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LongText Report for: 1JU3-pdb

Name Class
1JU3-pdb
HEADER    HYDROLASE                               23-AUG-01   1JU3              
TITLE     BACTERIAL COCAINE ESTERASE COMPLEX WITH TRANSITION STATE              
TITLE    2 ANALOG                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COCAINE ESTERASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. MB1;                            
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BACTERIA                                   
KEYWDS    ALPHA/BETA HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.A.LARSEN,J.M.TURNER,J.STEVENS,S.J.ROSSER,A.BASRAN,                  
AUTHOR   2 R.A.LERNER,N.C.BRUCE,I.A.WILSON                                      
REVDAT   2   09-JAN-02 1JU3    1       AUTHOR                                   
REVDAT   1   21-DEC-01 1JU3    0                                                
JRNL        AUTH   N.A.LARSEN,J.M.TURNER,J.STEVENS,S.J.ROSSER,                  
JRNL        AUTH 2 A.BASRAN,R.A.LERNER,N.C.BRUCE,I.A.WILSON                     
JRNL        TITL   CRYSTAL STRUCTURE OF A BACTERIAL COCAINE ESTERASE            
JRNL        REF    NAT.STRUCT.BIOL.              V.   9    17 2002              
JRNL        REFN   ASTM NSBIEW  US ISSN 1072-8368                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.58 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 90349                          
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 SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4517                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4351                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 544                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.60                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JU3 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-2001.                
REMARK 100 THE RCSB ID CODE IS RCSB014186.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-2001; 07-MAR-2001           
REMARK 200  TEMPERATURE           (KELVIN) : 120; 120                           
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL ; SSRL                        
REMARK 200  BEAMLINE                       : 11-1; 11-1                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.965; 0.965                       
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC QUANTUM 4     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1JU4, COCE ENZYME                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM DTT, 10MM TRIS PH 7.5, 25 MM        
REMARK 280  NACL, 1.6 M AMMONIUM SULFATE                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,2/3+Z                                            
REMARK 290       3555   -X+Y,-X,1/3+Z                                           
REMARK 290       4555   -X,-Y,1/2+Z                                             
REMARK 290       5555   Y,-X+Y,1/6+Z                                            
REMARK 290       6555   X-Y,X,5/6+Z                                             
REMARK 290       7555   Y,X,2/3-Z                                               
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,1/3-Z                                           
REMARK 290      10555   -Y,-X,1/6-Z                                             
REMARK 290      11555   -X+Y,Y,1/2-Z                                            
REMARK 290      12555   X,X-Y,5/6-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.68000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       73.84000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.76000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       36.92000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      184.60000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      147.68000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       73.84000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       36.92000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      110.76000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      184.60000            
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 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 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     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     PRO A   575                                                      
REMARK 465     LEU A   576                                                      
REMARK 465     GLU A   577                                                      
REMARK 465     HIS A   578                                                      
REMARK 465     HIS A   579                                                      
REMARK 465     HIS A   580                                                      
REMARK 465     HIS A   581                                                      
REMARK 465     HIS A   582                                                      
REMARK 465     HIS A   583                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 573    CG    CD    CE    NZ                                
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH     991     O    HOH     991    12564     1.95            
