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Database: PDB
Entry: 1FJ2
LinkDB: 1FJ2
Original site: 1FJ2 
HEADER    HYDROLASE                               07-AUG-00   1FJ2              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN ACYL PROTEIN THIOESTERASE 1 AT 1.5 A   
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (ACYL PROTEIN THIOESTERASE 1);                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.4.39;                                                        
COMPND   5 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA HYDROLASE, SERINE HYDROLASE, SAD, ANOMALOUS DIFFRACTION,   
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.DEVEDJIEV,Z.DAUTER,S.KUZNETSOV,T.JONES,Z.DEREWENDA                  
REVDAT   6   04-OCT-17 1FJ2    1       REMARK                                   
REVDAT   5   13-JUL-11 1FJ2    1       VERSN                                    
REVDAT   4   24-FEB-09 1FJ2    1       VERSN                                    
REVDAT   3   12-JUL-05 1FJ2    1       DBREF  REMARK                            
REVDAT   2   01-APR-03 1FJ2    1       JRNL                                     
REVDAT   1   29-NOV-00 1FJ2    0                                                
JRNL        AUTH   Y.DEVEDJIEV,Z.DAUTER,S.R.KUZNETSOV,T.L.JONES,Z.S.DEREWENDA   
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN ACYL PROTEIN THIOESTERASE I   
JRNL        TITL 2 FROM A SINGLE X-RAY DATA SET TO 1.5 A.                       
JRNL        REF    STRUCTURE FOLD.DES.           V.   8  1137 2000              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11080636                                                     
JRNL        DOI    10.1016/S0969-2126(00)00529-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 50223                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1293                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3454                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 465                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.200         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; 0.250               
REMARK   3    ANGLE DISTANCE                  (A) : 0.031 ; 0.400               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.038 ; 0.500               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.013 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.089 ; 0.100               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.180 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.260 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.120 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; 0.300               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 7.000 ; 10.000              
REMARK   3    STAGGERED                 (DEGREES) : 14.700; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 23.300; 25.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.400 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.100 ; 2.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.100 ; 2.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011628.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91374                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 27.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SNB, SHARP, DM                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 30.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28 - 32% OF SATURATED AMMONIUM           
REMARK 280  SULFATE, 0.1 M SODIUM ACETATE, DI-THIO-THREITOL, PH 5.0, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+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       63.94500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 300 REMARK: IN SOLUTION, THERE IS AN EQUILLIBRIUM OF MONOMERIC           
REMARK 300 AND DIMERIC SPECIES OF HUMAN ACYL PROTEIN THIOESTERASE               
REMARK 300 1. BIOLOGICAL UNIT OF THE ENZYME IS STILL UNCERTAIN.                 
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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     GLY A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     ASP A   225                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     ASP B   225                                                      
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  BR     BR B   822     O    HOH B  1079              1.77            
REMARK 500  BR     BR B   822     O    HOH B  1036              1.95            
REMARK 500   OG   SER A    42     O    HOH A   950              1.97            
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  40   CG  -  CD  -  NE  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ARG A  40   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A  40   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    LYS A  45   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG A  54   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 157   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    VAL A 188   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    VAL A 188   N   -  CA  -  CB  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ILE A 224   C   -  N   -  CA  ANGL. DEV. =  20.5 DEGREES          
REMARK 500    PHE B  21   CB  -  CG  -  CD1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ASP B  27   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP B  69   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    MET B 211   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ILE B 224   C   -  N   -  CA  ANGL. DEV. =  25.1 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    ASP A  -4     -179.03    -68.17                                   
REMARK 500    ARG A  13     -160.31    -76.85                                   
REMARK 500    ASN A  59       36.97    -99.69                                   
REMARK 500    SER A 114     -123.27     53.01                                   
REMARK 500    MET A 202     -142.13    -96.45                                   
