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HEADER HYDROLASE 24-AUG-12 4B80
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
TITLE 2 DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,W.QIAN,
AUTHOR 2 F.EKSTROM,A.LINUSSON
REVDAT 1 04-SEP-13 4B80 0
JRNL AUTH C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,
JRNL AUTH 2 W.QIAN,F.EKSTROM,A.LINUSSON
JRNL TITL DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY
JRNL TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.952
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.82
REMARK 3 NUMBER OF REFLECTIONS : 70141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1872
REMARK 3 R VALUE (WORKING SET) : 0.1865
REMARK 3 FREE R VALUE : 0.2229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.9536 - 5.3757 0.99 7188 140 0.1697 0.1837
REMARK 3 2 5.3757 - 4.2713 1.00 6981 135 0.1312 0.1273
REMARK 3 3 4.2713 - 3.7326 1.00 6898 136 0.1506 0.2058
REMARK 3 4 3.7326 - 3.3919 1.00 6865 145 0.1942 0.2355
REMARK 3 5 3.3919 - 3.1491 1.00 6846 126 0.2125 0.2770
REMARK 3 6 3.1491 - 2.9637 1.00 6826 151 0.2159 0.2430
REMARK 3 7 2.9637 - 2.8154 1.00 6798 137 0.2266 0.2645
REMARK 3 8 2.8154 - 2.6929 1.00 6827 135 0.2465 0.2898
REMARK 3 9 2.6929 - 2.5893 1.00 6731 156 0.2656 0.3544
REMARK 3 10 2.5893 - 2.5000 1.00 6774 146 0.3038 0.3742
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.330
REMARK 3 B_SOL : 39.902
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.38
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.4529
REMARK 3 B22 (A**2) : 9.1425
REMARK 3 B33 (A**2) : -21.5955
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 8835
REMARK 3 ANGLE : 1.082 12023
REMARK 3 CHIRALITY : 0.078 1281
REMARK 3 PLANARITY : 0.005 1566
REMARK 3 DIHEDRAL : 15.663 3239
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8793 13.0074 41.4702
REMARK 3 T TENSOR
REMARK 3 T11: 0.3394 T22: 0.2191
REMARK 3 T33: 0.2185 T12: 0.0003
REMARK 3 T13: -0.0604 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 5.0735 L22: 1.9980
REMARK 3 L33: 3.1893 L12: -1.6069
REMARK 3 L13: -1.4687 L23: -0.5918
REMARK 3 S TENSOR
REMARK 3 S11: -0.2166 S12: -0.2411 S13: 0.1140
REMARK 3 S21: 0.4844 S22: 0.1999 S23: -0.0451
REMARK 3 S31: 0.0918 S32: 0.0073 S33: -0.0460
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 46:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3954 16.3773 29.0978
REMARK 3 T TENSOR
REMARK 3 T11: 0.2161 T22: 0.2181
REMARK 3 T33: 0.1901 T12: 0.0071
REMARK 3 T13: -0.0360 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.6416 L22: 1.3124
REMARK 3 L33: 2.1473 L12: -0.1853
REMARK 3 L13: -0.1966 L23: -0.3536
REMARK 3 S TENSOR
REMARK 3 S11: -0.1218 S12: -0.3063 S13: 0.1051
REMARK 3 S21: 0.2115 S22: 0.0329 S23: -0.2339
REMARK 3 S31: -0.0272 S32: 0.0844 S33: 0.0910
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 119:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1701 8.0628 24.4114
REMARK 3 T TENSOR
REMARK 3 T11: 0.2818 T22: 0.2104
REMARK 3 T33: 0.2732 T12: 0.0456
