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HEADER HYDROLASE 24-AUG-12 4B84
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-DIETHYLAMINO-
TITLE 2 ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE
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 4B84 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. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.082
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.60
REMARK 3 NUMBER OF REFLECTIONS : 57214
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1775
REMARK 3 R VALUE (WORKING SET) : 0.1764
REMARK 3 FREE R VALUE : 0.2355
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1133
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 29.0837 - 5.1914 0.85 6893 143 0.1666 0.2151
REMARK 3 2 5.1914 - 4.1243 0.89 6938 136 0.1260 0.1513
REMARK 3 3 4.1243 - 3.6041 0.90 6950 138 0.1476 0.2448
REMARK 3 4 3.6041 - 3.2751 0.91 7024 134 0.1925 0.2694
REMARK 3 5 3.2751 - 3.0406 0.92 7035 144 0.1981 0.2730
REMARK 3 6 3.0406 - 2.8615 0.92 7077 141 0.2274 0.2698
REMARK 3 7 2.8615 - 2.7183 0.93 7083 146 0.2605 0.3391
REMARK 3 8 2.7183 - 2.6000 0.93 7081 151 0.2827 0.3233
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.307
REMARK 3 B_SOL : 54.455
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.38
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.4353
REMARK 3 B22 (A**2) : 0.3214
REMARK 3 B33 (A**2) : 0.1139
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 : 0.009 8731
REMARK 3 ANGLE : 1.212 11922
REMARK 3 CHIRALITY : 0.078 1274
REMARK 3 PLANARITY : 0.005 1557
REMARK 3 DIHEDRAL : 16.202 3195
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9961 12.9494 41.4493
REMARK 3 T TENSOR
REMARK 3 T11: 0.3050 T22: 0.1662
REMARK 3 T33: 0.1624 T12: -0.0251
REMARK 3 T13: -0.0367 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 3.7382 L22: 2.1587
REMARK 3 L33: 4.5265 L12: -0.5745
REMARK 3 L13: -1.7736 L23: -0.6047
REMARK 3 S TENSOR
REMARK 3 S11: -0.1756 S12: -0.1443 S13: 0.1772
REMARK 3 S21: 0.5574 S22: 0.2205 S23: 0.0033
REMARK 3 S31: 0.0926 S32: -0.0222 S33: -0.0559
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 46:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6108 16.6464 29.2931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2747 T22: 0.3205
REMARK 3 T33: 0.2249 T12: 0.0445
REMARK 3 T13: -0.0239 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 3.3114 L22: 1.7226
REMARK 3 L33: 1.9496 L12: -0.1147
REMARK 3 L13: 0.3456 L23: -0.0261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: -0.0624 S13: 0.3870
REMARK 3 S21: 0.1912 S22: -0.0874 S23: -0.1067
REMARK 3 S31: -0.2273 S32: 0.0334 S33: 0.0508
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 119:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1035 7.7230 20.8056
REMARK 3 T TENSOR
REMARK 3 T11: 0.3272 T22: 0.1422
REMARK 3 T33: 0.2638 T12: 0.0592
REMARK 3 T13: 0.0143 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 1.0818 L22: 0.6266
REMARK 3 L33: 2.3170 L12: 0.1156
REMARK 3 L13: -0.1527 L23: -0.5740
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.0496 S13: -0.2539
REMARK 3 S21: 0.0371 S22: 0.0115 S23: -0.0960
REMARK 3 S31: 0.3490 S32: 0.1347 S33: 0.0092
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 256:288)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.6097 17.6363 15.2458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1660 T22: 0.4905
REMARK 3 T33: 0.4136 T12: -0.0116
REMARK 3 T13: 0.0752 T23: 0.1167
REMARK 3 L TENSOR
REMARK 3 L11: 1.4395 L22: 4.3939
REMARK 3 L33: 4.2703 L12: 1.3923
