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HEADER HYDROLASE 02-SEP-10 2XQJ
TITLE X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
TITLE 2 PURE ENANTIOMER VX-(R)
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 2XQJ 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 5.5.0109
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) : 49.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.88
REMARK 3 NUMBER OF REFLECTIONS : 29799
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) : 0.17002
REMARK 3 R VALUE (WORKING SET) : 0.16782
REMARK 3 FREE R VALUE : 0.22291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1242
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) : 2165
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.203
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 161
REMARK 3 SOLVENT ATOMS : 346
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.695
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.82
REMARK 3 B22 (A**2) : 1.82
REMARK 3 B33 (A**2) : -3.63
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): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.249
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4536 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6183 ; 1.976 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 539 ; 6.884 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;35.793 ;24.155
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;17.440 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.910 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 674 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3467 ; 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): 2650 ; 1.054 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4286 ; 1.944 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1886 ; 3.313 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1891 ; 5.346 ; 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: 0.3103 T22: 0.1671
REMARK 3 T33: 0.5176 T12: -0.0526
REMARK 3 T13: -0.1046 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 1.2074 L22: 1.5087
REMARK 3 L33: 1.3988 L12: 0.1412
REMARK 3 L13: 0.3266 L23: 0.1958
REMARK 3 S TENSOR
REMARK 3 S11: -0.1004 S12: 0.3592 S13: -0.0268
REMARK 3 S21: -0.6359 S22: 0.0667 S23: 0.1292
REMARK 3 S31: -0.1219 S32: -0.0791 S33: 0.0338
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: 0.1107 T22: 0.0652
REMARK 3 T33: 0.5236 T12: -0.0296
REMARK 3 T13: -0.0261 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 0.8031 L22: 1.2565
REMARK 3 L33: 1.4881 L12: 0.1273
REMARK 3 L13: 0.2814 L23: 0.1304
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: 0.1689 S13: -0.0840
REMARK 3 S21: -0.3031 S22: 0.0729 S23: -0.0464
REMARK 3 S31: -0.0155 S32: 0.0675 S33: -0.0577
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: 0.1033 T22: 0.0776
REMARK 3 T33: 0.5911 T12: 0.0060
REMARK 3 T13: -0.0084 T23: -0.0822
REMARK 3 L TENSOR
REMARK 3 L11: 1.0106 L22: 1.1238
REMARK 3 L33: 1.3468 L12: 0.1507
REMARK 3 L13: 0.1865 L23: 0.1572
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: 0.1221 S13: -0.2165
REMARK 3 S21: -0.2058 S22: 0.0880 S23: -0.2107
REMARK 3 S31: 0.1613 S32: 0.2191 S33: -0.0934
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: 0.2021 T22: 0.1113
REMARK 3 T33: 0.5994 T12: -0.0488
REMARK 3 T13: -0.1135 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 2.6405 L22: 0.9696
REMARK 3 L33: 1.8528 L12: 0.1205
REMARK 3 L13: 0.9571 L23: -0.3504
REMARK 3 S TENSOR
REMARK 3 S11: 0.2166 S12: -0.3695 S13: -0.3970
REMARK 3 S21: 0.2359 S22: 0.0265 S23: -0.0592
REMARK 3 S31: 0.3868 S32: -0.1729 S33: -0.2430
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: 0.0403 T22: 0.1031
REMARK 3 T33: 0.5340 T12: 0.0011
REMARK 3 T13: -0.0301 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 1.1271 L22: 1.5950
REMARK 3 L33: 1.3871 L12: 0.3474
REMARK 3 L13: 0.3846 L23: 0.0923
REMARK 3 S TENSOR
REMARK 3 S11: 0.0397 S12: -0.1470 S13: 0.0341
REMARK 3 S21: 0.0259 S22: -0.0203 S23: 0.2435
REMARK 3 S31: -0.0328 S32: -0.2724 S33: -0.0194
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: 0.0796 T22: 0.0926
REMARK 3 T33: 0.5165 T12: 0.0097
REMARK 3 T13: -0.0347 T23: -0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 0.6877 L22: 2.1256
REMARK 3 L33: 1.4255 L12: 0.1891
REMARK 3 L13: 0.3120 L23: -0.1054
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: -0.1977 S13: 0.1019
REMARK 3 S21: 0.1923 S22: 0.0337 S23: 0.0002
REMARK 3 S31: -0.1883 S32: -0.1407 S33: -0.0178
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 2XQJ 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-45264.
