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HEADER HYDROLASE 08-DEC-10 2Y1K
TITLE STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (
TITLE 2 12H SOAK): PHOSPHOSERINE ADDUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-557;
COMPND 5 EC: 3.1.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS:
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, INHIBITION, AGING
EXPDTA X-RAY DIFFRACTION
AUTHOR E.CARLETTI,J.P.COLLETIER,F.NACHON,M.WEIK
REVDAT 1 29-JUN-11 2Y1K 0
JRNL AUTH E.CARLETTI,L.M.SCHOPFER,J.P.COLLETIER,M.T.FROMENT,F.NACHON,
JRNL AUTH 2 M.WEIK,O.LOCKRIDGE,P.MASSON
JRNL TITL REACTION OF CRESYL SALIGENIN PHOSPHATE, THE
JRNL TITL 2 ORGANOPHOSPHORUS AGENT IMPLICATED IN AEROTOXIC SYNDROME,
JRNL TITL 3 WITH HUMAN CHOLINESTERASES: MECHANISTIC STUDIES EMPLOYING
JRNL TITL 4 KINETICS, MASS SPECTROMETRY, AND X-RAY STRUCTURE ANALYSIS.
JRNL REF CHEM.RES.TOXICOL. V. 24 797 2011
JRNL REFN ISSN 0893-228X
JRNL PMID 21438623
JRNL DOI 10.1021/TX100447K
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0093
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.79
REMARK 3 NUMBER OF REFLECTIONS : 24577
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) : 0.18480
REMARK 3 R VALUE (WORKING SET) : 0.18281
REMARK 3 FREE R VALUE : 0.24706
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 760
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) : 2.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.565
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1713
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.265
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.432
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4193
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 175
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.361
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.02
REMARK 3 B33 (A**2) : -0.04
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): 0.405
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.275
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.173
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4484 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6097 ; 1.933 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 527 ; 7.481 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 201 ;37.736 ;24.030
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 700 ;18.567 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;15.683 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 673 ; 0.151 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3378 ; 0.009 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 22.5889 28.8405 18.6809
REMARK 3 T TENSOR
REMARK 3 T11: 0.4925 T22: 0.3015
REMARK 3 T33: 0.0393 T12: -0.0887
REMARK 3 T13: 0.1153 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 4.1174 L22: 4.3716
REMARK 3 L33: 2.6680 L12: -1.2092
REMARK 3 L13: -0.1780 L23: -0.3635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.9061 S13: 0.1341
REMARK 3 S21: -1.2883 S22: -0.0816 S23: -0.3160
REMARK 3 S31: 0.2084 S32: 0.3469 S33: 0.0912
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 233
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6657 28.3397 31.0946
REMARK 3 T TENSOR
REMARK 3 T11: 0.1602 T22: 0.0797
REMARK 3 T33: 0.0264 T12: -0.0663
REMARK 3 T13: 0.0206 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 2.1968 L22: 2.4159
REMARK 3 L33: 2.6600 L12: -0.0049
REMARK 3 L13: -0.6708 L23: -0.0284
REMARK 3 S TENSOR
REMARK 3 S11: -0.1515 S12: 0.2055 S13: 0.0925
REMARK 3 S21: -0.3452 S22: 0.1520 S23: -0.0099
REMARK 3 S31: 0.1843 S32: 0.0987 S33: -0.0005
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 234 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2214 49.8386 27.0455
REMARK 3 T TENSOR
REMARK 3 T11: 0.4594 T22: 0.3087
REMARK 3 T33: 0.5078 T12: 0.0479
REMARK 3 T13: -0.0633 T23: 0.1842
REMARK 3 L TENSOR
REMARK 3 L11: 5.6554 L22: 6.4919
REMARK 3 L33: 9.4734 L12: -0.1429
REMARK 3 L13: -0.0324 L23: -2.1078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: -0.0011 S13: 0.9013
REMARK 3 S21: -0.0403 S22: 0.2320 S23: 0.4281
REMARK 3 S31: -1.1427 S32: -0.7709 S33: -0.1959
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 283 A 373
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4193 39.9844 49.4328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1406 T22: 0.1351
REMARK 3 T33: 0.2263 T12: -0.0005
REMARK 3 T13: 0.0990 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.0609 L22: 2.3653
REMARK 3 L33: 3.1414 L12: 0.8796
REMARK 3 L13: 0.0899 L23: 0.8209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0698 S12: -0.1961 S13: 0.3864
REMARK 3 S21: -0.0054 S22: 0.0620 S23: 0.4718
REMARK 3 S31: -0.4771 S32: -0.0738 S33: -0.1318
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 374 A 472
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4372 30.4890 50.5303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0527 T22: 0.4568
REMARK 3 T33: 0.0665 T12: -0.0196
REMARK 3 T13: 0.0151 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 1.3627 L22: 5.5425
REMARK 3 L33: 3.1475 L12: -0.1568
REMARK 3 L13: -0.6040 L23: 0.5251
REMARK 3 S TENSOR
REMARK 3 S11: 0.0315 S12: -0.7712 S13: 0.1040
REMARK 3 S21: 0.2718 S22: 0.0816 S23: -0.4190
REMARK 3 S31: -0.0515 S32: 0.5795 S33: -0.1131
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 473 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5166 21.7678 54.6426
REMARK 3 T TENSOR
REMARK 3 T11: 0.1220 T22: 0.3879
REMARK 3 T33: 0.2665 T12: -0.0811
REMARK 3 T13: -0.0249 T23: 0.2653
REMARK 3 L TENSOR
REMARK 3 L11: 1.9092 L22: 8.6307
REMARK 3 L33: 4.4235 L12: -1.0811
REMARK 3 L13: -2.3015 L23: 3.0835
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.7168 S13: -0.4035
REMARK 3 S21: 0.4044 S22: -0.0681 S23: 0.3276
REMARK 3 S31: 0.2460 S32: 0.4220 S33: 0.0543
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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. THE ADPS OF THE ATOMS IN THE PHOPHONO GROUP
REMARK 3 OF SER 198 WERE REFINED SEPARATELY (AS ISOTROPIC) AND NOT
REMARK 3 INCLUDED IN THE TLS REFINEMENT OF RESIDUES 71-233.
