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HEADER HYDROLASE 28-AUG-06 2J4C
TITLE STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 10MM HGCL2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 4 BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;
COMPND 5 CHAIN: A;
COMPND 6 EC: 3.1.1.8;
COMPND 7 MUTATION: YES;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: ATYPICAL BOND BETWEEN CATALYTIC RESIDUE
COMPND 10 SER198 AND LIGAND BTY5 (BUTYRATE)
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 3 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN
KEYWDS HYDROLASE, INHIBITION, GLYCOPROTEIN, POLYMORPHISM,
KEYWDS 2 INORGANIC MERCURY, CHOLINESTERASE, SERINE ESTERASE,
KEYWDS 3 DISEASE MUTATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.COLLETIER,M.F.FRASCO,F.CARVALHO,L.GUILHERMINO,J.STOJAN,
AUTHOR 2 D.FOURNIER,M.WEIK
REVDAT 1 27-MAR-07 2J4C 0
JRNL AUTH M.F.FRASCO,J.P.COLLETIER,M.WEIK,F.CARVALHO,
JRNL AUTH 2 L.GUILHERMINO,J.STOJAN,D.FOURNIER
JRNL TITL MECHANISMS OF CHOLINESTERASE INHIBITION BY
JRNL TITL 2 INORGANIC MERCURY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 6821362.51
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 35972
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1789
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1772
REMARK 3 BIN R VALUE (WORKING SET) : 0.347
REMARK 3 BIN FREE R VALUE : 0.398
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.4
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4169
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 178
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.86
REMARK 3 B22 (A**2) : -6.86
REMARK 3 B33 (A**2) : 13.71
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.52
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.63
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.6
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.1
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.48 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.61 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.84 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.98 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.304861
REMARK 3 BSOL : 39.0382
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 4 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 PARAMETER FILE 5 : LIGAND.PARAM
REMARK 3 TOPOLOGY FILE 5 : LIGAND.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 1, 2, 3, 378, 479,
REMARK 3 455 MISSING
REMARK 4
REMARK 4 2J4C COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 29-AUG-2006.
REMARK 100 THE EBI ID CODE IS EBI-27952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-2005
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU R-AXIS IV
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35972
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.75
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.29
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 4.36
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.97
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.51
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.29
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE,
REMARK 280 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, 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 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1/2-X,1/2-Y,1/2+Z
REMARK 290 11555 1/2-Y,1/2+X,1/2+Z
REMARK 290 12555 1/2+Y,1/2-X,1/2+Z
REMARK 290 13555 1/2-X,1/2+Y,1/2-Z
REMARK 290 14555 1/2+X,1/2-Y,1/2-Z
REMARK 290 15555 1/2+Y,1/2+X,1/2-Z
REMARK 290 16555 1/2-Y,1/2-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 76.88000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.29000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 76.88000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.29000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 76.88000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.29000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 76.88000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.29000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 76.88000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.29000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 76.88000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.29000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 76.88000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.29000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 76.88000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 76.88000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.29000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 HG HG A1540 LIES ON A SPECIAL POSITION.