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    ASN A  58   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    TRP A  59   N   -  CA  -  C   ANGL. DEV. =  9.9 DEGREES           
REMARK 500    VAL A  85   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    HIS A  87   N   -  CA  -  C   ANGL. DEV. = 11.5 DEGREES           
REMARK 500    VAL A  88   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES           
REMARK 500    ARG A 482   N   -  CA  -  C   ANGL. DEV. =-10.5 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  78     -114.71     51.66                                   
REMARK 500    HIS A  87      -43.20     65.64                                   
REMARK 500    SER A 117     -114.21     64.03                                   
REMARK 500    ASP A 180      150.64     63.22                                   
REMARK 500    THR A 371      166.66     68.37                                   
REMARK 500    LEU A 508     -117.60     56.56                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JU4   RELATED DB: PDB                                   
REMARK 900 BACTERIAL COCAINE ESTERASE COMPLEX WITH PRODUCT                      
DBREF  1JU3 A    1   574  GB     7229394  AAF42807         1    574             
SEQADV 1JU3 PRO A  575  GB   7229394             CLONING ARTIFACT               
SEQADV 1JU3 LEU A  576  GB   7229394             CLONING ARTIFACT               
SEQADV 1JU3 GLU A  577  GB   7229394             CLONING ARTIFACT               
SEQADV 1JU3 HIS A  578  GB   7229394             HIS TAG                        
SEQADV 1JU3 HIS A  579  GB   7229394             HIS TAG                        
SEQADV 1JU3 HIS A  580  GB   7229394             HIS TAG                        
SEQADV 1JU3 HIS A  581  GB   7229394             HIS TAG                        
SEQADV 1JU3 HIS A  582  GB   7229394             HIS TAG                        
SEQADV 1JU3 HIS A  583  GB   7229394             HIS TAG                        
SEQRES   1 A  583  MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET          
SEQRES   2 A  583  VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU          
SEQRES   3 A  583  TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU          
SEQRES   4 A  583  VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP          
SEQRES   5 A  583  SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP          
SEQRES   6 A  583  GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE          
SEQRES   7 A  583  ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU          
SEQRES   8 A  583  ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN          
SEQRES   9 A  583  ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY VAL SER          
SEQRES  10 A  583  TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY          
SEQRES  11 A  583  VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER          
SEQRES  12 A  583  ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY          
SEQRES  13 A  583  ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU          
SEQRES  14 A  583  ILE GLY THR GLY LEU ILE THR SER ARG SER ASP ALA ARG          
SEQRES  15 A  583  PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE          
SEQRES  16 A  583  LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU          
SEQRES  17 A  583  ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL          
SEQRES  18 A  583  ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER          
SEQRES  19 A  583  TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU          
SEQRES  20 A  583  ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY          
SEQRES  21 A  583  PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS          
SEQRES  22 A  583  ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER          
SEQRES  23 A  583  HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE          
SEQRES  24 A  583  GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR          
SEQRES  25 A  583  MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU          
SEQRES  26 A  583  THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE          
SEQRES  27 A  583  VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP          
SEQRES  28 A  583  PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY          
SEQRES  29 A  583  GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR          
SEQRES  30 A  583  LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR          
SEQRES  31 A  583  TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY          
SEQRES  32 A  583  GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA          
SEQRES  33 A  583  ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS          
SEQRES  34 A  583  TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR          
SEQRES  35 A  583  GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA          
SEQRES  36 A  583  VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE          
SEQRES  37 A  583  PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL          
SEQRES  38 A  583  ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU          
SEQRES  39 A  583  ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET          
