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HEADER HYDROLASE 02-SEP-10 2XQK
TITLE X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
TITLE 2 PURE ENANTIOMER VX-(S)
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,
AUTHOR 2 F.NACHON
REVDAT 1 23-MAR-11 2XQK 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.55
REMARK 3 NUMBER OF REFLECTIONS : 29176
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) : 0.15959
REMARK 3 R VALUE (WORKING SET) : 0.15720
REMARK 3 FREE R VALUE : 0.21721
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1216
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) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.462
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2119
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.197
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.233
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4265
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 183
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.242
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.42
REMARK 3 B22 (A**2) : 1.42
REMARK 3 B33 (A**2) : -2.84
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): 0.264
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.243
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4555 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6209 ; 1.954 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 547 ; 6.711 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;36.882 ;24.218
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 721 ;17.688 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.228 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 674 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3486 ; 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): 2661 ; 1.064 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4307 ; 1.928 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1894 ; 3.231 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1892 ; 5.060 ; 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 70
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6430 -28.7140 -45.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.3229 T22: 0.1979
REMARK 3 T33: 0.4664 T12: -0.0550
REMARK 3 T13: -0.1102 T23: -0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 2.1814 L22: 1.8630
REMARK 3 L33: 1.8541 L12: -0.1798
REMARK 3 L13: 0.2277 L23: 0.2246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: 0.5564 S13: 0.0525
REMARK 3 S21: -0.6936 S22: -0.0040 S23: 0.1183
REMARK 3 S31: -0.0914 S32: -0.1534 S33: 0.0509
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 71 A 259
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9010 -31.3510 -33.2410
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.0545
REMARK 3 T33: 0.4574 T12: -0.0310
REMARK 3 T13: -0.0208 T23: -0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 0.9387 L22: 1.2737
REMARK 3 L33: 1.7068 L12: 0.0588
REMARK 3 L13: 0.2172 L23: 0.0919
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.1926 S13: -0.0873
REMARK 3 S21: -0.3142 S22: 0.0896 S23: -0.0410
REMARK 3 S31: 0.0351 S32: 0.0473 S33: -0.0599
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 260 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1940 -37.4700 -28.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0977 T22: 0.0583
REMARK 3 T33: 0.5087 T12: 0.0063
REMARK 3 T13: -0.0056 T23: -0.0730
REMARK 3 L TENSOR
REMARK 3 L11: 1.2577 L22: 1.1107
REMARK 3 L33: 1.4417 L12: -0.0254
REMARK 3 L13: 0.0416 L23: 0.2862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.0820 S13: -0.2626
REMARK 3 S21: -0.1694 S22: 0.0800 S23: -0.1697
REMARK 3 S31: 0.1925 S32: 0.1428 S33: -0.0747
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 324 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4190 -45.6100 -5.8740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1535 T22: 0.0780
REMARK 3 T33: 0.4810 T12: -0.0434
REMARK 3 T13: -0.1030 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 4.8256 L22: 2.0102
REMARK 3 L33: 2.2991 L12: 0.2383
REMARK 3 L13: 1.6405 L23: -0.5970
REMARK 3 S TENSOR
REMARK 3 S11: 0.2257 S12: -0.4146 S13: -0.4456
REMARK 3 S21: 0.1837 S22: 0.0842 S23: -0.0142
REMARK 3 S31: 0.3305 S32: -0.2335 S33: -0.3098
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 402 A 469
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8710 -27.1870 -16.6370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0800
REMARK 3 T33: 0.4458 T12: 0.0043
REMARK 3 T13: -0.0337 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 1.6482 L22: 1.7806
REMARK 3 L33: 1.7461 L12: 0.5137
REMARK 3 L13: 0.3753 L23: -0.0801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: -0.1410 S13: 0.0107
REMARK 3 S21: -0.0238 S22: 0.0414 S23: 0.2409
REMARK 3 S31: -0.0229 S32: -0.3080 S33: -0.0300
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 470 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2470 -21.4310 -9.7760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0821 T22: 0.1073
REMARK 3 T33: 0.4520 T12: 0.0179
REMARK 3 T13: -0.0272 T23: -0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 0.4819 L22: 4.0841
REMARK 3 L33: 1.8744 L12: -0.0900
REMARK 3 L13: 0.3078 L23: -0.3826
REMARK 3 S TENSOR
REMARK 3 S11: -0.1228 S12: -0.1399 S13: 0.2096
REMARK 3 S21: 0.3304 S22: 0.0779 S23: -0.0734
REMARK 3 S31: -0.2445 S32: -0.1917 S33: 0.0449
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2XQK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-10.
