -14.4129    5.0907  -21.0218 H   0  0
  -14.2564    4.8367  -18.6118 H   0  0
  -15.8324    5.5983  -18.6431 H   0  0
  -16.0503    5.7765  -16.4876 H   0  0
  -16.2965    8.2982  -12.5301 H   0  0
  -17.6351    7.3158  -10.7474 H   0  0
  -19.0450    4.3322  -13.3075 H   0  0
  -17.8121    5.2915  -15.1755 H   0  0
  -18.9152    6.3176   -8.3624 H   0  0
  -20.2981    8.0624   -7.3004 H   0  0
  -22.1834    9.0698   -8.5440 H   0  0
  -22.5945    8.4024  -10.8979 H   0  0
  -21.1710    6.7280  -11.9691 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372148527267856

> <LigScore1_Dreiding>
3.05

> <LigScore2_Dreiding>
5.52

> <-PLP1>
93.1

> <-PLP2>
84.23

> <Jain>
5.04

> <-PMF>
111.82

> <-PMF04>
40.15

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
93

> <LibDockScore>
81.685

> <HotSpots>
-15.00,10.92,-16.29,A,23,4
-16.20,6.52,-15.49,A,24,14
-21.80,7.92,-10.89,A,54,28

> <-In-Situ Starting Energy>
-701.448

> <-In-Situ Final Energy>
8.728

> <In-Situ Gradient>
0.009

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
   -9.2279   11.1382  -12.4791 N   0  0  0  1  0  0
   -9.6093   11.6388  -11.2819 C   0  0  0  1  0  0
   -8.6436   11.7020  -10.3422 N   0  0  0  1  0  0
   -8.9531   12.2195   -9.1379 C   0  0  0  1  0  0
  -10.1741   12.6001   -8.7699 N   0  0  0  1  0  0
  -11.1398   12.5156   -9.6982 C   0  0  0  1  0  0
  -10.8945   12.0479  -11.0117 C   0  0  0  1  0  0
  -12.4915   12.8295   -9.5767 N   0  0  0  1  0  0
  -13.1290   13.3049   -8.3272 C   0  0  0  1  0  0
  -13.0165   12.2796   -7.1812 C   0  0  0  1  0  0
  -14.4227   12.1072   -6.5978 C   0  0  0  1  0  0
  -15.2047   13.3289   -7.0691 C   0  0  0  1  0  0
  -14.6299   13.6203   -8.4500 C   0  0  0  1  0  0
  -13.0174   12.5987  -10.7956 C   0  0  0  1  0  0
  -12.1144   12.1215  -11.7260 C   0  0  0  1  0  0
  -12.4174   11.7634  -13.1396 C   0  0  0  1  0  0
  -11.6227   12.1850  -14.1909 C   0  0  0  1  0  0
  -11.8964   11.7930  -15.4993 C   0  0  0  1  0  0
  -12.9725   10.9601  -15.7723 C   0  0  0  1  0  0
  -13.8068   10.5838  -14.7270 C   0  0  0  1  0  0
  -13.5289   10.9928  -13.4269 C   0  0  0  1  0  0
  -13.2052   10.5351  -17.0716 O   0  0  0  1  0  0
  -13.2104    9.1564  -17.2605 C   0  0  0  1  0  0
  -14.1022    8.6304  -18.1873 C   0  0  0  1  0  0
  -14.1311    7.2653  -18.4427 C   0  0  0  1  0  0
  -13.2596    6.4164  -17.7736 C   0  0  0  1  0  0
  -12.3586    6.9344  -16.8527 C   0  0  0  1  0  0
  -12.3281    8.3002  -16.5996 C   0  0  0  1  0  0
   -8.2601   10.9918  -12.6776 H   0  0
   -9.8940   10.8986  -13.1858 H   0  0
   -8.1593   12.3312   -8.4125 H   0  0
  -12.6237   14.2222   -8.0179 H   0  0
  -12.3280   12.6590   -6.4268 H   0  0
  -12.6242   11.3184   -7.5155 H   0  0
  -14.8721   11.2099   -7.0203 H   0  0
  -14.4206   11.9972   -5.5133 H   0  0
  -16.2829   13.1755   -7.0929 H   0  0
  -15.0048   14.1625   -6.4025 H   0  0
  -14.8137   14.6467   -8.7670 H   0  0
  -15.1233   12.9568   -9.1590 H   0  0
  -14.0557   12.7646  -11.0397 H   0  0
  -10.7741   12.8296  -14.0117 H   0  0
  -11.2671   12.1221  -16.3123 H   0  0
  -14.6755    9.9747  -14.9264 H   0  0
  -14.2033   10.6888  -12.6392 H   0  0
  -14.7799    9.2902  -18.7067 H   0  0
  -14.8286    6.8655  -19.1640 H   0  0
  -13.2784    5.3547  -17.9718 H   0  0
  -11.6775    6.2760  -16.3337 H   0  0
  -11.6021    8.6819  -15.8965 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372152822235152