REMARK 3 L13: 0.8758 L23: -2.4581
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: 1.2233 S13: 0.6550
REMARK 3 S21: 0.5179 S22: -0.5735 S23: -0.9114
REMARK 3 S31: -0.0111 S32: 0.1942 S33: 0.3559
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 289:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1527 3.6658 9.2119
REMARK 3 T TENSOR
REMARK 3 T11: 0.4406 T22: 0.2163
REMARK 3 T33: 0.2277 T12: 0.0062
REMARK 3 T13: 0.0857 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 5.3773 L22: 1.0806
REMARK 3 L33: 2.1066 L12: 0.0559
REMARK 3 L13: 0.4773 L23: 0.4151
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.3287 S13: -0.6454
REMARK 3 S21: 0.1370 S22: 0.1986 S23: -0.2752
REMARK 3 S31: 0.6216 S32: 0.1226 S33: -0.0756
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1390 17.6242 6.3495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1806 T22: 0.2707
REMARK 3 T33: 0.2523 T12: -0.0405
REMARK 3 T13: -0.0105 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 1.2943 L22: 0.8977
REMARK 3 L33: 3.9305 L12: -0.0666
REMARK 3 L13: 0.0928 L23: -0.0492
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: 0.2047 S13: 0.0095
REMARK 3 S21: -0.0476 S22: 0.0661 S23: 0.1448
REMARK 3 S31: 0.0561 S32: -0.2628 S33: -0.0066
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3339 1.5656 13.5677
REMARK 3 T TENSOR
REMARK 3 T11: 0.3868 T22: 0.5574
REMARK 3 T33: 0.5331 T12: -0.2426
REMARK 3 T13: 0.0394 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 7.2650 L22: 9.0656
REMARK 3 L33: 4.3818 L12: -0.9087
REMARK 3 L13: -1.0690 L23: -2.7241
REMARK 3 S TENSOR
REMARK 3 S11: 0.1051 S12: -0.0588 S13: -1.0102
REMARK 3 S21: 0.5290 S22: -0.1494 S23: 1.1246
REMARK 3 S31: 0.9417 S32: -1.7414 S33: 0.1388
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:541)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2771 6.6048 -0.7575
REMARK 3 T TENSOR
REMARK 3 T11: 0.3858 T22: 0.5122
REMARK 3 T33: 0.2698 T12: -0.0446
REMARK 3 T13: -0.1240 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 4.1820 L22: 1.7345
REMARK 3 L33: 4.9543 L12: -0.3832
REMARK 3 L13: -3.5969 L23: 0.7055
REMARK 3 S TENSOR
REMARK 3 S11: -0.4698 S12: -0.1215 S13: 0.1982
REMARK 3 S21: -0.4095 S22: 0.3769 S23: 0.2703
REMARK 3 S31: 0.6213 S32: 0.0357 S33: 0.1100
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3705 6.3352 -61.6727
REMARK 3 T TENSOR
REMARK 3 T11: 0.3240 T22: 0.7106
REMARK 3 T33: 0.2308 T12: 0.1138
REMARK 3 T13: -0.1202 T23: -0.1586
REMARK 3 L TENSOR
REMARK 3 L11: 3.9402 L22: 1.5835
REMARK 3 L33: 1.8159 L12: 0.4573
REMARK 3 L13: -0.2875 L23: -0.1676
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: 0.2851 S13: 0.5466
REMARK 3 S21: -0.4133 S22: -0.0178 S23: 0.0152
REMARK 3 S31: -0.2134 S32: -0.6896 S33: 0.0540
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:111)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6682 -0.9027 -53.8257
REMARK 3 T TENSOR
REMARK 3 T11: 0.3394 T22: 0.4608
REMARK 3 T33: 0.3518 T12: 0.0597
REMARK 3 T13: -0.0813 T23: -0.1566
REMARK 3 L TENSOR
REMARK 3 L11: 1.0493 L22: 2.4696
REMARK 3 L33: 3.7175 L12: 0.2186
REMARK 3 L13: 0.4001 L23: 0.1011
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: 0.2669 S13: -0.1476
REMARK 3 S21: -0.2788 S22: -0.2846 S23: 0.2925
REMARK 3 S31: 0.5960 S32: -0.1659 S33: 0.0718
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 112:170)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8216 4.4042 -48.8618
REMARK 3 T TENSOR
REMARK 3 T11: 0.3162 T22: 0.4749
REMARK 3 T33: 0.2223 T12: -0.0426
REMARK 3 T13: -0.0302 T23: -0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 2.1876 L22: 2.4082
