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HEADER HYDROLASE 02-SEP-10 2XQG
TITLE X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC
TITLE 2 VR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 31-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 6 BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;
COMPND 7 EC: 3.1.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, NERVE AGENT, BIOSCAVENGER
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANDHAMMER,E.CARLETTI,E.GILLON,P.MASSON,M.GOELDNER,D.NOORT,F.NACHON
REVDAT 1 23-MAR-11 2XQG 0
JRNL AUTH M.WANDHAMMER,E.CARLETTI,M.VANDERSCHANS,E.GILLON,Y.NICOLET,
JRNL AUTH 2 P.MASSON,M.GOELDNER,D.NOORT,F.NACHON
JRNL TITL STRUCTURAL STUDY OF THE COMPLEX STEREOSELECTIVITY OF HUMAN
JRNL TITL 2 BUTYRYLCHOLINESTERASE FOR THE NEUROTOXIC V-AGENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.77
REMARK 3 NUMBER OF REFLECTIONS : 33383
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.16364
REMARK 3 R VALUE (WORKING SET) : 0.16207
REMARK 3 FREE R VALUE : 0.21461
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1036
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.300
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.360
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2390
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.217
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4258
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 185
REMARK 3 SOLVENT ATOMS : 419
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.092
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34
REMARK 3 B22 (A**2) : 0.34
REMARK 3 B33 (A**2) : -0.68
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.222
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.815
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4547 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6202 ; 2.051 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 543 ; 7.417 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 209 ;36.771 ;24.211
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;17.120 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.721 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 675 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3483 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2655 ; 1.084 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4295 ; 1.903 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1892 ; 3.385 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1899 ; 5.332 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 61
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8790 -26.6810 -46.6410
REMARK 3 T TENSOR
REMARK 3 T11: 0.3424 T22: 0.1814
REMARK 3 T33: 0.2916 T12: -0.0359
REMARK 3 T13: -0.1379 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 2.2656 L22: 2.2371
REMARK 3 L33: 2.1828 L12: -0.5723
REMARK 3 L13: -0.0972 L23: -0.0434
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: 0.5256 S13: 0.0879
REMARK 3 S21: -0.7579 S22: -0.0290 S23: 0.1270
REMARK 3 S31: -0.1510 S32: -0.1826 S33: 0.0411
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 62 A 254
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7770 -31.2650 -33.0530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0770 T22: 0.0426
REMARK 3 T33: 0.2866 T12: -0.0230
REMARK 3 T13: -0.0190 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 0.6671 L22: 1.1795
REMARK 3 L33: 1.6219 L12: 0.2319
REMARK 3 L13: 0.1273 L23: 0.1479
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: 0.1235 S13: -0.0813
REMARK 3 S21: -0.2502 S22: 0.0667 S23: -0.0391
REMARK 3 S31: 0.0173 S32: 0.0229 S33: -0.0294
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 255 A 333
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1060 -38.8480 -28.2380
REMARK 3 T TENSOR
REMARK 3 T11: 0.0817 T22: 0.0428
REMARK 3 T33: 0.3556 T12: 0.0099
REMARK 3 T13: 0.0025 T23: -0.0824
REMARK 3 L TENSOR
REMARK 3 L11: 1.3158 L22: 0.7034
REMARK 3 L33: 1.5878 L12: 0.2875
REMARK 3 L13: 0.0755 L23: -0.0779
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: 0.1235 S13: -0.2787
REMARK 3 S21: -0.0818 S22: 0.0890 S23: -0.2041
REMARK 3 S31: 0.2901 S32: 0.1545 S33: -0.0748
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 334 A 392
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1280 -47.2210 -3.6380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.0763
REMARK 3 T33: 0.3274 T12: -0.0436
REMARK 3 T13: -0.1219 T23: 0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 8.0806 L22: 1.7547
REMARK 3 L33: 3.5042 L12: 0.3596
REMARK 3 L13: 2.5191 L23: -0.2220
REMARK 3 S TENSOR
REMARK 3 S11: 0.2142 S12: -0.6152 S13: -0.5890
REMARK 3 S21: 0.2799 S22: 0.1123 S23: -0.0506
REMARK 3 S31: 0.3573 S32: -0.3485 S33: -0.3265
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 393 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2160 -25.2890 -16.8780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0291 T22: 0.0719
REMARK 3 T33: 0.2665 T12: 0.0030
REMARK 3 T13: -0.0206 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 1.0254 L22: 1.7873
REMARK 3 L33: 1.3453 L12: 0.5092
REMARK 3 L13: 0.2831 L23: -0.0058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: -0.0984 S13: 0.0578
REMARK 3 S21: -0.0088 S22: 0.0112 S23: 0.1902
REMARK 3 S31: -0.0457 S32: -0.2302 S33: -0.0189
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 486 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8020 -24.5350 -6.3990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0716
REMARK 3 T33: 0.2151 T12: -0.0137
REMARK 3 T13: -0.0207 T23: -0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 0.9116 L22: 5.2397
REMARK 3 L33: 2.3476 L12: -0.1143
REMARK 3 L13: 0.3527 L23: 0.4828
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: -0.0932 S13: 0.1994
REMARK 3 S21: 0.3759 S22: 0.0558 S23: -0.2856
REMARK 3 S31: -0.1512 S32: -0.1316 S33: 0.0043
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2XQG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-SEP-10.
