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HEADER HYDROLASE 24-AUG-12 4B85
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-CHLORANYL-
TITLE 2 N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE
CAVEAT 4B85 NAG A1546 WRONG CHIRALITY AT 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 4B85 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. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.189
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.82
REMARK 3 NUMBER OF REFLECTIONS : 119303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1773
REMARK 3 R VALUE (WORKING SET) : 0.1767
REMARK 3 FREE R VALUE : 0.2059
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2414
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 29.1917 - 5.3890 0.97 7085 141 0.1832 0.1909
REMARK 3 2 5.3890 - 4.2818 1.00 7041 137 0.1324 0.1523
REMARK 3 3 4.2818 - 3.7418 1.00 6945 140 0.1440 0.1498
REMARK 3 4 3.7418 - 3.4002 1.00 6954 141 0.1748 0.2078
REMARK 3 5 3.4002 - 3.1568 1.00 6894 131 0.1867 0.2039
REMARK 3 6 3.1568 - 2.9709 1.00 6881 150 0.1846 0.2201
REMARK 3 7 2.9709 - 2.8222 1.00 6857 135 0.1839 0.2421
REMARK 3 8 2.8222 - 2.6995 1.00 6874 141 0.1787 0.2335
REMARK 3 9 2.6995 - 2.5956 1.00 6851 146 0.1851 0.2179
REMARK 3 10 2.5956 - 2.5061 1.00 6819 156 0.1896 0.2468
REMARK 3 11 2.5061 - 2.4278 1.00 6869 107 0.1951 0.2547
REMARK 3 12 2.4278 - 2.3584 1.00 6832 137 0.2039 0.2483
REMARK 3 13 2.3584 - 2.2964 1.00 6817 148 0.2118 0.2410
REMARK 3 14 2.2964 - 2.2403 1.00 6832 147 0.2106 0.2533
REMARK 3 15 2.2403 - 2.1894 1.00 6771 157 0.2272 0.2847
REMARK 3 16 2.1894 - 2.1429 1.00 6800 149 0.2421 0.2838
REMARK 3 17 2.1429 - 2.1000 1.00 6767 151 0.2581 0.2753
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.340
REMARK 3 B_SOL : 53.925
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.29
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.3120
REMARK 3 B22 (A**2) : 1.8853
REMARK 3 B33 (A**2) : -2.1973
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 8850
REMARK 3 ANGLE : 1.119 12081
REMARK 3 CHIRALITY : 0.082 1293
REMARK 3 PLANARITY : 0.005 1577
REMARK 3 DIHEDRAL : 15.865 3266
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3796 11.2474 23.6276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1426 T22: 0.1024
REMARK 3 T33: 0.1667 T12: 0.0209
REMARK 3 T13: 0.0015 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.6366 L22: 0.3873
REMARK 3 L33: 1.5299 L12: -0.0602
REMARK 3 L13: -0.1965 L23: -0.2450
REMARK 3 S TENSOR
REMARK 3 S11: -0.0564 S12: -0.0543 S13: -0.0418
REMARK 3 S21: 0.0322 S22: -0.0032 S23: -0.0415
REMARK 3 S31: 0.1119 S32: 0.0823 S33: -0.0004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8385 17.6451 6.7079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2542 T22: 0.2418
REMARK 3 T33: 0.2621 T12: 0.0088
REMARK 3 T13: -0.0142 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.3751 L22: -0.1741
REMARK 3 L33: 1.2898 L12: -0.1368
REMARK 3 L13: 0.5603 L23: -0.3682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: 0.0558 S13: -0.0324
REMARK 3 S21: -0.0709 S22: -0.0196 S23: 0.0710
REMARK 3 S31: -0.0867 S32: -0.2515 S33: -0.0008
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3743 1.2027 14.1137
REMARK 3 T TENSOR
REMARK 3 T11: 0.3256 T22: 0.5579
REMARK 3 T33: 0.4312 T12: -0.2036
REMARK 3 T13: 0.0066 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.1723 L22: 0.5750
REMARK 3 L33: 0.1483 L12: -0.2545
REMARK 3 L13: -0.0411 L23: -0.0720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: 0.0205 S13: -0.3059
REMARK 3 S21: -0.1614 S22: -0.0076 S23: 0.6150
REMARK 3 S31: 0.3885 S32: -1.0297 S33: 0.0266
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3381 6.3857 -0.5931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2755 T22: 0.4088
REMARK 3 T33: 0.2894 T12: -0.0302
REMARK 3 T13: -0.0676 T23: -0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 0.1085 L22: 0.4726
REMARK 3 L33: 0.2702 L12: -0.2138
REMARK 3 L13: 0.2150 L23: -0.2876
REMARK 3 S TENSOR
REMARK 3 S11: 0.0919 S12: -0.1045 S13: -0.0118
