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HEADER HYDROLASE 02-SEP-10 2XQF
TITLE X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY RACEMIC
TITLE 2 VX
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 2XQF 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. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 43925
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) : 0.15003
REMARK 3 R VALUE (WORKING SET) : 0.14882
REMARK 3 FREE R VALUE : 0.18934
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1359
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) : 2.103
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.158
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3153
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.187
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.238
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4269
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 193
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.051
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59
REMARK 3 B22 (A**2) : -0.59
REMARK 3 B33 (A**2) : 1.18
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4558 ; 0.030 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6220 ; 2.291 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 547 ; 6.860 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;35.736 ;24.238
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 722 ;16.534 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.289 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 678 ; 0.207 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3495 ; 0.013 ; 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 ; 1.383 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4307 ; 2.263 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1897 ; 3.769 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1903 ; 5.782 ; 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 53
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8550 -26.5040 -46.3400
REMARK 3 T TENSOR
REMARK 3 T11: 0.3421 T22: 0.2506
REMARK 3 T33: 0.1163 T12: -0.0526
REMARK 3 T13: -0.0868 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 2.1098 L22: 1.5364
REMARK 3 L33: 1.6493 L12: -0.1799
REMARK 3 L13: 0.1023 L23: 0.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0695 S12: 0.5541 S13: 0.1477
REMARK 3 S21: -0.5662 S22: 0.0142 S23: 0.0548
REMARK 3 S31: -0.1637 S32: -0.1593 S33: 0.0553
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 54 A 236
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0330 -29.2570 -33.6560
REMARK 3 T TENSOR
REMARK 3 T11: 0.1162 T22: 0.0798
REMARK 3 T33: 0.0596 T12: -0.0282
REMARK 3 T13: -0.0339 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 0.7047 L22: 1.0948
REMARK 3 L33: 1.4203 L12: 0.2460
REMARK 3 L13: 0.0989 L23: 0.1839
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: 0.1521 S13: -0.0598
REMARK 3 S21: -0.2674 S22: 0.0663 S23: 0.0294
REMARK 3 S31: -0.0555 S32: -0.0307 S33: -0.0137
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 237 A 325
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5260 -40.7910 -30.4770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.0889
REMARK 3 T33: 0.1540 T12: 0.0327
REMARK 3 T13: 0.0089 T23: -0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 1.1717 L22: 0.9603
REMARK 3 L33: 1.4355 L12: 0.2286
REMARK 3 L13: 0.0958 L23: 0.2008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: 0.1486 S13: -0.3075
REMARK 3 S21: -0.1177 S22: 0.1401 S23: -0.2344
REMARK 3 S31: 0.3195 S32: 0.2586 S33: -0.0931
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 326 A 389
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9180 -47.3840 -4.9130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1875 T22: 0.0798
REMARK 3 T33: 0.1069 T12: -0.0515
REMARK 3 T13: -0.1009 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 5.4906 L22: 1.8783
REMARK 3 L33: 3.4708 L12: 0.5776
REMARK 3 L13: 2.1740 L23: -0.0471
REMARK 3 S TENSOR
REMARK 3 S11: 0.2135 S12: -0.4849 S13: -0.4459
REMARK 3 S21: 0.2624 S22: 0.0357 S23: -0.0326
REMARK 3 S31: 0.4108 S32: -0.2835 S33: -0.2491
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 390 A 484
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9200 -25.9000 -16.7040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0819 T22: 0.1234
REMARK 3 T33: 0.0853 T12: 0.0017
REMARK 3 T13: -0.0302 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 0.6651 L22: 1.4777
REMARK 3 L33: 1.2953 L12: 0.0294
REMARK 3 L13: 0.1169 L23: 0.0159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.0593 S13: 0.0288
REMARK 3 S21: 0.0026 S22: 0.0012 S23: 0.1661
REMARK 3 S31: -0.0373 S32: -0.1976 S33: -0.0206
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 485 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7580 -24.5870 -6.6210
REMARK 3 T TENSOR
REMARK 3 T11: 0.1493 T22: 0.1418
REMARK 3 T33: 0.0737 T12: -0.0192
REMARK 3 T13: -0.0319 T23: -0.0468
REMARK 3 L TENSOR
REMARK 3 L11: 0.9530 L22: 4.0680
REMARK 3 L33: 1.9251 L12: -0.2383
REMARK 3 L13: 0.1373 L23: 0.3294
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: -0.1062 S13: 0.0883
