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HEADER HYDROLASE 27-JUL-10 2XMD
TITLE G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 ECHOTHIOPHATE
CAVEAT 2XMD VAL A 361 C-ALPHA IS PLANAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 6 BUTYRYLCHOLINESTERASE, 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
KEYWDS GLYCOPROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,E.CARLETTI,M.WANDHAMMER,Y.NICOLET,L.M.SCHOPFER,P.MASSON,
AUTHOR 2 O.LOCKRIDGE
REVDAT 1 01-DEC-10 2XMD 0
JRNL AUTH F.NACHON,E.CARLETTI,M.WANDHAMMER,Y.NICOLET,L.M.SCHOPFER,
JRNL AUTH 2 P.MASSON,O.LOCKRIDGE
JRNL TITL X-RAY CRYSTALLOGRAPHIC SNAPSHOTS OF REACTION INTERMEDIATES
JRNL TITL 2 IN THE G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE, A NERVE
JRNL TITL 3 AGENT TARGET ENGINEERED INTO A CATALYTIC BIOSCAVENGE
JRNL REF BIOCHEM.J. 2010
JRNL REFN ESSN 1470-8728
JRNL DOI 10.1042/BJ20101648
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.03
REMARK 3 NUMBER OF REFLECTIONS : 32166
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) : 0.17154
REMARK 3 R VALUE (WORKING SET) : 0.17006
REMARK 3 FREE R VALUE : 0.21417
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.2
REMARK 3 FREE R VALUE TEST SET COUNT : 1050
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.300
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.359
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.206
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.305
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.079
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11
REMARK 3 B22 (A**2) : -0.11
REMARK 3 B33 (A**2) : 0.21
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): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.267
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4533 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6179 ; 2.090 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 7.818 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;36.854 ;24.078
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 706 ;18.046 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.703 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 680 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3450 ; 0.010 ; 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): 2635 ; 1.015 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4260 ; 1.839 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1898 ; 3.292 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1917 ; 5.258 ; 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 64
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9570 27.6250 17.5510
REMARK 3 T TENSOR
REMARK 3 T11: 0.4744 T22: 0.3852
REMARK 3 T33: 0.1692 T12: -0.0506
REMARK 3 T13: 0.1486 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 2.4269 L22: 3.0582
REMARK 3 L33: 1.1319 L12: -1.2540
REMARK 3 L13: -0.4065 L23: -0.2748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: 0.6942 S13: -0.0886
REMARK 3 S21: -0.8342 S22: -0.1002 S23: -0.2130
REMARK 3 S31: 0.1769 S32: 0.1308 S33: 0.0395
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 65 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1280 43.5050 32.4430
REMARK 3 T TENSOR
REMARK 3 T11: 0.2527 T22: 0.1995
REMARK 3 T33: 0.2133 T12: -0.0689
REMARK 3 T13: 0.0985 T23: 0.0818
REMARK 3 L TENSOR
REMARK 3 L11: 2.0219 L22: 0.6797
REMARK 3 L33: 4.3547 L12: 0.8924
REMARK 3 L13: 1.3930 L23: 0.6784
REMARK 3 S TENSOR
REMARK 3 S11: -0.1188 S12: -0.0026 S13: 0.2348
REMARK 3 S21: -0.1738 S22: 0.0530 S23: -0.0536
REMARK 3 S31: -0.3183 S32: 0.2141 S33: 0.0658
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 93 A 230
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4860 25.7270 30.5850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1815 T22: 0.1237
REMARK 3 T33: 0.0446 T12: -0.0461
REMARK 3 T13: 0.0442 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 1.6224 L22: 2.0740
REMARK 3 L33: 1.6134 L12: 0.1047
REMARK 3 L13: -0.2537 L23: -0.0883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 0.2042 S13: 0.0058
REMARK 3 S21: -0.3068 S22: 0.0687 S23: -0.0426
REMARK 3 S31: 0.1112 S32: 0.0155 S33: -0.0426
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 231 A 289
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2260 48.5170 29.7100
REMARK 3 T TENSOR
REMARK 3 T11: 0.5078 T22: 0.2728
REMARK 3 T33: 0.4412 T12: 0.0384
REMARK 3 T13: 0.0331 T23: 0.1281
REMARK 3 L TENSOR
REMARK 3 L11: 2.6173 L22: 3.4755
REMARK 3 L33: 5.9768 L12: -0.5757
REMARK 3 L13: 0.6498 L23: -3.3016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.2441 S13: 0.5801
REMARK 3 S21: -0.1063 S22: 0.2082 S23: 0.3105
REMARK 3 S31: -0.8841 S32: -0.4473 S33: -0.2109
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 290 A 332
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4560 29.8590 42.0040
REMARK 3 T TENSOR
REMARK 3 T11: 0.1108 T22: 0.1360
REMARK 3 T33: 0.0880 T12: -0.0104
REMARK 3 T13: 0.0541 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 1.3989 L22: 1.4390
REMARK 3 L33: 1.3100 L12: 0.7330
REMARK 3 L13: 0.0014 L23: 0.1475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: 0.0310 S13: 0.1430