REMARK 3 L33: 2.4243 L12: -0.6154
REMARK 3 L13: 1.5589 L23: 0.8525
REMARK 3 S TENSOR
REMARK 3 S11: 0.3168 S12: 0.6874 S13: -0.2269
REMARK 3 S21: -0.2347 S22: -0.3025 S23: 0.1743
REMARK 3 S31: 0.1484 S32: 0.1750 S33: -0.0004
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 171:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4418 9.6034 -47.3642
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.2595
REMARK 3 T33: 0.2263 T12: -0.0423
REMARK 3 T13: -0.0000 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 1.2631 L22: 2.3917
REMARK 3 L33: 4.0551 L12: -0.1952
REMARK 3 L13: 0.3413 L23: 0.4579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0543 S12: 0.0850 S13: 0.0470
REMARK 3 S21: -0.1597 S22: 0.0016 S23: -0.1354
REMARK 3 S31: -0.1477 S32: 0.2673 S33: -0.0072
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 256:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7587 -9.2444 -46.8229
REMARK 3 T TENSOR
REMARK 3 T11: 0.5657 T22: 0.4859
REMARK 3 T33: 0.2727 T12: 0.2317
REMARK 3 T13: -0.1059 T23: -0.1455
REMARK 3 L TENSOR
REMARK 3 L11: 0.6626 L22: 3.4676
REMARK 3 L33: 6.2155 L12: -1.0494
REMARK 3 L13: -0.5172 L23: 2.1951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1446 S12: -0.0674 S13: -0.5093
REMARK 3 S21: 0.1626 S22: 0.1330 S23: 0.2146
REMARK 3 S31: 0.9742 S32: 1.2605 S33: 0.0154
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 301:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5620 11.6610 -36.9279
REMARK 3 T TENSOR
REMARK 3 T11: 0.2746 T22: 0.4115
REMARK 3 T33: 0.2938 T12: -0.1066
REMARK 3 T13: -0.0501 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 3.5826 L22: 2.2681
REMARK 3 L33: 3.1923 L12: -1.4689
REMARK 3 L13: 0.5406 L23: 0.9746
REMARK 3 S TENSOR
REMARK 3 S11: 0.1398 S12: 0.4169 S13: 0.4567
REMARK 3 S21: -0.1454 S22: -0.0715 S23: 0.0391
REMARK 3 S31: -0.0697 S32: 0.2640 S33: -0.0875
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 341:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8672 2.7017 -26.8263
REMARK 3 T TENSOR
REMARK 3 T11: 0.3101 T22: 0.1800
REMARK 3 T33: 0.2804 T12: -0.1140
REMARK 3 T13: 0.0207 T23: -0.1202
REMARK 3 L TENSOR
REMARK 3 L11: 2.3359 L22: 1.4370
REMARK 3 L33: 4.0142 L12: 0.2141
REMARK 3 L13: 0.8594 L23: 0.4900
REMARK 3 S TENSOR
REMARK 3 S11: 0.2687 S12: -0.1998 S13: -0.3026
REMARK 3 S21: 0.3545 S22: -0.1751 S23: 0.3290
REMARK 3 S31: 0.6950 S32: -0.2693 S33: -0.0981
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3554 22.4320 -28.8043
REMARK 3 T TENSOR
REMARK 3 T11: 0.3607 T22: 0.5615
REMARK 3 T33: 0.3660 T12: 0.0654
REMARK 3 T13: 0.0031 T23: -0.1205
REMARK 3 L TENSOR
REMARK 3 L11: 5.3150 L22: 4.7723
REMARK 3 L33: 8.2754 L12: -0.4506
REMARK 3 L13: 2.2703 L23: -3.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.2851 S12: -0.7358 S13: 1.0677
REMARK 3 S21: 0.0525 S22: 0.1938 S23: 0.3031
REMARK 3 S31: -0.0868 S32: -1.5625 S33: 0.0266
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2848 12.0875 -21.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.4630 T22: 0.7140
REMARK 3 T33: 0.2607 T12: -0.0755
REMARK 3 T13: 0.0209 T23: -0.1378
REMARK 3 L TENSOR
REMARK 3 L11: 5.2539 L22: 0.9255
REMARK 3 L33: 3.2806 L12: -0.1328
REMARK 3 L13: 3.7298 L23: -1.0085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0517 S12: -0.2798 S13: 0.1665
REMARK 3 S21: 0.0252 S22: -0.1883 S23: -0.0648
REMARK 3 S31: -0.0531 S32: 0.2338 S33: 0.1575
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4B84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-12.
