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HEADER HYDROLASE 12-JUN-12 4AXB
TITLE CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE
TITLE 2 IN COMPLEX WITH 2-PAM
CAVEAT 4AXB ATOM C1 OF NAG A1548 HAS INCORRECT CHIRALITY
CAVEAT 2 4AXB ATOM C2 OF NAG A1548 HAS INCORRECT CHIRALITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 31-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, BUTYRYLCHOLINE ESTERASE,
COMPND 6 CHOLINE ESTERASE II, PSEUDOCHOLINESTERASE;
COMPND 7 EC: 3.1.1.8;
COMPND 8 ENGINEERED: 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, AGING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WANDHAMMER,M.DE KONING,D.NOORT,M.GOELDNER,F.NACHON
REVDAT 1 29-AUG-12 4AXB 0
JRNL AUTH M.WANDHAMMER,M.DE KONING,M.VAN GROL,M.LOIODICE,L.SAUREL,
JRNL AUTH 2 D.NOORT,M.GOELDNER,F.NACHON
JRNL TITL A STEP TOWARD THE REACTIVATION OF AGED CHOLINESTERASES -
JRNL TITL 2 CRYSTAL STRUCTURE OF LIGANDS BINDING TO AGED HUMAN
JRNL TITL 3 BUTYRYLCHOLINESTERASE
JRNL REF CHEM.BIOL.INTERACT 2012
JRNL REFN ESSN 1872-7786
JRNL DOI 10.1016/J.CBI.2012.08.005
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) : 110.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.55
REMARK 3 NUMBER OF REFLECTIONS : 29428
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) : 0.17070
REMARK 3 R VALUE (WORKING SET) : 0.16808
REMARK 3 FREE R VALUE : 0.22117
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1563
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) : 2.398
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.460
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2123
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.206
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.265
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 175
REMARK 3 SOLVENT ATOMS : 356
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.713
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27
REMARK 3 B22 (A**2) : 0.27
REMARK 3 B33 (A**2) : -0.54
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): 0.281
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.254
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4570 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6230 ; 1.998 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 545 ; 7.099 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;36.941 ;24.190
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 719 ;16.860 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.911 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.140 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3497 ; 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): 2651 ; 1.122 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4292 ; 2.045 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1919 ; 3.310 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1928 ; 5.261 ; 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 : 5
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): -22.8550 -29.2780 -44.9990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1908 T22: 0.0828
REMARK 3 T33: 0.1558 T12: -0.0800
REMARK 3 T13: -0.0913 T23: -0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 0.7237 L22: 1.3486
REMARK 3 L33: 0.9340 L12: -0.1336
REMARK 3 L13: 0.6680 L23: 0.1627
REMARK 3 S TENSOR
REMARK 3 S11: -0.1221 S12: 0.1887 S13: -0.1156
REMARK 3 S21: -0.5003 S22: 0.1084 S23: 0.1081
REMARK 3 S31: 0.0257 S32: -0.0606 S33: 0.0138
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): -15.2610 -31.2800 -33.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0954 T22: 0.0354
REMARK 3 T33: 0.2265 T12: -0.0280
REMARK 3 T13: -0.0178 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.1375 L22: 0.4561
REMARK 3 L33: 0.7905 L12: 0.1669
REMARK 3 L13: 0.3486 L23: 0.2679
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: 0.0360 S13: -0.0473
REMARK 3 S21: -0.1585 S22: 0.0868 S23: -0.0376
REMARK 3 S31: -0.0316 S32: 0.0318 S33: -0.0523
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 308
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0700 -42.4150 -31.6730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1011 T22: 0.0515
REMARK 3 T33: 0.3117 T12: 0.0573
REMARK 3 T13: 0.0035 T23: -0.1094
REMARK 3 L TENSOR
REMARK 3 L11: 1.2194 L22: 0.2153
REMARK 3 L33: 1.0033 L12: 0.1278
REMARK 3 L13: -0.4113 L23: 0.8712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0742 S12: -0.0141 S13: -0.2153
REMARK 3 S21: 0.1955 S22: 0.0247 S23: 0.0168
REMARK 3 S31: 0.2900 S32: 0.4416 S33: 0.0496
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 309 A 397
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0080 -42.3190 -7.8350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0760 T22: 0.0549
REMARK 3 T33: 0.2374 T12: -0.0235
REMARK 3 T13: -0.0870 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.9787 L22: 0.3622
REMARK 3 L33: 0.6583 L12: 0.2256
REMARK 3 L13: 0.4706 L23: -0.3277
REMARK 3 S TENSOR
REMARK 3 S11: 0.1453 S12: -0.1537 S13: -0.1482
REMARK 3 S21: 0.0187 S22: 0.0905 S23: -0.0708
REMARK 3 S31: 0.0838 S32: -0.1382 S33: -0.2357
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 398 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4790 -24.6150 -13.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.0390 T22: 0.0595
REMARK 3 T33: 0.2103 T12: 0.0009
REMARK 3 T13: -0.0197 T23: -0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 0.4515 L22: 1.1136
REMARK 3 L33: 0.8994 L12: -0.0160
REMARK 3 L13: 0.2186 L23: 0.0589
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: -0.1074 S13: 0.0324
REMARK 3 S21: 0.0346 S22: 0.0200 S23: 0.0498
REMARK 3 S31: -0.0709 S32: -0.1000 S33: -0.0186
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4AXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-12.
