longtext: 2J4C-pdb

content
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
END