REMARK 500    ASN B  59       39.66    -96.24                                   
REMARK 500    SER B 114     -126.89     52.35                                   
REMARK 500    MET B 202     -143.40    -98.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH A   902                                                      
REMARK 615     HOH A   973                                                      
REMARK 615     HOH A  1001                                                      
REMARK 615     HOH A  1028                                                      
REMARK 615     HOH A  1034                                                      
REMARK 615     HOH A  1051                                                      
REMARK 615     HOH B   849                                                      
REMARK 615     HOH B   864                                                      
REMARK 615     HOH B   939                                                      
REMARK 615     HOH B  1030                                                      
REMARK 615     HOH B  1035                                                      
REMARK 615     HOH B  1039                                                      
REMARK 615     HOH B  1056                                                      
REMARK 615     HOH B  1063                                                      
REMARK 615     HOH B  1080                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: Active site in Chain A                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ACB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: Active site in Chain B                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 808                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 810                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 812                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 813                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 814                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 815                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 816                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 817                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 818                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 819                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 820                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 821                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 822                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 823                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 824                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 825                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 826                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 827                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 828                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 829                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 830                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 831                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 832                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 833                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 834                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 835                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 836                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 837                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 838                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 839                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 840                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AUO   RELATED DB: PDB                                   
REMARK 900 HUMAN ACYL PROTEIN THIOESTERASE 1 AND CARBOXYLESTERASE FROM          
REMARK 900 PSEUDOMONAS FLUORESCENCE (1AUO) ARE 34% IDENTICAL ACCORDING TO THE   
REMARK 900 SEQUENCE, HOWEVER, OVERALL FOLD OF THE BOTH ENZYMES IS CLOSE WITH    
REMARK 900 R.M.S. VALUE OF 1.34 FOR 212 COMMON C-ALFA ATOMS.                    
DBREF  1FJ2 A    1   225  UNP    O75608   LYPA1_HUMAN      6    230             
DBREF  1FJ2 B    1   225  UNP    O75608   LYPA1_HUMAN      6    230             
SEQADV 1FJ2 GLY A   -7  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 ALA A   -6  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 MET A   -5  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 ASP A   -4  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 PRO A   -3  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 GLU A   -2  UNP  O75608              SEE REMARK 999                 
SEQADV 1FJ2 PHE A   -1  UNP  O75608              SEE REMARK 999                 
SEQRES   1 A  232  GLY ALA MET ASP PRO GLU PHE MET SER THR PRO LEU PRO          
SEQRES   2 A  232  ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL          
SEQRES   3 A  232  ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP          
SEQRES   4 A  232  ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS          
SEQRES   5 A  232  TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU          
SEQRES   6 A  232  ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE          
SEQRES   7 A  232  GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE          
SEQRES   8 A  232  LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN          
SEQRES   9 A  232  GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU          
SEQRES  10 A  232  GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR          
SEQRES  11 A  232  ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA          
SEQRES  12 A  232  LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN          
SEQRES  13 A  232  GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU          