REMARK 3 T13: -0.0385 T23: 0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 1.3790 L22: 0.8154
REMARK 3 L33: 2.7032 L12: 0.1256
REMARK 3 L13: -0.9140 L23: 0.3880
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.0971 S13: -0.1170
REMARK 3 S21: 0.1981 S22: -0.0312 S23: -0.1182
REMARK 3 S31: 0.1475 S32: 0.0847 S33: 0.0493
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 215:277)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0722 8.4979 13.4967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2110 T22: 0.1700
REMARK 3 T33: 0.2130 T12: 0.1045
REMARK 3 T13: 0.0131 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 1.6913 L22: 1.8956
REMARK 3 L33: 2.4723 L12: 0.6875
REMARK 3 L13: 0.5375 L23: -0.3458
REMARK 3 S TENSOR
REMARK 3 S11: -0.1132 S12: 0.2759 S13: -0.2727
REMARK 3 S21: -0.1100 S22: 0.0310 S23: -0.3641
REMARK 3 S31: 0.2881 S32: 0.4400 S33: 0.0791
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 278:324)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2203 8.0420 9.4446
REMARK 3 T TENSOR
REMARK 3 T11: 0.3028 T22: 0.2548
REMARK 3 T33: 0.2634 T12: 0.0786
REMARK 3 T13: 0.0543 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 3.2893 L22: 1.7345
REMARK 3 L33: 3.1406 L12: 0.4582
REMARK 3 L13: 0.7562 L23: 0.7345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: 0.2929 S13: -0.2539
REMARK 3 S21: 0.1066 S22: -0.0608 S23: -0.1904
REMARK 3 S31: 0.2782 S32: 0.1887 S33: 0.1331
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 325:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1350 22.2807 1.1300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2063 T22: 0.2542
REMARK 3 T33: 0.3054 T12: 0.0048
REMARK 3 T13: -0.0011 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 1.6805 L22: 2.6912
REMARK 3 L33: 3.8560 L12: 0.5124
REMARK 3 L13: -0.2587 L23: -1.6168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0724 S12: 0.2971 S13: 0.2625
REMARK 3 S21: -0.0425 S22: -0.0002 S23: 0.0358
REMARK 3 S31: -0.3777 S32: 0.0627 S33: 0.0797
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 367:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9116 17.9621 -8.4693
REMARK 3 T TENSOR
REMARK 3 T11: 0.2558 T22: 0.2756
REMARK 3 T33: 0.2018 T12: -0.0829
REMARK 3 T13: -0.0051 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 5.3910 L22: 4.3593
REMARK 3 L33: 2.6216 L12: -3.1496
REMARK 3 L13: 2.0870 L23: -0.5481
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.7632 S13: 0.2592
REMARK 3 S21: -0.3621 S22: -0.1367 S23: -0.0212
REMARK 3 S31: 0.0521 S32: -0.0248 S33: 0.1156
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 407:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3815 13.8358 16.2308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1388 T22: 0.2921
REMARK 3 T33: 0.2695 T12: -0.0424
REMARK 3 T13: -0.0282 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 2.2236 L22: 1.9641
REMARK 3 L33: 3.6002 L12: -0.0177
REMARK 3 L13: -0.0874 L23: 0.3891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: 0.0071 S13: -0.1249
REMARK 3 S21: 0.0148 S22: 0.0338 S23: 0.2257