REMARK 100 THE PDBE ID CODE IS EBI-45266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
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 : 30395
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.1
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.9
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.30
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 (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.1 M,
REMARK 280 2-(N-MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR
REMARK 280 DIFFUSION, 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 77.46000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.46000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.69500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.46000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.69500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.46000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.69500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.46000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.69500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.46000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.69500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.46000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.69500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.46000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.69500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.46000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.69500
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: 43200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 160820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -255.9 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 K K A1538 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 ND2 ASN A 241 C1 NAG A 1546 2.08
REMARK 500 OE2 GLU A 497 O HOH A 2290 2.16
REMARK 500 O6 NAG A 1542 O HOH A 2321 2.15
REMARK 500 O HOH A 2114 O HOH A 2266 2.18
REMARK 500 O HOH A 2139 O HOH A 2142 2.15
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 GLU A 255 CB GLU A 255 CG 0.155
REMARK 500 GLU A 404 CG GLU A 404 CD 0.091
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. = -3.6 DEGREES
REMARK 500 LEU A 370 CA - CB - CG ANGL. DEV. = 17.6 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 -2.93 80.55
REMARK 500 LYS A 51 140.94 121.51
REMARK 500 ASP A 54 179.74 55.98
REMARK 500 ALA A 58 62.96 -102.44
REMARK 500 CYS A 92 13.61 -140.18
REMARK 500 LYS A 103 124.55 -24.71
REMARK 500 ASN A 106 60.02 -156.10
REMARK 500 PHE A 118 13.59 56.21
REMARK 500 ALA A 162 72.12 -154.81
REMARK 500 SER A 198 -124.68 63.07
REMARK 500 ASP A 297 -77.51 -140.81
REMARK 500 ASP A 324 57.25 -119.74
REMARK 500 ASP A 379 156.44 -40.72
REMARK 500 GLN A 380 57.58 -91.00
REMARK 500 PHE A 398 -56.64 -125.26
REMARK 500 THR A 496 -87.72 98.77
REMARK 500 GLU A 506 -78.87 -79.90
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 GLN A 380 24.7 L L OUTSIDE RANGE
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 FUC A 1541
REMARK 610 NAG A 1543
REMARK 610 NAG A 1545
REMARK 610 NAG A 1546
REMARK 610 NAG A 1547
REMARK 610 FUC A 1548
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 A1534 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 443 OE1
REMARK 620 2 HOH A2246 O 69.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1535 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2056 O
REMARK 620 2 GLU A 80 OE1 50.2
REMARK 620 3 HOH A2059 O 117.4 82.5
REMARK 620 4 HOH A2059 O 72.1 111.5 97.2
REMARK 620 5 HOH A2055 O 95.2 53.4 81.0 164.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 341 RESIDUES 1539 TO 1540
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 10MM HGCL2
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH VX
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH SULFATE
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE
REMARK 900 HYDROLASE COMPLEX
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE
REMARK 900 SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-
REMARK 900 FLUORIDATE (DFP)INHIBITED BUTYRYLCHOLINESTERASE