REMARK 100 THE PDBE ID CODE IS EBI-45260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CDD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34420
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 41.50
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.3
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.30
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) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.4
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.1, M 2-(N
REMARK 280 -MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.0K .
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.30000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.80500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.30000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.80500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.30000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.80500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.30000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.80500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.30000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.80500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.30000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.80500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.30000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.80500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.30000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.30000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.80500
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 78560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 149640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -427.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NA NA A1555 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 45 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 483 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 509 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 514 TO GLN
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 UNK UNX A 1513 UNK UNX A 1514 1.64
REMARK 500 UNK UNX A 1520 UNK UNX A 1521 1.87
REMARK 500 N THR A 496 O HOH A 2379 1.90
REMARK 500 SG CYS A 66 O HOH A 2096 1.92
REMARK 500 UNK UNX A 1513 UNK UNX A 1515 1.96
REMARK 500 UNK UNX A 1516 UNK UNX A 1517 1.96
REMARK 500 O HOH A 2028 O HOH A 2096 2.02
REMARK 500 O TRP A 376 O HOH A 2289 2.04
REMARK 500 UNK UNX A 1517 UNK UNX A 1518 2.05
REMARK 500 UNK UNX A 1509 UNK UNX A 1510 2.11
REMARK 500 O SER A 495 O HOH A 2377 2.13
REMARK 500 OE1 GLU A 404 O HOH A 2313 2.15
REMARK 500 O HOH A 2080 O HOH A 2183 2.16
REMARK 500 O HOH A 2266 O HOH A 2331 2.17
REMARK 500 UNK UNX A 1508 UNK UNX A 1509 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 231 CE3 TRP A 231 CZ3 0.102
REMARK 500 GLN A 455 CD GLN A 455 NE2 0.899
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 LEU A 370 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLN A 455 OE1 - CD - NE2 ANGL. DEV. = 21.0 DEGREES
REMARK 500 GLN A 455 CG - CD - NE2 ANGL. DEV. = -25.6 DEGREES
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 43 -2.03 75.53
REMARK 500 LYS A 51 139.90 105.10
REMARK 500 ASP A 54 171.01 117.11
REMARK 500 ALA A 58 63.42 -101.53
REMARK 500 GLN A 67 149.75 -170.48
REMARK 500 CYS A 92 11.55 -141.08
REMARK 500 LYS A 103 119.28 -30.66
REMARK 500 ALA A 162 69.65 -162.10
REMARK 500 ASN A 165 16.52 58.44
REMARK 500 SER A 198 -123.70 60.07
REMARK 500 ASP A 297 -81.84 -135.44
REMARK 500 VAL A 377 25.58 89.09
REMARK 500 ASP A 378 -41.77 -140.05
REMARK 500 ASP A 379 146.37 -35.73
REMARK 500 GLN A 380 76.98 -106.26
REMARK 500 PHE A 398 -56.87 -126.06
REMARK 500 THR A 496 -78.27 92.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 377 ASP A 378 -31.52
REMARK 500 GLN A 380 ARG A 381 56.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLN A 455 0.08 SIDE CHAIN
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 VAL A 377 19.4 L L OUTSIDE RANGE
REMARK 500 ARG A 381 24.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1551 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2040 O
REMARK 620 2 HOH A2179 O 51.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1553 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 420 OH
REMARK 620 2 HOH A2393 O 73.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VR A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1566
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1567