REMARK 3 S31: 0.1638 S32: -0.6411 S33: 0.0112
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7984 1.2641 13.9365
REMARK 3 T TENSOR
REMARK 3 T11: 0.3467 T22: 0.4964
REMARK 3 T33: 0.4315 T12: -0.2325
REMARK 3 T13: -0.0110 T23: 0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 4.5213 L22: 8.1305
REMARK 3 L33: 5.2924 L12: -0.4868
REMARK 3 L13: 2.3781 L23: -0.1537
REMARK 3 S TENSOR
REMARK 3 S11: -0.3064 S12: 0.1372 S13: -0.4812
REMARK 3 S21: 0.1975 S22: 0.2450 S23: 0.8537
REMARK 3 S31: 0.3690 S32: -1.2263 S33: 0.1488
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7108 6.2965 -1.2817
REMARK 3 T TENSOR
REMARK 3 T11: 0.3016 T22: 0.4218
REMARK 3 T33: 0.2948 T12: -0.0235
REMARK 3 T13: -0.1447 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.4371 L22: 2.9496
REMARK 3 L33: 8.2484 L12: -1.2155
REMARK 3 L13: -3.0710 L23: 2.5318
REMARK 3 S TENSOR
REMARK 3 S11: -0.0454 S12: 0.0824 S13: -0.2713
REMARK 3 S21: -0.3701 S22: -0.1906 S23: 0.3572
REMARK 3 S31: 0.2785 S32: -0.1408 S33: 0.2243
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7112 6.2791 -61.8686
REMARK 3 T TENSOR
REMARK 3 T11: 0.3737 T22: 0.4590
REMARK 3 T33: 0.3008 T12: 0.0662
REMARK 3 T13: -0.0888 T23: -0.1409
REMARK 3 L TENSOR
REMARK 3 L11: 3.3718 L22: 2.3382
REMARK 3 L33: 3.6356 L12: -0.1917
REMARK 3 L13: -1.6748 L23: 0.3209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: 0.5464 S13: 0.1255
REMARK 3 S21: -0.2847 S22: -0.1001 S23: 0.2746
REMARK 3 S31: -0.2798 S32: -0.7027 S33: 0.0463
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3601 -4.0520 -53.2024
REMARK 3 T TENSOR
REMARK 3 T11: 0.5053 T22: 0.4563
REMARK 3 T33: 0.3333 T12: -0.0287
REMARK 3 T13: -0.0679 T23: -0.1080
REMARK 3 L TENSOR
REMARK 3 L11: 0.7756 L22: 1.1096
REMARK 3 L33: 1.8942 L12: -0.3888
REMARK 3 L13: 0.1841 L23: 0.1829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2961 S12: 0.2483 S13: -0.1665
REMARK 3 S21: -0.0856 S22: -0.1911 S23: 0.0940
REMARK 3 S31: 0.6275 S32: -0.0516 S33: -0.1154
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 87:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2181 5.9556 -53.9505
REMARK 3 T TENSOR
REMARK 3 T11: 0.3016 T22: 0.4800
REMARK 3 T33: 0.2894 T12: 0.0803
REMARK 3 T13: -0.1125 T23: -0.1398
REMARK 3 L TENSOR
REMARK 3 L11: 1.8226 L22: 0.5346
REMARK 3 L33: 1.6184 L12: 0.9065
REMARK 3 L13: -0.5806 L23: 0.0899
REMARK 3 S TENSOR
REMARK 3 S11: 0.0627 S12: 0.4360 S13: -0.1048
REMARK 3 S21: -0.3241 S22: -0.2362 S23: 0.2729
REMARK 3 S31: 0.2380 S32: -0.5021 S33: 0.0740
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 119:298)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9034 3.1834 -47.9983
REMARK 3 T TENSOR
REMARK 3 T11: 0.2413 T22: 0.2990
REMARK 3 T33: 0.1902 T12: 0.0105
REMARK 3 T13: -0.0418 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 1.3157 L22: 1.7095
REMARK 3 L33: 2.9125 L12: -0.3964
REMARK 3 L13: 0.1489 L23: 0.7049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0974 S12: 0.1009 S13: -0.1168
REMARK 3 S21: -0.0629 S22: 0.0008 S23: -0.0628
REMARK 3 S31: 0.2637 S32: 0.3387 S33: -0.0940