REMARK 900 AFTER AGING
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINEDBY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE INCOMPLEX WITH A CHOLINE
REMARK 900 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
REMARK 900 BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC VR
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC VX
DBREF 2XQK A 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQADV 2XQK GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XQK GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XQK GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XQK 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 GLY A1531 5
HET VX A1530 6
HET SO4 A1532 5
HET SO4 A1533 5
HET CA A1534 1
HET NA A1535 1
HET CL A1536 1
HET CL A1537 1
HET K A1538 1
HET NAG A1539 14
HET NAG A1540 14
HET FUC A1541 10
HET NAG A1542 14
HET NAG A1543 14
HET NAG A1544 14
HET NAG A1545 14
HET NAG A1546 14
HET NAG A1547 14
HET FUC A1548 10
HET UNX A1549 1
HET UNX A1550 1
HET UNX A1551 1
HET UNX A1552 1
HET UNX A1553 1
HET UNX A1554 1
HET UNX A1555 1
HET UNX A1556 1
HET UNX A1557 1
HET UNX A1558 1
HET UNX A1559 1
HET UNX A1560 1
HET UNX A1561 1
HET UNX A1562 1
HET UNX A1563 1
HET UNX A1564 1
HET UNX A1565 1
HET UNX A1566 1
HET UNX A1567 1
HET UNX A1568 1
HET UNX A1569 1
HET UNX A1570 1
HET UNX A1571 1
HET UNX A1572 1
HET UNX A1573 1
HETNAM GLY GLYCINE
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM K POTASSIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 GLY C2 H5 N O2
FORMUL 3 VX C3 H9 O3 P
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 CA CA 2+
FORMUL 6 NA NA 1+
FORMUL 7 CL 2(CL 1-)
FORMUL 8 K K 1+
FORMUL 9 NAG 8(C8 H15 N O6)
FORMUL 10 FUC 2(C6 H12 O5)
FORMUL 11 UNX 25(X)
FORMUL 12 HOH *323(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 LEU A 208 1 11
HELIX 9 9 SER A 210 PHE A 217 5 8
HELIX 10 10 SER A 235 THR A 250 1 16
HELIX 11 11 ASN A 256 ARG A 265 1 10
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 VAL A 331 1 6
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 ALA A 7 0
SHEET 2 AA 3 LYS A 12 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA 3 TRP A 56 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 2.08
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.11
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.08
LINK ND2 ASN A 106 C1 NAG A1542 1555 1555 1.45
LINK OG SER A 198 P1 VX A1530 1555 1555 1.73
LINK ND2 ASN A 341 C1 NAG A1539 1555 1555 1.42
LINK ND2 ASN A 485 C1 NAG A1544 1555 1555 1.44
LINK CA CA A1534 OE1 GLU A 443 1555 1555 3.19
LINK CA CA A1534 O HOH A2246 1555 1555 2.54
LINK NA NA A1535 O HOH A2056 1555 1555 3.10
LINK NA NA A1535 OE1 GLU A 80 1555 1555 2.80
LINK NA NA A1535 O HOH A2059 1555 1555 2.53
LINK NA NA A1535 O HOH A2059 1555 16444 2.33
LINK NA NA A1535 O HOH A2055 1555 1555 2.89
LINK O4 NAG A1539 C1 NAG A1540 1555 1555 1.43
CISPEP 1 ALA A 101 PRO A 102 0 0.57
CISPEP 2 VAL A 377 ASP A 378 0 -20.43
SITE 1 AC1 4 LEU A 18 TRP A 98 ASP A 129 LYS A 131
SITE 1 AC2 7 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC2 7 HIS A 438 HOH A2165 HOH A2318
SITE 1 AC3 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC4 3 HIS A 372 PHE A 521 PHE A 525
SITE 1 AC5 2 GLU A 443 HOH A2246
SITE 1 AC6 3 GLU A 80 HOH A2055 HOH A2059
SITE 1 AC7 2 ARG A 347 GLN A 351
SITE 1 AC8 2 THR A 512 HOH A2295
SITE 1 AC9 3 SER A 338 NAG A1539 NAG A1540
SITE 1 BC1 5 ASN A 106 ASN A 188 LYS A 190 HOH A2320
SITE 2 BC1 5 HOH A2321
SITE 1 BC2 1 ASN A 57
SITE 1 BC3 2 ARG A 465 ASN A 485
SITE 1 BC4 1 ASN A 256
SITE 1 BC5 7 TYR A 237 GLU A 238 ASN A 241 ASN A 245
SITE 2 BC5 7 PRO A 281 NAG A1547 FUC A1548
SITE 1 BC6 2 NAG A1546 FUC A1548
SITE 1 BC7 7 ASN A 245 PHE A 278 VAL A 280 PRO A 281
SITE 2 BC7 7 NAG A1546 NAG A1547 HOH A2323
SITE 1 BC8 7 PHE A 337 SER A 338 ASN A 341 ASN A 342
SITE 2 BC8 7 FUC A1541 HOH A2195 HOH A2319
CRYST1 154.920 154.920 127.390 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 0.006455 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007850 0.00000
TER 4266 VAL A 529
MASTER 715 0 44 26 14 0 22 6 4771 1 166 41
END |