REMARK 100 THE PDBE ID CODE IS EBI-53846.
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 : 57324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 29.75
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : 5.0
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.9
REMARK 200 R MERGE FOR SHELL (I) : 0.48
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.50
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 (%): 70.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 % (W/V)PEG750 MME, 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 39.57900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.62000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.17800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.62000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.57900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.17800
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: 6170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.8 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 ALA A 263
REMARK 465 ALA A 542
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 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 ALA B 542
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 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 258 CG CD
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 SER A 495 OG
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 SER A 541 OG
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 494 CG OD1 OD2
REMARK 470 SER B 495 OG
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 SER B 497 OG
REMARK 470 SER B 541 OG
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 ASN B 482 OG1 THR B 486 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 368 C - N - CA ANGL. DEV. = 9.1 DEGREES
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 PRO A 6 0.59 -66.23
REMARK 500 PHE A 47 -12.51 79.56
REMARK 500 ALA A 62 50.08 -111.15
REMARK 500 PRO A 104 163.94 -44.59
REMARK 500 ALA A 167 71.35 -150.56
REMARK 500 ASN A 170 11.52 60.00
REMARK 500 SER A 203 -112.61 34.94
REMARK 500 ASP A 306 -84.92 -146.63
REMARK 500 ASP A 310 -166.73 -128.82
REMARK 500 VAL A 407 -65.25 -122.89
REMARK 500 ASP A 494 41.93 -92.31
REMARK 500 ARG A 525 50.88 27.44
REMARK 500 PRO B 40 107.60 -45.29
REMARK 500 PHE B 47 -8.99 70.45
REMARK 500 THR B 75 23.49 -144.52
REMARK 500 ALA B 167 65.57 -168.02
REMARK 500 SER B 203 -122.97 50.41
REMARK 500 ALA B 264 -109.15 -118.52
REMARK 500 PRO B 301 152.33 -47.82
REMARK 500 ASP B 306 -79.09 -126.03
REMARK 500 TYR B 341 46.73 -101.32
REMARK 500 GLU B 351 6.29 -65.96
REMARK 500 VAL B 367 62.83 -150.41
REMARK 500 TRP B 385 2.27 -62.86
REMARK 500 VAL B 407 -63.27 -121.95
REMARK 500 SER B 495 166.92 88.28
REMARK 500 SER B 497 -153.93 -109.59
REMARK 500 PRO B 498 4.18 -52.70
REMARK 500 GLN B 499 134.17 76.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 P3G A 1542
REMARK 610 P3G A 1543
REMARK 610 P3G A 1545
REMARK 610 P3G B 1542
REMARK 610 P6G B 1546
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K B1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P3G A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z5K B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 701 BOUND TO ASN A 464
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: 4B80 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-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: 4B85 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-
REMARK 900 CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE
DBREF 4B84 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4B84 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4B84 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4B84 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4B84 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B84 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B84 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B84 ALA A 263 UNP P21836 GLY 294 CONFLICT