> <LigScore1_Dreiding>
2.49

> <LigScore2_Dreiding>
5.03

> <-PLP1>
72.74

> <-PLP2>
62.46

> <Jain>
1.86

> <-PMF>
90.71

> <-PMF04>
31.93

> <AbsoluteEnergy>
149.211

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
23

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
3.163

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
95

> <LibDockScore>
79.308

> <HotSpots>
-16.00,13.72,-7.29,A,87,12
-15.00,13.92,-8.49,A,79,13
-12.60,6.32,-17.69,A,17,26

> <-In-Situ Starting Energy>
-774.821

> <-In-Situ Final Energy>
19.602

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -16.7437    5.7485  -20.0619 N   0  0  0  1  0  0
  -17.2693    5.5923  -18.8262 C   0  0  0  1  0  0
  -18.4857    5.0234  -18.8033 N   0  0  0  1  0  0
  -19.0899    4.8466  -17.6207 C   0  0  0  1  0  0
  -18.5501    5.1333  -16.4459 N   0  0  0  1  0  0
  -17.3371    5.6957  -16.4562 C   0  0  0  1  0  0
  -16.6408    5.9719  -17.6597 C   0  0  0  1  0  0
  -16.5504    6.0955  -15.3743 N   0  0  0  1  0  0
  -16.8532    5.9156  -13.9365 C   0  0  0  1  0  0
  -18.1366    5.1852  -13.5209 C   0  0  0  1  0  0
  -18.2362    5.5092  -12.0349 C   0  0  0  1  0  0
  -17.7787    6.9557  -11.9274 C   0  0  0  1  0  0
  -16.9359    7.2449  -13.1801 C   0  0  0  1  0  0
  -15.4618    6.6606  -15.9259 C   0  0  0  1  0  0
  -15.4175    6.5893  -17.3047 C   0  0  0  1  0  0
  -14.2970    7.0600  -18.1614 C   0  0  0  1  0  0
  -12.9951    6.7380  -17.8249 C   0  0  0  1  0  0
  -11.9271    7.1460  -18.6168 C   0  0  0  1  0  0
  -12.1479    7.8647  -19.7804 C   0  0  0  1  0  0
  -13.4535    8.2182  -20.1022 C   0  0  0  1  0  0
  -14.5130    7.8253  -19.2900 C   0  0  0  1  0  0
  -11.0637    8.2457  -20.5593 O   0  0  0  1  0  0
  -11.1543    7.9964  -21.9268 C   0  0  0  1  0  0
  -11.8648    6.9254  -22.4719 C   0  0  0  1  0  0
  -11.9440    6.7657  -23.8496 C   0  0  0  1  0  0
  -11.2960    7.6598  -24.6915 C   0  0  0  1  0  0
  -10.5458    8.6967  -24.1537 C   0  0  0  1  0  0
  -10.4643    8.8508  -22.7758 C   0  0  0  1  0  0
  -17.3504    5.6504  -20.8574 H   0  0
  -15.7771    5.9565  -20.2024 H   0  0
  -20.0849    4.4444  -17.6283 H   0  0
  -16.0214    5.3422  -13.5252 H   0  0
  -18.1104    4.1136  -13.7222 H   0  0
  -19.0096    5.6037  -14.0229 H   0  0
  -19.2233    5.4112  -11.6123 H   0  0
  -17.5947    4.8420  -11.4675 H   0  0
  -18.6556    7.5963  -11.8965 H   0  0
  -17.2474    7.1165  -10.9966 H   0  0
  -15.9504    7.6414  -12.9423 H   0  0
  -17.4437    7.9877  -13.7969 H   0  0
  -14.6819    7.1226  -15.3380 H   0  0
  -12.7818    6.1577  -16.9383 H   0  0
  -10.9160    6.8875  -18.3481 H   0  0
  -13.6354    8.7963  -20.9918 H   0  0
  -15.5126    8.1378  -19.5484 H   0  0
  -12.3417    6.1975  -21.8321 H   0  0
  -12.5027    5.9403  -24.2656 H   0  0
  -11.3602    7.5400  -25.7636 H   0  0
  -10.0216    9.3789  -24.8076 H   0  0
   -9.8584    9.6356  -22.3516 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372157117202448

