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HEADER HYDROLASE 24-AUG-12 4B7Z
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-DIETHYLAMINO-
TITLE 2 ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,W.QIAN,
AUTHOR 2 F.EKSTROM,A.LINUSSON
REVDAT 1 04-SEP-13 4B7Z 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.797
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.90
REMARK 3 NUMBER OF REFLECTIONS : 90244
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1717
REMARK 3 R VALUE (WORKING SET) : 0.1711
REMARK 3 FREE R VALUE : 0.2006
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1784
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.7990 - 5.3971 0.99 7113 139 0.1834 0.1890
REMARK 3 2 5.3971 - 4.2884 1.00 6923 134 0.1379 0.1567
REMARK 3 3 4.2884 - 3.7476 1.00 6862 135 0.1401 0.1818
REMARK 3 4 3.7476 - 3.4056 1.00 6813 147 0.1579 0.2123
REMARK 3 5 3.4056 - 3.1618 1.00 6811 120 0.1714 0.1913
REMARK 3 6 3.1618 - 2.9756 1.00 6761 150 0.1691 0.1834
REMARK 3 7 2.9756 - 2.8267 1.00 6765 138 0.1761 0.2097
REMARK 3 8 2.8267 - 2.7038 1.00 6778 135 0.1974 0.2218
REMARK 3 9 2.7038 - 2.5997 1.00 6706 149 0.2172 0.2871
REMARK 3 10 2.5997 - 2.5101 1.00 6744 145 0.2172 0.2796
REMARK 3 11 2.5101 - 2.4316 1.00 6724 118 0.2183 0.2156
REMARK 3 12 2.4316 - 2.3622 1.00 6716 130 0.2276 0.2786
REMARK 3 13 2.3622 - 2.3000 1.00 6744 144 0.2296 0.2554
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.351
REMARK 3 B_SOL : 62.030
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.29
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.3320
REMARK 3 B22 (A**2) : 3.0582
REMARK 3 B33 (A**2) : -1.7261
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 8784
REMARK 3 ANGLE : 1.086 11948
REMARK 3 CHIRALITY : 0.077 1277
REMARK 3 PLANARITY : 0.005 1553
REMARK 3 DIHEDRAL : 17.868 3214
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7953 11.5420 29.3660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.1802
REMARK 3 T33: 0.2103 T12: -0.0062
REMARK 3 T13: -0.0112 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.5765 L22: 1.0172
REMARK 3 L33: 2.7638 L12: -0.0988
REMARK 3 L13: -0.1303 L23: -0.2103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0227 S12: -0.1189 S13: -0.0107
REMARK 3 S21: 0.1219 S22: 0.0154 S23: -0.0387
REMARK 3 S31: 0.1399 S32: 0.0828 S33: 0.0134
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 229:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9413 9.8054 10.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.2603 T22: 0.2375
REMARK 3 T33: 0.2451 T12: 0.0589
REMARK 3 T13: 0.0376 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 3.5045 L22: 1.0650
REMARK 3 L33: 2.3764 L12: 0.8468
REMARK 3 L13: 0.2906 L23: -0.3523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0619 S12: 0.1696 S13: -0.2285
REMARK 3 S21: -0.0796 S22: -0.0287 S23: -0.2235
REMARK 3 S31: 0.3030 S32: 0.3927 S33: 0.0745
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3198 17.6387 6.6510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1499 T22: 0.2283
REMARK 3 T33: 0.2458 T12: -0.0274
REMARK 3 T13: -0.0261 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.1271 L22: 1.2134
REMARK 3 L33: 3.1770 L12: 0.0642
REMARK 3 L13: 0.1004 L23: -0.4578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: 0.0774 S13: 0.0006
REMARK 3 S21: -0.0926 S22: 0.0274 S23: 0.1607
REMARK 3 S31: 0.0393 S32: -0.3399 S33: -0.0067
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3052 1.6734 14.7315
REMARK 3 T TENSOR
REMARK 3 T11: 0.3242 T22: 0.5971
REMARK 3 T33: 0.4400 T12: -0.2027
REMARK 3 T13: -0.0207 T23: 0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 5.3860 L22: 8.4780
REMARK 3 L33: 3.0491 L12: 0.0188
REMARK 3 L13: 1.3876 L23: -3.0132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.1832 S13: -0.3506
REMARK 3 S21: 0.4039 S22: 0.1323 S23: 0.8798