REMARK 3 S21: -0.2820 S22: -0.1316 S23: 0.1741
REMARK 3 S31: 0.0873 S32: -0.1440 S33: -0.0117
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0868 5.7336 -61.1897
REMARK 3 T TENSOR
REMARK 3 T11: 0.2861 T22: 0.4707
REMARK 3 T33: 0.3184 T12: 0.0783
REMARK 3 T13: -0.0919 T23: -0.1465
REMARK 3 L TENSOR
REMARK 3 L11: 0.1036 L22: 0.4884
REMARK 3 L33: 0.2357 L12: -0.0664
REMARK 3 L13: 0.0885 L23: 0.0645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0805 S12: 0.4036 S13: -0.1227
REMARK 3 S21: -0.3939 S22: -0.1688 S23: 0.1584
REMARK 3 S31: 0.0030 S32: -0.1780 S33: -0.0460
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4322 0.1139 -52.7859
REMARK 3 T TENSOR
REMARK 3 T11: 0.2798 T22: 0.3217
REMARK 3 T33: 0.2860 T12: 0.0033
REMARK 3 T13: -0.0625 T23: -0.1134
REMARK 3 L TENSOR
REMARK 3 L11: 0.2021 L22: 0.3677
REMARK 3 L33: 1.1118 L12: 0.1282
REMARK 3 L13: 0.0535 L23: 0.5284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0990 S12: 0.2580 S13: -0.1423
REMARK 3 S21: -0.0507 S22: -0.1918 S23: 0.1211
REMARK 3 S31: 0.2513 S32: -0.2028 S33: -0.0161
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 119:275)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5299 5.4773 -48.3994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2180 T22: 0.2793
REMARK 3 T33: 0.2472 T12: 0.0081
REMARK 3 T13: -0.0288 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 0.4581 L22: 0.5597
REMARK 3 L33: 1.5236 L12: -0.4843
REMARK 3 L13: 0.3021 L23: 0.7153
REMARK 3 S TENSOR
REMARK 3 S11: 0.1024 S12: 0.1021 S13: -0.0053
REMARK 3 S21: -0.0247 S22: -0.0098 S23: 0.0539
REMARK 3 S31: 0.0300 S32: 0.1471 S33: 0.0562
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 276:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7049 2.6990 -38.5321
REMARK 3 T TENSOR
REMARK 3 T11: 0.3109 T22: 0.1577
REMARK 3 T33: 0.2139 T12: 0.0187
REMARK 3 T13: -0.0904 T23: -0.1002
REMARK 3 L TENSOR
REMARK 3 L11: 0.9223 L22: 0.3591
REMARK 3 L33: 1.0010 L12: -0.0945
REMARK 3 L13: 0.4049 L23: 0.3069
REMARK 3 S TENSOR
REMARK 3 S11: 0.2239 S12: 0.3140 S13: 0.1684
REMARK 3 S21: 0.1195 S22: 0.0240 S23: 0.1344
REMARK 3 S31: 0.3457 S32: 0.3317 S33: 0.1666
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 342:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1684 -4.9116 -17.7905
REMARK 3 T TENSOR
REMARK 3 T11: 0.5368 T22: 0.2589
REMARK 3 T33: 0.2750 T12: -0.0351
REMARK 3 T13: -0.0970 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 0.3297 L22: 0.1204
REMARK 3 L33: 0.1162 L12: 0.1693
REMARK 3 L13: 0.0366 L23: -0.0357
REMARK 3 S TENSOR
REMARK 3 S11: 0.2003 S12: -0.1294 S13: -0.0485
REMARK 3 S21: 0.1015 S22: -0.0952 S23: 0.0067
REMARK 3 S31: 0.5756 S32: 0.0384 S33: -0.0007
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 407:486)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5944 8.5664 -32.8495
REMARK 3 T TENSOR
REMARK 3 T11: 0.2206 T22: 0.2881
REMARK 3 T33: 0.2955 T12: -0.0528
REMARK 3 T13: 0.0019 T23: -0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 0.2156 L22: 0.4202
REMARK 3 L33: 0.8929 L12: -0.3011
REMARK 3 L13: -0.0725 L23: 0.3934
REMARK 3 S TENSOR
REMARK 3 S11: 0.1259 S12: -0.0495 S13: 0.0313
REMARK 3 S21: 0.1690 S22: -0.1707 S23: 0.0955
REMARK 3 S31: -0.0273 S32: -0.2341 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0614 22.6409 -28.6634
REMARK 3 T TENSOR
REMARK 3 T11: 0.3181 T22: 0.2929
REMARK 3 T33: 0.3592 T12: 0.0018
REMARK 3 T13: 0.0059 T23: -0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 0.0552 L22: 0.1940
REMARK 3 L33: 0.2323 L12: -0.0530
REMARK 3 L13: -0.1173 L23: 0.0864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: -0.1549 S13: 0.1490
REMARK 3 S21: 0.0878 S22: -0.0177 S23: 0.1955
REMARK 3 S31: -0.2083 S32: -0.0610 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1768 11.7080 -21.3546
REMARK 3 T TENSOR
REMARK 3 T11: 0.3673 T22: 0.3584
REMARK 3 T33: 0.2884 T12: -0.0266
REMARK 3 T13: 0.0021 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 0.0376 L22: 0.0318
REMARK 3 L33: 0.2761 L12: -0.0979