REMARK 100 THE PDBE ID CODE IS EBI-52794.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 63
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MAR225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29874
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 110.27
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 8.8
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.60
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) : 2.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.0
REMARK 200 R MERGE FOR SHELL (I) : 0.34
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 60.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 2.1 M AMMONIUM SULFATE, 100 MM MES BUFFER PH 6.5. THEN
REMARK 280 SOAKED IN 20% GLYCEROL
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 77.97500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.97500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.95000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.97500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.95000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.97500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.95000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.97500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.95000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.97500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.95000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.97500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.95000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.97500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.95000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.97500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.97500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.95000
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: 54870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 156950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.6 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 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 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 O TRP A 376 O HOH A 2241 2.05
REMARK 500 N THR A 496 O HOH A 2317 2.03
REMARK 500 O2 SO4 A 1531 O HOH A 2269 1.93
REMARK 500 O HOH A 2229 O HOH A 2230 1.92
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 K K A 1538 K K A 1538 5555 1.93
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 VAL A 436 CB VAL A 436 CG2 0.135
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 219 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU A 236 CA - CB - CG ANGL. DEV. = -14.0 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 -4.71 80.51
REMARK 500 LYS A 51 147.13 99.57
REMARK 500 ASP A 54 -179.03 88.92
REMARK 500 ALA A 58 64.46 -103.48
REMARK 500 LYS A 103 120.99 -32.63
REMARK 500 ASN A 106 58.50 -155.24
REMARK 500 PHE A 118 6.65 58.10
REMARK 500 ALA A 162 72.46 -158.22
REMARK 500 ASP A 297 -80.80 -134.37
REMARK 500 PHE A 358 56.64 -140.06
REMARK 500 ASP A 378 -34.53 -143.46
REMARK 500 ASP A 379 143.30 -30.23
REMARK 500 PHE A 398 -56.71 -133.10
REMARK 500 ASN A 485 48.61 -109.87
REMARK 500 THR A 496 -84.47 87.16
REMARK 500 GLU A 506 -79.40 -74.81
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 21.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2356 DISTANCE = 5.42 ANGSTROMS
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 K A1530 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2208 O
REMARK 620 2 TYR A 420 OH 87.1
REMARK 620 3 HOH A2269 O 94.4 73.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K 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 GOL A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FP1 A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1545 BOUND TO ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1544 BOUND TO ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 241 RESIDUES 1548 TO 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1547 BOUND TO ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 341 RESIDUES 1541 TO 1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1546 BOUND TO ASN A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 INCOMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE
REMARK 900 ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (