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 299:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2472 14.9112 -40.3318
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.2466
REMARK 3 T33: 0.3089 T12: -0.0409
REMARK 3 T13: -0.0409 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 5.1329 L22: 1.6239
REMARK 3 L33: 3.4990 L12: -2.8505
REMARK 3 L13: -1.9487 L23: 1.5659
REMARK 3 S TENSOR
REMARK 3 S11: 0.1174 S12: 0.4408 S13: 0.7421
REMARK 3 S21: -0.0692 S22: -0.0528 S23: -0.4835
REMARK 3 S31: -0.1520 S32: 0.3166 S33: -0.0423
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 332:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0955 -6.2125 -22.0888
REMARK 3 T TENSOR
REMARK 3 T11: 0.6442 T22: 0.2720
REMARK 3 T33: 0.3400 T12: -0.0011
REMARK 3 T13: -0.0330 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 2.0226 L22: 3.3933
REMARK 3 L33: 2.4288 L12: 1.0299
REMARK 3 L13: 0.8617 L23: 0.4794
REMARK 3 S TENSOR
REMARK 3 S11: 0.3213 S12: -0.2192 S13: -0.3682
REMARK 3 S21: 0.3945 S22: -0.0608 S23: -0.0121
REMARK 3 S31: 0.7995 S32: 0.0866 S33: -0.2843
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 383:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5775 5.8957 -29.3366
REMARK 3 T TENSOR
REMARK 3 T11: 0.2723 T22: 0.3338
REMARK 3 T33: 0.2529 T12: -0.0611
REMARK 3 T13: 0.0165 T23: -0.0956
REMARK 3 L TENSOR
REMARK 3 L11: 1.3927 L22: 2.6135
REMARK 3 L33: 3.2755 L12: 0.0450
REMARK 3 L13: 0.2343 L23: -0.3617
REMARK 3 S TENSOR
REMARK 3 S11: 0.1478 S12: -0.1302 S13: -0.0553
REMARK 3 S21: 0.2257 S22: -0.1049 S23: 0.2043
REMARK 3 S31: 0.1429 S32: -0.3235 S33: -0.0509
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6434 22.5898 -28.9922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3157 T22: 0.2608
REMARK 3 T33: 0.2442 T12: 0.0161
REMARK 3 T13: 0.0694 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 4.0471 L22: 9.0608
REMARK 3 L33: 8.7963 L12: -1.3060
REMARK 3 L13: -0.7868 L23: -1.1541
REMARK 3 S TENSOR
REMARK 3 S11: 0.0688 S12: -0.1951 S13: 0.3408
REMARK 3 S21: 0.0461 S22: 0.1595 S23: 0.6287
REMARK 3 S31: -0.4237 S32: -0.8651 S33: -0.1938
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6924 11.6875 -21.7216
REMARK 3 T TENSOR
REMARK 3 T11: 0.4233 T22: 0.4295
REMARK 3 T33: 0.1781 T12: -0.0599
REMARK 3 T13: 0.0160 T23: -0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 4.7349 L22: 1.2398
REMARK 3 L33: 3.3032 L12: -0.4495
REMARK 3 L13: 3.7994 L23: -0.8072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: 0.3311 S13: -0.0347
REMARK 3 S21: 0.1805 S22: -0.0601 S23: -0.0735
REMARK 3 S31: 0.0040 S32: 0.3139 S33: 0.1558
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DUE TO INSUFFICIENT ELECTRON DENSITY THE
REMARK 3 FOLLOWING RESIDUES WERE NOT MODELED CHAIN A 259-262 AND 543-548,
REMARK 3 CHAIN B 1-3, 259-264 AND 543-548. DUE TO INSUFFICIENT ELECTRON
REMARK 3 DENSITY THE FOLLOWING RESIDUES WERE MODELED AS ALANINES, CHAIN A
REMARK 3 496.
REMARK 4
REMARK 4 4B80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-12.