SEQADV 4B84 ALA A 264 UNP P21836 GLY 295 CONFLICT
SEQADV 4B84 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4B84 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4B84 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B84 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B84 PRO B 548 UNP P21836 EXPRESSION TAG
SEQADV 4B84 ALA B 263 UNP P21836 GLY 294 CONFLICT
SEQADV 4B84 ALA B 264 UNP P21836 GLY 295 CONFLICT
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 ALA ALA 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 ALA ALA 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 NAG A 701 14
HET P3G B1542 7
HET P3G A1542 9
HET P3G A1543 9
HET Z5K B1543 21
HET SO4 B1544 5
HET SO4 A1544 5
HET P3G A1545 6
HET Z5K A1546 21
HET Z5K B1545 21
HET P6G B1546 17
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM P3G 3,6,9,12,15-PENTAOXAHEPTADECANE
HETNAM Z5K N-[2-(DIETHYLAMINO)ETHYL]-3-(TRIFLUOROMETHYL)
HETNAM 2 Z5K BENZENESULFONAMIDE
HETNAM SO4 SULFATE ION
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 NAG C8 H15 N O6
FORMUL 6 Z5K 3(C13 H19 F3 N2 O2 S)
FORMUL 7 SO4 2(O4 S 2-)
FORMUL 8 P6G C12 H26 O7
FORMUL 9 HOH *384(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 ARG A 219 5 4
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ALA A 264 ARG A 274 1 11
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 LEU A 289 5 4
HELIX 14 14 THR A 311 GLY A 319 1 9
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 PHE A 535 1 11
HELIX 26 26 ASP B 5 GLN B 7 5 3
HELIX 27 27 VAL B 42 ARG B 46 5 5
HELIX 28 28 PHE B 80 MET B 85 1 6
HELIX 29 29 LEU B 130 ASP B 134 5 5
HELIX 30 30 GLY B 135 GLU B 142 1 8
HELIX 31 31 VAL B 153 LEU B 159 1 7
HELIX 32 32 ASN B 170 ILE B 187 1 18
HELIX 33 33 ALA B 188 PHE B 190 5 3
HELIX 34 34 SER B 203 LEU B 214 1 12
HELIX 35 35 SER B 215 ARG B 219 5 5
HELIX 36 36 ALA B 241 GLY B 256 1 16
HELIX 37 37 ASN B 265 THR B 275 1 11
HELIX 38 38 PRO B 277 TRP B 286 1 10
HELIX 39 39 HIS B 287 LEU B 289 5 3
HELIX 40 40 THR B 311 GLY B 319 1 9
HELIX 41 41 GLY B 335 VAL B 340 1 6
HELIX 42 42 SER B 355 VAL B 367 1 13
HELIX 43 43 SER B 371 THR B 383 1 13
HELIX 44 44 ASP B 390 VAL B 407 1 18
HELIX 45 45 VAL B 407 GLN B 421 1 15
HELIX 46 46 PRO B 440 GLY B 444 5 5
HELIX 47 47 GLU B 450 PHE B 455 1 6
HELIX 48 48 GLY B 456 ASP B 460 5 5
HELIX 49 49 ASP B 460 ASN B 464 5 5
HELIX 50 50 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 PHE B 535 SER B 541 1 7
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
SHEET 1 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK ND2 ASN A 464 C1 NAG A 701 1555 1555 1.46
CISPEP 1 TYR A 105 PRO A 106 0 3.71
CISPEP 2 TYR B 105 PRO B 106 0 3.60
CISPEP 3 ASP B 494 SER B 495 0 11.56
CISPEP 4 LYS B 496 SER B 497 0 4.67
SITE 1 AC1 4 GLN A 527 HOH A2209 HIS B 381 TYR B 382
SITE 1 AC2 3 HIS A 381 THR A 383 GLN B 527
SITE 1 AC3 13 TRP B 86 GLY B 121 GLY B 122 TYR B 124
SITE 2 AC3 13 TYR B 133 GLU B 202 TRP B 286 TYR B 337
SITE 3 AC3 13 PHE B 338 TYR B 341 HIS B 447 HOH B2061
SITE 4 AC3 13 HOH B2122
SITE 1 AC4 5 LYS B 23 ALA B 24 PRO B 25 ASP B 460
SITE 2 AC4 5 HOH B2173
SITE 1 AC5 6 LYS A 23 ALA A 24 PRO A 25 ARG A 136
SITE 2 AC5 6 PHE A 137 ASP A 460
SITE 1 AC6 2 GLY A 305 SER A 309
SITE 1 AC7 11 TRP A 86 GLY A 120 GLY A 121 TYR A 124
SITE 2 AC7 11 GLU A 202 SER A 203 TRP A 286 PHE A 297
SITE 3 AC7 11 TYR A 337 TYR A 341 HIS A 447
SITE 1 AC8 9 GLY B 79 GLU B 81 GLU B 84 MET B 85
SITE 2 AC8 9 ASP B 131 LEU B 457 LEU B 463 HOH B2043
SITE 3 AC8 9 HOH B2049
SITE 1 AC9 9 LEU A 380 HIS A 381 GLN A 527 PHE A 531
SITE 2 AC9 9 HOH A2164 ALA B 377 LEU B 380 HIS B 381
SITE 3 AC9 9 PHE B 535
SITE 1 BC1 4 SER A 462 ASN A 464 HOH A2207 HOH A2208
CRYST1 79.158 112.356 227.240 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 0.012633 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004401 0.00000
TER 4194 SER A 541
TER 8346 SER B 541
MASTER 811 0 11 52 34 0 21 6 8863 2 148 86
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