| content |
HEADER HYDROLASE 24-AUG-12 4B81
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 1-(4-CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE
CAVEAT 4B81 NAG A 1549 PLANAR AT ATOM C1
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 4B81 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.003
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.71
REMARK 3 NUMBER OF REFLECTIONS : 48890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1973
REMARK 3 R VALUE (WORKING SET) : 0.1965
REMARK 3 FREE R VALUE : 0.2391
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 963
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 29.0043 - 5.3466 0.99 7109 137 0.1751 0.2029
REMARK 3 2 5.3466 - 4.2481 1.00 6913 137 0.1548 0.1824
REMARK 3 3 4.2481 - 3.7123 1.00 6834 125 0.1722 0.2263
REMARK 3 4 3.7123 - 3.3734 1.00 6809 150 0.2048 0.2473
REMARK 3 5 3.3734 - 3.1320 1.00 6793 115 0.2351 0.3018
REMARK 3 6 3.1320 - 2.9475 1.00 6757 158 0.2763 0.2958
REMARK 3 7 2.9475 - 2.8000 1.00 6712 141 0.3288 0.4254
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.328
REMARK 3 B_SOL : 43.069
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.39
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.9764
REMARK 3 B22 (A**2) : 9.7384
REMARK 3 B33 (A**2) : -27.7148
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 : 0.005 8745
REMARK 3 ANGLE : 0.920 11910
REMARK 3 CHIRALITY : 0.066 1276
REMARK 3 PLANARITY : 0.005 1551
REMARK 3 DIHEDRAL : 17.241 3187
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2320 12.9230 38.3778
REMARK 3 T TENSOR
REMARK 3 T11: 0.4112 T22: 0.4272
REMARK 3 T33: 0.3326 T12: -0.0032
REMARK 3 T13: -0.0495 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: -0.0995 L22: 0.2052
REMARK 3 L33: 0.8735 L12: 0.0115
REMARK 3 L13: -0.4680 L23: -0.3248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0978 S12: -0.2145 S13: 0.1629
REMARK 3 S21: 0.2589 S22: 0.1120 S23: -0.1084
REMARK 3 S31: 0.1459 S32: 0.1254 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 72:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3653 16.1540 26.1251
REMARK 3 T TENSOR
REMARK 3 T11: 0.3947 T22: 0.3250
REMARK 3 T33: 0.3962 T12: -0.0110
REMARK 3 T13: -0.0164 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.6897 L22: 0.2696
REMARK 3 L33: 0.9070 L12: -0.3060
REMARK 3 L13: 0.7414 L23: -0.0211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0790 S12: -0.0418 S13: 0.0776
REMARK 3 S21: 0.0516 S22: -0.0077 S23: -0.1416
REMARK 3 S31: -0.0417 S32: 0.0493 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 159:190)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0856 3.2553 25.7345
REMARK 3 T TENSOR
REMARK 3 T11: 0.4011 T22: 0.2834
REMARK 3 T33: 0.3345 T12: 0.1255
REMARK 3 T13: -0.0334 T23: 0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 0.1628 L22: 0.7217
REMARK 3 L33: 0.4572 L12: 0.2493
REMARK 3 L13: 0.0760 L23: -0.3549
REMARK 3 S TENSOR
REMARK 3 S11: 0.1963 S12: -0.4937 S13: 0.1543
REMARK 3 S21: 0.0881 S22: 0.0405 S23: 0.0154
REMARK 3 S31: 0.6820 S32: 0.4420 S33: 0.0456
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 191:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7237 0.6290 21.6739
REMARK 3 T TENSOR
REMARK 3 T11: 0.3654 T22: 0.2656
REMARK 3 T33: 0.3409 T12: -0.0506
REMARK 3 T13: -0.0061 T23: 0.0536
REMARK 3 L TENSOR
REMARK 3 L11: 0.1248 L22: 0.0963
REMARK 3 L33: 0.0516 L12: 0.0444