REMARK 375 HOH Z 364 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 ALA
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 378
REMARK 465 ASP A 379
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 30 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 VAL A 136 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 LEU A 156 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 LEU A 318 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG A 453 N - CA - C ANGL. DEV. = -14.9 DEGREES
REMARK 500 ASP A 454 N - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 TYR A 456 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLU A 482 N - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 THR A 483 N - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 OG SER A 198 C4 BUA A 1547 2.16
REMARK 500 ND1 HIS A 372 O1 SO4 A 1549 2.17
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 198 -119.42 51.93
REMARK 500 ASP A 454 23.13 6.00
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM HG HG A1540 THE COORDINATION ANGLES ARE:
REMARK 600 1 MET 511A CE
REMARK 600 2 MET 511A CE 114.7
REMARK 600 3 MET 511A CG 152.1 58.3
REMARK 600 4 MET 511A SD 124.7 34.6 33.3
REMARK 600 5 MET 511A CG 59.1 154.1 139.6 170.8
REMARK 600 6 MET 511A SD 35.1 125.7 172.1 153.9 33.9
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM HG HG A1541 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 423A ND1
REMARK 600 2 ASN 504A OD1 102.2
REMARK 600 3 THR 505A OG1 90.4 74.0
REMARK 600 1 2
REMARK 600
REMARK 600 FOR METAL ATOM HG HG A1542 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 77A NE2
REMARK 600 2 HOH 328W O 86.2
REMARK 600 3 HOH 94W O 116.1 149.8
REMARK 600 1 2
REMARK 600
REMARK 600 FOR METAL ATOM HG HG A3003 THE COORDINATION ANGLES ARE:
REMARK 600 1 SO4 1549A S
REMARK 600 2 SO4 1549A O1 29.2
REMARK 600 3 SO4 1549A O3 29.3 55.6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: FUC BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: FUC BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: HG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: HG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: HG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BUA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: MES BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
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
REMARK 900 HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
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: 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: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYL CHOLINESTERASE
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: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINEDBY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)
REMARK 900 OBTAINED BY REACTION WITH ECHOTHIOPHATE
DBREF 2J4C A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2J4C GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2J4C GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2J4C GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2J4C ALA 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 CSS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU 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 ALA SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
MODRES 2J4C CSS A 66 CYS S-METHYLCYSTEINE
HET NAG A1530 14
HET NAG A1531 14
HET NAG A1533 14
HET NAG A1534 14
HET FUC A1535 10
HET NAG A1536 14
HET NAG A1537 14
HET NAG A1538 14
HET CL A3001 1
HET CL A3002 1
HET CL A1539 1
HET HG A1540 1
HET HG A3003 1
HET HG A1541 1
HET HG A1542 1
HET SO4 A1543 5
HET GOL A1544 6
HET GOL A1545 6
HET GOL A1546 6
HET BUA A1547 6
HET MES A1548 12
HET SO4 A1549 5
HET CSS A 66 7
HETNAM SO4 SULFATE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
HETNAM CSS S-MERCAPTOCYSTEINE
HETNAM BUA BUTANOIC ACID
HETNAM GOL GLYCEROL
HETNAM FUC FUCOSE
HETNAM HG MERCURY (II) ION