REMARK 4
REMARK 4 2Y1K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-10
REMARK 100 THE PDBE ID CODE IS EBI-46641
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
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 : 25339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.8
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 6.7
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.0
REMARK 200 R MERGE FOR SHELL (I) : 0.40
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 2.1 M AMMONIUM
REMARK 280 SULFATE.
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 76.88500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 76.88500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.80000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 76.88500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.80000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 76.88500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.80000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 76.88500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.80000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 76.88500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.80000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 76.88500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.80000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 76.88500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.80000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 76.88500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 76.88500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.80000
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: 51750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 155080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -515.6 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 127.60000
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 127.60000
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 127.60000
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 127.60000
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 379
REMARK 465 GLN A 380
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 54 CG OD1 OD2
REMARK 470 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
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 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 391 O HOH A 2144 1.52
REMARK 500 O TRP A 522 O HOH A 2214 1.66
REMARK 500 N ASP A 395 O HOH A 2144 1.82
REMARK 500 O4 NAG A 1536 O5 NAG A 1538 1.86
REMARK 500 O LEU A 514 O HOH A 2210 1.89
REMARK 500 O TYR A 500 O HOH A 2199 1.89
REMARK 500 NH1 ARG A 347 O HOH A 2129 1.93
REMARK 500 O ILE A 510 O HOH A 2204 1.96
REMARK 500 CB ALA A 475 O HOH A 2179 1.98
REMARK 500 O4 NAG A 1536 C1 NAG A 1538 2.00
REMARK 500 O HOH A 2072 O HOH A 2134 2.00
REMARK 500 N THR A 496 O HOH A 2192 2.01
REMARK 500 N ARG A 381 O HOH A 2138 2.01
REMARK 500 C TRP A 522 O HOH A 2214 2.06
REMARK 500 CG2 THR A 300 O HOH A 2111 2.10
REMARK 500 O PRO A 157 O HOH A 2078 2.14
REMARK 500 NE2 GLN A 172 O HOH A 2081 2.17
REMARK 500 CL CL A 1533 O HOH A 2186 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 2089 O HOH A 2091 7556 1.50
REMARK 500 O HOH A 2198 O HOH A 2207 7556 2.11
REMARK 500 O HOH A 2204 O HOH A 2208 7556 1.56
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 ILE A 4 76.43 -159.39
REMARK 500 PHE A 43 -14.89 88.73
REMARK 500 THR A 50 -73.41 -23.26
REMARK 500 LYS A 51 172.90 137.85
REMARK 500 TRP A 52 136.33 169.20
REMARK 500 ASP A 54 169.92 58.21
REMARK 500 ALA A 58 65.06 -104.53
REMARK 500 GLN A 67 142.23 169.34
REMARK 500 SER A 89 145.30 -172.09
REMARK 500 LYS A 103 123.42 -32.26
REMARK 500 ASN A 106 52.46 -164.88
REMARK 500 ALA A 162 80.80 -153.24
REMARK 500 SEP A 198 -123.34 57.87
REMARK 500 TYR A 237 -71.26 -56.51
REMARK 500 PRO A 281 -95.16 -46.54
REMARK 500 ASP A 297 -83.90 -141.65
REMARK 500 VAL A 361 98.53 41.19
REMARK 500 PHE A 398 -59.14 -123.06
REMARK 500 LEU A 428 122.67 -39.39
REMARK 500 PRO A 480 46.93 -94.49
REMARK 500 ASN A 485 60.03 -100.23
REMARK 500 ASN A 486 48.64 36.74
REMARK 500 THR A 496 -77.99 111.80
REMARK 500 GLU A 506 -115.96 -101.76
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 LEU A 156 PRO A 157 -148.97
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 361 13.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 CATALYTIC SERINE 198 IS PHOSPHORYLATED (SEP).