REMARK 3 S21: -0.0643 S22: 0.0557 S23: 0.1992
REMARK 3 S31: -0.0086 S32: -0.0910 S33: -0.0918
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 333 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3800 31.4690 53.1400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.2190
REMARK 3 T33: 0.0584 T12: -0.0332
REMARK 3 T13: 0.0562 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.3942 L22: 2.4990
REMARK 3 L33: 1.3627 L12: -0.1772
REMARK 3 L13: -0.3881 L23: 0.3298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0809 S12: -0.2847 S13: 0.1444
REMARK 3 S21: 0.1912 S22: 0.0424 S23: -0.0571
REMARK 3 S31: -0.0690 S32: 0.1578 S33: -0.1233
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XMD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-06
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 : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33216
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 28.10
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 7.5
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.5
REMARK 200 R MERGE FOR SHELL (I) : 0.24
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.00
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, 2-(N
REMARK 280 -MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.44000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.76500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.44000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.76500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.44000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.76500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.44000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.76500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.44000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.76500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.44000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.76500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.44000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.76500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.44000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.44000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.76500
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: 55860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 156080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.2 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 127.53000
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 127.53000
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 127.53000
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 127.53000
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 HOH A2042 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, GLY 145 TO HIS
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 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 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 1569 UNK UNX A 1570 1.45
REMARK 500 UNK UNX A 1540 UNK UNX A 1542 1.55
REMARK 500 UNK UNX A 1568 UNK UNX A 1569 1.66
REMARK 500 OG1 THR A 508 O HOH A 2263 1.80
REMARK 500 UNK UNX A 1571 UNK UNX A 1572 1.82
REMARK 500 O HOH A 2243 O HOH A 2244 1.89
REMARK 500 UNK UNX A 1539 UNK UNX A 1540 1.89
REMARK 500 UNK UNX A 1570 UNK UNX A 1571 1.98
REMARK 500 UNK UNX A 1544 UNK UNX A 1570 2.02
REMARK 500 UNK UNX A 1548 UNK UNX A 1549 2.02
REMARK 500 UNK UNX A 1552 UNK UNX A 1553 2.07
REMARK 500 UNK UNX A 1569 UNK UNX A 1571 2.09
REMARK 500 UNK UNX A 1551 UNK UNX A 1552 2.11
REMARK 500 CD1 ILE A 99 O HOH A 2010 2.13
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 CA CA A 1537 CA CA A 1537 5556 1.55
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 0.094
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 219 CG - CD - NE ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO A 359 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 424 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 515 NE - CZ - NH1 ANGL. DEV. = 3.9 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 -4.42 77.67
REMARK 500 LYS A 51 135.48 108.06
REMARK 500 ASP A 54 171.70 75.02
REMARK 500 ALA A 58 73.23 -105.03
REMARK 500 ASP A 70 104.82 -59.49
REMARK 500 LYS A 103 130.62 -36.50
REMARK 500 ASN A 106 60.91 -162.01
REMARK 500 HIS A 117 17.80 53.13
REMARK 500 ALA A 162 65.83 -162.84
REMARK 500 SER A 198 -119.94 54.52
REMARK 500 ASP A 297 -81.20 -137.16
REMARK 500 THR A 315 -179.89 -172.94
REMARK 500 VAL A 361 83.23 37.27
REMARK 500 ASP A 378 -110.08 -101.84
REMARK 500 ASP A 379 -27.37 -162.50
REMARK 500 PHE A 398 -50.91 -129.84
REMARK 500 ASN A 485 43.83 -109.86
REMARK 500 GLN A 486 54.16 37.70
REMARK 500 THR A 496 -70.65 -64.61
REMARK 500 GLU A 506 -86.31 -96.09
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 GLY A 360 VAL A 361 53.28
REMARK 500 VAL A 377 ASP A 378 -40.84
REMARK 500 ASP A 378 ASP A 379 38.67
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 5.9 L L EXPECTING SP3
REMARK 500 PHE A 526 22.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1531