REMARK 3 L13: -0.0143 L23: 0.1320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: 0.0111 S13: -0.1559
REMARK 3 S21: 0.2509 S22: -0.0485 S23: 0.0432
REMARK 3 S31: 0.3062 S32: -0.2064 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 229:255)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1335 10.5019 7.4723
REMARK 3 T TENSOR
REMARK 3 T11: 0.4947 T22: 0.3598
REMARK 3 T33: 0.3701 T12: 0.1073
REMARK 3 T13: 0.0418 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.1542 L22: 0.1282
REMARK 3 L33: 0.6156 L12: -0.2292
REMARK 3 L13: 0.0735 L23: -0.2355
REMARK 3 S TENSOR
REMARK 3 S11: 0.1152 S12: 0.5208 S13: -0.3887
REMARK 3 S21: -0.0601 S22: -0.0933 S23: -0.0057
REMARK 3 S31: 0.2950 S32: 0.1734 S33: 0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 256:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2580 8.6738 11.6868
REMARK 3 T TENSOR
REMARK 3 T11: 0.3536 T22: 0.3560
REMARK 3 T33: 0.4104 T12: 0.0221
REMARK 3 T13: 0.0269 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.2197 L22: 0.3102
REMARK 3 L33: 1.4783 L12: 0.1504
REMARK 3 L13: 0.0026 L23: -0.4649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: 0.3033 S13: 0.0176
REMARK 3 S21: 0.0704 S22: -0.0042 S23: -0.0775
REMARK 3 S31: 0.2492 S32: 0.2731 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0377 21.4594 -3.9128
REMARK 3 T TENSOR
REMARK 3 T11: 0.4459 T22: 0.5083
REMARK 3 T33: 0.4973 T12: 0.0109
REMARK 3 T13: 0.0019 T23: 0.0744
REMARK 3 L TENSOR
REMARK 3 L11: 0.2959 L22: 0.3115
REMARK 3 L33: 0.4102 L12: 0.0743
REMARK 3 L13: -0.4416 L23: -0.1460
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: 0.2986 S13: 0.2406
REMARK 3 S21: -0.3732 S22: 0.0318 S23: -0.0661
REMARK 3 S31: -0.2938 S32: 0.0117 S33: -0.0001
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 383:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9948 15.0292 10.8805
REMARK 3 T TENSOR
REMARK 3 T11: 0.3193 T22: 0.3830
REMARK 3 T33: 0.3703 T12: -0.0370
REMARK 3 T13: -0.0115 T23: 0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 0.8540 L22: 0.4875
REMARK 3 L33: 1.0139 L12: -0.0024
REMARK 3 L13: 0.4250 L23: 0.0542
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: 0.0576 S13: -0.0679
REMARK 3 S21: -0.1021 S22: 0.0282 S23: 0.1461
REMARK 3 S31: 0.0125 S32: -0.3155 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0937 0.9211 13.9493
REMARK 3 T TENSOR
REMARK 3 T11: 0.5830 T22: 0.4938
REMARK 3 T33: 0.5577 T12: -0.1834
REMARK 3 T13: -0.0504 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.0873 L22: 0.1171
REMARK 3 L33: 0.1056 L12: -0.0290
REMARK 3 L13: 0.1523 L23: -0.0670
REMARK 3 S TENSOR
REMARK 3 S11: -0.2503 S12: 0.4204 S13: -0.4885
REMARK 3 S21: -0.0167 S22: 0.0865 S23: 0.4509
REMARK 3 S31: 0.1399 S32: -0.0862 S33: 0.0004
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3335 5.9990 -1.2280
REMARK 3 T TENSOR
REMARK 3 T11: 0.3021 T22: 0.7316
REMARK 3 T33: 0.4202 T12: -0.0691
REMARK 3 T13: -0.1465 T23: -0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 0.1973 L22: 0.6111
REMARK 3 L33: 0.5266 L12: -0.6018
REMARK 3 L13: 0.1005 L23: -0.5408
REMARK 3 S TENSOR
REMARK 3 S11: 0.2806 S12: -0.4191 S13: 0.2948
REMARK 3 S21: -0.5544 S22: -0.0697 S23: 0.0241
REMARK 3 S31: 0.3979 S32: 0.0179 S33: 0.0667
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6238 6.2001 -62.0388
REMARK 3 T TENSOR
REMARK 3 T11: 0.4734 T22: 0.6004
REMARK 3 T33: 0.4989 T12: 0.0393
REMARK 3 T13: -0.0689 T23: -0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 0.2556 L22: 0.1867