> <LigScore1_Dreiding>
3.42

> <LigScore2_Dreiding>
5.2

> <-PLP1>
80.72

> <-PLP2>
77.48

> <Jain>
5.76

> <-PMF>
77.47

> <-PMF04>
19.1

> <AbsoluteEnergy>
147.754

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
18

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
1.707

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
97

> <LibDockScore>
76.896

> <HotSpots>
-18.40,4.72,-11.29,A,50,11
-16.20,6.52,-15.49,A,24,14
-14.40,5.92,-18.29,A,15,17

> <-In-Situ Starting Energy>
-192.479

> <-In-Situ Final Energy>
14.634

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.0369   10.1734  -10.6617 N   0  0  0  1  0  0
  -10.8181    9.5779  -11.5896 C   0  0  0  1  0  0
  -10.5382    8.2864  -11.8287 N   0  0  0  1  0  0
  -11.2905    7.6173  -12.7169 C   0  0  0  1  0  0
  -12.3624    8.1207  -13.3322 N   0  0  0  1  0  0
  -12.6228    9.4225  -13.1165 C   0  0  0  1  0  0
  -11.8497   10.2121  -12.2360 C   0  0  0  1  0  0
  -13.6505   10.2107  -13.6326 N   0  0  0  1  0  0
  -14.7136    9.7219  -14.5418 C   0  0  0  1  0  0
  -16.0477    9.7026  -13.7861 C   0  0  0  1  0  0
  -16.6137   11.0990  -14.0082 C   0  0  0  1  0  0
  -16.3133   11.3390  -15.4779 C   0  0  0  1  0  0
  -14.9448   10.6844  -15.7269 C   0  0  0  1  0  0
  -13.4558   11.4420  -13.1076 C   0  0  0  1  0  0
  -12.3891   11.5159  -12.2366 C   0  0  0  1  0  0
  -11.9282   12.6944  -11.4603 C   0  0  0  1  0  0
  -12.8024   13.3858  -10.6408 C   0  0  0  1  0  0
  -12.3427   14.3992   -9.8017 C   0  0  0  1  0  0
  -10.9886   14.7061   -9.7679 C   0  0  0  1  0  0
  -10.1318   14.0868  -10.6687 C   0  0  0  1  0  0
  -10.6089   13.0995  -11.5198 C   0  0  0  1  0  0
  -10.4794   15.5600   -8.8084 O   0  0  0  1  0  0
   -9.6729   14.8739   -7.9063 C   0  0  0  1  0  0
  -10.1446   13.7634   -7.2071 C   0  0  0  1  0  0
   -9.3129   13.0821   -6.3273 C   0  0  0  1  0  0
   -8.0046   13.5074   -6.1404 C   0  0  0  1  0  0
   -7.5321   14.6131   -6.8342 C   0  0  0  1  0  0
   -8.3683   15.3017   -7.7055 C   0  0  0  1  0  0
   -9.2745    9.6603  -10.2761 H   0  0
  -10.2166   11.1078  -10.3528 H   0  0
  -11.0065    6.5987  -12.9393 H   0  0
  -14.4739    8.7159  -14.8908 H   0  0
  -15.9405    9.4406  -12.7363 H   0  0
  -16.7160    8.9668  -14.2360 H   0  0
  -17.6639   11.1987  -13.7864 H   0  0
  -16.1085   11.8188  -13.3702 H   0  0
  -16.3776   12.3759  -15.7840 H   0  0
  -17.0835   10.8340  -16.0425 H   0  0
  -14.9376   10.1554  -16.6795 H   0  0
  -14.1637   11.4432  -15.7853 H   0  0
  -14.0676   12.3045  -13.3338 H   0  0
  -13.8561   13.1310  -10.6310 H   0  0
  -13.0195   14.9010   -9.1228 H   0  0
   -9.0842   14.3490  -10.6764 H   0  0
   -9.9161   12.6161  -12.1952 H   0  0
  -11.1679   13.4406   -7.3265 H   0  0
   -9.6907   12.2334   -5.7760 H   0  0
   -7.3561   12.9941   -5.4439 H   0  0
   -6.5135   14.9390   -6.6836 H   0  0
   -8.0118   16.1711   -8.2360 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372161412169744