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 CL A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 106 RESIDUES 1557 TO 1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 241 RESIDUES 1563 TO 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 341 RESIDUES 1554 TO 1556
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA4
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 10MM HGCL2
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO- FLUORIDATE (DFP)
REMARK 900 INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH THE SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE INCOMPLEX
REMARK 900 WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED )
REMARK 900 OBTAINED BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA1
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA5
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
REMARK 900 ANALOGUE TA1
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 VX
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 SULFATE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 FLUORIDE ANION
DBREF 2XMD A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2XMD GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XMD HIS A 117 UNP P06276 GLY 145 ENGINEERED MUTATION
SEQADV 2XMD GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XMD GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XMD GLN A 486 UNP P06276 ASN 514 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 HIS
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 SER 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 GLN 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
HET UNX A1538 1
HET UNX A1539 1
HET UNX A1540 1
HET UNX A1541 1
HET UNX A1542 1
HET UNX A1543 1
HET UNX A1544 1
HET UNX A1545 1
HET UNX A1546 1
HET UNX A1547 1
HET UNX A1548 1
HET UNX A1549 1
HET UNX A1550 1
HET UNX A1551 1
HET UNX A1552 1
HET UNX A1553 1
HET UNX A1568 1
HET UNX A1569 1
HET UNX A1570 1
HET UNX A1571 1
HET UNX A1572 1
HET DEP A1530 8
HET SO4 A1531 5
HET CL A1532 1
HET CL A1533 1
HET CL A1534 1
HET BR A1535 1
HET NA A1536 1
HET CA A1537 1
HET NAG A1554 14
HET NAG A1555 14
HET FUL A1556 10
HET NAG A1557 14
HET FUL A1558 10
HET NAG A1559 14
HET NAG A1560 14
HET NAG A1561 14
HET NAG A1562 14
HET NAG A1563 14
HET NAG A1564 14
HET FUC A1565 10
HET CL A1566 1
HET NA A1567 1
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM DEP DIETHYL PHOSPHONATE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM BR BROMIDE ION
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM FUC ALPHA-L-FUCOSE
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 UNX 21(X)
FORMUL 3 DEP C4 H11 O3 P
FORMUL 4 SO4 O4 S 2-
FORMUL 5 CL 4(CL 1-)
FORMUL 6 BR BR 1-
FORMUL 7 NA 2(NA 1+)
FORMUL 8 CA CA 2+
FORMUL 9 NAG 9(C8 H15 N O6)
FORMUL 10 FUL 2(C6 H12 O5)
FORMUL 11 FUC C6 H12 O5
FORMUL 12 HOH *285(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 ARG A 265 1 10
HELIX 12 12 ASP A 268 ALA A 277 1 10
HELIX 13 13 MET A 302 LEU A 309 1 8
HELIX 14 14 GLY A 326 VAL A 331 1 6
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 SER A 524 1 10
HELIX 25 25 PHE A 525 VAL A 529 5 5
SHEET 1 AA 3 ILE A 5 ALA A 7 0
SHEET 2 AA 3 LYS A 12 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA 3 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 2.05
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.09
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.08
LINK ND2 ASN A 57 C1 NAG A1560 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A1557 1555 1555 1.44
LINK OG SER A 198 P DEP A1530 1555 1555 1.64
LINK ND2 ASN A 241 C1 NAG A1563 1555 1555 1.46
LINK ND2 ASN A 256 C1 NAG A1562 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG A1554 1555 1555 1.43
LINK ND2 ASN A 485 C1 NAG A1561 1555 1555 1.43
LINK NA NA A1536 O HOH A2140 1555 1555 3.19
LINK O4 NAG A1554 C1 NAG A1555 1555 1555 1.43
LINK O6 NAG A1554 C1 FUL A1556 1555 1555 1.45
LINK O6 NAG A1557 C1 FUL A1558 1555 1555 1.42
LINK O4 NAG A1557 C1 NAG A1559 1555 1555 1.46
LINK O6 NAG A1563 C1 FUC A1565 1555 1555 1.45
LINK O4 NAG A1563 C1 NAG A1564 1555 1555 1.46
LINK NA NA A1567 UNK UNX A1568 1555 1555 2.95
CISPEP 1 ALA A 101 PRO A 102 0 -0.13
CISPEP 2 ASP A 379 GLN A 380 0 -0.75
SITE 1 AC1 7 GLY A 116 HIS A 117 SER A 198 ALA A 199
SITE 2 AC1 7 TRP A 231 HIS A 438 HOH A2113
SITE 1 AC2 5 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 2 AC2 5 HOH A2276
SITE 1 AC3 4 CYS A 400 PRO A 401 THR A 523 HOH A2194
SITE 1 AC4 2 TYR A 420 HOH A2272
SITE 1 AC5 1 LEU A 236
SITE 1 AC6 2 ASN A 57 HOH A2280
SITE 1 AC7 5 ARG A 465 LYS A 469 ASN A 485 HOH A2281
SITE 2 AC7 5 HOH A2282
SITE 1 AC8 2 ASN A 256 HOH A2283
SITE 1 AC9 9 ASN A 106 ASN A 188 LYS A 190 SER A 191
SITE 2 AC9 9 ARG A 219 LYS A 476 HOH A2232 HOH A2278
SITE 3 AC9 9 HOH A2279
SITE 1 BC1 7 ASN A 241 ASN A 245 LYS A 248 PHE A 278
SITE 2 BC1 7 VAL A 280 PRO A 281 HOH A2284
SITE 1 BC2 3 SER A 338 ASN A 341 ASN A 342
CRYST1 154.880 154.880 127.530 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 0.006457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007841 0.00000
TER 4223 VAL A 529
MASTER 700 0 43 25 14 0 17 6 4705 1 186 41
END |