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 : 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 : 31042
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 49.30
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.2
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.90
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.7
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.20
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 77.91000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.91000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.14000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.91000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.14000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.91000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.14000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.91000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.14000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.91000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.14000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.91000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.14000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.91000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.14000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.91000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.91000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.14000
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: 48980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 160470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -437.8 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 A1534 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 OE2 GLU A 497 O HOH A 2306 2.13
REMARK 500 OG1 THR A 508 O HOH A 2317 1.98
REMARK 500 O HOH A 2304 O HOH A 2313 2.06
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 CL CL A 1537 O HOH A 2311 7555 2.10
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 404 CG GLU A 404 CD 0.103
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 CYS A 66 CA - CB - SG ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = -3.4 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 -0.50 77.98
REMARK 500 LYS A 51 130.26 129.91
REMARK 500 ASP A 54 176.86 114.84
REMARK 500 ALA A 58 65.72 -114.02
REMARK 500 ASN A 63 130.56 -38.05
REMARK 500 LYS A 103 126.61 -32.00
REMARK 500 ASN A 106 57.09 -148.15
REMARK 500 ALA A 162 70.92 -161.21
REMARK 500 SER A 198 -125.53 60.98
REMARK 500 ARG A 254 -159.68 -139.53
REMARK 500 GLU A 255 -64.40 -120.10
REMARK 500 ASP A 297 -78.39 -136.28
REMARK 500 ASP A 324 52.97 -118.05
REMARK 500 ASP A 378 -32.34 -160.12
REMARK 500 ASP A 379 142.23 -35.34
REMARK 500 PHE A 398 -57.88 -128.32
REMARK 500 ARG A 453 9.89 -59.87
REMARK 500 THR A 496 -79.02 92.48
REMARK 500 GLU A 506 -80.40 -91.88
REMARK 500 PHE A 525 -61.89 -101.16
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 20.6 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 VX A 1530
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 MG A1550 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2004 O
REMARK 620 2 HOH A2091 O 138.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1533 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 443 OE1
REMARK 620 2 HOH A2259 O 76.0
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 GLY A1551
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 A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1550
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 241 RESIDUES 1545 TO 1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
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: 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: 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: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY RACEMIC VX
DBREF 2XQJ A 3 529 UNP P06276 CHLE_HUMAN 31 557
SEQADV 2XQJ GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XQJ GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XQJ GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XQJ 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 A1551 5
HET VX A1530 6
HET SO4 A1531 5
HET SO4 A1532 5
HET NA A1533 1
HET K A1534 1
HET CA A1535 1
HET CL A1536 1
HET CL A1537 1
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 NA A1548 1
HET CA A1549 1
HET MG A1550 1
HETNAM GLY GLYCINE
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM K POTASSIUM ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM MG MAGNESIUM ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 GLY C2 H5 N O2
FORMUL 3 VX C3 H9 O3 P
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 K K 1+
FORMUL 7 CA 2(CA 2+)
FORMUL 8 CL 2(CL 1-)
FORMUL 9 NAG 8(C8 H15 N O6)
FORMUL 10 FUL 2(C6 H12 O5)
FORMUL 11 MG MG 2+
FORMUL 12 HOH *346(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 GLY A 149 LEU A 154 1 6
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 PRO A 211 PHE A 217 5 7
HELIX 10 10 SER A 235 GLY A 251 1 17
HELIX 11 11 ASN A 256 LYS A 267 1 12
HELIX 12 12 ASP A 268 ALA A 277 1 10
HELIX 13 13 MET A 302 GLY A 310 1 9
HELIX 14 14 GLY A 326 GLY A 333 5 8
HELIX 15 15 THR A 346 PHE A 358 1 13
HELIX 16 16 SER A 362 THR A 374 1 13
HELIX 17 17 GLU A 383 PHE A 398 1 16
HELIX 18 18 PHE A 398 GLU A 411 1 14
HELIX 19 19 PRO A 431 GLY A 435 5 5
HELIX 20 20 GLU A 441 PHE A 446 1 6
HELIX 21 21 GLY A 447 GLU A 451 5 5
HELIX 22 22 GLU A 451 GLN A 455 5 5
HELIX 23 23 THR A 457 GLY A 478 1 22
HELIX 24 24 ARG A 515 PHE A 525 1 11
HELIX 25 25 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
SHEET 1 AC 2 SER A 64 CYS A 65 0
SHEET 2 AC 2 LEU A 88 SER A 89 1 N SER A 89 O SER A 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.08
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.11
LINK ND2 ASN A 57 C1 NAG A1542 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A1541 1555 1555 1.45
LINK ND2 ASN A 241 C1 NAG A1545 1555 1555 1.47
LINK ND2 ASN A 256 C1 NAG A1544 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A1538 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A1543 1555 1555 1.45
LINK NA NA A1533 O HOH A2259 1555 1555 2.44
LINK NA NA A1533 OE1 GLU A 443 1555 1555 3.01
LINK O6 NAG A1538 C1 FUL A1540 1555 1555 1.46
LINK O4 NAG A1538 C1 NAG A1539 1555 1555 1.43
LINK O6 NAG A1545 C1 FUL A1547 1555 1555 1.44
LINK O4 NAG A1545 C1 NAG A1546 1555 1555 1.48
LINK CA CA A1549 O HOH A2102 1555 1555 2.72
LINK MG MG A1550 O HOH A2091 1555 1555 1.82
LINK MG MG A1550 O HOH A2004 1555 1555 2.35
CISPEP 1 ALA A 101 PRO A 102 0 -0.26
CISPEP 2 VAL A 377 ASP A 378 0 -11.03
SITE 1 AC1 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC1 5 LYS A 131
SITE 1 AC2 6 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC2 6 TRP A 231 HIS A 438
SITE 1 AC3 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC4 4 HIS A 372 PHE A 521 PHE A 525 HOH A2337
SITE 1 AC5 2 GLU A 443 HOH A2259
SITE 1 AC6 1 PHE A 525
SITE 1 AC7 3 THR A 512 HOH A2305 HOH A2311
SITE 1 AC8 4 ASN A 106 ASN A 188 LYS A 190 HOH A2339
SITE 1 AC9 1 ASN A 57
SITE 1 BC1 3 ARG A 465 ASN A 485 HOH A2280
SITE 1 BC2 2 ASN A 256 HOH A2341
SITE 1 BC3 2 ASN A 85 HOH A2102
SITE 1 BC4 2 HOH A2004 HOH A2091
SITE 1 BC5 7 GLU A 238 ASN A 241 ASN A 245 PHE A 278
SITE 2 BC5 7 PRO A 281 HOH A2342 HOH A2344
SITE 1 BC6 4 GLY A 336 SER A 338 ASN A 341 ASN A 342
CRYST1 155.820 155.820 128.280 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 0.006418 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006418 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007795 0.00000
TER 4247 VAL A 529
MASTER 719 0 22 25 16 0 18 6 4753 1 174 41
END |