SEQRES  14 A  232  GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET          
SEQRES  15 A  232  PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL          
SEQRES  16 A  232  ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET          
SEQRES  17 A  232  MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL LYS          
SEQRES  18 A  232  GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP                  
SEQRES   1 B  232  GLY ALA MET ASP PRO GLU PHE MET SER THR PRO LEU PRO          
SEQRES   2 B  232  ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL          
SEQRES   3 B  232  ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP          
SEQRES   4 B  232  ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS          
SEQRES   5 B  232  TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU          
SEQRES   6 B  232  ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE          
SEQRES   7 B  232  GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE          
SEQRES   8 B  232  LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN          
SEQRES   9 B  232  GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU          
SEQRES  10 B  232  GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR          
SEQRES  11 B  232  ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA          
SEQRES  12 B  232  LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN          
SEQRES  13 B  232  GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU          
SEQRES  14 B  232  GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET          
SEQRES  15 B  232  PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL          
SEQRES  16 B  232  ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET          
SEQRES  17 B  232  MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL LYS          
SEQRES  18 B  232  GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP                  
HET     BR  A 801       1                                                       
HET     BR  A 804       1                                                       
HET     BR  A 806       1                                                       
HET     BR  A 808       1                                                       
HET     BR  A 809       1                                                       
HET     BR  A 812       1                                                       
HET     BR  A 813       1                                                       
HET     BR  A 816       1                                                       
HET     BR  A 817       1                                                       
HET     BR  A 818       1                                                       
HET     BR  A 823       1                                                       
HET     BR  A 824       1                                                       
HET     BR  A 827       1                                                       
HET     BR  A 828       1                                                       
HET     BR  A 829       1                                                       
HET     BR  A 830       1                                                       
HET     BR  A 831       1                                                       
HET     BR  A 832       1                                                       
HET     BR  A 840       1                                                       
HET     BR  B 802       1                                                       
HET     BR  B 803       1                                                       
HET     BR  B 805       1                                                       
HET     BR  B 807       1                                                       
HET     BR  B 810       1                                                       
HET     BR  B 811       1                                                       
HET     BR  B 814       1                                                       
HET     BR  B 815       1                                                       
HET     BR  B 819       1                                                       
HET     BR  B 820       1                                                       
HET     BR  B 821       1                                                       
HET     BR  B 822       1                                                       
HET     BR  B 825       1                                                       
HET     BR  B 826       1                                                       
HET     BR  B 833       1                                                       
HET     BR  B 834       1                                                       
HET     BR  B 835       1                                                       
HET     BR  B 836       1                                                       
HET     BR  B 837       1                                                       
HET     BR  B 838       1                                                       
HET     BR  B 839       1                                                       
HETNAM      BR BROMIDE ION                                                      
FORMUL   3   BR    40(BR 1-)                                                    
FORMUL  43  HOH   *465(H2 O)                                                    
HELIX    1   1 ASP A   -4  THR A    3  5                                   7    
HELIX    2   2 THR A   28  GLY A   38  1                                  11    
HELIX    3   3 THR A   57  MET A   60  5                                   4    
HELIX    4   4 ASP A   80  ASN A  101  1                                  22    
HELIX    5   5 PRO A  104  ASN A  106  5                                   3    
HELIX    6   6 SER A  114  LEU A  125  1                                  12    
HELIX    7   7 LEU A  143  PHE A  147  5                                   5    
HELIX    8   8 PRO A  173  VAL A  188  1                                  16    