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 241 RESIDUES 1563 TO 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 341 RESIDUES 1556 TO 1558
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA4
REMARK 900 RELATED ID: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 SULFATE
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 10MM HGCL2
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 VX
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO- FLUORIDATE (DFP)
REMARK 900 INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH THE SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE INCOMPLEX
REMARK 900 WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED )
REMARK 900 OBTAINED BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 FLUORIDE ANION
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA1
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 RACEMIC VX
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA5
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA1
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 RACEMIC CVX
DBREF 2XQG A 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQADV 2XQG GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XQG GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XQG GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XQG GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 527 ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY
SEQRES 2 A 527 MET GLN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE
SEQRES 3 A 527 LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU
SEQRES 4 A 527 ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP
SEQRES 5 A 527 ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN
SEQRES 6 A 527 ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU
SEQRES 7 A 527 MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU
SEQRES 8 A 527 TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN
SEQRES 9 A 527 ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN
SEQRES 10 A 527 THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE
SEQRES 11 A 527 LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN
SEQRES 12 A 527 TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY
SEQRES 13 A 527 ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN
SEQRES 14 A 527 GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA
SEQRES 15 A 527 PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU
SEQRES 16 A 527 SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER
SEQRES 17 A 527 PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN
SEQRES 18 A 527 SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU
SEQRES 19 A 527 TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU
SEQRES 20 A 527 THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS
SEQRES 21 A 527 CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN
SEQRES 22 A 527 GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL
SEQRES 23 A 527 ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP
SEQRES 24 A 527 MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS
SEQRES 25 A 527 THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR
SEQRES 26 A 527 ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP
SEQRES 27 A 527 ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY
SEQRES 28 A 527 LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS
SEQRES 29 A 527 GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP
SEQRES 30 A 527 GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL
SEQRES 31 A 527 VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE
SEQRES 32 A 527 THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE
SEQRES 33 A 527 TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO
SEQRES 34 A 527 GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE
SEQRES 35 A 527 VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN TYR THR
SEQRES 36 A 527 LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG
SEQRES 37 A 527 TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN GLU THR
SEQRES 38 A 527 GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS SER THR
SEQRES 39 A 527 GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG
SEQRES 40 A 527 ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP
SEQRES 41 A 527 THR SER PHE PHE PRO LYS VAL
HET UNX A1501 1
HET UNX A1502 1
HET UNX A1503 1
HET UNX A1504 1
HET UNX A1505 1
HET UNX A1506 1
HET UNX A1507 1
HET UNX A1508 1
HET UNX A1509 1
HET UNX A1510 1
HET UNX A1511 1
HET UNX A1512 1
HET UNX A1513 1
HET UNX A1514 1
HET UNX A1515 1
HET UNX A1516 1
HET UNX A1517 1