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 HOH A2072 O
REMARK 620 2 HOH A2073 O 101.1
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 SO4 A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU4 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU4 A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 341 RESIDUES 1536 TO 1539
REMARK 900
REMARK 900 RELATED ENTRIES
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: 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: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH SULFATE
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: 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: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC CVX
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: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY PURE ENANTIOMER VX-(R)
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: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC VX
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: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC VR
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 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE NUMBERING IS FOR THE MATURE PROTEIN SEQUENCE.
DBREF 2Y1K A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2Y1K GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2Y1K GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2Y1K GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SEP ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES 38 A 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
MODRES 2Y1K SEP A 198 SER PHOSPHOSERINE
HET SEP A 198 10
HET SO4 A1531 5
HET NA A1532 1
HET CL A1533 1
HET GOL A1534 6
HET SO4 A1535 5
HET NAG A1536 14
HET FUC A1539 10
HET SO4 A1537 5
HET NAG A1538 14
HET SO4 A1540 5
HET SO4 A1541 5
HET NAG A1542 14
HET FU4 A1543 10
HET NAG A1544 14
HET NAG A1545 14
HET NAG A1546 14
HET NAG A1547 14
HET NAG A1548 14
HET FU4 A1549 10
HETNAM SEP PHOSPHOSERINE
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM FU4 2,6-ANHYDRO-1-DEOXY-D-GALACTITOL
HETSYN SEP PHOSPHONOSERINE
HETSYN GOL GLYCERIN
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 3 NA NA 1+
FORMUL 4 CL CL 1-
FORMUL 5 GOL C3 H8 O3
FORMUL 6 NAG 8(C8 H15 N O6)
FORMUL 7 FUC C6 H12 O5
FORMUL 8 FU4 2(C6 H12 O4)
FORMUL 9 HOH *229(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 SEP 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 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 SER A 524 1 10
HELIX 26 26 PHE A 525 VAL A 529 5 5
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 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 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.07
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.10
LINK C GLU A 197 N SEP A 198 1555 1555 1.34
LINK C SEP A 198 N ALA A 199 1555 1555 1.35
LINK ND2 ASN A 341 C1 NAG A1536 1555 1555 1.42
LINK NA NA A1532 O HOH A2073 1555 5556 2.37
LINK NA NA A1532 O HOH A2072 1555 5556 2.44
LINK O6 NAG A1536 C1 FUC A1539 1555 1555 1.46
CISPEP 1 ALA A 101 PRO A 102 0 1.44
CISPEP 2 GLY A 360 VAL A 361 0 24.46
SITE 1 AC1 2 ARG A 347 GLN A 351
SITE 1 AC2 4 PHE A 521 PHE A 525 HOH A2072 HOH A2073
SITE 1 AC3 3 THR A 488 THR A 508 HOH A2186
SITE 1 AC4 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC4 5 LYS A 131
SITE 1 AC5 5 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 2 AC5 5 HOH A2121
SITE 1 AC6 7 LYS A 323 TYR A 420 ARG A 509 ARG A 515
SITE 2 AC6 7 SO4 A1541 HOH A2219 HOH A2220
SITE 1 AC7 7 ARG A 509 LEU A 514 ARG A 515 GLN A 518
SITE 2 AC7 7 SO4 A1540 HOH A2206 HOH A2220
SITE 1 AC8 5 ASN A 106 ASN A 188 LYS A 190 FU4 A1543
SITE 2 AC8 5 HOH A2221
SITE 1 AC9 5 ASN A 188 LYS A 190 SER A 191 NAG A1542
SITE 2 AC9 5 HOH A2223
SITE 1 BC1 3 ARG A 14 ASN A 57 HOH A2224
SITE 1 BC2 3 ARG A 465 GLU A 482 ASN A 485
SITE 1 BC3 2 ASN A 256 THR A 258
SITE 1 BC4 4 TYR A 237 ASN A 241 ASN A 245 NAG A1548
SITE 1 BC5 4 LYS A 248 NAG A1547 FU4 A1549 HOH A2226
SITE 1 BC6 4 ASN A 245 PHE A 278 VAL A 280 NAG A1548
SITE 1 BC7 8 ARG A 242 LEU A 286 SER A 287 VAL A 288
SITE 2 BC7 8 SER A 338 ASN A 341 HOH A2217 HOH A2218
CRYST1 153.770 153.770 127.600 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 0.006503 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007837 0.00000
TER 4194 VAL A 529
MASTER 724 0 20 26 14 0 23 6 4597 1 192 41
END |