> <LigScore1_Dreiding>
2.09

> <LigScore2_Dreiding>
4.75

> <-PLP1>
94.5

> <-PLP2>
80.47

> <Jain>
3.62

> <-PMF>
116.84

> <-PMF04>
49.35

> <AbsoluteEnergy>
147.442

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
16

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
1.395

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
98

> <LibDockScore>
76.707

> <HotSpots>
-16.80,9.32,-14.09,A,31,10
-16.60,11.32,-15.29,A,27,12
-9.00,13.52,-7.09,A,99,28

> <-In-Situ Starting Energy>
-56713.848

> <-In-Situ Final Energy>
16.62

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -15.8310    9.9222  -13.5078 N   0  0  0  1  0  0
  -14.9230    9.4709  -14.4010 C   0  0  0  1  0  0
  -13.8434   10.2537  -14.5322 N   0  0  0  1  0  0
  -12.9527    9.9728  -15.4889 C   0  0  0  1  0  0
  -13.0454    8.9357  -16.3171 N   0  0  0  1  0  0
  -14.0908    8.1070  -16.1549 C   0  0  0  1  0  0
  -15.0673    8.3185  -15.1480 C   0  0  0  1  0  0
  -14.4436    6.9652  -16.8849 N   0  0  0  1  0  0
  -13.7339    6.3588  -18.0386 C   0  0  0  1  0  0
  -14.5581    6.5673  -19.3114 C   0  0  0  1  0  0
  -14.1093    7.9335  -19.8339 C   0  0  0  1  0  0
  -12.6531    8.1036  -19.3826 C   0  0  0  1  0  0
  -12.3697    6.9454  -18.4180 C   0  0  0  1  0  0
  -15.5775    6.5223  -16.3136 C   0  0  0  1  0  0
  -15.9769    7.2287  -15.1988 C   0  0  0  1  0  0
  -17.1172    6.8872  -14.2997 C   0  0  0  1  0  0
  -17.1307    7.2936  -12.9865 C   0  0  0  1  0  0
  -18.2687    7.1873  -12.2079 C   0  0  0  1  0  0
  -19.4403    6.6500  -12.7210 C   0  0  0  1  0  0
  -19.3683    6.0818  -13.9841 C   0  0  0  1  0  0
  -18.2083    6.1662  -14.7491 C   0  0  0  1  0  0
  -20.6831    6.7169  -12.0820 O   0  0  0  1  0  0
  -20.7416    7.0809  -10.7421 C   0  0  0  1  0  0
  -21.6616    8.0514  -10.3774 C   0  0  0  1  0  0
  -21.6716    8.5472   -9.0806 C   0  0  0  1  0  0
  -20.7533    8.0795   -8.1531 C   0  0  0  1  0  0
  -19.9146    7.0254   -8.4786 C   0  0  0  1  0  0
  -19.9374    6.5005   -9.7631 C   0  0  0  1  0  0
  -15.5884   10.6408  -12.8470 H   0  0
  -16.7647    9.5700  -13.4789 H   0  0
  -12.1034   10.6327  -15.5949 H   0  0
  -13.6161    5.2972  -17.8181 H   0  0
  -15.6355    6.5124  -19.1533 H   0  0
  -14.2992    5.8018  -20.0428 H   0  0
  -14.2053    8.0057  -20.9154 H   0  0
  -14.7256    8.7137  -19.3854 H   0  0
  -12.5154    9.0688  -18.8957 H   0  0
  -11.9663    8.0679  -20.2291 H   0  0
  -11.8171    6.1810  -18.9583 H   0  0
  -11.7436    7.2151  -17.5687 H   0  0
  -16.1173    5.6692  -16.6974 H   0  0
  -16.2581    7.7230  -12.5339 H   0  0
  -18.2317    7.5880  -11.2170 H   0  0
  -20.2433    5.6118  -14.3956 H   0  0
  -18.2330    5.7478  -15.7448 H   0  0
  -22.3411    8.4391  -11.1218 H   0  0
  -22.3726    9.3147   -8.7943 H   0  0
  -20.6984    8.5335   -7.1751 H   0  0
  -19.2339    6.6328   -7.7388 H   0  0
  -19.2803    5.6848  -10.0243 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372165707137040