REMARK 3 L33: 0.7611 L12: -0.0508
REMARK 3 L13: 0.3377 L23: 0.4231
REMARK 3 S TENSOR
REMARK 3 S11: -0.1383 S12: 0.4436 S13: -0.1002
REMARK 3 S21: -0.1818 S22: -0.0667 S23: -0.0378
REMARK 3 S31: -0.0404 S32: -0.1534 S33: 0.0002
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4853 1.1728 -51.7948
REMARK 3 T TENSOR
REMARK 3 T11: 0.3391 T22: 0.3753
REMARK 3 T33: 0.3184 T12: -0.0053
REMARK 3 T13: -0.0367 T23: -0.0458
REMARK 3 L TENSOR
REMARK 3 L11: -0.1329 L22: 1.0579
REMARK 3 L33: 1.4818 L12: 0.1189
REMARK 3 L13: 0.2871 L23: 0.6744
REMARK 3 S TENSOR
REMARK 3 S11: 0.1559 S12: 0.3308 S13: -0.0746
REMARK 3 S21: -0.1535 S22: -0.2017 S23: 0.0103
REMARK 3 S31: 0.3093 S32: 0.0644 S33: -0.0011
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 159:324)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9093 5.0111 -46.9468
REMARK 3 T TENSOR
REMARK 3 T11: 0.3682 T22: 0.4489
REMARK 3 T33: 0.4089 T12: 0.0412
REMARK 3 T13: -0.0543 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 0.2388 L22: 0.5533
REMARK 3 L33: 1.3784 L12: -0.5546
REMARK 3 L13: -0.0287 L23: -0.0753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0516 S12: 0.0756 S13: -0.0552
REMARK 3 S21: -0.0834 S22: 0.0137 S23: 0.0438
REMARK 3 S31: 0.0591 S32: 0.2793 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 325:355)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3549 -4.2751 -27.2483
REMARK 3 T TENSOR
REMARK 3 T11: 0.7887 T22: 0.3995
REMARK 3 T33: 0.5309 T12: -0.0622
REMARK 3 T13: -0.0365 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: -0.1972 L22: 0.1623
REMARK 3 L33: 0.1836 L12: 0.1925
REMARK 3 L13: 0.0734 L23: 0.0759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: -0.5281 S13: -0.0799
REMARK 3 S21: 0.2614 S22: 0.0649 S23: -0.0613
REMARK 3 S31: 0.5913 S32: -0.1267 S33: 0.0051
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 356:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4208 3.7837 -27.5554
REMARK 3 T TENSOR
REMARK 3 T11: 0.4174 T22: 0.3689
REMARK 3 T33: 0.3773 T12: -0.0219
REMARK 3 T13: -0.0069 T23: -0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 0.1416 L22: 0.6691
REMARK 3 L33: 1.7568 L12: 0.2362
REMARK 3 L13: 0.0797 L23: -0.0336
REMARK 3 S TENSOR
REMARK 3 S11: 0.1996 S12: -0.0722 S13: 0.0727
REMARK 3 S21: 0.1523 S22: -0.2018 S23: -0.0239
REMARK 3 S31: 0.2806 S32: -0.0546 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5618 16.1061 -24.8741
REMARK 3 T TENSOR
REMARK 3 T11: 0.6508 T22: 0.4764
REMARK 3 T33: 0.4262 T12: -0.0295
REMARK 3 T13: -0.0240 T23: -0.0485
REMARK 3 L TENSOR
REMARK 3 L11: 0.3633 L22: 0.2060
REMARK 3 L33: 0.8020 L12: 0.3407
REMARK 3 L13: -0.1501 L23: 0.0993
REMARK 3 S TENSOR
REMARK 3 S11: 0.1023 S12: -0.2372 S13: 0.0670
REMARK 3 S21: -0.0608 S22: -0.0259 S23: 0.0998
REMARK 3 S31: -0.0256 S32: 0.0309 S33: 0.0000
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 4B81 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-53843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-11
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 : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.039
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 : 49067
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 29.30
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.0
REMARK 200 R MERGE FOR SHELL (I) : 0.52
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.80