REMARK 3 S21: 0.2559 S22: 0.1192 S23: -0.2327
REMARK 3 S31: -0.1088 S32: -0.0822 S33: -0.0454
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 2XQF 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-45247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-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 : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.981
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 45286
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 48.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 9.0
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.7
REMARK 200 R MERGE FOR SHELL (I) : 0.29
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.90
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 77.55500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.55500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.05000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.55500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.05000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.55500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.05000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.55500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.05000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.55500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.05000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.55500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.05000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.55500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.05000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.55500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.55500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.05000
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: 49830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 154480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.7 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 A1535 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 1580 UNK UNX A 1581 1.38
REMARK 500 UNK UNX A 1554 UNK UNX A 1562 1.44
REMARK 500 UNK UNX A 1577 UNK UNX A 1578 1.60
REMARK 500 UNK UNX A 1554 UNK UNX A 1555 1.64
REMARK 500 O HOH A 2150 O HOH A 2339 1.74
REMARK 500 N THR A 496 O HOH A 2385 1.75
REMARK 500 UNK UNX A 1584 UNK UNX A 1585 1.77
REMARK 500 UNK UNX A 1570 UNK UNX A 1571 1.79
REMARK 500 UNK UNX A 1582 UNK UNX A 1583 1.79
REMARK 500 SG CYS A 66 O HOH A 2097 1.81
REMARK 500 O HOH A 2237 O HOH A 2238 1.84
REMARK 500 UNK UNX A 1575 UNK UNX A 1576 1.91
REMARK 500 NE2 GLN A 311 O HOH A 2238 1.91
REMARK 500 OE1 GLU A 451 O HOH A 2345 1.92
REMARK 500 UNK UNX A 1584 UNK UNX A 1586 1.94
REMARK 500 O HOH A 2195 O HOH A 2197 1.95
REMARK 500 UNK UNX A 1553 UNK UNX A 1573 1.98
REMARK 500 UNK UNX A 1555 UNK UNX A 1556 1.99
REMARK 500 UNK UNX A 1571 UNK UNX A 1572 1.99
REMARK 500 UNK UNX A 1578 UNK UNX A 1579 1.99
REMARK 500 CA SER A 495 O HOH A 2385 2.03
REMARK 500 UNK UNX A 1574 UNK UNX A 1575 2.04
REMARK 500 O HOH A 2150 O HOH A 2328 2.05
REMARK 500 UNK UNX A 1566 UNK UNX A 1567 2.06
REMARK 500 O6 NAG A 1541 O HOH A 2426 2.07
REMARK 500 OE2 GLU A 451 O HOH A 2343 2.10
REMARK 500 O HOH A 2181 O HOH A 2186 2.10
REMARK 500 UNK UNX A 1570 UNK UNX A 1572 2.11
REMARK 500 UNK UNX A 1585 UNK UNX A 1586 2.14
REMARK 500 O HOH A 2359 O HOH A 2400 2.14
REMARK 500 O HOH A 2018 O HOH A 2063 2.15
REMARK 500 UNK UNX A 1565 UNK UNX A 1566 2.15
REMARK 500 O HOH A 2083 O HOH A 2178 2.15
REMARK 500 O HOH A 2205 O HOH A 2206 2.16
REMARK 500 O HOH A 2021 O HOH A 2150 2.16
REMARK 500 OD1 ASP A 304 O HOH A 2232 2.16
REMARK 500 UNK UNX A 1557 UNK UNX A 1558 2.17
REMARK 500 O HOH A 2090 O HOH A 2091 2.17
REMARK 500 O HOH A 2089 O HOH A 2184 2.18
REMARK 500 C SER A 495 O HOH A 2385 2.18
REMARK 500 UNK UNX A 1564 O HOH A 2117 2.18
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 O HOH A 2179 O HOH A 2239 4555 2.14
REMARK 500 O HOH A 2233 O HOH A 2368 3555 2.19
REMARK 500 O HOH A 2239 O HOH A 2365 3555 2.05
REMARK 500 O HOH A 2240 O HOH A 2365 3555 1.86
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 ARG A 219 CG ARG A 219 CD 0.191
REMARK 500 TYR A 282 CE1 TYR A 282 CZ 0.080
REMARK 500 PHE A 371 CE1 PHE A 371 CZ 0.123
REMARK 500 TYR A 396 CD1 TYR A 396 CE1 0.103
REMARK 500 TYR A 396 CE2 TYR A 396 CD2 0.090
REMARK 500 GLN A 455 CD GLN A 455 NE2 0.746
REMARK 500 TRP A 471 CB TRP A 471 CG 0.152
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 LEU A 49 CB - CG - CD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 LEU A 154 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU A 370 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 GLN A 455 CG - CD - NE2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 THR A 508 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH2 ANGL. DEV. = -3.8 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 -1.22 71.30
REMARK 500 LYS A 51 128.36 104.02
REMARK 500 ASP A 54 179.80 91.29
REMARK 500 ALA A 58 63.33 -102.32
REMARK 500 ALA A 162 71.29 -155.95
REMARK 500 SER A 198 -122.22 52.96
REMARK 500 ASP A 297 -80.41 -136.34
REMARK 500 GLN A 311 75.44 -100.30