> <LigScore1_Dreiding>
3.53

> <LigScore2_Dreiding>
5.8

> <-PLP1>
86.35

> <-PLP2>
78.36

> <Jain>
4.3

> <-PMF>
117.05

> <-PMF04>
39.95

> <AbsoluteEnergy>
162.605

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
49

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
16.558

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
99

> <LibDockScore>
73.01

> <HotSpots>
-12.60,6.32,-17.69,A,17,10
-19.40,6.32,-13.69,A,35,20
-21.60,6.32,-8.29,A,80,27

> <-In-Situ Starting Energy>
-1444.257

> <-In-Situ Final Energy>
6.747

> <In-Situ Gradient>
0.001

$$$$
3GEN_ligand
  SciTegic09242210483D

 50 54  0  0  0  0            999 V2000
  -10.8425    9.7226  -10.9651 N   0  0  0  1  0  0
  -10.9139    8.8941  -12.0334 C   0  0  0  1  0  0
  -10.6333    7.6051  -11.7935 N   0  0  0  1  0  0
  -10.6489    6.7470  -12.8230 C   0  0  0  1  0  0
  -10.9485    7.0766  -14.0822 N   0  0  0  1  0  0
  -11.2406    8.3663  -14.3227 C   0  0  0  1  0  0
  -11.2547    9.3205  -13.2904 C   0  0  0  1  0  0
  -11.5740    9.0060  -15.5204 N   0  0  0  1  0  0
  -11.6208    8.3192  -16.8294 C   0  0  0  1  0  0
  -12.5742    7.1228  -16.8726 C   0  0  0  1  0  0
  -12.8596    6.8845  -18.3596 C   0  0  0  1  0  0
  -12.4870    8.1869  -19.0850 C   0  0  0  1  0  0
  -12.1007    9.1886  -17.9926 C   0  0  0  1  0  0
  -11.8111   10.3012  -15.1893 C   0  0  0  1  0  0
  -11.6543   10.5479  -13.8369 C   0  0  0  1  0  0
  -11.8777   11.7644  -13.0254 C   0  0  0  1  0  0
  -13.0543   11.8502  -12.3199 C   0  0  0  1  0  0
  -13.2118   12.8019  -11.3312 C   0  0  0  1  0  0
  -12.2001   13.7108  -11.0490 C   0  0  0  1  0  0
  -11.0793   13.7244  -11.8738 C   0  0  0  1  0  0
  -10.9256   12.7544  -12.8680 C   0  0  0  1  0  0
  -12.2902   14.5537   -9.9474 O   0  0  0  1  0  0
  -12.7153   13.8560   -8.8175 C   0  0  0  1  0  0
  -11.9087   12.8734   -8.2483 C   0  0  0  1  0  0
  -12.3822   12.1007   -7.1934 C   0  0  0  1  0  0
  -13.6640   12.3088   -6.6996 C   0  0  0  1  0  0
  -14.4642   13.3002   -7.2515 C   0  0  0  1  0  0
  -13.9872   14.0732   -8.3035 C   0  0  0  1  0  0
  -10.5707    9.3648  -10.0756 H   0  0
  -11.0609   10.6960  -11.0520 H   0  0
  -10.3913    5.7181  -12.6141 H   0  0
  -10.6156    7.9619  -17.0579 H   0  0
  -13.5021    7.3710  -16.3561 H   0  0
  -12.1527    6.2418  -16.3890 H   0  0
  -12.2495    6.0620  -18.7358 H   0  0
  -13.9035    6.6135  -18.5198 H   0  0
  -13.3012    8.5593  -19.7073 H   0  0
  -11.6327    8.0046  -19.7389 H   0  0
  -11.3463    9.9023  -18.3243 H   0  0
  -12.9880    9.7498  -17.6976 H   0  0
  -12.1001   11.0652  -15.8970 H   0  0
  -13.8724   11.1647  -12.4966 H   0  0
  -14.1396   12.8097  -10.7778 H   0  0
  -10.3016   14.4518  -11.6956 H   0  0
  -10.0157   12.7308  -13.4509 H   0  0
  -10.9177   12.7037   -8.6402 H   0  0
  -11.7574   11.3349   -6.7568 H   0  0
  -14.0351   11.7052   -5.8835 H   0  0
  -15.4554   13.4807   -6.8631 H   0  0
  -14.6082   14.8457   -8.7263 H   0  0
  1  2  1  0
  2  3  2  0
  2  7  1  0
  3  4  1  0
  4  5  2  0
  5  6  1  0
  6  7  2  0
  6  8  1  0
  7 15  1  0
  8  9  1  0
  8 14  1  0
  9 10  1  0
  9 13  1  0
 10 11  1  0
 11 12  1  0
 12 13  1  0
 14 15  2  0
 15 16  1  0
 16 17  2  0
 16 21  1  0
 17 18  1  0
 18 19  2  0
 19 20  1  0
 19 22  1  0
 20 21  2  0
 22 23  1  0
 23 24  2  0
 23 28  1  0
 24 25  1  0
 25 26  2  0
 26 27  1  0
 27 28  2  0
  1 29  1  0
  1 30  1  0
  4 31  1  0
  9 32  1  0
 10 33  1  0
 10 34  1  0
 11 35  1  0
 11 36  1  0
 12 37  1  0
 12 38  1  0
 13 39  1  0
 13 40  1  0
 14 41  1  0
 17 42  1  0
 18 43  1  0
 20 44  1  0
 21 45  1  0
 24 46  1  0
 25 47  1  0
 26 48  1  0
 27 49  1  0
 28 50  1  0
M  END
> <Name>
3GEN_ligand