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 (%): 41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
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 38.97950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.96300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.93800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.96300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.97950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.93800
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: 6640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.5 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 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
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 GLY B 263
REMARK 465 GLY B 264
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 470 ARG B 493 CG CD NE CZ NH1 NH2
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 OG1 THR A 238 O HOH A 2050 2.19
REMARK 500 SG CYS B 69 CB CYS B 96 1.74
REMARK 500 OD1 ASP B 95 OH TYR B 98 2.14
REMARK 500 ND2 ASN B 350 C2 NAG B 1549 1.95
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 -4.50 70.75
REMARK 500 ALA A 167 72.90 -160.43
REMARK 500 SER A 196 53.40 -140.42
REMARK 500 SER A 203 -119.23 55.59
REMARK 500 ASP A 306 -79.68 -143.94
REMARK 500 ASP A 310 -158.90 -137.94
REMARK 500 ASP A 323 58.98 -107.29
REMARK 500 VAL A 407 -65.11 -123.39
REMARK 500 ALA B 62 56.64 -111.44
REMARK 500 ARG B 90 -165.63 -117.95
REMARK 500 LEU B 97 73.85 -68.34
REMARK 500 PHE B 123 19.16 57.34
REMARK 500 ASP B 134 105.16 -56.70
REMARK 500 PHE B 158 -1.14 -140.74
REMARK 500 ALA B 167 64.47 -155.65
REMARK 500 SER B 203 -115.06 53.81
REMARK 500 ASP B 266 -71.56 -57.35
REMARK 500 VAL B 303 98.52 -68.10
REMARK 500 ASP B 306 -85.08 -113.41
REMARK 500 ASP B 333 78.05 -108.98
REMARK 500 ASN B 350 -128.95 -104.68
REMARK 500 SER B 355 -155.57 -73.31
REMARK 500 VAL B 407 -69.04 -123.80
REMARK 500 PRO B 492 32.47 -76.25
REMARK 500 LYS B 496 -28.13 65.30
REMARK 500 PRO B 498 -150.35 -91.16
REMARK 500 ALA B 506 -80.78 -69.26
REMARK 500 ALA B 542 -114.15 -85.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER B 497 24.9 L L OUTSIDE RANGE
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 P6G B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN4 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN4 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1544 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1546 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1549 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: 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: 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 4B81 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4B81 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4B81 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4B81 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4B81 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B81 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B81 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B81 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4B81 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4B81 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B81 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B81 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 P6G B1546 19
HET ZN4 A 600 19
HET SO4 A1543 5
HET NAG A1544 14