REMARK 3 S31: 0.5221 S32: -1.3913 S33: -0.0476
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0961 6.6215 -0.7443
REMARK 3 T TENSOR
REMARK 3 T11: 0.2341 T22: 0.2995
REMARK 3 T33: 0.2214 T12: -0.0897
REMARK 3 T13: -0.1003 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 2.5603 L22: 2.2088
REMARK 3 L33: 4.9592 L12: -0.9867
REMARK 3 L13: -2.1768 L23: 0.9395
REMARK 3 S TENSOR
REMARK 3 S11: 0.0192 S12: 0.1009 S13: -0.1719
REMARK 3 S21: -0.1237 S22: -0.1484 S23: 0.2718
REMARK 3 S31: 0.5139 S32: -0.2847 S33: 0.0900
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8034 5.9812 -61.6916
REMARK 3 T TENSOR
REMARK 3 T11: 0.2667 T22: 0.2695
REMARK 3 T33: 0.2672 T12: 0.0416
REMARK 3 T13: -0.1173 T23: -0.1077
REMARK 3 L TENSOR
REMARK 3 L11: 4.5521 L22: 2.5365
REMARK 3 L33: 4.6284 L12: -0.9053
REMARK 3 L13: -0.9867 L23: 0.3309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0424 S12: 0.5762 S13: 0.1250
REMARK 3 S21: -0.4695 S22: -0.1078 S23: 0.4213
REMARK 3 S31: -0.2929 S32: -0.6604 S33: -0.0057
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2447 1.1306 -51.2632
REMARK 3 T TENSOR
REMARK 3 T11: 0.2852 T22: 0.3123
REMARK 3 T33: 0.3072 T12: -0.0282
REMARK 3 T13: -0.0607 T23: -0.0927
REMARK 3 L TENSOR
REMARK 3 L11: 0.9556 L22: 1.0202
REMARK 3 L33: 2.4713 L12: -0.0017
REMARK 3 L13: -0.1277 L23: 0.5180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0822 S12: 0.1910 S13: -0.1725
REMARK 3 S21: -0.1562 S22: -0.0473 S23: 0.1773
REMARK 3 S31: 0.2938 S32: -0.2141 S33: -0.0378
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 159:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0992 5.3621 -45.8510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.2740
REMARK 3 T33: 0.2236 T12: -0.0199
REMARK 3 T13: -0.0271 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 1.4414 L22: 2.2228
REMARK 3 L33: 2.4788 L12: -0.6325
REMARK 3 L13: 0.0151 L23: 0.7504
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: 0.1870 S13: 0.0274
REMARK 3 S21: -0.0072 S22: 0.0217 S23: -0.2365
REMARK 3 S31: 0.0896 S32: 0.4016 S33: -0.0966
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3296 2.1532 -26.6972
REMARK 3 T TENSOR
REMARK 3 T11: 0.3665 T22: 0.2459
REMARK 3 T33: 0.3083 T12: -0.0502
REMARK 3 T13: 0.0124 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 1.4315 L22: 1.6101
REMARK 3 L33: 2.7191 L12: -0.1963
REMARK 3 L13: 0.6532 L23: -0.0928
REMARK 3 S TENSOR
REMARK 3 S11: 0.1605 S12: -0.1360 S13: -0.1579
REMARK 3 S21: 0.2645 S22: -0.0904 S23: 0.1347
REMARK 3 S31: 0.4062 S32: -0.1922 S33: -0.0883
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7116 22.3636 -28.5929
REMARK 3 T TENSOR
REMARK 3 T11: 0.3582 T22: 0.2444
REMARK 3 T33: 0.4185 T12: 0.0370
REMARK 3 T13: 0.0485 T23: -0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 4.8504 L22: 4.9483
REMARK 3 L33: 9.3840 L12: 0.9271
REMARK 3 L13: 1.3401 L23: -1.5298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: -0.2883 S13: 0.7693
REMARK 3 S21: 0.2373 S22: 0.1267 S23: 0.7816
REMARK 3 S31: -0.7455 S32: -0.5105 S33: -0.0754
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7370 11.3756 -21.3522
REMARK 3 T TENSOR
REMARK 3 T11: 0.3801 T22: 0.2832
REMARK 3 T33: 0.1813 T12: -0.0398
REMARK 3 T13: 0.0251 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 7.0129 L22: 2.0649
REMARK 3 L33: 3.9296 L12: 0.0059
REMARK 3 L13: 4.4969 L23: -0.1946
REMARK 3 S TENSOR
REMARK 3 S11: 0.2323 S12: 0.2270 S13: -0.1809
REMARK 3 S21: 0.2045 S22: -0.1174 S23: -0.0032
REMARK 3 S31: 0.0889 S32: 0.3944 S33: -0.0858
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DUE TO INSUFFICIENT ELECTRON DENSITY
REMARK 3 THE FOLLOWING RESIDUES WERE NOT MODELED: CHAIN A 258-264 AND
REMARK 3 543-548, CHAIN B 1-3, 258-264 AND 544-548. DUE TO INSUFFICIENT
REMARK 3 ELECTRON DENSITY THE FOLLOWING RESIDUES WERE MODELED AS ALANINES,
REMARK 3 CHAIN A 496 AND CHAIN B 493.