> <OBJECTID>
9223372170002104336

> <LigScore1_Dreiding>
2.17

> <LigScore2_Dreiding>
4.89

> <-PLP1>
74.19

> <-PLP2>
65.61

> <Jain>
1.52

> <-PMF>
97.37

> <-PMF04>
31.6

> <AbsoluteEnergy>
154.407

> <Angle Energy>
11.64

> <At pH>
7.4

> <Bond Energy>
0.992

> <CHARMm Energy>
0.978

> <ChiRotor E-elec>
-2.688

> <ChiRotor E-total>
-21.316

> <ChiRotor E-vdw>
-31.605

> <ChiRotor RMSD>
2.231

> <ConfNumber>
43

> <Dihedral Energy>
25.221

> <Electrostatic Energy>
-40.9

> <ForcefieldFFML>
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="3GEN_ligand-CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
<angle atom1="CR56" atom2="C5RP" atom3="C6RP">
<quadratic
refValue="126"
forceConstant="70"/>
</angle>
<angle atom1="N5R" atom2="C5R" atom3="C5RP">
<quadratic
refValue="118.125"
forceConstant="68.1667"/>
</angle>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="C6R" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C5R">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
<torsion atom1="CR56" atom2="CR56" atom3="C5RP" atom4="C6RP">
<multiplecos
v1="0"
v2="3.1"
v3="0"
v4="0"
v5="0"
v6="0"
gamma1="0"
gamma2="180"
gamma3="0"
gamma4="0"
gamma5="0"
gamma6="0"/>
</torsion>
</parameters>
</forcefield>
</ffml>

> <Hydrogen Bond Energy>
0

> <Improper Energy>
0.022

> <Initial Potential Energy>
36.253

> <Initial RMS Gradient>
24.835

> <Ionization pH>
7.4

> <IonizationIndex>
1

> <LoopList>
0:3GEN:A:GLY409:409:GLY:TGQ:3,

> <Minimization Criteria>
CONJUG> Minimization exiting with gradient tolerance ( 0.1000000) satisfied.

> <MOL_NUMBER>
1

> <Net Charge>
-4.97

> <NumberOfIonizations>
1

> <PartialChargeMethod>
MomanyRone

> <Potential Energy>
0.978

> <REMARK99>
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  3GEN
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

> <RMS Gradient>
0.088

> <Refined Residues>
6

> <RelativeEnergy>
8.36

> <Resolution>
1.6

> <SEQRES>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <Solvation Free Energy>
0