HETNAM CL CHLORIDE ION
FORMUL 2 MES C6 H13 N1 O4 S1
FORMUL 3 BUA C4 H8 O2
FORMUL 4 NAG 7(C8 H15 N1 O6)
FORMUL 5 CSS C3 H7 N1 O2 S2
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 7 FUC 2(C6 H12 O5)
FORMUL 8 HG 4(HG1 2+)
FORMUL 9 CL 3(CL1 1-)
FORMUL 10 SO4 2(O4 S1 2-)
FORMUL 11 HOH *365(H2 O1)
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 SER A 235 THR A 250 1 16
HELIX 10 10 ASN A 256 LYS A 267 1 12
HELIX 11 11 ASP A 268 ALA A 277 1 10
HELIX 12 12 MET A 302 LEU A 309 1 8
HELIX 13 13 GLY A 326 VAL A 331 1 6
HELIX 14 14 THR A 346 PHE A 358 1 13
HELIX 15 15 SER A 362 THR A 374 1 13
HELIX 16 16 GLU A 383 PHE A 398 1 16
HELIX 17 17 PHE A 398 GLU A 411 1 14
HELIX 18 18 PRO A 431 GLY A 435 5 5
HELIX 19 19 GLU A 441 PHE A 446 1 6
HELIX 20 20 GLY A 447 GLU A 451 5 5
HELIX 21 21 THR A 457 GLY A 478 1 22
HELIX 22 22 ARG A 515 SER A 524 1 10
HELIX 23 23 PHE A 525 VAL A 529 5 5
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 TRP A 56 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 MET A 16 THR A 19 0
SHEET 2 AB11 THR A 24 PRO A 32 -1 O VAL A 25 N LEU A 18
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 2.00
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.03
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.02
LINK ND2 ASN A 57 C1 NAG A1537 1555 1555 1.45
LINK C CYS A 65 N CSS A 66 1555 1555 1.33
LINK C CSS A 66 N GLN A 67 1555 1555 1.32
LINK ND2 ASN A 106 C1 NAG A1536 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG A1530 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A1533 1555 1555 1.45
LINK ND2 ASN A 485 C1 NAG A1538 1555 1555 1.49
LINK O4 NAG A1530 C1 NAG A1531 1555 1555 1.39
LINK O6 NAG A1530 C1 FUC A1532 1555 1555 1.40
LINK O4 NAG A1533 C1 NAG A1534 1555 1555 1.39
LINK O6 NAG A1533 C1 FUC A1535 1555 1555 1.40
LINK HG HG A1540 CG MET A 511 1555 1555 2.83
LINK HG HG A1540 SD MET A 511 1555 1555 3.16
LINK HG HG A1540 CE MET A 511 1555 1555 2.90
LINK HG HG A1540 CE MET A 511 1555 7556 2.92
LINK HG HG A1540 CG MET A 511 1555 7556 2.88
LINK HG HG A1540 SD MET A 511 1555 7556 3.22
LINK HG HG A1541 OD1 ASN A 504 1555 1555 2.96
LINK HG HG A1541 OG1 THR A 505 1555 1555 3.12
LINK HG HG A1541 ND1 HIS A 423 1555 1555 2.37
LINK HG HG A1542 O HOH Z 45 1555 1555 2.88
LINK HG HG A1542 O HOH Z 284 1555 1555 3.12
LINK HG HG A1542 NE2 HIS A 77 1555 1555 2.75
LINK HG HG A3003 O1 SO4 A1549 1555 1555 2.68
LINK HG HG A3003 O3 SO4 A1549 1555 1555 2.19
LINK HG HG A3003 S SO4 A1549 1555 1555 2.89
CISPEP 1 ALA A 101 PRO A 102 0 -0.06
SITE 1 AC1 5 ASN A 241 ASN A 245 HOH Z 175 HOH Z 340
SITE 2 AC1 5 HOH Z 342
SITE 1 AC2 2 HOH Z 341 HOH Z 342
SITE 1 AC3 5 ASN A 245 LEU A 249 PHE A 278 HOH Z 177
SITE 2 AC3 5 HOH Z 344
SITE 1 AC4 4 SER A 338 ASN A 341 ASN A 342 HOH Z 345
SITE 1 AC5 1 GLY A 336
SITE 1 AC6 1 HOH Z 346
SITE 1 AC7 4 ASN A 106 ASN A 188 HOH Z 347 HOH Z 349
SITE 1 AC9 4 ARG A 465 ASN A 485 HOH Z 350 HOH Z 351
SITE 1 BC1 2 ARG A 347 HOH Z 237
SITE 1 BC2 2 GLU A 80 HOH Z 74
SITE 1 BC3 2 THR A 488 THR A 508
SITE 1 BC4 1 MET A 511
SITE 1 BC6 3 HIS A 423 ASN A 504 THR A 505
SITE 1 BC7 3 HIS A 77 MET A 81 HOH Z 45
SITE 1 BC8 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 BC9 6 LEU A 18 LEU A 29 TYR A 61 TRP A 98
SITE 2 BC9 6 ASP A 129 LYS A 131
SITE 1 CC1 5 TRP A 231 THR A 234 GLU A 238 ARG A 242
SITE 2 CC1 5 SER A 287
SITE 1 CC2 2 HOH Z 355 HOH Z 358
SITE 1 CC3 8 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 CC3 8 LEU A 286 HIS A 438 HOH Z 198 HOH Z 356
SITE 1 CC4 6 LYS A 323 TYR A 420 ARG A 509 LEU A 514
SITE 2 CC4 6 ARG A 515 HOH Z 314
SITE 1 CC5 7 SER A 368 PHE A 371 HIS A 372 PHE A 521
SITE 2 CC5 7 PHE A 525 LYS A 528 HOH Z 329
CRYST1 153.760 153.760 128.580 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 0.006504 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007777 0.00000
TER 4177 VAL A 529
MASTER 475 0 23 23 14 0 28 6 4712 1 198 41
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