REMARK 4
REMARK 4 4B7Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-SEP-12.
REMARK 100 THE PDBE ID CODE IS EBI-53834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-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 : 90383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 29.12
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.9
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.8
REMARK 200 R MERGE FOR SHELL (I) : 0.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-30% (V/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 39.65350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.36900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.91650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.36900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.65350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.91650
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: 6470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 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 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 470 ALA B 544 CA C O CB
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 NH1 ARG A 45 OE1 GLU A 51 2.12
REMARK 500 OG SER A 203 O HOH A 2151 2.08
REMARK 500 O CYS B 257 O HOH B 2193 2.10
REMARK 500 O HOH A 2042 O HOH A 2128 2.17
REMARK 500 O HOH A 2098 O HOH A 2099 2.10
REMARK 500 O HOH A 2099 O HOH A 2140 2.09
REMARK 500 O HOH A 2115 O HOH A 2236 2.12
REMARK 500 O HOH B 2086 O HOH B 2179 2.19
REMARK 500 O HOH B 2284 O HOH B 2288 2.19
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 -2.46 72.86
REMARK 500 ALA A 62 50.90 -118.74
REMARK 500 SER A 203 -121.31 60.15
REMARK 500 ASP A 306 -87.85 -127.04
REMARK 500 VAL A 407 -61.19 -129.38
REMARK 500 ARG A 493 5.56 -69.42
REMARK 500 SER A 541 35.33 -82.79
REMARK 500 PHE B 47 -6.69 77.43
REMARK 500 PHE B 158 -1.73 -141.12
REMARK 500 ALA B 167 73.90 -154.39
REMARK 500 SER B 203 -120.13 58.92
REMARK 500 ASP B 306 -85.74 -125.31
REMARK 500 VAL B 407 -61.25 -126.72
REMARK 500 SER B 495 -177.42 -67.86
REMARK 500 LYS B 496 114.56 -24.90
REMARK 500 SER B 541 34.72 -74.26
REMARK 500 ALA B 542 4.05 -168.65
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 Q4Q A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G 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 A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Q4Q B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1546 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1548 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
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: 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
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 4B7Z A 1 545 UNP P21836 ACES_MOUSE 32 576
DBREF 4B7Z B 1 545 UNP P21836 ACES_MOUSE 32 576
SEQADV 4B7Z GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4B7Z ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4B7Z PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4B7Z GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4B7Z ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4B7Z 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 Q4Q A 600 19
HET PEG A1543 7
HET P6G A1544 19