> <Urey-Bradley Energy>
0

> <UseResidueTemplateCharge>
True

> <Van der Waals Energy>
4.002

> <__PDBRemarks__>
HEADER    TRANSFERASE                             25-FEB-09   3GEN
TITLE     THE 1.6 A CRYSTAL STRUCTURE OF HUMAN BRUTON'S TYROSINE
TITLE    2 KINASE BOUND TO A PYRROLOPYRIMIDINE-CONTAINING COMPOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PROTEIN KINASE, RESIDUES 382-659;
COMPND   5 SYNONYM: BRUTON TYROSINE KINASE, AGAMMAGLOBULINAEMIA
COMPND   6 TYROSINE KINASE, ATK, B-CELL PROGENITOR KINASE, BPK;
COMPND   7 EC: 2.7.10.2;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: AGMX1, ATK, BPK, BTK;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST20
KEYWDS    BRUTON'S TYROSINE KINASE, 4-AMINO-5-(4-PHENOXYPHENYL)-5H-
KEYWDS   2 PYRROLO[3, 2-D]PYRIMIDIN-7-YL-CYCLOPENTANE, TEC-FAMILY,
KEYWDS   3 COMPLEX, ACETYLATION, ATP-BINDING, CYTOPLASM, DISEASE
KEYWDS   4 MUTATION, KINASE, MEMBRANE, METAL-BINDING, NUCLEOTIDE-
KEYWDS   5 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS   6 SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE, ZINC,
KEYWDS   7 ZINC-FINGER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,K.MIATKOWSKI,
AUTHOR   2 C.P.WILDES,P.F.CULLEN,B.HOPKINS,E.MERTSCHING,T.J.JENKINS,
AUTHOR   3 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
REVDAT   2   09-MAR-10 3GEN    1       JRNL
REVDAT   1   19-JAN-10 3GEN    0
JRNL        AUTH   D.J.MARCOTTE,Y.T.LIU,R.M.ARDUINI,C.A.HESSION,
JRNL        AUTH 2 K.MIATKOWSKI,C.P.WILDES,P.F.CULLEN,V.HONG,
JRNL        AUTH 3 B.T.HOPKINS,E.MERTSCHING,T.J.JENKINS,
JRNL        AUTH 4 M.J.ROMANOWSKI,D.P.BAKER,L.F.SILVIAN
JRNL        TITL   STRUCTURES OF HUMAN BRUTON'S TYROSINE KINASE IN
JRNL        TITL 2 ACTIVE AND INACTIVE CONFORMATIONS SUGGEST A
JRNL        TITL 3 MECHANISM OF ACTIVATION FOR TEC FAMILY KINASES.
JRNL        REF    PROTEIN SCI.                  V.  19   429 2010
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   20052711
JRNL        DOI    10.1002/PRO.321
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.93
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 36291
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2680
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.3080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2161
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 495
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : -0.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.281
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2247 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):    22 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3038 ; 1.145 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    48 ; 1.265 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   270 ; 5.471 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;29.970 ;23.846
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   402 ;12.911 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.041 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   319 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1697 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):    15 ; 0.003 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1283 ; 0.218 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    27 ; 0.297 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1529 ; 0.309 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):     2 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.186 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    60 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.157 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1372 ; 0.977 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     7 ; 2.876 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2141 ; 1.179 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1027 ; 1.739 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   894 ; 2.390 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2453 ; 1.661 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   495 ; 1.677 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2211 ; 1.577 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3GEN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 93.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : VARIMAX HR OPTICS
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38206
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1K2P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 5000,0.2M AMMONIUM
REMARK 280  SULFATE, 0.1M MES PH 6.5 , VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.15300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.24850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.15300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   377
REMARK 465     PRO A   378
REMARK 465     LEU A   379
REMARK 465     GLY A   380
REMARK 465     SER A   381
REMARK 465     LYS A   382
REMARK 465     ASN A   383
REMARK 465     ALA A   384
REMARK 465     PRO A   385
REMARK 465     SER A   386
REMARK 465     THR A   387
REMARK 465     ALA A   388
REMARK 465     GLY A   389
REMARK 465     LEU A   390
REMARK 465     GLY A   391
REMARK 465     THR A   410
REMARK 465     GLY A   411
REMARK 465     GLN A   412
REMARK 465     SER A   659
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A 413    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A 433    CG   CD   CE   NZ
REMARK 470     GLN A 467    CG   CD   OE1  NE2
REMARK 470     GLN A 496    CG   CD   OE1  NE2
REMARK 470     THR A 552    OG1  CG2
REMARK 470     VAL A 555    CG1  CG2
REMARK 470     LYS A 637    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PRO A   565     O    HOH A   902              1.99
REMARK 500   O    TYR A   545     O    HOH A   863              2.04
REMARK 500   O    HOH A    34     O    HOH A   679              2.05
REMARK 500   O    HOH A    56     O    HOH A   696              2.08
REMARK 500   O    ASN A   526     O    HOH A   230              2.11
REMARK 500   O    GLY A   462     O    HOH A   687              2.12
REMARK 500   O    HOH A    41     O    HOH A   882              2.12
REMARK 500   O    HOH A   125     O    HOH A   714              2.18
REMARK 500   NE   ARG A   525     O    HOH A   881              2.18
REMARK 500   OE1  GLU A   636     O    HOH A   678              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A 424      -44.45   -131.04
REMARK 500    ARG A 520      -14.17     78.36
REMARK 500    ASP A 521       52.02   -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 770        DISTANCE =  6.78 ANGSTROMS
REMARK 525    HOH A 784        DISTANCE =  6.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B43 A 1
DBREF  3GEN A  382   659  UNP    Q06187   BTK_HUMAN      382    659
SEQADV 3GEN GLY A  377  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN PRO A  378  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN LEU A  379  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN GLY A  380  UNP  Q06187              EXPRESSION TAG
SEQADV 3GEN SER A  381  UNP  Q06187              EXPRESSION TAG
HET    B43  A   1      28
HETNAM     B43 4-AMINO-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM   2 B43  7-YL-CYCLOPENTANE
HETSYN     B43 7-CYCLOPENTYL-5-(4-PHENOXYPHENYL)-7H-PYRROLO[2,3-
HETSYN   2 B43  D]PYRIMIDIN-4-AMINE
FORMUL   2  B43    C23 H22 N4 O
FORMUL   3  HOH   *495(H2 O)
CRYST1   72.497  104.306   38.039  90.00  90.00  90.00 P 21 21 2     4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013794  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009587  0.000000        0.00000
SCALE3      0.000000  0.000000  0.026289        0.00000