REMARK 3 L13: 0.0580 L23: -0.0448
REMARK 3 S TENSOR
REMARK 3 S11: 0.0872 S12: 0.0975 S13: 0.1005
REMARK 3 S21: 0.2380 S22: -0.0940 S23: 0.1422
REMARK 3 S31: -0.0210 S32: 0.0568 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 4B85 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-53847.
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 : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : 119406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 29.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.8
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.8
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.50
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 (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
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 39.76350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.24800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.44600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.24800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.76350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.44600
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: 5140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.5 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 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 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 165 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 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 NH1A ARG A 433 O HOH A 2337 2.20
REMARK 500 ND2 ASN B 350 C2 NAG B 1547 2.11
REMARK 500 O HOH A 2093 O HOH A 2264 2.18
REMARK 500 O HOH B 2069 O HOH B 2160 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU A 91 NH2 ARG B 424 4555 2.20
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 -6.17 75.18
REMARK 500 ALA A 62 50.70 -115.77
REMARK 500 TYR A 77 70.02 53.08
REMARK 500 ALA A 167 73.95 -152.26
REMARK 500 SER A 203 -119.96 60.70
REMARK 500 CYS A 257 70.08 -118.45
REMARK 500 ASP A 306 -84.24 -121.32
REMARK 500 VAL A 343 101.19 113.73
REMARK 500 VAL A 407 -61.30 -130.24
REMARK 500 ASP A 494 15.90 -160.52
REMARK 500 SER A 495 5.03 -58.79
REMARK 500 PHE B 47 -2.62 75.33
REMARK 500 ALA B 62 52.21 -116.63
REMARK 500 SER B 203 -122.90 54.32
REMARK 500 ASP B 306 -87.15 -119.75
REMARK 500 VAL B 407 -62.00 -127.21
REMARK 500 ARG B 493 -6.27 -144.60
REMARK 500 SER B 495 -143.34 28.93
REMARK 500 LYS B 496 108.13 62.20
REMARK 500 ALA B 542 42.63 -100.98
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 PEG A 1547
REMARK 610 PEG A 1548
REMARK 610 PEG B 1546
REMARK 610 P6G B 1550
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B3W A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1544
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 B3W B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
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 B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
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: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1547 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 (1 MTH)
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (1 WK)
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (10 MTH)
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 WK)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 MTH)
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (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: 4B84 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE
DBREF 4B85 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4B85 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4B85 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4B85 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4B85 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B85 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B85 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B85 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4B85 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4B85 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B85 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B85 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