HELIX    9   9 ASN A  189  ALA A  191  5                                   3    
HELIX   10  10 CYS A  206  LEU A  221  1                                  16    
HELIX   11  11 PRO B   -3  SER B    2  5                                   5    
HELIX   12  12 THR B   28  GLY B   38  1                                  11    
HELIX   13  13 THR B   57  MET B   60  5                                   4    
HELIX   14  14 ASP B   80  ASN B  101  1                                  22    
HELIX   15  15 PRO B  104  ASN B  106  5                                   3    
HELIX   16  16 SER B  114  THR B  127  1                                  14    
HELIX   17  17 LEU B  143  PHE B  147  5                                   5    
HELIX   18  18 PRO B  173  VAL B  188  1                                  16    
HELIX   19  19 ASN B  189  ALA B  191  5                                   3    
HELIX   20  20 CYS B  206  LEU B  221  1                                  16    
SHEET    1   A 7 ALA A   7  VAL A   9  0                                        
SHEET    2   A 7 ILE A  44  CYS A  48 -1  N  TYR A  46   O  VAL A   9           
SHEET    3   A 7 ALA A  17  LEU A  22  1  O  ALA A  17   N  LYS A  45           
SHEET    4   A 7 ILE A 108  PHE A 113  1  O  ILE A 109   N  ILE A  20           
SHEET    5   A 7 GLY A 133  LEU A 137  1  O  GLY A 133   N  LEU A 110           
SHEET    6   A 7 ILE A 161  GLY A 166  1  O  LEU A 162   N  ALA A 136           
SHEET    7   A 7 VAL A 193  TYR A 198  1  N  THR A 194   O  ILE A 161           
SHEET    1   B 2 VAL A  53  PRO A  55  0                                        
SHEET    2   B 2 ALA A  63  PRO A  65 -1  N  MET A  64   O  ARG A  54           
SHEET    1   C 7 ALA B   7  VAL B   9  0                                        
SHEET    2   C 7 ILE B  44  CYS B  48 -1  N  TYR B  46   O  VAL B   9           
SHEET    3   C 7 ALA B  17  LEU B  22  1  O  ALA B  17   N  LYS B  45           
SHEET    4   C 7 ILE B 108  PHE B 113  1  O  ILE B 109   N  ILE B  20           
SHEET    5   C 7 GLY B 133  LEU B 137  1  O  GLY B 133   N  LEU B 110           
SHEET    6   C 7 ILE B 161  GLY B 166  1  O  LEU B 162   N  ALA B 136           
SHEET    7   C 7 VAL B 193  TYR B 198  1  O  THR B 194   N  GLN B 163           
SHEET    1   D 2 VAL B  53  PRO B  55  0                                        
SHEET    2   D 2 ALA B  63  PRO B  65 -1  N  MET B  64   O  ARG B  54           
SITE     1 ACA  3 SER A 114  ASP A 169  HIS A 203                               
SITE     1 ACB  3 SER B 114  ASP B 169  HIS B 203                               
SITE     1 AC1  3 LEU A  25  SER A 114  GLN A 115                               
SITE     1 AC2  3 LEU B  25  SER B 114  GLN B 115                               
SITE     1 AC3  4 ARG B  13  THR B  16  HIS B  43  ILE B 224                    
SITE     1 AC4  3 THR A  16  PRO A 223  ILE A 224                               
SITE     1 AC5  2 ALA B  11  HOH B1067                                          
SITE     1 AC6  1 ALA A  11                                                     
SITE     1 AC7  3 HOH A 905  HOH A 974  THR B  28                               
SITE     1 AC8  1 THR A  28                                                     
SITE     1 AC9  3 GLY A 200  GLN B 207  GLN B 208                               
SITE     1 BC1  1 ASN A 192                                                     
SITE     1 BC2  3 CYS A 206  GLN A 208  HOH A 962                               
SITE     1 BC3  4 PRO B   4  LEU B   5  THR B 197  HOH B1029                    
SITE     1 BC4  1 HOH B 847                                                     
SITE     1 BC5  2 MET A  -5  HOH A1030                                          
SITE     1 BC6  1 HOH A 926                                                     
SITE     1 BC7  1 PHE A 195                                                     
SITE     1 BC8  1 HOH B 858                                                     
SITE     1 BC9  4 HOH A 977  HOH A 990  HOH A1024  CYS B 168                    
SITE     1 CC1  1 GLU B 199                                                     
SITE     1 CC2  3 HIS B  23  HOH B1036  HOH B1079                               
SITE     1 CC3  2 LEU A   5  THR A 197                                          
SITE     1 CC4  2 HIS A  23  HIS A  50                                          
SITE     1 CC5  4 ASP A 167  GLY A 200  ASN B  61  GLN B 207                    
SITE     1 CC6  1 THR B 197                                                     
SITE     1 CC7  3 SER A 160  HOH A 898  HOH A 943                               
SITE     1 CC8  1 PRO A  75                                                     
SITE     1 CC9  3 ALA A  15  HOH A1011  HOH A1053                               
SITE     1 DC1  4 GLN A  86  HOH A 963  HOH A1032  HOH A1059                    
SITE     1 DC2  4 CYS A 168  MET A 202   BR A 832  HOH B1048                    
SITE     1 DC3  4 CYS A 168   BR A 831  HOH B1044  HOH B1048                    
SITE     1 DC4  2 LYS B 183  HOH B1020                                          
SITE     1 DC5  2 LYS B 185  HOH B1009                                          
SITE     1 DC6  4 SER B  41  HIS B  43  HOH B 889  HOH B 978                    
SITE     1 DC7  3 ASN B 106  HOH B 903  HOH B1023                               
SITE     1 DC8  2 GLN B 149  HOH B 917                                          
SITE     1 DC9  3 LYS B  92  GLN B 128  HOH B1061                               
SITE     1 EC1  3 LYS B 100  HOH B 851  HOH B1077                               
SITE     1 EC2  1 SER A 205                                                     
CRYST1   39.590  127.890   39.660  90.00 102.80  90.00 P 1 21 1      4          
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      0.025260  0.000000  0.005740        0.00000                         
SCALE2      0.000000  0.007820  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025860        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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