> <__PDBSeqres__>
SEQRES   1 A  283  GLY PRO LEU GLY SER LYS ASN ALA PRO SER THR ALA GLY
SEQRES   2 A  283  LEU GLY TYR GLY SER TRP GLU ILE ASP PRO LYS ASP LEU
SEQRES   3 A  283  THR PHE LEU LYS GLU LEU GLY THR GLY GLN PHE GLY VAL
SEQRES   4 A  283  VAL LYS TYR GLY LYS TRP ARG GLY GLN TYR ASP VAL ALA
SEQRES   5 A  283  ILE LYS MET ILE LYS GLU GLY SER MET SER GLU ASP GLU
SEQRES   6 A  283  PHE ILE GLU GLU ALA LYS VAL MET MET ASN LEU SER HIS
SEQRES   7 A  283  GLU LYS LEU VAL GLN LEU TYR GLY VAL CYS THR LYS GLN
SEQRES   8 A  283  ARG PRO ILE PHE ILE ILE THR GLU TYR MET ALA ASN GLY
SEQRES   9 A  283  CYS LEU LEU ASN TYR LEU ARG GLU MET ARG HIS ARG PHE
SEQRES  10 A  283  GLN THR GLN GLN LEU LEU GLU MET CYS LYS ASP VAL CYS
SEQRES  11 A  283  GLU ALA MET GLU TYR LEU GLU SER LYS GLN PHE LEU HIS
SEQRES  12 A  283  ARG ASP LEU ALA ALA ARG ASN CYS LEU VAL ASN ASP GLN
SEQRES  13 A  283  GLY VAL VAL LYS VAL SER ASP PHE GLY LEU SER ARG TYR
SEQRES  14 A  283  VAL LEU ASP ASP GLU TYR THR SER SER VAL GLY SER LYS
SEQRES  15 A  283  PHE PRO VAL ARG TRP SER PRO PRO GLU VAL LEU MET TYR
SEQRES  16 A  283  SER LYS PHE SER SER LYS SER ASP ILE TRP ALA PHE GLY
SEQRES  17 A  283  VAL LEU MET TRP GLU ILE TYR SER LEU GLY LYS MET PRO
SEQRES  18 A  283  TYR GLU ARG PHE THR ASN SER GLU THR ALA GLU HIS ILE
SEQRES  19 A  283  ALA GLN GLY LEU ARG LEU TYR ARG PRO HIS LEU ALA SER
SEQRES  20 A  283  GLU LYS VAL TYR THR ILE MET TYR SER CYS TRP HIS GLU
SEQRES  21 A  283  LYS ALA ASP GLU ARG PRO THR PHE LYS ILE LEU LEU SER
SEQRES  22 A  283  ASN ILE LEU ASP VAL MET ASP GLU GLU SER

> <pI>
6.32

> <POSE_NUMBER>
100

> <LibDockScore>
63.007

> <HotSpots>
-10.00,6.32,-12.49,P,52,3
-14.40,7.72,-18.49,A,11,12
-15.00,13.92,-8.49,A,79,28

> <-In-Situ Starting Energy>
-447.663

> <-In-Situ Final Energy>
10.067

> <In-Situ Gradient>
0.001

$$$$