REMARK 100 THE PDBE ID CODE IS EBI-53842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.041
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70343
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 29.01
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.6
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.6
REMARK 200 R MERGE FOR SHELL (I) : 0.66
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (W/V) PEG750MME, 0.1 M HEPES PH
REMARK 280 7.0-7.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.43350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.79450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.77150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.79450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.43350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.77150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 THR A 543
REMARK 465 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 THR B 543
REMARK 465 ALA B 544
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
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 LYS A 496 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 OD2 ASP B 390 ND1A HIS B 393 2.17
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 PHE A 47 -9.11 75.22
REMARK 500 ALA A 62 50.24 -118.33
REMARK 500 CYS A 96 0.65 -154.13
REMARK 500 PRO A 104 156.87 -47.29
REMARK 500 PHE A 123 13.56 59.62
REMARK 500 ALA A 167 72.16 -156.37
REMARK 500 SER A 203 -120.96 56.99
REMARK 500 ASP A 266 -56.77 100.67
REMARK 500 ASP A 306 -90.09 -134.36
REMARK 500 VAL A 407 -64.78 -125.44
REMARK 500 ASP A 488 117.57 -160.56
REMARK 500 PRO B 41 49.07 -79.38
REMARK 500 PHE B 47 -3.71 74.18
REMARK 500 CYS B 96 12.41 -140.36
REMARK 500 ALA B 167 70.50 -155.09
REMARK 500 SER B 203 -120.96 55.91
REMARK 500 VAL B 303 99.93 -68.05
REMARK 500 ASP B 306 -81.66 -128.15
REMARK 500 SER B 495 40.97 -98.49
REMARK 500 SER B 541 -78.77 -57.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A36 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A36 B1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P4C B1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1546 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NDG A1549 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1548 BOUND TO ASN B 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE
REMARK 900 APOFORM
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 DECIDIUM COMPLEX
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 GALLAMINE COMPLEX
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2H9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE
REMARK 900 RELATED ID: 2HA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND HLO-7
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND ORTHO-7
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED VX
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED VX AND SARIN
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN AND IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN (AGED) IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 K027
REMARK 900 RELATED ID: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 2WU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND HI-6
REMARK 900 RELATED ID: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND ORTHO-7
REMARK 900 RELATED ID: 2XUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2XUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 MTH)
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 WK)
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 WK)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 MTH)
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI INHIBITOR
REMARK 900 RELATED ID: 2XUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 SYN INHIBITOR
REMARK 900 RELATED ID: 2XUQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS
REMARK 900 RELATED ID: 4A16 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH
REMARK 900 HUPRINE DERIVATIVE
REMARK 900 RELATED ID: 4A23 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC
REMARK 900 C5685
REMARK 900 RELATED ID: 4ARA RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-
REMARK 900 C5685 AT 2.5 A RESOLUTION.
REMARK 900 RELATED ID: 4ARB RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-
REMARK 900 C5685 AT 2.25 A RESOLUTION.
REMARK 900 RELATED ID: 4B7Z RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B81 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH C-(4-
REMARK 900 CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B82 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B83 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B84 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B85 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-