HET PEG A1545 7
HET NAG A1546 14
HET PEG A1547 7
HET NAG A1548 14
HET PEG A1549 7
HET PEG A1550 7
HET PEG A1551 7
HET PEG A1552 7
HET PEG A1543 7
HET SO4 A1553 5
HET Q4Q B 600 19
HET PEG B1550 7
HET PEG B1544 7
HET PEG B1545 7
HET PEG B1546 7
HET PEG B1548 7
HET PEG B1550 7
HET PEG B1551 7
HET NAG B1547 14
HET SO4 B1549 5
HETNAM Q4Q N-[2-(DIETHYLAMINO)ETHYL]-1-(4-METHYLPHENYL)
HETNAM 2 Q4Q METHANESULFONAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 Q4Q 2(C14 H24 N2 O2 S)
FORMUL 4 PEG 13(C4 H10 O3)
FORMUL 6 P6G C12 H26 O7
FORMUL 7 NAG 3(C8 H15 N O6)
FORMUL 8 SO4 2(O4 S 2-)
FORMUL 9 HOH *748(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 SER A 215 SER A 220 1 6
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 ARG A 274 1 10
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
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 GLY B 143 1 9
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 SER B 215 SER B 220 1 6
HELIX 38 38 SER B 240 VAL B 255 1 16
HELIX 39 39 ASN B 265 THR B 275 1 11
HELIX 40 40 PRO B 277 ASP B 283 1 7
HELIX 41 41 HIS B 284 LEU B 289 5 6
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 VAL B 340 1 6
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 SER B 541 1 8
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 350 C1 NAG A1546 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A1548 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B1547 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -1.60
CISPEP 2 TYR B 105 PRO B 106 0 0.01
CISPEP 3 SER B 497 PRO B 498 0 -10.99
SITE 1 AC1 10 ASP A 74 TRP A 86 GLY A 120 GLY A 121
SITE 2 AC1 10 TYR A 124 GLU A 202 PHE A 297 PHE A 338
SITE 3 AC1 10 TYR A 341 HIS A 447
SITE 1 AC2 4 PRO A 113 GLU A 142 ARG A 485 HOH A2404
SITE 1 AC3 11 LEU A 380 GLN A 527 PHE A 531 PHE A 535
SITE 2 AC3 11 HOH A2327 HOH A2328 LEU B 380 HIS B 381
SITE 3 AC3 11 GLN B 527 PHE B 535 PEG B1546
SITE 1 AC4 3 ARG A 3 ASP A 5 HOH A2010
SITE 1 AC5 2 ASP A 304 GLY A 305
SITE 1 AC6 2 HOH A2329 HOH A2408
SITE 1 AC7 5 LEU A 289 SER A 293 HOH A2274 HOH A2409
SITE 2 AC7 5 HOH A2410
SITE 1 AC8 3 GLN A 413 ARG A 417 ARG A 534
SITE 1 AC9 3 GLY A 234 PRO A 235 HOH A2412
SITE 1 BC1 4 PRO A 113 GLU A 142 ARG A 485 HOH A2404
SITE 1 BC2 5 LYS A 23 PRO A 25 ARG A 136 PHE A 137
SITE 2 BC2 5 ASP A 460
SITE 1 BC3 8 TRP B 86 GLY B 121 TYR B 124 GLU B 202
SITE 2 BC3 8 TYR B 337 PHE B 338 TYR B 341 HIS B 447
SITE 1 BC4 3 VAL B 303 ASP B 304 SER B 309
SITE 1 BC5 2 LYS B 332 ASP B 333
SITE 1 BC6 4 THR B 112 GLU B 142 ALA B 144 ARG B 485
SITE 1 BC7 5 GLN A 527 P6G A1544 HIS B 381 TYR B 382
SITE 2 BC7 5 THR B 383
SITE 1 BC8 1 PRO B 235
SITE 1 BC9 3 VAL B 303 ASP B 304 SER B 309
SITE 1 CC1 2 ARG B 11 GLU B 185
SITE 1 CC2 7 LYS B 23 ALA B 24 PRO B 25 ARG B 136
SITE 2 CC2 7 PHE B 137 ASP B 460 HOH B2330
SITE 1 CC3 6 SER A 347 ASN A 350 HOH A2297 HOH A2314
SITE 2 CC3 6 HOH A2405 HOH A2406
SITE 1 CC4 2 SER A 462 ASN A 464
SITE 1 CC5 3 SER B 347 ASN B 350 HOH B2243
CRYST1 79.307 111.833 226.738 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 0.012609 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004410 0.00000
TER 4186 ALA A 542
TER 8346 ALA B 544
MASTER 752 0 23 54 32 0 33 6 9292 2 215 86
END |