MODRES 4B85 ASN A 464 ASN GLYCOSYLATION SITE
MODRES 4B85 ASN B 350 ASN GLYCOSYLATION SITE
HET B3W A 600 36
HET SO4 A1543 5
HET PEG A1544 7
HET PEG A1545 7
HET NAG A1546 14
HET PEG A1547 4
HET PEG A1548 4
HET B3W B 600 18
HET SO4 B1544 5
HET PEG B1545 7
HET PEG B1546 4
HET NAG B1547 14
HET PEG B1548 7
HET PEG B1549 7
HET P6G B1550 16
HETNAM B3W 4-CHLORANYL-N-[2-(DIETHYLAMINO)ETHYL]
HETNAM 2 B3W BENZENESULFONAMIDE
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 B3W 2(C12 H19 CL N2 O2 S)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 PEG 8(C4 H10 O3)
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 P6G C12 H26 O7
FORMUL 8 HOH *663(H2 O)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLY A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 SER A 215 1 13
HELIX 10 10 LEU A 216 PHE A 222 5 7
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 ARG A 276 1 12
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 VAL A 288 5 3
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 LEU A 339 5 5
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 ASP A 460 ASN A 464 5 5
HELIX 25 25 THR A 466 GLY A 487 1 22
HELIX 26 26 ARG A 525 ARG A 534 1 10
HELIX 27 27 ARG A 534 SER A 541 1 8
HELIX 28 28 ASP B 5 GLN B 7 5 3
HELIX 29 29 VAL B 42 ARG B 46 5 5
HELIX 30 30 PHE B 80 MET B 85 1 6
HELIX 31 31 LEU B 130 ASP B 134 5 5
HELIX 32 32 GLY B 135 GLU B 142 1 8
HELIX 33 33 VAL B 153 LEU B 159 1 7
HELIX 34 34 ASN B 170 ILE B 187 1 18
HELIX 35 35 ALA B 188 PHE B 190 5 3
HELIX 36 36 SER B 203 SER B 215 1 13
HELIX 37 37 LEU B 216 PHE B 222 5 7
HELIX 38 38 SER B 240 VAL B 255 1 16
HELIX 39 39 ASN B 265 ARG B 276 1 12
HELIX 40 40 PRO B 277 GLU B 285 1 9
HELIX 41 41 TRP B 286 VAL B 288 5 3
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 GLY B 342 5 8
HELIX 44 44 SER B 355 VAL B 367 1 13
HELIX 45 45 SER B 371 THR B 383 1 13
HELIX 46 46 ASP B 390 VAL B 407 1 18
HELIX 47 47 VAL B 407 GLN B 421 1 15
HELIX 48 48 PRO B 440 GLY B 444 5 5
HELIX 49 49 GLU B 450 PHE B 455 1 6
HELIX 50 50 GLY B 456 ASP B 460 5 5
HELIX 51 51 ASP B 460 ASN B 464 5 5
HELIX 52 52 THR B 466 GLY B 487 1 22
HELIX 53 53 ARG B 525 ARG B 534 1 10
HELIX 54 54 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 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 2.07
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.07
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 A1546 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG B1547 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -3.66
CISPEP 2 TYR B 105 PRO B 106 0 4.21
CISPEP 3 SER B 497 PRO B 498 0 16.62
SITE 1 AC1 14 TRP A 86 GLY A 120 GLY A 121 GLY A 122
SITE 2 AC1 14 TYR A 124 GLU A 202 PHE A 295 PHE A 297
SITE 3 AC1 14 TYR A 337 PHE A 338 TYR A 341 HIS A 447
SITE 4 AC1 14 HOH A2137 HOH A2140
SITE 1 AC2 4 LYS A 23 ALA A 24 ARG A 136 ASP A 460
SITE 1 AC3 3 HIS A 381 HIS A 393 HOH A2304
SITE 1 AC4 2 GLY A 305 SER A 309
SITE 1 AC5 1 THR B 275
SITE 1 AC6 3 SER A 57 VAL A 59 HOH A2380
SITE 1 AC7 10 TRP B 86 GLY B 121 GLY B 122 TYR B 124
SITE 2 AC7 10 PHE B 297 TYR B 337 PHE B 338 TYR B 341
SITE 3 AC7 10 HIS B 447 HOH B2095
SITE 1 AC8 5 LYS B 23 ALA B 24 PRO B 25 ARG B 136
SITE 2 AC8 5 ASP B 460
SITE 1 AC9 1 HIS B 381
SITE 1 BC1 5 THR B 112 PRO B 113 GLU B 142 GLY B 143
SITE 2 BC1 5 ARG B 485
SITE 1 BC2 3 ARG B 11 VAL B 12 GLU B 185
SITE 1 BC3 4 ASP B 304 GLY B 305 SER B 309 HOH B2273
SITE 1 BC4 10 LEU A 380 HIS A 381 GLN A 527 PHE A 531
SITE 2 BC4 10 PHE A 535 HOH A2303 LEU B 380 HIS B 381
SITE 3 BC4 10 PHE B 531 PHE B 535
SITE 1 BC5 2 SER A 462 ASN A 464
SITE 1 BC6 2 SER B 347 ASN B 350
CRYST1 79.527 112.892 226.496 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 0.012574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004415 0.00000
TER 4266 ALA A 542
TER 8435 THR B 543
MASTER 744 0 15 54 32 0 24 6 9251 2 169 86
END |