REMARK 900 CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE
DBREF 4B80 A 1 545 UNP P21836 ACES_MOUSE 32 576
DBREF 4B80 B 1 545 UNP P21836 ACES_MOUSE 32 576
SEQADV 4B80 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B80 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B80 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B80 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B80 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B80 PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
HET A36 A1543 19
HET EDO A1544 4
HET SO4 A1545 5
HET NAG A1546 14
HET PEG A1547 7
HET PEG A1548 7
HET NDG A1549 14
HET PEG A1550 7
HET PGE A1551 10
HET EDO A1552 4
HET A36 B1543 19
HET EDO B1544 4
HET SO4 B1545 5
HET PEG B1546 7
HET PGE B1547 10
HET NAG B1548 14
HET EDO B1549 4
HET EDO B1550 4
HET PEG B1551 7
HET EDO B1552 4
HET PEG B1553 7
HET P4C B1554 22
HETNAM A36 N-[2-(DIETHYLAMINO)ETHYL]-1-(4-FLUOROPHENYL)
HETNAM 2 A36 METHANESULFONAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM P4C O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN P4C POLYETHYLENE 400
FORMUL 3 A36 2(C13 H21 F N2 O2 S)
FORMUL 4 EDO 6(C2 H6 O2)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 PEG 6(C4 H10 O3)
FORMUL 8 NDG C8 H15 N O6
FORMUL 9 PGE 2(C6 H14 O4)
FORMUL 10 P4C C14 H28 O8
FORMUL 11 HOH *273(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 LEU A 216 PHE A 222 5 7
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASP A 266 ARG A 274 1 9
HELIX 12 12 PRO A 277 ASP A 283 1 7
HELIX 13 13 HIS A 284 LEU A 289 5 6
HELIX 14 14 THR A 311 THR A 318 1 8
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 ARG A 534 1 10
HELIX 26 26 ARG A 534 SER A 541 1 8
HELIX 27 27 ASP B 5 GLN B 7 5 3
HELIX 28 28 VAL B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 GLU B 142 1 8
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 ILE B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 SER B 215 1 13
HELIX 36 36 LEU B 216 PHE B 222 5 7
HELIX 37 37 SER B 240 GLY B 256 1 17
HELIX 38 38 ASN B 265 ARG B 276 1 12
HELIX 39 39 PRO B 277 ASP B 283 1 7
HELIX 40 40 HIS B 284 LEU B 289 5 6
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 VAL B 340 1 6
HELIX 43 43 SER B 355 VAL B 367 1 13
HELIX 44 44 SER B 371 THR B 383 1 13
HELIX 45 45 ASP B 390 VAL B 407 1 18
HELIX 46 46 VAL B 407 GLN B 421 1 15
HELIX 47 47 PRO B 440 GLY B 444 5 5
HELIX 48 48 GLU B 450 PHE B 455 1 6
HELIX 49 49 GLY B 456 ASP B 460 5 5
HELIX 50 50 ASP B 460 ASN B 464 5 5
HELIX 51 51 THR B 466 GLY B 487 1 22
HELIX 52 52 ARG B 525 ARG B 534 1 10
HELIX 53 53 PHE B 535 ALA B 542 1 8
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 350 C1 NAG A1546 1555 1555 1.45
LINK ND2 ASN A 464 C1 NDG A1549 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG B1548 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -3.44
CISPEP 2 CYS A 257 PRO A 258 0 -14.12
CISPEP 3 TYR B 105 PRO B 106 0 2.32
CISPEP 4 CYS B 257 PRO B 258 0 -4.31
CISPEP 5 SER B 497 PRO B 498 0 8.06
SITE 1 AC1 10 ASP A 74 TRP A 86 TYR A 124 TYR A 337
SITE 2 AC1 10 PHE A 338 TYR A 341 HIS A 447 PEG A1550
SITE 3 AC1 10 HOH A2062 HOH A2115
SITE 1 AC2 2 SER A 57 VAL A 59
SITE 1 AC3 6 LYS A 23 ALA A 24 PRO A 25 ARG A 136
SITE 2 AC3 6 PHE A 137 ASP A 460
SITE 1 AC4 3 HIS A 381 ASP A 384 GLN B 527
SITE 1 AC5 4 ASP A 304 GLY A 305 SER A 309 ASP A 310
SITE 1 AC6 3 TRP A 286 TYR A 341 A36 A1543
SITE 1 AC7 3 ASP A 333 GLU A 351 TRP A 442
SITE 1 AC8 1 ASP A 5
SITE 1 AC9 9 TRP B 86 GLY B 121 TYR B 124 TRP B 286
SITE 2 AC9 9 PHE B 297 TYR B 337 PHE B 338 TYR B 341
SITE 3 AC9 9 HIS B 447
SITE 1 BC1 1 GLN B 413
SITE 1 BC2 5 LYS B 23 PRO B 25 ARG B 136 PHE B 137
SITE 2 BC2 5 ASP B 460
SITE 1 BC3 1 GLU B 81
SITE 1 BC4 2 HIS B 381 TYR B 382
SITE 1 BC5 1 TYR B 341
SITE 1 BC6 6 THR B 112 PRO B 113 GLU B 142 GLY B 143
SITE 2 BC6 6 ALA B 144 ARG B 485
SITE 1 BC7 4 LYS B 332 ASP B 333 ASP B 396 TRP B 442
SITE 1 BC8 3 GLN B 325 ARG B 485 THR B 486
SITE 1 BC9 1 SER B 309
SITE 1 CC1 10 ALA A 377 LEU A 380 HIS A 381 GLN A 527
SITE 2 CC1 10 PHE A 531 PHE A 535 ALA B 377 LEU B 380
SITE 3 CC1 10 HIS B 381 PHE B 531
SITE 1 CC2 4 SER A 347 ASN A 350 HOH A2124 HOH A2160
SITE 1 CC3 2 SER A 462 ASN A 464
SITE 1 CC4 2 SER B 347 ASN B 350
CRYST1 78.867 111.543 227.589 90.00 90.00 90.00 P 21 21 21 8
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 0.012680 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008965 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004394 0.00000
TER 4206 ALA A 542
TER 8392 ALA B 542
MASTER 843 0 22 53 32 0 31 6 8861 2 213 86
END |