HET PEG A1545 7
HET NAG A1546 14
HET PEG A1547 7
HET PEG A1548 7
HET ZN4 B 600 19
HET PEG B1544 7
HET SO4 B1545 5
HET PEG B1547 7
HET PEG B1548 7
HET NAG B1549 14
HET PEG B1550 7
HET PEG B1551 7
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 P6G C12 H26 O7
FORMUL 4 ZN4
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 NAG 3(C8 H15 N O6)
FORMUL 7 PEG 8(C4 H10 O3)
FORMUL 8 HOH *180(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 GLU A 142 1 8
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 LEU A 221 5 6
HELIX 10 10 SER A 240 GLY A 256 1 17
HELIX 11 11 ASN A 265 ARG A 274 1 10
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 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 SER A 541 1 17
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 LEU B 130 ASP B 134 5 5
HELIX 29 29 GLY B 135 GLY B 143 1 9
HELIX 30 30 VAL B 153 LEU B 159 1 7
HELIX 31 31 ASN B 170 ILE B 187 1 18
HELIX 32 32 ALA B 188 PHE B 190 5 3
HELIX 33 33 SER B 203 SER B 215 1 13
HELIX 34 34 LEU B 216 LEU B 221 5 6
HELIX 35 35 SER B 240 GLY B 256 1 17
HELIX 36 36 ASP B 266 THR B 275 1 10
HELIX 37 37 PRO B 277 ASP B 283 1 7
HELIX 38 38 HIS B 284 LEU B 289 5 6
HELIX 39 39 THR B 311 ASN B 317 1 7
HELIX 40 40 GLY B 335 VAL B 340 5 6
HELIX 41 41 ARG B 356 VAL B 367 1 12
HELIX 42 42 SER B 371 THR B 383 1 13
HELIX 43 43 ASP B 390 VAL B 407 1 18
HELIX 44 44 VAL B 407 GLN B 421 1 15
HELIX 45 45 PRO B 440 GLY B 444 5 5
HELIX 46 46 GLU B 450 GLY B 456 1 7
HELIX 47 47 LEU B 457 ASN B 464 5 8
HELIX 48 48 THR B 466 GLY B 487 1 22
HELIX 49 49 ARG B 525 ARG B 534 1 10
HELIX 50 50 ARG B 534 ALA B 542 1 9
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 VAL A 520 ARG A 522 -1 O ARG A 521 N TYR A 510
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 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
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 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A1544 1555 1555 1.44
LINK ND2 ASN A 464 C1 NAG A1546 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B1549 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -0.41
CISPEP 2 TYR B 105 PRO B 106 0 2.74
CISPEP 3 SER B 497 PRO B 498 0 6.94
SITE 1 AC1 10 HIS A 381 GLN A 527 PHE A 535 HOH A2080
SITE 2 AC1 10 HOH A2099 LEU B 380 HIS B 381 GLN B 527
SITE 3 AC1 10 PHE B 535 PEG B1547
SITE 1 AC2 11 TRP A 86 GLY A 121 TYR A 124 GLU A 202
SITE 2 AC2 11 TRP A 286 TYR A 337 PHE A 338 TYR A 341
SITE 3 AC2 11 HIS A 447 HOH A2022 HOH A2033
SITE 1 AC3 5 LYS A 23 PRO A 25 ARG A 136 PHE A 137
SITE 2 AC3 5 ASP A 460
SITE 1 AC4 4 ASP A 304 GLY A 305 SER A 309 ASP A 310
SITE 1 AC5 3 HIS A 381 TYR A 382 ASP A 384
SITE 1 AC6 3 GLY A 234 PRO A 235 GLU A 313
SITE 1 AC7 8 TRP B 86 GLY B 121 TYR B 124 TYR B 337
SITE 2 AC7 8 PHE B 338 TYR B 341 HIS B 447 HOH B2047
SITE 1 AC8 4 LYS B 332 ASP B 333 ASP B 396 TRP B 442
SITE 1 AC9 4 LYS B 23 ARG B 136 PHE B 137 ASP B 460
SITE 1 BC1 4 GLN A 527 HIS B 381 ASP B 384 P6G B1546
SITE 1 BC2 1 ASP B 304
SITE 1 BC3 2 ARG B 11 ALA B 188
SITE 1 BC4 2 GLY B 234 PRO B 235
SITE 1 BC5 4 SER A 347 ASN A 350 HOH A2074 HOH A2100
SITE 1 BC6 2 SER A 462 ASN A 464
SITE 1 BC7 4 SER B 347 ASN B 350 HOH B2054 HOH B2076
CRYST1 77.959 109.876 227.926 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 0.012827 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004387 0.00000
TER 4178 ALA A 542
TER 8338 THR B 543
MASTER 800 0 16 50 32 0 22 6 8681 2 180 86
END |