SEQRES  40 A  583  LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE          
SEQRES  41 A  583  MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP          
SEQRES  42 A  583  ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN          
SEQRES  43 A  583  LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG          
SEQRES  44 A  583  GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE          
SEQRES  45 A  583  LYS ARG PRO LEU GLU HIS HIS HIS HIS HIS HIS                  
HET    PBC  A 575       9                                                       
HETNAM     PBC PHENYL BORONIC ACID                                              
FORMUL   2  PBC    C6 H7 O2 B1                                                  
FORMUL   3  HOH   *544(H2 O1)                                                   
HELIX    1   1 VAL A   49  THR A   54  1                                   6    
HELIX    2   2 TRP A   59  ASP A   65  1                                   7    
HELIX    3   3 ASP A   89  GLN A  104  1                                  16    
HELIX    4   4 SER A  117  VAL A  128  1                                  12    
HELIX    5   5 SER A  159  THR A  176  1                                  18    
HELIX    6   6 GLU A  184  ASP A  198  1                                  15    
HELIX    7   7 ASP A  198  SER A  204  1                                   7    
HELIX    8   8 LEU A  213  ILE A  218  1                                   6    
HELIX    9   9 PRO A  219  GLN A  224  1                                   6    
HELIX   10  10 ASP A  232  SER A  237  1                                   6    
HELIX   11  11 LEU A  240  GLY A  245  1                                   6    
HELIX   12  12 PHE A  261  LYS A  273  1                                  13    
HELIX   13  13 GLY A  300  THR A  304  5                                   5    
HELIX   14  14 PRO A  306  LEU A  322  1                                  17    
HELIX   15  15 GLN A  418  HIS A  422  5                                   5    
HELIX   16  16 ARG A  484  ARG A  486  5                                   3    
HELIX   17  17 VAL A  541  GLU A  545  5                                   5    
HELIX   18  18 GLN A  546  MET A  550  5                                   5    
SHEET    1   A 6 TYR A   6  PRO A  15  0                                        
SHEET    2   A 6 ARG A  21  PRO A  29 -1  O  LEU A  22   N  VAL A  14           
SHEET    3   A 6 ALA A  68  ASP A  73 -1  O  VAL A  69   N  TYR A  27           
SHEET    4   A 6 VAL A  35  ASN A  42  1  N  LEU A  38   O  VAL A  70           
SHEET    5   A 6 CYS A 107  MET A 113  1  O  GLY A 112   N  LEU A  39           
SHEET    6   A 6 LEU A 134  ALA A 136  1  O  LYS A 135   N  VAL A 111           
SHEET    1   B 2 GLY A 115  VAL A 116  0                                        
SHEET    2   B 2 PRO A 139  SER A 140  1  O  SER A 140   N  GLY A 115           
SHEET    1   C 4 ALA A 251  TYR A 258  0                                        
SHEET    2   C 4 ALA A 278  SER A 286  1  O  ARG A 279   N  ILE A 253           
SHEET    3   C 4 VAL A 335  VAL A 339  1  O  ARG A 336   N  VAL A 282           
SHEET    4   C 4 GLU A 344  GLU A 348 -1  O  GLU A 348   N  VAL A 335           
SHEET    1   D 2 ARG A 293  ASN A 294  0                                        
SHEET    2   D 2 ARG A 297  LYS A 298 -1  O  ARG A 297   N  ASN A 294           
SHEET    1   E 4 TYR A 501  PHE A 514  0                                        
SHEET    2   E 4 VAL A 439  SER A 453 -1  N  VAL A 441   O  ASN A 512           
SHEET    3   E 4 ALA A 553  ARG A 559 -1  O  HIS A 558   N  PHE A 450           
SHEET    4   E 4 SER A 387  TYR A 393 -1  N  SER A 387   O  ARG A 559           
SHEET    1   F 5 TYR A 501  PHE A 514  0                                        
SHEET    2   F 5 VAL A 439  SER A 453 -1  N  VAL A 441   O  ASN A 512           
SHEET    3   F 5 HIS A 566  ILE A 572 -1  O  VAL A 568   N  SER A 446           
SHEET    4   F 5 ALA A 357  GLY A 364 -1  N  THR A 359   O  LEU A 569           
SHEET    5   F 5 THR A 377  SER A 379 -1  O  SER A 379   N  TYR A 362           
SHEET    1   G 4 CYS A 429  SER A 431  0                                        
SHEET    2   G 4 ARG A 519  SER A 525 -1  O  VAL A 522   N  TYR A 430           
SHEET    3   G 4 ASP A 459  VAL A 467 -1  N  VAL A 465   O  MET A 521           
SHEET    4   G 4 ALA A 473  ARG A 482 -1  O  CYS A 477   N  LEU A 464           
LINK         OG  SER A 117                 B   PBC A 575                        
CISPEP   1 ALA A  149    PRO A  150          0        -0.17                     
CISPEP   2 THR A  206    PRO A  207          0        -0.88                     
CISPEP   3 TRP A  351    PRO A  352          0        -0.47                     
CISPEP   4 PHE A  529    PRO A  530          0         0.20                     
CRYST1  106.080  106.080  221.520  90.00  90.00 120.00 P 65 2 2     12          
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      0.009427  0.005443  0.000000        0.00000                         
SCALE2      0.000000  0.010885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004514        0.00000                         
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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