HET UNX A1518 1
HET UNX A1519 1
HET UNX A1520 1
HET UNX A1521 1
HET UNX A1522 1
HET UNX A1523 1
HET VR A1530 8
HET GLY A1548 5
HET SO4 A1549 5
HET SO4 A1550 5
HET CA A1551 1
HET CA A1552 1
HET CA A1553 1
HET BR A1554 1
HET NA A1555 1
HET NAG A1556 14
HET NAG A1557 14
HET FUL A1558 10
HET NAG A1559 14
HET NAG A1560 14
HET NAG A1561 14
HET NAG A1562 14
HET NAG A1563 14
HET NAG A1564 14
HET FUL A1565 10
HET CL A1566 1
HET NA A1567 1
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM VR 2-METHYLPROPYL HYDROGEN (R)-METHYLPHOSPHONATE
HETNAM GLY GLYCINE
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
HETNAM BR BROMIDE ION
HETNAM NA SODIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM CL CHLORIDE ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 UNX 23(X)
FORMUL 3 VR C5 H13 O3 P
FORMUL 4 GLY C2 H5 N O2
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 6 CA 3(CA 2+)
FORMUL 7 BR BR 1-
FORMUL 8 NA 2(NA 1+)
FORMUL 9 NAG 8(C8 H15 N O6)
FORMUL 10 FUL 2(C6 H12 O5)
FORMUL 11 CL CL 1-
FORMUL 12 HOH *419(H2 O)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 VAL A 148 LEU A 154 1 7
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 PRO A 211 PHE A 217 5 7
HELIX 10 10 SER A 235 GLY A 251 1 17
HELIX 11 11 ASN A 256 LYS A 267 1 12
HELIX 12 12 ASP A 268 GLU A 276 1 9
HELIX 13 13 ALA A 277 VAL A 280 5 4
HELIX 14 14 MET A 302 LEU A 309 1 8
HELIX 15 15 GLY A 326 GLY A 333 5 8
HELIX 16 16 THR A 346 PHE A 358 1 13
HELIX 17 17 SER A 362 THR A 374 1 13
HELIX 18 18 GLU A 383 PHE A 398 1 16
HELIX 19 19 PHE A 398 GLU A 411 1 14
HELIX 20 20 PRO A 431 GLY A 435 5 5
HELIX 21 21 GLU A 441 PHE A 446 1 6
HELIX 22 22 GLY A 447 GLU A 451 5 5
HELIX 23 23 GLU A 451 GLN A 455 5 5
HELIX 24 24 THR A 457 GLY A 478 1 22
HELIX 25 25 ARG A 515 PHE A 525 1 11
HELIX 26 26 PHE A 526 VAL A 529 5 4
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 MET A 16 VAL A 20 0
SHEET 2 AB11 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AB11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AB11 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AB11 ALA A 107 ILE A 113 1 O THR A 108 N ILE A 140
SHEET 6 AB11 GLY A 187 GLU A 197 1 N ASN A 188 O ALA A 107
SHEET 7 AB11 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AB11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AB11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AB11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AB11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.05
LINK ND2 ASN A 57 C1 NAG A1560 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A1559 1555 1555 1.44
LINK OG SER A 198 P1 VR A1530 1555 1555 1.67
LINK ND2 ASN A 241 C1 NAG A1563 1555 1555 1.47
LINK ND2 ASN A 256 C1 NAG A1562 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG A1556 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A1561 1555 1555 1.45
LINK CA CA A1551 O HOH A2040 1555 1555 2.18
LINK CA CA A1551 O HOH A2179 1555 1555 2.83
LINK CA CA A1552 O HOH A2355 1555 1555 2.87
LINK CA CA A1553 O HOH A2393 1555 7555 3.15
LINK CA CA A1553 OH TYR A 420 1555 1555 3.17
LINK O6 NAG A1556 C1 FUL A1558 1555 1555 1.45
LINK O4 NAG A1556 C1 NAG A1557 1555 1555 1.45
LINK O6 NAG A1563 C1 FUL A1565 1555 1555 1.45
LINK O4 NAG A1563 C1 NAG A1564 1555 1555 1.46
LINK NA NA A1567 O HOH A2290 1555 1555 3.15
CISPEP 1 ALA A 101 PRO A 102 0 -1.97
CISPEP 2 TRP A 376 VAL A 377 0 7.26
SITE 1 AC1 8 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC1 8 TRP A 231 LEU A 286 VAL A 288 HIS A 438
SITE 1 AC2 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC2 5 LYS A 131
SITE 1 AC3 3 GLN A 316 ASN A 414 ASN A 415
SITE 1 AC4 4 HIS A 372 PHE A 521 PHE A 525 HOH A2413
SITE 1 AC5 2 THR A 512 HOH A2381
SITE 1 AC6 2 HOH A2040 HOH A2179
SITE 1 AC7 2 THR A 508 HOH A2355
SITE 1 AC8 1 TYR A 420
SITE 1 AC9 2 ARG A 347 GLN A 351
SITE 1 BC1 1 TYR A 385
SITE 1 BC2 1 PHE A 525
SITE 1 BC3 5 ASN A 106 ASN A 188 LYS A 190 HOH A2416
SITE 2 BC3 5 HOH A2417
SITE 1 BC4 2 ASN A 57 HOH A2050
SITE 1 BC5 2 ARG A 465 ASN A 485
SITE 1 BC6 2 ASN A 256 HOH A2419
SITE 1 BC7 8 TYR A 237 GLU A 238 ASN A 241 ASN A 245
SITE 2 BC7 8 PHE A 278 VAL A 280 PRO A 281 HOH A2200
SITE 1 BC8 7 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 2 BC8 7 ASN A 342 HOH A2414 HOH A2415
CRYST1 154.600 154.600 127.610 90.00 90.00 90.00 I 4 2 2 16
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 0.006468 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006468 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007836 0.00000
TER 4259 VAL A 529
MASTER 738 0 44 26 14 0 22 6 4862 1 170 41
END |