REMARK 500 ASP A 378 -44.16 -153.54
REMARK 500 ASP A 379 150.82 -30.74
REMARK 500 PHE A 398 -56.86 -129.23
REMARK 500 THR A 496 -83.46 96.61
REMARK 500 GLU A 506 -79.23 -83.68
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 14.7 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 NA A1532 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 80 OE1
REMARK 620 2 HOH A2087 O 83.5
REMARK 620 3 HOH A2087 O 105.4 101.0
REMARK 620 4 HOH A2024 O 108.2 93.3 144.7
REMARK 620 5 HOH A2078 O 49.6 83.1 154.5 58.7
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 VX A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG 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 CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 241 RESIDUES 1545 TO 1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 341 RESIDUES 1538 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: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH SULFATE
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: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE
REMARK 900 HYDROLASE COMPLEX
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: 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: 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: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH FLUORIDE ANION
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: 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: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY PURE ENANTIOMER VX-(S)
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)
DBREF 2XQF A 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQADV 2XQF GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XQF GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XQF GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XQF 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 VX A1530 6
HET GLY A1531 5
HET NA A1532 1
HET CL A1533 1
HET CL A1534 1
HET K A1535 1
HET SO4 A1536 5
HET SO4 A1537 5
HET NAG A1538 14
HET NAG A1539 14
HET FUL A1540 10
HET NAG A1541 14
HET NAG A1542 14
HET NAG A1543 14
HET NAG A1544 14
HET NAG A1545 14
HET NAG A1546 14
HET FUL A1547 10
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
HET UNX A1574 1
HET UNX A1575 1
HET UNX A1576 1
HET UNX A1577 1
HET UNX A1578 1
HET UNX A1579 1
HET UNX A1580 1
HET UNX A1581 1
HET UNX A1582 1
HET UNX A1583 1
HET UNX A1584 1
HET UNX A1585 1
HET UNX A1586 1
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM GLY GLYCINE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM K POTASSIUM ION
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 VX C3 H9 O3 P
FORMUL 3 GLY C2 H5 N O2
FORMUL 4 NA NA 1+
FORMUL 5 CL 2(CL 1-)
FORMUL 6 K K 1+
FORMUL 7 SO4 2(O4 S 2-)
FORMUL 8 NAG 8(C8 H15 N O6)
FORMUL 9 FUL 2(C6 H12 O5)
FORMUL 10 UNX X
FORMUL 11 HOH *432(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 THR A 250 1 16
HELIX 11 11 ASN A 256 LYS A 267 1 12
HELIX 12 12 ASP A 268 ALA A 277 1 10
HELIX 13 13 PHE A 278 VAL A 280 5 3
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 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 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.13
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.12
LINK ND2 ASN A 57 C1 NAG A1542 1555 1555 1.48
LINK ND2 ASN A 106 C1 NAG A1541 1555 1555 1.45
LINK OG SER A 198 P1 VX A1530 1555 1555 1.70
LINK ND2 ASN A 241 C1 NAG A1545 1555 1555 1.47
LINK ND2 ASN A 256 C1 NAG A1544 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A1538 1555 1555 1.43
LINK ND2 ASN A 485 C1 NAG A1543 1555 1555 1.46
LINK NA NA A1532 O HOH A2087 1555 16444 2.45
LINK NA NA A1532 OE1 GLU A 80 1555 1555 3.09
LINK NA NA A1532 O HOH A2087 1555 1555 2.84
LINK NA NA A1532 O HOH A2078 1555 1555 3.01
LINK NA NA A1532 O HOH A2024 1555 1555 3.13
LINK O6 NAG A1538 C1 FUL A1540 1555 1555 1.45
LINK O4 NAG A1538 C1 NAG A1539 1555 1555 1.41
LINK O6 NAG A1545 C1 FUL A1547 1555 1555 1.44
LINK O4 NAG A1545 C1 NAG A1546 1555 1555 1.47
CISPEP 1 ALA A 101 PRO A 102 0 -6.55
CISPEP 2 VAL A 377 ASP A 378 0 -13.31
SITE 1 AC1 7 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC1 7 TRP A 231 LEU A 286 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 GLU A 80 HOH A2078 HOH A2087
SITE 1 AC4 2 ARG A 347 GLN A 351
SITE 1 AC5 3 THR A 512 HOH A2388 HOH A2394
SITE 1 AC6 1 PHE A 525
SITE 1 AC7 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC8 4 HIS A 372 PHE A 521 PHE A 525 HOH A2422
SITE 1 AC9 5 ASN A 106 ASN A 188 LYS A 190 HOH A2425
SITE 2 AC9 5 HOH A2426
SITE 1 BC1 3 ARG A 14 ASN A 57 HOH A2047
SITE 1 BC2 4 ARG A 465 ASN A 485 HOH A2428 HOH A2429
SITE 1 BC3 3 ASN A 256 HOH A2430 HOH A2431
SITE 1 BC4 10 TYR A 237 GLU A 238 ASN A 241 ASN A 245
SITE 2 BC4 10 LYS A 248 LEU A 249 PHE A 278 VAL A 280
SITE 3 BC4 10 PRO A 281 HOH A2432
SITE 1 BC5 9 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 2 BC5 9 ASN A 342 HOH A2259 HOH A2263 HOH A2423
SITE 3 BC5 9 HOH A2424
CRYST1 155.110 155.110 128.100 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 0.006447 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007806 0.00000
TER 4270 VAL A 529
MASTER 753 0 54 26 14 0 21 6 4894 1 171 41
END |