REMARK 900 DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED
REMARK 900 BY REACTION WITH ECHOTHIOPHATE
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: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
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: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
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: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH SULFATE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH VX
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VX
REMARK 900 RELATED ID: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VR
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2Y1K RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (12H SOAK): PHOSPHOSERINE ADDUCT
REMARK 900 RELATED ID: 4AQD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE
DBREF 4AXB A 3 529 UNP P06276 CHLE_HUMAN 31 557
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 SBG 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 GLN 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 ASN 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
MODRES 4AXB SBG A 198 SER O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HET SBG A 198 1
HET K A1530 1
HET SO4 A1531 5
HET GOL A1532 6
HET GOL A1533 6
HET CL A1534 1
HET FP1 A1535 10
HET CL A1536 1
HET CL A1537 1
HET K A1538 1
HET SO4 A1539 5
HET GOL A1540 6
HET NAG A1541 14
HET NAG A1542 14
HET FUL A1543 10
HET NAG A1544 14
HET NAG A1545 14
HET NAG A1546 14
HET NAG A1547 14
HET NAG A1548 14
HET NAG A1549 14
HET FUL A1550 10
HETNAM SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HETNAM K POTASSIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM FP1 N-HYDROXY-1-(1-METHYLPYRIDIN-2(1H)-YLIDENE)
HETNAM 2 FP1 METHANAMINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 1 SBG C4 H10 N O5 P
FORMUL 2 K 2(K 1+)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 CL 3(CL 1-)
FORMUL 6 FP1 C7 H10 N2 O
FORMUL 7 NAG 8(C8 H15 N O6)
FORMUL 8 FUL 2(C6 H12 O5)
FORMUL 9 HOH *356(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 ALA A 199 SER A 210 1 12
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 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
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 GLY A 196 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 2.09
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.07
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.08
LINK ND2 ASN A 57 C1 NAG A1545 1555 1555 1.48
LINK ND2 ASN A 106 C1 NAG A1544 1555 1555 1.46
LINK N SBG A 198 C GLU A 197 1555 1555 1.34
LINK C SBG A 198 N ALA A 199 1555 1555 1.33
LINK ND2 ASN A 241 C1 NAG A1548 1555 1555 1.47
LINK ND2 ASN A 256 C1 NAG A1547 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A1541 1555 1555 1.43
LINK ND2 ASN A 485 C1 NAG A1546 1555 1555 1.45
LINK K K A1530 O HOH A2269 1555 1555 2.77
LINK K K A1530 OH TYR A 420 1555 1555 3.11
LINK K K A1530 O HOH A2208 1555 1555 3.44
LINK O4 NAG A1541 C1 NAG A1542 1555 1555 1.41
LINK O6 NAG A1541 C1 FUL A1543 1555 1555 1.45
LINK O4 NAG A1548 C1 NAG A1549 1555 1555 1.46
LINK O6 NAG A1548 C1 FUL A1550 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 5.81
CISPEP 2 VAL A 377 ASP A 378 0 -27.57
SITE 1 AC1 2 TYR A 420 HOH A2269
SITE 1 AC2 5 ARG A 509 ARG A 515 HOH A2269 HOH A2339
SITE 2 AC2 5 HOH A2340
SITE 1 AC3 2 LYS A 45 LYS A 105
SITE 1 AC4 4 LEU A 18 TRP A 98 ASP A 129 LYS A 131
SITE 1 AC5 1 ASN A 414
SITE 1 AC6 6 TRP A 82 GLY A 115 GLY A 116 GLU A 197
SITE 2 AC6 6 HIS A 438 HOH A2341
SITE 1 AC7 3 ARG A 347 HOH A2229 HOH A2230
SITE 1 AC8 1 THR A 512
SITE 1 AC9 2 HIS A 372 PHE A 525
SITE 1 BC1 3 HIS A 372 SER A 524 LYS A 528
SITE 1 BC2 7 TRP A 231 THR A 234 GLU A 238 ARG A 242
SITE 2 BC2 7 VAL A 288 HOH A2190 HOH A2192
SITE 1 BC3 3 ARG A 14 ASN A 57 HOH A2348
SITE 1 BC4 3 ASN A 106 ASN A 188 LYS A 190
SITE 1 BC5 7 TYR A 237 ASN A 241 ASN A 245 PHE A 278
SITE 2 BC5 7 PRO A 281 HOH A2187 HOH A2353
SITE 1 BC6 1 ASN A 256
SITE 1 BC7 6 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 2 BC7 6 ASN A 342 HOH A2343
SITE 1 BC8 2 ARG A 465 ASN A 485
CRYST1 155.950 155.950 127.900 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 0.006412 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006412 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007819 0.00000
TER 4262 VAL A 529
MASTER 701 0 22 24 16 0 22 6 4792 1 198 41
END |